data_8ZVV
# 
_entry.id   8ZVV 
# 
_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   8ZVV         pdb_00008zvv 10.2210/pdb8zvv/pdb 
WWPDB D_1300048627 ?            ?                   
# 
_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                        8ZVV 
_pdbx_database_status.recvd_initial_deposition_date   2024-06-12 
_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 synthase complexed with citrate' 
_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' 48632.547 4   2.3.3.1 ? ? ? 
2 non-polymer syn 'CITRIC ACID'                     192.124   4   ?       ? ? ? 
3 water       nat water                             18.015    855 ?       ? ? ? 
# 
_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
LGVLAQLIWSRALGFPLERPKSMSTEGLMKFVDS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;STNLKDILADLIPKEQARIKTFRQQHGKTVVGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGFSIPECQKLLPKAK
GGEEPLPEGLFWLLVTGHIPTEEQVSWLSKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAVTALNSESNFARAYAQGI
SRTKYWELIYEDSMDLIAKLPCVAAKIYRNLYREGSGIGAIDSNLDWSHNFTNMLGYTDHQFTELTRLYLTIHSDHEGGN
VSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTQLQKEVGKDVSDEKLRDYIWNTLNSGRVVPGYGHAV
LRKTDPRYTCQREFALKHLPNDPMFKLVAQLYKIVPNVLLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRA
LGVLAQLIWSRALGFPLERPKSMSTEGLMKFVDS
;
_entity_poly.pdbx_strand_id                 A,B,C,D 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'CITRIC ACID' CIT 
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 
# 
_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                   434 
_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 
CIT non-polymer         . 'CITRIC ACID'   ? 'C6 H8 O7'       192.124 
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 
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 
B 1 1   SER 1   30  30  SER SER B . n 
B 1 2   THR 2   31  31  THR THR B . n 
B 1 3   ASN 3   32  32  ASN ASN B . n 
B 1 4   LEU 4   33  33  LEU LEU B . n 
B 1 5   LYS 5   34  34  LYS LYS B . n 
B 1 6   ASP 6   35  35  ASP ASP B . n 
B 1 7   ILE 7   36  36  ILE ILE B . n 
B 1 8   LEU 8   37  37  LEU LEU B . n 
B 1 9   ALA 9   38  38  ALA ALA B . n 
B 1 10  ASP 10  39  39  ASP ASP B . n 
B 1 11  LEU 11  40  40  LEU LEU B . n 
B 1 12  ILE 12  41  41  ILE ILE B . n 
B 1 13  PRO 13  42  42  PRO PRO B . n 
B 1 14  LYS 14  43  43  LYS LYS B . n 
B 1 15  GLU 15  44  44  GLU GLU B . n 
B 1 16  GLN 16  45  45  GLN GLN B . n 
B 1 17  ALA 17  46  46  ALA ALA B . n 
B 1 18  ARG 18  47  47  ARG ARG B . n 
B 1 19  ILE 19  48  48  ILE ILE B . n 
B 1 20  LYS 20  49  49  LYS LYS B . n 
B 1 21  THR 21  50  50  THR THR B . n 
B 1 22  PHE 22  51  51  PHE PHE B . n 
B 1 23  ARG 23  52  52  ARG ARG B . n 
B 1 24  GLN 24  53  53  GLN GLN B . n 
B 1 25  GLN 25  54  54  GLN GLN B . n 
B 1 26  HIS 26  55  55  HIS HIS B . n 
B 1 27  GLY 27  56  56  GLY GLY B . n 
B 1 28  LYS 28  57  57  LYS LYS B . n 
B 1 29  THR 29  58  58  THR THR B . n 
B 1 30  VAL 30  59  59  VAL VAL B . n 
B 1 31  VAL 31  60  60  VAL VAL B . n 
B 1 32  GLY 32  61  61  GLY GLY B . n 
B 1 33  GLN 33  62  62  GLN GLN B . n 
B 1 34  ILE 34  63  63  ILE ILE B . n 
B 1 35  THR 35  64  64  THR THR B . n 
B 1 36  VAL 36  65  65  VAL VAL B . n 
B 1 37  ASP 37  66  66  ASP ASP B . n 
B 1 38  MET 38  67  67  MET MET B . n 
B 1 39  MET 39  68  68  MET MET B . n 
B 1 40  TYR 40  69  69  TYR TYR B . n 
B 1 41  GLY 41  70  70  GLY GLY B . n 
B 1 42  GLY 42  71  71  GLY GLY B . n 
B 1 43  MET 43  72  72  MET MET B . n 
B 1 44  ARG 44  73  73  ARG ARG B . n 
B 1 45  GLY 45  74  74  GLY GLY B . n 
B 1 46  MET 46  75  75  MET MET B . n 
B 1 47  LYS 47  76  76  LYS LYS B . n 
B 1 48  GLY 48  77  77  GLY GLY B . n 
B 1 49  LEU 49  78  78  LEU LEU B . n 
B 1 50  VAL 50  79  79  VAL VAL B . n 
B 1 51  TYR 51  80  80  TYR TYR B . n 
B 1 52  GLU 52  81  81  GLU GLU B . n 
B 1 53  THR 53  82  82  THR THR B . n 
B 1 54  SER 54  83  83  SER SER B . n 
B 1 55  VAL 55  84  84  VAL VAL B . n 
B 1 56  LEU 56  85  85  LEU LEU B . n 
B 1 57  ASP 57  86  86  ASP ASP B . n 
B 1 58  PRO 58  87  87  PRO PRO B . n 
B 1 59  ASP 59  88  88  ASP ASP B . n 
B 1 60  GLU 60  89  89  GLU GLU B . n 
B 1 61  GLY 61  90  90  GLY GLY B . n 
B 1 62  ILE 62  91  91  ILE ILE B . n 
B 1 63  ARG 63  92  92  ARG ARG B . n 
B 1 64  PHE 64  93  93  PHE PHE B . n 
B 1 65  ARG 65  94  94  ARG ARG B . n 
B 1 66  GLY 66  95  95  GLY GLY B . n 
B 1 67  PHE 67  96  96  PHE PHE B . n 
B 1 68  SER 68  97  97  SER SER B . n 
B 1 69  ILE 69  98  98  ILE ILE B . n 
B 1 70  PRO 70  99  99  PRO PRO B . n 
B 1 71  GLU 71  100 100 GLU GLU B . n 
B 1 72  CYS 72  101 101 CYS CYS B . n 
B 1 73  GLN 73  102 102 GLN GLN B . n 
B 1 74  LYS 74  103 103 LYS LYS B . n 
B 1 75  LEU 75  104 104 LEU LEU B . n 
B 1 76  LEU 76  105 105 LEU LEU B . n 
B 1 77  PRO 77  106 106 PRO PRO B . n 
B 1 78  LYS 78  107 107 LYS LYS B . n 
B 1 79  ALA 79  108 108 ALA ALA B . n 
B 1 80  LYS 80  109 109 LYS LYS B . n 
B 1 81  GLY 81  110 110 GLY GLY B . n 
B 1 82  GLY 82  111 111 GLY GLY B . n 
B 1 83  GLU 83  112 112 GLU GLU B . n 
B 1 84  GLU 84  113 113 GLU GLU B . n 
B 1 85  PRO 85  114 114 PRO PRO B . n 
B 1 86  LEU 86  115 115 LEU LEU B . n 
B 1 87  PRO 87  116 116 PRO PRO B . n 
B 1 88  GLU 88  117 117 GLU GLU B . n 
B 1 89  GLY 89  118 118 GLY GLY B . n 
B 1 90  LEU 90  119 119 LEU LEU B . n 
B 1 91  PHE 91  120 120 PHE PHE B . n 
B 1 92  TRP 92  121 121 TRP TRP B . n 
B 1 93  LEU 93  122 122 LEU LEU B . n 
B 1 94  LEU 94  123 123 LEU LEU B . n 
B 1 95  VAL 95  124 124 VAL VAL B . n 
B 1 96  THR 96  125 125 THR THR B . n 
B 1 97  GLY 97  126 126 GLY GLY B . n 
B 1 98  HIS 98  127 127 HIS HIS B . n 
B 1 99  ILE 99  128 128 ILE ILE B . n 
B 1 100 PRO 100 129 129 PRO PRO B . n 
B 1 101 THR 101 130 130 THR THR B . n 
B 1 102 GLU 102 131 131 GLU GLU B . n 
B 1 103 GLU 103 132 132 GLU GLU B . n 
B 1 104 GLN 104 133 133 GLN GLN B . n 
B 1 105 VAL 105 134 134 VAL VAL B . n 
B 1 106 SER 106 135 135 SER SER B . n 
B 1 107 TRP 107 136 136 TRP TRP B . n 
B 1 108 LEU 108 137 137 LEU LEU B . n 
B 1 109 SER 109 138 138 SER SER B . n 
B 1 110 LYS 110 139 139 LYS LYS B . n 
B 1 111 GLU 111 140 140 GLU GLU B . n 
B 1 112 TRP 112 141 141 TRP TRP B . n 
B 1 113 ALA 113 142 142 ALA ALA B . n 
B 1 114 LYS 114 143 143 LYS LYS B . n 
B 1 115 ARG 115 144 144 ARG ARG B . n 
B 1 116 ALA 116 145 145 ALA ALA B . n 
B 1 117 ALA 117 146 146 ALA ALA B . n 
B 1 118 LEU 118 147 147 LEU LEU B . n 
B 1 119 PRO 119 148 148 PRO PRO B . n 
B 1 120 SER 120 149 149 SER SER B . n 
B 1 121 HIS 121 150 150 HIS HIS B . n 
B 1 122 VAL 122 151 151 VAL VAL B . n 
B 1 123 VAL 123 152 152 VAL VAL B . n 
B 1 124 THR 124 153 153 THR THR B . n 
B 1 125 MET 125 154 154 MET MET B . n 
B 1 126 LEU 126 155 155 LEU LEU B . n 
B 1 127 ASP 127 156 156 ASP ASP B . n 
B 1 128 ASN 128 157 157 ASN ASN B . n 
B 1 129 PHE 129 158 158 PHE PHE B . n 
B 1 130 PRO 130 159 159 PRO PRO B . n 
B 1 131 THR 131 160 160 THR THR B . n 
B 1 132 ASN 132 161 161 ASN ASN B . n 
B 1 133 LEU 133 162 162 LEU LEU B . n 
B 1 134 HIS 134 163 163 HIS HIS B . n 
B 1 135 PRO 135 164 164 PRO PRO B . n 
B 1 136 MET 136 165 165 MET MET B . n 
B 1 137 SER 137 166 166 SER SER B . n 
B 1 138 GLN 138 167 167 GLN GLN B . n 
B 1 139 LEU 139 168 168 LEU LEU B . n 
B 1 140 SER 140 169 169 SER SER B . n 
B 1 141 ALA 141 170 170 ALA ALA B . n 
B 1 142 ALA 142 171 171 ALA ALA B . n 
B 1 143 VAL 143 172 172 VAL VAL B . n 
B 1 144 THR 144 173 173 THR THR B . n 
B 1 145 ALA 145 174 174 ALA ALA B . n 
B 1 146 LEU 146 175 175 LEU LEU B . n 
B 1 147 ASN 147 176 176 ASN ASN B . n 
B 1 148 SER 148 177 177 SER SER B . n 
B 1 149 GLU 149 178 178 GLU GLU B . n 
B 1 150 SER 150 179 179 SER SER B . n 
B 1 151 ASN 151 180 180 ASN ASN B . n 
B 1 152 PHE 152 181 181 PHE PHE B . n 
B 1 153 ALA 153 182 182 ALA ALA B . n 
B 1 154 ARG 154 183 183 ARG ARG B . n 
B 1 155 ALA 155 184 184 ALA ALA B . n 
B 1 156 TYR 156 185 185 TYR TYR B . n 
B 1 157 ALA 157 186 186 ALA ALA B . n 
B 1 158 GLN 158 187 187 GLN GLN B . n 
B 1 159 GLY 159 188 188 GLY GLY B . n 
B 1 160 ILE 160 189 189 ILE ILE B . n 
B 1 161 SER 161 190 190 SER SER B . n 
B 1 162 ARG 162 191 191 ARG ARG B . n 
B 1 163 THR 163 192 192 THR THR B . n 
B 1 164 LYS 164 193 193 LYS LYS B . n 
B 1 165 TYR 165 194 194 TYR TYR B . n 
B 1 166 TRP 166 195 195 TRP TRP B . n 
B 1 167 GLU 167 196 196 GLU GLU B . n 
B 1 168 LEU 168 197 197 LEU LEU B . n 
B 1 169 ILE 169 198 198 ILE ILE B . n 
B 1 170 TYR 170 199 199 TYR TYR B . n 
B 1 171 GLU 171 200 200 GLU GLU B . n 
B 1 172 ASP 172 201 201 ASP ASP B . n 
B 1 173 SER 173 202 202 SER SER B . n 
B 1 174 MET 174 203 203 MET MET B . n 
B 1 175 ASP 175 204 204 ASP ASP B . n 
B 1 176 LEU 176 205 205 LEU LEU B . n 
B 1 177 ILE 177 206 206 ILE ILE B . n 
B 1 178 ALA 178 207 207 ALA ALA B . n 
B 1 179 LYS 179 208 208 LYS LYS B . n 
B 1 180 LEU 180 209 209 LEU LEU B . n 
B 1 181 PRO 181 210 210 PRO PRO B . n 
B 1 182 CYS 182 211 211 CYS CYS B . n 
B 1 183 VAL 183 212 212 VAL VAL B . n 
B 1 184 ALA 184 213 213 ALA ALA B . n 
B 1 185 ALA 185 214 214 ALA ALA B . n 
B 1 186 LYS 186 215 215 LYS LYS B . n 
B 1 187 ILE 187 216 216 ILE ILE B . n 
B 1 188 TYR 188 217 217 TYR TYR B . n 
B 1 189 ARG 189 218 218 ARG ARG B . n 
B 1 190 ASN 190 219 219 ASN ASN B . n 
B 1 191 LEU 191 220 220 LEU LEU B . n 
B 1 192 TYR 192 221 221 TYR TYR B . n 
B 1 193 ARG 193 222 222 ARG ARG B . n 
B 1 194 GLU 194 223 223 GLU GLU B . n 
B 1 195 GLY 195 224 224 GLY GLY B . n 
B 1 196 SER 196 225 225 SER SER B . n 
B 1 197 GLY 197 226 226 GLY GLY B . n 
B 1 198 ILE 198 227 227 ILE ILE B . n 
B 1 199 GLY 199 228 228 GLY GLY B . n 
B 1 200 ALA 200 229 229 ALA ALA B . n 
B 1 201 ILE 201 230 230 ILE ILE B . n 
B 1 202 ASP 202 231 231 ASP ASP B . n 
B 1 203 SER 203 232 232 SER SER B . n 
B 1 204 ASN 204 233 233 ASN ASN B . n 
B 1 205 LEU 205 234 234 LEU LEU B . n 
B 1 206 ASP 206 235 235 ASP ASP B . n 
B 1 207 TRP 207 236 236 TRP TRP B . n 
B 1 208 SER 208 237 237 SER SER B . n 
B 1 209 HIS 209 238 238 HIS HIS B . n 
B 1 210 ASN 210 239 239 ASN ASN B . n 
B 1 211 PHE 211 240 240 PHE PHE B . n 
B 1 212 THR 212 241 241 THR THR B . n 
B 1 213 ASN 213 242 242 ASN ASN B . n 
B 1 214 MET 214 243 243 MET MET B . n 
B 1 215 LEU 215 244 244 LEU LEU B . n 
B 1 216 GLY 216 245 245 GLY GLY B . n 
B 1 217 TYR 217 246 246 TYR TYR B . n 
B 1 218 THR 218 247 247 THR THR B . n 
B 1 219 ASP 219 248 248 ASP ASP B . n 
B 1 220 HIS 220 249 249 HIS HIS B . n 
B 1 221 GLN 221 250 250 GLN GLN B . n 
B 1 222 PHE 222 251 251 PHE PHE B . n 
B 1 223 THR 223 252 252 THR THR B . n 
B 1 224 GLU 224 253 253 GLU GLU B . n 
B 1 225 LEU 225 254 254 LEU LEU B . n 
B 1 226 THR 226 255 255 THR THR B . n 
B 1 227 ARG 227 256 256 ARG ARG B . n 
B 1 228 LEU 228 257 257 LEU LEU B . n 
B 1 229 TYR 229 258 258 TYR TYR B . n 
B 1 230 LEU 230 259 259 LEU LEU B . n 
B 1 231 THR 231 260 260 THR THR B . n 
B 1 232 ILE 232 261 261 ILE ILE B . n 
B 1 233 HIS 233 262 262 HIS HIS B . n 
B 1 234 SER 234 263 263 SER SER B . n 
B 1 235 ASP 235 264 264 ASP ASP B . n 
B 1 236 HIS 236 265 265 HIS HIS B . n 
B 1 237 GLU 237 266 266 GLU GLU B . n 
B 1 238 GLY 238 267 267 GLY GLY B . n 
B 1 239 GLY 239 268 268 GLY GLY B . n 
B 1 240 ASN 240 269 269 ASN ASN B . n 
B 1 241 VAL 241 270 270 VAL VAL B . n 
B 1 242 SER 242 271 271 SER SER B . n 
B 1 243 ALA 243 272 272 ALA ALA B . n 
B 1 244 HIS 244 273 273 HIS HIS B . n 
B 1 245 THR 245 274 274 THR THR B . n 
B 1 246 SER 246 275 275 SER SER B . n 
B 1 247 HIS 247 276 276 HIS HIS B . n 
B 1 248 LEU 248 277 277 LEU LEU B . n 
B 1 249 VAL 249 278 278 VAL VAL B . n 
B 1 250 GLY 250 279 279 GLY GLY B . n 
B 1 251 SER 251 280 280 SER SER B . n 
B 1 252 ALA 252 281 281 ALA ALA B . n 
B 1 253 LEU 253 282 282 LEU LEU B . n 
B 1 254 SER 254 283 283 SER SER B . n 
B 1 255 ASP 255 284 284 ASP ASP B . n 
B 1 256 PRO 256 285 285 PRO PRO B . n 
B 1 257 TYR 257 286 286 TYR TYR B . n 
B 1 258 LEU 258 287 287 LEU LEU B . n 
B 1 259 SER 259 288 288 SER SER B . n 
B 1 260 PHE 260 289 289 PHE PHE B . n 
B 1 261 ALA 261 290 290 ALA ALA B . n 
B 1 262 ALA 262 291 291 ALA ALA B . n 
B 1 263 ALA 263 292 292 ALA ALA B . n 
B 1 264 MET 264 293 293 MET MET B . n 
B 1 265 ASN 265 294 294 ASN ASN B . n 
B 1 266 GLY 266 295 295 GLY GLY B . n 
B 1 267 LEU 267 296 296 LEU LEU B . n 
B 1 268 ALA 268 297 297 ALA ALA B . n 
B 1 269 GLY 269 298 298 GLY GLY B . n 
B 1 270 PRO 270 299 299 PRO PRO B . n 
B 1 271 LEU 271 300 300 LEU LEU B . n 
B 1 272 HIS 272 301 301 HIS HIS B . n 
B 1 273 GLY 273 302 302 GLY GLY B . n 
B 1 274 LEU 274 303 303 LEU LEU B . n 
B 1 275 ALA 275 304 304 ALA ALA B . n 
B 1 276 ASN 276 305 305 ASN ASN B . n 
B 1 277 GLN 277 306 306 GLN GLN B . n 
B 1 278 GLU 278 307 307 GLU GLU B . n 
B 1 279 VAL 279 308 308 VAL VAL B . n 
B 1 280 LEU 280 309 309 LEU LEU B . n 
B 1 281 VAL 281 310 310 VAL VAL B . n 
B 1 282 TRP 282 311 311 TRP TRP B . n 
B 1 283 LEU 283 312 312 LEU LEU B . n 
B 1 284 THR 284 313 313 THR THR B . n 
B 1 285 GLN 285 314 314 GLN GLN B . n 
B 1 286 LEU 286 315 315 LEU LEU B . n 
B 1 287 GLN 287 316 316 GLN GLN B . n 
B 1 288 LYS 288 317 317 LYS LYS B . n 
B 1 289 GLU 289 318 318 GLU GLU B . n 
B 1 290 VAL 290 319 319 VAL VAL B . n 
B 1 291 GLY 291 320 320 GLY GLY B . n 
B 1 292 LYS 292 321 321 LYS LYS B . n 
B 1 293 ASP 293 322 322 ASP ASP B . n 
B 1 294 VAL 294 323 323 VAL VAL B . n 
B 1 295 SER 295 324 324 SER SER B . n 
B 1 296 ASP 296 325 325 ASP ASP B . n 
B 1 297 GLU 297 326 326 GLU GLU B . n 
B 1 298 LYS 298 327 327 LYS LYS B . n 
B 1 299 LEU 299 328 328 LEU LEU B . n 
B 1 300 ARG 300 329 329 ARG ARG B . n 
B 1 301 ASP 301 330 330 ASP ASP B . n 
B 1 302 TYR 302 331 331 TYR TYR B . n 
B 1 303 ILE 303 332 332 ILE ILE B . n 
B 1 304 TRP 304 333 333 TRP TRP B . n 
B 1 305 ASN 305 334 334 ASN ASN B . n 
B 1 306 THR 306 335 335 THR THR B . n 
B 1 307 LEU 307 336 336 LEU LEU B . n 
B 1 308 ASN 308 337 337 ASN ASN B . n 
B 1 309 SER 309 338 338 SER SER B . n 
B 1 310 GLY 310 339 339 GLY GLY B . n 
B 1 311 ARG 311 340 340 ARG ARG B . n 
B 1 312 VAL 312 341 341 VAL VAL B . n 
B 1 313 VAL 313 342 342 VAL VAL B . n 
B 1 314 PRO 314 343 343 PRO PRO B . n 
B 1 315 GLY 315 344 344 GLY GLY B . n 
B 1 316 TYR 316 345 345 TYR TYR B . n 
B 1 317 GLY 317 346 346 GLY GLY B . n 
B 1 318 HIS 318 347 347 HIS HIS B . n 
B 1 319 ALA 319 348 348 ALA ALA B . n 
B 1 320 VAL 320 349 349 VAL VAL B . n 
B 1 321 LEU 321 350 350 LEU LEU B . n 
B 1 322 ARG 322 351 351 ARG ARG B . n 
B 1 323 LYS 323 352 352 LYS LYS B . n 
B 1 324 THR 324 353 353 THR THR B . n 
B 1 325 ASP 325 354 354 ASP ASP B . n 
B 1 326 PRO 326 355 355 PRO PRO B . n 
B 1 327 ARG 327 356 356 ARG ARG B . n 
B 1 328 TYR 328 357 357 TYR TYR B . n 
B 1 329 THR 329 358 358 THR THR B . n 
B 1 330 CYS 330 359 359 CYS CYS B . n 
B 1 331 GLN 331 360 360 GLN GLN B . n 
B 1 332 ARG 332 361 361 ARG ARG B . n 
B 1 333 GLU 333 362 362 GLU GLU B . n 
B 1 334 PHE 334 363 363 PHE PHE B . n 
B 1 335 ALA 335 364 364 ALA ALA B . n 
B 1 336 LEU 336 365 365 LEU LEU B . n 
B 1 337 LYS 337 366 366 LYS LYS B . n 
B 1 338 HIS 338 367 367 HIS HIS B . n 
B 1 339 LEU 339 368 368 LEU LEU B . n 
B 1 340 PRO 340 369 369 PRO PRO B . n 
B 1 341 ASN 341 370 370 ASN ASN B . n 
B 1 342 ASP 342 371 371 ASP ASP B . n 
B 1 343 PRO 343 372 372 PRO PRO B . n 
B 1 344 MET 344 373 373 MET MET B . n 
B 1 345 PHE 345 374 374 PHE PHE B . n 
B 1 346 LYS 346 375 375 LYS LYS B . n 
B 1 347 LEU 347 376 376 LEU LEU B . n 
B 1 348 VAL 348 377 377 VAL VAL B . n 
B 1 349 ALA 349 378 378 ALA ALA B . n 
B 1 350 GLN 350 379 379 GLN GLN B . n 
B 1 351 LEU 351 380 380 LEU LEU B . n 
B 1 352 TYR 352 381 381 TYR TYR B . n 
B 1 353 LYS 353 382 382 LYS LYS B . n 
B 1 354 ILE 354 383 383 ILE ILE B . n 
B 1 355 VAL 355 384 384 VAL VAL B . n 
B 1 356 PRO 356 385 385 PRO PRO B . n 
B 1 357 ASN 357 386 386 ASN ASN B . n 
B 1 358 VAL 358 387 387 VAL VAL B . n 
B 1 359 LEU 359 388 388 LEU LEU B . n 
B 1 360 LEU 360 389 389 LEU LEU B . n 
B 1 361 GLU 361 390 390 GLU GLU B . n 
B 1 362 GLN 362 391 391 GLN GLN B . n 
B 1 363 GLY 363 392 392 GLY GLY B . n 
B 1 364 LYS 364 393 393 LYS LYS B . n 
B 1 365 ALA 365 394 394 ALA ALA B . n 
B 1 366 LYS 366 395 395 LYS LYS B . n 
B 1 367 ASN 367 396 396 ASN ASN B . n 
B 1 368 PRO 368 397 397 PRO PRO B . n 
B 1 369 TRP 369 398 398 TRP TRP B . n 
B 1 370 PRO 370 399 399 PRO PRO B . n 
B 1 371 ASN 371 400 400 ASN ASN B . n 
B 1 372 VAL 372 401 401 VAL VAL B . n 
B 1 373 ASP 373 402 402 ASP ASP B . n 
B 1 374 ALA 374 403 403 ALA ALA B . n 
B 1 375 HIS 375 404 404 HIS HIS B . n 
B 1 376 SER 376 405 405 SER SER B . n 
B 1 377 GLY 377 406 406 GLY GLY B . n 
B 1 378 VAL 378 407 407 VAL VAL B . n 
B 1 379 LEU 379 408 408 LEU LEU B . n 
B 1 380 LEU 380 409 409 LEU LEU B . n 
B 1 381 GLN 381 410 410 GLN GLN B . n 
B 1 382 TYR 382 411 411 TYR TYR B . n 
B 1 383 TYR 383 412 412 TYR TYR B . n 
B 1 384 GLY 384 413 413 GLY GLY B . n 
B 1 385 MET 385 414 414 MET MET B . n 
B 1 386 THR 386 415 415 THR THR B . n 
B 1 387 GLU 387 416 416 GLU GLU B . n 
B 1 388 MET 388 417 417 MET MET B . n 
B 1 389 ASN 389 418 418 ASN ASN B . n 
B 1 390 TYR 390 419 419 TYR TYR B . n 
B 1 391 TYR 391 420 420 TYR TYR B . n 
B 1 392 THR 392 421 421 THR THR B . n 
B 1 393 VAL 393 422 422 VAL VAL B . n 
B 1 394 LEU 394 423 423 LEU LEU B . n 
B 1 395 PHE 395 424 424 PHE PHE B . n 
B 1 396 GLY 396 425 425 GLY GLY B . n 
B 1 397 VAL 397 426 426 VAL VAL B . n 
B 1 398 SER 398 427 427 SER SER B . n 
B 1 399 ARG 399 428 428 ARG ARG B . n 
B 1 400 ALA 400 429 429 ALA ALA B . n 
B 1 401 LEU 401 430 430 LEU LEU B . n 
B 1 402 GLY 402 431 431 GLY GLY B . n 
B 1 403 VAL 403 432 432 VAL VAL B . n 
B 1 404 LEU 404 433 433 LEU LEU B . n 
B 1 405 ALA 405 434 434 ALA ALA B . n 
B 1 406 GLN 406 435 435 GLN GLN B . n 
B 1 407 LEU 407 436 436 LEU LEU B . n 
B 1 408 ILE 408 437 437 ILE ILE B . n 
B 1 409 TRP 409 438 438 TRP TRP B . n 
B 1 410 SER 410 439 439 SER SER B . n 
B 1 411 ARG 411 440 440 ARG ARG B . n 
B 1 412 ALA 412 441 441 ALA ALA B . n 
B 1 413 LEU 413 442 442 LEU LEU B . n 
B 1 414 GLY 414 443 443 GLY GLY B . n 
B 1 415 PHE 415 444 444 PHE PHE B . n 
B 1 416 PRO 416 445 445 PRO PRO B . n 
B 1 417 LEU 417 446 446 LEU LEU B . n 
B 1 418 GLU 418 447 447 GLU GLU B . n 
B 1 419 ARG 419 448 448 ARG ARG B . n 
B 1 420 PRO 420 449 449 PRO PRO B . n 
B 1 421 LYS 421 450 450 LYS LYS B . n 
B 1 422 SER 422 451 451 SER SER B . n 
B 1 423 MET 423 452 452 MET MET B . n 
B 1 424 SER 424 453 453 SER SER B . n 
B 1 425 THR 425 454 454 THR THR B . n 
B 1 426 GLU 426 455 455 GLU GLU B . n 
B 1 427 GLY 427 456 456 GLY GLY B . n 
B 1 428 LEU 428 457 457 LEU LEU B . n 
B 1 429 MET 429 458 458 MET MET B . n 
B 1 430 LYS 430 459 459 LYS LYS B . n 
B 1 431 PHE 431 460 460 PHE PHE B . n 
B 1 432 VAL 432 461 461 VAL VAL B . n 
B 1 433 ASP 433 462 462 ASP ASP B . n 
B 1 434 SER 434 463 463 SER SER B . n 
C 1 1   SER 1   30  30  SER SER C . n 
C 1 2   THR 2   31  31  THR THR C . n 
C 1 3   ASN 3   32  32  ASN ASN C . n 
C 1 4   LEU 4   33  33  LEU LEU C . n 
C 1 5   LYS 5   34  34  LYS LYS C . n 
C 1 6   ASP 6   35  35  ASP ASP C . n 
C 1 7   ILE 7   36  36  ILE ILE C . n 
C 1 8   LEU 8   37  37  LEU LEU C . n 
C 1 9   ALA 9   38  38  ALA ALA C . n 
C 1 10  ASP 10  39  39  ASP ASP C . n 
C 1 11  LEU 11  40  40  LEU LEU C . n 
C 1 12  ILE 12  41  41  ILE ILE C . n 
C 1 13  PRO 13  42  42  PRO PRO C . n 
C 1 14  LYS 14  43  43  LYS LYS C . n 
C 1 15  GLU 15  44  44  GLU GLU C . n 
C 1 16  GLN 16  45  45  GLN GLN C . n 
C 1 17  ALA 17  46  46  ALA ALA C . n 
C 1 18  ARG 18  47  47  ARG ARG C . n 
C 1 19  ILE 19  48  48  ILE ILE C . n 
C 1 20  LYS 20  49  49  LYS LYS C . n 
C 1 21  THR 21  50  50  THR THR C . n 
C 1 22  PHE 22  51  51  PHE PHE C . n 
C 1 23  ARG 23  52  52  ARG ARG C . n 
C 1 24  GLN 24  53  53  GLN GLN C . n 
C 1 25  GLN 25  54  54  GLN GLN C . n 
C 1 26  HIS 26  55  55  HIS HIS C . n 
C 1 27  GLY 27  56  56  GLY GLY C . n 
C 1 28  LYS 28  57  57  LYS LYS C . n 
C 1 29  THR 29  58  58  THR THR C . n 
C 1 30  VAL 30  59  59  VAL VAL C . n 
C 1 31  VAL 31  60  60  VAL VAL C . n 
C 1 32  GLY 32  61  61  GLY GLY C . n 
C 1 33  GLN 33  62  62  GLN GLN C . n 
C 1 34  ILE 34  63  63  ILE ILE C . n 
C 1 35  THR 35  64  64  THR THR C . n 
C 1 36  VAL 36  65  65  VAL VAL C . n 
C 1 37  ASP 37  66  66  ASP ASP C . n 
C 1 38  MET 38  67  67  MET MET C . n 
C 1 39  MET 39  68  68  MET MET C . n 
C 1 40  TYR 40  69  69  TYR TYR C . n 
C 1 41  GLY 41  70  70  GLY GLY C . n 
C 1 42  GLY 42  71  71  GLY GLY C . n 
C 1 43  MET 43  72  72  MET MET C . n 
C 1 44  ARG 44  73  73  ARG ARG C . n 
C 1 45  GLY 45  74  74  GLY GLY C . n 
C 1 46  MET 46  75  75  MET MET C . n 
C 1 47  LYS 47  76  76  LYS LYS C . n 
C 1 48  GLY 48  77  77  GLY GLY C . n 
C 1 49  LEU 49  78  78  LEU LEU C . n 
C 1 50  VAL 50  79  79  VAL VAL C . n 
C 1 51  TYR 51  80  80  TYR TYR C . n 
C 1 52  GLU 52  81  81  GLU GLU C . n 
C 1 53  THR 53  82  82  THR THR C . n 
C 1 54  SER 54  83  83  SER SER C . n 
C 1 55  VAL 55  84  84  VAL VAL C . n 
C 1 56  LEU 56  85  85  LEU LEU C . n 
C 1 57  ASP 57  86  86  ASP ASP C . n 
C 1 58  PRO 58  87  87  PRO PRO C . n 
C 1 59  ASP 59  88  88  ASP ASP C . n 
C 1 60  GLU 60  89  89  GLU GLU C . n 
C 1 61  GLY 61  90  90  GLY GLY C . n 
C 1 62  ILE 62  91  91  ILE ILE C . n 
C 1 63  ARG 63  92  92  ARG ARG C . n 
C 1 64  PHE 64  93  93  PHE PHE C . n 
C 1 65  ARG 65  94  94  ARG ARG C . n 
C 1 66  GLY 66  95  95  GLY GLY C . n 
C 1 67  PHE 67  96  96  PHE PHE C . n 
C 1 68  SER 68  97  97  SER SER C . n 
C 1 69  ILE 69  98  98  ILE ILE C . n 
C 1 70  PRO 70  99  99  PRO PRO C . n 
C 1 71  GLU 71  100 100 GLU GLU C . n 
C 1 72  CYS 72  101 101 CYS CYS C . n 
C 1 73  GLN 73  102 102 GLN GLN C . n 
C 1 74  LYS 74  103 103 LYS LYS C . n 
C 1 75  LEU 75  104 104 LEU LEU C . n 
C 1 76  LEU 76  105 105 LEU LEU C . n 
C 1 77  PRO 77  106 106 PRO PRO C . n 
C 1 78  LYS 78  107 107 LYS LYS C . n 
C 1 79  ALA 79  108 108 ALA ALA C . n 
C 1 80  LYS 80  109 109 LYS LYS C . n 
C 1 81  GLY 81  110 110 GLY GLY C . n 
C 1 82  GLY 82  111 111 GLY GLY C . n 
C 1 83  GLU 83  112 112 GLU GLU C . n 
C 1 84  GLU 84  113 113 GLU GLU C . n 
C 1 85  PRO 85  114 114 PRO PRO C . n 
C 1 86  LEU 86  115 115 LEU LEU C . n 
C 1 87  PRO 87  116 116 PRO PRO C . n 
C 1 88  GLU 88  117 117 GLU GLU C . n 
C 1 89  GLY 89  118 118 GLY GLY C . n 
C 1 90  LEU 90  119 119 LEU LEU C . n 
C 1 91  PHE 91  120 120 PHE PHE C . n 
C 1 92  TRP 92  121 121 TRP TRP C . n 
C 1 93  LEU 93  122 122 LEU LEU C . n 
C 1 94  LEU 94  123 123 LEU LEU C . n 
C 1 95  VAL 95  124 124 VAL VAL C . n 
C 1 96  THR 96  125 125 THR THR C . n 
C 1 97  GLY 97  126 126 GLY GLY C . n 
C 1 98  HIS 98  127 127 HIS HIS C . n 
C 1 99  ILE 99  128 128 ILE ILE C . n 
C 1 100 PRO 100 129 129 PRO PRO C . n 
C 1 101 THR 101 130 130 THR THR C . n 
C 1 102 GLU 102 131 131 GLU GLU C . n 
C 1 103 GLU 103 132 132 GLU GLU C . n 
C 1 104 GLN 104 133 133 GLN GLN C . n 
C 1 105 VAL 105 134 134 VAL VAL C . n 
C 1 106 SER 106 135 135 SER SER C . n 
C 1 107 TRP 107 136 136 TRP TRP C . n 
C 1 108 LEU 108 137 137 LEU LEU C . n 
C 1 109 SER 109 138 138 SER SER C . n 
C 1 110 LYS 110 139 139 LYS LYS C . n 
C 1 111 GLU 111 140 140 GLU GLU C . n 
C 1 112 TRP 112 141 141 TRP TRP C . n 
C 1 113 ALA 113 142 142 ALA ALA C . n 
C 1 114 LYS 114 143 143 LYS LYS C . n 
C 1 115 ARG 115 144 144 ARG ARG C . n 
C 1 116 ALA 116 145 145 ALA ALA C . n 
C 1 117 ALA 117 146 146 ALA ALA C . n 
C 1 118 LEU 118 147 147 LEU LEU C . n 
C 1 119 PRO 119 148 148 PRO PRO C . n 
C 1 120 SER 120 149 149 SER SER C . n 
C 1 121 HIS 121 150 150 HIS HIS C . n 
C 1 122 VAL 122 151 151 VAL VAL C . n 
C 1 123 VAL 123 152 152 VAL VAL C . n 
C 1 124 THR 124 153 153 THR THR C . n 
C 1 125 MET 125 154 154 MET MET C . n 
C 1 126 LEU 126 155 155 LEU LEU C . n 
C 1 127 ASP 127 156 156 ASP ASP C . n 
C 1 128 ASN 128 157 157 ASN ASN C . n 
C 1 129 PHE 129 158 158 PHE PHE C . n 
C 1 130 PRO 130 159 159 PRO PRO C . n 
C 1 131 THR 131 160 160 THR THR C . n 
C 1 132 ASN 132 161 161 ASN ASN C . n 
C 1 133 LEU 133 162 162 LEU LEU C . n 
C 1 134 HIS 134 163 163 HIS HIS C . n 
C 1 135 PRO 135 164 164 PRO PRO C . n 
C 1 136 MET 136 165 165 MET MET C . n 
C 1 137 SER 137 166 166 SER SER C . n 
C 1 138 GLN 138 167 167 GLN GLN C . n 
C 1 139 LEU 139 168 168 LEU LEU C . n 
C 1 140 SER 140 169 169 SER SER C . n 
C 1 141 ALA 141 170 170 ALA ALA C . n 
C 1 142 ALA 142 171 171 ALA ALA C . n 
C 1 143 VAL 143 172 172 VAL VAL C . n 
C 1 144 THR 144 173 173 THR THR C . n 
C 1 145 ALA 145 174 174 ALA ALA C . n 
C 1 146 LEU 146 175 175 LEU LEU C . n 
C 1 147 ASN 147 176 176 ASN ASN C . n 
C 1 148 SER 148 177 177 SER SER C . n 
C 1 149 GLU 149 178 178 GLU GLU C . n 
C 1 150 SER 150 179 179 SER SER C . n 
C 1 151 ASN 151 180 180 ASN ASN C . n 
C 1 152 PHE 152 181 181 PHE PHE C . n 
C 1 153 ALA 153 182 182 ALA ALA C . n 
C 1 154 ARG 154 183 183 ARG ARG C . n 
C 1 155 ALA 155 184 184 ALA ALA C . n 
C 1 156 TYR 156 185 185 TYR TYR C . n 
C 1 157 ALA 157 186 186 ALA ALA C . n 
C 1 158 GLN 158 187 187 GLN GLN C . n 
C 1 159 GLY 159 188 188 GLY GLY C . n 
C 1 160 ILE 160 189 189 ILE ILE C . n 
C 1 161 SER 161 190 190 SER SER C . n 
C 1 162 ARG 162 191 191 ARG ARG C . n 
C 1 163 THR 163 192 192 THR THR C . n 
C 1 164 LYS 164 193 193 LYS LYS C . n 
C 1 165 TYR 165 194 194 TYR TYR C . n 
C 1 166 TRP 166 195 195 TRP TRP C . n 
C 1 167 GLU 167 196 196 GLU GLU C . n 
C 1 168 LEU 168 197 197 LEU LEU C . n 
C 1 169 ILE 169 198 198 ILE ILE C . n 
C 1 170 TYR 170 199 199 TYR TYR C . n 
C 1 171 GLU 171 200 200 GLU GLU C . n 
C 1 172 ASP 172 201 201 ASP ASP C . n 
C 1 173 SER 173 202 202 SER SER C . n 
C 1 174 MET 174 203 203 MET MET C . n 
C 1 175 ASP 175 204 204 ASP ASP C . n 
C 1 176 LEU 176 205 205 LEU LEU C . n 
C 1 177 ILE 177 206 206 ILE ILE C . n 
C 1 178 ALA 178 207 207 ALA ALA C . n 
C 1 179 LYS 179 208 208 LYS LYS C . n 
C 1 180 LEU 180 209 209 LEU LEU C . n 
C 1 181 PRO 181 210 210 PRO PRO C . n 
C 1 182 CYS 182 211 211 CYS CYS C . n 
C 1 183 VAL 183 212 212 VAL VAL C . n 
C 1 184 ALA 184 213 213 ALA ALA C . n 
C 1 185 ALA 185 214 214 ALA ALA C . n 
C 1 186 LYS 186 215 215 LYS LYS C . n 
C 1 187 ILE 187 216 216 ILE ILE C . n 
C 1 188 TYR 188 217 217 TYR TYR C . n 
C 1 189 ARG 189 218 218 ARG ARG C . n 
C 1 190 ASN 190 219 219 ASN ASN C . n 
C 1 191 LEU 191 220 220 LEU LEU C . n 
C 1 192 TYR 192 221 221 TYR TYR C . n 
C 1 193 ARG 193 222 222 ARG ARG C . n 
C 1 194 GLU 194 223 223 GLU GLU C . n 
C 1 195 GLY 195 224 224 GLY GLY C . n 
C 1 196 SER 196 225 225 SER SER C . n 
C 1 197 GLY 197 226 226 GLY GLY C . n 
C 1 198 ILE 198 227 227 ILE ILE C . n 
C 1 199 GLY 199 228 228 GLY GLY C . n 
C 1 200 ALA 200 229 229 ALA ALA C . n 
C 1 201 ILE 201 230 230 ILE ILE C . n 
C 1 202 ASP 202 231 231 ASP ASP C . n 
C 1 203 SER 203 232 232 SER SER C . n 
C 1 204 ASN 204 233 233 ASN ASN C . n 
C 1 205 LEU 205 234 234 LEU LEU C . n 
C 1 206 ASP 206 235 235 ASP ASP C . n 
C 1 207 TRP 207 236 236 TRP TRP C . n 
C 1 208 SER 208 237 237 SER SER C . n 
C 1 209 HIS 209 238 238 HIS HIS C . n 
C 1 210 ASN 210 239 239 ASN ASN C . n 
C 1 211 PHE 211 240 240 PHE PHE C . n 
C 1 212 THR 212 241 241 THR THR C . n 
C 1 213 ASN 213 242 242 ASN ASN C . n 
C 1 214 MET 214 243 243 MET MET C . n 
C 1 215 LEU 215 244 244 LEU LEU C . n 
C 1 216 GLY 216 245 245 GLY GLY C . n 
C 1 217 TYR 217 246 246 TYR TYR C . n 
C 1 218 THR 218 247 247 THR THR C . n 
C 1 219 ASP 219 248 248 ASP ASP C . n 
C 1 220 HIS 220 249 249 HIS HIS C . n 
C 1 221 GLN 221 250 250 GLN GLN C . n 
C 1 222 PHE 222 251 251 PHE PHE C . n 
C 1 223 THR 223 252 252 THR THR C . n 
C 1 224 GLU 224 253 253 GLU GLU C . n 
C 1 225 LEU 225 254 254 LEU LEU C . n 
C 1 226 THR 226 255 255 THR THR C . n 
C 1 227 ARG 227 256 256 ARG ARG C . n 
C 1 228 LEU 228 257 257 LEU LEU C . n 
C 1 229 TYR 229 258 258 TYR TYR C . n 
C 1 230 LEU 230 259 259 LEU LEU C . n 
C 1 231 THR 231 260 260 THR THR C . n 
C 1 232 ILE 232 261 261 ILE ILE C . n 
C 1 233 HIS 233 262 262 HIS HIS C . n 
C 1 234 SER 234 263 263 SER SER C . n 
C 1 235 ASP 235 264 264 ASP ASP C . n 
C 1 236 HIS 236 265 265 HIS HIS C . n 
C 1 237 GLU 237 266 266 GLU GLU C . n 
C 1 238 GLY 238 267 267 GLY GLY C . n 
C 1 239 GLY 239 268 268 GLY GLY C . n 
C 1 240 ASN 240 269 269 ASN ASN C . n 
C 1 241 VAL 241 270 270 VAL VAL C . n 
C 1 242 SER 242 271 271 SER SER C . n 
C 1 243 ALA 243 272 272 ALA ALA C . n 
C 1 244 HIS 244 273 273 HIS HIS C . n 
C 1 245 THR 245 274 274 THR THR C . n 
C 1 246 SER 246 275 275 SER SER C . n 
C 1 247 HIS 247 276 276 HIS HIS C . n 
C 1 248 LEU 248 277 277 LEU LEU C . n 
C 1 249 VAL 249 278 278 VAL VAL C . n 
C 1 250 GLY 250 279 279 GLY GLY C . n 
C 1 251 SER 251 280 280 SER SER C . n 
C 1 252 ALA 252 281 281 ALA ALA C . n 
C 1 253 LEU 253 282 282 LEU LEU C . n 
C 1 254 SER 254 283 283 SER SER C . n 
C 1 255 ASP 255 284 284 ASP ASP C . n 
C 1 256 PRO 256 285 285 PRO PRO C . n 
C 1 257 TYR 257 286 286 TYR TYR C . n 
C 1 258 LEU 258 287 287 LEU LEU C . n 
C 1 259 SER 259 288 288 SER SER C . n 
C 1 260 PHE 260 289 289 PHE PHE C . n 
C 1 261 ALA 261 290 290 ALA ALA C . n 
C 1 262 ALA 262 291 291 ALA ALA C . n 
C 1 263 ALA 263 292 292 ALA ALA C . n 
C 1 264 MET 264 293 293 MET MET C . n 
C 1 265 ASN 265 294 294 ASN ASN C . n 
C 1 266 GLY 266 295 295 GLY GLY C . n 
C 1 267 LEU 267 296 296 LEU LEU C . n 
C 1 268 ALA 268 297 297 ALA ALA C . n 
C 1 269 GLY 269 298 298 GLY GLY C . n 
C 1 270 PRO 270 299 299 PRO PRO C . n 
C 1 271 LEU 271 300 300 LEU LEU C . n 
C 1 272 HIS 272 301 301 HIS HIS C . n 
C 1 273 GLY 273 302 302 GLY GLY C . n 
C 1 274 LEU 274 303 303 LEU LEU C . n 
C 1 275 ALA 275 304 304 ALA ALA C . n 
C 1 276 ASN 276 305 305 ASN ASN C . n 
C 1 277 GLN 277 306 306 GLN GLN C . n 
C 1 278 GLU 278 307 307 GLU GLU C . n 
C 1 279 VAL 279 308 308 VAL VAL C . n 
C 1 280 LEU 280 309 309 LEU LEU C . n 
C 1 281 VAL 281 310 310 VAL VAL C . n 
C 1 282 TRP 282 311 311 TRP TRP C . n 
C 1 283 LEU 283 312 312 LEU LEU C . n 
C 1 284 THR 284 313 313 THR THR C . n 
C 1 285 GLN 285 314 314 GLN GLN C . n 
C 1 286 LEU 286 315 315 LEU LEU C . n 
C 1 287 GLN 287 316 316 GLN GLN C . n 
C 1 288 LYS 288 317 317 LYS LYS C . n 
C 1 289 GLU 289 318 318 GLU GLU C . n 
C 1 290 VAL 290 319 319 VAL VAL C . n 
C 1 291 GLY 291 320 320 GLY GLY C . n 
C 1 292 LYS 292 321 321 LYS LYS C . n 
C 1 293 ASP 293 322 322 ASP ASP C . n 
C 1 294 VAL 294 323 323 VAL VAL C . n 
C 1 295 SER 295 324 324 SER SER C . n 
C 1 296 ASP 296 325 325 ASP ASP C . n 
C 1 297 GLU 297 326 326 GLU GLU C . n 
C 1 298 LYS 298 327 327 LYS LYS C . n 
C 1 299 LEU 299 328 328 LEU LEU C . n 
C 1 300 ARG 300 329 329 ARG ARG C . n 
C 1 301 ASP 301 330 330 ASP ASP C . n 
C 1 302 TYR 302 331 331 TYR TYR C . n 
C 1 303 ILE 303 332 332 ILE ILE C . n 
C 1 304 TRP 304 333 333 TRP TRP C . n 
C 1 305 ASN 305 334 334 ASN ASN C . n 
C 1 306 THR 306 335 335 THR THR C . n 
C 1 307 LEU 307 336 336 LEU LEU C . n 
C 1 308 ASN 308 337 337 ASN ASN C . n 
C 1 309 SER 309 338 338 SER SER C . n 
C 1 310 GLY 310 339 339 GLY GLY C . n 
C 1 311 ARG 311 340 340 ARG ARG C . n 
C 1 312 VAL 312 341 341 VAL VAL C . n 
C 1 313 VAL 313 342 342 VAL VAL C . n 
C 1 314 PRO 314 343 343 PRO PRO C . n 
C 1 315 GLY 315 344 344 GLY GLY C . n 
C 1 316 TYR 316 345 345 TYR TYR C . n 
C 1 317 GLY 317 346 346 GLY GLY C . n 
C 1 318 HIS 318 347 347 HIS HIS C . n 
C 1 319 ALA 319 348 348 ALA ALA C . n 
C 1 320 VAL 320 349 349 VAL VAL C . n 
C 1 321 LEU 321 350 350 LEU LEU C . n 
C 1 322 ARG 322 351 351 ARG ARG C . n 
C 1 323 LYS 323 352 352 LYS LYS C . n 
C 1 324 THR 324 353 353 THR THR C . n 
C 1 325 ASP 325 354 354 ASP ASP C . n 
C 1 326 PRO 326 355 355 PRO PRO C . n 
C 1 327 ARG 327 356 356 ARG ARG C . n 
C 1 328 TYR 328 357 357 TYR TYR C . n 
C 1 329 THR 329 358 358 THR THR C . n 
C 1 330 CYS 330 359 359 CYS CYS C . n 
C 1 331 GLN 331 360 360 GLN GLN C . n 
C 1 332 ARG 332 361 361 ARG ARG C . n 
C 1 333 GLU 333 362 362 GLU GLU C . n 
C 1 334 PHE 334 363 363 PHE PHE C . n 
C 1 335 ALA 335 364 364 ALA ALA C . n 
C 1 336 LEU 336 365 365 LEU LEU C . n 
C 1 337 LYS 337 366 366 LYS LYS C . n 
C 1 338 HIS 338 367 367 HIS HIS C . n 
C 1 339 LEU 339 368 368 LEU LEU C . n 
C 1 340 PRO 340 369 369 PRO PRO C . n 
C 1 341 ASN 341 370 370 ASN ASN C . n 
C 1 342 ASP 342 371 371 ASP ASP C . n 
C 1 343 PRO 343 372 372 PRO PRO C . n 
C 1 344 MET 344 373 373 MET MET C . n 
C 1 345 PHE 345 374 374 PHE PHE C . n 
C 1 346 LYS 346 375 375 LYS LYS C . n 
C 1 347 LEU 347 376 376 LEU LEU C . n 
C 1 348 VAL 348 377 377 VAL VAL C . n 
C 1 349 ALA 349 378 378 ALA ALA C . n 
C 1 350 GLN 350 379 379 GLN GLN C . n 
C 1 351 LEU 351 380 380 LEU LEU C . n 
C 1 352 TYR 352 381 381 TYR TYR C . n 
C 1 353 LYS 353 382 382 LYS LYS C . n 
C 1 354 ILE 354 383 383 ILE ILE C . n 
C 1 355 VAL 355 384 384 VAL VAL C . n 
C 1 356 PRO 356 385 385 PRO PRO C . n 
C 1 357 ASN 357 386 386 ASN ASN C . n 
C 1 358 VAL 358 387 387 VAL VAL C . n 
C 1 359 LEU 359 388 388 LEU LEU C . n 
C 1 360 LEU 360 389 389 LEU LEU C . n 
C 1 361 GLU 361 390 390 GLU GLU C . n 
C 1 362 GLN 362 391 391 GLN GLN C . n 
C 1 363 GLY 363 392 392 GLY GLY C . n 
C 1 364 LYS 364 393 393 LYS LYS C . n 
C 1 365 ALA 365 394 394 ALA ALA C . n 
C 1 366 LYS 366 395 395 LYS LYS C . n 
C 1 367 ASN 367 396 396 ASN ASN C . n 
C 1 368 PRO 368 397 397 PRO PRO C . n 
C 1 369 TRP 369 398 398 TRP TRP C . n 
C 1 370 PRO 370 399 399 PRO PRO C . n 
C 1 371 ASN 371 400 400 ASN ASN C . n 
C 1 372 VAL 372 401 401 VAL VAL C . n 
C 1 373 ASP 373 402 402 ASP ASP C . n 
C 1 374 ALA 374 403 403 ALA ALA C . n 
C 1 375 HIS 375 404 404 HIS HIS C . n 
C 1 376 SER 376 405 405 SER SER C . n 
C 1 377 GLY 377 406 406 GLY GLY C . n 
C 1 378 VAL 378 407 407 VAL VAL C . n 
C 1 379 LEU 379 408 408 LEU LEU C . n 
C 1 380 LEU 380 409 409 LEU LEU C . n 
C 1 381 GLN 381 410 410 GLN GLN C . n 
C 1 382 TYR 382 411 411 TYR TYR C . n 
C 1 383 TYR 383 412 412 TYR TYR C . n 
C 1 384 GLY 384 413 413 GLY GLY C . n 
C 1 385 MET 385 414 414 MET MET C . n 
C 1 386 THR 386 415 415 THR THR C . n 
C 1 387 GLU 387 416 416 GLU GLU C . n 
C 1 388 MET 388 417 417 MET MET C . n 
C 1 389 ASN 389 418 418 ASN ASN C . n 
C 1 390 TYR 390 419 419 TYR TYR C . n 
C 1 391 TYR 391 420 420 TYR TYR C . n 
C 1 392 THR 392 421 421 THR THR C . n 
C 1 393 VAL 393 422 422 VAL VAL C . n 
C 1 394 LEU 394 423 423 LEU LEU C . n 
C 1 395 PHE 395 424 424 PHE PHE C . n 
C 1 396 GLY 396 425 425 GLY GLY C . n 
C 1 397 VAL 397 426 426 VAL VAL C . n 
C 1 398 SER 398 427 427 SER SER C . n 
C 1 399 ARG 399 428 428 ARG ARG C . n 
C 1 400 ALA 400 429 429 ALA ALA C . n 
C 1 401 LEU 401 430 430 LEU LEU C . n 
C 1 402 GLY 402 431 431 GLY GLY C . n 
C 1 403 VAL 403 432 432 VAL VAL C . n 
C 1 404 LEU 404 433 433 LEU LEU C . n 
C 1 405 ALA 405 434 434 ALA ALA C . n 
C 1 406 GLN 406 435 435 GLN GLN C . n 
C 1 407 LEU 407 436 436 LEU LEU C . n 
C 1 408 ILE 408 437 437 ILE ILE C . n 
C 1 409 TRP 409 438 438 TRP TRP C . n 
C 1 410 SER 410 439 439 SER SER C . n 
C 1 411 ARG 411 440 440 ARG ARG C . n 
C 1 412 ALA 412 441 441 ALA ALA C . n 
C 1 413 LEU 413 442 442 LEU LEU C . n 
C 1 414 GLY 414 443 443 GLY GLY C . n 
C 1 415 PHE 415 444 444 PHE PHE C . n 
C 1 416 PRO 416 445 445 PRO PRO C . n 
C 1 417 LEU 417 446 446 LEU LEU C . n 
C 1 418 GLU 418 447 447 GLU GLU C . n 
C 1 419 ARG 419 448 448 ARG ARG C . n 
C 1 420 PRO 420 449 449 PRO PRO C . n 
C 1 421 LYS 421 450 450 LYS LYS C . n 
C 1 422 SER 422 451 451 SER SER C . n 
C 1 423 MET 423 452 452 MET MET C . n 
C 1 424 SER 424 453 453 SER SER C . n 
C 1 425 THR 425 454 454 THR THR C . n 
C 1 426 GLU 426 455 455 GLU GLU C . n 
C 1 427 GLY 427 456 456 GLY GLY C . n 
C 1 428 LEU 428 457 457 LEU LEU C . n 
C 1 429 MET 429 458 458 MET MET C . n 
C 1 430 LYS 430 459 459 LYS LYS C . n 
C 1 431 PHE 431 460 460 PHE PHE C . n 
C 1 432 VAL 432 461 461 VAL VAL C . n 
C 1 433 ASP 433 462 462 ASP ASP C . n 
C 1 434 SER 434 463 463 SER SER C . n 
D 1 1   SER 1   30  30  SER SER D . n 
D 1 2   THR 2   31  31  THR THR D . n 
D 1 3   ASN 3   32  32  ASN ASN D . n 
D 1 4   LEU 4   33  33  LEU LEU D . n 
D 1 5   LYS 5   34  34  LYS LYS D . n 
D 1 6   ASP 6   35  35  ASP ASP D . n 
D 1 7   ILE 7   36  36  ILE ILE D . n 
D 1 8   LEU 8   37  37  LEU LEU D . n 
D 1 9   ALA 9   38  38  ALA ALA D . n 
D 1 10  ASP 10  39  39  ASP ASP D . n 
D 1 11  LEU 11  40  40  LEU LEU D . n 
D 1 12  ILE 12  41  41  ILE ILE D . n 
D 1 13  PRO 13  42  42  PRO PRO D . n 
D 1 14  LYS 14  43  43  LYS LYS D . n 
D 1 15  GLU 15  44  44  GLU GLU D . n 
D 1 16  GLN 16  45  45  GLN GLN D . n 
D 1 17  ALA 17  46  46  ALA ALA D . n 
D 1 18  ARG 18  47  47  ARG ARG D . n 
D 1 19  ILE 19  48  48  ILE ILE D . n 
D 1 20  LYS 20  49  49  LYS LYS D . n 
D 1 21  THR 21  50  50  THR THR D . n 
D 1 22  PHE 22  51  51  PHE PHE D . n 
D 1 23  ARG 23  52  52  ARG ARG D . n 
D 1 24  GLN 24  53  53  GLN GLN D . n 
D 1 25  GLN 25  54  54  GLN GLN D . n 
D 1 26  HIS 26  55  55  HIS HIS D . n 
D 1 27  GLY 27  56  56  GLY GLY D . n 
D 1 28  LYS 28  57  57  LYS LYS D . n 
D 1 29  THR 29  58  58  THR THR D . n 
D 1 30  VAL 30  59  59  VAL VAL D . n 
D 1 31  VAL 31  60  60  VAL VAL D . n 
D 1 32  GLY 32  61  61  GLY GLY D . n 
D 1 33  GLN 33  62  62  GLN GLN D . n 
D 1 34  ILE 34  63  63  ILE ILE D . n 
D 1 35  THR 35  64  64  THR THR D . n 
D 1 36  VAL 36  65  65  VAL VAL D . n 
D 1 37  ASP 37  66  66  ASP ASP D . n 
D 1 38  MET 38  67  67  MET MET D . n 
D 1 39  MET 39  68  68  MET MET D . n 
D 1 40  TYR 40  69  69  TYR TYR D . n 
D 1 41  GLY 41  70  70  GLY GLY D . n 
D 1 42  GLY 42  71  71  GLY GLY D . n 
D 1 43  MET 43  72  72  MET MET D . n 
D 1 44  ARG 44  73  73  ARG ARG D . n 
D 1 45  GLY 45  74  74  GLY GLY D . n 
D 1 46  MET 46  75  75  MET MET D . n 
D 1 47  LYS 47  76  76  LYS LYS D . n 
D 1 48  GLY 48  77  77  GLY GLY D . n 
D 1 49  LEU 49  78  78  LEU LEU D . n 
D 1 50  VAL 50  79  79  VAL VAL D . n 
D 1 51  TYR 51  80  80  TYR TYR D . n 
D 1 52  GLU 52  81  81  GLU GLU D . n 
D 1 53  THR 53  82  82  THR THR D . n 
D 1 54  SER 54  83  83  SER SER D . n 
D 1 55  VAL 55  84  84  VAL VAL D . n 
D 1 56  LEU 56  85  85  LEU LEU D . n 
D 1 57  ASP 57  86  86  ASP ASP D . n 
D 1 58  PRO 58  87  87  PRO PRO D . n 
D 1 59  ASP 59  88  88  ASP ASP D . n 
D 1 60  GLU 60  89  89  GLU GLU D . n 
D 1 61  GLY 61  90  90  GLY GLY D . n 
D 1 62  ILE 62  91  91  ILE ILE D . n 
D 1 63  ARG 63  92  92  ARG ARG D . n 
D 1 64  PHE 64  93  93  PHE PHE D . n 
D 1 65  ARG 65  94  94  ARG ARG D . n 
D 1 66  GLY 66  95  95  GLY GLY D . n 
D 1 67  PHE 67  96  96  PHE PHE D . n 
D 1 68  SER 68  97  97  SER SER D . n 
D 1 69  ILE 69  98  98  ILE ILE D . n 
D 1 70  PRO 70  99  99  PRO PRO D . n 
D 1 71  GLU 71  100 100 GLU GLU D . n 
D 1 72  CYS 72  101 101 CYS CYS D . n 
D 1 73  GLN 73  102 102 GLN GLN D . n 
D 1 74  LYS 74  103 103 LYS LYS D . n 
D 1 75  LEU 75  104 104 LEU LEU D . n 
D 1 76  LEU 76  105 105 LEU LEU D . n 
D 1 77  PRO 77  106 106 PRO PRO D . n 
D 1 78  LYS 78  107 107 LYS LYS D . n 
D 1 79  ALA 79  108 108 ALA ALA D . n 
D 1 80  LYS 80  109 109 LYS LYS D . n 
D 1 81  GLY 81  110 110 GLY GLY D . n 
D 1 82  GLY 82  111 111 GLY GLY D . n 
D 1 83  GLU 83  112 112 GLU GLU D . n 
D 1 84  GLU 84  113 113 GLU GLU D . n 
D 1 85  PRO 85  114 114 PRO PRO D . n 
D 1 86  LEU 86  115 115 LEU LEU D . n 
D 1 87  PRO 87  116 116 PRO PRO D . n 
D 1 88  GLU 88  117 117 GLU GLU D . n 
D 1 89  GLY 89  118 118 GLY GLY D . n 
D 1 90  LEU 90  119 119 LEU LEU D . n 
D 1 91  PHE 91  120 120 PHE PHE D . n 
D 1 92  TRP 92  121 121 TRP TRP D . n 
D 1 93  LEU 93  122 122 LEU LEU D . n 
D 1 94  LEU 94  123 123 LEU LEU D . n 
D 1 95  VAL 95  124 124 VAL VAL D . n 
D 1 96  THR 96  125 125 THR THR D . n 
D 1 97  GLY 97  126 126 GLY GLY D . n 
D 1 98  HIS 98  127 127 HIS HIS D . n 
D 1 99  ILE 99  128 128 ILE ILE D . n 
D 1 100 PRO 100 129 129 PRO PRO D . n 
D 1 101 THR 101 130 130 THR THR D . n 
D 1 102 GLU 102 131 131 GLU GLU D . n 
D 1 103 GLU 103 132 132 GLU GLU D . n 
D 1 104 GLN 104 133 133 GLN GLN D . n 
D 1 105 VAL 105 134 134 VAL VAL D . n 
D 1 106 SER 106 135 135 SER SER D . n 
D 1 107 TRP 107 136 136 TRP TRP D . n 
D 1 108 LEU 108 137 137 LEU LEU D . n 
D 1 109 SER 109 138 138 SER SER D . n 
D 1 110 LYS 110 139 139 LYS LYS D . n 
D 1 111 GLU 111 140 140 GLU GLU D . n 
D 1 112 TRP 112 141 141 TRP TRP D . n 
D 1 113 ALA 113 142 142 ALA ALA D . n 
D 1 114 LYS 114 143 143 LYS LYS D . n 
D 1 115 ARG 115 144 144 ARG ARG D . n 
D 1 116 ALA 116 145 145 ALA ALA D . n 
D 1 117 ALA 117 146 146 ALA ALA D . n 
D 1 118 LEU 118 147 147 LEU LEU D . n 
D 1 119 PRO 119 148 148 PRO PRO D . n 
D 1 120 SER 120 149 149 SER SER D . n 
D 1 121 HIS 121 150 150 HIS HIS D . n 
D 1 122 VAL 122 151 151 VAL VAL D . n 
D 1 123 VAL 123 152 152 VAL VAL D . n 
D 1 124 THR 124 153 153 THR THR D . n 
D 1 125 MET 125 154 154 MET MET D . n 
D 1 126 LEU 126 155 155 LEU LEU D . n 
D 1 127 ASP 127 156 156 ASP ASP D . n 
D 1 128 ASN 128 157 157 ASN ASN D . n 
D 1 129 PHE 129 158 158 PHE PHE D . n 
D 1 130 PRO 130 159 159 PRO PRO D . n 
D 1 131 THR 131 160 160 THR THR D . n 
D 1 132 ASN 132 161 161 ASN ASN D . n 
D 1 133 LEU 133 162 162 LEU LEU D . n 
D 1 134 HIS 134 163 163 HIS HIS D . n 
D 1 135 PRO 135 164 164 PRO PRO D . n 
D 1 136 MET 136 165 165 MET MET D . n 
D 1 137 SER 137 166 166 SER SER D . n 
D 1 138 GLN 138 167 167 GLN GLN D . n 
D 1 139 LEU 139 168 168 LEU LEU D . n 
D 1 140 SER 140 169 169 SER SER D . n 
D 1 141 ALA 141 170 170 ALA ALA D . n 
D 1 142 ALA 142 171 171 ALA ALA D . n 
D 1 143 VAL 143 172 172 VAL VAL D . n 
D 1 144 THR 144 173 173 THR THR D . n 
D 1 145 ALA 145 174 174 ALA ALA D . n 
D 1 146 LEU 146 175 175 LEU LEU D . n 
D 1 147 ASN 147 176 176 ASN ASN D . n 
D 1 148 SER 148 177 177 SER SER D . n 
D 1 149 GLU 149 178 178 GLU GLU D . n 
D 1 150 SER 150 179 179 SER SER D . n 
D 1 151 ASN 151 180 180 ASN ASN D . n 
D 1 152 PHE 152 181 181 PHE PHE D . n 
D 1 153 ALA 153 182 182 ALA ALA D . n 
D 1 154 ARG 154 183 183 ARG ARG D . n 
D 1 155 ALA 155 184 184 ALA ALA D . n 
D 1 156 TYR 156 185 185 TYR TYR D . n 
D 1 157 ALA 157 186 186 ALA ALA D . n 
D 1 158 GLN 158 187 187 GLN GLN D . n 
D 1 159 GLY 159 188 188 GLY GLY D . n 
D 1 160 ILE 160 189 189 ILE ILE D . n 
D 1 161 SER 161 190 190 SER SER D . n 
D 1 162 ARG 162 191 191 ARG ARG D . n 
D 1 163 THR 163 192 192 THR THR D . n 
D 1 164 LYS 164 193 193 LYS LYS D . n 
D 1 165 TYR 165 194 194 TYR TYR D . n 
D 1 166 TRP 166 195 195 TRP TRP D . n 
D 1 167 GLU 167 196 196 GLU GLU D . n 
D 1 168 LEU 168 197 197 LEU LEU D . n 
D 1 169 ILE 169 198 198 ILE ILE D . n 
D 1 170 TYR 170 199 199 TYR TYR D . n 
D 1 171 GLU 171 200 200 GLU GLU D . n 
D 1 172 ASP 172 201 201 ASP ASP D . n 
D 1 173 SER 173 202 202 SER SER D . n 
D 1 174 MET 174 203 203 MET MET D . n 
D 1 175 ASP 175 204 204 ASP ASP D . n 
D 1 176 LEU 176 205 205 LEU LEU D . n 
D 1 177 ILE 177 206 206 ILE ILE D . n 
D 1 178 ALA 178 207 207 ALA ALA D . n 
D 1 179 LYS 179 208 208 LYS LYS D . n 
D 1 180 LEU 180 209 209 LEU LEU D . n 
D 1 181 PRO 181 210 210 PRO PRO D . n 
D 1 182 CYS 182 211 211 CYS CYS D . n 
D 1 183 VAL 183 212 212 VAL VAL D . n 
D 1 184 ALA 184 213 213 ALA ALA D . n 
D 1 185 ALA 185 214 214 ALA ALA D . n 
D 1 186 LYS 186 215 215 LYS LYS D . n 
D 1 187 ILE 187 216 216 ILE ILE D . n 
D 1 188 TYR 188 217 217 TYR TYR D . n 
D 1 189 ARG 189 218 218 ARG ARG D . n 
D 1 190 ASN 190 219 219 ASN ASN D . n 
D 1 191 LEU 191 220 220 LEU LEU D . n 
D 1 192 TYR 192 221 221 TYR TYR D . n 
D 1 193 ARG 193 222 222 ARG ARG D . n 
D 1 194 GLU 194 223 223 GLU GLU D . n 
D 1 195 GLY 195 224 224 GLY GLY D . n 
D 1 196 SER 196 225 225 SER SER D . n 
D 1 197 GLY 197 226 226 GLY GLY D . n 
D 1 198 ILE 198 227 227 ILE ILE D . n 
D 1 199 GLY 199 228 228 GLY GLY D . n 
D 1 200 ALA 200 229 229 ALA ALA D . n 
D 1 201 ILE 201 230 230 ILE ILE D . n 
D 1 202 ASP 202 231 231 ASP ASP D . n 
D 1 203 SER 203 232 232 SER SER D . n 
D 1 204 ASN 204 233 233 ASN ASN D . n 
D 1 205 LEU 205 234 234 LEU LEU D . n 
D 1 206 ASP 206 235 235 ASP ASP D . n 
D 1 207 TRP 207 236 236 TRP TRP D . n 
D 1 208 SER 208 237 237 SER SER D . n 
D 1 209 HIS 209 238 238 HIS HIS D . n 
D 1 210 ASN 210 239 239 ASN ASN D . n 
D 1 211 PHE 211 240 240 PHE PHE D . n 
D 1 212 THR 212 241 241 THR THR D . n 
D 1 213 ASN 213 242 242 ASN ASN D . n 
D 1 214 MET 214 243 243 MET MET D . n 
D 1 215 LEU 215 244 244 LEU LEU D . n 
D 1 216 GLY 216 245 245 GLY GLY D . n 
D 1 217 TYR 217 246 246 TYR TYR D . n 
D 1 218 THR 218 247 247 THR THR D . n 
D 1 219 ASP 219 248 248 ASP ASP D . n 
D 1 220 HIS 220 249 249 HIS HIS D . n 
D 1 221 GLN 221 250 250 GLN GLN D . n 
D 1 222 PHE 222 251 251 PHE PHE D . n 
D 1 223 THR 223 252 252 THR THR D . n 
D 1 224 GLU 224 253 253 GLU GLU D . n 
D 1 225 LEU 225 254 254 LEU LEU D . n 
D 1 226 THR 226 255 255 THR THR D . n 
D 1 227 ARG 227 256 256 ARG ARG D . n 
D 1 228 LEU 228 257 257 LEU LEU D . n 
D 1 229 TYR 229 258 258 TYR TYR D . n 
D 1 230 LEU 230 259 259 LEU LEU D . n 
D 1 231 THR 231 260 260 THR THR D . n 
D 1 232 ILE 232 261 261 ILE ILE D . n 
D 1 233 HIS 233 262 262 HIS HIS D . n 
D 1 234 SER 234 263 263 SER SER D . n 
D 1 235 ASP 235 264 264 ASP ASP D . n 
D 1 236 HIS 236 265 265 HIS HIS D . n 
D 1 237 GLU 237 266 266 GLU GLU D . n 
D 1 238 GLY 238 267 267 GLY GLY D . n 
D 1 239 GLY 239 268 268 GLY GLY D . n 
D 1 240 ASN 240 269 269 ASN ASN D . n 
D 1 241 VAL 241 270 270 VAL VAL D . n 
D 1 242 SER 242 271 271 SER SER D . n 
D 1 243 ALA 243 272 272 ALA ALA D . n 
D 1 244 HIS 244 273 273 HIS HIS D . n 
D 1 245 THR 245 274 274 THR THR D . n 
D 1 246 SER 246 275 275 SER SER D . n 
D 1 247 HIS 247 276 276 HIS HIS D . n 
D 1 248 LEU 248 277 277 LEU LEU D . n 
D 1 249 VAL 249 278 278 VAL VAL D . n 
D 1 250 GLY 250 279 279 GLY GLY D . n 
D 1 251 SER 251 280 280 SER SER D . n 
D 1 252 ALA 252 281 281 ALA ALA D . n 
D 1 253 LEU 253 282 282 LEU LEU D . n 
D 1 254 SER 254 283 283 SER SER D . n 
D 1 255 ASP 255 284 284 ASP ASP D . n 
D 1 256 PRO 256 285 285 PRO PRO D . n 
D 1 257 TYR 257 286 286 TYR TYR D . n 
D 1 258 LEU 258 287 287 LEU LEU D . n 
D 1 259 SER 259 288 288 SER SER D . n 
D 1 260 PHE 260 289 289 PHE PHE D . n 
D 1 261 ALA 261 290 290 ALA ALA D . n 
D 1 262 ALA 262 291 291 ALA ALA D . n 
D 1 263 ALA 263 292 292 ALA ALA D . n 
D 1 264 MET 264 293 293 MET MET D . n 
D 1 265 ASN 265 294 294 ASN ASN D . n 
D 1 266 GLY 266 295 295 GLY GLY D . n 
D 1 267 LEU 267 296 296 LEU LEU D . n 
D 1 268 ALA 268 297 297 ALA ALA D . n 
D 1 269 GLY 269 298 298 GLY GLY D . n 
D 1 270 PRO 270 299 299 PRO PRO D . n 
D 1 271 LEU 271 300 300 LEU LEU D . n 
D 1 272 HIS 272 301 301 HIS HIS D . n 
D 1 273 GLY 273 302 302 GLY GLY D . n 
D 1 274 LEU 274 303 303 LEU LEU D . n 
D 1 275 ALA 275 304 304 ALA ALA D . n 
D 1 276 ASN 276 305 305 ASN ASN D . n 
D 1 277 GLN 277 306 306 GLN GLN D . n 
D 1 278 GLU 278 307 307 GLU GLU D . n 
D 1 279 VAL 279 308 308 VAL VAL D . n 
D 1 280 LEU 280 309 309 LEU LEU D . n 
D 1 281 VAL 281 310 310 VAL VAL D . n 
D 1 282 TRP 282 311 311 TRP TRP D . n 
D 1 283 LEU 283 312 312 LEU LEU D . n 
D 1 284 THR 284 313 313 THR THR D . n 
D 1 285 GLN 285 314 314 GLN GLN D . n 
D 1 286 LEU 286 315 315 LEU LEU D . n 
D 1 287 GLN 287 316 316 GLN GLN D . n 
D 1 288 LYS 288 317 317 LYS LYS D . n 
D 1 289 GLU 289 318 318 GLU GLU D . n 
D 1 290 VAL 290 319 319 VAL VAL D . n 
D 1 291 GLY 291 320 320 GLY GLY D . n 
D 1 292 LYS 292 321 321 LYS LYS D . n 
D 1 293 ASP 293 322 322 ASP ASP D . n 
D 1 294 VAL 294 323 323 VAL VAL D . n 
D 1 295 SER 295 324 324 SER SER D . n 
D 1 296 ASP 296 325 325 ASP ASP D . n 
D 1 297 GLU 297 326 326 GLU GLU D . n 
D 1 298 LYS 298 327 327 LYS LYS D . n 
D 1 299 LEU 299 328 328 LEU LEU D . n 
D 1 300 ARG 300 329 329 ARG ARG D . n 
D 1 301 ASP 301 330 330 ASP ASP D . n 
D 1 302 TYR 302 331 331 TYR TYR D . n 
D 1 303 ILE 303 332 332 ILE ILE D . n 
D 1 304 TRP 304 333 333 TRP TRP D . n 
D 1 305 ASN 305 334 334 ASN ASN D . n 
D 1 306 THR 306 335 335 THR THR D . n 
D 1 307 LEU 307 336 336 LEU LEU D . n 
D 1 308 ASN 308 337 337 ASN ASN D . n 
D 1 309 SER 309 338 338 SER SER D . n 
D 1 310 GLY 310 339 339 GLY GLY D . n 
D 1 311 ARG 311 340 340 ARG ARG D . n 
D 1 312 VAL 312 341 341 VAL VAL D . n 
D 1 313 VAL 313 342 342 VAL VAL D . n 
D 1 314 PRO 314 343 343 PRO PRO D . n 
D 1 315 GLY 315 344 344 GLY GLY D . n 
D 1 316 TYR 316 345 345 TYR TYR D . n 
D 1 317 GLY 317 346 346 GLY GLY D . n 
D 1 318 HIS 318 347 347 HIS HIS D . n 
D 1 319 ALA 319 348 348 ALA ALA D . n 
D 1 320 VAL 320 349 349 VAL VAL D . n 
D 1 321 LEU 321 350 350 LEU LEU D . n 
D 1 322 ARG 322 351 351 ARG ARG D . n 
D 1 323 LYS 323 352 352 LYS LYS D . n 
D 1 324 THR 324 353 353 THR THR D . n 
D 1 325 ASP 325 354 354 ASP ASP D . n 
D 1 326 PRO 326 355 355 PRO PRO D . n 
D 1 327 ARG 327 356 356 ARG ARG D . n 
D 1 328 TYR 328 357 357 TYR TYR D . n 
D 1 329 THR 329 358 358 THR THR D . n 
D 1 330 CYS 330 359 359 CYS CYS D . n 
D 1 331 GLN 331 360 360 GLN GLN D . n 
D 1 332 ARG 332 361 361 ARG ARG D . n 
D 1 333 GLU 333 362 362 GLU GLU D . n 
D 1 334 PHE 334 363 363 PHE PHE D . n 
D 1 335 ALA 335 364 364 ALA ALA D . n 
D 1 336 LEU 336 365 365 LEU LEU D . n 
D 1 337 LYS 337 366 366 LYS LYS D . n 
D 1 338 HIS 338 367 367 HIS HIS D . n 
D 1 339 LEU 339 368 368 LEU LEU D . n 
D 1 340 PRO 340 369 369 PRO PRO D . n 
D 1 341 ASN 341 370 370 ASN ASN D . n 
D 1 342 ASP 342 371 371 ASP ASP D . n 
D 1 343 PRO 343 372 372 PRO PRO D . n 
D 1 344 MET 344 373 373 MET MET D . n 
D 1 345 PHE 345 374 374 PHE PHE D . n 
D 1 346 LYS 346 375 375 LYS LYS D . n 
D 1 347 LEU 347 376 376 LEU LEU D . n 
D 1 348 VAL 348 377 377 VAL VAL D . n 
D 1 349 ALA 349 378 378 ALA ALA D . n 
D 1 350 GLN 350 379 379 GLN GLN D . n 
D 1 351 LEU 351 380 380 LEU LEU D . n 
D 1 352 TYR 352 381 381 TYR TYR D . n 
D 1 353 LYS 353 382 382 LYS LYS D . n 
D 1 354 ILE 354 383 383 ILE ILE D . n 
D 1 355 VAL 355 384 384 VAL VAL D . n 
D 1 356 PRO 356 385 385 PRO PRO D . n 
D 1 357 ASN 357 386 386 ASN ASN D . n 
D 1 358 VAL 358 387 387 VAL VAL D . n 
D 1 359 LEU 359 388 388 LEU LEU D . n 
D 1 360 LEU 360 389 389 LEU LEU D . n 
D 1 361 GLU 361 390 390 GLU GLU D . n 
D 1 362 GLN 362 391 391 GLN GLN D . n 
D 1 363 GLY 363 392 392 GLY GLY D . n 
D 1 364 LYS 364 393 393 LYS LYS D . n 
D 1 365 ALA 365 394 394 ALA ALA D . n 
D 1 366 LYS 366 395 395 LYS LYS D . n 
D 1 367 ASN 367 396 396 ASN ASN D . n 
D 1 368 PRO 368 397 397 PRO PRO D . n 
D 1 369 TRP 369 398 398 TRP TRP D . n 
D 1 370 PRO 370 399 399 PRO PRO D . n 
D 1 371 ASN 371 400 400 ASN ASN D . n 
D 1 372 VAL 372 401 401 VAL VAL D . n 
D 1 373 ASP 373 402 402 ASP ASP D . n 
D 1 374 ALA 374 403 403 ALA ALA D . n 
D 1 375 HIS 375 404 404 HIS HIS D . n 
D 1 376 SER 376 405 405 SER SER D . n 
D 1 377 GLY 377 406 406 GLY GLY D . n 
D 1 378 VAL 378 407 407 VAL VAL D . n 
D 1 379 LEU 379 408 408 LEU LEU D . n 
D 1 380 LEU 380 409 409 LEU LEU D . n 
D 1 381 GLN 381 410 410 GLN GLN D . n 
D 1 382 TYR 382 411 411 TYR TYR D . n 
D 1 383 TYR 383 412 412 TYR TYR D . n 
D 1 384 GLY 384 413 413 GLY GLY D . n 
D 1 385 MET 385 414 414 MET MET D . n 
D 1 386 THR 386 415 415 THR THR D . n 
D 1 387 GLU 387 416 416 GLU GLU D . n 
D 1 388 MET 388 417 417 MET MET D . n 
D 1 389 ASN 389 418 418 ASN ASN D . n 
D 1 390 TYR 390 419 419 TYR TYR D . n 
D 1 391 TYR 391 420 420 TYR TYR D . n 
D 1 392 THR 392 421 421 THR THR D . n 
D 1 393 VAL 393 422 422 VAL VAL D . n 
D 1 394 LEU 394 423 423 LEU LEU D . n 
D 1 395 PHE 395 424 424 PHE PHE D . n 
D 1 396 GLY 396 425 425 GLY GLY D . n 
D 1 397 VAL 397 426 426 VAL VAL D . n 
D 1 398 SER 398 427 427 SER SER D . n 
D 1 399 ARG 399 428 428 ARG ARG D . n 
D 1 400 ALA 400 429 429 ALA ALA D . n 
D 1 401 LEU 401 430 430 LEU LEU D . n 
D 1 402 GLY 402 431 431 GLY GLY D . n 
D 1 403 VAL 403 432 432 VAL VAL D . n 
D 1 404 LEU 404 433 433 LEU LEU D . n 
D 1 405 ALA 405 434 434 ALA ALA D . n 
D 1 406 GLN 406 435 435 GLN GLN D . n 
D 1 407 LEU 407 436 436 LEU LEU D . n 
D 1 408 ILE 408 437 437 ILE ILE D . n 
D 1 409 TRP 409 438 438 TRP TRP D . n 
D 1 410 SER 410 439 439 SER SER D . n 
D 1 411 ARG 411 440 440 ARG ARG D . n 
D 1 412 ALA 412 441 441 ALA ALA D . n 
D 1 413 LEU 413 442 442 LEU LEU D . n 
D 1 414 GLY 414 443 443 GLY GLY D . n 
D 1 415 PHE 415 444 444 PHE PHE D . n 
D 1 416 PRO 416 445 445 PRO PRO D . n 
D 1 417 LEU 417 446 446 LEU LEU D . n 
D 1 418 GLU 418 447 447 GLU GLU D . n 
D 1 419 ARG 419 448 448 ARG ARG D . n 
D 1 420 PRO 420 449 449 PRO PRO D . n 
D 1 421 LYS 421 450 450 LYS LYS D . n 
D 1 422 SER 422 451 451 SER SER D . n 
D 1 423 MET 423 452 452 MET MET D . n 
D 1 424 SER 424 453 453 SER SER D . n 
D 1 425 THR 425 454 454 THR THR D . n 
D 1 426 GLU 426 455 455 GLU GLU D . n 
D 1 427 GLY 427 456 456 GLY GLY D . n 
D 1 428 LEU 428 457 457 LEU LEU D . n 
D 1 429 MET 429 458 458 MET MET D . n 
D 1 430 LYS 430 459 459 LYS LYS D . n 
D 1 431 PHE 431 460 460 PHE PHE D . n 
D 1 432 VAL 432 461 461 VAL VAL D . n 
D 1 433 ASP 433 462 462 ASP ASP D . n 
D 1 434 SER 434 463 463 SER SER D . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E 2 CIT 1   501 501 CIT CIT A . 
F 2 CIT 1   501 501 CIT CIT B . 
G 2 CIT 1   501 501 CIT CIT C . 
H 2 CIT 1   501 501 CIT CIT D . 
I 3 HOH 1   601 272 HOH HOH A . 
I 3 HOH 2   602 821 HOH HOH A . 
I 3 HOH 3   603 633 HOH HOH A . 
I 3 HOH 4   604 197 HOH HOH A . 
I 3 HOH 5   605 478 HOH HOH A . 
I 3 HOH 6   606 809 HOH HOH A . 
I 3 HOH 7   607 758 HOH HOH A . 
I 3 HOH 8   608 613 HOH HOH A . 
I 3 HOH 9   609 212 HOH HOH A . 
I 3 HOH 10  610 640 HOH HOH A . 
I 3 HOH 11  611 315 HOH HOH A . 
I 3 HOH 12  612 745 HOH HOH A . 
I 3 HOH 13  613 677 HOH HOH A . 
I 3 HOH 14  614 233 HOH HOH A . 
I 3 HOH 15  615 775 HOH HOH A . 
I 3 HOH 16  616 251 HOH HOH A . 
I 3 HOH 17  617 148 HOH HOH A . 
I 3 HOH 18  618 59  HOH HOH A . 
I 3 HOH 19  619 214 HOH HOH A . 
I 3 HOH 20  620 185 HOH HOH A . 
I 3 HOH 21  621 530 HOH HOH A . 
I 3 HOH 22  622 760 HOH HOH A . 
I 3 HOH 23  623 81  HOH HOH A . 
I 3 HOH 24  624 606 HOH HOH A . 
I 3 HOH 25  625 105 HOH HOH A . 
I 3 HOH 26  626 720 HOH HOH A . 
I 3 HOH 27  627 672 HOH HOH A . 
I 3 HOH 28  628 408 HOH HOH A . 
I 3 HOH 29  629 285 HOH HOH A . 
I 3 HOH 30  630 13  HOH HOH A . 
I 3 HOH 31  631 320 HOH HOH A . 
I 3 HOH 32  632 363 HOH HOH A . 
I 3 HOH 33  633 585 HOH HOH A . 
I 3 HOH 34  634 291 HOH HOH A . 
I 3 HOH 35  635 521 HOH HOH A . 
I 3 HOH 36  636 571 HOH HOH A . 
I 3 HOH 37  637 589 HOH HOH A . 
I 3 HOH 38  638 806 HOH HOH A . 
I 3 HOH 39  639 399 HOH HOH A . 
I 3 HOH 40  640 515 HOH HOH A . 
I 3 HOH 41  641 635 HOH HOH A . 
I 3 HOH 42  642 746 HOH HOH A . 
I 3 HOH 43  643 827 HOH HOH A . 
I 3 HOH 44  644 492 HOH HOH A . 
I 3 HOH 45  645 527 HOH HOH A . 
I 3 HOH 46  646 574 HOH HOH A . 
I 3 HOH 47  647 488 HOH HOH A . 
I 3 HOH 48  648 152 HOH HOH A . 
I 3 HOH 49  649 126 HOH HOH A . 
I 3 HOH 50  650 275 HOH HOH A . 
I 3 HOH 51  651 627 HOH HOH A . 
I 3 HOH 52  652 328 HOH HOH A . 
I 3 HOH 53  653 86  HOH HOH A . 
I 3 HOH 54  654 106 HOH HOH A . 
I 3 HOH 55  655 350 HOH HOH A . 
I 3 HOH 56  656 33  HOH HOH A . 
I 3 HOH 57  657 38  HOH HOH A . 
I 3 HOH 58  658 293 HOH HOH A . 
I 3 HOH 59  659 9   HOH HOH A . 
I 3 HOH 60  660 43  HOH HOH A . 
I 3 HOH 61  661 778 HOH HOH A . 
I 3 HOH 62  662 32  HOH HOH A . 
I 3 HOH 63  663 170 HOH HOH A . 
I 3 HOH 64  664 766 HOH HOH A . 
I 3 HOH 65  665 646 HOH HOH A . 
I 3 HOH 66  666 164 HOH HOH A . 
I 3 HOH 67  667 603 HOH HOH A . 
I 3 HOH 68  668 390 HOH HOH A . 
I 3 HOH 69  669 186 HOH HOH A . 
I 3 HOH 70  670 173 HOH HOH A . 
I 3 HOH 71  671 246 HOH HOH A . 
I 3 HOH 72  672 694 HOH HOH A . 
I 3 HOH 73  673 351 HOH HOH A . 
I 3 HOH 74  674 202 HOH HOH A . 
I 3 HOH 75  675 155 HOH HOH A . 
I 3 HOH 76  676 389 HOH HOH A . 
I 3 HOH 77  677 767 HOH HOH A . 
I 3 HOH 78  678 176 HOH HOH A . 
I 3 HOH 79  679 128 HOH HOH A . 
I 3 HOH 80  680 209 HOH HOH A . 
I 3 HOH 81  681 818 HOH HOH A . 
I 3 HOH 82  682 264 HOH HOH A . 
I 3 HOH 83  683 411 HOH HOH A . 
I 3 HOH 84  684 761 HOH HOH A . 
I 3 HOH 85  685 541 HOH HOH A . 
I 3 HOH 86  686 507 HOH HOH A . 
I 3 HOH 87  687 329 HOH HOH A . 
I 3 HOH 88  688 226 HOH HOH A . 
I 3 HOH 89  689 78  HOH HOH A . 
I 3 HOH 90  690 686 HOH HOH A . 
I 3 HOH 91  691 719 HOH HOH A . 
I 3 HOH 92  692 24  HOH HOH A . 
I 3 HOH 93  693 29  HOH HOH A . 
I 3 HOH 94  694 85  HOH HOH A . 
I 3 HOH 95  695 598 HOH HOH A . 
I 3 HOH 96  696 55  HOH HOH A . 
I 3 HOH 97  697 121 HOH HOH A . 
I 3 HOH 98  698 539 HOH HOH A . 
I 3 HOH 99  699 371 HOH HOH A . 
I 3 HOH 100 700 715 HOH HOH A . 
I 3 HOH 101 701 182 HOH HOH A . 
I 3 HOH 102 702 127 HOH HOH A . 
I 3 HOH 103 703 664 HOH HOH A . 
I 3 HOH 104 704 452 HOH HOH A . 
I 3 HOH 105 705 175 HOH HOH A . 
I 3 HOH 106 706 345 HOH HOH A . 
I 3 HOH 107 707 134 HOH HOH A . 
I 3 HOH 108 708 524 HOH HOH A . 
I 3 HOH 109 709 335 HOH HOH A . 
I 3 HOH 110 710 184 HOH HOH A . 
I 3 HOH 111 711 570 HOH HOH A . 
I 3 HOH 112 712 68  HOH HOH A . 
I 3 HOH 113 713 393 HOH HOH A . 
I 3 HOH 114 714 642 HOH HOH A . 
I 3 HOH 115 715 442 HOH HOH A . 
I 3 HOH 116 716 578 HOH HOH A . 
I 3 HOH 117 717 438 HOH HOH A . 
I 3 HOH 118 718 26  HOH HOH A . 
I 3 HOH 119 719 753 HOH HOH A . 
I 3 HOH 120 720 216 HOH HOH A . 
I 3 HOH 121 721 631 HOH HOH A . 
I 3 HOH 122 722 446 HOH HOH A . 
I 3 HOH 123 723 543 HOH HOH A . 
I 3 HOH 124 724 12  HOH HOH A . 
I 3 HOH 125 725 562 HOH HOH A . 
I 3 HOH 126 726 392 HOH HOH A . 
I 3 HOH 127 727 564 HOH HOH A . 
I 3 HOH 128 728 461 HOH HOH A . 
I 3 HOH 129 729 203 HOH HOH A . 
I 3 HOH 130 730 695 HOH HOH A . 
I 3 HOH 131 731 604 HOH HOH A . 
I 3 HOH 132 732 420 HOH HOH A . 
I 3 HOH 133 733 338 HOH HOH A . 
I 3 HOH 134 734 615 HOH HOH A . 
I 3 HOH 135 735 457 HOH HOH A . 
I 3 HOH 136 736 555 HOH HOH A . 
I 3 HOH 137 737 609 HOH HOH A . 
I 3 HOH 138 738 825 HOH HOH A . 
I 3 HOH 139 739 501 HOH HOH A . 
I 3 HOH 140 740 500 HOH HOH A . 
I 3 HOH 141 741 249 HOH HOH A . 
I 3 HOH 142 742 692 HOH HOH A . 
I 3 HOH 143 743 113 HOH HOH A . 
I 3 HOH 144 744 581 HOH HOH A . 
I 3 HOH 145 745 597 HOH HOH A . 
I 3 HOH 146 746 666 HOH HOH A . 
I 3 HOH 147 747 430 HOH HOH A . 
I 3 HOH 148 748 220 HOH HOH A . 
I 3 HOH 149 749 79  HOH HOH A . 
I 3 HOH 150 750 514 HOH HOH A . 
I 3 HOH 151 751 460 HOH HOH A . 
I 3 HOH 152 752 445 HOH HOH A . 
I 3 HOH 153 753 207 HOH HOH A . 
I 3 HOH 154 754 696 HOH HOH A . 
I 3 HOH 155 755 423 HOH HOH A . 
I 3 HOH 156 756 685 HOH HOH A . 
I 3 HOH 157 757 74  HOH HOH A . 
I 3 HOH 158 758 749 HOH HOH A . 
I 3 HOH 159 759 434 HOH HOH A . 
I 3 HOH 160 760 650 HOH HOH A . 
I 3 HOH 161 761 153 HOH HOH A . 
I 3 HOH 162 762 628 HOH HOH A . 
I 3 HOH 163 763 340 HOH HOH A . 
I 3 HOH 164 764 369 HOH HOH A . 
I 3 HOH 165 765 508 HOH HOH A . 
I 3 HOH 166 766 225 HOH HOH A . 
I 3 HOH 167 767 373 HOH HOH A . 
I 3 HOH 168 768 668 HOH HOH A . 
I 3 HOH 169 769 97  HOH HOH A . 
I 3 HOH 170 770 764 HOH HOH A . 
I 3 HOH 171 771 512 HOH HOH A . 
I 3 HOH 172 772 830 HOH HOH A . 
I 3 HOH 173 773 231 HOH HOH A . 
I 3 HOH 174 774 87  HOH HOH A . 
I 3 HOH 175 775 537 HOH HOH A . 
I 3 HOH 176 776 406 HOH HOH A . 
I 3 HOH 177 777 755 HOH HOH A . 
I 3 HOH 178 778 535 HOH HOH A . 
I 3 HOH 179 779 421 HOH HOH A . 
I 3 HOH 180 780 637 HOH HOH A . 
I 3 HOH 181 781 587 HOH HOH A . 
I 3 HOH 182 782 842 HOH HOH A . 
I 3 HOH 183 783 549 HOH HOH A . 
I 3 HOH 184 784 610 HOH HOH A . 
I 3 HOH 185 785 794 HOH HOH A . 
I 3 HOH 186 786 833 HOH HOH A . 
I 3 HOH 187 787 165 HOH HOH A . 
I 3 HOH 188 788 422 HOH HOH A . 
I 3 HOH 189 789 516 HOH HOH A . 
I 3 HOH 190 790 851 HOH HOH A . 
I 3 HOH 191 791 713 HOH HOH A . 
I 3 HOH 192 792 518 HOH HOH A . 
I 3 HOH 193 793 773 HOH HOH A . 
I 3 HOH 194 794 299 HOH HOH A . 
I 3 HOH 195 795 710 HOH HOH A . 
I 3 HOH 196 796 307 HOH HOH A . 
I 3 HOH 197 797 241 HOH HOH A . 
I 3 HOH 198 798 869 HOH HOH A . 
I 3 HOH 199 799 776 HOH HOH A . 
I 3 HOH 200 800 310 HOH HOH A . 
I 3 HOH 201 801 716 HOH HOH A . 
I 3 HOH 202 802 398 HOH HOH A . 
I 3 HOH 203 803 463 HOH HOH A . 
I 3 HOH 204 804 643 HOH HOH A . 
I 3 HOH 205 805 866 HOH HOH A . 
I 3 HOH 206 806 576 HOH HOH A . 
I 3 HOH 207 807 737 HOH HOH A . 
I 3 HOH 208 808 785 HOH HOH A . 
I 3 HOH 209 809 857 HOH HOH A . 
I 3 HOH 210 810 245 HOH HOH A . 
I 3 HOH 211 811 844 HOH HOH A . 
J 3 HOH 1   601 594 HOH HOH B . 
J 3 HOH 2   602 124 HOH HOH B . 
J 3 HOH 3   603 380 HOH HOH B . 
J 3 HOH 4   604 382 HOH HOH B . 
J 3 HOH 5   605 424 HOH HOH B . 
J 3 HOH 6   606 414 HOH HOH B . 
J 3 HOH 7   607 502 HOH HOH B . 
J 3 HOH 8   608 102 HOH HOH B . 
J 3 HOH 9   609 72  HOH HOH B . 
J 3 HOH 10  610 178 HOH HOH B . 
J 3 HOH 11  611 156 HOH HOH B . 
J 3 HOH 12  612 383 HOH HOH B . 
J 3 HOH 13  613 287 HOH HOH B . 
J 3 HOH 14  614 490 HOH HOH B . 
J 3 HOH 15  615 273 HOH HOH B . 
J 3 HOH 16  616 283 HOH HOH B . 
J 3 HOH 17  617 473 HOH HOH B . 
J 3 HOH 18  618 455 HOH HOH B . 
J 3 HOH 19  619 355 HOH HOH B . 
J 3 HOH 20  620 109 HOH HOH B . 
J 3 HOH 21  621 230 HOH HOH B . 
J 3 HOH 22  622 52  HOH HOH B . 
J 3 HOH 23  623 73  HOH HOH B . 
J 3 HOH 24  624 262 HOH HOH B . 
J 3 HOH 25  625 217 HOH HOH B . 
J 3 HOH 26  626 31  HOH HOH B . 
J 3 HOH 27  627 707 HOH HOH B . 
J 3 HOH 28  628 39  HOH HOH B . 
J 3 HOH 29  629 757 HOH HOH B . 
J 3 HOH 30  630 807 HOH HOH B . 
J 3 HOH 31  631 311 HOH HOH B . 
J 3 HOH 32  632 407 HOH HOH B . 
J 3 HOH 33  633 253 HOH HOH B . 
J 3 HOH 34  634 210 HOH HOH B . 
J 3 HOH 35  635 467 HOH HOH B . 
J 3 HOH 36  636 592 HOH HOH B . 
J 3 HOH 37  637 370 HOH HOH B . 
J 3 HOH 38  638 8   HOH HOH B . 
J 3 HOH 39  639 75  HOH HOH B . 
J 3 HOH 40  640 240 HOH HOH B . 
J 3 HOH 41  641 3   HOH HOH B . 
J 3 HOH 42  642 397 HOH HOH B . 
J 3 HOH 43  643 669 HOH HOH B . 
J 3 HOH 44  644 174 HOH HOH B . 
J 3 HOH 45  645 46  HOH HOH B . 
J 3 HOH 46  646 600 HOH HOH B . 
J 3 HOH 47  647 822 HOH HOH B . 
J 3 HOH 48  648 659 HOH HOH B . 
J 3 HOH 49  649 53  HOH HOH B . 
J 3 HOH 50  650 89  HOH HOH B . 
J 3 HOH 51  651 787 HOH HOH B . 
J 3 HOH 52  652 475 HOH HOH B . 
J 3 HOH 53  653 5   HOH HOH B . 
J 3 HOH 54  654 878 HOH HOH B . 
J 3 HOH 55  655 1   HOH HOH B . 
J 3 HOH 56  656 400 HOH HOH B . 
J 3 HOH 57  657 435 HOH HOH B . 
J 3 HOH 58  658 739 HOH HOH B . 
J 3 HOH 59  659 789 HOH HOH B . 
J 3 HOH 60  660 365 HOH HOH B . 
J 3 HOH 61  661 199 HOH HOH B . 
J 3 HOH 62  662 528 HOH HOH B . 
J 3 HOH 63  663 16  HOH HOH B . 
J 3 HOH 64  664 674 HOH HOH B . 
J 3 HOH 65  665 321 HOH HOH B . 
J 3 HOH 66  666 622 HOH HOH B . 
J 3 HOH 67  667 660 HOH HOH B . 
J 3 HOH 68  668 494 HOH HOH B . 
J 3 HOH 69  669 101 HOH HOH B . 
J 3 HOH 70  670 191 HOH HOH B . 
J 3 HOH 71  671 132 HOH HOH B . 
J 3 HOH 72  672 300 HOH HOH B . 
J 3 HOH 73  673 20  HOH HOH B . 
J 3 HOH 74  674 733 HOH HOH B . 
J 3 HOH 75  675 403 HOH HOH B . 
J 3 HOH 76  676 256 HOH HOH B . 
J 3 HOH 77  677 58  HOH HOH B . 
J 3 HOH 78  678 688 HOH HOH B . 
J 3 HOH 79  679 617 HOH HOH B . 
J 3 HOH 80  680 579 HOH HOH B . 
J 3 HOH 81  681 567 HOH HOH B . 
J 3 HOH 82  682 80  HOH HOH B . 
J 3 HOH 83  683 596 HOH HOH B . 
J 3 HOH 84  684 572 HOH HOH B . 
J 3 HOH 85  685 683 HOH HOH B . 
J 3 HOH 86  686 620 HOH HOH B . 
J 3 HOH 87  687 122 HOH HOH B . 
J 3 HOH 88  688 743 HOH HOH B . 
J 3 HOH 89  689 523 HOH HOH B . 
J 3 HOH 90  690 63  HOH HOH B . 
J 3 HOH 91  691 11  HOH HOH B . 
J 3 HOH 92  692 268 HOH HOH B . 
J 3 HOH 93  693 641 HOH HOH B . 
J 3 HOH 94  694 450 HOH HOH B . 
J 3 HOH 95  695 115 HOH HOH B . 
J 3 HOH 96  696 754 HOH HOH B . 
J 3 HOH 97  697 454 HOH HOH B . 
J 3 HOH 98  698 67  HOH HOH B . 
J 3 HOH 99  699 149 HOH HOH B . 
J 3 HOH 100 700 361 HOH HOH B . 
J 3 HOH 101 701 100 HOH HOH B . 
J 3 HOH 102 702 347 HOH HOH B . 
J 3 HOH 103 703 66  HOH HOH B . 
J 3 HOH 104 704 433 HOH HOH B . 
J 3 HOH 105 705 702 HOH HOH B . 
J 3 HOH 106 706 169 HOH HOH B . 
J 3 HOH 107 707 856 HOH HOH B . 
J 3 HOH 108 708 40  HOH HOH B . 
J 3 HOH 109 709 239 HOH HOH B . 
J 3 HOH 110 710 513 HOH HOH B . 
J 3 HOH 111 711 133 HOH HOH B . 
J 3 HOH 112 712 388 HOH HOH B . 
J 3 HOH 113 713 107 HOH HOH B . 
J 3 HOH 114 714 227 HOH HOH B . 
J 3 HOH 115 715 662 HOH HOH B . 
J 3 HOH 116 716 114 HOH HOH B . 
J 3 HOH 117 717 744 HOH HOH B . 
J 3 HOH 118 718 274 HOH HOH B . 
J 3 HOH 119 719 658 HOH HOH B . 
J 3 HOH 120 720 83  HOH HOH B . 
J 3 HOH 121 721 653 HOH HOH B . 
J 3 HOH 122 722 208 HOH HOH B . 
J 3 HOH 123 723 319 HOH HOH B . 
J 3 HOH 124 724 50  HOH HOH B . 
J 3 HOH 125 725 247 HOH HOH B . 
J 3 HOH 126 726 201 HOH HOH B . 
J 3 HOH 127 727 586 HOH HOH B . 
J 3 HOH 128 728 667 HOH HOH B . 
J 3 HOH 129 729 4   HOH HOH B . 
J 3 HOH 130 730 301 HOH HOH B . 
J 3 HOH 131 731 277 HOH HOH B . 
J 3 HOH 132 732 561 HOH HOH B . 
J 3 HOH 133 733 472 HOH HOH B . 
J 3 HOH 134 734 619 HOH HOH B . 
J 3 HOH 135 735 196 HOH HOH B . 
J 3 HOH 136 736 358 HOH HOH B . 
J 3 HOH 137 737 96  HOH HOH B . 
J 3 HOH 138 738 730 HOH HOH B . 
J 3 HOH 139 739 810 HOH HOH B . 
J 3 HOH 140 740 183 HOH HOH B . 
J 3 HOH 141 741 221 HOH HOH B . 
J 3 HOH 142 742 417 HOH HOH B . 
J 3 HOH 143 743 158 HOH HOH B . 
J 3 HOH 144 744 797 HOH HOH B . 
J 3 HOH 145 745 136 HOH HOH B . 
J 3 HOH 146 746 159 HOH HOH B . 
J 3 HOH 147 747 316 HOH HOH B . 
J 3 HOH 148 748 384 HOH HOH B . 
J 3 HOH 149 749 129 HOH HOH B . 
J 3 HOH 150 750 157 HOH HOH B . 
J 3 HOH 151 751 498 HOH HOH B . 
J 3 HOH 152 752 482 HOH HOH B . 
J 3 HOH 153 753 459 HOH HOH B . 
J 3 HOH 154 754 354 HOH HOH B . 
J 3 HOH 155 755 656 HOH HOH B . 
J 3 HOH 156 756 44  HOH HOH B . 
J 3 HOH 157 757 565 HOH HOH B . 
J 3 HOH 158 758 120 HOH HOH B . 
J 3 HOH 159 759 82  HOH HOH B . 
J 3 HOH 160 760 529 HOH HOH B . 
J 3 HOH 161 761 649 HOH HOH B . 
J 3 HOH 162 762 138 HOH HOH B . 
J 3 HOH 163 763 151 HOH HOH B . 
J 3 HOH 164 764 177 HOH HOH B . 
J 3 HOH 165 765 303 HOH HOH B . 
J 3 HOH 166 766 88  HOH HOH B . 
J 3 HOH 167 767 525 HOH HOH B . 
J 3 HOH 168 768 690 HOH HOH B . 
J 3 HOH 169 769 418 HOH HOH B . 
J 3 HOH 170 770 412 HOH HOH B . 
J 3 HOH 171 771 771 HOH HOH B . 
J 3 HOH 172 772 583 HOH HOH B . 
J 3 HOH 173 773 725 HOH HOH B . 
J 3 HOH 174 774 444 HOH HOH B . 
J 3 HOH 175 775 218 HOH HOH B . 
J 3 HOH 176 776 505 HOH HOH B . 
J 3 HOH 177 777 344 HOH HOH B . 
J 3 HOH 178 778 456 HOH HOH B . 
J 3 HOH 179 779 550 HOH HOH B . 
J 3 HOH 180 780 469 HOH HOH B . 
J 3 HOH 181 781 701 HOH HOH B . 
J 3 HOH 182 782 611 HOH HOH B . 
J 3 HOH 183 783 180 HOH HOH B . 
J 3 HOH 184 784 682 HOH HOH B . 
J 3 HOH 185 785 759 HOH HOH B . 
J 3 HOH 186 786 141 HOH HOH B . 
J 3 HOH 187 787 552 HOH HOH B . 
J 3 HOH 188 788 219 HOH HOH B . 
J 3 HOH 189 789 348 HOH HOH B . 
J 3 HOH 190 790 645 HOH HOH B . 
J 3 HOH 191 791 693 HOH HOH B . 
J 3 HOH 192 792 364 HOH HOH B . 
J 3 HOH 193 793 811 HOH HOH B . 
J 3 HOH 194 794 318 HOH HOH B . 
J 3 HOH 195 795 234 HOH HOH B . 
J 3 HOH 196 796 618 HOH HOH B . 
J 3 HOH 197 797 652 HOH HOH B . 
J 3 HOH 198 798 474 HOH HOH B . 
J 3 HOH 199 799 171 HOH HOH B . 
J 3 HOH 200 800 795 HOH HOH B . 
J 3 HOH 201 801 783 HOH HOH B . 
J 3 HOH 202 802 327 HOH HOH B . 
J 3 HOH 203 803 834 HOH HOH B . 
J 3 HOH 204 804 768 HOH HOH B . 
J 3 HOH 205 805 871 HOH HOH B . 
J 3 HOH 206 806 840 HOH HOH B . 
J 3 HOH 207 807 723 HOH HOH B . 
J 3 HOH 208 808 876 HOH HOH B . 
J 3 HOH 209 809 732 HOH HOH B . 
J 3 HOH 210 810 409 HOH HOH B . 
J 3 HOH 211 811 814 HOH HOH B . 
J 3 HOH 212 812 577 HOH HOH B . 
J 3 HOH 213 813 873 HOH HOH B . 
J 3 HOH 214 814 431 HOH HOH B . 
J 3 HOH 215 815 864 HOH HOH B . 
J 3 HOH 216 816 790 HOH HOH B . 
J 3 HOH 217 817 792 HOH HOH B . 
J 3 HOH 218 818 870 HOH HOH B . 
J 3 HOH 219 819 788 HOH HOH B . 
J 3 HOH 220 820 497 HOH HOH B . 
J 3 HOH 221 821 684 HOH HOH B . 
J 3 HOH 222 822 865 HOH HOH B . 
J 3 HOH 223 823 838 HOH HOH B . 
J 3 HOH 224 824 843 HOH HOH B . 
J 3 HOH 225 825 879 HOH HOH B . 
J 3 HOH 226 826 861 HOH HOH B . 
J 3 HOH 227 827 874 HOH HOH B . 
J 3 HOH 228 828 630 HOH HOH B . 
J 3 HOH 229 829 845 HOH HOH B . 
J 3 HOH 230 830 563 HOH HOH B . 
J 3 HOH 231 831 828 HOH HOH B . 
J 3 HOH 232 832 867 HOH HOH B . 
J 3 HOH 233 833 717 HOH HOH B . 
J 3 HOH 234 834 481 HOH HOH B . 
J 3 HOH 235 835 608 HOH HOH B . 
J 3 HOH 236 836 860 HOH HOH B . 
J 3 HOH 237 837 751 HOH HOH B . 
J 3 HOH 238 838 506 HOH HOH B . 
J 3 HOH 239 839 852 HOH HOH B . 
K 3 HOH 1   601 734 HOH HOH C . 
K 3 HOH 2   602 330 HOH HOH C . 
K 3 HOH 3   603 791 HOH HOH C . 
K 3 HOH 4   604 282 HOH HOH C . 
K 3 HOH 5   605 238 HOH HOH C . 
K 3 HOH 6   606 724 HOH HOH C . 
K 3 HOH 7   607 824 HOH HOH C . 
K 3 HOH 8   608 305 HOH HOH C . 
K 3 HOH 9   609 211 HOH HOH C . 
K 3 HOH 10  610 681 HOH HOH C . 
K 3 HOH 11  611 517 HOH HOH C . 
K 3 HOH 12  612 150 HOH HOH C . 
K 3 HOH 13  613 800 HOH HOH C . 
K 3 HOH 14  614 271 HOH HOH C . 
K 3 HOH 15  615 793 HOH HOH C . 
K 3 HOH 16  616 261 HOH HOH C . 
K 3 HOH 17  617 626 HOH HOH C . 
K 3 HOH 18  618 729 HOH HOH C . 
K 3 HOH 19  619 190 HOH HOH C . 
K 3 HOH 20  620 27  HOH HOH C . 
K 3 HOH 21  621 704 HOH HOH C . 
K 3 HOH 22  622 248 HOH HOH C . 
K 3 HOH 23  623 796 HOH HOH C . 
K 3 HOH 24  624 671 HOH HOH C . 
K 3 HOH 25  625 458 HOH HOH C . 
K 3 HOH 26  626 391 HOH HOH C . 
K 3 HOH 27  627 195 HOH HOH C . 
K 3 HOH 28  628 90  HOH HOH C . 
K 3 HOH 29  629 308 HOH HOH C . 
K 3 HOH 30  630 614 HOH HOH C . 
K 3 HOH 31  631 2   HOH HOH C . 
K 3 HOH 32  632 137 HOH HOH C . 
K 3 HOH 33  633 738 HOH HOH C . 
K 3 HOH 34  634 304 HOH HOH C . 
K 3 HOH 35  635 703 HOH HOH C . 
K 3 HOH 36  636 551 HOH HOH C . 
K 3 HOH 37  637 168 HOH HOH C . 
K 3 HOH 38  638 346 HOH HOH C . 
K 3 HOH 39  639 395 HOH HOH C . 
K 3 HOH 40  640 484 HOH HOH C . 
K 3 HOH 41  641 426 HOH HOH C . 
K 3 HOH 42  642 131 HOH HOH C . 
K 3 HOH 43  643 144 HOH HOH C . 
K 3 HOH 44  644 691 HOH HOH C . 
K 3 HOH 45  645 341 HOH HOH C . 
K 3 HOH 46  646 95  HOH HOH C . 
K 3 HOH 47  647 143 HOH HOH C . 
K 3 HOH 48  648 123 HOH HOH C . 
K 3 HOH 49  649 36  HOH HOH C . 
K 3 HOH 50  650 205 HOH HOH C . 
K 3 HOH 51  651 70  HOH HOH C . 
K 3 HOH 52  652 342 HOH HOH C . 
K 3 HOH 53  653 427 HOH HOH C . 
K 3 HOH 54  654 349 HOH HOH C . 
K 3 HOH 55  655 147 HOH HOH C . 
K 3 HOH 56  656 215 HOH HOH C . 
K 3 HOH 57  657 139 HOH HOH C . 
K 3 HOH 58  658 676 HOH HOH C . 
K 3 HOH 59  659 599 HOH HOH C . 
K 3 HOH 60  660 235 HOH HOH C . 
K 3 HOH 61  661 302 HOH HOH C . 
K 3 HOH 62  662 41  HOH HOH C . 
K 3 HOH 63  663 257 HOH HOH C . 
K 3 HOH 64  664 387 HOH HOH C . 
K 3 HOH 65  665 22  HOH HOH C . 
K 3 HOH 66  666 352 HOH HOH C . 
K 3 HOH 67  667 413 HOH HOH C . 
K 3 HOH 68  668 636 HOH HOH C . 
K 3 HOH 69  669 573 HOH HOH C . 
K 3 HOH 70  670 647 HOH HOH C . 
K 3 HOH 71  671 51  HOH HOH C . 
K 3 HOH 72  672 394 HOH HOH C . 
K 3 HOH 73  673 37  HOH HOH C . 
K 3 HOH 74  674 269 HOH HOH C . 
K 3 HOH 75  675 678 HOH HOH C . 
K 3 HOH 76  676 534 HOH HOH C . 
K 3 HOH 77  677 259 HOH HOH C . 
K 3 HOH 78  678 519 HOH HOH C . 
K 3 HOH 79  679 415 HOH HOH C . 
K 3 HOH 80  680 69  HOH HOH C . 
K 3 HOH 81  681 189 HOH HOH C . 
K 3 HOH 82  682 194 HOH HOH C . 
K 3 HOH 83  683 708 HOH HOH C . 
K 3 HOH 84  684 263 HOH HOH C . 
K 3 HOH 85  685 332 HOH HOH C . 
K 3 HOH 86  686 429 HOH HOH C . 
K 3 HOH 87  687 42  HOH HOH C . 
K 3 HOH 88  688 819 HOH HOH C . 
K 3 HOH 89  689 495 HOH HOH C . 
K 3 HOH 90  690 453 HOH HOH C . 
K 3 HOH 91  691 504 HOH HOH C . 
K 3 HOH 92  692 584 HOH HOH C . 
K 3 HOH 93  693 323 HOH HOH C . 
K 3 HOH 94  694 56  HOH HOH C . 
K 3 HOH 95  695 14  HOH HOH C . 
K 3 HOH 96  696 336 HOH HOH C . 
K 3 HOH 97  697 752 HOH HOH C . 
K 3 HOH 98  698 192 HOH HOH C . 
K 3 HOH 99  699 377 HOH HOH C . 
K 3 HOH 100 700 661 HOH HOH C . 
K 3 HOH 101 701 499 HOH HOH C . 
K 3 HOH 102 702 15  HOH HOH C . 
K 3 HOH 103 703 476 HOH HOH C . 
K 3 HOH 104 704 160 HOH HOH C . 
K 3 HOH 105 705 258 HOH HOH C . 
K 3 HOH 106 706 292 HOH HOH C . 
K 3 HOH 107 707 750 HOH HOH C . 
K 3 HOH 108 708 94  HOH HOH C . 
K 3 HOH 109 709 179 HOH HOH C . 
K 3 HOH 110 710 697 HOH HOH C . 
K 3 HOH 111 711 805 HOH HOH C . 
K 3 HOH 112 712 568 HOH HOH C . 
K 3 HOH 113 713 166 HOH HOH C . 
K 3 HOH 114 714 28  HOH HOH C . 
K 3 HOH 115 715 142 HOH HOH C . 
K 3 HOH 116 716 379 HOH HOH C . 
K 3 HOH 117 717 222 HOH HOH C . 
K 3 HOH 118 718 663 HOH HOH C . 
K 3 HOH 119 719 829 HOH HOH C . 
K 3 HOH 120 720 224 HOH HOH C . 
K 3 HOH 121 721 774 HOH HOH C . 
K 3 HOH 122 722 727 HOH HOH C . 
K 3 HOH 123 723 45  HOH HOH C . 
K 3 HOH 124 724 605 HOH HOH C . 
K 3 HOH 125 725 644 HOH HOH C . 
K 3 HOH 126 726 443 HOH HOH C . 
K 3 HOH 127 727 554 HOH HOH C . 
K 3 HOH 128 728 462 HOH HOH C . 
K 3 HOH 129 729 477 HOH HOH C . 
K 3 HOH 130 730 130 HOH HOH C . 
K 3 HOH 131 731 125 HOH HOH C . 
K 3 HOH 132 732 815 HOH HOH C . 
K 3 HOH 133 733 306 HOH HOH C . 
K 3 HOH 134 734 823 HOH HOH C . 
K 3 HOH 135 735 289 HOH HOH C . 
K 3 HOH 136 736 286 HOH HOH C . 
K 3 HOH 137 737 119 HOH HOH C . 
K 3 HOH 138 738 172 HOH HOH C . 
K 3 HOH 139 739 279 HOH HOH C . 
K 3 HOH 140 740 607 HOH HOH C . 
K 3 HOH 141 741 278 HOH HOH C . 
K 3 HOH 142 742 817 HOH HOH C . 
K 3 HOH 143 743 295 HOH HOH C . 
K 3 HOH 144 744 812 HOH HOH C . 
K 3 HOH 145 745 721 HOH HOH C . 
K 3 HOH 146 746 680 HOH HOH C . 
K 3 HOH 147 747 780 HOH HOH C . 
K 3 HOH 148 748 782 HOH HOH C . 
K 3 HOH 149 749 200 HOH HOH C . 
K 3 HOH 150 750 486 HOH HOH C . 
K 3 HOH 151 751 470 HOH HOH C . 
K 3 HOH 152 752 464 HOH HOH C . 
K 3 HOH 153 753 118 HOH HOH C . 
K 3 HOH 154 754 835 HOH HOH C . 
K 3 HOH 155 755 483 HOH HOH C . 
K 3 HOH 156 756 740 HOH HOH C . 
K 3 HOH 157 757 705 HOH HOH C . 
K 3 HOH 158 758 252 HOH HOH C . 
K 3 HOH 159 759 493 HOH HOH C . 
K 3 HOH 160 760 542 HOH HOH C . 
K 3 HOH 161 761 714 HOH HOH C . 
K 3 HOH 162 762 440 HOH HOH C . 
K 3 HOH 163 763 722 HOH HOH C . 
K 3 HOH 164 764 553 HOH HOH C . 
K 3 HOH 165 765 858 HOH HOH C . 
K 3 HOH 166 766 747 HOH HOH C . 
K 3 HOH 167 767 108 HOH HOH C . 
K 3 HOH 168 768 569 HOH HOH C . 
K 3 HOH 169 769 777 HOH HOH C . 
K 3 HOH 170 770 425 HOH HOH C . 
K 3 HOH 171 771 841 HOH HOH C . 
K 3 HOH 172 772 485 HOH HOH C . 
K 3 HOH 173 773 875 HOH HOH C . 
K 3 HOH 174 774 309 HOH HOH C . 
K 3 HOH 175 775 736 HOH HOH C . 
K 3 HOH 176 776 313 HOH HOH C . 
K 3 HOH 177 777 772 HOH HOH C . 
K 3 HOH 178 778 765 HOH HOH C . 
K 3 HOH 179 779 839 HOH HOH C . 
K 3 HOH 180 780 634 HOH HOH C . 
K 3 HOH 181 781 526 HOH HOH C . 
K 3 HOH 182 782 204 HOH HOH C . 
K 3 HOH 183 783 281 HOH HOH C . 
K 3 HOH 184 784 859 HOH HOH C . 
K 3 HOH 185 785 654 HOH HOH C . 
K 3 HOH 186 786 872 HOH HOH C . 
K 3 HOH 187 787 779 HOH HOH C . 
K 3 HOH 188 788 612 HOH HOH C . 
K 3 HOH 189 789 804 HOH HOH C . 
K 3 HOH 190 790 439 HOH HOH C . 
K 3 HOH 191 791 770 HOH HOH C . 
K 3 HOH 192 792 447 HOH HOH C . 
K 3 HOH 193 793 848 HOH HOH C . 
K 3 HOH 194 794 503 HOH HOH C . 
K 3 HOH 195 795 850 HOH HOH C . 
L 3 HOH 1   601 255 HOH HOH D . 
L 3 HOH 2   602 575 HOH HOH D . 
L 3 HOH 3   603 242 HOH HOH D . 
L 3 HOH 4   604 698 HOH HOH D . 
L 3 HOH 5   605 531 HOH HOH D . 
L 3 HOH 6   606 374 HOH HOH D . 
L 3 HOH 7   607 77  HOH HOH D . 
L 3 HOH 8   608 366 HOH HOH D . 
L 3 HOH 9   609 582 HOH HOH D . 
L 3 HOH 10  610 546 HOH HOH D . 
L 3 HOH 11  611 538 HOH HOH D . 
L 3 HOH 12  612 339 HOH HOH D . 
L 3 HOH 13  613 556 HOH HOH D . 
L 3 HOH 14  614 23  HOH HOH D . 
L 3 HOH 15  615 61  HOH HOH D . 
L 3 HOH 16  616 297 HOH HOH D . 
L 3 HOH 17  617 648 HOH HOH D . 
L 3 HOH 18  618 742 HOH HOH D . 
L 3 HOH 19  619 432 HOH HOH D . 
L 3 HOH 20  620 104 HOH HOH D . 
L 3 HOH 21  621 632 HOH HOH D . 
L 3 HOH 22  622 48  HOH HOH D . 
L 3 HOH 23  623 560 HOH HOH D . 
L 3 HOH 24  624 540 HOH HOH D . 
L 3 HOH 25  625 362 HOH HOH D . 
L 3 HOH 26  626 34  HOH HOH D . 
L 3 HOH 27  627 545 HOH HOH D . 
L 3 HOH 28  628 19  HOH HOH D . 
L 3 HOH 29  629 655 HOH HOH D . 
L 3 HOH 30  630 229 HOH HOH D . 
L 3 HOH 31  631 623 HOH HOH D . 
L 3 HOH 32  632 6   HOH HOH D . 
L 3 HOH 33  633 673 HOH HOH D . 
L 3 HOH 34  634 532 HOH HOH D . 
L 3 HOH 35  635 337 HOH HOH D . 
L 3 HOH 36  636 163 HOH HOH D . 
L 3 HOH 37  637 396 HOH HOH D . 
L 3 HOH 38  638 54  HOH HOH D . 
L 3 HOH 39  639 781 HOH HOH D . 
L 3 HOH 40  640 267 HOH HOH D . 
L 3 HOH 41  641 162 HOH HOH D . 
L 3 HOH 42  642 60  HOH HOH D . 
L 3 HOH 43  643 92  HOH HOH D . 
L 3 HOH 44  644 416 HOH HOH D . 
L 3 HOH 45  645 441 HOH HOH D . 
L 3 HOH 46  646 99  HOH HOH D . 
L 3 HOH 47  647 471 HOH HOH D . 
L 3 HOH 48  648 536 HOH HOH D . 
L 3 HOH 49  649 188 HOH HOH D . 
L 3 HOH 50  650 111 HOH HOH D . 
L 3 HOH 51  651 30  HOH HOH D . 
L 3 HOH 52  652 181 HOH HOH D . 
L 3 HOH 53  653 479 HOH HOH D . 
L 3 HOH 54  654 237 HOH HOH D . 
L 3 HOH 55  655 558 HOH HOH D . 
L 3 HOH 56  656 401 HOH HOH D . 
L 3 HOH 57  657 25  HOH HOH D . 
L 3 HOH 58  658 65  HOH HOH D . 
L 3 HOH 59  659 375 HOH HOH D . 
L 3 HOH 60  660 84  HOH HOH D . 
L 3 HOH 61  661 547 HOH HOH D . 
L 3 HOH 62  662 356 HOH HOH D . 
L 3 HOH 63  663 276 HOH HOH D . 
L 3 HOH 64  664 404 HOH HOH D . 
L 3 HOH 65  665 381 HOH HOH D . 
L 3 HOH 66  666 64  HOH HOH D . 
L 3 HOH 67  667 621 HOH HOH D . 
L 3 HOH 68  668 322 HOH HOH D . 
L 3 HOH 69  669 10  HOH HOH D . 
L 3 HOH 70  670 437 HOH HOH D . 
L 3 HOH 71  671 509 HOH HOH D . 
L 3 HOH 72  672 665 HOH HOH D . 
L 3 HOH 73  673 7   HOH HOH D . 
L 3 HOH 74  674 405 HOH HOH D . 
L 3 HOH 75  675 35  HOH HOH D . 
L 3 HOH 76  676 140 HOH HOH D . 
L 3 HOH 77  677 265 HOH HOH D . 
L 3 HOH 78  678 228 HOH HOH D . 
L 3 HOH 79  679 489 HOH HOH D . 
L 3 HOH 80  680 167 HOH HOH D . 
L 3 HOH 81  681 595 HOH HOH D . 
L 3 HOH 82  682 402 HOH HOH D . 
L 3 HOH 83  683 146 HOH HOH D . 
L 3 HOH 84  684 353 HOH HOH D . 
L 3 HOH 85  685 359 HOH HOH D . 
L 3 HOH 86  686 223 HOH HOH D . 
L 3 HOH 87  687 98  HOH HOH D . 
L 3 HOH 88  688 372 HOH HOH D . 
L 3 HOH 89  689 284 HOH HOH D . 
L 3 HOH 90  690 110 HOH HOH D . 
L 3 HOH 91  691 706 HOH HOH D . 
L 3 HOH 92  692 206 HOH HOH D . 
L 3 HOH 93  693 290 HOH HOH D . 
L 3 HOH 94  694 333 HOH HOH D . 
L 3 HOH 95  695 187 HOH HOH D . 
L 3 HOH 96  696 496 HOH HOH D . 
L 3 HOH 97  697 116 HOH HOH D . 
L 3 HOH 98  698 376 HOH HOH D . 
L 3 HOH 99  699 544 HOH HOH D . 
L 3 HOH 100 700 590 HOH HOH D . 
L 3 HOH 101 701 687 HOH HOH D . 
L 3 HOH 102 702 410 HOH HOH D . 
L 3 HOH 103 703 343 HOH HOH D . 
L 3 HOH 104 704 71  HOH HOH D . 
L 3 HOH 105 705 232 HOH HOH D . 
L 3 HOH 106 706 112 HOH HOH D . 
L 3 HOH 107 707 280 HOH HOH D . 
L 3 HOH 108 708 193 HOH HOH D . 
L 3 HOH 109 709 510 HOH HOH D . 
L 3 HOH 110 710 762 HOH HOH D . 
L 3 HOH 111 711 213 HOH HOH D . 
L 3 HOH 112 712 449 HOH HOH D . 
L 3 HOH 113 713 47  HOH HOH D . 
L 3 HOH 114 714 533 HOH HOH D . 
L 3 HOH 115 715 298 HOH HOH D . 
L 3 HOH 116 716 288 HOH HOH D . 
L 3 HOH 117 717 17  HOH HOH D . 
L 3 HOH 118 718 260 HOH HOH D . 
L 3 HOH 119 719 465 HOH HOH D . 
L 3 HOH 120 720 763 HOH HOH D . 
L 3 HOH 121 721 145 HOH HOH D . 
L 3 HOH 122 722 331 HOH HOH D . 
L 3 HOH 123 723 294 HOH HOH D . 
L 3 HOH 124 724 520 HOH HOH D . 
L 3 HOH 125 725 244 HOH HOH D . 
L 3 HOH 126 726 367 HOH HOH D . 
L 3 HOH 127 727 49  HOH HOH D . 
L 3 HOH 128 728 57  HOH HOH D . 
L 3 HOH 129 729 624 HOH HOH D . 
L 3 HOH 130 730 557 HOH HOH D . 
L 3 HOH 131 731 161 HOH HOH D . 
L 3 HOH 132 732 748 HOH HOH D . 
L 3 HOH 133 733 154 HOH HOH D . 
L 3 HOH 134 734 820 HOH HOH D . 
L 3 HOH 135 735 808 HOH HOH D . 
L 3 HOH 136 736 334 HOH HOH D . 
L 3 HOH 137 737 266 HOH HOH D . 
L 3 HOH 138 738 657 HOH HOH D . 
L 3 HOH 139 739 784 HOH HOH D . 
L 3 HOH 140 740 566 HOH HOH D . 
L 3 HOH 141 741 468 HOH HOH D . 
L 3 HOH 142 742 511 HOH HOH D . 
L 3 HOH 143 743 198 HOH HOH D . 
L 3 HOH 144 744 580 HOH HOH D . 
L 3 HOH 145 745 135 HOH HOH D . 
L 3 HOH 146 746 254 HOH HOH D . 
L 3 HOH 147 747 250 HOH HOH D . 
L 3 HOH 148 748 314 HOH HOH D . 
L 3 HOH 149 749 670 HOH HOH D . 
L 3 HOH 150 750 826 HOH HOH D . 
L 3 HOH 151 751 616 HOH HOH D . 
L 3 HOH 152 752 548 HOH HOH D . 
L 3 HOH 153 753 741 HOH HOH D . 
L 3 HOH 154 754 324 HOH HOH D . 
L 3 HOH 155 755 21  HOH HOH D . 
L 3 HOH 156 756 816 HOH HOH D . 
L 3 HOH 157 757 629 HOH HOH D . 
L 3 HOH 158 758 801 HOH HOH D . 
L 3 HOH 159 759 726 HOH HOH D . 
L 3 HOH 160 760 360 HOH HOH D . 
L 3 HOH 161 761 270 HOH HOH D . 
L 3 HOH 162 762 559 HOH HOH D . 
L 3 HOH 163 763 76  HOH HOH D . 
L 3 HOH 164 764 243 HOH HOH D . 
L 3 HOH 165 765 689 HOH HOH D . 
L 3 HOH 166 766 317 HOH HOH D . 
L 3 HOH 167 767 731 HOH HOH D . 
L 3 HOH 168 768 832 HOH HOH D . 
L 3 HOH 169 769 91  HOH HOH D . 
L 3 HOH 170 770 296 HOH HOH D . 
L 3 HOH 171 771 846 HOH HOH D . 
L 3 HOH 172 772 357 HOH HOH D . 
L 3 HOH 173 773 378 HOH HOH D . 
L 3 HOH 174 774 709 HOH HOH D . 
L 3 HOH 175 775 62  HOH HOH D . 
L 3 HOH 176 776 786 HOH HOH D . 
L 3 HOH 177 777 436 HOH HOH D . 
L 3 HOH 178 778 601 HOH HOH D . 
L 3 HOH 179 779 699 HOH HOH D . 
L 3 HOH 180 780 325 HOH HOH D . 
L 3 HOH 181 781 103 HOH HOH D . 
L 3 HOH 182 782 831 HOH HOH D . 
L 3 HOH 183 783 756 HOH HOH D . 
L 3 HOH 184 784 326 HOH HOH D . 
L 3 HOH 185 785 368 HOH HOH D . 
L 3 HOH 186 786 735 HOH HOH D . 
L 3 HOH 187 787 428 HOH HOH D . 
L 3 HOH 188 788 651 HOH HOH D . 
L 3 HOH 189 789 639 HOH HOH D . 
L 3 HOH 190 790 837 HOH HOH D . 
L 3 HOH 191 791 602 HOH HOH D . 
L 3 HOH 192 792 487 HOH HOH D . 
L 3 HOH 193 793 480 HOH HOH D . 
L 3 HOH 194 794 813 HOH HOH D . 
L 3 HOH 195 795 451 HOH HOH D . 
L 3 HOH 196 796 718 HOH HOH D . 
L 3 HOH 197 797 448 HOH HOH D . 
L 3 HOH 198 798 803 HOH HOH D . 
L 3 HOH 199 799 638 HOH HOH D . 
L 3 HOH 200 800 836 HOH HOH D . 
L 3 HOH 201 801 419 HOH HOH D . 
L 3 HOH 202 802 847 HOH HOH D . 
L 3 HOH 203 803 675 HOH HOH D . 
L 3 HOH 204 804 877 HOH HOH D . 
L 3 HOH 205 805 712 HOH HOH D . 
L 3 HOH 206 806 853 HOH HOH D . 
L 3 HOH 207 807 855 HOH HOH D . 
L 3 HOH 208 808 854 HOH HOH D . 
L 3 HOH 209 809 799 HOH HOH D . 
L 3 HOH 210 810 880 HOH HOH D . 
# 
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 LYS 321 ? CG ? A LYS 292 CG 
3  1 Y 1 A LYS 321 ? CD ? A LYS 292 CD 
4  1 Y 1 A LYS 321 ? CE ? A LYS 292 CE 
5  1 Y 1 A LYS 321 ? NZ ? A LYS 292 NZ 
6  1 Y 1 B LYS 215 ? NZ ? B LYS 186 NZ 
7  1 Y 1 C LYS 215 ? NZ ? C LYS 186 NZ 
8  1 Y 1 D LYS 215 ? NZ ? D LYS 186 NZ 
9  1 Y 1 D LYS 395 ? CG ? D LYS 366 CG 
10 1 Y 1 D LYS 395 ? CD ? D LYS 366 CD 
11 1 Y 1 D LYS 395 ? CE ? D LYS 366 CE 
12 1 Y 1 D 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 ? ? ? 5.8.0411 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.40 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8ZVV 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     57.548 
_cell.length_a_esd                 ? 
_cell.length_b                     194.332 
_cell.length_b_esd                 ? 
_cell.length_c                     69.369 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_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                         8ZVV 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_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                   8ZVV 
_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             1.99 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          38.31 
_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         2023-12-15 
_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                                       8ZVV 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.59 
_reflns.d_resolution_low                               97.17 
_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                                     201557 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.1 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          6.5 
_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                                0.150 
_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                                   0.987 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.134 
_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                                    1.59 
_reflns_shell.d_res_low                                     1.68 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             28976 
_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                               1.456 
_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                                  0.323 
_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                                  1.272 
_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]                            -0.92 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            -0.96 
_refine.aniso_B[2][2]                            2.76 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            -1.83 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               29.190 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.942 
_refine.correlation_coeff_Fo_to_Fc_free          0.907 
_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                                 8ZVV 
_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                            1.59 
_refine.ls_d_res_low                             97.17 
_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                     191015 
_refine.ls_number_reflns_R_free                  10100 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.88 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.24419 
_refine.ls_R_factor_R_free                       0.29543 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.24144 
_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                       0.130 
_refine.pdbx_overall_ESU_R_Free                  0.133 
_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                             4.957 
_refine.overall_SU_ML                            0.161 
_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                       1.59 
_refine_hist.d_res_low                        97.17 
_refine_hist.number_atoms_solvent             855 
_refine_hist.number_atoms_total               14583 
_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        13728 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_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' ? 0.006  0.012  14088 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  13288 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.413  1.646  19132 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.490  1.569  30620 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 7.161  5.000  1740  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 9.286  5.000  76    ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 17.986 10.000 2372  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.072  0.200  2100  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.007  0.020  16356 ? 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' ? 2.460  2.911  6948  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.459  2.911  6948  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 3.621  5.229  8680  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 3.621  5.229  8681  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 2.818  3.192  7140  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.816  3.192  7137  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 4.279  5.721  10449 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 8.364  36.89  18353 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 8.321  36.49  18253 ? 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                       1.590 
_refine_ls_shell.d_res_low                        1.631 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             676 
_refine_ls_shell.number_reflns_R_work             13670 
_refine_ls_shell.percent_reflns_obs               95.57 
_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                  0.428 
_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                  0.462 
# 
_struct.entry_id                     8ZVV 
_struct.title                        'human citrate synthase complexed with citrate' 
_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        8ZVV 
_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 2 ? 
I N N 3 ? 
J N N 3 ? 
K N N 3 ? 
L 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
LGVLAQLIWSRALGFPLERPKSMSTEGLMKFVDS
;
_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 8ZVV A 1 ? 434 ? O75390 30 ? 463 ? 30 463 
2 1 8ZVV B 1 ? 434 ? O75390 30 ? 463 ? 30 463 
3 1 8ZVV C 1 ? 434 ? O75390 30 ? 463 ? 30 463 
4 1 8ZVV D 1 ? 434 ? O75390 30 ? 463 ? 30 463 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   octameric 
_pdbx_struct_assembly.oligomeric_count     8 
# 
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)' 10270 ? 
1 MORE         -57   ? 
1 'SSA (A^2)'  30050 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L 
# 
_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                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'       1_555 x,y,z 1.0 0.0 0.0 0.0           0.0 1.0 0.0 0.0 0.0 0.0 1.0 0.0           
2 'point symmetry operation' ?     ?     1.0 0.0 0.0 -0.4842830456 0.0 1.0 0.0 0.0 0.0 0.0 1.0 69.3673095264 
# 
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 ? ALA A 116 ? THR A 130 ALA A 145 1 ? 16 
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 ? LYS A 288 ? LEU A 303 LYS A 317 1 ? 15 
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 ? VAL A 355 ? ASP A 371 VAL A 384 1 ? 14 
HELX_P HELX_P20 AC2 PRO A 356 ? GLU A 361 ? PRO A 385 GLU A 390 1 ? 6  
HELX_P HELX_P21 AC3 ASN A 371 ? ALA A 374 ? ASN A 400 ALA A 403 5 ? 4  
HELX_P HELX_P22 AC4 HIS A 375 ? TYR A 383 ? HIS A 404 TYR A 412 1 ? 9  
HELX_P HELX_P23 AC5 GLU A 387 ? ASN A 389 ? GLU A 416 ASN A 418 5 ? 3  
HELX_P HELX_P24 AC6 TYR A 390 ? LEU A 413 ? TYR A 419 LEU A 442 1 ? 24 
HELX_P HELX_P25 AC7 SER A 424 ? SER A 434 ? SER A 453 SER A 463 1 ? 11 
HELX_P HELX_P26 AC8 ASN B 3   ? GLY B 27  ? ASN B 32  GLY B 56  1 ? 25 
HELX_P HELX_P27 AC9 VAL B 36  ? GLY B 41  ? VAL B 65  GLY B 70  1 ? 6  
HELX_P HELX_P28 AD1 SER B 68  ? LEU B 76  ? SER B 97  LEU B 105 1 ? 9  
HELX_P HELX_P29 AD2 LEU B 86  ? GLY B 97  ? LEU B 115 GLY B 126 1 ? 12 
HELX_P HELX_P30 AD3 THR B 101 ? ARG B 115 ? THR B 130 ARG B 144 1 ? 15 
HELX_P HELX_P31 AD4 PRO B 119 ? PHE B 129 ? PRO B 148 PHE B 158 1 ? 11 
HELX_P HELX_P32 AD5 HIS B 134 ? LEU B 146 ? HIS B 163 LEU B 175 1 ? 13 
HELX_P HELX_P33 AD6 ASN B 147 ? GLU B 149 ? ASN B 176 GLU B 178 5 ? 3  
HELX_P HELX_P34 AD7 SER B 150 ? GLN B 158 ? SER B 179 GLN B 187 1 ? 9  
HELX_P HELX_P35 AD8 SER B 161 ? THR B 163 ? SER B 190 THR B 192 5 ? 3  
HELX_P HELX_P36 AD9 LYS B 164 ? ARG B 193 ? LYS B 193 ARG B 222 1 ? 30 
HELX_P HELX_P37 AE1 ASP B 206 ? GLY B 216 ? ASP B 235 GLY B 245 1 ? 11 
HELX_P HELX_P38 AE2 ASP B 219 ? HIS B 233 ? ASP B 248 HIS B 262 1 ? 15 
HELX_P HELX_P39 AE3 ASN B 240 ? ALA B 252 ? ASN B 269 ALA B 281 1 ? 13 
HELX_P HELX_P40 AE4 ASP B 255 ? ALA B 268 ? ASP B 284 ALA B 297 1 ? 14 
HELX_P HELX_P41 AE5 LEU B 274 ? GLU B 289 ? LEU B 303 GLU B 318 1 ? 16 
HELX_P HELX_P42 AE6 SER B 295 ? SER B 309 ? SER B 324 SER B 338 1 ? 15 
HELX_P HELX_P43 AE7 ASP B 325 ? LEU B 339 ? ASP B 354 LEU B 368 1 ? 15 
HELX_P HELX_P44 AE8 ASP B 342 ? VAL B 355 ? ASP B 371 VAL B 384 1 ? 14 
HELX_P HELX_P45 AE9 PRO B 356 ? GLU B 361 ? PRO B 385 GLU B 390 1 ? 6  
HELX_P HELX_P46 AF1 VAL B 372 ? TYR B 383 ? VAL B 401 TYR B 412 1 ? 12 
HELX_P HELX_P47 AF2 GLU B 387 ? ASN B 389 ? GLU B 416 ASN B 418 5 ? 3  
HELX_P HELX_P48 AF3 TYR B 390 ? LEU B 413 ? TYR B 419 LEU B 442 1 ? 24 
HELX_P HELX_P49 AF4 SER B 424 ? VAL B 432 ? SER B 453 VAL B 461 1 ? 9  
HELX_P HELX_P50 AF5 ASN C 3   ? GLY C 27  ? ASN C 32  GLY C 56  1 ? 25 
HELX_P HELX_P51 AF6 THR C 35  ? GLY C 41  ? THR C 64  GLY C 70  1 ? 7  
HELX_P HELX_P52 AF7 SER C 68  ? LEU C 76  ? SER C 97  LEU C 105 1 ? 9  
HELX_P HELX_P53 AF8 LEU C 86  ? GLY C 97  ? LEU C 115 GLY C 126 1 ? 12 
HELX_P HELX_P54 AF9 THR C 101 ? ARG C 115 ? THR C 130 ARG C 144 1 ? 15 
HELX_P HELX_P55 AG1 PRO C 119 ? PHE C 129 ? PRO C 148 PHE C 158 1 ? 11 
HELX_P HELX_P56 AG2 HIS C 134 ? LEU C 146 ? HIS C 163 LEU C 175 1 ? 13 
HELX_P HELX_P57 AG3 ASN C 147 ? GLU C 149 ? ASN C 176 GLU C 178 5 ? 3  
HELX_P HELX_P58 AG4 SER C 150 ? GLY C 159 ? SER C 179 GLY C 188 1 ? 10 
HELX_P HELX_P59 AG5 SER C 161 ? THR C 163 ? SER C 190 THR C 192 5 ? 3  
HELX_P HELX_P60 AG6 LYS C 164 ? ARG C 193 ? LYS C 193 ARG C 222 1 ? 30 
HELX_P HELX_P61 AG7 ASP C 206 ? GLY C 216 ? ASP C 235 GLY C 245 1 ? 11 
HELX_P HELX_P62 AG8 ASP C 219 ? HIS C 233 ? ASP C 248 HIS C 262 1 ? 15 
HELX_P HELX_P63 AG9 ASN C 240 ? SER C 251 ? ASN C 269 SER C 280 1 ? 12 
HELX_P HELX_P64 AH1 ASP C 255 ? ALA C 268 ? ASP C 284 ALA C 297 1 ? 14 
HELX_P HELX_P65 AH2 LEU C 274 ? VAL C 290 ? LEU C 303 VAL C 319 1 ? 17 
HELX_P HELX_P66 AH3 SER C 295 ? SER C 309 ? SER C 324 SER C 338 1 ? 15 
HELX_P HELX_P67 AH4 ASP C 325 ? LEU C 339 ? ASP C 354 LEU C 368 1 ? 15 
HELX_P HELX_P68 AH5 ASP C 342 ? GLY C 363 ? ASP C 371 GLY C 392 1 ? 22 
HELX_P HELX_P69 AH6 ASN C 371 ? ALA C 374 ? ASN C 400 ALA C 403 5 ? 4  
HELX_P HELX_P70 AH7 HIS C 375 ? TYR C 383 ? HIS C 404 TYR C 412 1 ? 9  
HELX_P HELX_P71 AH8 GLU C 387 ? ASN C 389 ? GLU C 416 ASN C 418 5 ? 3  
HELX_P HELX_P72 AH9 TYR C 390 ? LEU C 413 ? TYR C 419 LEU C 442 1 ? 24 
HELX_P HELX_P73 AI1 SER C 424 ? SER C 434 ? SER C 453 SER C 463 1 ? 11 
HELX_P HELX_P74 AI2 ASN D 3   ? GLY D 27  ? ASN D 32  GLY D 56  1 ? 25 
HELX_P HELX_P75 AI3 THR D 35  ? GLY D 41  ? THR D 64  GLY D 70  1 ? 7  
HELX_P HELX_P76 AI4 SER D 68  ? LEU D 76  ? SER D 97  LEU D 105 1 ? 9  
HELX_P HELX_P77 AI5 LEU D 86  ? GLY D 97  ? LEU D 115 GLY D 126 1 ? 12 
HELX_P HELX_P78 AI6 THR D 101 ? ARG D 115 ? THR D 130 ARG D 144 1 ? 15 
HELX_P HELX_P79 AI7 PRO D 119 ? PHE D 129 ? PRO D 148 PHE D 158 1 ? 11 
HELX_P HELX_P80 AI8 HIS D 134 ? LEU D 146 ? HIS D 163 LEU D 175 1 ? 13 
HELX_P HELX_P81 AI9 ASN D 147 ? GLU D 149 ? ASN D 176 GLU D 178 5 ? 3  
HELX_P HELX_P82 AJ1 SER D 150 ? GLN D 158 ? SER D 179 GLN D 187 1 ? 9  
HELX_P HELX_P83 AJ2 SER D 161 ? THR D 163 ? SER D 190 THR D 192 5 ? 3  
HELX_P HELX_P84 AJ3 LYS D 164 ? ARG D 193 ? LYS D 193 ARG D 222 1 ? 30 
HELX_P HELX_P85 AJ4 ASP D 206 ? GLY D 216 ? ASP D 235 GLY D 245 1 ? 11 
HELX_P HELX_P86 AJ5 ASP D 219 ? HIS D 233 ? ASP D 248 HIS D 262 1 ? 15 
HELX_P HELX_P87 AJ6 ASN D 240 ? SER D 251 ? ASN D 269 SER D 280 1 ? 12 
HELX_P HELX_P88 AJ7 ASP D 255 ? ALA D 268 ? ASP D 284 ALA D 297 1 ? 14 
HELX_P HELX_P89 AJ8 LEU D 274 ? GLY D 291 ? LEU D 303 GLY D 320 1 ? 18 
HELX_P HELX_P90 AJ9 SER D 295 ? SER D 309 ? SER D 324 SER D 338 1 ? 15 
HELX_P HELX_P91 AK1 ASP D 325 ? LEU D 339 ? ASP D 354 LEU D 368 1 ? 15 
HELX_P HELX_P92 AK2 ASP D 342 ? GLY D 363 ? ASP D 371 GLY D 392 1 ? 22 
HELX_P HELX_P93 AK3 ASN D 371 ? ALA D 374 ? ASN D 400 ALA D 403 5 ? 4  
HELX_P HELX_P94 AK4 HIS D 375 ? TYR D 383 ? HIS D 404 TYR D 412 1 ? 9  
HELX_P HELX_P95 AK5 GLU D 387 ? ASN D 389 ? GLU D 416 ASN D 418 5 ? 3  
HELX_P HELX_P96 AK6 TYR D 390 ? LEU D 413 ? TYR D 419 LEU D 442 1 ? 24 
HELX_P HELX_P97 AK7 SER D 424 ? VAL D 432 ? SER D 453 VAL D 461 1 ? 9  
# 
_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 ? 2 ? 
AA6 ? 2 ? 
AA7 ? 2 ? 
# 
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 
AA6 1 2 ? anti-parallel 
AA7 1 2 ? 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 B 59  THR B 64  
AA2 1 LYS A 47  ? VAL A 50  ? LYS A 76  VAL A 79  
AA2 2 LYS B 421 ? MET B 423 ? LYS B 450 MET B 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 B 76  VAL B 79  
AA5 1 SER B 54  ? ASP B 57  ? SER B 83  ASP B 86  
AA5 2 GLY B 61  ? PHE B 64  ? GLY B 90  PHE B 93  
AA6 1 SER C 54  ? ASP C 57  ? SER C 83  ASP C 86  
AA6 2 GLY C 61  ? PHE C 64  ? GLY C 90  PHE C 93  
AA7 1 SER D 54  ? ASP D 57  ? SER D 83  ASP D 86  
AA7 2 GLY D 61  ? PHE D 64  ? GLY D 90  PHE D 93  
# 
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 VAL A 31  ? N VAL A 60  O ILE B 34  ? O ILE B 63  
AA2 1 2 N GLY A 48  ? N GLY A 77  O LYS B 421 ? O LYS B 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 MET A 423 ? N MET A 452 O LEU B 49  ? O LEU B 78  
AA5 1 2 N VAL B 55  ? N VAL B 84  O ARG B 63  ? O ARG B 92  
AA6 1 2 N ASP C 57  ? N ASP C 86  O GLY C 61  ? O GLY C 90  
AA7 1 2 N ASP D 57  ? N ASP D 86  O GLY D 61  ? O GLY D 90  
# 
_pdbx_entry_details.entry_id                   8ZVV 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     N 
_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 SG  B CYS 211 ? ? O   B HOH 738 ? ? 1.68 
2  1 SG  A CYS 211 ? ? O   A HOH 688 ? ? 1.75 
3  1 SG  A CYS 101 ? ? O   A HOH 638 ? ? 1.76 
4  1 O   C MET 75  ? ? O   C HOH 601 ? ? 1.78 
5  1 O   A HOH 644 ? ? O   A HOH 712 ? ? 1.86 
6  1 O   B HOH 627 ? ? O   B HOH 708 ? ? 1.87 
7  1 SG  B CYS 211 ? ? O   B HOH 823 ? ? 1.90 
8  1 CD1 A TYR 194 ? ? O   A HOH 636 ? ? 1.93 
9  1 CD2 A HIS 404 ? ? O   A HOH 637 ? ? 1.97 
10 1 CG  B PHE 120 ? ? O   B HOH 822 ? ? 1.97 
11 1 O   B HOH 744 ? ? O   B HOH 773 ? ? 1.97 
12 1 CE2 B TRP 141 ? ? O   B HOH 629 ? ? 1.98 
13 1 CE1 C TYR 420 ? ? O   C HOH 618 ? ? 1.99 
14 1 SG  C CYS 211 ? ? O   C HOH 689 ? ? 1.99 
15 1 O   D HOH 715 ? ? O   D HOH 778 ? ? 2.00 
16 1 O   C SER 190 ? ? O   C HOH 602 ? ? 2.01 
17 1 CE1 A TYR 420 ? ? O   A HOH 781 ? ? 2.03 
18 1 O   B TYR 357 ? ? O   B HOH 601 ? ? 2.07 
19 1 CB  A PHE 424 ? ? O   A HOH 607 ? ? 2.07 
20 1 CD1 A LEU 409 ? ? O   A HOH 781 ? ? 2.09 
21 1 CD2 D PHE 240 ? ? O   D HOH 808 ? ? 2.09 
22 1 CG  A TYR 217 ? ? O   A HOH 784 ? ? 2.10 
23 1 CB  A CYS 359 ? ? O   A HOH 698 ? ? 2.10 
24 1 CE1 A TYR 419 ? ? O   A HOH 601 ? ? 2.10 
25 1 CG2 A ILE 227 ? ? O   A HOH 624 ? ? 2.12 
26 1 CE1 A TYR 411 ? ? O   A HOH 703 ? ? 2.12 
27 1 CD1 D PHE 251 ? ? O   D HOH 794 ? ? 2.12 
28 1 CE3 B TRP 438 ? ? O   B HOH 710 ? ? 2.13 
29 1 O   D HOH 799 ? ? O   D HOH 808 ? ? 2.13 
30 1 N   A TYR 217 ? ? O   A HOH 601 ? ? 2.13 
31 1 O   A HOH 738 ? ? O   A HOH 805 ? ? 2.13 
32 1 CB  B PHE 120 ? ? O   B HOH 822 ? ? 2.13 
33 1 CD2 D PHE 120 ? ? O   D HOH 605 ? ? 2.13 
34 1 CD2 B PHE 120 ? ? O   B HOH 822 ? ? 2.14 
35 1 O   C GLY 70  ? ? O   C HOH 603 ? ? 2.15 
36 1 SG  C CYS 211 ? ? O   C HOH 711 ? ? 2.16 
37 1 CE1 B HIS 262 ? ? O   B HOH 712 ? ? 2.16 
38 1 CG2 B VAL 426 ? ? O   B HOH 686 ? ? 2.16 
39 1 CD1 A TYR 420 ? ? O   A HOH 781 ? ? 2.16 
40 1 CA  A VAL 212 ? ? O   A HOH 732 ? ? 2.17 
41 1 O   A HOH 770 ? ? O   A HOH 801 ? ? 2.17 
42 1 CG1 D VAL 422 ? ? O   D HOH 762 ? ? 2.17 
43 1 O   D TYR 331 ? ? OD1 D ASN 334 ? ? 2.18 
44 1 CH2 B TRP 141 ? ? O   B HOH 822 ? ? 2.19 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 OH  A TYR 411 ? ? 1_555 OE1 B GLU 89  ? ? 1_554 1.69 
2 1 O   A HIS 367 ? ? 1_555 OE2 B GLU 89  ? ? 1_554 1.85 
3 1 OE2 C GLU 196 ? ? 1_555 NZ  D LYS 193 ? ? 1_456 2.12 
# 
_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            D 
_pdbx_validate_rmsd_bond.auth_comp_id_1            GLY 
_pdbx_validate_rmsd_bond.auth_seq_id_1             392 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            O 
_pdbx_validate_rmsd_bond.auth_asym_id_2            D 
_pdbx_validate_rmsd_bond.auth_comp_id_2            GLY 
_pdbx_validate_rmsd_bond.auth_seq_id_2             392 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.343 
_pdbx_validate_rmsd_bond.bond_target_value         1.232 
_pdbx_validate_rmsd_bond.bond_deviation            0.111 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.016 
_pdbx_validate_rmsd_bond.linker_flag               N 
# 
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 N D ARG 329 ? ? CA D ARG 329 ? ? CB D ARG 329 ? ? 98.33  110.60 -12.27 1.80 N 
2 1 O D GLY 392 ? ? C  D GLY 392 ? ? N  D LYS 393 ? ? 134.58 122.70 11.88  1.60 Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ALA A 146 ? ? -170.78 127.45  
2  1 GLU A 266 ? ? 51.37   -168.38 
3  1 HIS A 301 ? ? -117.29 -92.61  
4  1 VAL A 349 ? ? -135.35 -44.16  
5  1 LEU A 368 ? ? -146.03 48.54   
6  1 LEU A 388 ? ? 75.11   -59.20  
7  1 ALA A 394 ? ? -134.64 -42.88  
8  1 LYS A 395 ? ? 69.99   -63.45  
9  1 ARG A 448 ? ? -162.27 83.41   
10 1 ALA B 146 ? ? -175.69 127.58  
11 1 HIS B 265 ? ? -150.60 55.26   
12 1 GLU B 266 ? ? 65.39   -176.41 
13 1 HIS B 301 ? ? -124.73 -129.67 
14 1 VAL B 349 ? ? -133.72 -44.92  
15 1 LEU B 368 ? ? -146.12 50.27   
16 1 LEU B 388 ? ? 73.10   -61.32  
17 1 LYS B 393 ? ? -89.16  38.69   
18 1 ASP B 462 ? ? -106.13 60.29   
19 1 HIS C 265 ? ? -151.86 60.49   
20 1 GLU C 266 ? ? 62.18   -174.74 
21 1 HIS C 301 ? ? -120.95 -99.59  
22 1 VAL C 349 ? ? -131.05 -35.91  
23 1 LEU C 368 ? ? -154.64 47.15   
24 1 ARG C 448 ? ? -159.91 79.50   
25 1 ALA D 229 ? ? -59.43  101.15  
26 1 HIS D 265 ? ? -153.02 54.32   
27 1 GLU D 266 ? ? 63.20   -172.93 
28 1 HIS D 301 ? ? -118.01 -121.61 
29 1 VAL D 349 ? ? -132.32 -35.56  
30 1 LEU D 368 ? ? -148.43 54.08   
31 1 LYS D 393 ? ? 51.71   -75.93  
32 1 ARG D 448 ? ? -152.68 80.19   
33 1 ASP D 462 ? ? -110.92 53.70   
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   GLY 
_pdbx_validate_peptide_omega.auth_asym_id_1   A 
_pdbx_validate_peptide_omega.auth_seq_id_1    110 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   GLY 
_pdbx_validate_peptide_omega.auth_asym_id_2   A 
_pdbx_validate_peptide_omega.auth_seq_id_2    111 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            -148.61 
# 
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 440 ? ? 0.096 'SIDE CHAIN' 
2  1 ARG B 73  ? ? 0.077 'SIDE CHAIN' 
3  1 ARG B 440 ? ? 0.137 'SIDE CHAIN' 
4  1 ARG C 222 ? ? 0.252 'SIDE CHAIN' 
5  1 ARG C 361 ? ? 0.081 'SIDE CHAIN' 
6  1 ARG C 440 ? ? 0.094 'SIDE CHAIN' 
7  1 ARG D 218 ? ? 0.140 'SIDE CHAIN' 
8  1 ARG D 222 ? ? 0.287 'SIDE CHAIN' 
9  1 ARG D 329 ? ? 0.183 'SIDE CHAIN' 
10 1 ARG D 361 ? ? 0.084 'SIDE CHAIN' 
11 1 ARG D 440 ? ? 0.076 '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 811 ? 5.82 . 
2 1 O ? D HOH 810 ? 5.81 . 
# 
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  
CIT C1   C N N 74  
CIT O1   O N N 75  
CIT O2   O N N 76  
CIT C2   C N N 77  
CIT C3   C N N 78  
CIT O7   O N N 79  
CIT C4   C N N 80  
CIT C5   C N N 81  
CIT O3   O N N 82  
CIT O4   O N N 83  
CIT C6   C N N 84  
CIT O5   O N N 85  
CIT O6   O N N 86  
CIT HO2  H N N 87  
CIT H21  H N N 88  
CIT H22  H N N 89  
CIT HO7  H N N 90  
CIT H41  H N N 91  
CIT H42  H N N 92  
CIT HO4  H N N 93  
CIT HO6  H N N 94  
CYS N    N N N 95  
CYS CA   C N R 96  
CYS C    C N N 97  
CYS O    O N N 98  
CYS CB   C N N 99  
CYS SG   S N N 100 
CYS OXT  O N N 101 
CYS H    H N N 102 
CYS H2   H N N 103 
CYS HA   H N N 104 
CYS HB2  H N N 105 
CYS HB3  H N N 106 
CYS HG   H N N 107 
CYS HXT  H N N 108 
GLN N    N N N 109 
GLN CA   C N S 110 
GLN C    C N N 111 
GLN O    O N N 112 
GLN CB   C N N 113 
GLN CG   C N N 114 
GLN CD   C N N 115 
GLN OE1  O N N 116 
GLN NE2  N N N 117 
GLN OXT  O N N 118 
GLN H    H N N 119 
GLN H2   H N N 120 
GLN HA   H N N 121 
GLN HB2  H N N 122 
GLN HB3  H N N 123 
GLN HG2  H N N 124 
GLN HG3  H N N 125 
GLN HE21 H N N 126 
GLN HE22 H N N 127 
GLN HXT  H N N 128 
GLU N    N N N 129 
GLU CA   C N S 130 
GLU C    C N N 131 
GLU O    O N N 132 
GLU CB   C N N 133 
GLU CG   C N N 134 
GLU CD   C N N 135 
GLU OE1  O N N 136 
GLU OE2  O N N 137 
GLU OXT  O N N 138 
GLU H    H N N 139 
GLU H2   H N N 140 
GLU HA   H N N 141 
GLU HB2  H N N 142 
GLU HB3  H N N 143 
GLU HG2  H N N 144 
GLU HG3  H N N 145 
GLU HE2  H N N 146 
GLU HXT  H N N 147 
GLY N    N N N 148 
GLY CA   C N N 149 
GLY C    C N N 150 
GLY O    O N N 151 
GLY OXT  O N N 152 
GLY H    H N N 153 
GLY H2   H N N 154 
GLY HA2  H N N 155 
GLY HA3  H N N 156 
GLY HXT  H N N 157 
HIS N    N N N 158 
HIS CA   C N S 159 
HIS C    C N N 160 
HIS O    O N N 161 
HIS CB   C N N 162 
HIS CG   C Y N 163 
HIS ND1  N Y N 164 
HIS CD2  C Y N 165 
HIS CE1  C Y N 166 
HIS NE2  N Y N 167 
HIS OXT  O N N 168 
HIS H    H N N 169 
HIS H2   H N N 170 
HIS HA   H N N 171 
HIS HB2  H N N 172 
HIS HB3  H N N 173 
HIS HD1  H N N 174 
HIS HD2  H N N 175 
HIS HE1  H N N 176 
HIS HE2  H N N 177 
HIS HXT  H N N 178 
HOH O    O N N 179 
HOH H1   H N N 180 
HOH H2   H N N 181 
ILE N    N N N 182 
ILE CA   C N S 183 
ILE C    C N N 184 
ILE O    O N N 185 
ILE CB   C N S 186 
ILE CG1  C N N 187 
ILE CG2  C N N 188 
ILE CD1  C N N 189 
ILE OXT  O N N 190 
ILE H    H N N 191 
ILE H2   H N N 192 
ILE HA   H N N 193 
ILE HB   H N N 194 
ILE HG12 H N N 195 
ILE HG13 H N N 196 
ILE HG21 H N N 197 
ILE HG22 H N N 198 
ILE HG23 H N N 199 
ILE HD11 H N N 200 
ILE HD12 H N N 201 
ILE HD13 H N N 202 
ILE HXT  H N N 203 
LEU N    N N N 204 
LEU CA   C N S 205 
LEU C    C N N 206 
LEU O    O N N 207 
LEU CB   C N N 208 
LEU CG   C N N 209 
LEU CD1  C N N 210 
LEU CD2  C N N 211 
LEU OXT  O N N 212 
LEU H    H N N 213 
LEU H2   H N N 214 
LEU HA   H N N 215 
LEU HB2  H N N 216 
LEU HB3  H N N 217 
LEU HG   H N N 218 
LEU HD11 H N N 219 
LEU HD12 H N N 220 
LEU HD13 H N N 221 
LEU HD21 H N N 222 
LEU HD22 H N N 223 
LEU HD23 H N N 224 
LEU HXT  H N N 225 
LYS N    N N N 226 
LYS CA   C N S 227 
LYS C    C N N 228 
LYS O    O N N 229 
LYS CB   C N N 230 
LYS CG   C N N 231 
LYS CD   C N N 232 
LYS CE   C N N 233 
LYS NZ   N N N 234 
LYS OXT  O N N 235 
LYS H    H N N 236 
LYS H2   H N N 237 
LYS HA   H N N 238 
LYS HB2  H N N 239 
LYS HB3  H N N 240 
LYS HG2  H N N 241 
LYS HG3  H N N 242 
LYS HD2  H N N 243 
LYS HD3  H N N 244 
LYS HE2  H N N 245 
LYS HE3  H N N 246 
LYS HZ1  H N N 247 
LYS HZ2  H N N 248 
LYS HZ3  H N N 249 
LYS HXT  H N N 250 
MET N    N N N 251 
MET CA   C N S 252 
MET C    C N N 253 
MET O    O N N 254 
MET CB   C N N 255 
MET CG   C N N 256 
MET SD   S N N 257 
MET CE   C N N 258 
MET OXT  O N N 259 
MET H    H N N 260 
MET H2   H N N 261 
MET HA   H N N 262 
MET HB2  H N N 263 
MET HB3  H N N 264 
MET HG2  H N N 265 
MET HG3  H N N 266 
MET HE1  H N N 267 
MET HE2  H N N 268 
MET HE3  H N N 269 
MET HXT  H N N 270 
PHE N    N N N 271 
PHE CA   C N S 272 
PHE C    C N N 273 
PHE O    O N N 274 
PHE CB   C N N 275 
PHE CG   C Y N 276 
PHE CD1  C Y N 277 
PHE CD2  C Y N 278 
PHE CE1  C Y N 279 
PHE CE2  C Y N 280 
PHE CZ   C Y N 281 
PHE OXT  O N N 282 
PHE H    H N N 283 
PHE H2   H N N 284 
PHE HA   H N N 285 
PHE HB2  H N N 286 
PHE HB3  H N N 287 
PHE HD1  H N N 288 
PHE HD2  H N N 289 
PHE HE1  H N N 290 
PHE HE2  H N N 291 
PHE HZ   H N N 292 
PHE HXT  H N N 293 
PRO N    N N N 294 
PRO CA   C N S 295 
PRO C    C N N 296 
PRO O    O N N 297 
PRO CB   C N N 298 
PRO CG   C N N 299 
PRO CD   C N N 300 
PRO OXT  O N N 301 
PRO H    H N N 302 
PRO HA   H N N 303 
PRO HB2  H N N 304 
PRO HB3  H N N 305 
PRO HG2  H N N 306 
PRO HG3  H N N 307 
PRO HD2  H N N 308 
PRO HD3  H N N 309 
PRO HXT  H N N 310 
SER N    N N N 311 
SER CA   C N S 312 
SER C    C N N 313 
SER O    O N N 314 
SER CB   C N N 315 
SER OG   O N N 316 
SER OXT  O N N 317 
SER H    H N N 318 
SER H2   H N N 319 
SER HA   H N N 320 
SER HB2  H N N 321 
SER HB3  H N N 322 
SER HG   H N N 323 
SER HXT  H N N 324 
THR N    N N N 325 
THR CA   C N S 326 
THR C    C N N 327 
THR O    O N N 328 
THR CB   C N R 329 
THR OG1  O N N 330 
THR CG2  C N N 331 
THR OXT  O N N 332 
THR H    H N N 333 
THR H2   H N N 334 
THR HA   H N N 335 
THR HB   H N N 336 
THR HG1  H N N 337 
THR HG21 H N N 338 
THR HG22 H N N 339 
THR HG23 H N N 340 
THR HXT  H N N 341 
TRP N    N N N 342 
TRP CA   C N S 343 
TRP C    C N N 344 
TRP O    O N N 345 
TRP CB   C N N 346 
TRP CG   C Y N 347 
TRP CD1  C Y N 348 
TRP CD2  C Y N 349 
TRP NE1  N Y N 350 
TRP CE2  C Y N 351 
TRP CE3  C Y N 352 
TRP CZ2  C Y N 353 
TRP CZ3  C Y N 354 
TRP CH2  C Y N 355 
TRP OXT  O N N 356 
TRP H    H N N 357 
TRP H2   H N N 358 
TRP HA   H N N 359 
TRP HB2  H N N 360 
TRP HB3  H N N 361 
TRP HD1  H N N 362 
TRP HE1  H N N 363 
TRP HE3  H N N 364 
TRP HZ2  H N N 365 
TRP HZ3  H N N 366 
TRP HH2  H N N 367 
TRP HXT  H N N 368 
TYR N    N N N 369 
TYR CA   C N S 370 
TYR C    C N N 371 
TYR O    O N N 372 
TYR CB   C N N 373 
TYR CG   C Y N 374 
TYR CD1  C Y N 375 
TYR CD2  C Y N 376 
TYR CE1  C Y N 377 
TYR CE2  C Y N 378 
TYR CZ   C Y N 379 
TYR OH   O N N 380 
TYR OXT  O N N 381 
TYR H    H N N 382 
TYR H2   H N N 383 
TYR HA   H N N 384 
TYR HB2  H N N 385 
TYR HB3  H N N 386 
TYR HD1  H N N 387 
TYR HD2  H N N 388 
TYR HE1  H N N 389 
TYR HE2  H N N 390 
TYR HH   H N N 391 
TYR HXT  H N N 392 
VAL N    N N N 393 
VAL CA   C N S 394 
VAL C    C N N 395 
VAL O    O N N 396 
VAL CB   C N N 397 
VAL CG1  C N N 398 
VAL CG2  C N N 399 
VAL OXT  O N N 400 
VAL H    H N N 401 
VAL H2   H N N 402 
VAL HA   H N N 403 
VAL HB   H N N 404 
VAL HG11 H N N 405 
VAL HG12 H N N 406 
VAL HG13 H N N 407 
VAL HG21 H N N 408 
VAL HG22 H N N 409 
VAL HG23 H N N 410 
VAL HXT  H N N 411 
# 
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  
CIT C1  O1   doub N N 70  
CIT C1  O2   sing N N 71  
CIT C1  C2   sing N N 72  
CIT O2  HO2  sing N N 73  
CIT C2  C3   sing N N 74  
CIT C2  H21  sing N N 75  
CIT C2  H22  sing N N 76  
CIT C3  O7   sing N N 77  
CIT C3  C4   sing N N 78  
CIT C3  C6   sing N N 79  
CIT O7  HO7  sing N N 80  
CIT C4  C5   sing N N 81  
CIT C4  H41  sing N N 82  
CIT C4  H42  sing N N 83  
CIT C5  O3   doub N N 84  
CIT C5  O4   sing N N 85  
CIT O4  HO4  sing N N 86  
CIT C6  O5   doub N N 87  
CIT C6  O6   sing N N 88  
CIT O6  HO6  sing N N 89  
CYS N   CA   sing N N 90  
CYS N   H    sing N N 91  
CYS N   H2   sing N N 92  
CYS CA  C    sing N N 93  
CYS CA  CB   sing N N 94  
CYS CA  HA   sing N N 95  
CYS C   O    doub N N 96  
CYS C   OXT  sing N N 97  
CYS CB  SG   sing N N 98  
CYS CB  HB2  sing N N 99  
CYS CB  HB3  sing N N 100 
CYS SG  HG   sing N N 101 
CYS OXT HXT  sing N N 102 
GLN N   CA   sing N N 103 
GLN N   H    sing N N 104 
GLN N   H2   sing N N 105 
GLN CA  C    sing N N 106 
GLN CA  CB   sing N N 107 
GLN CA  HA   sing N N 108 
GLN C   O    doub N N 109 
GLN C   OXT  sing N N 110 
GLN CB  CG   sing N N 111 
GLN CB  HB2  sing N N 112 
GLN CB  HB3  sing N N 113 
GLN CG  CD   sing N N 114 
GLN CG  HG2  sing N N 115 
GLN CG  HG3  sing N N 116 
GLN CD  OE1  doub N N 117 
GLN CD  NE2  sing N N 118 
GLN NE2 HE21 sing N N 119 
GLN NE2 HE22 sing N N 120 
GLN OXT HXT  sing N N 121 
GLU N   CA   sing N N 122 
GLU N   H    sing N N 123 
GLU N   H2   sing N N 124 
GLU CA  C    sing N N 125 
GLU CA  CB   sing N N 126 
GLU CA  HA   sing N N 127 
GLU C   O    doub N N 128 
GLU C   OXT  sing N N 129 
GLU CB  CG   sing N N 130 
GLU CB  HB2  sing N N 131 
GLU CB  HB3  sing N N 132 
GLU CG  CD   sing N N 133 
GLU CG  HG2  sing N N 134 
GLU CG  HG3  sing N N 135 
GLU CD  OE1  doub N N 136 
GLU CD  OE2  sing N N 137 
GLU OE2 HE2  sing N N 138 
GLU OXT HXT  sing N N 139 
GLY N   CA   sing N N 140 
GLY N   H    sing N N 141 
GLY N   H2   sing N N 142 
GLY CA  C    sing N N 143 
GLY CA  HA2  sing N N 144 
GLY CA  HA3  sing N N 145 
GLY C   O    doub N N 146 
GLY C   OXT  sing N N 147 
GLY OXT HXT  sing N N 148 
HIS N   CA   sing N N 149 
HIS N   H    sing N N 150 
HIS N   H2   sing N N 151 
HIS CA  C    sing N N 152 
HIS CA  CB   sing N N 153 
HIS CA  HA   sing N N 154 
HIS C   O    doub N N 155 
HIS C   OXT  sing N N 156 
HIS CB  CG   sing N N 157 
HIS CB  HB2  sing N N 158 
HIS CB  HB3  sing N N 159 
HIS CG  ND1  sing Y N 160 
HIS CG  CD2  doub Y N 161 
HIS ND1 CE1  doub Y N 162 
HIS ND1 HD1  sing N N 163 
HIS CD2 NE2  sing Y N 164 
HIS CD2 HD2  sing N N 165 
HIS CE1 NE2  sing Y N 166 
HIS CE1 HE1  sing N N 167 
HIS NE2 HE2  sing N N 168 
HIS OXT HXT  sing N N 169 
HOH O   H1   sing N N 170 
HOH O   H2   sing N N 171 
ILE N   CA   sing N N 172 
ILE N   H    sing N N 173 
ILE N   H2   sing N N 174 
ILE CA  C    sing N N 175 
ILE CA  CB   sing N N 176 
ILE CA  HA   sing N N 177 
ILE C   O    doub N N 178 
ILE C   OXT  sing N N 179 
ILE CB  CG1  sing N N 180 
ILE CB  CG2  sing N N 181 
ILE CB  HB   sing N N 182 
ILE CG1 CD1  sing N N 183 
ILE CG1 HG12 sing N N 184 
ILE CG1 HG13 sing N N 185 
ILE CG2 HG21 sing N N 186 
ILE CG2 HG22 sing N N 187 
ILE CG2 HG23 sing N N 188 
ILE CD1 HD11 sing N N 189 
ILE CD1 HD12 sing N N 190 
ILE CD1 HD13 sing N N 191 
ILE OXT HXT  sing N N 192 
LEU N   CA   sing N N 193 
LEU N   H    sing N N 194 
LEU N   H2   sing N N 195 
LEU CA  C    sing N N 196 
LEU CA  CB   sing N N 197 
LEU CA  HA   sing N N 198 
LEU C   O    doub N N 199 
LEU C   OXT  sing N N 200 
LEU CB  CG   sing N N 201 
LEU CB  HB2  sing N N 202 
LEU CB  HB3  sing N N 203 
LEU CG  CD1  sing N N 204 
LEU CG  CD2  sing N N 205 
LEU CG  HG   sing N N 206 
LEU CD1 HD11 sing N N 207 
LEU CD1 HD12 sing N N 208 
LEU CD1 HD13 sing N N 209 
LEU CD2 HD21 sing N N 210 
LEU CD2 HD22 sing N N 211 
LEU CD2 HD23 sing N N 212 
LEU OXT HXT  sing N N 213 
LYS N   CA   sing N N 214 
LYS N   H    sing N N 215 
LYS N   H2   sing N N 216 
LYS CA  C    sing N N 217 
LYS CA  CB   sing N N 218 
LYS CA  HA   sing N N 219 
LYS C   O    doub N N 220 
LYS C   OXT  sing N N 221 
LYS CB  CG   sing N N 222 
LYS CB  HB2  sing N N 223 
LYS CB  HB3  sing N N 224 
LYS CG  CD   sing N N 225 
LYS CG  HG2  sing N N 226 
LYS CG  HG3  sing N N 227 
LYS CD  CE   sing N N 228 
LYS CD  HD2  sing N N 229 
LYS CD  HD3  sing N N 230 
LYS CE  NZ   sing N N 231 
LYS CE  HE2  sing N N 232 
LYS CE  HE3  sing N N 233 
LYS NZ  HZ1  sing N N 234 
LYS NZ  HZ2  sing N N 235 
LYS NZ  HZ3  sing N N 236 
LYS OXT HXT  sing N N 237 
MET N   CA   sing N N 238 
MET N   H    sing N N 239 
MET N   H2   sing N N 240 
MET CA  C    sing N N 241 
MET CA  CB   sing N N 242 
MET CA  HA   sing N N 243 
MET C   O    doub N N 244 
MET C   OXT  sing N N 245 
MET CB  CG   sing N N 246 
MET CB  HB2  sing N N 247 
MET CB  HB3  sing N N 248 
MET CG  SD   sing N N 249 
MET CG  HG2  sing N N 250 
MET CG  HG3  sing N N 251 
MET SD  CE   sing N N 252 
MET CE  HE1  sing N N 253 
MET CE  HE2  sing N N 254 
MET CE  HE3  sing N N 255 
MET OXT HXT  sing N N 256 
PHE N   CA   sing N N 257 
PHE N   H    sing N N 258 
PHE N   H2   sing N N 259 
PHE CA  C    sing N N 260 
PHE CA  CB   sing N N 261 
PHE CA  HA   sing N N 262 
PHE C   O    doub N N 263 
PHE C   OXT  sing N N 264 
PHE CB  CG   sing N N 265 
PHE CB  HB2  sing N N 266 
PHE CB  HB3  sing N N 267 
PHE CG  CD1  doub Y N 268 
PHE CG  CD2  sing Y N 269 
PHE CD1 CE1  sing Y N 270 
PHE CD1 HD1  sing N N 271 
PHE CD2 CE2  doub Y N 272 
PHE CD2 HD2  sing N N 273 
PHE CE1 CZ   doub Y N 274 
PHE CE1 HE1  sing N N 275 
PHE CE2 CZ   sing Y N 276 
PHE CE2 HE2  sing N N 277 
PHE CZ  HZ   sing N N 278 
PHE OXT HXT  sing N N 279 
PRO N   CA   sing N N 280 
PRO N   CD   sing N N 281 
PRO N   H    sing N N 282 
PRO CA  C    sing N N 283 
PRO CA  CB   sing N N 284 
PRO CA  HA   sing N N 285 
PRO C   O    doub N N 286 
PRO C   OXT  sing N N 287 
PRO CB  CG   sing N N 288 
PRO CB  HB2  sing N N 289 
PRO CB  HB3  sing N N 290 
PRO CG  CD   sing N N 291 
PRO CG  HG2  sing N N 292 
PRO CG  HG3  sing N N 293 
PRO CD  HD2  sing N N 294 
PRO CD  HD3  sing N N 295 
PRO OXT HXT  sing N N 296 
SER N   CA   sing N N 297 
SER N   H    sing N N 298 
SER N   H2   sing N N 299 
SER CA  C    sing N N 300 
SER CA  CB   sing N N 301 
SER CA  HA   sing N N 302 
SER C   O    doub N N 303 
SER C   OXT  sing N N 304 
SER CB  OG   sing N N 305 
SER CB  HB2  sing N N 306 
SER CB  HB3  sing N N 307 
SER OG  HG   sing N N 308 
SER OXT HXT  sing N N 309 
THR N   CA   sing N N 310 
THR N   H    sing N N 311 
THR N   H2   sing N N 312 
THR CA  C    sing N N 313 
THR CA  CB   sing N N 314 
THR CA  HA   sing N N 315 
THR C   O    doub N N 316 
THR C   OXT  sing N N 317 
THR CB  OG1  sing N N 318 
THR CB  CG2  sing N N 319 
THR CB  HB   sing N N 320 
THR OG1 HG1  sing N N 321 
THR CG2 HG21 sing N N 322 
THR CG2 HG22 sing N N 323 
THR CG2 HG23 sing N N 324 
THR OXT HXT  sing N N 325 
TRP N   CA   sing N N 326 
TRP N   H    sing N N 327 
TRP N   H2   sing N N 328 
TRP CA  C    sing N N 329 
TRP CA  CB   sing N N 330 
TRP CA  HA   sing N N 331 
TRP C   O    doub N N 332 
TRP C   OXT  sing N N 333 
TRP CB  CG   sing N N 334 
TRP CB  HB2  sing N N 335 
TRP CB  HB3  sing N N 336 
TRP CG  CD1  doub Y N 337 
TRP CG  CD2  sing Y N 338 
TRP CD1 NE1  sing Y N 339 
TRP CD1 HD1  sing N N 340 
TRP CD2 CE2  doub Y N 341 
TRP CD2 CE3  sing Y N 342 
TRP NE1 CE2  sing Y N 343 
TRP NE1 HE1  sing N N 344 
TRP CE2 CZ2  sing Y N 345 
TRP CE3 CZ3  doub Y N 346 
TRP CE3 HE3  sing N N 347 
TRP CZ2 CH2  doub Y N 348 
TRP CZ2 HZ2  sing N N 349 
TRP CZ3 CH2  sing Y N 350 
TRP CZ3 HZ3  sing N N 351 
TRP CH2 HH2  sing N N 352 
TRP OXT HXT  sing N N 353 
TYR N   CA   sing N N 354 
TYR N   H    sing N N 355 
TYR N   H2   sing N N 356 
TYR CA  C    sing N N 357 
TYR CA  CB   sing N N 358 
TYR CA  HA   sing N N 359 
TYR C   O    doub N N 360 
TYR C   OXT  sing N N 361 
TYR CB  CG   sing N N 362 
TYR CB  HB2  sing N N 363 
TYR CB  HB3  sing N N 364 
TYR CG  CD1  doub Y N 365 
TYR CG  CD2  sing Y N 366 
TYR CD1 CE1  sing Y N 367 
TYR CD1 HD1  sing N N 368 
TYR CD2 CE2  doub Y N 369 
TYR CD2 HD2  sing N N 370 
TYR CE1 CZ   doub Y N 371 
TYR CE1 HE1  sing N N 372 
TYR CE2 CZ   sing Y N 373 
TYR CE2 HE2  sing N N 374 
TYR CZ  OH   sing N N 375 
TYR OH  HH   sing N N 376 
TYR OXT HXT  sing N N 377 
VAL N   CA   sing N N 378 
VAL N   H    sing N N 379 
VAL N   H2   sing N N 380 
VAL CA  C    sing N N 381 
VAL CA  CB   sing N N 382 
VAL CA  HA   sing N N 383 
VAL C   O    doub N N 384 
VAL C   OXT  sing N N 385 
VAL CB  CG1  sing N N 386 
VAL CB  CG2  sing N N 387 
VAL CB  HB   sing N N 388 
VAL CG1 HG11 sing N N 389 
VAL CG1 HG12 sing N N 390 
VAL CG1 HG13 sing N N 391 
VAL CG2 HG21 sing N N 392 
VAL CG2 HG22 sing N N 393 
VAL CG2 HG23 sing N N 394 
VAL OXT HXT  sing N N 395 
# 
_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                    8ZVV 
_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]   0.017377 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000120 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.005146 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.014416 
_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   ? 39.404  10.500  6.377   1.00 52.65  ? 30  SER A N   1 
ATOM   2     C CA  . SER A 1 1   ? 39.717  10.223  4.948   1.00 56.66  ? 30  SER A CA  1 
ATOM   3     C C   . SER A 1 1   ? 38.445  9.822   4.201   1.00 66.25  ? 30  SER A C   1 
ATOM   4     O O   . SER A 1 1   ? 37.727  10.676  3.676   1.00 67.78  ? 30  SER A O   1 
ATOM   5     C CB  . SER A 1 1   ? 40.791  9.175   4.831   1.00 55.15  ? 30  SER A CB  1 
ATOM   6     O OG  . SER A 1 1   ? 40.831  8.641   3.520   1.00 56.13  ? 30  SER A OG  1 
ATOM   7     N N   . THR A 1 2   ? 38.170  8.515   4.143   1.00 66.58  ? 31  THR A N   1 
ATOM   8     C CA  . THR A 1 2   ? 36.862  8.056   3.711   1.00 63.54  ? 31  THR A CA  1 
ATOM   9     C C   . THR A 1 2   ? 36.126  7.387   4.873   1.00 53.00  ? 31  THR A C   1 
ATOM   10    O O   . THR A 1 2   ? 34.903  7.295   4.822   1.00 58.59  ? 31  THR A O   1 
ATOM   11    C CB  . THR A 1 2   ? 36.945  7.164   2.461   1.00 66.04  ? 31  THR A CB  1 
ATOM   12    O OG1 . THR A 1 2   ? 37.961  6.178   2.650   1.00 70.18  ? 31  THR A OG1 1 
ATOM   13    C CG2 . THR A 1 2   ? 37.220  7.956   1.200   1.00 64.51  ? 31  THR A CG2 1 
ATOM   14    N N   . ASN A 1 3   ? 36.812  6.925   5.930   1.00 42.94  ? 32  ASN A N   1 
ATOM   15    C CA  . ASN A 1 3   ? 36.058  6.172   6.921   1.00 33.18  ? 32  ASN A CA  1 
ATOM   16    C C   . ASN A 1 3   ? 35.247  7.124   7.793   1.00 26.19  ? 32  ASN A C   1 
ATOM   17    O O   . ASN A 1 3   ? 35.774  7.881   8.612   1.00 24.54  ? 32  ASN A O   1 
ATOM   18    C CB  . ASN A 1 3   ? 36.853  5.192   7.772   1.00 34.37  ? 32  ASN A CB  1 
ATOM   19    C CG  . ASN A 1 3   ? 35.945  4.068   8.233   1.00 36.61  ? 32  ASN A CG  1 
ATOM   20    O OD1 . ASN A 1 3   ? 34.912  4.321   8.856   1.00 34.28  ? 32  ASN A OD1 1 
ATOM   21    N ND2 . ASN A 1 3   ? 36.266  2.840   7.854   1.00 34.91  ? 32  ASN A ND2 1 
ATOM   22    N N   . LEU A 1 4   ? 33.933  7.003   7.616   1.00 23.10  ? 33  LEU A N   1 
ATOM   23    C CA  . LEU A 1 4   ? 32.976  7.850   8.294   1.00 20.62  ? 33  LEU A CA  1 
ATOM   24    C C   . LEU A 1 4   ? 33.109  7.728   9.807   1.00 19.59  ? 33  LEU A C   1 
ATOM   25    O O   . LEU A 1 4   ? 32.912  8.693   10.525  1.00 18.91  ? 33  LEU A O   1 
ATOM   26    C CB  . LEU A 1 4   ? 31.577  7.436   7.815   1.00 21.45  ? 33  LEU A CB  1 
ATOM   27    C CG  . LEU A 1 4   ? 30.412  8.067   8.556   1.00 20.62  ? 33  LEU A CG  1 
ATOM   28    C CD1 . LEU A 1 4   ? 30.439  9.565   8.395   1.00 22.47  ? 33  LEU A CD1 1 
ATOM   29    C CD2 . LEU A 1 4   ? 29.096  7.494   8.078   1.00 21.88  ? 33  LEU A CD2 1 
ATOM   30    N N   . LYS A 1 5   ? 33.393  6.534   10.322  1.00 21.78  ? 34  LYS A N   1 
ATOM   31    C CA  . LYS A 1 5   ? 33.517  6.393   11.763  1.00 22.21  ? 34  LYS A CA  1 
ATOM   32    C C   . LYS A 1 5   ? 34.642  7.279   12.295  1.00 21.76  ? 34  LYS A C   1 
ATOM   33    O O   . LYS A 1 5   ? 34.508  7.865   13.367  1.00 22.08  ? 34  LYS A O   1 
ATOM   34    C CB  . LYS A 1 5   ? 33.727  4.918   12.129  1.00 23.56  ? 34  LYS A CB  1 
ATOM   35    C CG  . LYS A 1 5   ? 33.484  4.578   13.594  1.00 23.82  ? 34  LYS A CG  1 
ATOM   36    C CD  . LYS A 1 5   ? 33.583  3.090   13.832  1.00 25.19  ? 34  LYS A CD  1 
ATOM   37    C CE  . LYS A 1 5   ? 33.178  2.682   15.235  1.00 26.19  ? 34  LYS A CE  1 
ATOM   38    N NZ  . LYS A 1 5   ? 33.360  1.215   15.406  1.00 25.33  ? 34  LYS A NZ  1 
ATOM   39    N N   . ASP A 1 6   ? 35.753  7.367   11.543  1.00 20.98  ? 35  ASP A N   1 
ATOM   40    C CA  . ASP A 1 6   ? 36.942  8.086   11.974  1.00 23.49  ? 35  ASP A CA  1 
ATOM   41    C C   . ASP A 1 6   ? 36.683  9.583   11.934  1.00 22.59  ? 35  ASP A C   1 
ATOM   42    O O   . ASP A 1 6   ? 37.060  10.305  12.848  1.00 24.66  ? 35  ASP A O   1 
ATOM   43    C CB  . ASP A 1 6   ? 38.168  7.678   11.160  1.00 24.75  ? 35  ASP A CB  1 
ATOM   44    C CG  . ASP A 1 6   ? 38.594  6.280   11.561  1.00 26.96  ? 35  ASP A CG  1 
ATOM   45    O OD1 . ASP A 1 6   ? 38.742  6.056   12.787  1.00 30.61  ? 35  ASP A OD1 1 
ATOM   46    O OD2 . ASP A 1 6   ? 38.777  5.431   10.658  1.00 31.25  ? 35  ASP A OD2 1 
ATOM   47    N N   . ILE A 1 7   ? 35.945  10.008  10.920  1.00 22.64  ? 36  ILE A N   1 
ATOM   48    C CA  . ILE A 1 7   ? 35.575  11.404  10.819  1.00 23.01  ? 36  ILE A CA  1 
ATOM   49    C C   . ILE A 1 7   ? 34.675  11.749  12.002  1.00 22.52  ? 36  ILE A C   1 
ATOM   50    O O   . ILE A 1 7   ? 34.883  12.751  12.659  1.00 20.11  ? 36  ILE A O   1 
ATOM   51    C CB  . ILE A 1 7   ? 34.966  11.713  9.445   1.00 25.15  ? 36  ILE A CB  1 
ATOM   52    C CG1 . ILE A 1 7   ? 36.018  11.484  8.353   1.00 27.67  ? 36  ILE A CG1 1 
ATOM   53    C CG2 . ILE A 1 7   ? 34.419  13.123  9.419   1.00 25.63  ? 36  ILE A CG2 1 
ATOM   54    C CD1 . ILE A 1 7   ? 35.476  11.377  6.944   1.00 28.86  ? 36  ILE A CD1 1 
ATOM   55    N N   . LEU A 1 8   ? 33.753  10.845  12.327  1.00 23.47  ? 37  LEU A N   1 
ATOM   56    C CA  . LEU A 1 8   ? 32.817  11.074  13.416  1.00 22.73  ? 37  LEU A CA  1 
ATOM   57    C C   . LEU A 1 8   ? 33.544  11.103  14.773  1.00 25.11  ? 37  LEU A C   1 
ATOM   58    O O   . LEU A 1 8   ? 33.324  11.998  15.596  1.00 23.35  ? 37  LEU A O   1 
ATOM   59    C CB  . LEU A 1 8   ? 31.754  9.973   13.311  1.00 21.51  ? 37  LEU A CB  1 
ATOM   60    C CG  . LEU A 1 8   ? 30.768  9.846   14.461  1.00 25.31  ? 37  LEU A CG  1 
ATOM   61    C CD1 . LEU A 1 8   ? 29.928  11.113  14.612  1.00 24.04  ? 37  LEU A CD1 1 
ATOM   62    C CD2 . LEU A 1 8   ? 29.875  8.628   14.246  1.00 24.27  ? 37  LEU A CD2 1 
ATOM   63    N N   . ALA A 1 9   ? 34.426  10.121  15.008  1.00 23.85  ? 38  ALA A N   1 
ATOM   64    C CA  . ALA A 1 9   ? 35.250  10.086  16.208  1.00 26.11  ? 38  ALA A CA  1 
ATOM   65    C C   . ALA A 1 9   ? 35.900  11.440  16.477  1.00 25.90  ? 38  ALA A C   1 
ATOM   66    O O   . ALA A 1 9   ? 35.849  11.951  17.591  1.00 25.99  ? 38  ALA A O   1 
ATOM   67    C CB  . ALA A 1 9   ? 36.290  9.014   16.087  1.00 22.24  ? 38  ALA A CB  1 
ATOM   68    N N   . ASP A 1 10  ? 36.448  12.047  15.426  1.00 25.40  ? 39  ASP A N   1 
ATOM   69    C CA  . ASP A 1 10  ? 37.099  13.339  15.533  1.00 25.50  ? 39  ASP A CA  1 
ATOM   70    C C   . ASP A 1 10  ? 36.134  14.458  15.901  1.00 23.80  ? 39  ASP A C   1 
ATOM   71    O O   . ASP A 1 10  ? 36.555  15.446  16.487  1.00 27.12  ? 39  ASP A O   1 
ATOM   72    C CB  . ASP A 1 10  ? 37.822  13.707  14.239  1.00 27.79  ? 39  ASP A CB  1 
ATOM   73    C CG  . ASP A 1 10  ? 39.277  13.282  14.222  1.00 34.09  ? 39  ASP A CG  1 
ATOM   74    O OD1 . ASP A 1 10  ? 39.532  12.080  14.355  1.00 31.19  ? 39  ASP A OD1 1 
ATOM   75    O OD2 . ASP A 1 10  ? 40.145  14.178  14.115  1.00 39.85  ? 39  ASP A OD2 1 
ATOM   76    N N   . LEU A 1 11  ? 34.855  14.337  15.522  1.00 24.70  ? 40  LEU A N   1 
ATOM   77    C CA  . LEU A 1 11  ? 33.916  15.432  15.724  1.00 24.32  ? 40  LEU A CA  1 
ATOM   78    C C   . LEU A 1 11  ? 33.353  15.464  17.144  1.00 23.52  ? 40  LEU A C   1 
ATOM   79    O O   . LEU A 1 11  ? 32.995  16.521  17.644  1.00 22.72  ? 40  LEU A O   1 
ATOM   80    C CB  . LEU A 1 11  ? 32.783  15.287  14.715  1.00 23.43  ? 40  LEU A CB  1 
ATOM   81    C CG  . LEU A 1 11  ? 33.162  15.589  13.264  1.00 24.89  ? 40  LEU A CG  1 
ATOM   82    C CD1 . LEU A 1 11  ? 31.996  15.279  12.345  1.00 26.56  ? 40  LEU A CD1 1 
ATOM   83    C CD2 . LEU A 1 11  ? 33.595  17.043  13.114  1.00 24.75  ? 40  LEU A CD2 1 
ATOM   84    N N   . ILE A 1 12  ? 33.222  14.297  17.767  1.00 24.29  ? 41  ILE A N   1 
ATOM   85    C CA  . ILE A 1 12  ? 32.447  14.167  18.980  1.00 24.60  ? 41  ILE A CA  1 
ATOM   86    C C   . ILE A 1 12  ? 33.052  14.995  20.108  1.00 28.46  ? 41  ILE A C   1 
ATOM   87    O O   . ILE A 1 12  ? 32.333  15.812  20.687  1.00 31.35  ? 41  ILE A O   1 
ATOM   88    C CB  . ILE A 1 12  ? 32.240  12.681  19.319  1.00 23.91  ? 41  ILE A CB  1 
ATOM   89    C CG1 . ILE A 1 12  ? 31.316  12.019  18.297  1.00 20.96  ? 41  ILE A CG1 1 
ATOM   90    C CG2 . ILE A 1 12  ? 31.700  12.535  20.731  1.00 26.36  ? 41  ILE A CG2 1 
ATOM   91    C CD1 . ILE A 1 12  ? 31.257  10.507  18.357  1.00 21.80  ? 41  ILE A CD1 1 
ATOM   92    N N   . PRO A 1 13  ? 34.367  14.875  20.436  1.00 28.61  ? 42  PRO A N   1 
ATOM   93    C CA  . PRO A 1 13  ? 34.986  15.708  21.467  1.00 33.15  ? 42  PRO A CA  1 
ATOM   94    C C   . PRO A 1 13  ? 34.679  17.198  21.338  1.00 33.19  ? 42  PRO A C   1 
ATOM   95    O O   . PRO A 1 13  ? 34.327  17.843  22.321  1.00 33.38  ? 42  PRO A O   1 
ATOM   96    C CB  . PRO A 1 13  ? 36.504  15.465  21.279  1.00 32.77  ? 42  PRO A CB  1 
ATOM   97    C CG  . PRO A 1 13  ? 36.584  14.051  20.740  1.00 31.92  ? 42  PRO A CG  1 
ATOM   98    C CD  . PRO A 1 13  ? 35.314  13.872  19.917  1.00 29.62  ? 42  PRO A CD  1 
ATOM   99    N N   . LYS A 1 14  ? 34.786  17.704  20.109  1.00 33.27  ? 43  LYS A N   1 
ATOM   100   C CA  . LYS A 1 14  ? 34.511  19.098  19.783  1.00 34.96  ? 43  LYS A CA  1 
ATOM   101   C C   . LYS A 1 14  ? 33.111  19.475  20.260  1.00 31.67  ? 43  LYS A C   1 
ATOM   102   O O   . LYS A 1 14  ? 32.889  20.518  20.891  1.00 29.13  ? 43  LYS A O   1 
ATOM   103   C CB  . LYS A 1 14  ? 34.563  19.303  18.267  1.00 40.37  ? 43  LYS A CB  1 
ATOM   104   C CG  . LYS A 1 14  ? 35.670  18.562  17.537  1.00 47.24  ? 43  LYS A CG  1 
ATOM   105   C CD  . LYS A 1 14  ? 36.733  19.454  16.976  1.00 50.82  ? 43  LYS A CD  1 
ATOM   106   C CE  . LYS A 1 14  ? 36.334  20.074  15.654  1.00 56.42  ? 43  LYS A CE  1 
ATOM   107   N NZ  . LYS A 1 14  ? 37.341  21.067  15.209  1.00 61.26  ? 43  LYS A NZ  1 
ATOM   108   N N   . GLU A 1 15  ? 32.162  18.609  19.907  1.00 31.86  ? 44  GLU A N   1 
ATOM   109   C CA  . GLU A 1 15  ? 30.756  18.885  20.128  1.00 30.88  ? 44  GLU A CA  1 
ATOM   110   C C   . GLU A 1 15  ? 30.444  18.671  21.606  1.00 27.97  ? 44  GLU A C   1 
ATOM   111   O O   . GLU A 1 15  ? 29.618  19.390  22.169  1.00 24.34  ? 44  GLU A O   1 
ATOM   112   C CB  . GLU A 1 15  ? 29.878  18.029  19.205  1.00 35.54  ? 44  GLU A CB  1 
ATOM   113   C CG  . GLU A 1 15  ? 29.623  18.655  17.843  1.00 39.36  ? 44  GLU A CG  1 
ATOM   114   C CD  . GLU A 1 15  ? 29.114  20.087  17.931  1.00 39.76  ? 44  GLU A CD  1 
ATOM   115   O OE1 . GLU A 1 15  ? 28.256  20.362  18.802  1.00 43.62  ? 44  GLU A OE1 1 
ATOM   116   O OE2 . GLU A 1 15  ? 29.575  20.922  17.141  1.00 44.21  ? 44  GLU A OE2 1 
ATOM   117   N N   . GLN A 1 16  ? 31.105  17.678  22.223  1.00 25.27  ? 45  GLN A N   1 
ATOM   118   C CA  . GLN A 1 16  ? 31.020  17.508  23.664  1.00 28.27  ? 45  GLN A CA  1 
ATOM   119   C C   . GLN A 1 16  ? 31.423  18.828  24.303  1.00 26.86  ? 45  GLN A C   1 
ATOM   120   O O   . GLN A 1 16  ? 30.697  19.374  25.126  1.00 25.14  ? 45  GLN A O   1 
ATOM   121   C CB  . GLN A 1 16  ? 31.852  16.305  24.116  1.00 29.42  ? 45  GLN A CB  1 
ATOM   122   C CG  . GLN A 1 16  ? 31.200  14.976  23.762  1.00 30.54  ? 45  GLN A CG  1 
ATOM   123   C CD  . GLN A 1 16  ? 32.088  13.773  23.991  1.00 33.91  ? 45  GLN A CD  1 
ATOM   124   O OE1 . GLN A 1 16  ? 33.309  13.874  24.085  1.00 34.97  ? 45  GLN A OE1 1 
ATOM   125   N NE2 . GLN A 1 16  ? 31.473  12.601  24.058  1.00 37.40  ? 45  GLN A NE2 1 
ATOM   126   N N   . ALA A 1 17  ? 32.561  19.361  23.856  1.00 30.51  ? 46  ALA A N   1 
ATOM   127   C CA  . ALA A 1 17  ? 33.093  20.561  24.470  1.00 32.48  ? 46  ALA A CA  1 
ATOM   128   C C   . ALA A 1 17  ? 32.130  21.717  24.221  1.00 30.30  ? 46  ALA A C   1 
ATOM   129   O O   . ALA A 1 17  ? 31.853  22.470  25.147  1.00 28.73  ? 46  ALA A O   1 
ATOM   130   C CB  . ALA A 1 17  ? 34.486  20.865  23.962  1.00 33.74  ? 46  ALA A CB  1 
ATOM   131   N N   . ARG A 1 18  ? 31.620  21.848  22.991  1.00 30.68  ? 47  ARG A N   1 
ATOM   132   C CA  . ARG A 1 18  ? 30.734  22.957  22.701  1.00 31.99  ? 47  ARG A CA  1 
ATOM   133   C C   . ARG A 1 18  ? 29.555  22.932  23.674  1.00 30.77  ? 47  ARG A C   1 
ATOM   134   O O   . ARG A 1 18  ? 29.191  23.961  24.220  1.00 27.67  ? 47  ARG A O   1 
ATOM   135   C CB  . ARG A 1 18  ? 30.244  22.983  21.253  1.00 39.26  ? 47  ARG A CB  1 
ATOM   136   C CG  . ARG A 1 18  ? 29.501  24.267  20.912  1.00 45.55  ? 47  ARG A CG  1 
ATOM   137   C CD  . ARG A 1 18  ? 29.504  24.647  19.438  1.00 48.66  ? 47  ARG A CD  1 
ATOM   138   N NE  . ARG A 1 18  ? 28.512  23.887  18.686  1.00 53.51  ? 47  ARG A NE  1 
ATOM   139   C CZ  . ARG A 1 18  ? 27.521  24.413  17.967  1.00 57.63  ? 47  ARG A CZ  1 
ATOM   140   N NH1 . ARG A 1 18  ? 26.683  23.622  17.320  1.00 58.45  ? 47  ARG A NH1 1 
ATOM   141   N NH2 . ARG A 1 18  ? 27.371  25.724  17.882  1.00 64.21  ? 47  ARG A NH2 1 
ATOM   142   N N   . ILE A 1 19  ? 28.968  21.763  23.922  1.00 27.68  ? 48  ILE A N   1 
ATOM   143   C CA  . ILE A 1 19  ? 27.786  21.703  24.764  1.00 30.92  ? 48  ILE A CA  1 
ATOM   144   C C   . ILE A 1 19  ? 28.132  21.949  26.231  1.00 29.69  ? 48  ILE A C   1 
ATOM   145   O O   . ILE A 1 19  ? 27.332  22.555  26.936  1.00 30.64  ? 48  ILE A O   1 
ATOM   146   C CB  . ILE A 1 19  ? 27.055  20.366  24.572  1.00 29.27  ? 48  ILE A CB  1 
ATOM   147   C CG1 . ILE A 1 19  ? 26.281  20.374  23.255  1.00 28.67  ? 48  ILE A CG1 1 
ATOM   148   C CG2 . ILE A 1 19  ? 26.148  20.032  25.758  1.00 30.58  ? 48  ILE A CG2 1 
ATOM   149   C CD1 . ILE A 1 19  ? 26.017  18.993  22.758  1.00 29.97  ? 48  ILE A CD1 1 
ATOM   150   N N   . LYS A 1 20  ? 29.289  21.451  26.694  1.00 30.24  ? 49  LYS A N   1 
ATOM   151   C CA  . LYS A 1 20  ? 29.644  21.564  28.103  1.00 32.63  ? 49  LYS A CA  1 
ATOM   152   C C   . LYS A 1 20  ? 29.660  23.047  28.468  1.00 33.61  ? 49  LYS A C   1 
ATOM   153   O O   . LYS A 1 20  ? 29.045  23.453  29.458  1.00 35.23  ? 49  LYS A O   1 
ATOM   154   C CB  . LYS A 1 20  ? 30.979  20.860  28.400  1.00 35.43  ? 49  LYS A CB  1 
ATOM   155   C CG  . LYS A 1 20  ? 31.344  20.730  29.878  1.00 36.63  ? 49  LYS A CG  1 
ATOM   156   C CD  . LYS A 1 20  ? 32.615  19.942  30.129  1.00 39.97  ? 49  LYS A CD  1 
ATOM   157   C CE  . LYS A 1 20  ? 32.900  19.713  31.600  1.00 43.01  ? 49  LYS A CE  1 
ATOM   158   N NZ  . LYS A 1 20  ? 33.307  20.971  32.272  1.00 44.96  ? 49  LYS A NZ  1 
ATOM   159   N N   . THR A 1 21  ? 30.306  23.844  27.608  1.00 35.65  ? 50  THR A N   1 
ATOM   160   C CA  . THR A 1 21  ? 30.474  25.268  27.840  1.00 34.71  ? 50  THR A CA  1 
ATOM   161   C C   . THR A 1 21  ? 29.126  25.972  27.752  1.00 37.14  ? 50  THR A C   1 
ATOM   162   O O   . THR A 1 21  ? 28.815  26.803  28.613  1.00 34.57  ? 50  THR A O   1 
ATOM   163   C CB  . THR A 1 21  ? 31.508  25.851  26.875  1.00 35.28  ? 50  THR A CB  1 
ATOM   164   O OG1 . THR A 1 21  ? 32.746  25.222  27.203  1.00 33.72  ? 50  THR A OG1 1 
ATOM   165   C CG2 . THR A 1 21  ? 31.661  27.354  26.975  1.00 31.99  ? 50  THR A CG2 1 
ATOM   166   N N   . PHE A 1 22  ? 28.349  25.626  26.705  1.00 31.59  ? 51  PHE A N   1 
ATOM   167   C CA  . PHE A 1 22  ? 27.029  26.194  26.507  1.00 29.36  ? 51  PHE A CA  1 
ATOM   168   C C   . PHE A 1 22  ? 26.202  26.009  27.777  1.00 28.14  ? 51  PHE A C   1 
ATOM   169   O O   . PHE A 1 22  ? 25.668  26.970  28.325  1.00 30.67  ? 51  PHE A O   1 
ATOM   170   C CB  . PHE A 1 22  ? 26.375  25.580  25.267  1.00 30.99  ? 51  PHE A CB  1 
ATOM   171   C CG  . PHE A 1 22  ? 25.059  26.210  24.862  1.00 31.51  ? 51  PHE A CG  1 
ATOM   172   C CD1 . PHE A 1 22  ? 24.937  27.587  24.750  1.00 31.39  ? 51  PHE A CD1 1 
ATOM   173   C CD2 . PHE A 1 22  ? 23.951  25.423  24.564  1.00 31.83  ? 51  PHE A CD2 1 
ATOM   174   C CE1 . PHE A 1 22  ? 23.734  28.163  24.375  1.00 28.89  ? 51  PHE A CE1 1 
ATOM   175   C CE2 . PHE A 1 22  ? 22.746  26.004  24.189  1.00 31.35  ? 51  PHE A CE2 1 
ATOM   176   C CZ  . PHE A 1 22  ? 22.643  27.375  24.088  1.00 30.90  ? 51  PHE A CZ  1 
ATOM   177   N N   . ARG A 1 23  ? 26.145  24.781  28.278  1.00 28.56  ? 52  ARG A N   1 
ATOM   178   C CA  . ARG A 1 23  ? 25.296  24.482  29.423  1.00 28.25  ? 52  ARG A CA  1 
ATOM   179   C C   . ARG A 1 23  ? 25.845  25.142  30.685  1.00 31.85  ? 52  ARG A C   1 
ATOM   180   O O   . ARG A 1 23  ? 25.083  25.475  31.593  1.00 27.22  ? 52  ARG A O   1 
ATOM   181   C CB  . ARG A 1 23  ? 25.170  22.970  29.612  1.00 28.96  ? 52  ARG A CB  1 
ATOM   182   C CG  . ARG A 1 23  ? 24.309  22.302  28.547  1.00 31.06  ? 52  ARG A CG  1 
ATOM   183   C CD  . ARG A 1 23  ? 24.141  20.811  28.781  1.00 30.24  ? 52  ARG A CD  1 
ATOM   184   N NE  . ARG A 1 23  ? 23.263  20.577  29.909  1.00 30.14  ? 52  ARG A NE  1 
ATOM   185   C CZ  . ARG A 1 23  ? 22.954  19.382  30.388  1.00 29.96  ? 52  ARG A CZ  1 
ATOM   186   N NH1 . ARG A 1 23  ? 23.581  18.311  29.948  1.00 31.34  ? 52  ARG A NH1 1 
ATOM   187   N NH2 . ARG A 1 23  ? 22.048  19.263  31.339  1.00 32.26  ? 52  ARG A NH2 1 
ATOM   188   N N   . GLN A 1 24  ? 27.171  25.284  30.756  1.00 32.72  ? 53  GLN A N   1 
ATOM   189   C CA  . GLN A 1 24  ? 27.797  25.928  31.893  1.00 37.41  ? 53  GLN A CA  1 
ATOM   190   C C   . GLN A 1 24  ? 27.236  27.344  31.971  1.00 37.01  ? 53  GLN A C   1 
ATOM   191   O O   . GLN A 1 24  ? 26.687  27.743  32.993  1.00 37.97  ? 53  GLN A O   1 
ATOM   192   C CB  . GLN A 1 24  ? 29.324  25.850  31.744  1.00 39.73  ? 53  GLN A CB  1 
ATOM   193   C CG  . GLN A 1 24  ? 30.124  26.450  32.891  1.00 40.84  ? 53  GLN A CG  1 
ATOM   194   C CD  . GLN A 1 24  ? 29.929  25.768  34.225  1.00 44.49  ? 53  GLN A CD  1 
ATOM   195   O OE1 . GLN A 1 24  ? 29.479  26.382  35.185  1.00 51.13  ? 53  GLN A OE1 1 
ATOM   196   N NE2 . GLN A 1 24  ? 30.301  24.501  34.314  1.00 49.88  ? 53  GLN A NE2 1 
ATOM   197   N N   . GLN A 1 25  ? 27.303  28.058  30.848  1.00 36.56  ? 54  GLN A N   1 
ATOM   198   C CA  . GLN A 1 25  ? 26.999  29.479  30.825  1.00 42.24  ? 54  GLN A CA  1 
ATOM   199   C C   . GLN A 1 25  ? 25.497  29.736  30.711  1.00 44.73  ? 54  GLN A C   1 
ATOM   200   O O   . GLN A 1 25  ? 25.034  30.790  31.152  1.00 38.14  ? 54  GLN A O   1 
ATOM   201   C CB  . GLN A 1 25  ? 27.722  30.162  29.663  1.00 45.71  ? 54  GLN A CB  1 
ATOM   202   C CG  . GLN A 1 25  ? 29.237  30.020  29.738  1.00 50.47  ? 54  GLN A CG  1 
ATOM   203   C CD  . GLN A 1 25  ? 29.963  31.117  28.994  1.00 55.54  ? 54  GLN A CD  1 
ATOM   204   O OE1 . GLN A 1 25  ? 29.767  32.302  29.255  1.00 54.33  ? 54  GLN A OE1 1 
ATOM   205   N NE2 . GLN A 1 25  ? 30.824  30.727  28.065  1.00 60.05  ? 54  GLN A NE2 1 
ATOM   206   N N   . HIS A 1 26  ? 24.754  28.795  30.103  1.00 36.35  ? 55  HIS A N   1 
ATOM   207   C CA  . HIS A 1 26  ? 23.374  29.053  29.721  1.00 34.41  ? 55  HIS A CA  1 
ATOM   208   C C   . HIS A 1 26  ? 22.407  27.957  30.168  1.00 32.02  ? 55  HIS A C   1 
ATOM   209   O O   . HIS A 1 26  ? 21.230  28.018  29.826  1.00 41.14  ? 55  HIS A O   1 
ATOM   210   C CB  . HIS A 1 26  ? 23.292  29.251  28.206  1.00 30.00  ? 55  HIS A CB  1 
ATOM   211   C CG  . HIS A 1 26  ? 24.011  30.465  27.713  1.00 33.52  ? 55  HIS A CG  1 
ATOM   212   N ND1 . HIS A 1 26  ? 23.625  31.730  28.094  1.00 31.26  ? 55  HIS A ND1 1 
ATOM   213   C CD2 . HIS A 1 26  ? 25.066  30.628  26.885  1.00 33.86  ? 55  HIS A CD2 1 
ATOM   214   C CE1 . HIS A 1 26  ? 24.416  32.622  27.506  1.00 32.63  ? 55  HIS A CE1 1 
ATOM   215   N NE2 . HIS A 1 26  ? 25.301  31.980  26.771  1.00 35.05  ? 55  HIS A NE2 1 
ATOM   216   N N   . GLY A 1 27  ? 22.883  26.984  30.949  1.00 33.82  ? 56  GLY A N   1 
ATOM   217   C CA  . GLY A 1 27  ? 22.053  25.884  31.414  1.00 34.65  ? 56  GLY A CA  1 
ATOM   218   C C   . GLY A 1 27  ? 20.735  26.335  32.038  1.00 36.61  ? 56  GLY A C   1 
ATOM   219   O O   . GLY A 1 27  ? 19.703  25.692  31.831  1.00 33.25  ? 56  GLY A O   1 
ATOM   220   N N   . LYS A 1 28  ? 20.763  27.429  32.815  1.00 36.00  ? 57  LYS A N   1 
ATOM   221   C CA  . LYS A 1 28  ? 19.604  27.832  33.607  1.00 40.43  ? 57  LYS A CA  1 
ATOM   222   C C   . LYS A 1 28  ? 18.705  28.829  32.870  1.00 38.42  ? 57  LYS A C   1 
ATOM   223   O O   . LYS A 1 28  ? 17.680  29.235  33.421  1.00 40.39  ? 57  LYS A O   1 
ATOM   224   C CB  . LYS A 1 28  ? 20.041  28.382  34.971  1.00 44.38  ? 57  LYS A CB  1 
ATOM   225   C CG  . LYS A 1 28  ? 20.258  27.297  36.014  1.00 50.89  ? 57  LYS A CG  1 
ATOM   226   C CD  . LYS A 1 28  ? 20.958  27.728  37.273  1.00 51.53  ? 57  LYS A CD  1 
ATOM   227   C CE  . LYS A 1 28  ? 21.480  26.537  38.048  1.00 56.87  ? 57  LYS A CE  1 
ATOM   228   N NZ  . LYS A 1 28  ? 20.382  25.704  38.593  1.00 56.26  ? 57  LYS A NZ  1 
ATOM   229   N N   . THR A 1 29  ? 19.062  29.187  31.631  1.00 35.12  ? 58  THR A N   1 
ATOM   230   C CA  . THR A 1 29  ? 18.240  30.065  30.805  1.00 35.77  ? 58  THR A CA  1 
ATOM   231   C C   . THR A 1 29  ? 16.878  29.430  30.528  1.00 36.42  ? 58  THR A C   1 
ATOM   232   O O   . THR A 1 29  ? 16.774  28.253  30.175  1.00 30.82  ? 58  THR A O   1 
ATOM   233   C CB  . THR A 1 29  ? 18.907  30.391  29.463  1.00 37.70  ? 58  THR A CB  1 
ATOM   234   O OG1 . THR A 1 29  ? 20.090  31.140  29.721  1.00 37.78  ? 58  THR A OG1 1 
ATOM   235   C CG2 . THR A 1 29  ? 18.019  31.194  28.540  1.00 39.35  ? 58  THR A CG2 1 
ATOM   236   N N   . VAL A 1 30  ? 15.834  30.249  30.673  1.00 36.95  ? 59  VAL A N   1 
ATOM   237   C CA  . VAL A 1 30  ? 14.479  29.843  30.368  1.00 37.39  ? 59  VAL A CA  1 
ATOM   238   C C   . VAL A 1 30  ? 14.286  30.051  28.867  1.00 39.03  ? 59  VAL A C   1 
ATOM   239   O O   . VAL A 1 30  ? 14.611  31.106  28.324  1.00 38.01  ? 59  VAL A O   1 
ATOM   240   C CB  . VAL A 1 30  ? 13.474  30.627  31.236  1.00 34.97  ? 59  VAL A CB  1 
ATOM   241   C CG1 . VAL A 1 30  ? 12.042  30.492  30.747  1.00 35.64  ? 59  VAL A CG1 1 
ATOM   242   C CG2 . VAL A 1 30  ? 13.580  30.226  32.701  1.00 35.85  ? 59  VAL A CG2 1 
ATOM   243   N N   . VAL A 1 31  ? 13.840  28.995  28.184  1.00 38.55  ? 60  VAL A N   1 
ATOM   244   C CA  . VAL A 1 31  ? 13.623  29.074  26.751  1.00 35.78  ? 60  VAL A CA  1 
ATOM   245   C C   . VAL A 1 31  ? 12.131  29.058  26.445  1.00 31.00  ? 60  VAL A C   1 
ATOM   246   O O   . VAL A 1 31  ? 11.743  29.386  25.326  1.00 34.57  ? 60  VAL A O   1 
ATOM   247   C CB  . VAL A 1 31  ? 14.359  27.957  25.988  1.00 37.53  ? 60  VAL A CB  1 
ATOM   248   C CG1 . VAL A 1 31  ? 15.856  28.180  25.999  1.00 38.24  ? 60  VAL A CG1 1 
ATOM   249   C CG2 . VAL A 1 31  ? 14.022  26.580  26.527  1.00 38.15  ? 60  VAL A CG2 1 
ATOM   250   N N   . GLY A 1 32  ? 11.302  28.665  27.412  1.00 31.07  ? 61  GLY A N   1 
ATOM   251   C CA  . GLY A 1 32  ? 9.871   28.588  27.170  1.00 31.03  ? 61  GLY A CA  1 
ATOM   252   C C   . GLY A 1 32  ? 9.068   28.366  28.442  1.00 33.11  ? 61  GLY A C   1 
ATOM   253   O O   . GLY A 1 32  ? 9.613   27.998  29.487  1.00 35.01  ? 61  GLY A O   1 
ATOM   254   N N   . GLN A 1 33  ? 7.760   28.621  28.314  1.00 34.58  ? 62  GLN A N   1 
ATOM   255   C CA  . GLN A 1 33  ? 6.794   28.428  29.378  1.00 34.46  ? 62  GLN A CA  1 
ATOM   256   C C   . GLN A 1 33  ? 5.944   27.209  29.040  1.00 31.40  ? 62  GLN A C   1 
ATOM   257   O O   . GLN A 1 33  ? 5.873   26.792  27.886  1.00 33.22  ? 62  GLN A O   1 
ATOM   258   C CB  . GLN A 1 33  ? 5.894   29.659  29.533  1.00 37.32  ? 62  GLN A CB  1 
ATOM   259   C CG  . GLN A 1 33  ? 6.635   30.998  29.559  1.00 45.42  ? 62  GLN A CG  1 
ATOM   260   C CD  . GLN A 1 33  ? 7.258   31.315  30.898  1.00 56.00  ? 62  GLN A CD  1 
ATOM   261   O OE1 . GLN A 1 33  ? 8.479   31.405  31.029  1.00 70.82  ? 62  GLN A OE1 1 
ATOM   262   N NE2 . GLN A 1 33  ? 6.420   31.498  31.908  1.00 54.22  ? 62  GLN A NE2 1 
ATOM   263   N N   . ILE A 1 34  ? 5.256   26.684  30.055  1.00 28.45  ? 63  ILE A N   1 
ATOM   264   C CA  . ILE A 1 34  ? 4.375   25.546  29.878  1.00 28.25  ? 63  ILE A CA  1 
ATOM   265   C C   . ILE A 1 34  ? 2.998   25.894  30.420  1.00 23.97  ? 63  ILE A C   1 
ATOM   266   O O   . ILE A 1 34  ? 2.851   26.057  31.620  1.00 24.35  ? 63  ILE A O   1 
ATOM   267   C CB  . ILE A 1 34  ? 4.934   24.304  30.584  1.00 26.20  ? 63  ILE A CB  1 
ATOM   268   C CG1 . ILE A 1 34  ? 6.332   23.964  30.065  1.00 28.62  ? 63  ILE A CG1 1 
ATOM   269   C CG2 . ILE A 1 34  ? 3.945   23.147  30.454  1.00 26.68  ? 63  ILE A CG2 1 
ATOM   270   C CD1 . ILE A 1 34  ? 6.859   22.605  30.484  1.00 27.62  ? 63  ILE A CD1 1 
ATOM   271   N N   . THR A 1 35  ? 1.975   25.903  29.553  1.00 25.60  ? 64  THR A N   1 
ATOM   272   C CA  . THR A 1 35  ? 0.630   26.176  30.028  1.00 25.02  ? 64  THR A CA  1 
ATOM   273   C C   . THR A 1 35  ? -0.114  24.867  30.238  1.00 26.12  ? 64  THR A C   1 
ATOM   274   O O   . THR A 1 35  ? 0.347   23.807  29.825  1.00 26.17  ? 64  THR A O   1 
ATOM   275   C CB  . THR A 1 35  ? -0.161  27.118  29.112  1.00 25.55  ? 64  THR A CB  1 
ATOM   276   O OG1 . THR A 1 35  ? -0.368  26.456  27.863  1.00 26.64  ? 64  THR A OG1 1 
ATOM   277   C CG2 . THR A 1 35  ? 0.512   28.463  28.920  1.00 25.65  ? 64  THR A CG2 1 
ATOM   278   N N   . VAL A 1 36  ? -1.249  24.975  30.934  1.00 25.53  ? 65  VAL A N   1 
ATOM   279   C CA  . VAL A 1 36  ? -2.191  23.883  31.078  1.00 25.77  ? 65  VAL A CA  1 
ATOM   280   C C   . VAL A 1 36  ? -2.616  23.374  29.699  1.00 27.47  ? 65  VAL A C   1 
ATOM   281   O O   . VAL A 1 36  ? -2.751  22.165  29.485  1.00 24.64  ? 65  VAL A O   1 
ATOM   282   C CB  . VAL A 1 36  ? -3.411  24.346  31.892  1.00 25.45  ? 65  VAL A CB  1 
ATOM   283   C CG1 . VAL A 1 36  ? -4.554  23.351  31.821  1.00 24.91  ? 65  VAL A CG1 1 
ATOM   284   C CG2 . VAL A 1 36  ? -3.015  24.625  33.333  1.00 26.10  ? 65  VAL A CG2 1 
ATOM   285   N N   . ASP A 1 37  ? -2.843  24.308  28.772  1.00 27.55  ? 66  ASP A N   1 
ATOM   286   C CA  . ASP A 1 37  ? -3.355  23.977  27.451  1.00 32.29  ? 66  ASP A CA  1 
ATOM   287   C C   . ASP A 1 37  ? -2.355  23.124  26.671  1.00 29.03  ? 66  ASP A C   1 
ATOM   288   O O   . ASP A 1 37  ? -2.752  22.217  25.941  1.00 31.35  ? 66  ASP A O   1 
ATOM   289   C CB  . ASP A 1 37  ? -3.734  25.240  26.679  1.00 33.33  ? 66  ASP A CB  1 
ATOM   290   C CG  . ASP A 1 37  ? -5.179  25.658  26.881  1.00 33.10  ? 66  ASP A CG  1 
ATOM   291   O OD1 . ASP A 1 37  ? -5.991  24.786  27.294  1.00 31.07  ? 66  ASP A OD1 1 
ATOM   292   O OD2 . ASP A 1 37  ? -5.487  26.862  26.604  1.00 32.27  ? 66  ASP A OD2 1 
ATOM   293   N N   . MET A 1 38  ? -1.070  23.410  26.861  1.00 28.67  ? 67  MET A N   1 
ATOM   294   C CA  . MET A 1 38  ? 0.002   22.714  26.168  1.00 28.13  ? 67  MET A CA  1 
ATOM   295   C C   . MET A 1 38  ? 0.098   21.285  26.681  1.00 26.31  ? 67  MET A C   1 
ATOM   296   O O   . MET A 1 38  ? 0.360   20.371  25.908  1.00 25.62  ? 67  MET A O   1 
ATOM   297   C CB  . MET A 1 38  ? 1.342   23.408  26.416  1.00 31.35  ? 67  MET A CB  1 
ATOM   298   C CG  . MET A 1 38  ? 1.511   24.712  25.634  1.00 34.54  ? 67  MET A CG  1 
ATOM   299   S SD  . MET A 1 38  ? 2.958   25.620  26.246  1.00 41.15  ? 67  MET A SD  1 
ATOM   300   C CE  . MET A 1 38  ? 2.814   27.156  25.337  1.00 37.11  ? 67  MET A CE  1 
ATOM   301   N N   . MET A 1 39  ? -0.060  21.131  28.002  1.00 24.45  ? 68  MET A N   1 
ATOM   302   C CA  . MET A 1 39  ? -0.045  19.831  28.651  1.00 24.75  ? 68  MET A CA  1 
ATOM   303   C C   . MET A 1 39  ? -1.179  18.966  28.129  1.00 24.28  ? 68  MET A C   1 
ATOM   304   O O   . MET A 1 39  ? -1.004  17.761  27.917  1.00 24.06  ? 68  MET A O   1 
ATOM   305   C CB  . MET A 1 39  ? -0.153  19.997  30.166  1.00 25.22  ? 68  MET A CB  1 
ATOM   306   C CG  . MET A 1 39  ? 1.174   20.390  30.801  1.00 26.35  ? 68  MET A CG  1 
ATOM   307   S SD  . MET A 1 39  ? 1.074   20.460  32.580  1.00 28.95  ? 68  MET A SD  1 
ATOM   308   C CE  . MET A 1 39  ? 1.162   18.704  32.945  1.00 29.22  ? 68  MET A CE  1 
ATOM   309   N N   . TYR A 1 40  ? -2.343  19.579  27.878  1.00 23.77  ? 69  TYR A N   1 
ATOM   310   C CA  . TYR A 1 40  ? -3.466  18.870  27.283  1.00 24.22  ? 69  TYR A CA  1 
ATOM   311   C C   . TYR A 1 40  ? -3.294  18.708  25.769  1.00 23.56  ? 69  TYR A C   1 
ATOM   312   O O   . TYR A 1 40  ? -3.770  17.742  25.202  1.00 26.80  ? 69  TYR A O   1 
ATOM   313   C CB  . TYR A 1 40  ? -4.783  19.586  27.588  1.00 21.42  ? 69  TYR A CB  1 
ATOM   314   C CG  . TYR A 1 40  ? -5.346  19.307  28.954  1.00 22.56  ? 69  TYR A CG  1 
ATOM   315   C CD1 . TYR A 1 40  ? -5.928  18.089  29.255  1.00 22.19  ? 69  TYR A CD1 1 
ATOM   316   C CD2 . TYR A 1 40  ? -5.269  20.249  29.961  1.00 21.47  ? 69  TYR A CD2 1 
ATOM   317   C CE1 . TYR A 1 40  ? -6.413  17.818  30.523  1.00 22.65  ? 69  TYR A CE1 1 
ATOM   318   C CE2 . TYR A 1 40  ? -5.764  20.005  31.224  1.00 21.74  ? 69  TYR A CE2 1 
ATOM   319   C CZ  . TYR A 1 40  ? -6.340  18.786  31.508  1.00 21.42  ? 69  TYR A CZ  1 
ATOM   320   O OH  . TYR A 1 40  ? -6.815  18.560  32.766  1.00 27.41  ? 69  TYR A OH  1 
ATOM   321   N N   . GLY A 1 41  ? -2.583  19.632  25.115  1.00 24.08  ? 70  GLY A N   1 
ATOM   322   C CA  . GLY A 1 41  ? -2.563  19.722  23.659  1.00 23.23  ? 70  GLY A CA  1 
ATOM   323   C C   . GLY A 1 41  ? -1.338  19.043  23.030  1.00 24.08  ? 70  GLY A C   1 
ATOM   324   O O   . GLY A 1 41  ? -0.910  19.439  21.954  1.00 23.17  ? 70  GLY A O   1 
ATOM   325   N N   . GLY A 1 42  ? -0.770  18.032  23.704  1.00 22.27  ? 71  GLY A N   1 
ATOM   326   C CA  . GLY A 1 42  ? 0.300   17.232  23.110  1.00 23.76  ? 71  GLY A CA  1 
ATOM   327   C C   . GLY A 1 42  ? 1.615   17.991  22.953  1.00 24.73  ? 71  GLY A C   1 
ATOM   328   O O   . GLY A 1 42  ? 2.294   17.879  21.928  1.00 22.79  ? 71  GLY A O   1 
ATOM   329   N N   . MET A 1 43  ? 1.945   18.760  23.991  1.00 23.89  ? 72  MET A N   1 
ATOM   330   C CA  . MET A 1 43  ? 3.164   19.541  24.068  1.00 23.85  ? 72  MET A CA  1 
ATOM   331   C C   . MET A 1 43  ? 3.321   20.466  22.865  1.00 25.04  ? 72  MET A C   1 
ATOM   332   O O   . MET A 1 43  ? 4.445   20.798  22.512  1.00 23.22  ? 72  MET A O   1 
ATOM   333   C CB  . MET A 1 43  ? 4.406   18.648  24.111  1.00 25.00  ? 72  MET A CB  1 
ATOM   334   C CG  . MET A 1 43  ? 4.390   17.573  25.166  1.00 24.73  ? 72  MET A CG  1 
ATOM   335   S SD  . MET A 1 43  ? 5.858   16.547  24.922  1.00 28.85  ? 72  MET A SD  1 
ATOM   336   C CE  . MET A 1 43  ? 5.916   15.718  26.505  1.00 27.52  ? 72  MET A CE  1 
ATOM   337   N N   . ARG A 1 44  ? 2.213   20.943  22.303  1.00 26.86  ? 73  ARG A N   1 
ATOM   338   C CA  . ARG A 1 44  ? 2.239   21.804  21.124  1.00 31.64  ? 73  ARG A CA  1 
ATOM   339   C C   . ARG A 1 44  ? 2.875   23.128  21.537  1.00 28.36  ? 73  ARG A C   1 
ATOM   340   O O   . ARG A 1 44  ? 2.491   23.695  22.544  1.00 28.01  ? 73  ARG A O   1 
ATOM   341   C CB  . ARG A 1 44  ? 0.803   21.980  20.612  1.00 34.59  ? 73  ARG A CB  1 
ATOM   342   C CG  . ARG A 1 44  ? 0.651   22.783  19.329  1.00 42.41  ? 73  ARG A CG  1 
ATOM   343   C CD  . ARG A 1 44  ? -0.820  23.017  18.992  1.00 45.98  ? 73  ARG A CD  1 
ATOM   344   N NE  . ARG A 1 44  ? -1.027  23.377  17.586  1.00 54.88  ? 73  ARG A NE  1 
ATOM   345   C CZ  . ARG A 1 44  ? -1.012  22.522  16.558  1.00 55.13  ? 73  ARG A CZ  1 
ATOM   346   N NH1 . ARG A 1 44  ? -1.001  21.215  16.760  1.00 54.61  ? 73  ARG A NH1 1 
ATOM   347   N NH2 . ARG A 1 44  ? -1.046  22.983  15.318  1.00 58.96  ? 73  ARG A NH2 1 
ATOM   348   N N   . GLY A 1 45  ? 3.911   23.554  20.814  1.00 30.04  ? 74  GLY A N   1 
ATOM   349   C CA  . GLY A 1 45  ? 4.618   24.779  21.154  1.00 33.91  ? 74  GLY A CA  1 
ATOM   350   C C   . GLY A 1 45  ? 5.713   24.605  22.211  1.00 30.09  ? 74  GLY A C   1 
ATOM   351   O O   . GLY A 1 45  ? 6.414   25.561  22.506  1.00 33.83  ? 74  GLY A O   1 
ATOM   352   N N   . MET A 1 46  ? 5.889   23.407  22.774  1.00 30.27  ? 75  MET A N   1 
ATOM   353   C CA  . MET A 1 46  ? 6.882   23.222  23.825  1.00 30.43  ? 75  MET A CA  1 
ATOM   354   C C   . MET A 1 46  ? 8.245   22.935  23.196  1.00 30.22  ? 75  MET A C   1 
ATOM   355   O O   . MET A 1 46  ? 8.360   22.046  22.359  1.00 26.28  ? 75  MET A O   1 
ATOM   356   C CB  . MET A 1 46  ? 6.526   22.037  24.723  1.00 30.40  ? 75  MET A CB  1 
ATOM   357   C CG  . MET A 1 46  ? 5.576   22.348  25.832  1.00 35.10  ? 75  MET A CG  1 
ATOM   358   S SD  . MET A 1 46  ? 5.629   21.014  27.080  1.00 44.49  ? 75  MET A SD  1 
ATOM   359   C CE  . MET A 1 46  ? 3.890   20.798  27.452  1.00 45.35  ? 75  MET A CE  1 
ATOM   360   N N   . LYS A 1 47  ? 9.291   23.644  23.629  1.00 32.65  ? 76  LYS A N   1 
ATOM   361   C CA  . LYS A 1 47  ? 10.650  23.276  23.247  1.00 35.08  ? 76  LYS A CA  1 
ATOM   362   C C   . LYS A 1 47  ? 11.127  22.156  24.175  1.00 35.00  ? 76  LYS A C   1 
ATOM   363   O O   . LYS A 1 47  ? 11.524  22.385  25.325  1.00 40.14  ? 76  LYS A O   1 
ATOM   364   C CB  . LYS A 1 47  ? 11.531  24.527  23.198  1.00 39.85  ? 76  LYS A CB  1 
ATOM   365   C CG  . LYS A 1 47  ? 11.305  25.378  21.955  1.00 43.60  ? 76  LYS A CG  1 
ATOM   366   C CD  . LYS A 1 47  ? 11.777  26.818  22.055  1.00 50.13  ? 76  LYS A CD  1 
ATOM   367   C CE  . LYS A 1 47  ? 13.262  26.972  21.794  1.00 59.05  ? 76  LYS A CE  1 
ATOM   368   N NZ  . LYS A 1 47  ? 14.087  26.366  22.869  1.00 60.96  ? 76  LYS A NZ  1 
ATOM   369   N N   . GLY A 1 48  ? 11.081  20.920  23.666  1.00 30.35  ? 77  GLY A N   1 
ATOM   370   C CA  . GLY A 1 48  ? 11.164  19.761  24.539  1.00 29.60  ? 77  GLY A CA  1 
ATOM   371   C C   . GLY A 1 48  ? 12.470  18.975  24.445  1.00 26.28  ? 77  GLY A C   1 
ATOM   372   O O   . GLY A 1 48  ? 12.823  18.288  25.400  1.00 27.30  ? 77  GLY A O   1 
ATOM   373   N N   . LEU A 1 49  ? 13.143  18.981  23.288  1.00 24.13  ? 78  LEU A N   1 
ATOM   374   C CA  . LEU A 1 49  ? 14.315  18.130  23.150  1.00 21.95  ? 78  LEU A CA  1 
ATOM   375   C C   . LEU A 1 49  ? 15.327  18.758  22.208  1.00 21.95  ? 78  LEU A C   1 
ATOM   376   O O   . LEU A 1 49  ? 14.972  19.575  21.367  1.00 24.18  ? 78  LEU A O   1 
ATOM   377   C CB  . LEU A 1 49  ? 13.917  16.712  22.712  1.00 22.18  ? 78  LEU A CB  1 
ATOM   378   C CG  . LEU A 1 49  ? 13.485  16.520  21.258  1.00 23.98  ? 78  LEU A CG  1 
ATOM   379   C CD1 . LEU A 1 49  ? 13.797  15.103  20.763  1.00 26.62  ? 78  LEU A CD1 1 
ATOM   380   C CD2 . LEU A 1 49  ? 11.988  16.783  21.094  1.00 24.42  ? 78  LEU A CD2 1 
ATOM   381   N N   . VAL A 1 50  ? 16.606  18.408  22.412  1.00 23.61  ? 79  VAL A N   1 
ATOM   382   C CA  . VAL A 1 50  ? 17.646  18.767  21.470  1.00 23.75  ? 79  VAL A CA  1 
ATOM   383   C C   . VAL A 1 50  ? 17.760  17.632  20.458  1.00 22.10  ? 79  VAL A C   1 
ATOM   384   O O   . VAL A 1 50  ? 17.856  16.465  20.828  1.00 21.21  ? 79  VAL A O   1 
ATOM   385   C CB  . VAL A 1 50  ? 18.999  19.068  22.141  1.00 24.35  ? 79  VAL A CB  1 
ATOM   386   C CG1 . VAL A 1 50  ? 20.125  19.192  21.121  1.00 23.36  ? 79  VAL A CG1 1 
ATOM   387   C CG2 . VAL A 1 50  ? 18.921  20.301  23.025  1.00 28.49  ? 79  VAL A CG2 1 
ATOM   388   N N   . TYR A 1 51  ? 17.730  18.007  19.186  1.00 21.50  ? 80  TYR A N   1 
ATOM   389   C CA  . TYR A 1 51  ? 17.829  17.089  18.066  1.00 20.58  ? 80  TYR A CA  1 
ATOM   390   C C   . TYR A 1 51  ? 18.717  17.792  17.051  1.00 23.72  ? 80  TYR A C   1 
ATOM   391   O O   . TYR A 1 51  ? 18.432  18.935  16.721  1.00 27.34  ? 80  TYR A O   1 
ATOM   392   C CB  . TYR A 1 51  ? 16.424  16.773  17.542  1.00 20.88  ? 80  TYR A CB  1 
ATOM   393   C CG  . TYR A 1 51  ? 16.265  15.616  16.598  1.00 20.69  ? 80  TYR A CG  1 
ATOM   394   C CD1 . TYR A 1 51  ? 16.437  15.755  15.229  1.00 21.47  ? 80  TYR A CD1 1 
ATOM   395   C CD2 . TYR A 1 51  ? 15.913  14.378  17.083  1.00 21.77  ? 80  TYR A CD2 1 
ATOM   396   C CE1 . TYR A 1 51  ? 16.201  14.696  14.365  1.00 23.13  ? 80  TYR A CE1 1 
ATOM   397   C CE2 . TYR A 1 51  ? 15.720  13.295  16.247  1.00 20.90  ? 80  TYR A CE2 1 
ATOM   398   C CZ  . TYR A 1 51  ? 15.879  13.452  14.882  1.00 22.42  ? 80  TYR A CZ  1 
ATOM   399   O OH  . TYR A 1 51  ? 15.659  12.368  14.075  1.00 23.18  ? 80  TYR A OH  1 
ATOM   400   N N   . GLU A 1 52  ? 19.843  17.161  16.659  1.00 23.49  ? 81  GLU A N   1 
ATOM   401   C CA  . GLU A 1 52  ? 20.934  17.898  16.036  1.00 22.79  ? 81  GLU A CA  1 
ATOM   402   C C   . GLU A 1 52  ? 20.835  17.824  14.512  1.00 21.75  ? 81  GLU A C   1 
ATOM   403   O O   . GLU A 1 52  ? 21.321  18.686  13.802  1.00 25.64  ? 81  GLU A O   1 
ATOM   404   C CB  . GLU A 1 52  ? 22.291  17.307  16.432  1.00 25.24  ? 81  GLU A CB  1 
ATOM   405   C CG  . GLU A 1 52  ? 22.608  17.325  17.930  1.00 23.80  ? 81  GLU A CG  1 
ATOM   406   C CD  . GLU A 1 52  ? 22.909  18.708  18.489  1.00 26.40  ? 81  GLU A CD  1 
ATOM   407   O OE1 . GLU A 1 52  ? 22.708  19.702  17.751  1.00 27.55  ? 81  GLU A OE1 1 
ATOM   408   O OE2 . GLU A 1 52  ? 23.276  18.808  19.694  1.00 29.36  ? 81  GLU A OE2 1 
ATOM   409   N N   . THR A 1 53  ? 20.310  16.722  14.001  1.00 20.20  ? 82  THR A N   1 
ATOM   410   C CA  . THR A 1 53  ? 20.485  16.411  12.596  1.00 21.66  ? 82  THR A CA  1 
ATOM   411   C C   . THR A 1 53  ? 19.679  17.347  11.697  1.00 20.27  ? 82  THR A C   1 
ATOM   412   O O   . THR A 1 53  ? 20.125  17.665  10.602  1.00 25.35  ? 82  THR A O   1 
ATOM   413   C CB  . THR A 1 53  ? 20.129  14.947  12.334  1.00 23.21  ? 82  THR A CB  1 
ATOM   414   O OG1 . THR A 1 53  ? 18.847  14.618  12.871  1.00 24.66  ? 82  THR A OG1 1 
ATOM   415   C CG2 . THR A 1 53  ? 21.181  14.025  12.894  1.00 23.53  ? 82  THR A CG2 1 
ATOM   416   N N   . SER A 1 54  ? 18.453  17.697  12.092  1.00 22.92  ? 83  SER A N   1 
ATOM   417   C CA  . SER A 1 54  ? 17.649  18.647  11.327  1.00 22.65  ? 83  SER A CA  1 
ATOM   418   C C   . SER A 1 54  ? 16.799  19.514  12.249  1.00 23.55  ? 83  SER A C   1 
ATOM   419   O O   . SER A 1 54  ? 16.497  19.150  13.400  1.00 23.14  ? 83  SER A O   1 
ATOM   420   C CB  . SER A 1 54  ? 16.812  17.969  10.289  1.00 23.91  ? 83  SER A CB  1 
ATOM   421   O OG  . SER A 1 54  ? 15.888  17.079  10.893  1.00 21.67  ? 83  SER A OG  1 
ATOM   422   N N   . VAL A 1 55  ? 16.456  20.691  11.715  1.00 22.12  ? 84  VAL A N   1 
ATOM   423   C CA  . VAL A 1 55  ? 15.587  21.668  12.350  1.00 26.04  ? 84  VAL A CA  1 
ATOM   424   C C   . VAL A 1 55  ? 14.541  22.154  11.347  1.00 27.01  ? 84  VAL A C   1 
ATOM   425   O O   . VAL A 1 55  ? 14.892  22.539  10.229  1.00 25.64  ? 84  VAL A O   1 
ATOM   426   C CB  . VAL A 1 55  ? 16.395  22.869  12.867  1.00 25.57  ? 84  VAL A CB  1 
ATOM   427   C CG1 . VAL A 1 55  ? 15.482  23.881  13.547  1.00 25.67  ? 84  VAL A CG1 1 
ATOM   428   C CG2 . VAL A 1 55  ? 17.517  22.439  13.795  1.00 26.99  ? 84  VAL A CG2 1 
ATOM   429   N N   . LEU A 1 56  ? 13.268  22.138  11.781  1.00 26.58  ? 85  LEU A N   1 
ATOM   430   C CA  . LEU A 1 56  ? 12.122  22.582  11.004  1.00 27.15  ? 85  LEU A CA  1 
ATOM   431   C C   . LEU A 1 56  ? 11.746  24.005  11.397  1.00 31.05  ? 85  LEU A C   1 
ATOM   432   O O   . LEU A 1 56  ? 11.218  24.247  12.497  1.00 30.44  ? 85  LEU A O   1 
ATOM   433   C CB  . LEU A 1 56  ? 10.954  21.632  11.275  1.00 28.02  ? 85  LEU A CB  1 
ATOM   434   C CG  . LEU A 1 56  ? 9.617   22.011  10.644  1.00 28.40  ? 85  LEU A CG  1 
ATOM   435   C CD1 . LEU A 1 56  ? 9.734   22.036  9.120   1.00 28.49  ? 85  LEU A CD1 1 
ATOM   436   C CD2 . LEU A 1 56  ? 8.534   21.034  11.086  1.00 27.59  ? 85  LEU A CD2 1 
ATOM   437   N N   . ASP A 1 57  ? 12.022  24.933  10.483  1.00 30.90  ? 86  ASP A N   1 
ATOM   438   C CA  . ASP A 1 57  ? 11.575  26.303  10.637  1.00 36.84  ? 86  ASP A CA  1 
ATOM   439   C C   . ASP A 1 57  ? 10.097  26.383  10.257  1.00 37.34  ? 86  ASP A C   1 
ATOM   440   O O   . ASP A 1 57  ? 9.704   25.911  9.201   1.00 36.79  ? 86  ASP A O   1 
ATOM   441   C CB  . ASP A 1 57  ? 12.419  27.252  9.784   1.00 38.33  ? 86  ASP A CB  1 
ATOM   442   C CG  . ASP A 1 57  ? 11.853  28.661  9.736   1.00 40.51  ? 86  ASP A CG  1 
ATOM   443   O OD1 . ASP A 1 57  ? 11.633  29.227  10.812  1.00 41.15  ? 86  ASP A OD1 1 
ATOM   444   O OD2 . ASP A 1 57  ? 11.623  29.170  8.620   1.00 45.39  ? 86  ASP A OD2 1 
ATOM   445   N N   . PRO A 1 58  ? 9.214   26.998  11.078  1.00 40.69  ? 87  PRO A N   1 
ATOM   446   C CA  . PRO A 1 58  ? 7.802   27.122  10.707  1.00 40.06  ? 87  PRO A CA  1 
ATOM   447   C C   . PRO A 1 58  ? 7.562   27.644  9.291   1.00 41.66  ? 87  PRO A C   1 
ATOM   448   O O   . PRO A 1 58  ? 6.678   27.160  8.583   1.00 37.88  ? 87  PRO A O   1 
ATOM   449   C CB  . PRO A 1 58  ? 7.286   28.132  11.739  1.00 40.30  ? 87  PRO A CB  1 
ATOM   450   C CG  . PRO A 1 58  ? 8.118   27.834  12.961  1.00 39.23  ? 87  PRO A CG  1 
ATOM   451   C CD  . PRO A 1 58  ? 9.499   27.544  12.417  1.00 39.47  ? 87  PRO A CD  1 
ATOM   452   N N   . ASP A 1 59  ? 8.365   28.633  8.893   1.00 44.46  ? 88  ASP A N   1 
ATOM   453   C CA  . ASP A 1 59  ? 8.113   29.386  7.677   1.00 47.73  ? 88  ASP A CA  1 
ATOM   454   C C   . ASP A 1 59  ? 8.802   28.728  6.484   1.00 45.89  ? 88  ASP A C   1 
ATOM   455   O O   . ASP A 1 59  ? 8.187   28.623  5.424   1.00 47.26  ? 88  ASP A O   1 
ATOM   456   C CB  . ASP A 1 59  ? 8.539   30.848  7.845   1.00 51.37  ? 88  ASP A CB  1 
ATOM   457   C CG  . ASP A 1 59  ? 7.819   31.568  8.979   1.00 54.65  ? 88  ASP A CG  1 
ATOM   458   O OD1 . ASP A 1 59  ? 6.611   31.326  9.153   1.00 55.33  ? 88  ASP A OD1 1 
ATOM   459   O OD2 . ASP A 1 59  ? 8.463   32.383  9.665   1.00 60.89  ? 88  ASP A OD2 1 
ATOM   460   N N   . GLU A 1 60  ? 10.067  28.297  6.649   1.00 45.78  ? 89  GLU A N   1 
ATOM   461   C CA  . GLU A 1 60  ? 10.910  27.903  5.521   1.00 44.60  ? 89  GLU A CA  1 
ATOM   462   C C   . GLU A 1 60  ? 11.028  26.382  5.377   1.00 36.66  ? 89  GLU A C   1 
ATOM   463   O O   . GLU A 1 60  ? 11.564  25.898  4.387   1.00 34.07  ? 89  GLU A O   1 
ATOM   464   C CB  . GLU A 1 60  ? 12.316  28.493  5.659   1.00 48.18  ? 89  GLU A CB  1 
ATOM   465   C CG  . GLU A 1 60  ? 12.346  30.003  5.813   1.00 57.50  ? 89  GLU A CG  1 
ATOM   466   C CD  . GLU A 1 60  ? 11.871  30.794  4.609   1.00 62.49  ? 89  GLU A CD  1 
ATOM   467   O OE1 . GLU A 1 60  ? 12.609  30.835  3.605   1.00 65.91  ? 89  GLU A OE1 1 
ATOM   468   O OE2 . GLU A 1 60  ? 10.760  31.368  4.680   1.00 71.99  ? 89  GLU A OE2 1 
ATOM   469   N N   . GLY A 1 61  ? 10.564  25.608  6.362   1.00 33.27  ? 90  GLY A N   1 
ATOM   470   C CA  . GLY A 1 61  ? 10.634  24.156  6.251   1.00 27.19  ? 90  GLY A CA  1 
ATOM   471   C C   . GLY A 1 61  ? 11.998  23.594  6.666   1.00 27.48  ? 90  GLY A C   1 
ATOM   472   O O   . GLY A 1 61  ? 12.826  24.268  7.281   1.00 27.35  ? 90  GLY A O   1 
ATOM   473   N N   . ILE A 1 62  ? 12.230  22.332  6.305   1.00 24.58  ? 91  ILE A N   1 
ATOM   474   C CA  . ILE A 1 62  ? 13.250  21.533  6.953   1.00 25.82  ? 91  ILE A CA  1 
ATOM   475   C C   . ILE A 1 62  ? 14.632  21.926  6.438   1.00 27.28  ? 91  ILE A C   1 
ATOM   476   O O   . ILE A 1 62  ? 14.809  22.164  5.244   1.00 30.61  ? 91  ILE A O   1 
ATOM   477   C CB  . ILE A 1 62  ? 12.927  20.035  6.764   1.00 25.43  ? 91  ILE A CB  1 
ATOM   478   C CG1 . ILE A 1 62  ? 13.811  19.155  7.651   1.00 25.02  ? 91  ILE A CG1 1 
ATOM   479   C CG2 . ILE A 1 62  ? 12.993  19.639  5.310   1.00 23.24  ? 91  ILE A CG2 1 
ATOM   480   C CD1 . ILE A 1 62  ? 13.513  19.296  9.137   1.00 23.92  ? 91  ILE A CD1 1 
ATOM   481   N N   . ARG A 1 63  ? 15.592  22.012  7.371   1.00 27.35  ? 92  ARG A N   1 
ATOM   482   C CA  . ARG A 1 63  ? 17.007  22.142  7.058   1.00 26.41  ? 92  ARG A CA  1 
ATOM   483   C C   . ARG A 1 63  ? 17.741  20.941  7.636   1.00 22.31  ? 92  ARG A C   1 
ATOM   484   O O   . ARG A 1 63  ? 17.526  20.591  8.782   1.00 21.04  ? 92  ARG A O   1 
ATOM   485   C CB  . ARG A 1 63  ? 17.591  23.453  7.570   1.00 27.27  ? 92  ARG A CB  1 
ATOM   486   C CG  . ARG A 1 63  ? 16.916  24.658  6.931   1.00 32.51  ? 92  ARG A CG  1 
ATOM   487   C CD  . ARG A 1 63  ? 17.704  25.943  7.055   1.00 35.79  ? 92  ARG A CD  1 
ATOM   488   N NE  . ARG A 1 63  ? 17.317  26.933  6.046   1.00 40.58  ? 92  ARG A NE  1 
ATOM   489   C CZ  . ARG A 1 63  ? 18.017  27.252  4.955   1.00 46.52  ? 92  ARG A CZ  1 
ATOM   490   N NH1 . ARG A 1 63  ? 19.070  26.544  4.585   1.00 50.38  ? 92  ARG A NH1 1 
ATOM   491   N NH2 . ARG A 1 63  ? 17.645  28.278  4.204   1.00 50.18  ? 92  ARG A NH2 1 
ATOM   492   N N   . PHE A 1 64  ? 18.531  20.293  6.782   1.00 23.67  ? 93  PHE A N   1 
ATOM   493   C CA  . PHE A 1 64  ? 19.388  19.192  7.182   1.00 24.91  ? 93  PHE A CA  1 
ATOM   494   C C   . PHE A 1 64  ? 20.791  19.722  7.418   1.00 25.21  ? 93  PHE A C   1 
ATOM   495   O O   . PHE A 1 64  ? 21.479  20.028  6.430   1.00 24.99  ? 93  PHE A O   1 
ATOM   496   C CB  . PHE A 1 64  ? 19.448  18.124  6.097   1.00 25.86  ? 93  PHE A CB  1 
ATOM   497   C CG  . PHE A 1 64  ? 18.113  17.577  5.665   1.00 25.32  ? 93  PHE A CG  1 
ATOM   498   C CD1 . PHE A 1 64  ? 17.268  16.993  6.591   1.00 24.15  ? 93  PHE A CD1 1 
ATOM   499   C CD2 . PHE A 1 64  ? 17.746  17.538  4.328   1.00 29.13  ? 93  PHE A CD2 1 
ATOM   500   C CE1 . PHE A 1 64  ? 16.043  16.470  6.207   1.00 24.88  ? 93  PHE A CE1 1 
ATOM   501   C CE2 . PHE A 1 64  ? 16.524  16.998  3.938   1.00 26.69  ? 93  PHE A CE2 1 
ATOM   502   C CZ  . PHE A 1 64  ? 15.677  16.460  4.882   1.00 26.18  ? 93  PHE A CZ  1 
ATOM   503   N N   . ARG A 1 65  ? 21.172  19.817  8.713   1.00 24.07  ? 94  ARG A N   1 
ATOM   504   C CA  . ARG A 1 65  ? 22.433  20.385  9.182   1.00 21.49  ? 94  ARG A CA  1 
ATOM   505   C C   . ARG A 1 65  ? 22.665  21.767  8.557   1.00 22.76  ? 94  ARG A C   1 
ATOM   506   O O   . ARG A 1 65  ? 23.783  22.136  8.166   1.00 19.41  ? 94  ARG A O   1 
ATOM   507   C CB  . ARG A 1 65  ? 23.601  19.434  8.889   1.00 23.91  ? 94  ARG A CB  1 
ATOM   508   C CG  . ARG A 1 65  ? 23.615  18.150  9.724   1.00 23.39  ? 94  ARG A CG  1 
ATOM   509   C CD  . ARG A 1 65  ? 24.073  18.349  11.165  1.00 25.12  ? 94  ARG A CD  1 
ATOM   510   N NE  . ARG A 1 65  ? 24.411  17.119  11.866  1.00 23.78  ? 94  ARG A NE  1 
ATOM   511   C CZ  . ARG A 1 65  ? 24.809  17.054  13.128  1.00 23.25  ? 94  ARG A CZ  1 
ATOM   512   N NH1 . ARG A 1 65  ? 24.915  18.149  13.859  1.00 22.32  ? 94  ARG A NH1 1 
ATOM   513   N NH2 . ARG A 1 65  ? 25.072  15.882  13.670  1.00 23.93  ? 94  ARG A NH2 1 
ATOM   514   N N   . GLY A 1 66  ? 21.600  22.577  8.500   1.00 22.97  ? 95  GLY A N   1 
ATOM   515   C CA  . GLY A 1 66  ? 21.755  23.936  7.997   1.00 22.73  ? 95  GLY A CA  1 
ATOM   516   C C   . GLY A 1 66  ? 21.317  24.078  6.539   1.00 25.01  ? 95  GLY A C   1 
ATOM   517   O O   . GLY A 1 66  ? 20.955  25.180  6.108   1.00 27.63  ? 95  GLY A O   1 
ATOM   518   N N   . PHE A 1 67  ? 21.302  22.966  5.795   1.00 24.39  ? 96  PHE A N   1 
ATOM   519   C CA  . PHE A 1 67  ? 21.068  23.017  4.359   1.00 26.79  ? 96  PHE A CA  1 
ATOM   520   C C   . PHE A 1 67  ? 19.592  22.754  4.055   1.00 25.53  ? 96  PHE A C   1 
ATOM   521   O O   . PHE A 1 67  ? 19.017  21.757  4.494   1.00 25.68  ? 96  PHE A O   1 
ATOM   522   C CB  . PHE A 1 67  ? 21.981  22.037  3.622   1.00 29.06  ? 96  PHE A CB  1 
ATOM   523   C CG  . PHE A 1 67  ? 23.462  22.318  3.728   1.00 28.96  ? 96  PHE A CG  1 
ATOM   524   C CD1 . PHE A 1 67  ? 24.209  21.838  4.793   1.00 29.44  ? 96  PHE A CD1 1 
ATOM   525   C CD2 . PHE A 1 67  ? 24.119  23.018  2.726   1.00 31.99  ? 96  PHE A CD2 1 
ATOM   526   C CE1 . PHE A 1 67  ? 25.571  22.096  4.884   1.00 28.93  ? 96  PHE A CE1 1 
ATOM   527   C CE2 . PHE A 1 67  ? 25.487  23.241  2.798   1.00 36.07  ? 96  PHE A CE2 1 
ATOM   528   C CZ  . PHE A 1 67  ? 26.211  22.785  3.881   1.00 29.32  ? 96  PHE A CZ  1 
ATOM   529   N N   . SER A 1 68  ? 18.986  23.668  3.279   1.00 27.73  ? 97  SER A N   1 
ATOM   530   C CA  . SER A 1 68  ? 17.653  23.473  2.734   1.00 25.32  ? 97  SER A CA  1 
ATOM   531   C C   . SER A 1 68  ? 17.669  22.317  1.728   1.00 25.12  ? 97  SER A C   1 
ATOM   532   O O   . SER A 1 68  ? 18.721  21.888  1.249   1.00 23.82  ? 97  SER A O   1 
ATOM   533   C CB  . SER A 1 68  ? 17.167  24.747  2.087   1.00 29.06  ? 97  SER A CB  1 
ATOM   534   O OG  . SER A 1 68  ? 17.846  24.953  0.843   1.00 27.58  ? 97  SER A OG  1 
ATOM   535   N N   . ILE A 1 69  ? 16.491  21.804  1.380   1.00 25.11  ? 98  ILE A N   1 
ATOM   536   C CA  . ILE A 1 69  ? 16.424  20.729  0.408   1.00 26.61  ? 98  ILE A CA  1 
ATOM   537   C C   . ILE A 1 69  ? 16.989  21.165  -0.949  1.00 28.76  ? 98  ILE A C   1 
ATOM   538   O O   . ILE A 1 69  ? 17.778  20.434  -1.545  1.00 28.35  ? 98  ILE A O   1 
ATOM   539   C CB  . ILE A 1 69  ? 14.993  20.169  0.286   1.00 25.62  ? 98  ILE A CB  1 
ATOM   540   C CG1 . ILE A 1 69  ? 14.657  19.318  1.517   1.00 25.07  ? 98  ILE A CG1 1 
ATOM   541   C CG2 . ILE A 1 69  ? 14.843  19.390  -1.003  1.00 26.51  ? 98  ILE A CG2 1 
ATOM   542   C CD1 . ILE A 1 69  ? 13.272  18.701  1.504   1.00 27.96  ? 98  ILE A CD1 1 
ATOM   543   N N   . PRO A 1 70  ? 16.586  22.321  -1.523  1.00 28.92  ? 99  PRO A N   1 
ATOM   544   C CA  . PRO A 1 70  ? 17.207  22.800  -2.761  1.00 29.63  ? 99  PRO A CA  1 
ATOM   545   C C   . PRO A 1 70  ? 18.739  22.805  -2.768  1.00 29.36  ? 99  PRO A C   1 
ATOM   546   O O   . PRO A 1 70  ? 19.342  22.360  -3.743  1.00 35.71  ? 99  PRO A O   1 
ATOM   547   C CB  . PRO A 1 70  ? 16.686  24.238  -2.863  1.00 27.22  ? 99  PRO A CB  1 
ATOM   548   C CG  . PRO A 1 70  ? 15.339  24.181  -2.202  1.00 29.86  ? 99  PRO A CG  1 
ATOM   549   C CD  . PRO A 1 70  ? 15.520  23.219  -1.039  1.00 28.88  ? 99  PRO A CD  1 
ATOM   550   N N   . GLU A 1 71  ? 19.354  23.290  -1.679  1.00 30.26  ? 100 GLU A N   1 
ATOM   551   C CA  . GLU A 1 71  ? 20.805  23.255  -1.509  1.00 31.44  ? 100 GLU A CA  1 
ATOM   552   C C   . GLU A 1 71  ? 21.321  21.811  -1.557  1.00 31.13  ? 100 GLU A C   1 
ATOM   553   O O   . GLU A 1 71  ? 22.383  21.542  -2.112  1.00 31.04  ? 100 GLU A O   1 
ATOM   554   C CB  . GLU A 1 71  ? 21.217  23.952  -0.206  1.00 33.48  ? 100 GLU A CB  1 
ATOM   555   C CG  . GLU A 1 71  ? 20.830  25.430  -0.129  1.00 34.24  ? 100 GLU A CG  1 
ATOM   556   C CD  . GLU A 1 71  ? 21.179  26.189  1.151   1.00 35.85  ? 100 GLU A CD  1 
ATOM   557   O OE1 . GLU A 1 71  ? 20.705  25.796  2.247   1.00 32.03  ? 100 GLU A OE1 1 
ATOM   558   O OE2 . GLU A 1 71  ? 21.886  27.225  1.058   1.00 36.94  ? 100 GLU A OE2 1 
ATOM   559   N N   . CYS A 1 72  ? 20.595  20.873  -0.938  1.00 30.76  ? 101 CYS A N   1 
ATOM   560   C CA  . CYS A 1 72  ? 20.978  19.469  -0.976  1.00 29.28  ? 101 CYS A CA  1 
ATOM   561   C C   . CYS A 1 72  ? 20.887  18.900  -2.394  1.00 30.49  ? 101 CYS A C   1 
ATOM   562   O O   . CYS A 1 72  ? 21.712  18.089  -2.811  1.00 28.10  ? 101 CYS A O   1 
ATOM   563   C CB  . CYS A 1 72  ? 20.115  18.637  -0.041  1.00 30.97  ? 101 CYS A CB  1 
ATOM   564   S SG  . CYS A 1 72  ? 20.554  18.852  1.700   1.00 29.03  ? 101 CYS A SG  1 
ATOM   565   N N   . GLN A 1 73  ? 19.844  19.293  -3.115  1.00 29.28  ? 102 GLN A N   1 
ATOM   566   C CA  . GLN A 1 73  ? 19.666  18.836  -4.478  1.00 32.32  ? 102 GLN A CA  1 
ATOM   567   C C   . GLN A 1 73  ? 20.899  19.212  -5.299  1.00 31.80  ? 102 GLN A C   1 
ATOM   568   O O   . GLN A 1 73  ? 21.345  18.406  -6.112  1.00 36.31  ? 102 GLN A O   1 
ATOM   569   C CB  . GLN A 1 73  ? 18.340  19.373  -5.020  1.00 32.28  ? 102 GLN A CB  1 
ATOM   570   C CG  . GLN A 1 73  ? 17.156  18.601  -4.453  1.00 31.04  ? 102 GLN A CG  1 
ATOM   571   C CD  . GLN A 1 73  ? 15.856  18.948  -5.134  1.00 32.08  ? 102 GLN A CD  1 
ATOM   572   O OE1 . GLN A 1 73  ? 15.345  20.052  -5.006  1.00 30.66  ? 102 GLN A OE1 1 
ATOM   573   N NE2 . GLN A 1 73  ? 15.308  18.002  -5.877  1.00 32.88  ? 102 GLN A NE2 1 
ATOM   574   N N   . LYS A 1 74  ? 21.474  20.389  -5.035  1.00 32.22  ? 103 LYS A N   1 
ATOM   575   C CA  . LYS A 1 74  ? 22.605  20.867  -5.821  1.00 36.22  ? 103 LYS A CA  1 
ATOM   576   C C   . LYS A 1 74  ? 23.932  20.280  -5.318  1.00 36.49  ? 103 LYS A C   1 
ATOM   577   O O   . LYS A 1 74  ? 24.732  19.817  -6.134  1.00 33.51  ? 103 LYS A O   1 
ATOM   578   C CB  . LYS A 1 74  ? 22.601  22.398  -5.834  1.00 41.16  ? 103 LYS A CB  1 
ATOM   579   C CG  . LYS A 1 74  ? 21.561  23.053  -6.739  1.00 46.17  ? 103 LYS A CG  1 
ATOM   580   C CD  . LYS A 1 74  ? 21.665  22.614  -8.193  1.00 49.26  ? 103 LYS A CD  1 
ATOM   581   C CE  . LYS A 1 74  ? 21.342  23.711  -9.187  1.00 49.78  ? 103 LYS A CE  1 
ATOM   582   N NZ  . LYS A 1 74  ? 21.954  23.415  -10.502 1.00 49.70  ? 103 LYS A NZ  1 
ATOM   583   N N   . LEU A 1 75  ? 24.166  20.277  -3.988  1.00 33.41  ? 104 LEU A N   1 
ATOM   584   C CA  . LEU A 1 75  ? 25.483  19.961  -3.429  1.00 32.41  ? 104 LEU A CA  1 
ATOM   585   C C   . LEU A 1 75  ? 25.690  18.455  -3.266  1.00 30.44  ? 104 LEU A C   1 
ATOM   586   O O   . LEU A 1 75  ? 26.811  17.974  -3.414  1.00 33.39  ? 104 LEU A O   1 
ATOM   587   C CB  . LEU A 1 75  ? 25.664  20.648  -2.067  1.00 33.09  ? 104 LEU A CB  1 
ATOM   588   C CG  . LEU A 1 75  ? 25.694  22.173  -2.070  1.00 29.75  ? 104 LEU A CG  1 
ATOM   589   C CD1 . LEU A 1 75  ? 25.905  22.712  -0.671  1.00 29.90  ? 104 LEU A CD1 1 
ATOM   590   C CD2 . LEU A 1 75  ? 26.756  22.713  -3.022  1.00 31.08  ? 104 LEU A CD2 1 
ATOM   591   N N   . LEU A 1 76  ? 24.649  17.711  -2.860  1.00 30.68  ? 105 LEU A N   1 
ATOM   592   C CA  . LEU A 1 76  ? 24.850  16.313  -2.496  1.00 29.46  ? 105 LEU A CA  1 
ATOM   593   C C   . LEU A 1 76  ? 25.160  15.523  -3.758  1.00 31.36  ? 105 LEU A C   1 
ATOM   594   O O   . LEU A 1 76  ? 24.479  15.714  -4.770  1.00 30.53  ? 105 LEU A O   1 
ATOM   595   C CB  . LEU A 1 76  ? 23.608  15.739  -1.802  1.00 29.31  ? 105 LEU A CB  1 
ATOM   596   C CG  . LEU A 1 76  ? 23.376  16.176  -0.353  1.00 30.06  ? 105 LEU A CG  1 
ATOM   597   C CD1 . LEU A 1 76  ? 22.090  15.570  0.176   1.00 29.89  ? 105 LEU A CD1 1 
ATOM   598   C CD2 . LEU A 1 76  ? 24.555  15.788  0.534   1.00 31.76  ? 105 LEU A CD2 1 
ATOM   599   N N   . PRO A 1 77  ? 26.179  14.625  -3.739  1.00 29.52  ? 106 PRO A N   1 
ATOM   600   C CA  . PRO A 1 77  ? 26.458  13.768  -4.888  1.00 32.88  ? 106 PRO A CA  1 
ATOM   601   C C   . PRO A 1 77  ? 25.232  13.054  -5.457  1.00 31.56  ? 106 PRO A C   1 
ATOM   602   O O   . PRO A 1 77  ? 24.296  12.691  -4.736  1.00 29.57  ? 106 PRO A O   1 
ATOM   603   C CB  . PRO A 1 77  ? 27.493  12.785  -4.314  1.00 30.68  ? 106 PRO A CB  1 
ATOM   604   C CG  . PRO A 1 77  ? 28.253  13.642  -3.342  1.00 31.48  ? 106 PRO A CG  1 
ATOM   605   C CD  . PRO A 1 77  ? 27.155  14.426  -2.659  1.00 30.08  ? 106 PRO A CD  1 
ATOM   606   N N   . LYS A 1 78  ? 25.250  12.877  -6.785  1.00 32.12  ? 107 LYS A N   1 
ATOM   607   C CA  . LYS A 1 78  ? 24.199  12.160  -7.486  1.00 32.46  ? 107 LYS A CA  1 
ATOM   608   C C   . LYS A 1 78  ? 24.798  10.861  -8.003  1.00 29.93  ? 107 LYS A C   1 
ATOM   609   O O   . LYS A 1 78  ? 26.015  10.735  -8.002  1.00 32.06  ? 107 LYS A O   1 
ATOM   610   C CB  . LYS A 1 78  ? 23.665  13.062  -8.602  1.00 34.95  ? 107 LYS A CB  1 
ATOM   611   C CG  . LYS A 1 78  ? 23.112  14.399  -8.121  1.00 36.22  ? 107 LYS A CG  1 
ATOM   612   C CD  . LYS A 1 78  ? 23.351  15.526  -9.110  1.00 40.32  ? 107 LYS A CD  1 
ATOM   613   C CE  . LYS A 1 78  ? 23.085  16.902  -8.539  1.00 43.16  ? 107 LYS A CE  1 
ATOM   614   N NZ  . LYS A 1 78  ? 23.828  17.156  -7.282  1.00 41.90  ? 107 LYS A NZ  1 
ATOM   615   N N   . ALA A 1 79  ? 23.964  9.917   -8.459  1.00 30.88  ? 108 ALA A N   1 
ATOM   616   C CA  . ALA A 1 79  ? 24.459  8.786   -9.238  1.00 32.99  ? 108 ALA A CA  1 
ATOM   617   C C   . ALA A 1 79  ? 25.071  9.332   -10.530 1.00 33.07  ? 108 ALA A C   1 
ATOM   618   O O   . ALA A 1 79  ? 24.774  10.461  -10.899 1.00 31.48  ? 108 ALA A O   1 
ATOM   619   C CB  . ALA A 1 79  ? 23.354  7.793   -9.518  1.00 33.09  ? 108 ALA A CB  1 
ATOM   620   N N   . LYS A 1 80  ? 25.959  8.576   -11.191 1.00 37.93  ? 109 LYS A N   1 
ATOM   621   C CA  . LYS A 1 80  ? 26.602  9.087   -12.401 1.00 42.95  ? 109 LYS A CA  1 
ATOM   622   C C   . LYS A 1 80  ? 25.566  9.521   -13.441 1.00 42.78  ? 109 LYS A C   1 
ATOM   623   O O   . LYS A 1 80  ? 25.672  10.602  -14.016 1.00 40.79  ? 109 LYS A O   1 
ATOM   624   C CB  . LYS A 1 80  ? 27.552  8.082   -13.054 1.00 43.91  ? 109 LYS A CB  1 
ATOM   625   C CG  . LYS A 1 80  ? 28.993  8.114   -12.560 1.00 46.12  ? 109 LYS A CG  1 
ATOM   626   C CD  . LYS A 1 80  ? 29.334  6.962   -11.659 1.00 48.86  ? 109 LYS A CD  1 
ATOM   627   C CE  . LYS A 1 80  ? 29.256  5.624   -12.364 1.00 48.14  ? 109 LYS A CE  1 
ATOM   628   N NZ  . LYS A 1 80  ? 29.210  4.509   -11.389 1.00 50.17  ? 109 LYS A NZ  1 
ATOM   629   N N   . GLY A 1 81  ? 24.549  8.692   -13.682 1.00 43.20  ? 110 GLY A N   1 
ATOM   630   C CA  . GLY A 1 81  ? 23.559  9.038   -14.691 1.00 46.97  ? 110 GLY A CA  1 
ATOM   631   C C   . GLY A 1 81  ? 22.428  9.930   -14.171 1.00 44.28  ? 110 GLY A C   1 
ATOM   632   O O   . GLY A 1 81  ? 21.316  9.857   -14.692 1.00 51.69  ? 110 GLY A O   1 
ATOM   633   N N   . GLY A 1 82  ? 22.716  10.783  -13.172 1.00 39.93  ? 111 GLY A N   1 
ATOM   634   C CA  . GLY A 1 82  ? 21.703  11.143  -12.191 1.00 33.00  ? 111 GLY A CA  1 
ATOM   635   C C   . GLY A 1 82  ? 21.515  12.642  -11.972 1.00 31.11  ? 111 GLY A C   1 
ATOM   636   O O   . GLY A 1 82  ? 22.456  13.422  -12.031 1.00 33.37  ? 111 GLY A O   1 
ATOM   637   N N   . GLU A 1 83  ? 20.271  13.013  -11.648 1.00 30.43  ? 112 GLU A N   1 
ATOM   638   C CA  . GLU A 1 83  ? 19.940  14.375  -11.277 1.00 33.71  ? 112 GLU A CA  1 
ATOM   639   C C   . GLU A 1 83  ? 19.611  14.468  -9.785  1.00 30.23  ? 112 GLU A C   1 
ATOM   640   O O   . GLU A 1 83  ? 19.819  15.516  -9.192  1.00 31.03  ? 112 GLU A O   1 
ATOM   641   C CB  . GLU A 1 83  ? 18.771  14.887  -12.123 1.00 37.28  ? 112 GLU A CB  1 
ATOM   642   C CG  . GLU A 1 83  ? 18.970  14.730  -13.623 1.00 38.61  ? 112 GLU A CG  1 
ATOM   643   C CD  . GLU A 1 83  ? 20.324  15.146  -14.183 1.00 45.73  ? 112 GLU A CD  1 
ATOM   644   O OE1 . GLU A 1 83  ? 20.728  16.311  -13.971 1.00 47.99  ? 112 GLU A OE1 1 
ATOM   645   O OE2 . GLU A 1 83  ? 20.977  14.300  -14.842 1.00 49.48  ? 112 GLU A OE2 1 
ATOM   646   N N   . GLU A 1 84  ? 19.136  13.377  -9.173  1.00 29.86  ? 113 GLU A N   1 
ATOM   647   C CA  . GLU A 1 84  ? 18.603  13.452  -7.817  1.00 30.89  ? 113 GLU A CA  1 
ATOM   648   C C   . GLU A 1 84  ? 19.696  13.124  -6.787  1.00 29.67  ? 113 GLU A C   1 
ATOM   649   O O   . GLU A 1 84  ? 20.593  12.333  -7.061  1.00 28.33  ? 113 GLU A O   1 
ATOM   650   C CB  . GLU A 1 84  ? 17.376  12.539  -7.697  1.00 33.36  ? 113 GLU A CB  1 
ATOM   651   C CG  . GLU A 1 84  ? 16.221  12.919  -8.626  1.00 34.76  ? 113 GLU A CG  1 
ATOM   652   C CD  . GLU A 1 84  ? 15.640  14.304  -8.378  1.00 38.94  ? 113 GLU A CD  1 
ATOM   653   O OE1 . GLU A 1 84  ? 15.903  14.873  -7.293  1.00 39.40  ? 113 GLU A OE1 1 
ATOM   654   O OE2 . GLU A 1 84  ? 14.957  14.836  -9.284  1.00 39.16  ? 113 GLU A OE2 1 
ATOM   655   N N   . PRO A 1 85  ? 19.646  13.714  -5.563  1.00 28.45  ? 114 PRO A N   1 
ATOM   656   C CA  . PRO A 1 85  ? 20.600  13.407  -4.489  1.00 28.23  ? 114 PRO A CA  1 
ATOM   657   C C   . PRO A 1 85  ? 20.475  11.994  -3.921  1.00 25.40  ? 114 PRO A C   1 
ATOM   658   O O   . PRO A 1 85  ? 19.371  11.520  -3.640  1.00 23.72  ? 114 PRO A O   1 
ATOM   659   C CB  . PRO A 1 85  ? 20.241  14.400  -3.379  1.00 31.94  ? 114 PRO A CB  1 
ATOM   660   C CG  . PRO A 1 85  ? 18.768  14.698  -3.619  1.00 29.05  ? 114 PRO A CG  1 
ATOM   661   C CD  . PRO A 1 85  ? 18.627  14.695  -5.131  1.00 30.00  ? 114 PRO A CD  1 
ATOM   662   N N   . LEU A 1 86  ? 21.628  11.330  -3.752  1.00 23.12  ? 115 LEU A N   1 
ATOM   663   C CA  . LEU A 1 86  ? 21.642  9.997   -3.186  1.00 21.36  ? 115 LEU A CA  1 
ATOM   664   C C   . LEU A 1 86  ? 21.433  10.108  -1.677  1.00 20.45  ? 115 LEU A C   1 
ATOM   665   O O   . LEU A 1 86  ? 22.033  10.959  -1.027  1.00 19.16  ? 115 LEU A O   1 
ATOM   666   C CB  . LEU A 1 86  ? 22.988  9.331   -3.488  1.00 22.90  ? 115 LEU A CB  1 
ATOM   667   C CG  . LEU A 1 86  ? 23.275  9.066   -4.960  1.00 22.97  ? 115 LEU A CG  1 
ATOM   668   C CD1 . LEU A 1 86  ? 24.647  8.414   -5.118  1.00 23.66  ? 115 LEU A CD1 1 
ATOM   669   C CD2 . LEU A 1 86  ? 22.190  8.199   -5.585  1.00 23.65  ? 115 LEU A CD2 1 
ATOM   670   N N   . PRO A 1 87  ? 20.574  9.259   -1.084  1.00 19.94  ? 116 PRO A N   1 
ATOM   671   C CA  . PRO A 1 87  ? 20.408  9.236   0.377   1.00 19.89  ? 116 PRO A CA  1 
ATOM   672   C C   . PRO A 1 87  ? 21.680  8.911   1.176   1.00 20.35  ? 116 PRO A C   1 
ATOM   673   O O   . PRO A 1 87  ? 21.856  9.399   2.288   1.00 20.48  ? 116 PRO A O   1 
ATOM   674   C CB  . PRO A 1 87  ? 19.335  8.181   0.648   1.00 22.37  ? 116 PRO A CB  1 
ATOM   675   C CG  . PRO A 1 87  ? 19.133  7.429   -0.652  1.00 23.04  ? 116 PRO A CG  1 
ATOM   676   C CD  . PRO A 1 87  ? 19.745  8.264   -1.763  1.00 21.99  ? 116 PRO A CD  1 
ATOM   677   N N   . GLU A 1 88  ? 22.595  8.131   0.595   1.00 21.89  ? 117 GLU A N   1 
ATOM   678   C CA  . GLU A 1 88  ? 23.939  7.965   1.131   1.00 21.45  ? 117 GLU A CA  1 
ATOM   679   C C   . GLU A 1 88  ? 24.519  9.300   1.576   1.00 24.62  ? 117 GLU A C   1 
ATOM   680   O O   . GLU A 1 88  ? 24.991  9.466   2.697   1.00 22.23  ? 117 GLU A O   1 
ATOM   681   C CB  . GLU A 1 88  ? 24.910  7.403   0.086   1.00 22.45  ? 117 GLU A CB  1 
ATOM   682   C CG  . GLU A 1 88  ? 24.801  5.909   -0.115  1.00 22.22  ? 117 GLU A CG  1 
ATOM   683   C CD  . GLU A 1 88  ? 23.848  5.503   -1.216  1.00 25.83  ? 117 GLU A CD  1 
ATOM   684   O OE1 . GLU A 1 88  ? 22.839  6.243   -1.412  1.00 20.59  ? 117 GLU A OE1 1 
ATOM   685   O OE2 . GLU A 1 88  ? 24.088  4.424   -1.852  1.00 23.83  ? 117 GLU A OE2 1 
ATOM   686   N N   . GLY A 1 89  ? 24.527  10.258  0.649   1.00 23.74  ? 118 GLY A N   1 
ATOM   687   C CA  . GLY A 1 89  ? 25.147  11.540  0.919   1.00 22.17  ? 118 GLY A CA  1 
ATOM   688   C C   . GLY A 1 89  ? 24.374  12.376  1.939   1.00 24.58  ? 118 GLY A C   1 
ATOM   689   O O   . GLY A 1 89  ? 24.964  13.150  2.676   1.00 23.87  ? 118 GLY A O   1 
ATOM   690   N N   . LEU A 1 90  ? 23.043  12.268  1.964   1.00 25.13  ? 119 LEU A N   1 
ATOM   691   C CA  . LEU A 1 90  ? 22.315  12.917  3.040   1.00 24.89  ? 119 LEU A CA  1 
ATOM   692   C C   . LEU A 1 90  ? 22.732  12.337  4.394   1.00 22.20  ? 119 LEU A C   1 
ATOM   693   O O   . LEU A 1 90  ? 22.941  13.066  5.354   1.00 20.20  ? 119 LEU A O   1 
ATOM   694   C CB  . LEU A 1 90  ? 20.817  12.716  2.850   1.00 25.56  ? 119 LEU A CB  1 
ATOM   695   C CG  . LEU A 1 90  ? 20.009  13.245  4.024   1.00 28.71  ? 119 LEU A CG  1 
ATOM   696   C CD1 . LEU A 1 90  ? 18.920  14.186  3.576   1.00 31.79  ? 119 LEU A CD1 1 
ATOM   697   C CD2 . LEU A 1 90  ? 19.480  12.107  4.865   1.00 28.03  ? 119 LEU A CD2 1 
ATOM   698   N N   . PHE A 1 91  ? 22.770  11.006  4.504   1.00 22.45  ? 120 PHE A N   1 
ATOM   699   C CA  . PHE A 1 91  ? 23.065  10.413  5.790   1.00 20.97  ? 120 PHE A CA  1 
ATOM   700   C C   . PHE A 1 91  ? 24.417  10.957  6.265   1.00 19.42  ? 120 PHE A C   1 
ATOM   701   O O   . PHE A 1 91  ? 24.567  11.311  7.437   1.00 21.19  ? 120 PHE A O   1 
ATOM   702   C CB  . PHE A 1 91  ? 23.046  8.885   5.700   1.00 20.71  ? 120 PHE A CB  1 
ATOM   703   C CG  . PHE A 1 91  ? 23.432  8.190   6.985   1.00 20.70  ? 120 PHE A CG  1 
ATOM   704   C CD1 . PHE A 1 91  ? 22.547  8.101   8.050   1.00 19.67  ? 120 PHE A CD1 1 
ATOM   705   C CD2 . PHE A 1 91  ? 24.727  7.734   7.181   1.00 19.78  ? 120 PHE A CD2 1 
ATOM   706   C CE1 . PHE A 1 91  ? 22.918  7.480   9.237   1.00 19.04  ? 120 PHE A CE1 1 
ATOM   707   C CE2 . PHE A 1 91  ? 25.076  7.065   8.345   1.00 21.22  ? 120 PHE A CE2 1 
ATOM   708   C CZ  . PHE A 1 91  ? 24.193  6.973   9.385   1.00 19.12  ? 120 PHE A CZ  1 
ATOM   709   N N   . TRP A 1 92  ? 25.374  11.052  5.332   1.00 20.27  ? 121 TRP A N   1 
ATOM   710   C CA  . TRP A 1 92  ? 26.728  11.520  5.633   1.00 20.48  ? 121 TRP A CA  1 
ATOM   711   C C   . TRP A 1 92  ? 26.661  12.928  6.202   1.00 19.04  ? 121 TRP A C   1 
ATOM   712   O O   . TRP A 1 92  ? 27.338  13.280  7.166   1.00 23.80  ? 121 TRP A O   1 
ATOM   713   C CB  . TRP A 1 92  ? 27.599  11.498  4.378   1.00 22.38  ? 121 TRP A CB  1 
ATOM   714   C CG  . TRP A 1 92  ? 29.045  11.784  4.627   1.00 21.58  ? 121 TRP A CG  1 
ATOM   715   C CD1 . TRP A 1 92  ? 29.593  12.986  4.950   1.00 21.11  ? 121 TRP A CD1 1 
ATOM   716   C CD2 . TRP A 1 92  ? 30.132  10.845  4.642   1.00 23.08  ? 121 TRP A CD2 1 
ATOM   717   N NE1 . TRP A 1 92  ? 30.938  12.862  5.150   1.00 24.62  ? 121 TRP A NE1 1 
ATOM   718   C CE2 . TRP A 1 92  ? 31.302  11.559  4.960   1.00 23.17  ? 121 TRP A CE2 1 
ATOM   719   C CE3 . TRP A 1 92  ? 30.244  9.485   4.357   1.00 23.64  ? 121 TRP A CE3 1 
ATOM   720   C CZ2 . TRP A 1 92  ? 32.566  10.970  4.999   1.00 22.03  ? 121 TRP A CZ2 1 
ATOM   721   C CZ3 . TRP A 1 92  ? 31.493  8.896   4.417   1.00 22.49  ? 121 TRP A CZ3 1 
ATOM   722   C CH2 . TRP A 1 92  ? 32.631  9.625   4.757   1.00 22.54  ? 121 TRP A CH2 1 
ATOM   723   N N   . LEU A 1 93  ? 25.851  13.752  5.559   1.00 20.49  ? 122 LEU A N   1 
ATOM   724   C CA  . LEU A 1 93  ? 25.680  15.112  6.021   1.00 19.36  ? 122 LEU A CA  1 
ATOM   725   C C   . LEU A 1 93  ? 25.100  15.123  7.437   1.00 18.19  ? 122 LEU A C   1 
ATOM   726   O O   . LEU A 1 93  ? 25.511  15.913  8.270   1.00 22.68  ? 122 LEU A O   1 
ATOM   727   C CB  . LEU A 1 93  ? 24.772  15.863  5.046   1.00 21.59  ? 122 LEU A CB  1 
ATOM   728   C CG  . LEU A 1 93  ? 24.340  17.256  5.504   1.00 21.75  ? 122 LEU A CG  1 
ATOM   729   C CD1 . LEU A 1 93  ? 25.535  18.196  5.548   1.00 21.12  ? 122 LEU A CD1 1 
ATOM   730   C CD2 . LEU A 1 93  ? 23.222  17.788  4.610   1.00 24.32  ? 122 LEU A CD2 1 
ATOM   731   N N   . LEU A 1 94  ? 24.076  14.316  7.708   1.00 18.64  ? 123 LEU A N   1 
ATOM   732   C CA  . LEU A 1 94  ? 23.448  14.398  9.017   1.00 19.31  ? 123 LEU A CA  1 
ATOM   733   C C   . LEU A 1 94  ? 24.456  14.000  10.096  1.00 20.44  ? 123 LEU A C   1 
ATOM   734   O O   . LEU A 1 94  ? 24.481  14.605  11.162  1.00 19.56  ? 123 LEU A O   1 
ATOM   735   C CB  . LEU A 1 94  ? 22.198  13.509  9.057   1.00 19.92  ? 123 LEU A CB  1 
ATOM   736   C CG  . LEU A 1 94  ? 21.078  13.885  8.082   1.00 17.03  ? 123 LEU A CG  1 
ATOM   737   C CD1 . LEU A 1 94  ? 19.830  13.075  8.350   1.00 15.98  ? 123 LEU A CD1 1 
ATOM   738   C CD2 . LEU A 1 94  ? 20.763  15.370  8.124   1.00 16.31  ? 123 LEU A CD2 1 
ATOM   739   N N   . VAL A 1 95  ? 25.259  12.977  9.779   1.00 21.46  ? 124 VAL A N   1 
ATOM   740   C CA  . VAL A 1 95  ? 26.236  12.401  10.685  1.00 25.01  ? 124 VAL A CA  1 
ATOM   741   C C   . VAL A 1 95  ? 27.384  13.364  10.933  1.00 23.75  ? 124 VAL A C   1 
ATOM   742   O O   . VAL A 1 95  ? 27.799  13.491  12.071  1.00 27.94  ? 124 VAL A O   1 
ATOM   743   C CB  . VAL A 1 95  ? 26.773  11.059  10.160  1.00 24.78  ? 124 VAL A CB  1 
ATOM   744   C CG1 . VAL A 1 95  ? 28.009  10.593  10.915  1.00 25.58  ? 124 VAL A CG1 1 
ATOM   745   C CG2 . VAL A 1 95  ? 25.685  10.004  10.188  1.00 24.76  ? 124 VAL A CG2 1 
ATOM   746   N N   . THR A 1 96  ? 27.857  14.065  9.895   1.00 24.76  ? 125 THR A N   1 
ATOM   747   C CA  . THR A 1 96  ? 29.101  14.805  10.008  1.00 23.87  ? 125 THR A CA  1 
ATOM   748   C C   . THR A 1 96  ? 28.853  16.302  10.115  1.00 23.72  ? 125 THR A C   1 
ATOM   749   O O   . THR A 1 96  ? 29.751  17.023  10.542  1.00 23.60  ? 125 THR A O   1 
ATOM   750   C CB  . THR A 1 96  ? 30.010  14.503  8.815   1.00 23.28  ? 125 THR A CB  1 
ATOM   751   O OG1 . THR A 1 96  ? 29.388  14.975  7.622   1.00 27.35  ? 125 THR A OG1 1 
ATOM   752   C CG2 . THR A 1 96  ? 30.298  13.024  8.715   1.00 24.01  ? 125 THR A CG2 1 
ATOM   753   N N   . GLY A 1 97  ? 27.697  16.757  9.620   1.00 26.08  ? 126 GLY A N   1 
ATOM   754   C CA  . GLY A 1 97  ? 27.454  18.177  9.441   1.00 26.10  ? 126 GLY A CA  1 
ATOM   755   C C   . GLY A 1 97  ? 28.064  18.737  8.152   1.00 27.51  ? 126 GLY A C   1 
ATOM   756   O O   . GLY A 1 97  ? 28.058  19.959  7.954   1.00 27.07  ? 126 GLY A O   1 
ATOM   757   N N   . HIS A 1 98  ? 28.573  17.849  7.291   1.00 28.45  ? 127 HIS A N   1 
ATOM   758   C CA  . HIS A 1 98  ? 29.376  18.244  6.143   1.00 29.66  ? 127 HIS A CA  1 
ATOM   759   C C   . HIS A 1 98  ? 28.924  17.549  4.866   1.00 28.85  ? 127 HIS A C   1 
ATOM   760   O O   . HIS A 1 98  ? 28.585  16.363  4.847   1.00 27.58  ? 127 HIS A O   1 
ATOM   761   C CB  . HIS A 1 98  ? 30.853  17.867  6.304   1.00 32.28  ? 127 HIS A CB  1 
ATOM   762   C CG  . HIS A 1 98  ? 31.464  18.510  7.491   1.00 40.52  ? 127 HIS A CG  1 
ATOM   763   N ND1 . HIS A 1 98  ? 31.403  19.873  7.679   1.00 46.55  ? 127 HIS A ND1 1 
ATOM   764   C CD2 . HIS A 1 98  ? 32.077  18.001  8.561   1.00 43.42  ? 127 HIS A CD2 1 
ATOM   765   C CE1 . HIS A 1 98  ? 31.998  20.172  8.826   1.00 52.76  ? 127 HIS A CE1 1 
ATOM   766   N NE2 . HIS A 1 98  ? 32.411  19.045  9.375   1.00 51.09  ? 127 HIS A NE2 1 
ATOM   767   N N   . ILE A 1 99  ? 28.992  18.300  3.767   1.00 27.82  ? 128 ILE A N   1 
ATOM   768   C CA  . ILE A 1 99  ? 28.599  17.762  2.484   1.00 27.84  ? 128 ILE A CA  1 
ATOM   769   C C   . ILE A 1 99  ? 29.673  16.764  2.071   1.00 28.39  ? 128 ILE A C   1 
ATOM   770   O O   . ILE A 1 99  ? 30.849  17.122  2.031   1.00 28.41  ? 128 ILE A O   1 
ATOM   771   C CB  . ILE A 1 99  ? 28.437  18.866  1.422   1.00 27.55  ? 128 ILE A CB  1 
ATOM   772   C CG1 . ILE A 1 99  ? 27.430  19.940  1.847   1.00 28.76  ? 128 ILE A CG1 1 
ATOM   773   C CG2 . ILE A 1 99  ? 28.079  18.229  0.094   1.00 24.59  ? 128 ILE A CG2 1 
ATOM   774   C CD1 . ILE A 1 99  ? 26.001  19.495  1.798   1.00 29.21  ? 128 ILE A CD1 1 
ATOM   775   N N   . PRO A 1 100 ? 29.300  15.509  1.728   1.00 25.83  ? 129 PRO A N   1 
ATOM   776   C CA  . PRO A 1 100 ? 30.272  14.514  1.302   1.00 24.85  ? 129 PRO A CA  1 
ATOM   777   C C   . PRO A 1 100 ? 30.813  14.782  -0.095  1.00 27.87  ? 129 PRO A C   1 
ATOM   778   O O   . PRO A 1 100 ? 30.183  15.481  -0.890  1.00 27.56  ? 129 PRO A O   1 
ATOM   779   C CB  . PRO A 1 100 ? 29.478  13.200  1.255   1.00 24.21  ? 129 PRO A CB  1 
ATOM   780   C CG  . PRO A 1 100 ? 28.045  13.637  1.032   1.00 24.79  ? 129 PRO A CG  1 
ATOM   781   C CD  . PRO A 1 100 ? 27.921  15.003  1.685   1.00 25.41  ? 129 PRO A CD  1 
ATOM   782   N N   . THR A 1 101 ? 32.006  14.236  -0.353  1.00 31.05  ? 130 THR A N   1 
ATOM   783   C CA  . THR A 1 101 ? 32.539  14.186  -1.699  1.00 28.89  ? 130 THR A CA  1 
ATOM   784   C C   . THR A 1 101 ? 31.946  12.954  -2.354  1.00 30.55  ? 130 THR A C   1 
ATOM   785   O O   . THR A 1 101 ? 31.351  12.131  -1.664  1.00 31.05  ? 130 THR A O   1 
ATOM   786   C CB  . THR A 1 101 ? 34.073  14.132  -1.720  1.00 29.32  ? 130 THR A CB  1 
ATOM   787   O OG1 . THR A 1 101 ? 34.438  12.893  -1.119  1.00 29.28  ? 130 THR A OG1 1 
ATOM   788   C CG2 . THR A 1 101 ? 34.728  15.292  -1.006  1.00 29.08  ? 130 THR A CG2 1 
ATOM   789   N N   . GLU A 1 102 ? 32.135  12.852  -3.680  1.00 30.15  ? 131 GLU A N   1 
ATOM   790   C CA  . GLU A 1 102 ? 31.662  11.740  -4.488  1.00 30.94  ? 131 GLU A CA  1 
ATOM   791   C C   . GLU A 1 102 ? 32.269  10.426  -4.008  1.00 30.56  ? 131 GLU A C   1 
ATOM   792   O O   . GLU A 1 102 ? 31.604  9.395   -4.015  1.00 29.32  ? 131 GLU A O   1 
ATOM   793   C CB  . GLU A 1 102 ? 32.116  11.932  -5.938  1.00 36.37  ? 131 GLU A CB  1 
ATOM   794   C CG  . GLU A 1 102 ? 31.585  13.199  -6.585  1.00 41.63  ? 131 GLU A CG  1 
ATOM   795   C CD  . GLU A 1 102 ? 30.199  13.051  -7.177  1.00 46.45  ? 131 GLU A CD  1 
ATOM   796   O OE1 . GLU A 1 102 ? 29.772  11.888  -7.383  1.00 47.69  ? 131 GLU A OE1 1 
ATOM   797   O OE2 . GLU A 1 102 ? 29.549  14.097  -7.413  1.00 49.12  ? 131 GLU A OE2 1 
ATOM   798   N N   . GLU A 1 103 ? 33.554  10.488  -3.646  1.00 32.59  ? 132 GLU A N   1 
ATOM   799   C CA  . GLU A 1 103 ? 34.316  9.328   -3.203  1.00 36.17  ? 132 GLU A CA  1 
ATOM   800   C C   . GLU A 1 103 ? 33.753  8.824   -1.878  1.00 31.10  ? 132 GLU A C   1 
ATOM   801   O O   . GLU A 1 103 ? 33.609  7.621   -1.681  1.00 34.49  ? 132 GLU A O   1 
ATOM   802   C CB  . GLU A 1 103 ? 35.795  9.705   -3.067  1.00 40.54  ? 132 GLU A CB  1 
ATOM   803   C CG  . GLU A 1 103 ? 36.467  10.111  -4.382  1.00 43.04  ? 132 GLU A CG  1 
ATOM   804   C CD  . GLU A 1 103 ? 36.255  11.535  -4.894  1.00 50.73  ? 132 GLU A CD  1 
ATOM   805   O OE1 . GLU A 1 103 ? 35.737  12.389  -4.142  1.00 53.97  ? 132 GLU A OE1 1 
ATOM   806   O OE2 . GLU A 1 103 ? 36.612  11.800  -6.068  1.00 58.07  ? 132 GLU A OE2 1 
ATOM   807   N N   . GLN A 1 104 ? 33.447  9.765   -0.984  1.00 31.17  ? 133 GLN A N   1 
ATOM   808   C CA  . GLN A 1 104 ? 32.904  9.460   0.337   1.00 28.31  ? 133 GLN A CA  1 
ATOM   809   C C   . GLN A 1 104 ? 31.545  8.776   0.182   1.00 27.78  ? 133 GLN A C   1 
ATOM   810   O O   . GLN A 1 104 ? 31.307  7.761   0.828   1.00 25.59  ? 133 GLN A O   1 
ATOM   811   C CB  . GLN A 1 104 ? 32.831  10.738  1.175   1.00 28.44  ? 133 GLN A CB  1 
ATOM   812   C CG  . GLN A 1 104 ? 34.195  11.143  1.713   1.00 29.77  ? 133 GLN A CG  1 
ATOM   813   C CD  . GLN A 1 104 ? 34.215  12.444  2.468   1.00 28.68  ? 133 GLN A CD  1 
ATOM   814   O OE1 . GLN A 1 104 ? 33.357  13.307  2.322   1.00 31.96  ? 133 GLN A OE1 1 
ATOM   815   N NE2 . GLN A 1 104 ? 35.280  12.642  3.213   1.00 33.17  ? 133 GLN A NE2 1 
ATOM   816   N N   . VAL A 1 105 ? 30.703  9.274   -0.746  1.00 25.81  ? 134 VAL A N   1 
ATOM   817   C CA  . VAL A 1 105 ? 29.410  8.672   -1.036  1.00 24.93  ? 134 VAL A CA  1 
ATOM   818   C C   . VAL A 1 105 ? 29.612  7.289   -1.630  1.00 25.92  ? 134 VAL A C   1 
ATOM   819   O O   . VAL A 1 105 ? 28.972  6.334   -1.200  1.00 26.36  ? 134 VAL A O   1 
ATOM   820   C CB  . VAL A 1 105 ? 28.548  9.557   -1.956  1.00 27.90  ? 134 VAL A CB  1 
ATOM   821   C CG1 . VAL A 1 105 ? 27.344  8.806   -2.511  1.00 29.21  ? 134 VAL A CG1 1 
ATOM   822   C CG2 . VAL A 1 105 ? 28.121  10.814  -1.231  1.00 29.98  ? 134 VAL A CG2 1 
ATOM   823   N N   . SER A 1 106 ? 30.487  7.210   -2.637  1.00 25.43  ? 135 SER A N   1 
ATOM   824   C CA  A SER A 1 106 ? 30.878  5.945   -3.240  0.50 28.38  ? 135 SER A CA  1 
ATOM   825   C CA  B SER A 1 106 ? 30.796  5.925   -3.232  0.50 27.55  ? 135 SER A CA  1 
ATOM   826   C C   . SER A 1 106 ? 31.225  4.934   -2.154  1.00 27.31  ? 135 SER A C   1 
ATOM   827   O O   . SER A 1 106 ? 30.781  3.777   -2.185  1.00 25.38  ? 135 SER A O   1 
ATOM   828   C CB  A SER A 1 106 ? 32.045  6.138   -4.193  0.50 30.28  ? 135 SER A CB  1 
ATOM   829   C CB  B SER A 1 106 ? 31.803  6.068   -4.343  0.50 28.82  ? 135 SER A CB  1 
ATOM   830   O OG  A SER A 1 106 ? 32.389  4.920   -4.836  0.50 29.08  ? 135 SER A OG  1 
ATOM   831   O OG  B SER A 1 106 ? 31.269  6.918   -5.348  0.50 25.60  ? 135 SER A OG  1 
ATOM   832   N N   . TRP A 1 107 ? 32.045  5.399   -1.201  1.00 30.21  ? 136 TRP A N   1 
ATOM   833   C CA  . TRP A 1 107 ? 32.497  4.547   -0.111  1.00 32.08  ? 136 TRP A CA  1 
ATOM   834   C C   . TRP A 1 107 ? 31.272  4.028   0.640   1.00 28.48  ? 136 TRP A C   1 
ATOM   835   O O   . TRP A 1 107 ? 31.111  2.822   0.830   1.00 26.28  ? 136 TRP A O   1 
ATOM   836   C CB  . TRP A 1 107 ? 33.505  5.271   0.794   1.00 35.06  ? 136 TRP A CB  1 
ATOM   837   C CG  . TRP A 1 107 ? 33.863  4.466   2.007   1.00 37.22  ? 136 TRP A CG  1 
ATOM   838   C CD1 . TRP A 1 107 ? 34.809  3.481   2.120   1.00 37.57  ? 136 TRP A CD1 1 
ATOM   839   C CD2 . TRP A 1 107 ? 33.155  4.482   3.255   1.00 32.92  ? 136 TRP A CD2 1 
ATOM   840   N NE1 . TRP A 1 107 ? 34.766  2.922   3.370   1.00 35.18  ? 136 TRP A NE1 1 
ATOM   841   C CE2 . TRP A 1 107 ? 33.767  3.521   4.091   1.00 35.87  ? 136 TRP A CE2 1 
ATOM   842   C CE3 . TRP A 1 107 ? 32.082  5.230   3.748   1.00 32.03  ? 136 TRP A CE3 1 
ATOM   843   C CZ2 . TRP A 1 107 ? 33.339  3.305   5.401   1.00 34.43  ? 136 TRP A CZ2 1 
ATOM   844   C CZ3 . TRP A 1 107 ? 31.660  5.012   5.044   1.00 31.76  ? 136 TRP A CZ3 1 
ATOM   845   C CH2 . TRP A 1 107 ? 32.276  4.054   5.852   1.00 33.49  ? 136 TRP A CH2 1 
ATOM   846   N N   . LEU A 1 108 ? 30.353  4.934   0.982   1.00 27.47  ? 137 LEU A N   1 
ATOM   847   C CA  . LEU A 1 108 ? 29.209  4.555   1.800   1.00 24.80  ? 137 LEU A CA  1 
ATOM   848   C C   . LEU A 1 108 ? 28.282  3.583   1.075   1.00 23.61  ? 137 LEU A C   1 
ATOM   849   O O   . LEU A 1 108 ? 27.837  2.611   1.694   1.00 26.10  ? 137 LEU A O   1 
ATOM   850   C CB  . LEU A 1 108 ? 28.456  5.813   2.228   1.00 26.02  ? 137 LEU A CB  1 
ATOM   851   C CG  . LEU A 1 108 ? 27.399  5.624   3.317   1.00 27.54  ? 137 LEU A CG  1 
ATOM   852   C CD1 . LEU A 1 108 ? 27.981  4.981   4.561   1.00 27.77  ? 137 LEU A CD1 1 
ATOM   853   C CD2 . LEU A 1 108 ? 26.737  6.953   3.659   1.00 28.26  ? 137 LEU A CD2 1 
ATOM   854   N N   . SER A 1 109 ? 28.032  3.772   -0.239  1.00 21.75  ? 138 SER A N   1 
ATOM   855   C CA  . SER A 1 109 ? 27.236  2.799   -0.983  1.00 22.67  ? 138 SER A CA  1 
ATOM   856   C C   . SER A 1 109 ? 27.837  1.411   -0.815  1.00 22.44  ? 138 SER A C   1 
ATOM   857   O O   . SER A 1 109 ? 27.156  0.404   -0.634  1.00 22.37  ? 138 SER A O   1 
ATOM   858   C CB  . SER A 1 109 ? 27.150  3.137   -2.466  1.00 24.80  ? 138 SER A CB  1 
ATOM   859   O OG  . SER A 1 109 ? 26.703  4.482   -2.640  1.00 22.26  ? 138 SER A OG  1 
ATOM   860   N N   . LYS A 1 110 ? 29.155  1.326   -0.898  1.00 25.62  ? 139 LYS A N   1 
ATOM   861   C CA  . LYS A 1 110 ? 29.731  -0.012  -0.878  1.00 26.90  ? 139 LYS A CA  1 
ATOM   862   C C   . LYS A 1 110 ? 29.687  -0.538  0.560   1.00 25.34  ? 139 LYS A C   1 
ATOM   863   O O   . LYS A 1 110 ? 29.443  -1.726  0.755   1.00 26.93  ? 139 LYS A O   1 
ATOM   864   C CB  . LYS A 1 110 ? 31.083  0.006   -1.599  1.00 32.92  ? 139 LYS A CB  1 
ATOM   865   C CG  . LYS A 1 110 ? 30.979  0.448   -3.053  1.00 34.72  ? 139 LYS A CG  1 
ATOM   866   C CD  . LYS A 1 110 ? 32.301  0.523   -3.834  1.00 38.81  ? 139 LYS A CD  1 
ATOM   867   C CE  . LYS A 1 110 ? 33.173  1.690   -3.419  1.00 40.23  ? 139 LYS A CE  1 
ATOM   868   N NZ  . LYS A 1 110 ? 33.785  2.370   -4.589  1.00 39.01  ? 139 LYS A NZ  1 
ATOM   869   N N   . GLU A 1 111 ? 29.847  0.339   1.564   1.00 26.41  ? 140 GLU A N   1 
ATOM   870   C CA  . GLU A 1 111 ? 29.709  -0.089  2.957   1.00 29.58  ? 140 GLU A CA  1 
ATOM   871   C C   . GLU A 1 111 ? 28.340  -0.718  3.184   1.00 27.20  ? 140 GLU A C   1 
ATOM   872   O O   . GLU A 1 111 ? 28.216  -1.769  3.829   1.00 26.67  ? 140 GLU A O   1 
ATOM   873   C CB  . GLU A 1 111 ? 29.783  1.046   3.985   1.00 30.17  ? 140 GLU A CB  1 
ATOM   874   C CG  . GLU A 1 111 ? 30.934  0.981   4.979   1.00 33.57  ? 140 GLU A CG  1 
ATOM   875   C CD  . GLU A 1 111 ? 31.602  -0.354  5.255   1.00 33.00  ? 140 GLU A CD  1 
ATOM   876   O OE1 . GLU A 1 111 ? 31.161  -1.100  6.172   1.00 30.51  ? 140 GLU A OE1 1 
ATOM   877   O OE2 . GLU A 1 111 ? 32.564  -0.634  4.538   1.00 33.31  ? 140 GLU A OE2 1 
ATOM   878   N N   . TRP A 1 112 ? 27.311  -0.028  2.677   1.00 25.17  ? 141 TRP A N   1 
ATOM   879   C CA  . TRP A 1 112 ? 25.951  -0.491  2.879   1.00 20.18  ? 141 TRP A CA  1 
ATOM   880   C C   . TRP A 1 112 ? 25.710  -1.782  2.131   1.00 22.35  ? 141 TRP A C   1 
ATOM   881   O O   . TRP A 1 112 ? 25.089  -2.660  2.681   1.00 21.85  ? 141 TRP A O   1 
ATOM   882   C CB  . TRP A 1 112 ? 24.943  0.596   2.556   1.00 21.81  ? 141 TRP A CB  1 
ATOM   883   C CG  . TRP A 1 112 ? 24.869  1.612   3.656   1.00 21.82  ? 141 TRP A CG  1 
ATOM   884   C CD1 . TRP A 1 112 ? 25.427  1.535   4.901   1.00 23.60  ? 141 TRP A CD1 1 
ATOM   885   C CD2 . TRP A 1 112 ? 24.171  2.860   3.614   1.00 21.05  ? 141 TRP A CD2 1 
ATOM   886   N NE1 . TRP A 1 112 ? 25.140  2.665   5.623   1.00 26.86  ? 141 TRP A NE1 1 
ATOM   887   C CE2 . TRP A 1 112 ? 24.358  3.485   4.864   1.00 22.78  ? 141 TRP A CE2 1 
ATOM   888   C CE3 . TRP A 1 112 ? 23.394  3.496   2.641   1.00 23.54  ? 141 TRP A CE3 1 
ATOM   889   C CZ2 . TRP A 1 112 ? 23.850  4.752   5.139   1.00 22.95  ? 141 TRP A CZ2 1 
ATOM   890   C CZ3 . TRP A 1 112 ? 22.873  4.738   2.923   1.00 24.00  ? 141 TRP A CZ3 1 
ATOM   891   C CH2 . TRP A 1 112 ? 23.072  5.335   4.163   1.00 23.19  ? 141 TRP A CH2 1 
ATOM   892   N N   . ALA A 1 113 ? 26.220  -1.889  0.902   1.00 23.98  ? 142 ALA A N   1 
ATOM   893   C CA  . ALA A 1 113 ? 25.966  -3.081  0.110   1.00 25.37  ? 142 ALA A CA  1 
ATOM   894   C C   . ALA A 1 113 ? 26.531  -4.311  0.808   1.00 26.52  ? 142 ALA A C   1 
ATOM   895   O O   . ALA A 1 113 ? 25.962  -5.397  0.700   1.00 25.26  ? 142 ALA A O   1 
ATOM   896   C CB  . ALA A 1 113 ? 26.552  -2.922  -1.277  1.00 26.68  ? 142 ALA A CB  1 
ATOM   897   N N   . LYS A 1 114 ? 27.634  -4.128  1.545   1.00 31.65  ? 143 LYS A N   1 
ATOM   898   C CA  . LYS A 1 114 ? 28.347  -5.242  2.160   1.00 31.48  ? 143 LYS A CA  1 
ATOM   899   C C   . LYS A 1 114 ? 27.674  -5.677  3.453   1.00 29.85  ? 143 LYS A C   1 
ATOM   900   O O   . LYS A 1 114 ? 27.852  -6.809  3.885   1.00 28.52  ? 143 LYS A O   1 
ATOM   901   C CB  . LYS A 1 114 ? 29.793  -4.869  2.501   1.00 34.55  ? 143 LYS A CB  1 
ATOM   902   C CG  . LYS A 1 114 ? 30.775  -4.957  1.335   1.00 38.85  ? 143 LYS A CG  1 
ATOM   903   C CD  . LYS A 1 114 ? 32.218  -4.701  1.742   1.00 42.79  ? 143 LYS A CD  1 
ATOM   904   C CE  . LYS A 1 114 ? 32.449  -3.321  2.323   1.00 43.38  ? 143 LYS A CE  1 
ATOM   905   N NZ  . LYS A 1 114 ? 33.888  -3.070  2.564   1.00 42.20  ? 143 LYS A NZ  1 
ATOM   906   N N   . ARG A 1 115 ? 26.929  -4.770  4.088   1.00 28.29  ? 144 ARG A N   1 
ATOM   907   C CA  . ARG A 1 115 ? 26.315  -5.088  5.366   1.00 26.56  ? 144 ARG A CA  1 
ATOM   908   C C   . ARG A 1 115 ? 24.914  -5.653  5.171   1.00 27.61  ? 144 ARG A C   1 
ATOM   909   O O   . ARG A 1 115 ? 24.271  -6.050  6.141   1.00 24.64  ? 144 ARG A O   1 
ATOM   910   C CB  . ARG A 1 115 ? 26.282  -3.844  6.248   1.00 27.19  ? 144 ARG A CB  1 
ATOM   911   C CG  . ARG A 1 115 ? 27.656  -3.374  6.708   1.00 25.60  ? 144 ARG A CG  1 
ATOM   912   C CD  . ARG A 1 115 ? 27.523  -2.000  7.309   1.00 23.38  ? 144 ARG A CD  1 
ATOM   913   N NE  . ARG A 1 115 ? 28.796  -1.518  7.778   1.00 23.53  ? 144 ARG A NE  1 
ATOM   914   C CZ  . ARG A 1 115 ? 29.125  -1.377  9.059   1.00 21.62  ? 144 ARG A CZ  1 
ATOM   915   N NH1 . ARG A 1 115 ? 28.365  -1.936  9.981   1.00 21.28  ? 144 ARG A NH1 1 
ATOM   916   N NH2 . ARG A 1 115 ? 30.217  -0.708  9.399   1.00 19.78  ? 144 ARG A NH2 1 
ATOM   917   N N   . ALA A 1 116 ? 24.461  -5.693  3.917   1.00 28.01  ? 145 ALA A N   1 
ATOM   918   C CA  . ALA A 1 116 ? 23.095  -6.043  3.577   1.00 29.69  ? 145 ALA A CA  1 
ATOM   919   C C   . ALA A 1 116 ? 22.917  -7.551  3.672   1.00 34.48  ? 145 ALA A C   1 
ATOM   920   O O   . ALA A 1 116 ? 23.406  -8.295  2.820   1.00 35.60  ? 145 ALA A O   1 
ATOM   921   C CB  . ALA A 1 116 ? 22.768  -5.541  2.188   1.00 30.57  ? 145 ALA A CB  1 
ATOM   922   N N   . ALA A 1 117 ? 22.181  -7.985  4.700   1.00 33.16  ? 146 ALA A N   1 
ATOM   923   C CA  . ALA A 1 117 ? 22.131  -9.391  5.036   1.00 33.23  ? 146 ALA A CA  1 
ATOM   924   C C   . ALA A 1 117 ? 21.057  -9.628  6.084   1.00 27.79  ? 146 ALA A C   1 
ATOM   925   O O   . ALA A 1 117 ? 21.098  -9.045  7.158   1.00 31.05  ? 146 ALA A O   1 
ATOM   926   C CB  . ALA A 1 117 ? 23.485  -9.837  5.541   1.00 37.08  ? 146 ALA A CB  1 
ATOM   927   N N   . LEU A 1 118 ? 20.156  -10.567 5.813   1.00 29.27  ? 147 LEU A N   1 
ATOM   928   C CA  . LEU A 1 118 ? 19.182  -10.967 6.810   1.00 28.56  ? 147 LEU A CA  1 
ATOM   929   C C   . LEU A 1 118 ? 19.556  -12.339 7.357   1.00 27.82  ? 147 LEU A C   1 
ATOM   930   O O   . LEU A 1 118 ? 19.997  -13.183 6.585   1.00 29.02  ? 147 LEU A O   1 
ATOM   931   C CB  . LEU A 1 118 ? 17.799  -11.012 6.165   1.00 26.12  ? 147 LEU A CB  1 
ATOM   932   C CG  . LEU A 1 118 ? 17.291  -9.683  5.623   1.00 27.72  ? 147 LEU A CG  1 
ATOM   933   C CD1 . LEU A 1 118 ? 15.842  -9.795  5.209   1.00 28.94  ? 147 LEU A CD1 1 
ATOM   934   C CD2 . LEU A 1 118 ? 17.460  -8.576  6.653   1.00 27.89  ? 147 LEU A CD2 1 
ATOM   935   N N   . PRO A 1 119 ? 19.386  -12.585 8.675   1.00 26.02  ? 148 PRO A N   1 
ATOM   936   C CA  . PRO A 1 119 ? 19.468  -13.930 9.232   1.00 25.76  ? 148 PRO A CA  1 
ATOM   937   C C   . PRO A 1 119 ? 18.211  -14.749 8.960   1.00 25.93  ? 148 PRO A C   1 
ATOM   938   O O   . PRO A 1 119 ? 17.108  -14.235 8.833   1.00 23.16  ? 148 PRO A O   1 
ATOM   939   C CB  . PRO A 1 119 ? 19.603  -13.684 10.744  1.00 27.12  ? 148 PRO A CB  1 
ATOM   940   C CG  . PRO A 1 119 ? 18.865  -12.388 10.968  1.00 28.97  ? 148 PRO A CG  1 
ATOM   941   C CD  . PRO A 1 119 ? 19.015  -11.586 9.691   1.00 26.45  ? 148 PRO A CD  1 
ATOM   942   N N   . SER A 1 120 ? 18.364  -16.070 8.940   1.00 24.49  ? 149 SER A N   1 
ATOM   943   C CA  . SER A 1 120 ? 17.266  -16.952 8.601   1.00 25.83  ? 149 SER A CA  1 
ATOM   944   C C   . SER A 1 120 ? 16.009  -16.749 9.461   1.00 25.51  ? 149 SER A C   1 
ATOM   945   O O   . SER A 1 120 ? 14.891  -16.953 8.969   1.00 23.25  ? 149 SER A O   1 
ATOM   946   C CB  . SER A 1 120 ? 17.739  -18.387 8.690   1.00 26.97  ? 149 SER A CB  1 
ATOM   947   O OG  . SER A 1 120 ? 18.129  -18.662 10.023  1.00 34.89  ? 149 SER A OG  1 
ATOM   948   N N   . HIS A 1 121 ? 16.138  -16.454 10.772  1.00 25.16  ? 150 HIS A N   1 
ATOM   949   C CA  . HIS A 1 121 ? 14.920  -16.415 11.559  1.00 24.67  ? 150 HIS A CA  1 
ATOM   950   C C   . HIS A 1 121 ? 14.033  -15.265 11.083  1.00 22.37  ? 150 HIS A C   1 
ATOM   951   O O   . HIS A 1 121 ? 12.820  -15.409 11.106  1.00 22.49  ? 150 HIS A O   1 
ATOM   952   C CB  . HIS A 1 121 ? 15.130  -16.356 13.070  1.00 24.84  ? 150 HIS A CB  1 
ATOM   953   C CG  . HIS A 1 121 ? 15.586  -15.032 13.550  1.00 24.20  ? 150 HIS A CG  1 
ATOM   954   N ND1 . HIS A 1 121 ? 16.909  -14.692 13.424  1.00 24.35  ? 150 HIS A ND1 1 
ATOM   955   C CD2 . HIS A 1 121 ? 14.989  -14.028 14.173  1.00 27.69  ? 150 HIS A CD2 1 
ATOM   956   C CE1 . HIS A 1 121 ? 17.108  -13.513 13.979  1.00 28.62  ? 150 HIS A CE1 1 
ATOM   957   N NE2 . HIS A 1 121 ? 15.961  -13.082 14.436  1.00 28.82  ? 150 HIS A NE2 1 
ATOM   958   N N   . VAL A 1 122 ? 14.632  -14.152 10.651  1.00 23.41  ? 151 VAL A N   1 
ATOM   959   C CA  . VAL A 1 122 ? 13.860  -13.023 10.151  1.00 22.19  ? 151 VAL A CA  1 
ATOM   960   C C   . VAL A 1 122 ? 13.271  -13.329 8.777   1.00 25.67  ? 151 VAL A C   1 
ATOM   961   O O   . VAL A 1 122 ? 12.111  -12.994 8.545   1.00 22.97  ? 151 VAL A O   1 
ATOM   962   C CB  . VAL A 1 122 ? 14.678  -11.725 10.128  1.00 21.83  ? 151 VAL A CB  1 
ATOM   963   C CG1 . VAL A 1 122 ? 13.948  -10.599 9.413   1.00 21.90  ? 151 VAL A CG1 1 
ATOM   964   C CG2 . VAL A 1 122 ? 15.083  -11.314 11.546  1.00 21.45  ? 151 VAL A CG2 1 
ATOM   965   N N   . VAL A 1 123 ? 14.066  -13.932 7.879   1.00 25.52  ? 152 VAL A N   1 
ATOM   966   C CA  . VAL A 1 123 ? 13.557  -14.360 6.586   1.00 28.23  ? 152 VAL A CA  1 
ATOM   967   C C   . VAL A 1 123 ? 12.349  -15.279 6.808   1.00 26.12  ? 152 VAL A C   1 
ATOM   968   O O   . VAL A 1 123 ? 11.326  -15.090 6.176   1.00 24.21  ? 152 VAL A O   1 
ATOM   969   C CB  . VAL A 1 123 ? 14.633  -15.048 5.718   1.00 26.47  ? 152 VAL A CB  1 
ATOM   970   C CG1 . VAL A 1 123 ? 14.015  -15.663 4.482   1.00 28.15  ? 152 VAL A CG1 1 
ATOM   971   C CG2 . VAL A 1 123 ? 15.770  -14.123 5.317   1.00 26.42  ? 152 VAL A CG2 1 
ATOM   972   N N   . THR A 1 124 ? 12.475  -16.285 7.691   1.00 26.16  ? 153 THR A N   1 
ATOM   973   C CA  . THR A 1 124 ? 11.398  -17.233 7.957   1.00 27.50  ? 153 THR A CA  1 
ATOM   974   C C   . THR A 1 124 ? 10.134  -16.519 8.447   1.00 28.77  ? 153 THR A C   1 
ATOM   975   O O   . THR A 1 124 ? 9.023   -16.800 7.995   1.00 27.16  ? 153 THR A O   1 
ATOM   976   C CB  . THR A 1 124 ? 11.839  -18.282 8.988   1.00 28.08  ? 153 THR A CB  1 
ATOM   977   O OG1 . THR A 1 124 ? 12.915  -19.007 8.388   1.00 29.81  ? 153 THR A OG1 1 
ATOM   978   C CG2 . THR A 1 124 ? 10.735  -19.236 9.394   1.00 27.12  ? 153 THR A CG2 1 
ATOM   979   N N   . MET A 1 125 ? 10.320  -15.582 9.387   1.00 26.87  ? 154 MET A N   1 
ATOM   980   C CA  . MET A 1 125 ? 9.196   -14.908 10.014  1.00 29.42  ? 154 MET A CA  1 
ATOM   981   C C   . MET A 1 125 ? 8.392   -14.155 8.958   1.00 26.33  ? 154 MET A C   1 
ATOM   982   O O   . MET A 1 125 ? 7.168   -14.189 8.949   1.00 22.77  ? 154 MET A O   1 
ATOM   983   C CB  . MET A 1 125 ? 9.698   -13.904 11.053  1.00 31.84  ? 154 MET A CB  1 
ATOM   984   C CG  . MET A 1 125 ? 8.639   -13.522 12.054  1.00 35.45  ? 154 MET A CG  1 
ATOM   985   S SD  . MET A 1 125 ? 9.081   -12.093 13.075  1.00 38.99  ? 154 MET A SD  1 
ATOM   986   C CE  . MET A 1 125 ? 10.833  -11.961 12.716  1.00 37.49  ? 154 MET A CE  1 
ATOM   987   N N   . LEU A 1 126 ? 9.102   -13.405 8.120   1.00 26.87  ? 155 LEU A N   1 
ATOM   988   C CA  . LEU A 1 126 ? 8.499   -12.639 7.041   1.00 27.74  ? 155 LEU A CA  1 
ATOM   989   C C   . LEU A 1 126 ? 7.784   -13.602 6.097   1.00 27.71  ? 155 LEU A C   1 
ATOM   990   O O   . LEU A 1 126 ? 6.591   -13.458 5.830   1.00 22.63  ? 155 LEU A O   1 
ATOM   991   C CB  . LEU A 1 126 ? 9.606   -11.846 6.339   1.00 30.11  ? 155 LEU A CB  1 
ATOM   992   C CG  . LEU A 1 126 ? 10.188  -10.674 7.124   1.00 29.05  ? 155 LEU A CG  1 
ATOM   993   C CD1 . LEU A 1 126 ? 11.436  -10.151 6.471   1.00 29.99  ? 155 LEU A CD1 1 
ATOM   994   C CD2 . LEU A 1 126 ? 9.187   -9.549  7.271   1.00 28.13  ? 155 LEU A CD2 1 
ATOM   995   N N   . ASP A 1 127 ? 8.485   -14.663 5.675   1.00 26.55  ? 156 ASP A N   1 
ATOM   996   C CA  . ASP A 1 127 ? 7.867   -15.622 4.771   1.00 30.92  ? 156 ASP A CA  1 
ATOM   997   C C   . ASP A 1 127 ? 6.612   -16.259 5.387   1.00 31.63  ? 156 ASP A C   1 
ATOM   998   O O   . ASP A 1 127 ? 5.808   -16.828 4.662   1.00 27.83  ? 156 ASP A O   1 
ATOM   999   C CB  . ASP A 1 127 ? 8.890   -16.667 4.313   1.00 29.84  ? 156 ASP A CB  1 
ATOM   1000  C CG  . ASP A 1 127 ? 9.957   -16.120 3.375   1.00 31.78  ? 156 ASP A CG  1 
ATOM   1001  O OD1 . ASP A 1 127 ? 9.901   -14.904 2.997   1.00 28.63  ? 156 ASP A OD1 1 
ATOM   1002  O OD2 . ASP A 1 127 ? 10.870  -16.892 3.045   1.00 31.48  ? 156 ASP A OD2 1 
ATOM   1003  N N   . ASN A 1 128 ? 6.416   -16.188 6.717   1.00 32.06  ? 157 ASN A N   1 
ATOM   1004  C CA  . ASN A 1 128 ? 5.312   -16.905 7.349   1.00 31.29  ? 157 ASN A CA  1 
ATOM   1005  C C   . ASN A 1 128 ? 4.166   -15.967 7.724   1.00 28.23  ? 157 ASN A C   1 
ATOM   1006  O O   . ASN A 1 128 ? 3.097   -16.426 8.100   1.00 28.02  ? 157 ASN A O   1 
ATOM   1007  C CB  . ASN A 1 128 ? 5.784   -17.676 8.583   1.00 32.37  ? 157 ASN A CB  1 
ATOM   1008  C CG  . ASN A 1 128 ? 6.620   -18.893 8.242   1.00 33.73  ? 157 ASN A CG  1 
ATOM   1009  O OD1 . ASN A 1 128 ? 6.709   -19.287 7.082   1.00 35.01  ? 157 ASN A OD1 1 
ATOM   1010  N ND2 . ASN A 1 128 ? 7.253   -19.480 9.242   1.00 32.98  ? 157 ASN A ND2 1 
ATOM   1011  N N   . PHE A 1 129 ? 4.387   -14.656 7.642   1.00 26.90  ? 158 PHE A N   1 
ATOM   1012  C CA  . PHE A 1 129 ? 3.347   -13.696 7.968   1.00 28.20  ? 158 PHE A CA  1 
ATOM   1013  C C   . PHE A 1 129 ? 2.169   -13.831 7.004   1.00 30.47  ? 158 PHE A C   1 
ATOM   1014  O O   . PHE A 1 129 ? 2.364   -13.910 5.782   1.00 28.26  ? 158 PHE A O   1 
ATOM   1015  C CB  . PHE A 1 129 ? 3.909   -12.271 7.910   1.00 26.92  ? 158 PHE A CB  1 
ATOM   1016  C CG  . PHE A 1 129 ? 4.662   -11.805 9.126   1.00 26.95  ? 158 PHE A CG  1 
ATOM   1017  C CD1 . PHE A 1 129 ? 4.417   -12.347 10.377  1.00 27.64  ? 158 PHE A CD1 1 
ATOM   1018  C CD2 . PHE A 1 129 ? 5.621   -10.809 9.015   1.00 29.84  ? 158 PHE A CD2 1 
ATOM   1019  C CE1 . PHE A 1 129 ? 5.095   -11.890 11.498  1.00 28.34  ? 158 PHE A CE1 1 
ATOM   1020  C CE2 . PHE A 1 129 ? 6.311   -10.370 10.138  1.00 28.19  ? 158 PHE A CE2 1 
ATOM   1021  C CZ  . PHE A 1 129 ? 6.044   -10.909 11.366  1.00 29.47  ? 158 PHE A CZ  1 
ATOM   1022  N N   . PRO A 1 130 ? 0.912   -13.770 7.501   1.00 33.03  ? 159 PRO A N   1 
ATOM   1023  C CA  . PRO A 1 130 ? -0.252  -13.863 6.622   1.00 32.80  ? 159 PRO A CA  1 
ATOM   1024  C C   . PRO A 1 130 ? -0.394  -12.569 5.835   1.00 32.68  ? 159 PRO A C   1 
ATOM   1025  O O   . PRO A 1 130 ? 0.172   -11.546 6.219   1.00 32.01  ? 159 PRO A O   1 
ATOM   1026  C CB  . PRO A 1 130 ? -1.405  -14.028 7.615   1.00 37.40  ? 159 PRO A CB  1 
ATOM   1027  C CG  . PRO A 1 130 ? -0.949  -13.180 8.779   1.00 34.77  ? 159 PRO A CG  1 
ATOM   1028  C CD  . PRO A 1 130 ? 0.531   -13.504 8.892   1.00 35.26  ? 159 PRO A CD  1 
ATOM   1029  N N   . THR A 1 131 ? -1.218  -12.610 4.783   1.00 28.85  ? 160 THR A N   1 
ATOM   1030  C CA  . THR A 1 131 ? -1.359  -11.496 3.859   1.00 33.32  ? 160 THR A CA  1 
ATOM   1031  C C   . THR A 1 131 ? -2.168  -10.349 4.465   1.00 32.95  ? 160 THR A C   1 
ATOM   1032  O O   . THR A 1 131 ? -2.115  -9.237  3.954   1.00 35.99  ? 160 THR A O   1 
ATOM   1033  C CB  . THR A 1 131 ? -2.081  -11.946 2.588   1.00 34.14  ? 160 THR A CB  1 
ATOM   1034  O OG1 . THR A 1 131 ? -3.367  -12.377 3.035   1.00 35.77  ? 160 THR A OG1 1 
ATOM   1035  C CG2 . THR A 1 131 ? -1.363  -13.056 1.857   1.00 35.69  ? 160 THR A CG2 1 
ATOM   1036  N N   . ASN A 1 132 ? -2.922  -10.614 5.537   1.00 33.57  ? 161 ASN A N   1 
ATOM   1037  C CA  . ASN A 1 132 ? -3.738  -9.578  6.170   1.00 32.48  ? 161 ASN A CA  1 
ATOM   1038  C C   . ASN A 1 132 ? -2.990  -8.946  7.347   1.00 28.46  ? 161 ASN A C   1 
ATOM   1039  O O   . ASN A 1 132 ? -3.598  -8.295  8.205   1.00 28.29  ? 161 ASN A O   1 
ATOM   1040  C CB  . ASN A 1 132 ? -5.091  -10.149 6.619   1.00 32.37  ? 161 ASN A CB  1 
ATOM   1041  C CG  . ASN A 1 132 ? -5.027  -10.936 7.913   1.00 35.04  ? 161 ASN A CG  1 
ATOM   1042  O OD1 . ASN A 1 132 ? -5.908  -10.802 8.767   1.00 40.72  ? 161 ASN A OD1 1 
ATOM   1043  N ND2 . ASN A 1 132 ? -4.012  -11.775 8.070   1.00 34.13  ? 161 ASN A ND2 1 
ATOM   1044  N N   . LEU A 1 133 ? -1.673  -9.193  7.438   1.00 28.79  ? 162 LEU A N   1 
ATOM   1045  C CA  . LEU A 1 133 ? -0.822  -8.466  8.367   1.00 23.54  ? 162 LEU A CA  1 
ATOM   1046  C C   . LEU A 1 133 ? -0.246  -7.259  7.646   1.00 20.23  ? 162 LEU A C   1 
ATOM   1047  O O   . LEU A 1 133 ? 0.452   -7.404  6.648   1.00 24.89  ? 162 LEU A O   1 
ATOM   1048  C CB  . LEU A 1 133 ? 0.280   -9.382  8.906   1.00 22.54  ? 162 LEU A CB  1 
ATOM   1049  C CG  . LEU A 1 133 ? 1.132   -8.750  10.010  1.00 25.36  ? 162 LEU A CG  1 
ATOM   1050  C CD1 . LEU A 1 133 ? 0.263   -8.258  11.157  1.00 23.55  ? 162 LEU A CD1 1 
ATOM   1051  C CD2 . LEU A 1 133 ? 2.202   -9.713  10.522  1.00 24.08  ? 162 LEU A CD2 1 
ATOM   1052  N N   . HIS A 1 134 ? -0.546  -6.062  8.151   1.00 21.05  ? 163 HIS A N   1 
ATOM   1053  C CA  . HIS A 1 134 ? -0.197  -4.850  7.445   1.00 20.76  ? 163 HIS A CA  1 
ATOM   1054  C C   . HIS A 1 134 ? 1.313   -4.778  7.226   1.00 21.54  ? 163 HIS A C   1 
ATOM   1055  O O   . HIS A 1 134 ? 2.075   -5.225  8.084   1.00 20.21  ? 163 HIS A O   1 
ATOM   1056  C CB  . HIS A 1 134 ? -0.618  -3.639  8.276   1.00 23.03  ? 163 HIS A CB  1 
ATOM   1057  C CG  . HIS A 1 134 ? -0.452  -2.324  7.606   1.00 22.27  ? 163 HIS A CG  1 
ATOM   1058  N ND1 . HIS A 1 134 ? 0.716   -1.623  7.373   1.00 19.59  ? 163 HIS A ND1 1 
ATOM   1059  C CD2 . HIS A 1 134 ? -1.455  -1.548  7.158   1.00 25.45  ? 163 HIS A CD2 1 
ATOM   1060  C CE1 . HIS A 1 134 ? 0.428   -0.487  6.783   1.00 22.16  ? 163 HIS A CE1 1 
ATOM   1061  N NE2 . HIS A 1 134 ? -0.903  -0.408  6.644   1.00 24.01  ? 163 HIS A NE2 1 
ATOM   1062  N N   . PRO A 1 135 ? 1.806   -4.187  6.112   1.00 20.94  ? 164 PRO A N   1 
ATOM   1063  C CA  . PRO A 1 135 ? 3.252   -4.096  5.890   1.00 21.03  ? 164 PRO A CA  1 
ATOM   1064  C C   . PRO A 1 135 ? 4.043   -3.347  6.969   1.00 21.10  ? 164 PRO A C   1 
ATOM   1065  O O   . PRO A 1 135 ? 5.223   -3.627  7.194   1.00 19.64  ? 164 PRO A O   1 
ATOM   1066  C CB  . PRO A 1 135 ? 3.418   -3.363  4.546   1.00 22.56  ? 164 PRO A CB  1 
ATOM   1067  C CG  . PRO A 1 135 ? 2.069   -3.477  3.866   1.00 22.67  ? 164 PRO A CG  1 
ATOM   1068  C CD  . PRO A 1 135 ? 1.040   -3.760  4.935   1.00 22.25  ? 164 PRO A CD  1 
ATOM   1069  N N   . MET A 1 136 ? 3.434   -2.361  7.641   1.00 21.15  ? 165 MET A N   1 
ATOM   1070  C CA  . MET A 1 136 ? 4.143   -1.667  8.705   1.00 22.81  ? 165 MET A CA  1 
ATOM   1071  C C   . MET A 1 136 ? 4.306   -2.538  9.958   1.00 18.63  ? 165 MET A C   1 
ATOM   1072  O O   . MET A 1 136 ? 5.301   -2.424  10.677  1.00 19.71  ? 165 MET A O   1 
ATOM   1073  C CB  . MET A 1 136 ? 3.419   -0.360  9.029   1.00 21.94  ? 165 MET A CB  1 
ATOM   1074  C CG  . MET A 1 136 ? 3.697   0.674   7.980   1.00 21.45  ? 165 MET A CG  1 
ATOM   1075  S SD  . MET A 1 136 ? 5.431   1.143   7.919   1.00 20.05  ? 165 MET A SD  1 
ATOM   1076  C CE  . MET A 1 136 ? 5.550   1.794   9.580   1.00 20.22  ? 165 MET A CE  1 
ATOM   1077  N N   . SER A 1 137 ? 3.375   -3.480  10.170  1.00 20.21  ? 166 SER A N   1 
ATOM   1078  C CA  . SER A 1 137 ? 3.449   -4.436  11.270  1.00 20.11  ? 166 SER A CA  1 
ATOM   1079  C C   . SER A 1 137 ? 4.526   -5.479  10.961  1.00 22.11  ? 166 SER A C   1 
ATOM   1080  O O   . SER A 1 137 ? 5.299   -5.837  11.822  1.00 20.68  ? 166 SER A O   1 
ATOM   1081  C CB  . SER A 1 137 ? 2.130   -5.092  11.531  1.00 22.14  ? 166 SER A CB  1 
ATOM   1082  O OG  . SER A 1 137 ? 1.089   -4.125  11.759  1.00 22.33  ? 166 SER A OG  1 
ATOM   1083  N N   . GLN A 1 138 ? 4.591   -5.935  9.713   1.00 20.83  ? 167 GLN A N   1 
ATOM   1084  C CA  . GLN A 1 138 ? 5.661   -6.844  9.296   1.00 19.65  ? 167 GLN A CA  1 
ATOM   1085  C C   . GLN A 1 138 ? 7.029   -6.168  9.428   1.00 18.37  ? 167 GLN A C   1 
ATOM   1086  O O   . GLN A 1 138 ? 7.973   -6.762  9.922   1.00 22.22  ? 167 GLN A O   1 
ATOM   1087  C CB  . GLN A 1 138 ? 5.453   -7.315  7.861   1.00 20.50  ? 167 GLN A CB  1 
ATOM   1088  C CG  . GLN A 1 138 ? 4.104   -7.971  7.605   1.00 22.84  ? 167 GLN A CG  1 
ATOM   1089  C CD  . GLN A 1 138 ? 4.079   -8.846  6.377   1.00 25.04  ? 167 GLN A CD  1 
ATOM   1090  O OE1 . GLN A 1 138 ? 5.117   -9.308  5.910   1.00 28.61  ? 167 GLN A OE1 1 
ATOM   1091  N NE2 . GLN A 1 138 ? 2.881   -9.141  5.884   1.00 23.21  ? 167 GLN A NE2 1 
ATOM   1092  N N   . LEU A 1 139 ? 7.134   -4.898  9.057   1.00 17.24  ? 168 LEU A N   1 
ATOM   1093  C CA  . LEU A 1 139 ? 8.401   -4.190  9.163   1.00 19.53  ? 168 LEU A CA  1 
ATOM   1094  C C   . LEU A 1 139 ? 8.855   -4.061  10.621  1.00 20.30  ? 168 LEU A C   1 
ATOM   1095  O O   . LEU A 1 139 ? 10.017  -4.330  10.942  1.00 19.02  ? 168 LEU A O   1 
ATOM   1096  C CB  . LEU A 1 139 ? 8.241   -2.814  8.525   1.00 20.44  ? 168 LEU A CB  1 
ATOM   1097  C CG  . LEU A 1 139 ? 9.491   -1.943  8.504   1.00 21.40  ? 168 LEU A CG  1 
ATOM   1098  C CD1 . LEU A 1 139 ? 10.552  -2.479  7.543   1.00 19.71  ? 168 LEU A CD1 1 
ATOM   1099  C CD2 . LEU A 1 139 ? 9.101   -0.513  8.166   1.00 22.65  ? 168 LEU A CD2 1 
ATOM   1100  N N   . SER A 1 140 ? 7.936   -3.591  11.469  1.00 19.30  ? 169 SER A N   1 
ATOM   1101  C CA  . SER A 1 140 ? 8.153   -3.384  12.883  1.00 21.01  ? 169 SER A CA  1 
ATOM   1102  C C   . SER A 1 140 ? 8.619   -4.675  13.552  1.00 20.28  ? 169 SER A C   1 
ATOM   1103  O O   . SER A 1 140 ? 9.719   -4.710  14.081  1.00 20.26  ? 169 SER A O   1 
ATOM   1104  C CB  . SER A 1 140 ? 6.910   -2.873  13.542  1.00 23.30  ? 169 SER A CB  1 
ATOM   1105  O OG  . SER A 1 140 ? 7.207   -2.465  14.866  1.00 24.07  ? 169 SER A OG  1 
ATOM   1106  N N   . ALA A 1 141 ? 7.804   -5.731  13.419  1.00 20.20  ? 170 ALA A N   1 
ATOM   1107  C CA  . ALA A 1 141 ? 8.113   -7.022  14.016  1.00 21.75  ? 170 ALA A CA  1 
ATOM   1108  C C   . ALA A 1 141 ? 9.467   -7.549  13.533  1.00 21.97  ? 170 ALA A C   1 
ATOM   1109  O O   . ALA A 1 141 ? 10.254  -8.045  14.345  1.00 20.95  ? 170 ALA A O   1 
ATOM   1110  C CB  . ALA A 1 141 ? 7.022   -7.994  13.696  1.00 21.21  ? 170 ALA A CB  1 
ATOM   1111  N N   . ALA A 1 142 ? 9.712   -7.465  12.216  1.00 20.52  ? 171 ALA A N   1 
ATOM   1112  C CA  . ALA A 1 142 ? 10.970  -7.892  11.630  1.00 21.07  ? 171 ALA A CA  1 
ATOM   1113  C C   . ALA A 1 142 ? 12.154  -7.084  12.156  1.00 18.70  ? 171 ALA A C   1 
ATOM   1114  O O   . ALA A 1 142 ? 13.209  -7.633  12.407  1.00 18.64  ? 171 ALA A O   1 
ATOM   1115  C CB  . ALA A 1 142 ? 10.914  -7.878  10.124  1.00 21.17  ? 171 ALA A CB  1 
ATOM   1116  N N   . VAL A 1 143 ? 12.053  -5.766  12.310  1.00 18.23  ? 172 VAL A N   1 
ATOM   1117  C CA  . VAL A 1 143 ? 13.191  -5.036  12.810  1.00 18.47  ? 172 VAL A CA  1 
ATOM   1118  C C   . VAL A 1 143 ? 13.448  -5.378  14.286  1.00 17.66  ? 172 VAL A C   1 
ATOM   1119  O O   . VAL A 1 143 ? 14.598  -5.470  14.687  1.00 19.76  ? 172 VAL A O   1 
ATOM   1120  C CB  . VAL A 1 143 ? 13.017  -3.526  12.596  1.00 19.06  ? 172 VAL A CB  1 
ATOM   1121  C CG1 . VAL A 1 143 ? 14.114  -2.723  13.279  1.00 20.72  ? 172 VAL A CG1 1 
ATOM   1122  C CG2 . VAL A 1 143 ? 12.973  -3.218  11.125  1.00 19.21  ? 172 VAL A CG2 1 
ATOM   1123  N N   . THR A 1 144 ? 12.388  -5.677  15.031  1.00 18.76  ? 173 THR A N   1 
ATOM   1124  C CA  . THR A 1 144 ? 12.499  -6.061  16.435  1.00 20.24  ? 173 THR A CA  1 
ATOM   1125  C C   . THR A 1 144 ? 13.250  -7.391  16.520  1.00 20.61  ? 173 THR A C   1 
ATOM   1126  O O   . THR A 1 144 ? 14.180  -7.543  17.308  1.00 21.99  ? 173 THR A O   1 
ATOM   1127  C CB  . THR A 1 144 ? 11.126  -6.158  17.111  1.00 19.30  ? 173 THR A CB  1 
ATOM   1128  O OG1 . THR A 1 144 ? 10.679  -4.809  17.235  1.00 19.09  ? 173 THR A OG1 1 
ATOM   1129  C CG2 . THR A 1 144 ? 11.156  -6.749  18.505  1.00 18.67  ? 173 THR A CG2 1 
ATOM   1130  N N   . ALA A 1 145 ? 12.835  -8.326  15.661  1.00 24.06  ? 174 ALA A N   1 
ATOM   1131  C CA  . ALA A 1 145 ? 13.469  -9.631  15.604  1.00 21.99  ? 174 ALA A CA  1 
ATOM   1132  C C   . ALA A 1 145 ? 14.930  -9.530  15.162  1.00 21.74  ? 174 ALA A C   1 
ATOM   1133  O O   . ALA A 1 145 ? 15.710  -10.428 15.465  1.00 25.65  ? 174 ALA A O   1 
ATOM   1134  C CB  . ALA A 1 145 ? 12.678  -10.526 14.701  1.00 22.77  ? 174 ALA A CB  1 
ATOM   1135  N N   . LEU A 1 146 ? 15.317  -8.440  14.490  1.00 20.90  ? 175 LEU A N   1 
ATOM   1136  C CA  . LEU A 1 146 ? 16.693  -8.252  14.070  1.00 22.03  ? 175 LEU A CA  1 
ATOM   1137  C C   . LEU A 1 146 ? 17.611  -7.881  15.241  1.00 23.17  ? 175 LEU A C   1 
ATOM   1138  O O   . LEU A 1 146 ? 18.835  -7.907  15.080  1.00 21.04  ? 175 LEU A O   1 
ATOM   1139  C CB  . LEU A 1 146 ? 16.748  -7.179  12.968  1.00 22.59  ? 175 LEU A CB  1 
ATOM   1140  C CG  . LEU A 1 146 ? 16.442  -7.619  11.534  1.00 23.54  ? 175 LEU A CG  1 
ATOM   1141  C CD1 . LEU A 1 146 ? 16.462  -6.431  10.587  1.00 21.92  ? 175 LEU A CD1 1 
ATOM   1142  C CD2 . LEU A 1 146 ? 17.441  -8.660  11.048  1.00 23.03  ? 175 LEU A CD2 1 
ATOM   1143  N N   . ASN A 1 147 ? 17.070  -7.545  16.432  1.00 19.96  ? 176 ASN A N   1 
ATOM   1144  C CA  . ASN A 1 147 ? 17.927  -7.104  17.524  1.00 20.08  ? 176 ASN A CA  1 
ATOM   1145  C C   . ASN A 1 147 ? 18.773  -8.272  18.059  1.00 18.74  ? 176 ASN A C   1 
ATOM   1146  O O   . ASN A 1 147 ? 19.692  -8.050  18.843  1.00 20.49  ? 176 ASN A O   1 
ATOM   1147  C CB  . ASN A 1 147 ? 17.114  -6.376  18.596  1.00 20.18  ? 176 ASN A CB  1 
ATOM   1148  C CG  . ASN A 1 147 ? 16.971  -7.129  19.889  1.00 22.76  ? 176 ASN A CG  1 
ATOM   1149  O OD1 . ASN A 1 147 ? 16.608  -8.296  19.900  1.00 25.75  ? 176 ASN A OD1 1 
ATOM   1150  N ND2 . ASN A 1 147 ? 17.326  -6.482  20.978  1.00 20.84  ? 176 ASN A ND2 1 
ATOM   1151  N N   . SER A 1 148 ? 18.462  -9.517  17.647  1.00 22.16  ? 177 SER A N   1 
ATOM   1152  C CA  . SER A 1 148 ? 19.353  -10.624 17.939  1.00 23.87  ? 177 SER A CA  1 
ATOM   1153  C C   . SER A 1 148 ? 20.734  -10.347 17.357  1.00 25.96  ? 177 SER A C   1 
ATOM   1154  O O   . SER A 1 148 ? 21.707  -10.962 17.781  1.00 27.22  ? 177 SER A O   1 
ATOM   1155  C CB  . SER A 1 148 ? 18.831  -11.926 17.419  1.00 24.11  ? 177 SER A CB  1 
ATOM   1156  O OG  . SER A 1 148 ? 18.701  -11.892 16.006  1.00 27.39  ? 177 SER A OG  1 
ATOM   1157  N N   . GLU A 1 149 ? 20.805  -9.461  16.346  1.00 25.77  ? 178 GLU A N   1 
ATOM   1158  C CA  . GLU A 1 149 ? 22.062  -9.131  15.702  1.00 28.77  ? 178 GLU A CA  1 
ATOM   1159  C C   . GLU A 1 149 ? 22.724  -7.907  16.324  1.00 27.16  ? 178 GLU A C   1 
ATOM   1160  O O   . GLU A 1 149 ? 23.750  -7.468  15.809  1.00 30.36  ? 178 GLU A O   1 
ATOM   1161  C CB  . GLU A 1 149 ? 21.850  -8.873  14.201  1.00 31.29  ? 178 GLU A CB  1 
ATOM   1162  C CG  . GLU A 1 149 ? 21.087  -9.976  13.507  1.00 35.81  ? 178 GLU A CG  1 
ATOM   1163  C CD  . GLU A 1 149 ? 21.663  -11.368 13.700  1.00 38.30  ? 178 GLU A CD  1 
ATOM   1164  O OE1 . GLU A 1 149 ? 22.837  -11.564 13.346  1.00 38.54  ? 178 GLU A OE1 1 
ATOM   1165  O OE2 . GLU A 1 149 ? 20.930  -12.241 14.217  1.00 39.82  ? 178 GLU A OE2 1 
ATOM   1166  N N   . SER A 1 150 ? 22.165  -7.368  17.422  1.00 24.91  ? 179 SER A N   1 
ATOM   1167  C CA  . SER A 1 150 ? 22.619  -6.091  17.950  1.00 23.00  ? 179 SER A CA  1 
ATOM   1168  C C   . SER A 1 150 ? 23.969  -6.210  18.646  1.00 24.34  ? 179 SER A C   1 
ATOM   1169  O O   . SER A 1 150 ? 24.092  -6.829  19.710  1.00 25.74  ? 179 SER A O   1 
ATOM   1170  C CB  . SER A 1 150 ? 21.643  -5.494  18.907  1.00 21.69  ? 179 SER A CB  1 
ATOM   1171  O OG  . SER A 1 150 ? 22.216  -4.327  19.455  1.00 23.11  ? 179 SER A OG  1 
ATOM   1172  N N   . ASN A 1 151 ? 24.955  -5.520  18.081  1.00 26.49  ? 180 ASN A N   1 
ATOM   1173  C CA  . ASN A 1 151 ? 26.243  -5.332  18.717  1.00 28.21  ? 180 ASN A CA  1 
ATOM   1174  C C   . ASN A 1 151 ? 26.081  -4.556  20.021  1.00 25.23  ? 180 ASN A C   1 
ATOM   1175  O O   . ASN A 1 151 ? 26.643  -4.950  21.028  1.00 25.88  ? 180 ASN A O   1 
ATOM   1176  C CB  . ASN A 1 151 ? 27.225  -4.615  17.792  1.00 32.08  ? 180 ASN A CB  1 
ATOM   1177  C CG  . ASN A 1 151 ? 27.462  -5.390  16.516  1.00 34.96  ? 180 ASN A CG  1 
ATOM   1178  O OD1 . ASN A 1 151 ? 27.825  -6.562  16.565  1.00 33.97  ? 180 ASN A OD1 1 
ATOM   1179  N ND2 . ASN A 1 151 ? 27.200  -4.762  15.380  1.00 39.09  ? 180 ASN A ND2 1 
ATOM   1180  N N   . PHE A 1 152 ? 25.336  -3.440  20.001  1.00 23.64  ? 181 PHE A N   1 
ATOM   1181  C CA  . PHE A 1 152 ? 25.196  -2.629  21.192  1.00 23.41  ? 181 PHE A CA  1 
ATOM   1182  C C   . PHE A 1 152 ? 24.571  -3.438  22.325  1.00 22.82  ? 181 PHE A C   1 
ATOM   1183  O O   . PHE A 1 152 ? 25.053  -3.347  23.447  1.00 26.26  ? 181 PHE A O   1 
ATOM   1184  C CB  . PHE A 1 152 ? 24.431  -1.319  20.952  1.00 21.32  ? 181 PHE A CB  1 
ATOM   1185  C CG  . PHE A 1 152 ? 24.319  -0.481  22.201  1.00 21.73  ? 181 PHE A CG  1 
ATOM   1186  C CD1 . PHE A 1 152 ? 25.404  0.257   22.652  1.00 20.90  ? 181 PHE A CD1 1 
ATOM   1187  C CD2 . PHE A 1 152 ? 23.186  -0.543  22.996  1.00 22.07  ? 181 PHE A CD2 1 
ATOM   1188  C CE1 . PHE A 1 152 ? 25.327  0.984   23.829  1.00 23.06  ? 181 PHE A CE1 1 
ATOM   1189  C CE2 . PHE A 1 152 ? 23.093  0.222   24.150  1.00 21.80  ? 181 PHE A CE2 1 
ATOM   1190  C CZ  . PHE A 1 152 ? 24.160  0.985   24.561  1.00 24.61  ? 181 PHE A CZ  1 
ATOM   1191  N N   . ALA A 1 153 ? 23.510  -4.211  22.052  1.00 23.92  ? 182 ALA A N   1 
ATOM   1192  C CA  . ALA A 1 153 ? 22.872  -4.967  23.123  1.00 24.38  ? 182 ALA A CA  1 
ATOM   1193  C C   . ALA A 1 153 ? 23.893  -5.923  23.730  1.00 24.23  ? 182 ALA A C   1 
ATOM   1194  O O   . ALA A 1 153 ? 23.999  -6.010  24.948  1.00 24.43  ? 182 ALA A O   1 
ATOM   1195  C CB  . ALA A 1 153 ? 21.632  -5.707  22.666  1.00 23.07  ? 182 ALA A CB  1 
ATOM   1196  N N   . ARG A 1 154 ? 24.651  -6.625  22.885  1.00 27.06  ? 183 ARG A N   1 
ATOM   1197  C CA  . ARG A 1 154 ? 25.595  -7.626  23.387  1.00 31.72  ? 183 ARG A CA  1 
ATOM   1198  C C   . ARG A 1 154 ? 26.680  -6.954  24.233  1.00 30.41  ? 183 ARG A C   1 
ATOM   1199  O O   . ARG A 1 154 ? 26.941  -7.350  25.375  1.00 32.52  ? 183 ARG A O   1 
ATOM   1200  C CB  . ARG A 1 154 ? 26.256  -8.387  22.236  1.00 34.26  ? 183 ARG A CB  1 
ATOM   1201  C CG  . ARG A 1 154 ? 27.312  -9.393  22.678  1.00 40.06  ? 183 ARG A CG  1 
ATOM   1202  C CD  . ARG A 1 154 ? 26.943  -10.858 22.537  1.00 43.30  ? 183 ARG A CD  1 
ATOM   1203  N NE  . ARG A 1 154 ? 25.575  -11.193 22.912  1.00 47.79  ? 183 ARG A NE  1 
ATOM   1204  C CZ  . ARG A 1 154 ? 25.092  -12.432 22.934  1.00 47.50  ? 183 ARG A CZ  1 
ATOM   1205  N NH1 . ARG A 1 154 ? 23.815  -12.646 23.211  1.00 47.29  ? 183 ARG A NH1 1 
ATOM   1206  N NH2 . ARG A 1 154 ? 25.889  -13.454 22.664  1.00 45.85  ? 183 ARG A NH2 1 
ATOM   1207  N N   . ALA A 1 155 ? 27.295  -5.919  23.650  1.00 28.47  ? 184 ALA A N   1 
ATOM   1208  C CA  . ALA A 1 155 ? 28.343  -5.144  24.278  1.00 27.14  ? 184 ALA A CA  1 
ATOM   1209  C C   . ALA A 1 155 ? 27.876  -4.527  25.596  1.00 27.22  ? 184 ALA A C   1 
ATOM   1210  O O   . ALA A 1 155 ? 28.668  -4.391  26.521  1.00 30.07  ? 184 ALA A O   1 
ATOM   1211  C CB  . ALA A 1 155 ? 28.847  -4.090  23.331  1.00 26.18  ? 184 ALA A CB  1 
ATOM   1212  N N   . TYR A 1 156 ? 26.603  -4.118  25.687  1.00 28.01  ? 185 TYR A N   1 
ATOM   1213  C CA  . TYR A 1 156 ? 26.127  -3.531  26.931  1.00 25.17  ? 185 TYR A CA  1 
ATOM   1214  C C   . TYR A 1 156 ? 26.003  -4.640  27.965  1.00 25.10  ? 185 TYR A C   1 
ATOM   1215  O O   . TYR A 1 156 ? 26.350  -4.428  29.123  1.00 26.68  ? 185 TYR A O   1 
ATOM   1216  C CB  . TYR A 1 156 ? 24.809  -2.754  26.778  1.00 24.17  ? 185 TYR A CB  1 
ATOM   1217  C CG  . TYR A 1 156 ? 24.382  -2.077  28.053  1.00 25.80  ? 185 TYR A CG  1 
ATOM   1218  C CD1 . TYR A 1 156 ? 23.797  -2.791  29.085  1.00 25.83  ? 185 TYR A CD1 1 
ATOM   1219  C CD2 . TYR A 1 156 ? 24.660  -0.742  28.272  1.00 28.59  ? 185 TYR A CD2 1 
ATOM   1220  C CE1 . TYR A 1 156 ? 23.477  -2.194  30.297  1.00 25.39  ? 185 TYR A CE1 1 
ATOM   1221  C CE2 . TYR A 1 156 ? 24.331  -0.125  29.467  1.00 28.27  ? 185 TYR A CE2 1 
ATOM   1222  C CZ  . TYR A 1 156 ? 23.731  -0.848  30.481  1.00 25.95  ? 185 TYR A CZ  1 
ATOM   1223  O OH  . TYR A 1 156 ? 23.417  -0.221  31.668  1.00 29.30  ? 185 TYR A OH  1 
ATOM   1224  N N   . ALA A 1 157 ? 25.549  -5.820  27.539  1.00 27.75  ? 186 ALA A N   1 
ATOM   1225  C CA  . ALA A 1 157 ? 25.371  -6.935  28.453  1.00 31.65  ? 186 ALA A CA  1 
ATOM   1226  C C   . ALA A 1 157 ? 26.705  -7.336  29.086  1.00 36.64  ? 186 ALA A C   1 
ATOM   1227  O O   . ALA A 1 157 ? 26.744  -7.829  30.206  1.00 39.66  ? 186 ALA A O   1 
ATOM   1228  C CB  . ALA A 1 157 ? 24.744  -8.112  27.754  1.00 32.09  ? 186 ALA A CB  1 
ATOM   1229  N N   . GLN A 1 158 ? 27.802  -7.124  28.369  1.00 37.28  ? 187 GLN A N   1 
ATOM   1230  C CA  . GLN A 1 158 ? 29.104  -7.555  28.837  1.00 40.81  ? 187 GLN A CA  1 
ATOM   1231  C C   . GLN A 1 158 ? 29.754  -6.433  29.638  1.00 42.20  ? 187 GLN A C   1 
ATOM   1232  O O   . GLN A 1 158 ? 30.850  -6.610  30.166  1.00 44.97  ? 187 GLN A O   1 
ATOM   1233  C CB  . GLN A 1 158 ? 29.958  -7.958  27.637  1.00 43.43  ? 187 GLN A CB  1 
ATOM   1234  C CG  . GLN A 1 158 ? 29.470  -9.234  26.967  1.00 48.11  ? 187 GLN A CG  1 
ATOM   1235  C CD  . GLN A 1 158 ? 30.209  -9.501  25.678  1.00 52.91  ? 187 GLN A CD  1 
ATOM   1236  O OE1 . GLN A 1 158 ? 30.112  -8.740  24.719  1.00 53.30  ? 187 GLN A OE1 1 
ATOM   1237  N NE2 . GLN A 1 158 ? 30.974  -10.579 25.651  1.00 54.29  ? 187 GLN A NE2 1 
ATOM   1238  N N   . GLY A 1 159 ? 29.069  -5.287  29.706  1.00 34.41  ? 188 GLY A N   1 
ATOM   1239  C CA  . GLY A 1 159 ? 29.575  -4.114  30.383  1.00 33.53  ? 188 GLY A CA  1 
ATOM   1240  C C   . GLY A 1 159 ? 30.529  -3.354  29.484  1.00 32.85  ? 188 GLY A C   1 
ATOM   1241  O O   . GLY A 1 159 ? 31.396  -3.954  28.869  1.00 36.05  ? 188 GLY A O   1 
ATOM   1242  N N   . ILE A 1 160 ? 30.355  -2.038  29.422  1.00 30.54  ? 189 ILE A N   1 
ATOM   1243  C CA  . ILE A 1 160 ? 31.158  -1.195  28.570  1.00 30.63  ? 189 ILE A CA  1 
ATOM   1244  C C   . ILE A 1 160 ? 31.000  0.227   29.096  1.00 26.51  ? 189 ILE A C   1 
ATOM   1245  O O   . ILE A 1 160 ? 29.967  0.580   29.666  1.00 28.41  ? 189 ILE A O   1 
ATOM   1246  C CB  . ILE A 1 160 ? 30.716  -1.336  27.097  1.00 35.87  ? 189 ILE A CB  1 
ATOM   1247  C CG1 . ILE A 1 160 ? 31.761  -0.813  26.104  1.00 42.58  ? 189 ILE A CG1 1 
ATOM   1248  C CG2 . ILE A 1 160 ? 29.359  -0.678  26.883  1.00 35.59  ? 189 ILE A CG2 1 
ATOM   1249  C CD1 . ILE A 1 160 ? 32.795  -1.848  25.664  1.00 46.95  ? 189 ILE A CD1 1 
ATOM   1250  N N   . SER A 1 161 ? 32.041  1.015   28.900  1.00 23.15  ? 190 SER A N   1 
ATOM   1251  C CA  . SER A 1 161 ? 32.044  2.408   29.294  1.00 25.15  ? 190 SER A CA  1 
ATOM   1252  C C   . SER A 1 161 ? 30.966  3.213   28.558  1.00 24.04  ? 190 SER A C   1 
ATOM   1253  O O   . SER A 1 161 ? 30.760  3.012   27.358  1.00 25.34  ? 190 SER A O   1 
ATOM   1254  C CB  . SER A 1 161 ? 33.401  2.945   29.046  1.00 24.45  ? 190 SER A CB  1 
ATOM   1255  O OG  . SER A 1 161 ? 33.389  4.354   28.914  1.00 30.11  ? 190 SER A OG  1 
ATOM   1256  N N   . ARG A 1 162 ? 30.283  4.115   29.294  1.00 25.46  ? 191 ARG A N   1 
ATOM   1257  C CA  . ARG A 1 162 ? 29.360  5.093   28.720  1.00 30.49  ? 191 ARG A CA  1 
ATOM   1258  C C   . ARG A 1 162 ? 29.967  5.822   27.521  1.00 28.69  ? 191 ARG A C   1 
ATOM   1259  O O   . ARG A 1 162 ? 29.263  6.089   26.546  1.00 27.24  ? 191 ARG A O   1 
ATOM   1260  C CB  . ARG A 1 162 ? 28.990  6.159   29.755  1.00 30.57  ? 191 ARG A CB  1 
ATOM   1261  C CG  . ARG A 1 162 ? 27.894  5.758   30.725  1.00 41.28  ? 191 ARG A CG  1 
ATOM   1262  C CD  . ARG A 1 162 ? 27.487  6.918   31.625  1.00 44.74  ? 191 ARG A CD  1 
ATOM   1263  N NE  . ARG A 1 162 ? 26.218  7.581   31.298  1.00 52.98  ? 191 ARG A NE  1 
ATOM   1264  C CZ  . ARG A 1 162 ? 25.898  8.157   30.133  1.00 55.67  ? 191 ARG A CZ  1 
ATOM   1265  N NH1 . ARG A 1 162 ? 26.611  7.931   29.041  1.00 59.36  ? 191 ARG A NH1 1 
ATOM   1266  N NH2 . ARG A 1 162 ? 24.833  8.941   30.059  1.00 51.58  ? 191 ARG A NH2 1 
ATOM   1267  N N   . THR A 1 163 ? 31.264  6.177   27.636  1.00 27.13  ? 192 THR A N   1 
ATOM   1268  C CA  . THR A 1 163 ? 32.006  6.903   26.614  1.00 29.52  ? 192 THR A CA  1 
ATOM   1269  C C   . THR A 1 163 ? 32.074  6.171   25.274  1.00 26.81  ? 192 THR A C   1 
ATOM   1270  O O   . THR A 1 163 ? 32.442  6.769   24.267  1.00 28.85  ? 192 THR A O   1 
ATOM   1271  C CB  . THR A 1 163 ? 33.466  7.123   27.031  1.00 30.94  ? 192 THR A CB  1 
ATOM   1272  O OG1 . THR A 1 163 ? 34.039  5.819   27.149  1.00 31.92  ? 192 THR A OG1 1 
ATOM   1273  C CG2 . THR A 1 163 ? 33.614  7.891   28.327  1.00 36.81  ? 192 THR A CG2 1 
ATOM   1274  N N   . LYS A 1 164 ? 31.803  4.862   25.258  1.00 26.29  ? 193 LYS A N   1 
ATOM   1275  C CA  . LYS A 1 164 ? 31.970  4.089   24.041  1.00 26.93  ? 193 LYS A CA  1 
ATOM   1276  C C   . LYS A 1 164 ? 30.633  3.620   23.451  1.00 25.25  ? 193 LYS A C   1 
ATOM   1277  O O   . LYS A 1 164 ? 30.595  2.964   22.412  1.00 24.59  ? 193 LYS A O   1 
ATOM   1278  C CB  . LYS A 1 164 ? 32.901  2.920   24.353  1.00 29.87  ? 193 LYS A CB  1 
ATOM   1279  C CG  . LYS A 1 164 ? 34.311  3.334   24.765  1.00 35.33  ? 193 LYS A CG  1 
ATOM   1280  C CD  . LYS A 1 164 ? 35.365  2.324   24.358  1.00 37.13  ? 193 LYS A CD  1 
ATOM   1281  C CE  . LYS A 1 164 ? 35.538  2.255   22.855  1.00 41.77  ? 193 LYS A CE  1 
ATOM   1282  N NZ  . LYS A 1 164 ? 36.227  1.011   22.444  1.00 44.68  ? 193 LYS A NZ  1 
ATOM   1283  N N   . TYR A 1 165 ? 29.508  3.958   24.081  1.00 21.24  ? 194 TYR A N   1 
ATOM   1284  C CA  . TYR A 1 165 ? 28.217  3.618   23.499  1.00 21.13  ? 194 TYR A CA  1 
ATOM   1285  C C   . TYR A 1 165 ? 28.153  3.956   22.001  1.00 19.75  ? 194 TYR A C   1 
ATOM   1286  O O   . TYR A 1 165 ? 27.640  3.177   21.218  1.00 22.67  ? 194 TYR A O   1 
ATOM   1287  C CB  . TYR A 1 165 ? 27.082  4.373   24.187  1.00 20.31  ? 194 TYR A CB  1 
ATOM   1288  C CG  . TYR A 1 165 ? 26.788  3.991   25.612  1.00 21.66  ? 194 TYR A CG  1 
ATOM   1289  C CD1 . TYR A 1 165 ? 27.170  2.769   26.140  1.00 21.76  ? 194 TYR A CD1 1 
ATOM   1290  C CD2 . TYR A 1 165 ? 26.058  4.845   26.408  1.00 23.81  ? 194 TYR A CD2 1 
ATOM   1291  C CE1 . TYR A 1 165 ? 26.848  2.423   27.445  1.00 25.34  ? 194 TYR A CE1 1 
ATOM   1292  C CE2 . TYR A 1 165 ? 25.762  4.532   27.726  1.00 25.01  ? 194 TYR A CE2 1 
ATOM   1293  C CZ  . TYR A 1 165 ? 26.131  3.301   28.235  1.00 25.02  ? 194 TYR A CZ  1 
ATOM   1294  O OH  . TYR A 1 165 ? 25.857  2.943   29.539  1.00 28.01  ? 194 TYR A OH  1 
ATOM   1295  N N   . TRP A 1 166 ? 28.619  5.137   21.591  1.00 20.71  ? 195 TRP A N   1 
ATOM   1296  C CA  . TRP A 1 166 ? 28.324  5.625   20.248  1.00 21.66  ? 195 TRP A CA  1 
ATOM   1297  C C   . TRP A 1 166 ? 28.890  4.707   19.172  1.00 22.39  ? 195 TRP A C   1 
ATOM   1298  O O   . TRP A 1 166 ? 28.240  4.539   18.146  1.00 19.05  ? 195 TRP A O   1 
ATOM   1299  C CB  . TRP A 1 166 ? 28.784  7.069   20.052  1.00 22.12  ? 195 TRP A CB  1 
ATOM   1300  C CG  . TRP A 1 166 ? 30.263  7.204   19.885  1.00 23.97  ? 195 TRP A CG  1 
ATOM   1301  C CD1 . TRP A 1 166 ? 31.156  7.535   20.863  1.00 25.40  ? 195 TRP A CD1 1 
ATOM   1302  C CD2 . TRP A 1 166 ? 31.019  7.081   18.663  1.00 25.17  ? 195 TRP A CD2 1 
ATOM   1303  N NE1 . TRP A 1 166 ? 32.426  7.558   20.346  1.00 28.13  ? 195 TRP A NE1 1 
ATOM   1304  C CE2 . TRP A 1 166 ? 32.376  7.297   18.997  1.00 26.60  ? 195 TRP A CE2 1 
ATOM   1305  C CE3 . TRP A 1 166 ? 30.699  6.779   17.336  1.00 23.53  ? 195 TRP A CE3 1 
ATOM   1306  C CZ2 . TRP A 1 166 ? 33.398  7.250   18.039  1.00 26.30  ? 195 TRP A CZ2 1 
ATOM   1307  C CZ3 . TRP A 1 166 ? 31.704  6.735   16.395  1.00 23.22  ? 195 TRP A CZ3 1 
ATOM   1308  C CH2 . TRP A 1 166 ? 33.035  6.964   16.738  1.00 22.79  ? 195 TRP A CH2 1 
ATOM   1309  N N   . GLU A 1 167 ? 30.077  4.103   19.416  1.00 22.81  ? 196 GLU A N   1 
ATOM   1310  C CA  . GLU A 1 167 ? 30.730  3.291   18.405  1.00 22.79  ? 196 GLU A CA  1 
ATOM   1311  C C   . GLU A 1 167 ? 29.866  2.090   18.021  1.00 22.78  ? 196 GLU A C   1 
ATOM   1312  O O   . GLU A 1 167 ? 29.815  1.728   16.837  1.00 22.62  ? 196 GLU A O   1 
ATOM   1313  C CB  . GLU A 1 167 ? 32.112  2.833   18.883  1.00 26.55  ? 196 GLU A CB  1 
ATOM   1314  C CG  . GLU A 1 167 ? 33.071  3.991   19.060  1.00 29.99  ? 196 GLU A CG  1 
ATOM   1315  C CD  . GLU A 1 167 ? 34.459  3.606   19.541  1.00 34.12  ? 196 GLU A CD  1 
ATOM   1316  O OE1 . GLU A 1 167 ? 35.067  2.742   18.923  1.00 40.48  ? 196 GLU A OE1 1 
ATOM   1317  O OE2 . GLU A 1 167 ? 34.916  4.188   20.527  1.00 40.09  ? 196 GLU A OE2 1 
ATOM   1318  N N   . LEU A 1 168 ? 29.235  1.448   19.018  1.00 24.02  ? 197 LEU A N   1 
ATOM   1319  C CA  . LEU A 1 168 ? 28.416  0.269   18.738  1.00 24.43  ? 197 LEU A CA  1 
ATOM   1320  C C   . LEU A 1 168 ? 27.028  0.668   18.238  1.00 21.95  ? 197 LEU A C   1 
ATOM   1321  O O   . LEU A 1 168 ? 26.420  -0.060  17.468  1.00 21.31  ? 197 LEU A O   1 
ATOM   1322  C CB  . LEU A 1 168 ? 28.315  -0.607  19.991  1.00 25.89  ? 197 LEU A CB  1 
ATOM   1323  C CG  . LEU A 1 168 ? 29.629  -1.272  20.388  1.00 32.38  ? 197 LEU A CG  1 
ATOM   1324  C CD1 . LEU A 1 168 ? 30.124  -0.738  21.733  1.00 39.25  ? 197 LEU A CD1 1 
ATOM   1325  C CD2 . LEU A 1 168 ? 29.488  -2.773  20.404  1.00 29.66  ? 197 LEU A CD2 1 
ATOM   1326  N N   . ILE A 1 169 ? 26.542  1.844   18.659  1.00 19.88  ? 198 ILE A N   1 
ATOM   1327  C CA  . ILE A 1 169 ? 25.319  2.384   18.079  1.00 20.22  ? 198 ILE A CA  1 
ATOM   1328  C C   . ILE A 1 169 ? 25.546  2.708   16.594  1.00 19.81  ? 198 ILE A C   1 
ATOM   1329  O O   . ILE A 1 169 ? 24.674  2.434   15.784  1.00 16.98  ? 198 ILE A O   1 
ATOM   1330  C CB  . ILE A 1 169 ? 24.848  3.606   18.880  1.00 19.21  ? 198 ILE A CB  1 
ATOM   1331  C CG1 . ILE A 1 169 ? 24.515  3.209   20.319  1.00 19.72  ? 198 ILE A CG1 1 
ATOM   1332  C CG2 . ILE A 1 169 ? 23.683  4.331   18.211  1.00 20.23  ? 198 ILE A CG2 1 
ATOM   1333  C CD1 . ILE A 1 169 ? 23.194  2.547   20.473  1.00 20.37  ? 198 ILE A CD1 1 
ATOM   1334  N N   . TYR A 1 170 ? 26.734  3.229   16.254  1.00 19.35  ? 199 TYR A N   1 
ATOM   1335  C CA  . TYR A 1 170 ? 27.113  3.488   14.876  1.00 20.86  ? 199 TYR A CA  1 
ATOM   1336  C C   . TYR A 1 170 ? 27.077  2.198   14.055  1.00 21.84  ? 199 TYR A C   1 
ATOM   1337  O O   . TYR A 1 170 ? 26.518  2.202   12.961  1.00 19.51  ? 199 TYR A O   1 
ATOM   1338  C CB  . TYR A 1 170 ? 28.473  4.189   14.760  1.00 21.79  ? 199 TYR A CB  1 
ATOM   1339  C CG  . TYR A 1 170 ? 29.051  4.233   13.358  1.00 21.71  ? 199 TYR A CG  1 
ATOM   1340  C CD1 . TYR A 1 170 ? 29.796  3.183   12.835  1.00 23.00  ? 199 TYR A CD1 1 
ATOM   1341  C CD2 . TYR A 1 170 ? 28.914  5.354   12.561  1.00 20.62  ? 199 TYR A CD2 1 
ATOM   1342  C CE1 . TYR A 1 170 ? 30.322  3.220   11.552  1.00 20.95  ? 199 TYR A CE1 1 
ATOM   1343  C CE2 . TYR A 1 170 ? 29.428  5.409   11.278  1.00 20.06  ? 199 TYR A CE2 1 
ATOM   1344  C CZ  . TYR A 1 170 ? 30.150  4.342   10.770  1.00 20.17  ? 199 TYR A CZ  1 
ATOM   1345  O OH  . TYR A 1 170 ? 30.708  4.399   9.499   1.00 23.14  ? 199 TYR A OH  1 
ATOM   1346  N N   . GLU A 1 171 ? 27.695  1.107   14.548  1.00 22.25  ? 200 GLU A N   1 
ATOM   1347  C CA  . GLU A 1 171 ? 27.797  -0.090  13.725  1.00 21.65  ? 200 GLU A CA  1 
ATOM   1348  C C   . GLU A 1 171 ? 26.415  -0.725  13.539  1.00 20.57  ? 200 GLU A C   1 
ATOM   1349  O O   . GLU A 1 171 ? 26.073  -1.179  12.461  1.00 19.73  ? 200 GLU A O   1 
ATOM   1350  C CB  . GLU A 1 171 ? 28.751  -1.108  14.346  1.00 23.53  ? 200 GLU A CB  1 
ATOM   1351  C CG  . GLU A 1 171 ? 30.205  -0.654  14.375  1.00 22.98  ? 200 GLU A CG  1 
ATOM   1352  C CD  . GLU A 1 171 ? 30.910  -0.595  13.029  1.00 25.09  ? 200 GLU A CD  1 
ATOM   1353  O OE1 . GLU A 1 171 ? 30.379  -1.149  12.036  1.00 22.67  ? 200 GLU A OE1 1 
ATOM   1354  O OE2 . GLU A 1 171 ? 31.958  0.061   12.967  1.00 23.21  ? 200 GLU A OE2 1 
ATOM   1355  N N   . ASP A 1 172 ? 25.612  -0.724  14.594  1.00 20.26  ? 201 ASP A N   1 
ATOM   1356  C CA  . ASP A 1 172 ? 24.270  -1.275  14.513  1.00 19.60  ? 201 ASP A CA  1 
ATOM   1357  C C   . ASP A 1 172 ? 23.393  -0.472  13.551  1.00 19.98  ? 201 ASP A C   1 
ATOM   1358  O O   . ASP A 1 172 ? 22.592  -1.063  12.821  1.00 20.52  ? 201 ASP A O   1 
ATOM   1359  C CB  . ASP A 1 172 ? 23.622  -1.312  15.897  1.00 19.58  ? 201 ASP A CB  1 
ATOM   1360  C CG  . ASP A 1 172 ? 23.954  -2.514  16.751  1.00 22.56  ? 201 ASP A CG  1 
ATOM   1361  O OD1 . ASP A 1 172 ? 24.539  -3.470  16.218  1.00 22.54  ? 201 ASP A OD1 1 
ATOM   1362  O OD2 . ASP A 1 172 ? 23.671  -2.453  17.963  1.00 23.49  ? 201 ASP A OD2 1 
ATOM   1363  N N   . SER A 1 173 ? 23.530  0.872   13.571  1.00 19.21  ? 202 SER A N   1 
ATOM   1364  C CA  . SER A 1 173 ? 22.695  1.754   12.768  1.00 19.42  ? 202 SER A CA  1 
ATOM   1365  C C   . SER A 1 173 ? 23.067  1.595   11.292  1.00 20.08  ? 202 SER A C   1 
ATOM   1366  O O   . SER A 1 173 ? 22.238  1.618   10.380  1.00 19.59  ? 202 SER A O   1 
ATOM   1367  C CB  . SER A 1 173 ? 22.893  3.183   13.200  1.00 18.72  ? 202 SER A CB  1 
ATOM   1368  O OG  . SER A 1 173 ? 22.475  3.426   14.540  1.00 17.91  ? 202 SER A OG  1 
ATOM   1369  N N   . MET A 1 174 ? 24.376  1.385   11.069  1.00 18.78  ? 203 MET A N   1 
ATOM   1370  C CA  . MET A 1 174 ? 24.868  1.164   9.727   1.00 18.88  ? 203 MET A CA  1 
ATOM   1371  C C   . MET A 1 174 ? 24.354  -0.186  9.214   1.00 18.25  ? 203 MET A C   1 
ATOM   1372  O O   . MET A 1 174 ? 23.944  -0.326  8.055   1.00 15.87  ? 203 MET A O   1 
ATOM   1373  C CB  . MET A 1 174 ? 26.393  1.251   9.741   1.00 19.27  ? 203 MET A CB  1 
ATOM   1374  C CG  . MET A 1 174 ? 26.872  2.698   9.901   1.00 22.65  ? 203 MET A CG  1 
ATOM   1375  S SD  . MET A 1 174 ? 27.099  3.635   8.369   1.00 22.54  ? 203 MET A SD  1 
ATOM   1376  C CE  . MET A 1 174 ? 28.461  2.728   7.626   1.00 25.58  ? 203 MET A CE  1 
ATOM   1377  N N   . ASP A 1 175 ? 24.345  -1.189  10.095  1.00 18.48  ? 204 ASP A N   1 
ATOM   1378  C CA  . ASP A 1 175 ? 23.847  -2.499  9.718   1.00 18.86  ? 204 ASP A CA  1 
ATOM   1379  C C   . ASP A 1 175 ? 22.350  -2.448  9.392   1.00 21.23  ? 204 ASP A C   1 
ATOM   1380  O O   . ASP A 1 175 ? 21.867  -3.074  8.443   1.00 18.83  ? 204 ASP A O   1 
ATOM   1381  C CB  . ASP A 1 175 ? 24.062  -3.527  10.824  1.00 21.85  ? 204 ASP A CB  1 
ATOM   1382  C CG  . ASP A 1 175 ? 25.507  -3.969  10.936  1.00 23.74  ? 204 ASP A CG  1 
ATOM   1383  O OD1 . ASP A 1 175 ? 26.345  -3.501  10.078  1.00 25.46  ? 204 ASP A OD1 1 
ATOM   1384  O OD2 . ASP A 1 175 ? 25.786  -4.732  11.873  1.00 23.90  ? 204 ASP A OD2 1 
ATOM   1385  N N   . LEU A 1 176 ? 21.608  -1.706  10.204  1.00 17.25  ? 205 LEU A N   1 
ATOM   1386  C CA  . LEU A 1 176 ? 20.165  -1.656  10.054  1.00 20.11  ? 205 LEU A CA  1 
ATOM   1387  C C   . LEU A 1 176 ? 19.795  -0.901  8.781   1.00 17.34  ? 205 LEU A C   1 
ATOM   1388  O O   . LEU A 1 176 ? 18.940  -1.351  8.068   1.00 18.50  ? 205 LEU A O   1 
ATOM   1389  C CB  . LEU A 1 176 ? 19.508  -1.038  11.286  1.00 18.68  ? 205 LEU A CB  1 
ATOM   1390  C CG  . LEU A 1 176 ? 17.998  -0.795  11.182  1.00 19.37  ? 205 LEU A CG  1 
ATOM   1391  C CD1 . LEU A 1 176 ? 17.249  -2.068  10.851  1.00 22.00  ? 205 LEU A CD1 1 
ATOM   1392  C CD2 . LEU A 1 176 ? 17.471  -0.215  12.487  1.00 21.58  ? 205 LEU A CD2 1 
ATOM   1393  N N   . ILE A 1 177 ? 20.364  0.288   8.554   1.00 17.01  ? 206 ILE A N   1 
ATOM   1394  C CA  . ILE A 1 177 ? 20.147  1.011   7.318   1.00 20.78  ? 206 ILE A CA  1 
ATOM   1395  C C   . ILE A 1 177 ? 20.442  0.123   6.112   1.00 19.50  ? 206 ILE A C   1 
ATOM   1396  O O   . ILE A 1 177 ? 19.657  0.010   5.195   1.00 20.24  ? 206 ILE A O   1 
ATOM   1397  C CB  . ILE A 1 177 ? 20.996  2.295   7.309   1.00 22.43  ? 206 ILE A CB  1 
ATOM   1398  C CG1 . ILE A 1 177 ? 20.495  3.251   8.398   1.00 24.74  ? 206 ILE A CG1 1 
ATOM   1399  C CG2 . ILE A 1 177 ? 21.008  2.923   5.918   1.00 22.70  ? 206 ILE A CG2 1 
ATOM   1400  C CD1 . ILE A 1 177 ? 21.440  4.384   8.720   1.00 26.51  ? 206 ILE A CD1 1 
ATOM   1401  N N   . ALA A 1 178 ? 21.579  -0.574  6.174   1.00 20.40  ? 207 ALA A N   1 
ATOM   1402  C CA  . ALA A 1 178 ? 21.959  -1.524  5.146   1.00 20.91  ? 207 ALA A CA  1 
ATOM   1403  C C   . ALA A 1 178 ? 20.853  -2.531  4.848   1.00 21.25  ? 207 ALA A C   1 
ATOM   1404  O O   . ALA A 1 178 ? 20.562  -2.768  3.676   1.00 21.52  ? 207 ALA A O   1 
ATOM   1405  C CB  . ALA A 1 178 ? 23.229  -2.211  5.559   1.00 19.57  ? 207 ALA A CB  1 
ATOM   1406  N N   . LYS A 1 179 ? 20.277  -3.125  5.906   1.00 20.09  ? 208 LYS A N   1 
ATOM   1407  C CA  . LYS A 1 179 ? 19.386  -4.276  5.817   1.00 21.21  ? 208 LYS A CA  1 
ATOM   1408  C C   . LYS A 1 179 ? 17.947  -3.884  5.482   1.00 19.89  ? 208 LYS A C   1 
ATOM   1409  O O   . LYS A 1 179 ? 17.116  -4.746  5.187   1.00 21.35  ? 208 LYS A O   1 
ATOM   1410  C CB  . LYS A 1 179 ? 19.327  -4.995  7.170   1.00 21.54  ? 208 LYS A CB  1 
ATOM   1411  C CG  . LYS A 1 179 ? 20.654  -5.563  7.654   1.00 25.85  ? 208 LYS A CG  1 
ATOM   1412  C CD  . LYS A 1 179 ? 20.600  -6.072  9.092   1.00 28.27  ? 208 LYS A CD  1 
ATOM   1413  C CE  . LYS A 1 179 ? 21.829  -6.858  9.486   1.00 29.56  ? 208 LYS A CE  1 
ATOM   1414  N NZ  . LYS A 1 179 ? 23.006  -6.466  8.689   1.00 32.09  ? 208 LYS A NZ  1 
ATOM   1415  N N   . LEU A 1 180 ? 17.610  -2.615  5.700   1.00 18.02  ? 209 LEU A N   1 
ATOM   1416  C CA  . LEU A 1 180 ? 16.207  -2.224  5.674   1.00 21.70  ? 209 LEU A CA  1 
ATOM   1417  C C   . LEU A 1 180 ? 15.574  -2.497  4.314   1.00 20.73  ? 209 LEU A C   1 
ATOM   1418  O O   . LEU A 1 180 ? 14.542  -3.154  4.265   1.00 22.86  ? 209 LEU A O   1 
ATOM   1419  C CB  . LEU A 1 180 ? 16.062  -0.768  6.122   1.00 19.66  ? 209 LEU A CB  1 
ATOM   1420  C CG  . LEU A 1 180 ? 15.778  -0.627  7.614   1.00 19.69  ? 209 LEU A CG  1 
ATOM   1421  C CD1 . LEU A 1 180 ? 15.944  0.820   8.054   1.00 19.59  ? 209 LEU A CD1 1 
ATOM   1422  C CD2 . LEU A 1 180 ? 14.390  -1.138  7.958   1.00 21.73  ? 209 LEU A CD2 1 
ATOM   1423  N N   . PRO A 1 181 ? 16.194  -2.101  3.169   1.00 22.29  ? 210 PRO A N   1 
ATOM   1424  C CA  . PRO A 1 181 ? 15.644  -2.395  1.850   1.00 21.70  ? 210 PRO A CA  1 
ATOM   1425  C C   . PRO A 1 181 ? 15.446  -3.892  1.660   1.00 21.82  ? 210 PRO A C   1 
ATOM   1426  O O   . PRO A 1 181 ? 14.473  -4.279  1.023   1.00 22.37  ? 210 PRO A O   1 
ATOM   1427  C CB  . PRO A 1 181 ? 16.690  -1.844  0.868   1.00 23.28  ? 210 PRO A CB  1 
ATOM   1428  C CG  . PRO A 1 181 ? 17.352  -0.778  1.674   1.00 23.22  ? 210 PRO A CG  1 
ATOM   1429  C CD  . PRO A 1 181 ? 17.454  -1.368  3.069   1.00 20.55  ? 210 PRO A CD  1 
ATOM   1430  N N   . CYS A 1 182 ? 16.320  -4.734  2.254   1.00 23.33  ? 211 CYS A N   1 
ATOM   1431  C CA  . CYS A 1 182 ? 16.088  -6.175  2.173   1.00 21.76  ? 211 CYS A CA  1 
ATOM   1432  C C   . CYS A 1 182 ? 14.808  -6.571  2.909   1.00 21.60  ? 211 CYS A C   1 
ATOM   1433  O O   . CYS A 1 182 ? 14.056  -7.402  2.430   1.00 18.85  ? 211 CYS A O   1 
ATOM   1434  C CB  . CYS A 1 182 ? 17.237  -7.028  2.705   1.00 24.72  ? 211 CYS A CB  1 
ATOM   1435  S SG  . CYS A 1 182 ? 18.797  -6.786  1.813   1.00 26.50  ? 211 CYS A SG  1 
ATOM   1436  N N   . VAL A 1 183 ? 14.565  -6.014  4.100   1.00 20.79  ? 212 VAL A N   1 
ATOM   1437  C CA  . VAL A 1 183 ? 13.328  -6.299  4.815   1.00 18.21  ? 212 VAL A CA  1 
ATOM   1438  C C   . VAL A 1 183 ? 12.140  -5.727  4.032   1.00 17.29  ? 212 VAL A C   1 
ATOM   1439  O O   . VAL A 1 183 ? 11.149  -6.391  3.795   1.00 18.16  ? 212 VAL A O   1 
ATOM   1440  C CB  . VAL A 1 183 ? 13.352  -5.749  6.254   1.00 20.58  ? 212 VAL A CB  1 
ATOM   1441  C CG1 . VAL A 1 183 ? 12.021  -5.983  6.969   1.00 17.94  ? 212 VAL A CG1 1 
ATOM   1442  C CG2 . VAL A 1 183 ? 14.520  -6.318  7.055   1.00 21.83  ? 212 VAL A CG2 1 
ATOM   1443  N N   . ALA A 1 184 ? 12.256  -4.480  3.588   1.00 18.28  ? 213 ALA A N   1 
ATOM   1444  C CA  . ALA A 1 184 ? 11.125  -3.811  2.977   1.00 19.27  ? 213 ALA A CA  1 
ATOM   1445  C C   . ALA A 1 184 ? 10.753  -4.492  1.644   1.00 20.94  ? 213 ALA A C   1 
ATOM   1446  O O   . ALA A 1 184 ? 9.573   -4.589  1.307   1.00 20.15  ? 213 ALA A O   1 
ATOM   1447  C CB  . ALA A 1 184 ? 11.479  -2.346  2.817   1.00 19.88  ? 213 ALA A CB  1 
ATOM   1448  N N   . ALA A 1 185 ? 11.744  -5.026  0.924   1.00 21.74  ? 214 ALA A N   1 
ATOM   1449  C CA  . ALA A 1 185 ? 11.513  -5.620  -0.387  1.00 20.64  ? 214 ALA A CA  1 
ATOM   1450  C C   . ALA A 1 185 ? 10.986  -7.048  -0.239  1.00 22.51  ? 214 ALA A C   1 
ATOM   1451  O O   . ALA A 1 185 ? 10.099  -7.446  -0.980  1.00 25.69  ? 214 ALA A O   1 
ATOM   1452  C CB  . ALA A 1 185 ? 12.764  -5.518  -1.219  1.00 20.54  ? 214 ALA A CB  1 
ATOM   1453  N N   . LYS A 1 186 ? 11.501  -7.812  0.736   1.00 20.42  ? 215 LYS A N   1 
ATOM   1454  C CA  . LYS A 1 186 ? 10.889  -9.078  1.084   1.00 23.08  ? 215 LYS A CA  1 
ATOM   1455  C C   . LYS A 1 186 ? 9.409   -8.880  1.406   1.00 21.06  ? 215 LYS A C   1 
ATOM   1456  O O   . LYS A 1 186 ? 8.612   -9.705  1.009   1.00 25.11  ? 215 LYS A O   1 
ATOM   1457  C CB  . LYS A 1 186 ? 11.653  -9.794  2.212   1.00 25.30  ? 215 LYS A CB  1 
ATOM   1458  C CG  . LYS A 1 186 ? 11.161  -11.204 2.546   1.00 27.80  ? 215 LYS A CG  1 
ATOM   1459  C CD  . LYS A 1 186 ? 12.231  -12.206 3.016   1.00 28.50  ? 215 LYS A CD  1 
ATOM   1460  C CE  . LYS A 1 186 ? 12.372  -13.403 2.099   1.00 29.73  ? 215 LYS A CE  1 
ATOM   1461  N N   . ILE A 1 187 ? 9.008   -7.809  2.121   1.00 19.74  ? 216 ILE A N   1 
ATOM   1462  C CA  . ILE A 1 187 ? 7.603   -7.637  2.459   1.00 21.24  ? 216 ILE A CA  1 
ATOM   1463  C C   . ILE A 1 187 ? 6.803   -7.392  1.179   1.00 20.59  ? 216 ILE A C   1 
ATOM   1464  O O   . ILE A 1 187 ? 5.746   -7.986  1.013   1.00 23.44  ? 216 ILE A O   1 
ATOM   1465  C CB  . ILE A 1 187 ? 7.365   -6.528  3.513   1.00 21.73  ? 216 ILE A CB  1 
ATOM   1466  C CG1 . ILE A 1 187 ? 8.100   -6.826  4.814   1.00 22.20  ? 216 ILE A CG1 1 
ATOM   1467  C CG2 . ILE A 1 187 ? 5.881   -6.299  3.745   1.00 21.80  ? 216 ILE A CG2 1 
ATOM   1468  C CD1 . ILE A 1 187 ? 7.907   -5.794  5.918   1.00 24.61  ? 216 ILE A CD1 1 
ATOM   1469  N N   . TYR A 1 188 ? 7.298   -6.515  0.293   1.00 22.12  ? 217 TYR A N   1 
ATOM   1470  C CA  . TYR A 1 188 ? 6.580   -6.199  -0.942  1.00 23.18  ? 217 TYR A CA  1 
ATOM   1471  C C   . TYR A 1 188 ? 6.375   -7.447  -1.790  1.00 23.24  ? 217 TYR A C   1 
ATOM   1472  O O   . TYR A 1 188 ? 5.259   -7.737  -2.206  1.00 29.30  ? 217 TYR A O   1 
ATOM   1473  C CB  . TYR A 1 188 ? 7.360   -5.180  -1.764  1.00 24.13  ? 217 TYR A CB  1 
ATOM   1474  C CG  . TYR A 1 188 ? 6.637   -4.582  -2.947  1.00 26.65  ? 217 TYR A CG  1 
ATOM   1475  C CD1 . TYR A 1 188 ? 5.583   -3.693  -2.774  1.00 28.99  ? 217 TYR A CD1 1 
ATOM   1476  C CD2 . TYR A 1 188 ? 6.990   -4.912  -4.246  1.00 28.69  ? 217 TYR A CD2 1 
ATOM   1477  C CE1 . TYR A 1 188 ? 4.932   -3.112  -3.856  1.00 28.00  ? 217 TYR A CE1 1 
ATOM   1478  C CE2 . TYR A 1 188 ? 6.363   -4.332  -5.337  1.00 32.13  ? 217 TYR A CE2 1 
ATOM   1479  C CZ  . TYR A 1 188 ? 5.330   -3.428  -5.148  1.00 31.43  ? 217 TYR A CZ  1 
ATOM   1480  O OH  . TYR A 1 188 ? 4.733   -2.901  -6.267  1.00 27.19  ? 217 TYR A OH  1 
ATOM   1481  N N   . ARG A 1 189 ? 7.476   -8.164  -2.036  1.00 26.17  ? 218 ARG A N   1 
ATOM   1482  C CA  . ARG A 1 189 ? 7.474   -9.358  -2.866  1.00 24.45  ? 218 ARG A CA  1 
ATOM   1483  C C   . ARG A 1 189 ? 6.567   -10.414 -2.263  1.00 22.02  ? 218 ARG A C   1 
ATOM   1484  O O   . ARG A 1 189 ? 5.852   -11.070 -3.024  1.00 26.50  ? 218 ARG A O   1 
ATOM   1485  C CB  . ARG A 1 189 ? 8.905   -9.868  -3.086  1.00 26.04  ? 218 ARG A CB  1 
ATOM   1486  C CG  . ARG A 1 189 ? 9.761   -8.875  -3.868  1.00 30.44  ? 218 ARG A CG  1 
ATOM   1487  C CD  . ARG A 1 189 ? 10.323  -9.471  -5.164  1.00 36.75  ? 218 ARG A CD  1 
ATOM   1488  N NE  . ARG A 1 189 ? 11.255  -8.634  -5.918  1.00 42.54  ? 218 ARG A NE  1 
ATOM   1489  C CZ  . ARG A 1 189 ? 11.998  -9.043  -6.956  1.00 47.20  ? 218 ARG A CZ  1 
ATOM   1490  N NH1 . ARG A 1 189 ? 11.914  -10.288 -7.406  1.00 50.09  ? 218 ARG A NH1 1 
ATOM   1491  N NH2 . ARG A 1 189 ? 12.848  -8.203  -7.528  1.00 46.96  ? 218 ARG A NH2 1 
ATOM   1492  N N   . ASN A 1 190 ? 6.586   -10.592 -0.927  1.00 20.24  ? 219 ASN A N   1 
ATOM   1493  C CA  . ASN A 1 190 ? 5.736   -11.588 -0.296  1.00 21.95  ? 219 ASN A CA  1 
ATOM   1494  C C   . ASN A 1 190 ? 4.261   -11.229 -0.456  1.00 23.35  ? 219 ASN A C   1 
ATOM   1495  O O   . ASN A 1 190 ? 3.412   -12.093 -0.673  1.00 27.94  ? 219 ASN A O   1 
ATOM   1496  C CB  . ASN A 1 190 ? 6.095   -11.830 1.173   1.00 24.88  ? 219 ASN A CB  1 
ATOM   1497  C CG  . ASN A 1 190 ? 7.309   -12.729 1.326   1.00 26.96  ? 219 ASN A CG  1 
ATOM   1498  O OD1 . ASN A 1 190 ? 7.828   -13.238 0.335   1.00 28.13  ? 219 ASN A OD1 1 
ATOM   1499  N ND2 . ASN A 1 190 ? 7.799   -12.885 2.539   1.00 27.09  ? 219 ASN A ND2 1 
ATOM   1500  N N   . LEU A 1 191 ? 3.958   -9.946  -0.309  1.00 24.20  ? 220 LEU A N   1 
ATOM   1501  C CA  . LEU A 1 191 ? 2.577   -9.499  -0.291  1.00 24.78  ? 220 LEU A CA  1 
ATOM   1502  C C   . LEU A 1 191 ? 2.028   -9.401  -1.713  1.00 25.50  ? 220 LEU A C   1 
ATOM   1503  O O   . LEU A 1 191 ? 0.894   -9.812  -1.946  1.00 28.45  ? 220 LEU A O   1 
ATOM   1504  C CB  . LEU A 1 191 ? 2.514   -8.139  0.415   1.00 22.46  ? 220 LEU A CB  1 
ATOM   1505  C CG  . LEU A 1 191 ? 2.435   -8.172  1.935   1.00 22.45  ? 220 LEU A CG  1 
ATOM   1506  C CD1 . LEU A 1 191 ? 2.432   -6.764  2.480   1.00 23.23  ? 220 LEU A CD1 1 
ATOM   1507  C CD2 . LEU A 1 191 ? 1.195   -8.881  2.410   1.00 21.78  ? 220 LEU A CD2 1 
ATOM   1508  N N   . TYR A 1 192 ? 2.814   -8.815  -2.628  1.00 27.30  ? 221 TYR A N   1 
ATOM   1509  C CA  . TYR A 1 192 ? 2.317   -8.313  -3.899  1.00 28.83  ? 221 TYR A CA  1 
ATOM   1510  C C   . TYR A 1 192 ? 2.945   -8.974  -5.130  1.00 31.24  ? 221 TYR A C   1 
ATOM   1511  O O   . TYR A 1 192 ? 2.602   -8.588  -6.239  1.00 28.17  ? 221 TYR A O   1 
ATOM   1512  C CB  . TYR A 1 192 ? 2.518   -6.797  -3.945  1.00 27.94  ? 221 TYR A CB  1 
ATOM   1513  C CG  . TYR A 1 192 ? 2.036   -6.091  -2.697  1.00 28.17  ? 221 TYR A CG  1 
ATOM   1514  C CD1 . TYR A 1 192 ? 0.704   -6.150  -2.299  1.00 28.99  ? 221 TYR A CD1 1 
ATOM   1515  C CD2 . TYR A 1 192 ? 2.917   -5.374  -1.900  1.00 26.15  ? 221 TYR A CD2 1 
ATOM   1516  C CE1 . TYR A 1 192 ? 0.256   -5.501  -1.153  1.00 29.69  ? 221 TYR A CE1 1 
ATOM   1517  C CE2 . TYR A 1 192 ? 2.498   -4.766  -0.726  1.00 31.15  ? 221 TYR A CE2 1 
ATOM   1518  C CZ  . TYR A 1 192 ? 1.161   -4.815  -0.358  1.00 30.98  ? 221 TYR A CZ  1 
ATOM   1519  O OH  . TYR A 1 192 ? 0.743   -4.174  0.788   1.00 35.38  ? 221 TYR A OH  1 
ATOM   1520  N N   . ARG A 1 193 ? 3.864   -9.937  -4.959  1.00 32.60  ? 222 ARG A N   1 
ATOM   1521  C CA  . ARG A 1 193 ? 4.427   -10.663 -6.087  1.00 34.62  ? 222 ARG A CA  1 
ATOM   1522  C C   . ARG A 1 193 ? 4.438   -12.164 -5.804  1.00 35.32  ? 222 ARG A C   1 
ATOM   1523  O O   . ARG A 1 193 ? 5.262   -12.885 -6.347  1.00 33.04  ? 222 ARG A O   1 
ATOM   1524  C CB  . ARG A 1 193 ? 5.851   -10.175 -6.388  1.00 36.72  ? 222 ARG A CB  1 
ATOM   1525  C CG  . ARG A 1 193 ? 5.958   -8.716  -6.807  1.00 40.48  ? 222 ARG A CG  1 
ATOM   1526  C CD  . ARG A 1 193 ? 7.088   -8.552  -7.808  1.00 49.53  ? 222 ARG A CD  1 
ATOM   1527  N NE  . ARG A 1 193 ? 7.502   -7.190  -8.132  1.00 57.22  ? 222 ARG A NE  1 
ATOM   1528  C CZ  . ARG A 1 193 ? 6.723   -6.252  -8.673  1.00 55.38  ? 222 ARG A CZ  1 
ATOM   1529  N NH1 . ARG A 1 193 ? 5.408   -6.395  -8.680  1.00 53.63  ? 222 ARG A NH1 1 
ATOM   1530  N NH2 . ARG A 1 193 ? 7.268   -5.149  -9.166  1.00 49.34  ? 222 ARG A NH2 1 
ATOM   1531  N N   . GLU A 1 194 ? 3.520   -12.629 -4.953  1.00 36.77  ? 223 GLU A N   1 
ATOM   1532  C CA  . GLU A 1 194 ? 3.387   -14.043 -4.624  1.00 46.04  ? 223 GLU A CA  1 
ATOM   1533  C C   . GLU A 1 194 ? 4.707   -14.674 -4.162  1.00 41.87  ? 223 GLU A C   1 
ATOM   1534  O O   . GLU A 1 194 ? 4.895   -15.877 -4.307  1.00 43.55  ? 223 GLU A O   1 
ATOM   1535  C CB  . GLU A 1 194 ? 2.825   -14.810 -5.828  1.00 50.54  ? 223 GLU A CB  1 
ATOM   1536  C CG  . GLU A 1 194 ? 1.369   -14.497 -6.151  1.00 55.10  ? 223 GLU A CG  1 
ATOM   1537  C CD  . GLU A 1 194 ? 0.768   -15.471 -7.155  1.00 62.80  ? 223 GLU A CD  1 
ATOM   1538  O OE1 . GLU A 1 194 ? -0.214  -16.175 -6.813  1.00 61.37  ? 223 GLU A OE1 1 
ATOM   1539  O OE2 . GLU A 1 194 ? 1.303   -15.543 -8.280  1.00 74.30  ? 223 GLU A OE2 1 
ATOM   1540  N N   . GLY A 1 195 ? 5.613   -13.874 -3.586  1.00 41.14  ? 224 GLY A N   1 
ATOM   1541  C CA  . GLY A 1 195 ? 6.808   -14.396 -2.945  1.00 42.58  ? 224 GLY A CA  1 
ATOM   1542  C C   . GLY A 1 195 ? 7.968   -14.682 -3.898  1.00 46.96  ? 224 GLY A C   1 
ATOM   1543  O O   . GLY A 1 195 ? 8.751   -15.585 -3.626  1.00 52.67  ? 224 GLY A O   1 
ATOM   1544  N N   . SER A 1 196 ? 8.124   -13.890 -4.967  1.00 51.92  ? 225 SER A N   1 
ATOM   1545  C CA  . SER A 1 196 ? 9.199   -14.104 -5.929  1.00 58.20  ? 225 SER A CA  1 
ATOM   1546  C C   . SER A 1 196 ? 10.532  -13.639 -5.350  1.00 63.74  ? 225 SER A C   1 
ATOM   1547  O O   . SER A 1 196 ? 10.557  -12.783 -4.467  1.00 63.67  ? 225 SER A O   1 
ATOM   1548  C CB  . SER A 1 196 ? 8.926   -13.390 -7.218  1.00 63.86  ? 225 SER A CB  1 
ATOM   1549  O OG  . SER A 1 196 ? 9.267   -12.016 -7.103  1.00 68.50  ? 225 SER A OG  1 
ATOM   1550  N N   . GLY A 1 197 ? 11.632  -14.167 -5.907  1.00 64.87  ? 226 GLY A N   1 
ATOM   1551  C CA  . GLY A 1 197 ? 12.955  -14.053 -5.308  1.00 65.52  ? 226 GLY A CA  1 
ATOM   1552  C C   . GLY A 1 197 ? 13.490  -12.624 -5.313  1.00 65.84  ? 226 GLY A C   1 
ATOM   1553  O O   . GLY A 1 197 ? 13.853  -12.129 -6.376  1.00 65.09  ? 226 GLY A O   1 
ATOM   1554  N N   . ILE A 1 198 ? 13.589  -12.010 -4.112  1.00 73.21  ? 227 ILE A N   1 
ATOM   1555  C CA  . ILE A 1 198 ? 13.836  -10.574 -3.958  1.00 71.01  ? 227 ILE A CA  1 
ATOM   1556  C C   . ILE A 1 198 ? 15.073  -10.185 -4.767  1.00 63.36  ? 227 ILE A C   1 
ATOM   1557  O O   . ILE A 1 198 ? 15.118  -9.112  -5.366  1.00 55.91  ? 227 ILE A O   1 
ATOM   1558  C CB  . ILE A 1 198 ? 13.943  -10.113 -2.477  1.00 68.32  ? 227 ILE A CB  1 
ATOM   1559  C CG1 . ILE A 1 198 ? 15.184  -10.669 -1.767  1.00 76.07  ? 227 ILE A CG1 1 
ATOM   1560  C CG2 . ILE A 1 198 ? 12.670  -10.388 -1.681  1.00 61.72  ? 227 ILE A CG2 1 
ATOM   1561  C CD1 . ILE A 1 198 ? 15.145  -10.562 -0.247  1.00 78.81  ? 227 ILE A CD1 1 
ATOM   1562  N N   . GLY A 1 199 ? 16.071  -11.070 -4.795  1.00 58.06  ? 228 GLY A N   1 
ATOM   1563  C CA  . GLY A 1 199 ? 17.175  -10.899 -5.718  1.00 58.09  ? 228 GLY A CA  1 
ATOM   1564  C C   . GLY A 1 199 ? 18.346  -10.144 -5.096  1.00 52.54  ? 228 GLY A C   1 
ATOM   1565  O O   . GLY A 1 199 ? 18.300  -9.714  -3.945  1.00 45.66  ? 228 GLY A O   1 
ATOM   1566  N N   . ALA A 1 200 ? 19.376  -9.955  -5.920  1.00 48.87  ? 229 ALA A N   1 
ATOM   1567  C CA  . ALA A 1 200 ? 20.721  -9.742  -5.432  1.00 47.82  ? 229 ALA A CA  1 
ATOM   1568  C C   . ALA A 1 200 ? 20.951  -8.279  -5.070  1.00 44.49  ? 229 ALA A C   1 
ATOM   1569  O O   . ALA A 1 200 ? 20.113  -7.416  -5.342  1.00 45.70  ? 229 ALA A O   1 
ATOM   1570  C CB  . ALA A 1 200 ? 21.706  -10.224 -6.468  1.00 50.85  ? 229 ALA A CB  1 
ATOM   1571  N N   . ILE A 1 201 ? 22.085  -8.075  -4.392  1.00 36.27  ? 230 ILE A N   1 
ATOM   1572  C CA  . ILE A 1 201 ? 22.675  -6.787  -4.084  1.00 36.71  ? 230 ILE A CA  1 
ATOM   1573  C C   . ILE A 1 201 ? 23.872  -6.628  -5.013  1.00 33.40  ? 230 ILE A C   1 
ATOM   1574  O O   . ILE A 1 201 ? 24.725  -7.506  -5.077  1.00 31.97  ? 230 ILE A O   1 
ATOM   1575  C CB  . ILE A 1 201 ? 23.119  -6.712  -2.604  1.00 40.17  ? 230 ILE A CB  1 
ATOM   1576  C CG1 . ILE A 1 201 ? 21.980  -6.975  -1.614  1.00 39.74  ? 230 ILE A CG1 1 
ATOM   1577  C CG2 . ILE A 1 201 ? 23.788  -5.382  -2.321  1.00 39.42  ? 230 ILE A CG2 1 
ATOM   1578  C CD1 . ILE A 1 201 ? 20.924  -5.892  -1.596  1.00 44.33  ? 230 ILE A CD1 1 
ATOM   1579  N N   . ASP A 1 202 ? 23.897  -5.538  -5.766  1.00 30.64  ? 231 ASP A N   1 
ATOM   1580  C CA  . ASP A 1 202 ? 25.015  -5.230  -6.636  1.00 35.40  ? 231 ASP A CA  1 
ATOM   1581  C C   . ASP A 1 202 ? 25.939  -4.302  -5.857  1.00 32.44  ? 231 ASP A C   1 
ATOM   1582  O O   . ASP A 1 202 ? 25.578  -3.165  -5.554  1.00 24.39  ? 231 ASP A O   1 
ATOM   1583  C CB  . ASP A 1 202 ? 24.511  -4.642  -7.960  1.00 38.07  ? 231 ASP A CB  1 
ATOM   1584  C CG  . ASP A 1 202 ? 25.583  -4.374  -9.005  1.00 38.56  ? 231 ASP A CG  1 
ATOM   1585  O OD1 . ASP A 1 202 ? 26.743  -4.243  -8.628  1.00 40.72  ? 231 ASP A OD1 1 
ATOM   1586  O OD2 . ASP A 1 202 ? 25.231  -4.285  -10.199 1.00 40.59  ? 231 ASP A OD2 1 
ATOM   1587  N N   . SER A 1 203 ? 27.144  -4.789  -5.545  1.00 31.02  ? 232 SER A N   1 
ATOM   1588  C CA  . SER A 1 203 ? 27.999  -4.077  -4.610  1.00 33.05  ? 232 SER A CA  1 
ATOM   1589  C C   . SER A 1 203 ? 28.518  -2.761  -5.194  1.00 34.39  ? 232 SER A C   1 
ATOM   1590  O O   . SER A 1 203 ? 29.125  -2.006  -4.455  1.00 32.71  ? 232 SER A O   1 
ATOM   1591  C CB  . SER A 1 203 ? 29.134  -4.939  -4.123  1.00 34.53  ? 232 SER A CB  1 
ATOM   1592  O OG  . SER A 1 203 ? 30.088  -5.168  -5.152  1.00 37.95  ? 232 SER A OG  1 
ATOM   1593  N N   . ASN A 1 204 ? 28.271  -2.468  -6.488  1.00 34.24  ? 233 ASN A N   1 
ATOM   1594  C CA  . ASN A 1 204 ? 28.726  -1.217  -7.079  1.00 34.00  ? 233 ASN A CA  1 
ATOM   1595  C C   . ASN A 1 204 ? 27.582  -0.240  -7.346  1.00 36.34  ? 233 ASN A C   1 
ATOM   1596  O O   . ASN A 1 204 ? 27.853  0.888   -7.767  1.00 36.59  ? 233 ASN A O   1 
ATOM   1597  C CB  . ASN A 1 204 ? 29.512  -1.473  -8.362  1.00 36.84  ? 233 ASN A CB  1 
ATOM   1598  C CG  . ASN A 1 204 ? 30.790  -2.225  -8.075  1.00 35.79  ? 233 ASN A CG  1 
ATOM   1599  O OD1 . ASN A 1 204 ? 31.031  -3.295  -8.623  1.00 36.19  ? 233 ASN A OD1 1 
ATOM   1600  N ND2 . ASN A 1 204 ? 31.604  -1.678  -7.191  1.00 41.45  ? 233 ASN A ND2 1 
ATOM   1601  N N   . LEU A 1 205 ? 26.333  -0.679  -7.106  1.00 30.30  ? 234 LEU A N   1 
ATOM   1602  C CA  . LEU A 1 205 ? 25.145  0.155   -7.221  1.00 28.63  ? 234 LEU A CA  1 
ATOM   1603  C C   . LEU A 1 205 ? 24.837  0.838   -5.890  1.00 29.37  ? 234 LEU A C   1 
ATOM   1604  O O   . LEU A 1 205 ? 25.123  0.298   -4.835  1.00 25.92  ? 234 LEU A O   1 
ATOM   1605  C CB  . LEU A 1 205 ? 23.942  -0.718  -7.613  1.00 28.40  ? 234 LEU A CB  1 
ATOM   1606  C CG  . LEU A 1 205 ? 23.883  -1.224  -9.061  1.00 30.34  ? 234 LEU A CG  1 
ATOM   1607  C CD1 . LEU A 1 205 ? 22.598  -2.011  -9.276  1.00 29.33  ? 234 LEU A CD1 1 
ATOM   1608  C CD2 . LEU A 1 205 ? 23.980  -0.091  -10.081 1.00 30.48  ? 234 LEU A CD2 1 
ATOM   1609  N N   . ASP A 1 206 ? 24.183  2.009   -5.962  1.00 27.58  ? 235 ASP A N   1 
ATOM   1610  C CA  . ASP A 1 206 ? 23.791  2.746   -4.770  1.00 25.32  ? 235 ASP A CA  1 
ATOM   1611  C C   . ASP A 1 206 ? 22.581  2.093   -4.079  1.00 23.73  ? 235 ASP A C   1 
ATOM   1612  O O   . ASP A 1 206 ? 21.934  1.165   -4.584  1.00 22.82  ? 235 ASP A O   1 
ATOM   1613  C CB  . ASP A 1 206 ? 23.591  4.223   -5.107  1.00 24.85  ? 235 ASP A CB  1 
ATOM   1614  C CG  . ASP A 1 206 ? 22.519  4.502   -6.147  1.00 30.05  ? 235 ASP A CG  1 
ATOM   1615  O OD1 . ASP A 1 206 ? 22.805  4.302   -7.370  1.00 29.85  ? 235 ASP A OD1 1 
ATOM   1616  O OD2 . ASP A 1 206 ? 21.392  4.921   -5.740  1.00 24.84  ? 235 ASP A OD2 1 
ATOM   1617  N N   . TRP A 1 207 ? 22.356  2.523   -2.828  1.00 22.31  ? 236 TRP A N   1 
ATOM   1618  C CA  . TRP A 1 207 ? 21.404  1.904   -1.918  1.00 22.98  ? 236 TRP A CA  1 
ATOM   1619  C C   . TRP A 1 207 ? 19.976  1.923   -2.492  1.00 23.31  ? 236 TRP A C   1 
ATOM   1620  O O   . TRP A 1 207 ? 19.298  0.895   -2.525  1.00 21.63  ? 236 TRP A O   1 
ATOM   1621  C CB  . TRP A 1 207 ? 21.546  2.649   -0.591  1.00 21.28  ? 236 TRP A CB  1 
ATOM   1622  C CG  . TRP A 1 207 ? 20.737  2.177   0.575   1.00 19.32  ? 236 TRP A CG  1 
ATOM   1623  C CD1 . TRP A 1 207 ? 20.811  0.978   1.214   1.00 20.39  ? 236 TRP A CD1 1 
ATOM   1624  C CD2 . TRP A 1 207 ? 19.785  2.951   1.312   1.00 20.24  ? 236 TRP A CD2 1 
ATOM   1625  N NE1 . TRP A 1 207 ? 20.007  0.965   2.319   1.00 20.78  ? 236 TRP A NE1 1 
ATOM   1626  C CE2 . TRP A 1 207 ? 19.375  2.172   2.414   1.00 19.29  ? 236 TRP A CE2 1 
ATOM   1627  C CE3 . TRP A 1 207 ? 19.267  4.241   1.166   1.00 21.16  ? 236 TRP A CE3 1 
ATOM   1628  C CZ2 . TRP A 1 207 ? 18.365  2.589   3.270   1.00 21.58  ? 236 TRP A CZ2 1 
ATOM   1629  C CZ3 . TRP A 1 207 ? 18.311  4.679   2.049   1.00 19.21  ? 236 TRP A CZ3 1 
ATOM   1630  C CH2 . TRP A 1 207 ? 17.882  3.866   3.101   1.00 20.94  ? 236 TRP A CH2 1 
ATOM   1631  N N   . SER A 1 208 ? 19.552  3.082   -3.020  1.00 24.59  ? 237 SER A N   1 
ATOM   1632  C CA  . SER A 1 208 ? 18.238  3.207   -3.641  1.00 26.26  ? 237 SER A CA  1 
ATOM   1633  C C   . SER A 1 208 ? 18.110  2.283   -4.860  1.00 23.75  ? 237 SER A C   1 
ATOM   1634  O O   . SER A 1 208 ? 17.035  1.751   -5.135  1.00 23.66  ? 237 SER A O   1 
ATOM   1635  C CB  . SER A 1 208 ? 17.960  4.615   -4.097  1.00 25.27  ? 237 SER A CB  1 
ATOM   1636  O OG  . SER A 1 208 ? 18.233  5.568   -3.104  1.00 25.43  ? 237 SER A OG  1 
ATOM   1637  N N   . HIS A 1 209 ? 19.204  2.118   -5.621  1.00 24.76  ? 238 HIS A N   1 
ATOM   1638  C CA  . HIS A 1 209 ? 19.145  1.372   -6.876  1.00 24.96  ? 238 HIS A CA  1 
ATOM   1639  C C   . HIS A 1 209 ? 19.013  -0.121  -6.558  1.00 25.93  ? 238 HIS A C   1 
ATOM   1640  O O   . HIS A 1 209 ? 18.180  -0.811  -7.143  1.00 25.52  ? 238 HIS A O   1 
ATOM   1641  C CB  . HIS A 1 209 ? 20.284  1.796   -7.814  1.00 26.63  ? 238 HIS A CB  1 
ATOM   1642  C CG  . HIS A 1 209 ? 20.222  1.237   -9.200  1.00 26.27  ? 238 HIS A CG  1 
ATOM   1643  N ND1 . HIS A 1 209 ? 21.017  1.769   -10.194 1.00 32.45  ? 238 HIS A ND1 1 
ATOM   1644  C CD2 . HIS A 1 209 ? 19.526  0.255   -9.775  1.00 28.90  ? 238 HIS A CD2 1 
ATOM   1645  C CE1 . HIS A 1 209 ? 20.801  1.124   -11.328 1.00 30.75  ? 238 HIS A CE1 1 
ATOM   1646  N NE2 . HIS A 1 209 ? 19.908  0.187   -11.096 1.00 28.82  ? 238 HIS A NE2 1 
ATOM   1647  N N   . ASN A 1 210 ? 19.745  -0.610  -5.560  1.00 26.58  ? 239 ASN A N   1 
ATOM   1648  C CA  . ASN A 1 210 ? 19.571  -1.987  -5.104  1.00 25.43  ? 239 ASN A CA  1 
ATOM   1649  C C   . ASN A 1 210 ? 18.160  -2.190  -4.554  1.00 25.05  ? 239 ASN A C   1 
ATOM   1650  O O   . ASN A 1 210 ? 17.589  -3.276  -4.702  1.00 22.46  ? 239 ASN A O   1 
ATOM   1651  C CB  . ASN A 1 210 ? 20.619  -2.406  -4.073  1.00 25.49  ? 239 ASN A CB  1 
ATOM   1652  C CG  . ASN A 1 210 ? 21.963  -2.768  -4.670  1.00 27.86  ? 239 ASN A CG  1 
ATOM   1653  O OD1 . ASN A 1 210 ? 22.039  -3.449  -5.693  1.00 26.93  ? 239 ASN A OD1 1 
ATOM   1654  N ND2 . ASN A 1 210 ? 23.030  -2.274  -4.062  1.00 30.20  ? 239 ASN A ND2 1 
ATOM   1655  N N   . PHE A 1 211 ? 17.589  -1.159  -3.915  1.00 22.55  ? 240 PHE A N   1 
ATOM   1656  C CA  . PHE A 1 211 ? 16.227  -1.249  -3.406  1.00 25.21  ? 240 PHE A CA  1 
ATOM   1657  C C   . PHE A 1 211 ? 15.216  -1.366  -4.567  1.00 23.60  ? 240 PHE A C   1 
ATOM   1658  O O   . PHE A 1 211 ? 14.413  -2.292  -4.616  1.00 24.42  ? 240 PHE A O   1 
ATOM   1659  C CB  . PHE A 1 211 ? 15.972  -0.072  -2.443  1.00 22.93  ? 240 PHE A CB  1 
ATOM   1660  C CG  . PHE A 1 211 ? 14.676  -0.144  -1.669  1.00 23.23  ? 240 PHE A CG  1 
ATOM   1661  C CD1 . PHE A 1 211 ? 14.056  -1.353  -1.391  1.00 21.57  ? 240 PHE A CD1 1 
ATOM   1662  C CD2 . PHE A 1 211 ? 14.051  1.012   -1.236  1.00 23.63  ? 240 PHE A CD2 1 
ATOM   1663  C CE1 . PHE A 1 211 ? 12.880  -1.405  -0.672  1.00 22.08  ? 240 PHE A CE1 1 
ATOM   1664  C CE2 . PHE A 1 211 ? 12.849  0.952   -0.552  1.00 23.15  ? 240 PHE A CE2 1 
ATOM   1665  C CZ  . PHE A 1 211 ? 12.262  -0.251  -0.282  1.00 22.29  ? 240 PHE A CZ  1 
ATOM   1666  N N   . THR A 1 212 ? 15.252  -0.462  -5.548  1.00 23.74  ? 241 THR A N   1 
ATOM   1667  C CA  . THR A 1 212 ? 14.305  -0.513  -6.662  1.00 27.16  ? 241 THR A CA  1 
ATOM   1668  C C   . THR A 1 212 ? 14.445  -1.800  -7.491  1.00 27.08  ? 241 THR A C   1 
ATOM   1669  O O   . THR A 1 212 ? 13.437  -2.405  -7.893  1.00 25.52  ? 241 THR A O   1 
ATOM   1670  C CB  . THR A 1 212 ? 14.396  0.743   -7.532  1.00 26.21  ? 241 THR A CB  1 
ATOM   1671  O OG1 . THR A 1 212 ? 15.715  0.797   -8.078  1.00 24.33  ? 241 THR A OG1 1 
ATOM   1672  C CG2 . THR A 1 212 ? 14.056  1.986   -6.736  1.00 25.23  ? 241 THR A CG2 1 
ATOM   1673  N N   . ASN A 1 213 ? 15.684  -2.277  -7.668  1.00 31.10  ? 242 ASN A N   1 
ATOM   1674  C CA  . ASN A 1 213 ? 15.904  -3.593  -8.251  1.00 28.32  ? 242 ASN A CA  1 
ATOM   1675  C C   . ASN A 1 213 ? 15.219  -4.687  -7.440  1.00 26.92  ? 242 ASN A C   1 
ATOM   1676  O O   . ASN A 1 213 ? 14.581  -5.601  -7.985  1.00 26.05  ? 242 ASN A O   1 
ATOM   1677  C CB  . ASN A 1 213 ? 17.388  -3.939  -8.318  1.00 28.99  ? 242 ASN A CB  1 
ATOM   1678  C CG  . ASN A 1 213 ? 18.087  -3.336  -9.513  1.00 35.92  ? 242 ASN A CG  1 
ATOM   1679  O OD1 . ASN A 1 213 ? 17.446  -2.754  -10.384 1.00 40.37  ? 242 ASN A OD1 1 
ATOM   1680  N ND2 . ASN A 1 213 ? 19.398  -3.506  -9.575  1.00 38.09  ? 242 ASN A ND2 1 
ATOM   1681  N N   . MET A 1 214 ? 15.343  -4.618  -6.111  1.00 22.77  ? 243 MET A N   1 
ATOM   1682  C CA  . MET A 1 214 ? 14.806  -5.718  -5.315  1.00 21.62  ? 243 MET A CA  1 
ATOM   1683  C C   . MET A 1 214 ? 13.273  -5.658  -5.277  1.00 22.89  ? 243 MET A C   1 
ATOM   1684  O O   . MET A 1 214 ? 12.604  -6.677  -5.161  1.00 24.74  ? 243 MET A O   1 
ATOM   1685  C CB  . MET A 1 214 ? 15.351  -5.705  -3.881  1.00 21.93  ? 243 MET A CB  1 
ATOM   1686  C CG  . MET A 1 214 ? 16.787  -6.225  -3.756  1.00 23.17  ? 243 MET A CG  1 
ATOM   1687  S SD  . MET A 1 214 ? 17.215  -6.545  -2.019  1.00 26.49  ? 243 MET A SD  1 
ATOM   1688  C CE  . MET A 1 214 ? 17.452  -4.852  -1.487  1.00 22.18  ? 243 MET A CE  1 
ATOM   1689  N N   . LEU A 1 215 ? 12.706  -4.456  -5.344  1.00 21.81  ? 244 LEU A N   1 
ATOM   1690  C CA  . LEU A 1 215 ? 11.260  -4.322  -5.447  1.00 22.90  ? 244 LEU A CA  1 
ATOM   1691  C C   . LEU A 1 215 ? 10.736  -4.905  -6.767  1.00 26.06  ? 244 LEU A C   1 
ATOM   1692  O O   . LEU A 1 215 ? 9.564   -5.275  -6.863  1.00 26.32  ? 244 LEU A O   1 
ATOM   1693  C CB  . LEU A 1 215 ? 10.905  -2.837  -5.330  1.00 23.85  ? 244 LEU A CB  1 
ATOM   1694  C CG  . LEU A 1 215 ? 11.149  -2.202  -3.969  1.00 23.65  ? 244 LEU A CG  1 
ATOM   1695  C CD1 . LEU A 1 215 ? 10.913  -0.698  -3.998  1.00 23.09  ? 244 LEU A CD1 1 
ATOM   1696  C CD2 . LEU A 1 215 ? 10.296  -2.849  -2.934  1.00 23.59  ? 244 LEU A CD2 1 
ATOM   1697  N N   . GLY A 1 216 ? 11.584  -4.964  -7.805  1.00 27.04  ? 245 GLY A N   1 
ATOM   1698  C CA  . GLY A 1 216 ? 11.151  -5.478  -9.093  1.00 28.93  ? 245 GLY A CA  1 
ATOM   1699  C C   . GLY A 1 216 ? 10.837  -4.374  -10.104 1.00 31.19  ? 245 GLY A C   1 
ATOM   1700  O O   . GLY A 1 216 ? 10.127  -4.626  -11.071 1.00 37.89  ? 245 GLY A O   1 
ATOM   1701  N N   . TYR A 1 217 ? 11.363  -3.168  -9.874  1.00 33.13  ? 246 TYR A N   1 
ATOM   1702  C CA  . TYR A 1 217 ? 11.237  -2.054  -10.796 1.00 32.96  ? 246 TYR A CA  1 
ATOM   1703  C C   . TYR A 1 217 ? 12.563  -1.847  -11.529 1.00 39.75  ? 246 TYR A C   1 
ATOM   1704  O O   . TYR A 1 217 ? 13.627  -2.161  -10.988 1.00 42.71  ? 246 TYR A O   1 
ATOM   1705  C CB  . TYR A 1 217 ? 10.797  -0.799  -10.039 1.00 29.98  ? 246 TYR A CB  1 
ATOM   1706  C CG  . TYR A 1 217 ? 9.403   -0.885  -9.473  1.00 28.40  ? 246 TYR A CG  1 
ATOM   1707  C CD1 . TYR A 1 217 ? 9.087   -1.797  -8.477  1.00 25.36  ? 246 TYR A CD1 1 
ATOM   1708  C CD2 . TYR A 1 217 ? 8.381   -0.078  -9.953  1.00 28.58  ? 246 TYR A CD2 1 
ATOM   1709  C CE1 . TYR A 1 217 ? 7.798   -1.915  -7.986  1.00 27.87  ? 246 TYR A CE1 1 
ATOM   1710  C CE2 . TYR A 1 217 ? 7.091   -0.168  -9.457  1.00 26.31  ? 246 TYR A CE2 1 
ATOM   1711  C CZ  . TYR A 1 217 ? 6.795   -1.089  -8.468  1.00 29.42  ? 246 TYR A CZ  1 
ATOM   1712  O OH  . TYR A 1 217 ? 5.528   -1.182  -7.948  1.00 31.35  ? 246 TYR A OH  1 
ATOM   1713  N N   . THR A 1 218 ? 12.492  -1.276  -12.743 1.00 38.41  ? 247 THR A N   1 
ATOM   1714  C CA  . THR A 1 218 ? 13.685  -0.988  -13.529 1.00 46.99  ? 247 THR A CA  1 
ATOM   1715  C C   . THR A 1 218 ? 13.802  0.462   -13.989 1.00 39.19  ? 247 THR A C   1 
ATOM   1716  O O   . THR A 1 218 ? 14.906  0.930   -14.231 1.00 46.40  ? 247 THR A O   1 
ATOM   1717  C CB  . THR A 1 218 ? 13.737  -1.833  -14.801 1.00 50.99  ? 247 THR A CB  1 
ATOM   1718  O OG1 . THR A 1 218 ? 12.373  -2.026  -15.181 1.00 53.12  ? 247 THR A OG1 1 
ATOM   1719  C CG2 . THR A 1 218 ? 14.483  -3.130  -14.580 1.00 57.23  ? 247 THR A CG2 1 
ATOM   1720  N N   . ASP A 1 219 ? 12.682  1.143   -14.201 1.00 40.64  ? 248 ASP A N   1 
ATOM   1721  C CA  . ASP A 1 219 ? 12.742  2.480   -14.756 1.00 37.85  ? 248 ASP A CA  1 
ATOM   1722  C C   . ASP A 1 219 ? 13.768  3.267   -13.943 1.00 36.46  ? 248 ASP A C   1 
ATOM   1723  O O   . ASP A 1 219 ? 13.626  3.469   -12.731 1.00 33.89  ? 248 ASP A O   1 
ATOM   1724  C CB  . ASP A 1 219 ? 11.363  3.138   -14.781 1.00 38.45  ? 248 ASP A CB  1 
ATOM   1725  C CG  . ASP A 1 219 ? 11.246  4.360   -15.681 1.00 44.30  ? 248 ASP A CG  1 
ATOM   1726  O OD1 . ASP A 1 219 ? 12.283  4.826   -16.214 1.00 44.62  ? 248 ASP A OD1 1 
ATOM   1727  O OD2 . ASP A 1 219 ? 10.098  4.839   -15.866 1.00 49.96  ? 248 ASP A OD2 1 
ATOM   1728  N N   . HIS A 1 220 ? 14.834  3.682   -14.619 1.00 31.93  ? 249 HIS A N   1 
ATOM   1729  C CA  . HIS A 1 220 ? 15.778  4.605   -14.029 1.00 29.03  ? 249 HIS A CA  1 
ATOM   1730  C C   . HIS A 1 220 ? 15.066  5.800   -13.392 1.00 30.79  ? 249 HIS A C   1 
ATOM   1731  O O   . HIS A 1 220 ? 15.507  6.296   -12.357 1.00 29.76  ? 249 HIS A O   1 
ATOM   1732  C CB  . HIS A 1 220 ? 16.797  5.043   -15.073 1.00 27.10  ? 249 HIS A CB  1 
ATOM   1733  C CG  . HIS A 1 220 ? 17.534  6.274   -14.725 1.00 24.74  ? 249 HIS A CG  1 
ATOM   1734  N ND1 . HIS A 1 220 ? 17.024  7.528   -14.970 1.00 30.20  ? 249 HIS A ND1 1 
ATOM   1735  C CD2 . HIS A 1 220 ? 18.750  6.461   -14.233 1.00 25.05  ? 249 HIS A CD2 1 
ATOM   1736  C CE1 . HIS A 1 220 ? 17.912  8.442   -14.623 1.00 23.13  ? 249 HIS A CE1 1 
ATOM   1737  N NE2 . HIS A 1 220 ? 18.970  7.815   -14.159 1.00 27.83  ? 249 HIS A NE2 1 
ATOM   1738  N N   . GLN A 1 221 ? 13.985  6.282   -14.018 1.00 28.71  ? 250 GLN A N   1 
ATOM   1739  C CA  . GLN A 1 221 ? 13.261  7.421   -13.456 1.00 34.25  ? 250 GLN A CA  1 
ATOM   1740  C C   . GLN A 1 221 ? 12.602  7.053   -12.123 1.00 28.86  ? 250 GLN A C   1 
ATOM   1741  O O   . GLN A 1 221 ? 12.503  7.907   -11.238 1.00 28.08  ? 250 GLN A O   1 
ATOM   1742  C CB  . GLN A 1 221 ? 12.224  8.007   -14.421 1.00 38.75  ? 250 GLN A CB  1 
ATOM   1743  C CG  . GLN A 1 221 ? 12.781  9.100   -15.322 1.00 43.31  ? 250 GLN A CG  1 
ATOM   1744  C CD  . GLN A 1 221 ? 13.723  10.078  -14.654 1.00 43.02  ? 250 GLN A CD  1 
ATOM   1745  O OE1 . GLN A 1 221 ? 13.349  10.840  -13.760 1.00 37.10  ? 250 GLN A OE1 1 
ATOM   1746  N NE2 . GLN A 1 221 ? 14.959  10.097  -15.128 1.00 44.48  ? 250 GLN A NE2 1 
ATOM   1747  N N   . PHE A 1 222 ? 12.175  5.794   -11.957 1.00 26.10  ? 251 PHE A N   1 
ATOM   1748  C CA  . PHE A 1 222 ? 11.644  5.373   -10.670 1.00 27.11  ? 251 PHE A CA  1 
ATOM   1749  C C   . PHE A 1 222 ? 12.752  5.306   -9.622  1.00 28.37  ? 251 PHE A C   1 
ATOM   1750  O O   . PHE A 1 222 ? 12.510  5.536   -8.422  1.00 26.59  ? 251 PHE A O   1 
ATOM   1751  C CB  . PHE A 1 222 ? 10.931  4.020   -10.731 1.00 25.45  ? 251 PHE A CB  1 
ATOM   1752  C CG  . PHE A 1 222 ? 10.318  3.648   -9.406  1.00 27.16  ? 251 PHE A CG  1 
ATOM   1753  C CD1 . PHE A 1 222 ? 9.331   4.444   -8.848  1.00 27.79  ? 251 PHE A CD1 1 
ATOM   1754  C CD2 . PHE A 1 222 ? 10.754  2.543   -8.689  1.00 26.01  ? 251 PHE A CD2 1 
ATOM   1755  C CE1 . PHE A 1 222 ? 8.779   4.135   -7.615  1.00 25.37  ? 251 PHE A CE1 1 
ATOM   1756  C CE2 . PHE A 1 222 ? 10.198  2.238   -7.457  1.00 26.04  ? 251 PHE A CE2 1 
ATOM   1757  C CZ  . PHE A 1 222 ? 9.197   3.022   -6.935  1.00 26.90  ? 251 PHE A CZ  1 
ATOM   1758  N N   . THR A 1 223 ? 13.958  4.923   -10.070 1.00 27.16  ? 252 THR A N   1 
ATOM   1759  C CA  . THR A 1 223 ? 15.105  4.902   -9.188  1.00 24.43  ? 252 THR A CA  1 
ATOM   1760  C C   . THR A 1 223 ? 15.444  6.328   -8.796  1.00 24.53  ? 252 THR A C   1 
ATOM   1761  O O   . THR A 1 223 ? 15.730  6.554   -7.642  1.00 25.97  ? 252 THR A O   1 
ATOM   1762  C CB  . THR A 1 223 ? 16.308  4.187   -9.817  1.00 24.06  ? 252 THR A CB  1 
ATOM   1763  O OG1 . THR A 1 223 ? 15.779  2.905   -10.135 1.00 23.41  ? 252 THR A OG1 1 
ATOM   1764  C CG2 . THR A 1 223 ? 17.505  4.096   -8.892  1.00 25.62  ? 252 THR A CG2 1 
ATOM   1765  N N   . GLU A 1 224 ? 15.363  7.268   -9.748  1.00 22.27  ? 253 GLU A N   1 
ATOM   1766  C CA  . GLU A 1 224 ? 15.577  8.676   -9.466  1.00 24.47  ? 253 GLU A CA  1 
ATOM   1767  C C   . GLU A 1 224 ? 14.510  9.181   -8.492  1.00 24.82  ? 253 GLU A C   1 
ATOM   1768  O O   . GLU A 1 224 ? 14.862  9.881   -7.543  1.00 23.95  ? 253 GLU A O   1 
ATOM   1769  C CB  . GLU A 1 224 ? 15.629  9.486   -10.768 1.00 27.60  ? 253 GLU A CB  1 
ATOM   1770  C CG  . GLU A 1 224 ? 16.901  9.253   -11.571 1.00 27.30  ? 253 GLU A CG  1 
ATOM   1771  C CD  . GLU A 1 224 ? 18.109  10.020  -11.061 1.00 28.44  ? 253 GLU A CD  1 
ATOM   1772  O OE1 . GLU A 1 224 ? 18.271  11.185  -11.430 1.00 33.60  ? 253 GLU A OE1 1 
ATOM   1773  O OE2 . GLU A 1 224 ? 18.860  9.479   -10.241 1.00 32.41  ? 253 GLU A OE2 1 
ATOM   1774  N N   . LEU A 1 225 ? 13.244  8.772   -8.679  1.00 24.35  ? 254 LEU A N   1 
ATOM   1775  C CA  . LEU A 1 225 ? 12.188  9.122   -7.734  1.00 25.68  ? 254 LEU A CA  1 
ATOM   1776  C C   . LEU A 1 225 ? 12.563  8.633   -6.331  1.00 23.86  ? 254 LEU A C   1 
ATOM   1777  O O   . LEU A 1 225 ? 12.413  9.378   -5.373  1.00 23.91  ? 254 LEU A O   1 
ATOM   1778  C CB  . LEU A 1 225 ? 10.824  8.544   -8.153  1.00 25.98  ? 254 LEU A CB  1 
ATOM   1779  C CG  . LEU A 1 225 ? 9.648   8.888   -7.223  1.00 26.79  ? 254 LEU A CG  1 
ATOM   1780  C CD1 . LEU A 1 225 ? 9.415   10.396  -7.145  1.00 26.04  ? 254 LEU A CD1 1 
ATOM   1781  C CD2 . LEU A 1 225 ? 8.350   8.206   -7.645  1.00 28.20  ? 254 LEU A CD2 1 
ATOM   1782  N N   . THR A 1 226 ? 13.067  7.393   -6.227  1.00 24.30  ? 255 THR A N   1 
ATOM   1783  C CA  . THR A 1 226 ? 13.313  6.744   -4.940  1.00 23.94  ? 255 THR A CA  1 
ATOM   1784  C C   . THR A 1 226 ? 14.488  7.418   -4.220  1.00 22.83  ? 255 THR A C   1 
ATOM   1785  O O   . THR A 1 226 ? 14.469  7.630   -2.999  1.00 21.39  ? 255 THR A O   1 
ATOM   1786  C CB  . THR A 1 226 ? 13.506  5.232   -5.164  1.00 22.29  ? 255 THR A CB  1 
ATOM   1787  O OG1 . THR A 1 226 ? 12.268  4.713   -5.643  1.00 23.51  ? 255 THR A OG1 1 
ATOM   1788  C CG2 . THR A 1 226 ? 13.907  4.464   -3.923  1.00 25.69  ? 255 THR A CG2 1 
ATOM   1789  N N   . ARG A 1 227 ? 15.520  7.769   -4.996  1.00 20.37  ? 256 ARG A N   1 
ATOM   1790  C CA  . ARG A 1 227 ? 16.611  8.597   -4.518  1.00 21.97  ? 256 ARG A CA  1 
ATOM   1791  C C   . ARG A 1 227 ? 16.090  9.888   -3.883  1.00 24.74  ? 256 ARG A C   1 
ATOM   1792  O O   . ARG A 1 227 ? 16.441  10.176  -2.758  1.00 24.59  ? 256 ARG A O   1 
ATOM   1793  C CB  . ARG A 1 227 ? 17.583  8.924   -5.653  1.00 22.46  ? 256 ARG A CB  1 
ATOM   1794  C CG  . ARG A 1 227 ? 18.270  7.682   -6.204  1.00 23.76  ? 256 ARG A CG  1 
ATOM   1795  C CD  . ARG A 1 227 ? 19.159  8.000   -7.396  1.00 24.92  ? 256 ARG A CD  1 
ATOM   1796  N NE  . ARG A 1 227 ? 19.918  6.786   -7.672  1.00 25.91  ? 256 ARG A NE  1 
ATOM   1797  C CZ  . ARG A 1 227 ? 20.127  6.261   -8.870  1.00 24.63  ? 256 ARG A CZ  1 
ATOM   1798  N NH1 . ARG A 1 227 ? 19.607  6.809   -9.950  1.00 24.36  ? 256 ARG A NH1 1 
ATOM   1799  N NH2 . ARG A 1 227 ? 20.891  5.191   -8.980  1.00 26.01  ? 256 ARG A NH2 1 
ATOM   1800  N N   . LEU A 1 228 ? 15.263  10.655  -4.596  1.00 24.37  ? 257 LEU A N   1 
ATOM   1801  C CA  . LEU A 1 228 ? 14.707  11.880  -4.032  1.00 25.56  ? 257 LEU A CA  1 
ATOM   1802  C C   . LEU A 1 228 ? 13.836  11.544  -2.823  1.00 21.19  ? 257 LEU A C   1 
ATOM   1803  O O   . LEU A 1 228 ? 14.008  12.157  -1.785  1.00 23.80  ? 257 LEU A O   1 
ATOM   1804  C CB  . LEU A 1 228 ? 13.908  12.644  -5.100  1.00 25.95  ? 257 LEU A CB  1 
ATOM   1805  C CG  . LEU A 1 228 ? 13.362  14.021  -4.712  1.00 26.89  ? 257 LEU A CG  1 
ATOM   1806  C CD1 . LEU A 1 228 ? 14.471  15.014  -4.399  1.00 27.90  ? 257 LEU A CD1 1 
ATOM   1807  C CD2 . LEU A 1 228 ? 12.488  14.569  -5.829  1.00 27.14  ? 257 LEU A CD2 1 
ATOM   1808  N N   . TYR A 1 229 ? 12.933  10.563  -2.947  1.00 20.07  ? 258 TYR A N   1 
ATOM   1809  C CA  . TYR A 1 229 ? 11.971  10.250  -1.902  1.00 20.70  ? 258 TYR A CA  1 
ATOM   1810  C C   . TYR A 1 229 ? 12.674  9.851   -0.601  1.00 18.65  ? 258 TYR A C   1 
ATOM   1811  O O   . TYR A 1 229 ? 12.245  10.222  0.488   1.00 18.00  ? 258 TYR A O   1 
ATOM   1812  C CB  . TYR A 1 229 ? 11.033  9.117   -2.329  1.00 21.20  ? 258 TYR A CB  1 
ATOM   1813  C CG  . TYR A 1 229 ? 9.985   8.697   -1.317  1.00 24.40  ? 258 TYR A CG  1 
ATOM   1814  C CD1 . TYR A 1 229 ? 10.311  7.925   -0.217  1.00 27.94  ? 258 TYR A CD1 1 
ATOM   1815  C CD2 . TYR A 1 229 ? 8.654   9.036   -1.473  1.00 29.62  ? 258 TYR A CD2 1 
ATOM   1816  C CE1 . TYR A 1 229 ? 9.362   7.524   0.714   1.00 28.99  ? 258 TYR A CE1 1 
ATOM   1817  C CE2 . TYR A 1 229 ? 7.684   8.629   -0.567  1.00 31.02  ? 258 TYR A CE2 1 
ATOM   1818  C CZ  . TYR A 1 229 ? 8.035   7.862   0.532   1.00 30.18  ? 258 TYR A CZ  1 
ATOM   1819  O OH  . TYR A 1 229 ? 7.101   7.442   1.465   1.00 33.38  ? 258 TYR A OH  1 
ATOM   1820  N N   . LEU A 1 230 ? 13.717  9.013   -0.703  1.00 20.02  ? 259 LEU A N   1 
ATOM   1821  C CA  . LEU A 1 230 ? 14.404  8.524   0.477   1.00 21.34  ? 259 LEU A CA  1 
ATOM   1822  C C   . LEU A 1 230 ? 15.214  9.658   1.091   1.00 22.82  ? 259 LEU A C   1 
ATOM   1823  O O   . LEU A 1 230 ? 15.397  9.723   2.310   1.00 23.19  ? 259 LEU A O   1 
ATOM   1824  C CB  . LEU A 1 230 ? 15.278  7.324   0.094   1.00 20.05  ? 259 LEU A CB  1 
ATOM   1825  C CG  . LEU A 1 230 ? 14.481  6.073   -0.229  1.00 22.28  ? 259 LEU A CG  1 
ATOM   1826  C CD1 . LEU A 1 230 ? 15.402  4.919   -0.626  1.00 23.67  ? 259 LEU A CD1 1 
ATOM   1827  C CD2 . LEU A 1 230 ? 13.618  5.684   0.956   1.00 22.53  ? 259 LEU A CD2 1 
ATOM   1828  N N   . THR A 1 231 ? 15.632  10.586  0.234   1.00 23.44  ? 260 THR A N   1 
ATOM   1829  C CA  . THR A 1 231 ? 16.405  11.725  0.669   1.00 21.82  ? 260 THR A CA  1 
ATOM   1830  C C   . THR A 1 231 ? 15.539  12.691  1.470   1.00 20.00  ? 260 THR A C   1 
ATOM   1831  O O   . THR A 1 231 ? 15.887  13.031  2.593   1.00 19.58  ? 260 THR A O   1 
ATOM   1832  C CB  . THR A 1 231 ? 17.049  12.438  -0.520  1.00 20.07  ? 260 THR A CB  1 
ATOM   1833  O OG1 . THR A 1 231 ? 18.117  11.590  -0.901  1.00 21.05  ? 260 THR A OG1 1 
ATOM   1834  C CG2 . THR A 1 231 ? 17.562  13.824  -0.189  1.00 18.78  ? 260 THR A CG2 1 
ATOM   1835  N N   . ILE A 1 232 ? 14.372  13.041  0.930   1.00 17.45  ? 261 ILE A N   1 
ATOM   1836  C CA  . ILE A 1 232 ? 13.587  14.118  1.513   1.00 18.49  ? 261 ILE A CA  1 
ATOM   1837  C C   . ILE A 1 232 ? 12.736  13.660  2.701   1.00 18.67  ? 261 ILE A C   1 
ATOM   1838  O O   . ILE A 1 232 ? 12.374  14.473  3.529   1.00 20.67  ? 261 ILE A O   1 
ATOM   1839  C CB  . ILE A 1 232 ? 12.721  14.782  0.431   1.00 20.32  ? 261 ILE A CB  1 
ATOM   1840  C CG1 . ILE A 1 232 ? 11.621  13.833  -0.034  1.00 20.29  ? 261 ILE A CG1 1 
ATOM   1841  C CG2 . ILE A 1 232 ? 13.593  15.311  -0.691  1.00 20.61  ? 261 ILE A CG2 1 
ATOM   1842  C CD1 . ILE A 1 232 ? 10.779  14.331  -1.184  1.00 22.49  ? 261 ILE A CD1 1 
ATOM   1843  N N   . HIS A 1 233 ? 12.409  12.371  2.826   1.00 17.86  ? 262 HIS A N   1 
ATOM   1844  C CA  . HIS A 1 233 ? 11.651  11.925  4.001   1.00 19.34  ? 262 HIS A CA  1 
ATOM   1845  C C   . HIS A 1 233 ? 12.552  11.461  5.160   1.00 18.04  ? 262 HIS A C   1 
ATOM   1846  O O   . HIS A 1 233 ? 12.059  10.910  6.166   1.00 17.53  ? 262 HIS A O   1 
ATOM   1847  C CB  . HIS A 1 233 ? 10.677  10.789  3.662   1.00 20.50  ? 262 HIS A CB  1 
ATOM   1848  C CG  . HIS A 1 233 ? 9.521   11.099  2.750   1.00 23.88  ? 262 HIS A CG  1 
ATOM   1849  N ND1 . HIS A 1 233 ? 9.628   11.206  1.376   1.00 22.64  ? 262 HIS A ND1 1 
ATOM   1850  C CD2 . HIS A 1 233 ? 8.204   11.207  3.027   1.00 24.64  ? 262 HIS A CD2 1 
ATOM   1851  C CE1 . HIS A 1 233 ? 8.421   11.417  0.868   1.00 24.49  ? 262 HIS A CE1 1 
ATOM   1852  N NE2 . HIS A 1 233 ? 7.549   11.426  1.861   1.00 22.38  ? 262 HIS A NE2 1 
ATOM   1853  N N   . SER A 1 234 ? 13.843  11.782  5.066   1.00 17.88  ? 263 SER A N   1 
ATOM   1854  C CA  . SER A 1 234 ? 14.899  11.236  5.905   1.00 18.07  ? 263 SER A CA  1 
ATOM   1855  C C   . SER A 1 234 ? 14.764  11.673  7.361   1.00 19.28  ? 263 SER A C   1 
ATOM   1856  O O   . SER A 1 234 ? 14.999  10.887  8.252   1.00 18.96  ? 263 SER A O   1 
ATOM   1857  C CB  . SER A 1 234 ? 16.222  11.612  5.390   1.00 15.97  ? 263 SER A CB  1 
ATOM   1858  O OG  . SER A 1 234 ? 16.431  13.035  5.471   1.00 15.75  ? 263 SER A OG  1 
ATOM   1859  N N   . ASP A 1 235 ? 14.453  12.955  7.566   1.00 19.98  ? 264 ASP A N   1 
ATOM   1860  C CA  . ASP A 1 235 ? 14.442  13.543  8.893   1.00 20.87  ? 264 ASP A CA  1 
ATOM   1861  C C   . ASP A 1 235 ? 13.492  14.732  8.861   1.00 21.57  ? 264 ASP A C   1 
ATOM   1862  O O   . ASP A 1 235 ? 13.416  15.425  7.849   1.00 22.29  ? 264 ASP A O   1 
ATOM   1863  C CB  . ASP A 1 235 ? 15.868  13.973  9.259   1.00 22.78  ? 264 ASP A CB  1 
ATOM   1864  C CG  . ASP A 1 235 ? 16.199  13.928  10.738  1.00 23.88  ? 264 ASP A CG  1 
ATOM   1865  O OD1 . ASP A 1 235 ? 15.738  12.979  11.411  1.00 24.82  ? 264 ASP A OD1 1 
ATOM   1866  O OD2 . ASP A 1 235 ? 16.923  14.824  11.192  1.00 26.30  ? 264 ASP A OD2 1 
ATOM   1867  N N   . HIS A 1 236 ? 12.804  14.986  9.974   1.00 21.07  ? 265 HIS A N   1 
ATOM   1868  C CA  . HIS A 1 236 ? 12.003  16.198  10.090  1.00 21.61  ? 265 HIS A CA  1 
ATOM   1869  C C   . HIS A 1 236 ? 12.031  16.724  11.532  1.00 19.81  ? 265 HIS A C   1 
ATOM   1870  O O   . HIS A 1 236 ? 10.967  16.853  12.133  1.00 20.42  ? 265 HIS A O   1 
ATOM   1871  C CB  . HIS A 1 236 ? 10.589  15.919  9.569   1.00 20.93  ? 265 HIS A CB  1 
ATOM   1872  C CG  . HIS A 1 236 ? 9.889   17.114  8.995   1.00 23.15  ? 265 HIS A CG  1 
ATOM   1873  N ND1 . HIS A 1 236 ? 10.321  17.733  7.838   1.00 24.81  ? 265 HIS A ND1 1 
ATOM   1874  C CD2 . HIS A 1 236 ? 8.767   17.748  9.349   1.00 22.65  ? 265 HIS A CD2 1 
ATOM   1875  C CE1 . HIS A 1 236 ? 9.527   18.761  7.568   1.00 22.63  ? 265 HIS A CE1 1 
ATOM   1876  N NE2 . HIS A 1 236 ? 8.596   18.801  8.462   1.00 26.48  ? 265 HIS A NE2 1 
ATOM   1877  N N   . GLU A 1 237 ? 13.241  17.079  12.013  1.00 19.25  ? 266 GLU A N   1 
ATOM   1878  C CA  . GLU A 1 237 ? 13.570  17.440  13.387  1.00 20.09  ? 266 GLU A CA  1 
ATOM   1879  C C   . GLU A 1 237 ? 13.068  16.381  14.370  1.00 19.12  ? 266 GLU A C   1 
ATOM   1880  O O   . GLU A 1 237 ? 12.784  15.245  13.985  1.00 17.97  ? 266 GLU A O   1 
ATOM   1881  C CB  . GLU A 1 237 ? 13.162  18.886  13.707  1.00 21.39  ? 266 GLU A CB  1 
ATOM   1882  C CG  . GLU A 1 237 ? 11.717  19.110  14.102  1.00 21.26  ? 266 GLU A CG  1 
ATOM   1883  C CD  . GLU A 1 237 ? 11.462  20.472  14.751  1.00 25.51  ? 266 GLU A CD  1 
ATOM   1884  O OE1 . GLU A 1 237 ? 12.205  21.449  14.444  1.00 26.00  ? 266 GLU A OE1 1 
ATOM   1885  O OE2 . GLU A 1 237 ? 10.549  20.544  15.622  1.00 24.80  ? 266 GLU A OE2 1 
ATOM   1886  N N   . GLY A 1 238 ? 13.098  16.717  15.658  1.00 20.27  ? 267 GLY A N   1 
ATOM   1887  C CA  . GLY A 1 238 ? 13.083  15.701  16.697  1.00 20.84  ? 267 GLY A CA  1 
ATOM   1888  C C   . GLY A 1 238 ? 11.704  15.459  17.280  1.00 22.35  ? 267 GLY A C   1 
ATOM   1889  O O   . GLY A 1 238 ? 11.526  14.519  18.043  1.00 20.71  ? 267 GLY A O   1 
ATOM   1890  N N   . GLY A 1 239 ? 10.739  16.311  16.900  1.00 21.50  ? 268 GLY A N   1 
ATOM   1891  C CA  . GLY A 1 239 ? 9.467   16.348  17.578  1.00 20.70  ? 268 GLY A CA  1 
ATOM   1892  C C   . GLY A 1 239 ? 8.371   15.529  16.911  1.00 18.62  ? 268 GLY A C   1 
ATOM   1893  O O   . GLY A 1 239 ? 7.371   15.325  17.560  1.00 19.56  ? 268 GLY A O   1 
ATOM   1894  N N   . ASN A 1 240 ? 8.527   15.121  15.629  1.00 17.93  ? 269 ASN A N   1 
ATOM   1895  C CA  . ASN A 1 240 ? 7.554   14.270  14.960  1.00 15.49  ? 269 ASN A CA  1 
ATOM   1896  C C   . ASN A 1 240 ? 7.518   12.924  15.681  1.00 17.81  ? 269 ASN A C   1 
ATOM   1897  O O   . ASN A 1 240 ? 8.485   12.543  16.345  1.00 19.60  ? 269 ASN A O   1 
ATOM   1898  C CB  . ASN A 1 240 ? 7.821   14.102  13.457  1.00 15.27  ? 269 ASN A CB  1 
ATOM   1899  C CG  . ASN A 1 240 ? 9.094   13.333  13.199  1.00 16.06  ? 269 ASN A CG  1 
ATOM   1900  O OD1 . ASN A 1 240 ? 9.065   12.109  13.280  1.00 17.12  ? 269 ASN A OD1 1 
ATOM   1901  N ND2 . ASN A 1 240 ? 10.174  14.015  12.856  1.00 17.85  ? 269 ASN A ND2 1 
ATOM   1902  N N   . VAL A 1 241 ? 6.378   12.246  15.586  1.00 17.70  ? 270 VAL A N   1 
ATOM   1903  C CA  . VAL A 1 241 ? 6.142   11.068  16.404  1.00 19.70  ? 270 VAL A CA  1 
ATOM   1904  C C   . VAL A 1 241 ? 7.251   10.021  16.247  1.00 20.00  ? 270 VAL A C   1 
ATOM   1905  O O   . VAL A 1 241 ? 7.730   9.473   17.234  1.00 21.24  ? 270 VAL A O   1 
ATOM   1906  C CB  . VAL A 1 241 ? 4.737   10.489  16.162  1.00 19.98  ? 270 VAL A CB  1 
ATOM   1907  C CG1 . VAL A 1 241 ? 4.588   9.108   16.780  1.00 21.75  ? 270 VAL A CG1 1 
ATOM   1908  C CG2 . VAL A 1 241 ? 3.653   11.402  16.705  1.00 22.59  ? 270 VAL A CG2 1 
ATOM   1909  N N   . SER A 1 242 ? 7.620   9.697   15.008  1.00 16.40  ? 271 SER A N   1 
ATOM   1910  C CA  . SER A 1 242 ? 8.562   8.621   14.747  1.00 16.11  ? 271 SER A CA  1 
ATOM   1911  C C   . SER A 1 242 ? 9.948   9.011   15.271  1.00 16.75  ? 271 SER A C   1 
ATOM   1912  O O   . SER A 1 242 ? 10.636  8.206   15.886  1.00 19.05  ? 271 SER A O   1 
ATOM   1913  C CB  . SER A 1 242 ? 8.570   8.239   13.254  1.00 15.16  ? 271 SER A CB  1 
ATOM   1914  O OG  . SER A 1 242 ? 8.879   9.337   12.384  1.00 16.56  ? 271 SER A OG  1 
ATOM   1915  N N   . ALA A 1 243 ? 10.393  10.250  15.024  1.00 15.96  ? 272 ALA A N   1 
ATOM   1916  C CA  . ALA A 1 243 ? 11.711  10.671  15.479  1.00 16.59  ? 272 ALA A CA  1 
ATOM   1917  C C   . ALA A 1 243 ? 11.733  10.660  17.009  1.00 16.00  ? 272 ALA A C   1 
ATOM   1918  O O   . ALA A 1 243 ? 12.639  10.142  17.629  1.00 17.45  ? 272 ALA A O   1 
ATOM   1919  C CB  . ALA A 1 243 ? 12.011  12.043  14.944  1.00 15.82  ? 272 ALA A CB  1 
ATOM   1920  N N   . HIS A 1 244 ? 10.688  11.221  17.625  1.00 15.11  ? 273 HIS A N   1 
ATOM   1921  C CA  . HIS A 1 244 ? 10.590  11.344  19.059  1.00 15.86  ? 273 HIS A CA  1 
ATOM   1922  C C   . HIS A 1 244 ? 10.576  9.967   19.725  1.00 15.54  ? 273 HIS A C   1 
ATOM   1923  O O   . HIS A 1 244 ? 11.235  9.774   20.755  1.00 17.17  ? 273 HIS A O   1 
ATOM   1924  C CB  . HIS A 1 244 ? 9.339   12.181  19.391  1.00 17.68  ? 273 HIS A CB  1 
ATOM   1925  C CG  . HIS A 1 244 ? 9.253   12.507  20.845  1.00 18.82  ? 273 HIS A CG  1 
ATOM   1926  N ND1 . HIS A 1 244 ? 8.155   13.093  21.435  1.00 20.06  ? 273 HIS A ND1 1 
ATOM   1927  C CD2 . HIS A 1 244 ? 10.155  12.344  21.822  1.00 20.78  ? 273 HIS A CD2 1 
ATOM   1928  C CE1 . HIS A 1 244 ? 8.389   13.253  22.731  1.00 20.35  ? 273 HIS A CE1 1 
ATOM   1929  N NE2 . HIS A 1 244 ? 9.613   12.836  22.976  1.00 20.62  ? 273 HIS A NE2 1 
ATOM   1930  N N   . THR A 1 245 ? 9.799   9.046   19.146  1.00 14.57  ? 274 THR A N   1 
ATOM   1931  C CA  . THR A 1 245 ? 9.721   7.673   19.613  1.00 15.39  ? 274 THR A CA  1 
ATOM   1932  C C   . THR A 1 245 ? 11.122  7.068   19.662  1.00 16.95  ? 274 THR A C   1 
ATOM   1933  O O   . THR A 1 245 ? 11.523  6.459   20.686  1.00 14.92  ? 274 THR A O   1 
ATOM   1934  C CB  . THR A 1 245 ? 8.716   6.874   18.788  1.00 13.70  ? 274 THR A CB  1 
ATOM   1935  O OG1 . THR A 1 245 ? 7.417   7.457   18.965  1.00 14.96  ? 274 THR A OG1 1 
ATOM   1936  C CG2 . THR A 1 245 ? 8.627   5.416   19.195  1.00 13.67  ? 274 THR A CG2 1 
ATOM   1937  N N   . SER A 1 246 ? 11.832  7.185   18.523  1.00 16.13  ? 275 SER A N   1 
ATOM   1938  C CA  . SER A 1 246 ? 13.169  6.611   18.450  1.00 18.02  ? 275 SER A CA  1 
ATOM   1939  C C   . SER A 1 246 ? 14.072  7.230   19.535  1.00 17.48  ? 275 SER A C   1 
ATOM   1940  O O   . SER A 1 246 ? 14.886  6.556   20.157  1.00 19.99  ? 275 SER A O   1 
ATOM   1941  C CB  . SER A 1 246 ? 13.746  6.780   17.060  1.00 16.83  ? 275 SER A CB  1 
ATOM   1942  O OG  . SER A 1 246 ? 14.037  8.173   16.854  1.00 18.52  ? 275 SER A OG  1 
ATOM   1943  N N   . HIS A 1 247 ? 13.959  8.552   19.789  1.00 16.47  ? 276 HIS A N   1 
ATOM   1944  C CA  . HIS A 1 247 ? 14.787  9.242   20.751  1.00 17.28  ? 276 HIS A CA  1 
ATOM   1945  C C   . HIS A 1 247 ? 14.478  8.797   22.191  1.00 16.07  ? 276 HIS A C   1 
ATOM   1946  O O   . HIS A 1 247 ? 15.355  8.481   22.979  1.00 16.23  ? 276 HIS A O   1 
ATOM   1947  C CB  . HIS A 1 247 ? 14.513  10.733  20.528  1.00 17.69  ? 276 HIS A CB  1 
ATOM   1948  C CG  . HIS A 1 247 ? 15.360  11.658  21.272  1.00 21.04  ? 276 HIS A CG  1 
ATOM   1949  N ND1 . HIS A 1 247 ? 14.943  12.272  22.435  1.00 24.16  ? 276 HIS A ND1 1 
ATOM   1950  C CD2 . HIS A 1 247 ? 16.603  12.088  21.037  1.00 21.65  ? 276 HIS A CD2 1 
ATOM   1951  C CE1 . HIS A 1 247 ? 15.918  13.070  22.849  1.00 22.99  ? 276 HIS A CE1 1 
ATOM   1952  N NE2 . HIS A 1 247 ? 16.920  12.971  22.018  1.00 26.79  ? 276 HIS A NE2 1 
ATOM   1953  N N   . LEU A 1 248 ? 13.186  8.674   22.484  1.00 16.16  ? 277 LEU A N   1 
ATOM   1954  C CA  . LEU A 1 248 ? 12.682  8.338   23.792  1.00 17.36  ? 277 LEU A CA  1 
ATOM   1955  C C   . LEU A 1 248 ? 13.075  6.903   24.147  1.00 16.25  ? 277 LEU A C   1 
ATOM   1956  O O   . LEU A 1 248 ? 13.620  6.657   25.216  1.00 17.54  ? 277 LEU A O   1 
ATOM   1957  C CB  . LEU A 1 248 ? 11.165  8.524   23.730  1.00 19.28  ? 277 LEU A CB  1 
ATOM   1958  C CG  . LEU A 1 248 ? 10.368  7.946   24.893  1.00 22.26  ? 277 LEU A CG  1 
ATOM   1959  C CD1 . LEU A 1 248 ? 10.885  8.489   26.233  1.00 24.95  ? 277 LEU A CD1 1 
ATOM   1960  C CD2 . LEU A 1 248 ? 8.880   8.259   24.699  1.00 21.92  ? 277 LEU A CD2 1 
ATOM   1961  N N   . VAL A 1 249 ? 12.794  5.984   23.232  1.00 16.14  ? 278 VAL A N   1 
ATOM   1962  C CA  . VAL A 1 249 ? 13.172  4.604   23.447  1.00 14.53  ? 278 VAL A CA  1 
ATOM   1963  C C   . VAL A 1 249 ? 14.692  4.491   23.483  1.00 15.62  ? 278 VAL A C   1 
ATOM   1964  O O   . VAL A 1 249 ? 15.250  3.814   24.369  1.00 16.46  ? 278 VAL A O   1 
ATOM   1965  C CB  . VAL A 1 249 ? 12.511  3.663   22.445  1.00 13.97  ? 278 VAL A CB  1 
ATOM   1966  C CG1 . VAL A 1 249 ? 13.067  2.226   22.565  1.00 13.76  ? 278 VAL A CG1 1 
ATOM   1967  C CG2 . VAL A 1 249 ? 10.986  3.679   22.553  1.00 14.93  ? 278 VAL A CG2 1 
ATOM   1968  N N   . GLY A 1 250 ? 15.398  5.144   22.544  1.00 13.26  ? 279 GLY A N   1 
ATOM   1969  C CA  . GLY A 1 250 ? 16.860  5.097   22.572  1.00 14.80  ? 279 GLY A CA  1 
ATOM   1970  C C   . GLY A 1 250 ? 17.552  5.596   23.854  1.00 15.20  ? 279 GLY A C   1 
ATOM   1971  O O   . GLY A 1 250 ? 18.657  5.166   24.190  1.00 16.02  ? 279 GLY A O   1 
ATOM   1972  N N   . SER A 1 251 ? 16.959  6.582   24.537  1.00 15.21  ? 280 SER A N   1 
ATOM   1973  C CA  . SER A 1 251 ? 17.477  7.194   25.733  1.00 17.52  ? 280 SER A CA  1 
ATOM   1974  C C   . SER A 1 251 ? 17.504  6.232   26.931  1.00 17.31  ? 280 SER A C   1 
ATOM   1975  O O   . SER A 1 251 ? 18.162  6.551   27.912  1.00 20.30  ? 280 SER A O   1 
ATOM   1976  C CB  . SER A 1 251 ? 16.702  8.455   26.052  1.00 17.29  ? 280 SER A CB  1 
ATOM   1977  O OG  . SER A 1 251 ? 15.430  8.141   26.612  1.00 19.41  ? 280 SER A OG  1 
ATOM   1978  N N   . ALA A 1 252 ? 16.783  5.093   26.860  1.00 16.57  ? 281 ALA A N   1 
ATOM   1979  C CA  . ALA A 1 252 ? 16.868  4.047   27.864  1.00 18.51  ? 281 ALA A CA  1 
ATOM   1980  C C   . ALA A 1 252 ? 17.959  3.037   27.481  1.00 18.54  ? 281 ALA A C   1 
ATOM   1981  O O   . ALA A 1 252 ? 18.057  1.995   28.119  1.00 17.47  ? 281 ALA A O   1 
ATOM   1982  C CB  . ALA A 1 252 ? 15.564  3.324   28.030  1.00 18.45  ? 281 ALA A CB  1 
ATOM   1983  N N   . LEU A 1 253 ? 18.654  3.300   26.369  1.00 18.69  ? 282 LEU A N   1 
ATOM   1984  C CA  . LEU A 1 253 ? 19.763  2.487   25.875  1.00 19.35  ? 282 LEU A CA  1 
ATOM   1985  C C   . LEU A 1 253 ? 19.223  1.183   25.293  1.00 19.80  ? 282 LEU A C   1 
ATOM   1986  O O   . LEU A 1 253 ? 19.937  0.187   25.154  1.00 23.01  ? 282 LEU A O   1 
ATOM   1987  C CB  . LEU A 1 253 ? 20.818  2.242   26.964  1.00 19.41  ? 282 LEU A CB  1 
ATOM   1988  C CG  . LEU A 1 253 ? 21.414  3.478   27.630  1.00 20.82  ? 282 LEU A CG  1 
ATOM   1989  C CD1 . LEU A 1 253 ? 22.545  3.121   28.592  1.00 21.14  ? 282 LEU A CD1 1 
ATOM   1990  C CD2 . LEU A 1 253 ? 21.869  4.471   26.593  1.00 21.31  ? 282 LEU A CD2 1 
ATOM   1991  N N   . SER A 1 254 ? 17.967  1.202   24.831  1.00 19.10  ? 283 SER A N   1 
ATOM   1992  C CA  . SER A 1 254 ? 17.539  0.207   23.873  1.00 19.53  ? 283 SER A CA  1 
ATOM   1993  C C   . SER A 1 254 ? 18.315  0.410   22.567  1.00 19.53  ? 283 SER A C   1 
ATOM   1994  O O   . SER A 1 254 ? 18.673  1.526   22.169  1.00 20.28  ? 283 SER A O   1 
ATOM   1995  C CB  . SER A 1 254 ? 16.051  0.273   23.631  1.00 18.92  ? 283 SER A CB  1 
ATOM   1996  O OG  . SER A 1 254 ? 15.368  0.252   24.837  1.00 18.66  ? 283 SER A OG  1 
ATOM   1997  N N   . ASP A 1 255 ? 18.590  -0.699  21.907  1.00 20.04  ? 284 ASP A N   1 
ATOM   1998  C CA  . ASP A 1 255 ? 19.481  -0.684  20.762  1.00 20.13  ? 284 ASP A CA  1 
ATOM   1999  C C   . ASP A 1 255 ? 18.762  -0.112  19.545  1.00 20.49  ? 284 ASP A C   1 
ATOM   2000  O O   . ASP A 1 255 ? 17.531  -0.037  19.493  1.00 20.89  ? 284 ASP A O   1 
ATOM   2001  C CB  . ASP A 1 255 ? 20.025  -2.091  20.501  1.00 21.65  ? 284 ASP A CB  1 
ATOM   2002  C CG  . ASP A 1 255 ? 18.926  -3.033  20.065  1.00 22.10  ? 284 ASP A CG  1 
ATOM   2003  O OD1 . ASP A 1 255 ? 18.298  -2.736  19.039  1.00 22.11  ? 284 ASP A OD1 1 
ATOM   2004  O OD2 . ASP A 1 255 ? 18.691  -4.031  20.772  1.00 25.43  ? 284 ASP A OD2 1 
ATOM   2005  N N   . PRO A 1 256 ? 19.519  0.272   18.492  1.00 19.89  ? 285 PRO A N   1 
ATOM   2006  C CA  . PRO A 1 256 ? 18.937  0.858   17.290  1.00 19.67  ? 285 PRO A CA  1 
ATOM   2007  C C   . PRO A 1 256 ? 17.765  0.080   16.701  1.00 19.51  ? 285 PRO A C   1 
ATOM   2008  O O   . PRO A 1 256 ? 16.821  0.659   16.203  1.00 19.89  ? 285 PRO A O   1 
ATOM   2009  C CB  . PRO A 1 256 ? 20.126  0.826   16.332  1.00 20.43  ? 285 PRO A CB  1 
ATOM   2010  C CG  . PRO A 1 256 ? 21.296  1.069   17.237  1.00 19.18  ? 285 PRO A CG  1 
ATOM   2011  C CD  . PRO A 1 256 ? 20.986  0.181   18.421  1.00 21.19  ? 285 PRO A CD  1 
ATOM   2012  N N   . TYR A 1 257 ? 17.856  -1.246  16.701  1.00 17.25  ? 286 TYR A N   1 
ATOM   2013  C CA  . TYR A 1 257 ? 16.787  -2.081  16.183  1.00 18.41  ? 286 TYR A CA  1 
ATOM   2014  C C   . TYR A 1 257 ? 15.475  -1.854  16.939  1.00 16.49  ? 286 TYR A C   1 
ATOM   2015  O O   . TYR A 1 257 ? 14.406  -1.633  16.373  1.00 16.44  ? 286 TYR A O   1 
ATOM   2016  C CB  . TYR A 1 257 ? 17.231  -3.542  16.245  1.00 17.53  ? 286 TYR A CB  1 
ATOM   2017  C CG  . TYR A 1 257 ? 18.375  -3.877  15.329  1.00 19.56  ? 286 TYR A CG  1 
ATOM   2018  C CD1 . TYR A 1 257 ? 18.162  -4.094  13.978  1.00 19.74  ? 286 TYR A CD1 1 
ATOM   2019  C CD2 . TYR A 1 257 ? 19.680  -3.929  15.788  1.00 21.01  ? 286 TYR A CD2 1 
ATOM   2020  C CE1 . TYR A 1 257 ? 19.208  -4.382  13.113  1.00 21.62  ? 286 TYR A CE1 1 
ATOM   2021  C CE2 . TYR A 1 257 ? 20.744  -4.221  14.935  1.00 22.65  ? 286 TYR A CE2 1 
ATOM   2022  C CZ  . TYR A 1 257 ? 20.511  -4.455  13.588  1.00 21.47  ? 286 TYR A CZ  1 
ATOM   2023  O OH  . TYR A 1 257 ? 21.524  -4.782  12.696  1.00 23.50  ? 286 TYR A OH  1 
ATOM   2024  N N   . LEU A 1 258 ? 15.526  -1.933  18.258  1.00 17.73  ? 287 LEU A N   1 
ATOM   2025  C CA  . LEU A 1 258 ? 14.326  -1.707  19.043  1.00 16.16  ? 287 LEU A CA  1 
ATOM   2026  C C   . LEU A 1 258 ? 13.865  -0.264  18.898  1.00 13.68  ? 287 LEU A C   1 
ATOM   2027  O O   . LEU A 1 258 ? 12.650  -0.069  18.894  1.00 16.19  ? 287 LEU A O   1 
ATOM   2028  C CB  . LEU A 1 258 ? 14.627  -2.007  20.510  1.00 18.00  ? 287 LEU A CB  1 
ATOM   2029  C CG  . LEU A 1 258 ? 15.162  -3.406  20.811  1.00 18.16  ? 287 LEU A CG  1 
ATOM   2030  C CD1 . LEU A 1 258 ? 15.362  -3.584  22.311  1.00 18.40  ? 287 LEU A CD1 1 
ATOM   2031  C CD2 . LEU A 1 258 ? 14.214  -4.474  20.272  1.00 18.42  ? 287 LEU A CD2 1 
ATOM   2032  N N   . SER A 1 259 ? 14.816  0.680   18.836  1.00 14.62  ? 288 SER A N   1 
ATOM   2033  C CA  . SER A 1 259 ? 14.471  2.095   18.833  1.00 16.09  ? 288 SER A CA  1 
ATOM   2034  C C   . SER A 1 259 ? 13.718  2.433   17.553  1.00 17.31  ? 288 SER A C   1 
ATOM   2035  O O   . SER A 1 259 ? 12.683  3.123   17.567  1.00 16.16  ? 288 SER A O   1 
ATOM   2036  C CB  . SER A 1 259 ? 15.705  2.975   18.994  1.00 16.58  ? 288 SER A CB  1 
ATOM   2037  O OG  . SER A 1 259 ? 16.307  2.810   20.274  1.00 19.72  ? 288 SER A OG  1 
ATOM   2038  N N   . PHE A 1 260 ? 14.224  1.857   16.453  1.00 16.45  ? 289 PHE A N   1 
ATOM   2039  C CA  . PHE A 1 260 ? 13.665  2.056   15.133  1.00 16.86  ? 289 PHE A CA  1 
ATOM   2040  C C   . PHE A 1 260 ? 12.299  1.397   15.003  1.00 18.51  ? 289 PHE A C   1 
ATOM   2041  O O   . PHE A 1 260 ? 11.396  2.021   14.470  1.00 21.37  ? 289 PHE A O   1 
ATOM   2042  C CB  . PHE A 1 260 ? 14.596  1.508   14.062  1.00 17.20  ? 289 PHE A CB  1 
ATOM   2043  C CG  . PHE A 1 260 ? 14.067  1.825   12.691  1.00 18.15  ? 289 PHE A CG  1 
ATOM   2044  C CD1 . PHE A 1 260 ? 14.024  3.141   12.235  1.00 18.38  ? 289 PHE A CD1 1 
ATOM   2045  C CD2 . PHE A 1 260 ? 13.507  0.849   11.908  1.00 17.34  ? 289 PHE A CD2 1 
ATOM   2046  C CE1 . PHE A 1 260 ? 13.540  3.427   10.970  1.00 20.19  ? 289 PHE A CE1 1 
ATOM   2047  C CE2 . PHE A 1 260 ? 13.033  1.137   10.639  1.00 18.79  ? 289 PHE A CE2 1 
ATOM   2048  C CZ  . PHE A 1 260 ? 13.047  2.426   10.177  1.00 19.42  ? 289 PHE A CZ  1 
ATOM   2049  N N   . ALA A 1 261 ? 12.165  0.145   15.460  1.00 17.57  ? 290 ALA A N   1 
ATOM   2050  C CA  . ALA A 1 261 ? 10.903  -0.584  15.424  1.00 19.31  ? 290 ALA A CA  1 
ATOM   2051  C C   . ALA A 1 261 ? 9.799   0.151   16.188  1.00 20.32  ? 290 ALA A C   1 
ATOM   2052  O O   . ALA A 1 261 ? 8.651   0.184   15.731  1.00 19.70  ? 290 ALA A O   1 
ATOM   2053  C CB  . ALA A 1 261 ? 11.104  -1.994  15.912  1.00 19.71  ? 290 ALA A CB  1 
ATOM   2054  N N   . ALA A 1 262 ? 10.125  0.686   17.377  1.00 18.84  ? 291 ALA A N   1 
ATOM   2055  C CA  . ALA A 1 262 ? 9.169   1.516   18.097  1.00 19.44  ? 291 ALA A CA  1 
ATOM   2056  C C   . ALA A 1 262 ? 8.770   2.716   17.243  1.00 20.13  ? 291 ALA A C   1 
ATOM   2057  O O   . ALA A 1 262 ? 7.582   3.051   17.163  1.00 17.17  ? 291 ALA A O   1 
ATOM   2058  C CB  . ALA A 1 262 ? 9.752   1.958   19.418  1.00 18.62  ? 291 ALA A CB  1 
ATOM   2059  N N   . ALA A 1 263 ? 9.758   3.358   16.622  1.00 19.64  ? 292 ALA A N   1 
ATOM   2060  C CA  . ALA A 1 263 ? 9.488   4.498   15.750  1.00 21.54  ? 292 ALA A CA  1 
ATOM   2061  C C   . ALA A 1 263 ? 8.521   4.102   14.633  1.00 22.08  ? 292 ALA A C   1 
ATOM   2062  O O   . ALA A 1 263 ? 7.615   4.861   14.310  1.00 17.26  ? 292 ALA A O   1 
ATOM   2063  C CB  . ALA A 1 263 ? 10.764  5.063   15.174  1.00 23.17  ? 292 ALA A CB  1 
ATOM   2064  N N   . MET A 1 264 ? 8.677   2.889   14.063  1.00 19.76  ? 293 MET A N   1 
ATOM   2065  C CA  . MET A 1 264 ? 7.803   2.436   12.987  1.00 19.63  ? 293 MET A CA  1 
ATOM   2066  C C   . MET A 1 264 ? 6.366   2.222   13.474  1.00 18.90  ? 293 MET A C   1 
ATOM   2067  O O   . MET A 1 264 ? 5.435   2.366   12.696  1.00 21.77  ? 293 MET A O   1 
ATOM   2068  C CB  . MET A 1 264 ? 8.337   1.127   12.380  1.00 18.07  ? 293 MET A CB  1 
ATOM   2069  C CG  . MET A 1 264 ? 9.595   1.349   11.543  1.00 18.47  ? 293 MET A CG  1 
ATOM   2070  S SD  . MET A 1 264 ? 9.555   2.703   10.282  1.00 19.52  ? 293 MET A SD  1 
ATOM   2071  C CE  . MET A 1 264 ? 10.215  4.130   11.127  1.00 21.86  ? 293 MET A CE  1 
ATOM   2072  N N   . ASN A 1 265 ? 6.187   1.881   14.750  1.00 18.19  ? 294 ASN A N   1 
ATOM   2073  C CA  . ASN A 1 265 ? 4.860   1.715   15.318  1.00 19.41  ? 294 ASN A CA  1 
ATOM   2074  C C   . ASN A 1 265 ? 4.199   3.099   15.440  1.00 17.25  ? 294 ASN A C   1 
ATOM   2075  O O   . ASN A 1 265 ? 2.994   3.200   15.277  1.00 20.98  ? 294 ASN A O   1 
ATOM   2076  C CB  . ASN A 1 265 ? 4.896   0.904   16.620  1.00 18.36  ? 294 ASN A CB  1 
ATOM   2077  C CG  . ASN A 1 265 ? 5.057   -0.585  16.385  1.00 21.63  ? 294 ASN A CG  1 
ATOM   2078  O OD1 . ASN A 1 265 ? 5.219   -1.034  15.254  1.00 19.33  ? 294 ASN A OD1 1 
ATOM   2079  N ND2 . ASN A 1 265 ? 5.018   -1.356  17.448  1.00 22.09  ? 294 ASN A ND2 1 
ATOM   2080  N N   . GLY A 1 266 ? 4.997   4.134   15.718  1.00 17.97  ? 295 GLY A N   1 
ATOM   2081  C CA  . GLY A 1 266 ? 4.534   5.504   15.638  1.00 18.73  ? 295 GLY A CA  1 
ATOM   2082  C C   . GLY A 1 266 ? 4.196   5.938   14.206  1.00 19.21  ? 295 GLY A C   1 
ATOM   2083  O O   . GLY A 1 266 ? 3.130   6.479   13.930  1.00 19.01  ? 295 GLY A O   1 
ATOM   2084  N N   . LEU A 1 267 ? 5.110   5.690   13.276  1.00 17.12  ? 296 LEU A N   1 
ATOM   2085  C CA  . LEU A 1 267 ? 4.880   6.030   11.878  1.00 19.49  ? 296 LEU A CA  1 
ATOM   2086  C C   . LEU A 1 267 ? 3.601   5.397   11.315  1.00 20.76  ? 296 LEU A C   1 
ATOM   2087  O O   . LEU A 1 267 ? 3.007   5.973   10.406  1.00 24.07  ? 296 LEU A O   1 
ATOM   2088  C CB  . LEU A 1 267 ? 6.110   5.642   11.068  1.00 22.11  ? 296 LEU A CB  1 
ATOM   2089  C CG  . LEU A 1 267 ? 6.267   6.332   9.719   1.00 22.22  ? 296 LEU A CG  1 
ATOM   2090  C CD1 . LEU A 1 267 ? 6.257   7.862   9.892   1.00 23.10  ? 296 LEU A CD1 1 
ATOM   2091  C CD2 . LEU A 1 267 ? 7.561   5.863   9.081   1.00 24.09  ? 296 LEU A CD2 1 
ATOM   2092  N N   . ALA A 1 268 ? 3.238   4.203   11.809  1.00 19.72  ? 297 ALA A N   1 
ATOM   2093  C CA  . ALA A 1 268 ? 2.091   3.436   11.367  1.00 22.42  ? 297 ALA A CA  1 
ATOM   2094  C C   . ALA A 1 268 ? 0.784   4.104   11.781  1.00 21.63  ? 297 ALA A C   1 
ATOM   2095  O O   . ALA A 1 268 ? -0.269  3.664   11.331  1.00 20.79  ? 297 ALA A O   1 
ATOM   2096  C CB  . ALA A 1 268 ? 2.133   2.044   11.974  1.00 22.51  ? 297 ALA A CB  1 
ATOM   2097  N N   . GLY A 1 269 ? 0.880   5.112   12.659  1.00 20.01  ? 298 GLY A N   1 
ATOM   2098  C CA  . GLY A 1 269 ? -0.288  5.832   13.148  1.00 18.81  ? 298 GLY A CA  1 
ATOM   2099  C C   . GLY A 1 269 ? -0.937  6.662   12.047  1.00 19.75  ? 298 GLY A C   1 
ATOM   2100  O O   . GLY A 1 269 ? -0.258  7.313   11.252  1.00 20.23  ? 298 GLY A O   1 
ATOM   2101  N N   . PRO A 1 270 ? -2.278  6.600   11.898  1.00 20.36  ? 299 PRO A N   1 
ATOM   2102  C CA  . PRO A 1 270 ? -2.989  7.428   10.927  1.00 19.68  ? 299 PRO A CA  1 
ATOM   2103  C C   . PRO A 1 270 ? -2.659  8.902   10.911  1.00 20.57  ? 299 PRO A C   1 
ATOM   2104  O O   . PRO A 1 270 ? -2.764  9.525   9.865   1.00 19.42  ? 299 PRO A O   1 
ATOM   2105  C CB  . PRO A 1 270 ? -4.421  7.316   11.431  1.00 20.61  ? 299 PRO A CB  1 
ATOM   2106  C CG  . PRO A 1 270 ? -4.495  5.858   11.832  1.00 20.87  ? 299 PRO A CG  1 
ATOM   2107  C CD  . PRO A 1 270 ? -3.179  5.640   12.551  1.00 21.58  ? 299 PRO A CD  1 
ATOM   2108  N N   . LEU A 1 271 ? -2.350  9.467   12.088  1.00 21.16  ? 300 LEU A N   1 
ATOM   2109  C CA  . LEU A 1 271 ? -2.088  10.899  12.129  1.00 18.84  ? 300 LEU A CA  1 
ATOM   2110  C C   . LEU A 1 271 ? -0.645  11.184  11.731  1.00 22.48  ? 300 LEU A C   1 
ATOM   2111  O O   . LEU A 1 271 ? -0.242  12.340  11.629  1.00 25.45  ? 300 LEU A O   1 
ATOM   2112  C CB  . LEU A 1 271 ? -2.429  11.423  13.530  1.00 21.49  ? 300 LEU A CB  1 
ATOM   2113  C CG  . LEU A 1 271 ? -3.912  11.398  13.890  1.00 24.50  ? 300 LEU A CG  1 
ATOM   2114  C CD1 . LEU A 1 271 ? -4.186  12.273  15.108  1.00 28.18  ? 300 LEU A CD1 1 
ATOM   2115  C CD2 . LEU A 1 271 ? -4.793  11.820  12.729  1.00 26.56  ? 300 LEU A CD2 1 
ATOM   2116  N N   . HIS A 1 272 ? 0.139   10.135  11.474  1.00 23.40  ? 301 HIS A N   1 
ATOM   2117  C CA  . HIS A 1 272 ? 1.541   10.321  11.134  1.00 23.87  ? 301 HIS A CA  1 
ATOM   2118  C C   . HIS A 1 272 ? 1.717   9.785   9.716   1.00 25.36  ? 301 HIS A C   1 
ATOM   2119  O O   . HIS A 1 272 ? 1.379   10.448  8.755   1.00 27.85  ? 301 HIS A O   1 
ATOM   2120  C CB  . HIS A 1 272 ? 2.467   9.732   12.218  1.00 22.26  ? 301 HIS A CB  1 
ATOM   2121  C CG  . HIS A 1 272 ? 3.911   10.137  12.115  1.00 20.52  ? 301 HIS A CG  1 
ATOM   2122  N ND1 . HIS A 1 272 ? 4.996   9.524   12.716  1.00 20.36  ? 301 HIS A ND1 1 
ATOM   2123  C CD2 . HIS A 1 272 ? 4.428   11.199  11.474  1.00 18.49  ? 301 HIS A CD2 1 
ATOM   2124  C CE1 . HIS A 1 272 ? 6.104   10.203  12.446  1.00 19.60  ? 301 HIS A CE1 1 
ATOM   2125  N NE2 . HIS A 1 272 ? 5.787   11.216  11.684  1.00 20.50  ? 301 HIS A NE2 1 
ATOM   2126  N N   . GLY A 1 273 ? 2.087   8.514   9.578   1.00 28.15  ? 302 GLY A N   1 
ATOM   2127  C CA  . GLY A 1 273 ? 2.628   8.037   8.318   1.00 32.88  ? 302 GLY A CA  1 
ATOM   2128  C C   . GLY A 1 273 ? 1.589   7.527   7.319   1.00 32.59  ? 302 GLY A C   1 
ATOM   2129  O O   . GLY A 1 273 ? 1.947   7.309   6.171   1.00 35.58  ? 302 GLY A O   1 
ATOM   2130  N N   . LEU A 1 274 ? 0.326   7.363   7.737   1.00 36.13  ? 303 LEU A N   1 
ATOM   2131  C CA  . LEU A 1 274 ? -0.726  6.867   6.855   1.00 40.37  ? 303 LEU A CA  1 
ATOM   2132  C C   . LEU A 1 274 ? -1.460  7.990   6.123   1.00 46.26  ? 303 LEU A C   1 
ATOM   2133  O O   . LEU A 1 274 ? -2.540  7.736   5.593   1.00 58.71  ? 303 LEU A O   1 
ATOM   2134  C CB  . LEU A 1 274 ? -1.722  6.030   7.669   1.00 37.73  ? 303 LEU A CB  1 
ATOM   2135  C CG  . LEU A 1 274 ? -1.374  4.550   7.788   1.00 37.28  ? 303 LEU A CG  1 
ATOM   2136  C CD1 . LEU A 1 274 ? -0.019  4.382   8.439   1.00 39.21  ? 303 LEU A CD1 1 
ATOM   2137  C CD2 . LEU A 1 274 ? -2.428  3.777   8.561   1.00 32.59  ? 303 LEU A CD2 1 
ATOM   2138  N N   . ALA A 1 275 ? -0.879  9.200   6.045   1.00 42.66  ? 304 ALA A N   1 
ATOM   2139  C CA  . ALA A 1 275 ? -1.532  10.323  5.383   1.00 39.37  ? 304 ALA A CA  1 
ATOM   2140  C C   . ALA A 1 275 ? -1.448  10.217  3.850   1.00 40.76  ? 304 ALA A C   1 
ATOM   2141  O O   . ALA A 1 275 ? -2.432  10.478  3.164   1.00 38.54  ? 304 ALA A O   1 
ATOM   2142  C CB  . ALA A 1 275 ? -0.941  11.621  5.881   1.00 41.65  ? 304 ALA A CB  1 
ATOM   2143  N N   . ASN A 1 276 ? -0.278  9.839   3.312   1.00 38.18  ? 305 ASN A N   1 
ATOM   2144  C CA  . ASN A 1 276 ? -0.054  9.709   1.878   1.00 39.22  ? 305 ASN A CA  1 
ATOM   2145  C C   . ASN A 1 276 ? -1.207  8.912   1.266   1.00 36.55  ? 305 ASN A C   1 
ATOM   2146  O O   . ASN A 1 276 ? -1.688  9.250   0.185   1.00 34.58  ? 305 ASN A O   1 
ATOM   2147  C CB  . ASN A 1 276 ? 1.337   9.106   1.622   1.00 40.33  ? 305 ASN A CB  1 
ATOM   2148  C CG  . ASN A 1 276 ? 1.608   8.539   0.239   1.00 42.65  ? 305 ASN A CG  1 
ATOM   2149  O OD1 . ASN A 1 276 ? 0.797   8.618   -0.682  1.00 41.02  ? 305 ASN A OD1 1 
ATOM   2150  N ND2 . ASN A 1 276 ? 2.783   7.952   0.074   1.00 42.39  ? 305 ASN A ND2 1 
ATOM   2151  N N   . GLN A 1 277 ? -1.662  7.884   1.994   1.00 38.32  ? 306 GLN A N   1 
ATOM   2152  C CA  . GLN A 1 277 ? -2.713  6.998   1.527   1.00 39.56  ? 306 GLN A CA  1 
ATOM   2153  C C   . GLN A 1 277 ? -4.073  7.693   1.606   1.00 41.50  ? 306 GLN A C   1 
ATOM   2154  O O   . GLN A 1 277 ? -4.868  7.583   0.675   1.00 38.53  ? 306 GLN A O   1 
ATOM   2155  C CB  . GLN A 1 277 ? -2.744  5.707   2.351   1.00 39.36  ? 306 GLN A CB  1 
ATOM   2156  C CG  . GLN A 1 277 ? -1.562  4.796   2.100   1.00 40.37  ? 306 GLN A CG  1 
ATOM   2157  C CD  . GLN A 1 277 ? -0.359  5.112   2.954   1.00 41.12  ? 306 GLN A CD  1 
ATOM   2158  O OE1 . GLN A 1 277 ? -0.044  6.277   3.219   1.00 39.55  ? 306 GLN A OE1 1 
ATOM   2159  N NE2 . GLN A 1 277 ? 0.309   4.057   3.402   1.00 35.59  ? 306 GLN A NE2 1 
ATOM   2160  N N   . GLU A 1 278 ? -4.369  8.330   2.753   1.00 40.94  ? 307 GLU A N   1 
ATOM   2161  C CA  . GLU A 1 278 ? -5.617  9.064   2.921   1.00 43.05  ? 307 GLU A CA  1 
ATOM   2162  C C   . GLU A 1 278 ? -5.799  10.017  1.745   1.00 37.70  ? 307 GLU A C   1 
ATOM   2163  O O   . GLU A 1 278 ? -6.890  10.117  1.191   1.00 38.88  ? 307 GLU A O   1 
ATOM   2164  C CB  . GLU A 1 278 ? -5.636  9.858   4.233   1.00 48.55  ? 307 GLU A CB  1 
ATOM   2165  C CG  . GLU A 1 278 ? -5.943  9.012   5.453   1.00 54.35  ? 307 GLU A CG  1 
ATOM   2166  C CD  . GLU A 1 278 ? -6.145  9.762   6.767   1.00 62.06  ? 307 GLU A CD  1 
ATOM   2167  O OE1 . GLU A 1 278 ? -6.593  10.933  6.722   1.00 60.44  ? 307 GLU A OE1 1 
ATOM   2168  O OE2 . GLU A 1 278 ? -5.899  9.156   7.846   1.00 68.71  ? 307 GLU A OE2 1 
ATOM   2169  N N   . VAL A 1 279 ? -4.719  10.729  1.402   1.00 32.84  ? 308 VAL A N   1 
ATOM   2170  C CA  . VAL A 1 279 ? -4.709  11.667  0.298   1.00 31.19  ? 308 VAL A CA  1 
ATOM   2171  C C   . VAL A 1 279 ? -5.127  10.960  -0.985  1.00 30.49  ? 308 VAL A C   1 
ATOM   2172  O O   . VAL A 1 279 ? -6.074  11.388  -1.640  1.00 32.34  ? 308 VAL A O   1 
ATOM   2173  C CB  . VAL A 1 279 ? -3.341  12.359  0.129   1.00 31.67  ? 308 VAL A CB  1 
ATOM   2174  C CG1 . VAL A 1 279 ? -3.269  13.158  -1.170  1.00 32.84  ? 308 VAL A CG1 1 
ATOM   2175  C CG2 . VAL A 1 279 ? -3.050  13.262  1.306   1.00 31.79  ? 308 VAL A CG2 1 
ATOM   2176  N N   . LEU A 1 280 ? -4.449  9.860   -1.321  1.00 31.27  ? 309 LEU A N   1 
ATOM   2177  C CA  . LEU A 1 280 ? -4.683  9.212   -2.596  1.00 32.66  ? 309 LEU A CA  1 
ATOM   2178  C C   . LEU A 1 280 ? -6.120  8.697   -2.677  1.00 33.28  ? 309 LEU A C   1 
ATOM   2179  O O   . LEU A 1 280 ? -6.751  8.852   -3.712  1.00 36.18  ? 309 LEU A O   1 
ATOM   2180  C CB  . LEU A 1 280 ? -3.653  8.098   -2.800  1.00 34.39  ? 309 LEU A CB  1 
ATOM   2181  C CG  . LEU A 1 280 ? -3.421  7.712   -4.257  1.00 33.62  ? 309 LEU A CG  1 
ATOM   2182  C CD1 . LEU A 1 280 ? -2.949  8.897   -5.076  1.00 31.17  ? 309 LEU A CD1 1 
ATOM   2183  C CD2 . LEU A 1 280 ? -2.432  6.567   -4.371  1.00 32.13  ? 309 LEU A CD2 1 
ATOM   2184  N N   . VAL A 1 281 ? -6.644  8.129   -1.582  1.00 35.79  ? 310 VAL A N   1 
ATOM   2185  C CA  . VAL A 1 281 ? -8.016  7.641   -1.545  1.00 34.55  ? 310 VAL A CA  1 
ATOM   2186  C C   . VAL A 1 281 ? -8.992  8.809   -1.642  1.00 32.81  ? 310 VAL A C   1 
ATOM   2187  O O   . VAL A 1 281 ? -10.118 8.621   -2.094  1.00 32.16  ? 310 VAL A O   1 
ATOM   2188  C CB  . VAL A 1 281 ? -8.276  6.772   -0.297  1.00 35.36  ? 310 VAL A CB  1 
ATOM   2189  C CG1 . VAL A 1 281 ? -9.694  6.875   0.253   1.00 37.37  ? 310 VAL A CG1 1 
ATOM   2190  C CG2 . VAL A 1 281 ? -7.923  5.320   -0.563  1.00 37.32  ? 310 VAL A CG2 1 
ATOM   2191  N N   . TRP A 1 282 ? -8.572  10.003  -1.217  1.00 32.47  ? 311 TRP A N   1 
ATOM   2192  C CA  . TRP A 1 282 ? -9.433  11.174  -1.285  1.00 35.24  ? 311 TRP A CA  1 
ATOM   2193  C C   . TRP A 1 282 ? -9.379  11.780  -2.687  1.00 35.35  ? 311 TRP A C   1 
ATOM   2194  O O   . TRP A 1 282 ? -10.406 12.174  -3.230  1.00 38.03  ? 311 TRP A O   1 
ATOM   2195  C CB  . TRP A 1 282 ? -9.062  12.187  -0.192  1.00 36.95  ? 311 TRP A CB  1 
ATOM   2196  C CG  . TRP A 1 282 ? -9.907  13.427  -0.150  1.00 32.55  ? 311 TRP A CG  1 
ATOM   2197  C CD1 . TRP A 1 282 ? -11.090 13.599  0.509   1.00 32.82  ? 311 TRP A CD1 1 
ATOM   2198  C CD2 . TRP A 1 282 ? -9.617  14.683  -0.794  1.00 33.06  ? 311 TRP A CD2 1 
ATOM   2199  N NE1 . TRP A 1 282 ? -11.551 14.875  0.325   1.00 31.61  ? 311 TRP A NE1 1 
ATOM   2200  C CE2 . TRP A 1 282 ? -10.686 15.555  -0.497  1.00 31.34  ? 311 TRP A CE2 1 
ATOM   2201  C CE3 . TRP A 1 282 ? -8.578  15.151  -1.604  1.00 29.84  ? 311 TRP A CE3 1 
ATOM   2202  C CZ2 . TRP A 1 282 ? -10.710 16.873  -0.948  1.00 33.07  ? 311 TRP A CZ2 1 
ATOM   2203  C CZ3 . TRP A 1 282 ? -8.606  16.453  -2.056  1.00 32.68  ? 311 TRP A CZ3 1 
ATOM   2204  C CH2 . TRP A 1 282 ? -9.666  17.300  -1.740  1.00 33.58  ? 311 TRP A CH2 1 
ATOM   2205  N N   . LEU A 1 283 ? -8.174  11.862  -3.266  1.00 37.66  ? 312 LEU A N   1 
ATOM   2206  C CA  . LEU A 1 283 ? -8.009  12.292  -4.646  1.00 34.35  ? 312 LEU A CA  1 
ATOM   2207  C C   . LEU A 1 283 ? -8.805  11.366  -5.572  1.00 37.63  ? 312 LEU A C   1 
ATOM   2208  O O   . LEU A 1 283 ? -9.528  11.830  -6.451  1.00 36.87  ? 312 LEU A O   1 
ATOM   2209  C CB  . LEU A 1 283 ? -6.515  12.306  -4.989  1.00 32.65  ? 312 LEU A CB  1 
ATOM   2210  C CG  . LEU A 1 283 ? -5.674  13.346  -4.249  1.00 31.86  ? 312 LEU A CG  1 
ATOM   2211  C CD1 . LEU A 1 283 ? -4.184  13.198  -4.543  1.00 29.83  ? 312 LEU A CD1 1 
ATOM   2212  C CD2 . LEU A 1 283 ? -6.137  14.760  -4.575  1.00 34.99  ? 312 LEU A CD2 1 
ATOM   2213  N N   . THR A 1 284 ? -8.680  10.052  -5.366  1.00 36.28  ? 313 THR A N   1 
ATOM   2214  C CA  . THR A 1 284 ? -9.300  9.062   -6.232  1.00 42.04  ? 313 THR A CA  1 
ATOM   2215  C C   . THR A 1 284 ? -10.811 9.251   -6.268  1.00 43.85  ? 313 THR A C   1 
ATOM   2216  O O   . THR A 1 284 ? -11.405 9.366   -7.342  1.00 46.20  ? 313 THR A O   1 
ATOM   2217  C CB  . THR A 1 284 ? -8.964  7.640   -5.770  1.00 43.93  ? 313 THR A CB  1 
ATOM   2218  O OG1 . THR A 1 284 ? -7.545  7.507   -5.879  1.00 49.26  ? 313 THR A OG1 1 
ATOM   2219  C CG2 . THR A 1 284 ? -9.645  6.569   -6.591  1.00 46.14  ? 313 THR A CG2 1 
ATOM   2220  N N   . GLN A 1 285 ? -11.414 9.269   -5.079  1.00 44.52  ? 314 GLN A N   1 
ATOM   2221  C CA  . GLN A 1 285 ? -12.836 9.523   -4.935  1.00 48.09  ? 314 GLN A CA  1 
ATOM   2222  C C   . GLN A 1 285 ? -13.206 10.803  -5.681  1.00 46.41  ? 314 GLN A C   1 
ATOM   2223  O O   . GLN A 1 285 ? -14.138 10.822  -6.478  1.00 51.53  ? 314 GLN A O   1 
ATOM   2224  C CB  . GLN A 1 285 ? -13.186 9.636   -3.449  1.00 46.27  ? 314 GLN A CB  1 
ATOM   2225  C CG  . GLN A 1 285 ? -14.632 10.028  -3.189  1.00 48.54  ? 314 GLN A CG  1 
ATOM   2226  C CD  . GLN A 1 285 ? -15.590 8.944   -3.618  1.00 51.97  ? 314 GLN A CD  1 
ATOM   2227  O OE1 . GLN A 1 285 ? -15.199 7.804   -3.875  1.00 53.61  ? 314 GLN A OE1 1 
ATOM   2228  N NE2 . GLN A 1 285 ? -16.866 9.289   -3.675  1.00 53.05  ? 314 GLN A NE2 1 
ATOM   2229  N N   . LEU A 1 286 ? -12.450 11.869  -5.414  1.00 46.50  ? 315 LEU A N   1 
ATOM   2230  C CA  . LEU A 1 286 ? -12.752 13.187  -5.941  1.00 46.66  ? 315 LEU A CA  1 
ATOM   2231  C C   . LEU A 1 286 ? -12.778 13.166  -7.474  1.00 46.15  ? 315 LEU A C   1 
ATOM   2232  O O   . LEU A 1 286 ? -13.645 13.785  -8.084  1.00 46.33  ? 315 LEU A O   1 
ATOM   2233  C CB  . LEU A 1 286 ? -11.725 14.173  -5.375  1.00 42.47  ? 315 LEU A CB  1 
ATOM   2234  C CG  . LEU A 1 286 ? -11.720 15.572  -5.988  1.00 43.97  ? 315 LEU A CG  1 
ATOM   2235  C CD1 . LEU A 1 286 ? -13.080 16.231  -5.879  1.00 45.53  ? 315 LEU A CD1 1 
ATOM   2236  C CD2 . LEU A 1 286 ? -10.670 16.448  -5.322  1.00 43.73  ? 315 LEU A CD2 1 
ATOM   2237  N N   . GLN A 1 287 ? -11.869 12.427  -8.112  1.00 50.17  ? 316 GLN A N   1 
ATOM   2238  C CA  . GLN A 1 287 ? -11.844 12.400  -9.568  1.00 52.91  ? 316 GLN A CA  1 
ATOM   2239  C C   . GLN A 1 287 ? -13.003 11.559  -10.105 1.00 56.76  ? 316 GLN A C   1 
ATOM   2240  O O   . GLN A 1 287 ? -13.301 11.612  -11.296 1.00 70.76  ? 316 GLN A O   1 
ATOM   2241  C CB  . GLN A 1 287 ? -10.486 11.914  -10.081 1.00 54.83  ? 316 GLN A CB  1 
ATOM   2242  C CG  . GLN A 1 287 ? -10.168 12.390  -11.491 1.00 54.14  ? 316 GLN A CG  1 
ATOM   2243  C CD  . GLN A 1 287 ? -8.777  12.048  -11.974 1.00 58.22  ? 316 GLN A CD  1 
ATOM   2244  O OE1 . GLN A 1 287 ? -8.408  10.882  -12.114 1.00 54.97  ? 316 GLN A OE1 1 
ATOM   2245  N NE2 . GLN A 1 287 ? -7.990  13.077  -12.251 1.00 61.07  ? 316 GLN A NE2 1 
ATOM   2246  N N   . LYS A 1 288 ? -13.681 10.811  -9.227  1.00 60.02  ? 317 LYS A N   1 
ATOM   2247  C CA  . LYS A 1 288 ? -14.825 9.993   -9.606  1.00 60.07  ? 317 LYS A CA  1 
ATOM   2248  C C   . LYS A 1 288 ? -16.104 10.584  -9.004  1.00 59.78  ? 317 LYS A C   1 
ATOM   2249  O O   . LYS A 1 288 ? -17.111 9.893   -8.874  1.00 60.31  ? 317 LYS A O   1 
ATOM   2250  C CB  . LYS A 1 288 ? -14.546 8.562   -9.135  1.00 59.15  ? 317 LYS A CB  1 
ATOM   2251  C CG  . LYS A 1 288 ? -15.535 7.485   -9.565  1.00 62.59  ? 317 LYS A CG  1 
ATOM   2252  C CD  . LYS A 1 288 ? -15.622 6.333   -8.581  1.00 67.06  ? 317 LYS A CD  1 
ATOM   2253  C CE  . LYS A 1 288 ? -16.243 6.737   -7.257  1.00 68.87  ? 317 LYS A CE  1 
ATOM   2254  N NZ  . LYS A 1 288 ? -15.945 5.761   -6.183  1.00 70.46  ? 317 LYS A NZ  1 
ATOM   2255  N N   . GLU A 1 289 ? -16.052 11.863  -8.614  1.00 61.95  ? 318 GLU A N   1 
ATOM   2256  C CA  . GLU A 1 289 ? -17.194 12.563  -8.041  1.00 66.11  ? 318 GLU A CA  1 
ATOM   2257  C C   . GLU A 1 289 ? -17.482 13.840  -8.823  1.00 64.31  ? 318 GLU A C   1 
ATOM   2258  O O   . GLU A 1 289 ? -18.618 14.312  -8.827  1.00 68.54  ? 318 GLU A O   1 
ATOM   2259  C CB  . GLU A 1 289 ? -16.949 12.948  -6.579  1.00 72.07  ? 318 GLU A CB  1 
ATOM   2260  C CG  . GLU A 1 289 ? -17.488 11.953  -5.567  1.00 73.89  ? 318 GLU A CG  1 
ATOM   2261  C CD  . GLU A 1 289 ? -17.566 12.495  -4.149  1.00 81.90  ? 318 GLU A CD  1 
ATOM   2262  O OE1 . GLU A 1 289 ? -16.527 12.962  -3.632  1.00 92.90  ? 318 GLU A OE1 1 
ATOM   2263  O OE2 . GLU A 1 289 ? -18.665 12.453  -3.560  1.00 88.10  ? 318 GLU A OE2 1 
ATOM   2264  N N   . VAL A 1 290 ? -16.430 14.429  -9.404  1.00 60.92  ? 319 VAL A N   1 
ATOM   2265  C CA  . VAL A 1 290 ? -16.559 15.574  -10.289 1.00 58.73  ? 319 VAL A CA  1 
ATOM   2266  C C   . VAL A 1 290 ? -15.857 15.247  -11.604 1.00 58.46  ? 319 VAL A C   1 
ATOM   2267  O O   . VAL A 1 290 ? -15.360 16.139  -12.291 1.00 54.22  ? 319 VAL A O   1 
ATOM   2268  C CB  . VAL A 1 290 ? -16.003 16.854  -9.634  1.00 58.45  ? 319 VAL A CB  1 
ATOM   2269  C CG1 . VAL A 1 290 ? -16.656 17.109  -8.279  1.00 56.80  ? 319 VAL A CG1 1 
ATOM   2270  C CG2 . VAL A 1 290 ? -14.483 16.825  -9.501  1.00 60.03  ? 319 VAL A CG2 1 
ATOM   2271  N N   . GLY A 1 291 ? -15.786 13.957  -11.947 1.00 60.62  ? 320 GLY A N   1 
ATOM   2272  C CA  . GLY A 1 291 ? -15.205 13.560  -13.246 1.00 64.83  ? 320 GLY A CA  1 
ATOM   2273  C C   . GLY A 1 291 ? -13.699 13.740  -13.313 1.00 71.20  ? 320 GLY A C   1 
ATOM   2274  O O   . GLY A 1 291 ? -13.122 14.381  -12.408 1.00 74.63  ? 320 GLY A O   1 
ATOM   2275  N N   . LYS A 1 292 ? -13.069 13.167  -14.343 1.00 78.23  ? 321 LYS A N   1 
ATOM   2276  C CA  . LYS A 1 292 ? -11.601 13.311  -14.519 1.00 75.81  ? 321 LYS A CA  1 
ATOM   2277  C C   . LYS A 1 292 ? -11.270 14.801  -14.677 1.00 71.58  ? 321 LYS A C   1 
ATOM   2278  O O   . LYS A 1 292 ? -10.540 15.345  -13.819 1.00 73.45  ? 321 LYS A O   1 
ATOM   2279  C CB  . LYS A 1 292 ? -11.122 12.507  -15.732 1.00 78.69  ? 321 LYS A CB  1 
ATOM   2280  N N   . ASP A 1 293 ? -11.794 15.428  -15.733 1.00 70.83  ? 322 ASP A N   1 
ATOM   2281  C CA  . ASP A 1 293 ? -11.555 16.880  -15.958 1.00 71.43  ? 322 ASP A CA  1 
ATOM   2282  C C   . ASP A 1 293 ? -12.494 17.686  -15.057 1.00 67.07  ? 322 ASP A C   1 
ATOM   2283  O O   . ASP A 1 293 ? -13.678 17.299  -14.938 1.00 69.74  ? 322 ASP A O   1 
ATOM   2284  C CB  . ASP A 1 293 ? -11.711 17.248  -17.425 1.00 72.33  ? 322 ASP A CB  1 
ATOM   2285  C CG  . ASP A 1 293 ? -12.223 18.656  -17.693 1.00 74.73  ? 322 ASP A CG  1 
ATOM   2286  O OD1 . ASP A 1 293 ? -11.441 19.611  -17.501 1.00 75.70  ? 322 ASP A OD1 1 
ATOM   2287  O OD2 . ASP A 1 293 ? -13.401 18.786  -18.085 1.00 70.87  ? 322 ASP A OD2 1 
ATOM   2288  N N   . VAL A 1 294 ? -11.982 18.757  -14.446 1.00 60.29  ? 323 VAL A N   1 
ATOM   2289  C CA  . VAL A 1 294 ? -12.834 19.642  -13.595 1.00 58.04  ? 323 VAL A CA  1 
ATOM   2290  C C   . VAL A 1 294 ? -12.275 21.073  -13.696 1.00 59.86  ? 323 VAL A C   1 
ATOM   2291  O O   . VAL A 1 294 ? -11.046 21.233  -13.544 1.00 62.53  ? 323 VAL A O   1 
ATOM   2292  C CB  . VAL A 1 294 ? -12.908 19.141  -12.139 1.00 62.87  ? 323 VAL A CB  1 
ATOM   2293  C CG1 . VAL A 1 294 ? -11.554 18.691  -11.602 1.00 64.62  ? 323 VAL A CG1 1 
ATOM   2294  C CG2 . VAL A 1 294 ? -13.564 20.153  -11.210 1.00 64.43  ? 323 VAL A CG2 1 
ATOM   2295  N N   . SER A 1 295 ? -13.127 22.065  -13.973 1.00 53.82  ? 324 SER A N   1 
ATOM   2296  C CA  . SER A 1 295 ? -12.612 23.425  -14.029 1.00 53.07  ? 324 SER A CA  1 
ATOM   2297  C C   . SER A 1 295 ? -12.430 24.018  -12.627 1.00 48.51  ? 324 SER A C   1 
ATOM   2298  O O   . SER A 1 295 ? -13.065 23.582  -11.668 1.00 41.51  ? 324 SER A O   1 
ATOM   2299  C CB  . SER A 1 295 ? -13.495 24.290  -14.894 1.00 58.21  ? 324 SER A CB  1 
ATOM   2300  O OG  . SER A 1 295 ? -13.194 24.095  -16.267 1.00 65.55  ? 324 SER A OG  1 
ATOM   2301  N N   . ASP A 1 296 ? -11.566 25.045  -12.547 1.00 47.71  ? 325 ASP A N   1 
ATOM   2302  C CA  . ASP A 1 296 ? -11.160 25.693  -11.303 1.00 45.16  ? 325 ASP A CA  1 
ATOM   2303  C C   . ASP A 1 296 ? -12.363 26.235  -10.531 1.00 45.11  ? 325 ASP A C   1 
ATOM   2304  O O   . ASP A 1 296 ? -12.269 26.454  -9.327  1.00 38.45  ? 325 ASP A O   1 
ATOM   2305  C CB  . ASP A 1 296 ? -10.177 26.842  -11.567 1.00 45.59  ? 325 ASP A CB  1 
ATOM   2306  C CG  . ASP A 1 296 ? -8.886  26.426  -12.255 1.00 48.09  ? 325 ASP A CG  1 
ATOM   2307  O OD1 . ASP A 1 296 ? -8.685  25.208  -12.446 1.00 49.57  ? 325 ASP A OD1 1 
ATOM   2308  O OD2 . ASP A 1 296 ? -8.082  27.327  -12.590 1.00 49.56  ? 325 ASP A OD2 1 
ATOM   2309  N N   . GLU A 1 297 ? -13.478 26.489  -11.234 1.00 49.73  ? 326 GLU A N   1 
ATOM   2310  C CA  . GLU A 1 297 ? -14.729 26.893  -10.603 1.00 52.66  ? 326 GLU A CA  1 
ATOM   2311  C C   . GLU A 1 297 ? -15.359 25.718  -9.852  1.00 48.06  ? 326 GLU A C   1 
ATOM   2312  O O   . GLU A 1 297 ? -15.731 25.847  -8.687  1.00 48.58  ? 326 GLU A O   1 
ATOM   2313  C CB  . GLU A 1 297 ? -15.672 27.455  -11.674 1.00 58.36  ? 326 GLU A CB  1 
ATOM   2314  C CG  . GLU A 1 297 ? -17.120 27.626  -11.233 1.00 58.98  ? 326 GLU A CG  1 
ATOM   2315  C CD  . GLU A 1 297 ? -17.937 28.512  -12.160 1.00 60.76  ? 326 GLU A CD  1 
ATOM   2316  O OE1 . GLU A 1 297 ? -17.529 29.675  -12.358 1.00 59.74  ? 326 GLU A OE1 1 
ATOM   2317  O OE2 . GLU A 1 297 ? -18.972 28.042  -12.687 1.00 59.00  ? 326 GLU A OE2 1 
ATOM   2318  N N   . LYS A 1 298 ? -15.480 24.570  -10.525 1.00 51.09  ? 327 LYS A N   1 
ATOM   2319  C CA  . LYS A 1 298 ? -16.211 23.436  -9.978  1.00 50.97  ? 327 LYS A CA  1 
ATOM   2320  C C   . LYS A 1 298 ? -15.341 22.693  -8.963  1.00 48.31  ? 327 LYS A C   1 
ATOM   2321  O O   . LYS A 1 298 ? -15.868 22.014  -8.076  1.00 47.15  ? 327 LYS A O   1 
ATOM   2322  C CB  . LYS A 1 298 ? -16.689 22.515  -11.108 1.00 53.31  ? 327 LYS A CB  1 
ATOM   2323  C CG  . LYS A 1 298 ? -18.110 21.988  -10.964 1.00 57.72  ? 327 LYS A CG  1 
ATOM   2324  C CD  . LYS A 1 298 ? -18.242 20.575  -10.432 1.00 58.54  ? 327 LYS A CD  1 
ATOM   2325  C CE  . LYS A 1 298 ? -18.559 19.570  -11.522 1.00 55.14  ? 327 LYS A CE  1 
ATOM   2326  N NZ  . LYS A 1 298 ? -19.135 18.325  -10.965 1.00 53.08  ? 327 LYS A NZ  1 
ATOM   2327  N N   . LEU A 1 299 ? -14.014 22.820  -9.083  1.00 45.85  ? 328 LEU A N   1 
ATOM   2328  C CA  . LEU A 1 299 ? -13.140 22.259  -8.065  1.00 45.08  ? 328 LEU A CA  1 
ATOM   2329  C C   . LEU A 1 299 ? -13.199 23.115  -6.800  1.00 41.95  ? 328 LEU A C   1 
ATOM   2330  O O   . LEU A 1 299 ? -13.400 22.591  -5.706  1.00 41.67  ? 328 LEU A O   1 
ATOM   2331  C CB  . LEU A 1 299 ? -11.702 22.152  -8.577  1.00 42.93  ? 328 LEU A CB  1 
ATOM   2332  C CG  . LEU A 1 299 ? -10.773 21.364  -7.652  1.00 38.93  ? 328 LEU A CG  1 
ATOM   2333  C CD1 . LEU A 1 299 ? -11.125 19.881  -7.662  1.00 39.79  ? 328 LEU A CD1 1 
ATOM   2334  C CD2 . LEU A 1 299 ? -9.320  21.566  -8.042  1.00 38.43  ? 328 LEU A CD2 1 
ATOM   2335  N N   . ARG A 1 300 ? -13.028 24.433  -6.969  1.00 42.24  ? 329 ARG A N   1 
ATOM   2336  C CA  . ARG A 1 300 ? -13.149 25.382  -5.872  1.00 41.85  ? 329 ARG A CA  1 
ATOM   2337  C C   . ARG A 1 300 ? -14.444 25.154  -5.102  1.00 44.26  ? 329 ARG A C   1 
ATOM   2338  O O   . ARG A 1 300 ? -14.476 25.287  -3.887  1.00 46.72  ? 329 ARG A O   1 
ATOM   2339  C CB  . ARG A 1 300 ? -13.106 26.816  -6.397  1.00 41.29  ? 329 ARG A CB  1 
ATOM   2340  C CG  . ARG A 1 300 ? -13.120 27.860  -5.291  1.00 41.12  ? 329 ARG A CG  1 
ATOM   2341  C CD  . ARG A 1 300 ? -12.807 29.228  -5.844  1.00 43.37  ? 329 ARG A CD  1 
ATOM   2342  N NE  . ARG A 1 300 ? -11.564 29.355  -6.588  1.00 46.37  ? 329 ARG A NE  1 
ATOM   2343  C CZ  . ARG A 1 300 ? -11.492 29.529  -7.904  1.00 50.41  ? 329 ARG A CZ  1 
ATOM   2344  N NH1 . ARG A 1 300 ? -12.592 29.528  -8.631  1.00 55.96  ? 329 ARG A NH1 1 
ATOM   2345  N NH2 . ARG A 1 300 ? -10.322 29.685  -8.496  1.00 50.42  ? 329 ARG A NH2 1 
ATOM   2346  N N   . ASP A 1 301 ? -15.507 24.821  -5.836  1.00 55.25  ? 330 ASP A N   1 
ATOM   2347  C CA  . ASP A 1 301 ? -16.826 24.593  -5.278  1.00 58.11  ? 330 ASP A CA  1 
ATOM   2348  C C   . ASP A 1 301 ? -16.843 23.324  -4.427  1.00 57.74  ? 330 ASP A C   1 
ATOM   2349  O O   . ASP A 1 301 ? -17.470 23.294  -3.366  1.00 50.89  ? 330 ASP A O   1 
ATOM   2350  C CB  . ASP A 1 301 ? -17.852 24.512  -6.409  1.00 69.61  ? 330 ASP A CB  1 
ATOM   2351  C CG  . ASP A 1 301 ? -19.250 24.147  -5.944  1.00 81.87  ? 330 ASP A CG  1 
ATOM   2352  O OD1 . ASP A 1 301 ? -19.955 25.055  -5.456  1.00 89.78  ? 330 ASP A OD1 1 
ATOM   2353  O OD2 . ASP A 1 301 ? -19.626 22.964  -6.098  1.00 90.65  ? 330 ASP A OD2 1 
ATOM   2354  N N   . TYR A 1 302 ? -16.174 22.266  -4.905  1.00 54.46  ? 331 TYR A N   1 
ATOM   2355  C CA  . TYR A 1 302 ? -16.141 21.011  -4.175  1.00 52.66  ? 331 TYR A CA  1 
ATOM   2356  C C   . TYR A 1 302 ? -15.429 21.221  -2.841  1.00 50.18  ? 331 TYR A C   1 
ATOM   2357  O O   . TYR A 1 302 ? -15.795 20.607  -1.843  1.00 47.63  ? 331 TYR A O   1 
ATOM   2358  C CB  . TYR A 1 302 ? -15.470 19.903  -4.997  1.00 50.90  ? 331 TYR A CB  1 
ATOM   2359  C CG  . TYR A 1 302 ? -15.290 18.596  -4.261  1.00 47.56  ? 331 TYR A CG  1 
ATOM   2360  C CD1 . TYR A 1 302 ? -14.217 18.402  -3.404  1.00 51.82  ? 331 TYR A CD1 1 
ATOM   2361  C CD2 . TYR A 1 302 ? -16.212 17.568  -4.377  1.00 46.35  ? 331 TYR A CD2 1 
ATOM   2362  C CE1 . TYR A 1 302 ? -14.045 17.214  -2.709  1.00 49.04  ? 331 TYR A CE1 1 
ATOM   2363  C CE2 . TYR A 1 302 ? -16.059 16.375  -3.690  1.00 44.78  ? 331 TYR A CE2 1 
ATOM   2364  C CZ  . TYR A 1 302 ? -14.969 16.197  -2.854  1.00 45.20  ? 331 TYR A CZ  1 
ATOM   2365  O OH  . TYR A 1 302 ? -14.771 15.029  -2.168  1.00 49.87  ? 331 TYR A OH  1 
ATOM   2366  N N   . ILE A 1 303 ? -14.405 22.081  -2.848  1.00 50.86  ? 332 ILE A N   1 
ATOM   2367  C CA  . ILE A 1 303 ? -13.548 22.265  -1.687  1.00 51.01  ? 332 ILE A CA  1 
ATOM   2368  C C   . ILE A 1 303 ? -14.338 22.996  -0.599  1.00 49.64  ? 332 ILE A C   1 
ATOM   2369  O O   . ILE A 1 303 ? -14.199 22.692  0.586   1.00 53.81  ? 332 ILE A O   1 
ATOM   2370  C CB  . ILE A 1 303 ? -12.243 22.996  -2.074  1.00 50.26  ? 332 ILE A CB  1 
ATOM   2371  C CG1 . ILE A 1 303 ? -11.453 22.247  -3.156  1.00 51.05  ? 332 ILE A CG1 1 
ATOM   2372  C CG2 . ILE A 1 303 ? -11.374 23.270  -0.854  1.00 53.20  ? 332 ILE A CG2 1 
ATOM   2373  C CD1 . ILE A 1 303 ? -11.126 20.812  -2.824  1.00 49.47  ? 332 ILE A CD1 1 
ATOM   2374  N N   . TRP A 1 304 ? -15.190 23.942  -1.005  1.00 47.52  ? 333 TRP A N   1 
ATOM   2375  C CA  . TRP A 1 304 ? -15.933 24.749  -0.050  1.00 45.81  ? 333 TRP A CA  1 
ATOM   2376  C C   . TRP A 1 304 ? -17.002 23.909  0.647   1.00 49.00  ? 333 TRP A C   1 
ATOM   2377  O O   . TRP A 1 304 ? -17.224 24.066  1.844   1.00 51.07  ? 333 TRP A O   1 
ATOM   2378  C CB  . TRP A 1 304 ? -16.510 25.993  -0.736  1.00 43.45  ? 333 TRP A CB  1 
ATOM   2379  C CG  . TRP A 1 304 ? -15.628 27.204  -0.654  1.00 37.82  ? 333 TRP A CG  1 
ATOM   2380  C CD1 . TRP A 1 304 ? -15.115 27.943  -1.681  1.00 37.03  ? 333 TRP A CD1 1 
ATOM   2381  C CD2 . TRP A 1 304 ? -15.190 27.845  0.556   1.00 39.49  ? 333 TRP A CD2 1 
ATOM   2382  N NE1 . TRP A 1 304 ? -14.390 29.003  -1.195  1.00 35.81  ? 333 TRP A NE1 1 
ATOM   2383  C CE2 . TRP A 1 304 ? -14.413 28.959  0.173   1.00 39.01  ? 333 TRP A CE2 1 
ATOM   2384  C CE3 . TRP A 1 304 ? -15.382 27.584  1.918   1.00 41.26  ? 333 TRP A CE3 1 
ATOM   2385  C CZ2 . TRP A 1 304 ? -13.818 29.795  1.115   1.00 43.08  ? 333 TRP A CZ2 1 
ATOM   2386  C CZ3 . TRP A 1 304 ? -14.798 28.414  2.848   1.00 44.39  ? 333 TRP A CZ3 1 
ATOM   2387  C CH2 . TRP A 1 304 ? -14.022 29.503  2.447   1.00 44.00  ? 333 TRP A CH2 1 
ATOM   2388  N N   . ASN A 1 305 ? -17.640 23.001  -0.099  1.00 57.26  ? 334 ASN A N   1 
ATOM   2389  C CA  . ASN A 1 305 ? -18.665 22.129  0.452   1.00 60.24  ? 334 ASN A CA  1 
ATOM   2390  C C   . ASN A 1 305 ? -18.009 21.107  1.366   1.00 62.74  ? 334 ASN A C   1 
ATOM   2391  O O   . ASN A 1 305 ? -18.477 20.867  2.476   1.00 69.85  ? 334 ASN A O   1 
ATOM   2392  C CB  . ASN A 1 305 ? -19.474 21.423  -0.636  1.00 62.16  ? 334 ASN A CB  1 
ATOM   2393  C CG  . ASN A 1 305 ? -20.383 22.349  -1.417  1.00 66.21  ? 334 ASN A CG  1 
ATOM   2394  O OD1 . ASN A 1 305 ? -21.091 21.901  -2.317  1.00 75.05  ? 334 ASN A OD1 1 
ATOM   2395  N ND2 . ASN A 1 305 ? -20.384 23.634  -1.093  1.00 63.74  ? 334 ASN A ND2 1 
ATOM   2396  N N   . THR A 1 306 ? -16.915 20.523  0.874   1.00 65.09  ? 335 THR A N   1 
ATOM   2397  C CA  . THR A 1 306 ? -16.081 19.649  1.678   1.00 60.44  ? 335 THR A CA  1 
ATOM   2398  C C   . THR A 1 306 ? -15.911 20.282  3.064   1.00 56.64  ? 335 THR A C   1 
ATOM   2399  O O   . THR A 1 306 ? -16.222 19.659  4.080   1.00 54.89  ? 335 THR A O   1 
ATOM   2400  C CB  . THR A 1 306 ? -14.794 19.331  0.902   1.00 62.52  ? 335 THR A CB  1 
ATOM   2401  O OG1 . THR A 1 306 ? -15.151 18.611  -0.281  1.00 60.35  ? 335 THR A OG1 1 
ATOM   2402  C CG2 . THR A 1 306 ? -13.804 18.512  1.695   1.00 63.12  ? 335 THR A CG2 1 
ATOM   2403  N N   . LEU A 1 307 ? -15.485 21.550  3.091   1.00 52.12  ? 336 LEU A N   1 
ATOM   2404  C CA  . LEU A 1 307 ? -15.200 22.242  4.339   1.00 55.72  ? 336 LEU A CA  1 
ATOM   2405  C C   . LEU A 1 307 ? -16.478 22.496  5.146   1.00 57.11  ? 336 LEU A C   1 
ATOM   2406  O O   . LEU A 1 307 ? -16.420 22.532  6.373   1.00 51.81  ? 336 LEU A O   1 
ATOM   2407  C CB  . LEU A 1 307 ? -14.454 23.548  4.032   1.00 53.72  ? 336 LEU A CB  1 
ATOM   2408  C CG  . LEU A 1 307 ? -12.971 23.395  3.683   1.00 50.61  ? 336 LEU A CG  1 
ATOM   2409  C CD1 . LEU A 1 307 ? -12.316 24.753  3.477   1.00 50.53  ? 336 LEU A CD1 1 
ATOM   2410  C CD2 . LEU A 1 307 ? -12.221 22.600  4.750   1.00 47.06  ? 336 LEU A CD2 1 
ATOM   2411  N N   . ASN A 1 308 ? -17.625 22.652  4.468   1.00 58.26  ? 337 ASN A N   1 
ATOM   2412  C CA  . ASN A 1 308 ? -18.883 22.938  5.144   1.00 60.59  ? 337 ASN A CA  1 
ATOM   2413  C C   . ASN A 1 308 ? -19.469 21.676  5.772   1.00 63.58  ? 337 ASN A C   1 
ATOM   2414  O O   . ASN A 1 308 ? -20.330 21.780  6.640   1.00 68.04  ? 337 ASN A O   1 
ATOM   2415  C CB  . ASN A 1 308 ? -19.918 23.566  4.210   1.00 60.99  ? 337 ASN A CB  1 
ATOM   2416  C CG  . ASN A 1 308 ? -19.403 24.812  3.526   1.00 63.91  ? 337 ASN A CG  1 
ATOM   2417  O OD1 . ASN A 1 308 ? -18.724 25.627  4.145   1.00 63.12  ? 337 ASN A OD1 1 
ATOM   2418  N ND2 . ASN A 1 308 ? -19.691 24.952  2.242   1.00 63.44  ? 337 ASN A ND2 1 
ATOM   2419  N N   . SER A 1 309 ? -19.016 20.492  5.339   1.00 66.22  ? 338 SER A N   1 
ATOM   2420  C CA  . SER A 1 309 ? -19.429 19.243  5.964   1.00 68.58  ? 338 SER A CA  1 
ATOM   2421  C C   . SER A 1 309 ? -18.673 19.016  7.273   1.00 73.72  ? 338 SER A C   1 
ATOM   2422  O O   . SER A 1 309 ? -18.873 17.996  7.933   1.00 72.76  ? 338 SER A O   1 
ATOM   2423  C CB  . SER A 1 309 ? -19.232 18.079  5.028   1.00 69.63  ? 338 SER A CB  1 
ATOM   2424  O OG  . SER A 1 309 ? -19.399 16.832  5.697   1.00 68.81  ? 338 SER A OG  1 
ATOM   2425  N N   . GLY A 1 310 ? -17.794 19.963  7.633   1.00 76.27  ? 339 GLY A N   1 
ATOM   2426  C CA  . GLY A 1 310 ? -16.957 19.835  8.813   1.00 74.77  ? 339 GLY A CA  1 
ATOM   2427  C C   . GLY A 1 310 ? -15.821 18.845  8.575   1.00 72.87  ? 339 GLY A C   1 
ATOM   2428  O O   . GLY A 1 310 ? -15.496 18.057  9.462   1.00 68.61  ? 339 GLY A O   1 
ATOM   2429  N N   . ARG A 1 311 ? -15.240 18.902  7.364   1.00 72.17  ? 340 ARG A N   1 
ATOM   2430  C CA  . ARG A 1 311 ? -14.223 17.955  6.930   1.00 66.56  ? 340 ARG A CA  1 
ATOM   2431  C C   . ARG A 1 311 ? -13.053 18.708  6.288   1.00 62.27  ? 340 ARG A C   1 
ATOM   2432  O O   . ARG A 1 311 ? -13.265 19.633  5.499   1.00 54.40  ? 340 ARG A O   1 
ATOM   2433  C CB  . ARG A 1 311 ? -14.832 16.927  5.965   1.00 67.79  ? 340 ARG A CB  1 
ATOM   2434  C CG  . ARG A 1 311 ? -16.066 16.210  6.497   1.00 71.40  ? 340 ARG A CG  1 
ATOM   2435  C CD  . ARG A 1 311 ? -16.398 14.936  5.737   1.00 74.32  ? 340 ARG A CD  1 
ATOM   2436  N NE  . ARG A 1 311 ? -16.258 15.077  4.292   1.00 76.48  ? 340 ARG A NE  1 
ATOM   2437  C CZ  . ARG A 1 311 ? -17.259 15.038  3.421   1.00 82.74  ? 340 ARG A CZ  1 
ATOM   2438  N NH1 . ARG A 1 311 ? -17.013 15.141  2.126   1.00 84.64  ? 340 ARG A NH1 1 
ATOM   2439  N NH2 . ARG A 1 311 ? -18.503 14.894  3.844   1.00 85.28  ? 340 ARG A NH2 1 
ATOM   2440  N N   . VAL A 1 312 ? -11.822 18.264  6.613   1.00 59.21  ? 341 VAL A N   1 
ATOM   2441  C CA  . VAL A 1 312 ? -10.585 18.883  6.150   1.00 54.69  ? 341 VAL A CA  1 
ATOM   2442  C C   . VAL A 1 312 ? -10.143 18.248  4.830   1.00 47.79  ? 341 VAL A C   1 
ATOM   2443  O O   . VAL A 1 312 ? -10.439 17.088  4.553   1.00 49.05  ? 341 VAL A O   1 
ATOM   2444  C CB  . VAL A 1 312 ? -9.454  18.770  7.197   1.00 57.90  ? 341 VAL A CB  1 
ATOM   2445  C CG1 . VAL A 1 312 ? -9.675  19.691  8.386   1.00 58.60  ? 341 VAL A CG1 1 
ATOM   2446  C CG2 . VAL A 1 312 ? -9.233  17.337  7.672   1.00 59.91  ? 341 VAL A CG2 1 
ATOM   2447  N N   . VAL A 1 313 ? -9.412  19.029  4.031   1.00 39.61  ? 342 VAL A N   1 
ATOM   2448  C CA  . VAL A 1 313 ? -8.762  18.552  2.823   1.00 38.13  ? 342 VAL A CA  1 
ATOM   2449  C C   . VAL A 1 313 ? -7.462  17.850  3.220   1.00 36.79  ? 342 VAL A C   1 
ATOM   2450  O O   . VAL A 1 313 ? -6.524  18.490  3.678   1.00 34.15  ? 342 VAL A O   1 
ATOM   2451  C CB  . VAL A 1 313 ? -8.495  19.732  1.866   1.00 40.47  ? 342 VAL A CB  1 
ATOM   2452  C CG1 . VAL A 1 313 ? -7.625  19.333  0.680   1.00 44.81  ? 342 VAL A CG1 1 
ATOM   2453  C CG2 . VAL A 1 313 ? -9.796  20.362  1.399   1.00 43.53  ? 342 VAL A CG2 1 
ATOM   2454  N N   . PRO A 1 314 ? -7.333  16.520  3.042   1.00 34.66  ? 343 PRO A N   1 
ATOM   2455  C CA  . PRO A 1 314 ? -6.100  15.830  3.439   1.00 31.66  ? 343 PRO A CA  1 
ATOM   2456  C C   . PRO A 1 314 ? -4.845  16.274  2.678   1.00 29.31  ? 343 PRO A C   1 
ATOM   2457  O O   . PRO A 1 314 ? -4.907  16.718  1.525   1.00 27.29  ? 343 PRO A O   1 
ATOM   2458  C CB  . PRO A 1 314 ? -6.436  14.347  3.218   1.00 33.58  ? 343 PRO A CB  1 
ATOM   2459  C CG  . PRO A 1 314 ? -7.612  14.341  2.248   1.00 36.01  ? 343 PRO A CG  1 
ATOM   2460  C CD  . PRO A 1 314 ? -8.372  15.619  2.514   1.00 32.68  ? 343 PRO A CD  1 
ATOM   2461  N N   . GLY A 1 315 ? -3.687  16.145  3.355   1.00 30.41  ? 344 GLY A N   1 
ATOM   2462  C CA  . GLY A 1 315 ? -2.398  16.554  2.820   1.00 26.55  ? 344 GLY A CA  1 
ATOM   2463  C C   . GLY A 1 315 ? -2.131  18.053  2.914   1.00 25.71  ? 344 GLY A C   1 
ATOM   2464  O O   . GLY A 1 315 ? -1.101  18.521  2.436   1.00 25.39  ? 344 GLY A O   1 
ATOM   2465  N N   . TYR A 1 316 ? -3.065  18.788  3.516   1.00 24.80  ? 345 TYR A N   1 
ATOM   2466  C CA  . TYR A 1 316 ? -2.879  20.199  3.797   1.00 26.15  ? 345 TYR A CA  1 
ATOM   2467  C C   . TYR A 1 316 ? -2.844  20.398  5.306   1.00 28.22  ? 345 TYR A C   1 
ATOM   2468  O O   . TYR A 1 316 ? -3.484  19.649  6.031   1.00 33.58  ? 345 TYR A O   1 
ATOM   2469  C CB  . TYR A 1 316 ? -4.006  21.027  3.164   1.00 25.55  ? 345 TYR A CB  1 
ATOM   2470  C CG  . TYR A 1 316 ? -3.826  21.181  1.678   1.00 22.94  ? 345 TYR A CG  1 
ATOM   2471  C CD1 . TYR A 1 316 ? -3.957  20.082  0.848   1.00 24.50  ? 345 TYR A CD1 1 
ATOM   2472  C CD2 . TYR A 1 316 ? -3.391  22.369  1.119   1.00 22.65  ? 345 TYR A CD2 1 
ATOM   2473  C CE1 . TYR A 1 316 ? -3.724  20.170  -0.514  1.00 23.91  ? 345 TYR A CE1 1 
ATOM   2474  C CE2 . TYR A 1 316 ? -3.146  22.470  -0.245  1.00 25.59  ? 345 TYR A CE2 1 
ATOM   2475  C CZ  . TYR A 1 316 ? -3.322  21.366  -1.066  1.00 23.48  ? 345 TYR A CZ  1 
ATOM   2476  O OH  . TYR A 1 316 ? -3.065  21.424  -2.421  1.00 29.27  ? 345 TYR A OH  1 
ATOM   2477  N N   . GLY A 1 317 ? -2.094  21.407  5.763   1.00 31.93  ? 346 GLY A N   1 
ATOM   2478  C CA  . GLY A 1 317 ? -1.923  21.638  7.193   1.00 33.47  ? 346 GLY A CA  1 
ATOM   2479  C C   . GLY A 1 317 ? -0.737  20.859  7.767   1.00 31.05  ? 346 GLY A C   1 
ATOM   2480  O O   . GLY A 1 317 ? -0.196  19.973  7.121   1.00 29.34  ? 346 GLY A O   1 
ATOM   2481  N N   . HIS A 1 318 ? -0.328  21.223  8.984   1.00 32.47  ? 347 HIS A N   1 
ATOM   2482  C CA  . HIS A 1 318 ? 0.809   20.605  9.651   1.00 30.87  ? 347 HIS A CA  1 
ATOM   2483  C C   . HIS A 1 318 ? 0.878   21.094  11.092  1.00 30.39  ? 347 HIS A C   1 
ATOM   2484  O O   . HIS A 1 318 ? 0.419   22.197  11.405  1.00 33.74  ? 347 HIS A O   1 
ATOM   2485  C CB  . HIS A 1 318 ? 2.118   20.918  8.913   1.00 30.14  ? 347 HIS A CB  1 
ATOM   2486  C CG  . HIS A 1 318 ? 3.215   19.958  9.221   1.00 30.80  ? 347 HIS A CG  1 
ATOM   2487  N ND1 . HIS A 1 318 ? 4.159   20.217  10.185  1.00 32.32  ? 347 HIS A ND1 1 
ATOM   2488  C CD2 . HIS A 1 318 ? 3.500   18.742  8.728   1.00 33.63  ? 347 HIS A CD2 1 
ATOM   2489  C CE1 . HIS A 1 318 ? 5.006   19.187  10.244  1.00 34.81  ? 347 HIS A CE1 1 
ATOM   2490  N NE2 . HIS A 1 318 ? 4.622   18.282  9.367   1.00 34.28  ? 347 HIS A NE2 1 
ATOM   2491  N N   . ALA A 1 319 ? 1.497   20.281  11.956  1.00 31.58  ? 348 ALA A N   1 
ATOM   2492  C CA  . ALA A 1 319 ? 1.640   20.610  13.365  1.00 30.55  ? 348 ALA A CA  1 
ATOM   2493  C C   . ALA A 1 319 ? 2.491   21.866  13.547  1.00 28.74  ? 348 ALA A C   1 
ATOM   2494  O O   . ALA A 1 319 ? 2.264   22.619  14.491  1.00 27.60  ? 348 ALA A O   1 
ATOM   2495  C CB  . ALA A 1 319 ? 2.252   19.438  14.090  1.00 31.29  ? 348 ALA A CB  1 
ATOM   2496  N N   . VAL A 1 320 ? 3.476   22.077  12.655  1.00 27.97  ? 349 VAL A N   1 
ATOM   2497  C CA  . VAL A 1 320 ? 4.537   23.050  12.895  1.00 29.14  ? 349 VAL A CA  1 
ATOM   2498  C C   . VAL A 1 320 ? 4.822   23.910  11.661  1.00 29.42  ? 349 VAL A C   1 
ATOM   2499  O O   . VAL A 1 320 ? 5.032   25.122  11.798  1.00 28.82  ? 349 VAL A O   1 
ATOM   2500  C CB  . VAL A 1 320 ? 5.817   22.366  13.419  1.00 29.99  ? 349 VAL A CB  1 
ATOM   2501  C CG1 . VAL A 1 320 ? 5.960   20.940  12.923  1.00 31.28  ? 349 VAL A CG1 1 
ATOM   2502  C CG2 . VAL A 1 320 ? 7.067   23.176  13.115  1.00 27.69  ? 349 VAL A CG2 1 
ATOM   2503  N N   . LEU A 1 321 ? 4.893   23.277  10.485  1.00 26.50  ? 350 LEU A N   1 
ATOM   2504  C CA  . LEU A 1 321 ? 4.982   23.962  9.199   1.00 33.29  ? 350 LEU A CA  1 
ATOM   2505  C C   . LEU A 1 321 ? 3.898   25.031  9.158   1.00 31.50  ? 350 LEU A C   1 
ATOM   2506  O O   . LEU A 1 321 ? 2.734   24.733  9.436   1.00 32.87  ? 350 LEU A O   1 
ATOM   2507  C CB  . LEU A 1 321 ? 4.742   22.941  8.074   1.00 34.19  ? 350 LEU A CB  1 
ATOM   2508  C CG  . LEU A 1 321 ? 5.778   22.781  6.956   1.00 38.18  ? 350 LEU A CG  1 
ATOM   2509  C CD1 . LEU A 1 321 ? 6.966   23.730  7.059   1.00 35.81  ? 350 LEU A CD1 1 
ATOM   2510  C CD2 . LEU A 1 321 ? 6.239   21.334  6.875   1.00 40.85  ? 350 LEU A CD2 1 
ATOM   2511  N N   . ARG A 1 322 ? 4.292   26.262  8.826   1.00 34.27  ? 351 ARG A N   1 
ATOM   2512  C CA  . ARG A 1 322 ? 3.339   27.352  8.672   1.00 37.63  ? 351 ARG A CA  1 
ATOM   2513  C C   . ARG A 1 322 ? 3.305   27.848  7.225   1.00 36.37  ? 351 ARG A C   1 
ATOM   2514  O O   . ARG A 1 322 ? 2.625   28.825  6.931   1.00 39.26  ? 351 ARG A O   1 
ATOM   2515  C CB  . ARG A 1 322 ? 3.693   28.500  9.627   1.00 38.68  ? 351 ARG A CB  1 
ATOM   2516  C CG  . ARG A 1 322 ? 3.460   28.187  11.100  1.00 39.37  ? 351 ARG A CG  1 
ATOM   2517  C CD  . ARG A 1 322 ? 1.988   28.006  11.409  1.00 38.94  ? 351 ARG A CD  1 
ATOM   2518  N NE  . ARG A 1 322 ? 1.717   27.428  12.718  1.00 36.81  ? 351 ARG A NE  1 
ATOM   2519  C CZ  . ARG A 1 322 ? 1.405   26.150  12.932  1.00 39.01  ? 351 ARG A CZ  1 
ATOM   2520  N NH1 . ARG A 1 322 ? 1.025   25.758  14.138  1.00 39.98  ? 351 ARG A NH1 1 
ATOM   2521  N NH2 . ARG A 1 322 ? 1.464   25.266  11.945  1.00 35.01  ? 351 ARG A NH2 1 
ATOM   2522  N N   . LYS A 1 323 ? 4.041   27.186  6.326   1.00 36.95  ? 352 LYS A N   1 
ATOM   2523  C CA  . LYS A 1 323 ? 4.057   27.544  4.911   1.00 38.21  ? 352 LYS A CA  1 
ATOM   2524  C C   . LYS A 1 323 ? 4.248   26.259  4.102   1.00 33.25  ? 352 LYS A C   1 
ATOM   2525  O O   . LYS A 1 323 ? 4.330   25.170  4.670   1.00 33.82  ? 352 LYS A O   1 
ATOM   2526  C CB  . LYS A 1 323 ? 5.082   28.663  4.668   1.00 45.64  ? 352 LYS A CB  1 
ATOM   2527  C CG  . LYS A 1 323 ? 5.837   28.605  3.344   1.00 54.93  ? 352 LYS A CG  1 
ATOM   2528  C CD  . LYS A 1 323 ? 6.231   29.948  2.739   1.00 62.28  ? 352 LYS A CD  1 
ATOM   2529  C CE  . LYS A 1 323 ? 6.666   29.812  1.289   1.00 62.78  ? 352 LYS A CE  1 
ATOM   2530  N NZ  . LYS A 1 323 ? 6.479   31.073  0.531   1.00 64.19  ? 352 LYS A NZ  1 
ATOM   2531  N N   . THR A 1 324 ? 4.199   26.380  2.772   1.00 29.88  ? 353 THR A N   1 
ATOM   2532  C CA  . THR A 1 324 ? 4.377   25.261  1.873   1.00 25.95  ? 353 THR A CA  1 
ATOM   2533  C C   . THR A 1 324 ? 5.590   24.423  2.261   1.00 23.55  ? 353 THR A C   1 
ATOM   2534  O O   . THR A 1 324 ? 6.688   24.917  2.486   1.00 24.63  ? 353 THR A O   1 
ATOM   2535  C CB  . THR A 1 324 ? 4.533   25.714  0.421   1.00 26.26  ? 353 THR A CB  1 
ATOM   2536  O OG1 . THR A 1 324 ? 3.314   26.378  0.079   1.00 28.76  ? 353 THR A OG1 1 
ATOM   2537  C CG2 . THR A 1 324 ? 4.810   24.531  -0.476  1.00 27.31  ? 353 THR A CG2 1 
ATOM   2538  N N   . ASP A 1 325 ? 5.370   23.117  2.318   1.00 23.32  ? 354 ASP A N   1 
ATOM   2539  C CA  . ASP A 1 325 ? 6.427   22.183  2.647   1.00 24.49  ? 354 ASP A CA  1 
ATOM   2540  C C   . ASP A 1 325 ? 7.401   22.063  1.479   1.00 25.03  ? 354 ASP A C   1 
ATOM   2541  O O   . ASP A 1 325 ? 7.015   21.645  0.403   1.00 28.35  ? 354 ASP A O   1 
ATOM   2542  C CB  . ASP A 1 325 ? 5.777   20.838  2.948   1.00 23.45  ? 354 ASP A CB  1 
ATOM   2543  C CG  . ASP A 1 325 ? 6.677   19.766  3.539   1.00 22.89  ? 354 ASP A CG  1 
ATOM   2544  O OD1 . ASP A 1 325 ? 7.906   19.926  3.538   1.00 27.37  ? 354 ASP A OD1 1 
ATOM   2545  O OD2 . ASP A 1 325 ? 6.121   18.774  3.970   1.00 25.08  ? 354 ASP A OD2 1 
ATOM   2546  N N   . PRO A 1 326 ? 8.712   22.345  1.660   1.00 29.13  ? 355 PRO A N   1 
ATOM   2547  C CA  . PRO A 1 326 ? 9.702   22.136  0.597   1.00 26.69  ? 355 PRO A CA  1 
ATOM   2548  C C   . PRO A 1 326 ? 9.791   20.702  0.062   1.00 24.47  ? 355 PRO A C   1 
ATOM   2549  O O   . PRO A 1 326 ? 10.242  20.504  -1.061  1.00 22.44  ? 355 PRO A O   1 
ATOM   2550  C CB  . PRO A 1 326 ? 11.052  22.562  1.215   1.00 28.84  ? 355 PRO A CB  1 
ATOM   2551  C CG  . PRO A 1 326 ? 10.795  22.625  2.728   1.00 30.16  ? 355 PRO A CG  1 
ATOM   2552  C CD  . PRO A 1 326 ? 9.311   22.901  2.883   1.00 29.42  ? 355 PRO A CD  1 
ATOM   2553  N N   . ARG A 1 327 ? 9.288   19.731  0.837   1.00 24.91  ? 356 ARG A N   1 
ATOM   2554  C CA  . ARG A 1 327 ? 9.182   18.354  0.395   1.00 23.21  ? 356 ARG A CA  1 
ATOM   2555  C C   . ARG A 1 327 ? 8.079   18.190  -0.653  1.00 23.49  ? 356 ARG A C   1 
ATOM   2556  O O   . ARG A 1 327 ? 8.244   17.428  -1.597  1.00 25.77  ? 356 ARG A O   1 
ATOM   2557  C CB  . ARG A 1 327 ? 8.951   17.452  1.617   1.00 24.94  ? 356 ARG A CB  1 
ATOM   2558  C CG  . ARG A 1 327 ? 10.097  17.453  2.618   1.00 24.67  ? 356 ARG A CG  1 
ATOM   2559  C CD  . ARG A 1 327 ? 9.774   16.570  3.804   1.00 25.10  ? 356 ARG A CD  1 
ATOM   2560  N NE  . ARG A 1 327 ? 8.681   17.089  4.601   1.00 25.48  ? 356 ARG A NE  1 
ATOM   2561  C CZ  . ARG A 1 327 ? 8.072   16.413  5.575   1.00 27.54  ? 356 ARG A CZ  1 
ATOM   2562  N NH1 . ARG A 1 327 ? 8.481   15.198  5.898   1.00 25.31  ? 356 ARG A NH1 1 
ATOM   2563  N NH2 . ARG A 1 327 ? 7.038   16.938  6.200   1.00 26.63  ? 356 ARG A NH2 1 
ATOM   2564  N N   . TYR A 1 328 ? 6.976   18.938  -0.512  1.00 25.43  ? 357 TYR A N   1 
ATOM   2565  C CA  . TYR A 1 328 ? 5.968   19.000  -1.559  1.00 27.46  ? 357 TYR A CA  1 
ATOM   2566  C C   . TYR A 1 328 ? 6.571   19.655  -2.806  1.00 28.25  ? 357 TYR A C   1 
ATOM   2567  O O   . TYR A 1 328 ? 6.475   19.102  -3.895  1.00 27.97  ? 357 TYR A O   1 
ATOM   2568  C CB  . TYR A 1 328 ? 4.714   19.710  -1.047  1.00 25.76  ? 357 TYR A CB  1 
ATOM   2569  C CG  . TYR A 1 328 ? 3.571   19.837  -2.014  1.00 28.08  ? 357 TYR A CG  1 
ATOM   2570  C CD1 . TYR A 1 328 ? 3.542   20.860  -2.948  1.00 30.96  ? 357 TYR A CD1 1 
ATOM   2571  C CD2 . TYR A 1 328 ? 2.491   18.965  -1.972  1.00 26.33  ? 357 TYR A CD2 1 
ATOM   2572  C CE1 . TYR A 1 328 ? 2.491   20.995  -3.844  1.00 28.40  ? 357 TYR A CE1 1 
ATOM   2573  C CE2 . TYR A 1 328 ? 1.429   19.093  -2.852  1.00 27.21  ? 357 TYR A CE2 1 
ATOM   2574  C CZ  . TYR A 1 328 ? 1.432   20.109  -3.794  1.00 29.18  ? 357 TYR A CZ  1 
ATOM   2575  O OH  . TYR A 1 328 ? 0.364   20.241  -4.656  1.00 27.59  ? 357 TYR A OH  1 
ATOM   2576  N N   . THR A 1 329 ? 7.219   20.814  -2.625  1.00 31.98  ? 358 THR A N   1 
ATOM   2577  C CA  . THR A 1 329 ? 7.752   21.591  -3.734  1.00 30.80  ? 358 THR A CA  1 
ATOM   2578  C C   . THR A 1 329 ? 8.610   20.704  -4.627  1.00 33.62  ? 358 THR A C   1 
ATOM   2579  O O   . THR A 1 329 ? 8.480   20.734  -5.845  1.00 30.59  ? 358 THR A O   1 
ATOM   2580  C CB  . THR A 1 329 ? 8.572   22.793  -3.248  1.00 29.08  ? 358 THR A CB  1 
ATOM   2581  O OG1 . THR A 1 329 ? 7.722   23.616  -2.453  1.00 32.10  ? 358 THR A OG1 1 
ATOM   2582  C CG2 . THR A 1 329 ? 9.154   23.625  -4.364  1.00 28.43  ? 358 THR A CG2 1 
ATOM   2583  N N   . CYS A 1 330 ? 9.499   19.919  -4.006  1.00 33.42  ? 359 CYS A N   1 
ATOM   2584  C CA  . CYS A 1 330 ? 10.502  19.223  -4.772  1.00 32.76  ? 359 CYS A CA  1 
ATOM   2585  C C   . CYS A 1 330 ? 9.839   18.070  -5.513  1.00 29.42  ? 359 CYS A C   1 
ATOM   2586  O O   . CYS A 1 330 ? 10.253  17.737  -6.614  1.00 30.86  ? 359 CYS A O   1 
ATOM   2587  C CB  . CYS A 1 330 ? 11.676  18.816  -3.892  1.00 37.13  ? 359 CYS A CB  1 
ATOM   2588  S SG  . CYS A 1 330 ? 11.407  17.316  -2.916  1.00 44.25  ? 359 CYS A SG  1 
ATOM   2589  N N   . GLN A 1 331 ? 8.772   17.505  -4.934  1.00 27.11  ? 360 GLN A N   1 
ATOM   2590  C CA  . GLN A 1 331 ? 8.034   16.437  -5.591  1.00 29.12  ? 360 GLN A CA  1 
ATOM   2591  C C   . GLN A 1 331 ? 7.304   16.997  -6.815  1.00 30.86  ? 360 GLN A C   1 
ATOM   2592  O O   . GLN A 1 331 ? 7.254   16.354  -7.862  1.00 33.97  ? 360 GLN A O   1 
ATOM   2593  C CB  . GLN A 1 331 ? 7.079   15.778  -4.601  1.00 29.01  ? 360 GLN A CB  1 
ATOM   2594  C CG  . GLN A 1 331 ? 7.796   14.830  -3.657  1.00 32.69  ? 360 GLN A CG  1 
ATOM   2595  C CD  . GLN A 1 331 ? 6.868   14.150  -2.679  1.00 29.25  ? 360 GLN A CD  1 
ATOM   2596  O OE1 . GLN A 1 331 ? 6.279   14.777  -1.807  1.00 30.64  ? 360 GLN A OE1 1 
ATOM   2597  N NE2 . GLN A 1 331 ? 6.761   12.839  -2.802  1.00 33.10  ? 360 GLN A NE2 1 
ATOM   2598  N N   . ARG A 1 332 ? 6.761   18.210  -6.663  1.00 33.43  ? 361 ARG A N   1 
ATOM   2599  C CA  . ARG A 1 332 ? 6.072   18.904  -7.740  1.00 34.04  ? 361 ARG A CA  1 
ATOM   2600  C C   . ARG A 1 332 ? 7.031   19.175  -8.894  1.00 33.43  ? 361 ARG A C   1 
ATOM   2601  O O   . ARG A 1 332 ? 6.673   18.980  -10.048 1.00 31.48  ? 361 ARG A O   1 
ATOM   2602  C CB  . ARG A 1 332 ? 5.493   20.223  -7.232  1.00 37.23  ? 361 ARG A CB  1 
ATOM   2603  C CG  . ARG A 1 332 ? 4.748   21.027  -8.285  1.00 37.62  ? 361 ARG A CG  1 
ATOM   2604  C CD  . ARG A 1 332 ? 4.404   22.425  -7.814  1.00 39.35  ? 361 ARG A CD  1 
ATOM   2605  N NE  . ARG A 1 332 ? 4.026   23.261  -8.947  1.00 40.42  ? 361 ARG A NE  1 
ATOM   2606  C CZ  . ARG A 1 332 ? 2.949   23.079  -9.703  1.00 41.18  ? 361 ARG A CZ  1 
ATOM   2607  N NH1 . ARG A 1 332 ? 2.021   22.203  -9.352  1.00 36.08  ? 361 ARG A NH1 1 
ATOM   2608  N NH2 . ARG A 1 332 ? 2.792   23.807  -10.797 1.00 42.21  ? 361 ARG A NH2 1 
ATOM   2609  N N   . GLU A 1 333 ? 8.229   19.682  -8.576  1.00 34.81  ? 362 GLU A N   1 
ATOM   2610  C CA  . GLU A 1 333 ? 9.234   19.917  -9.597  1.00 33.11  ? 362 GLU A CA  1 
ATOM   2611  C C   . GLU A 1 333 ? 9.489   18.616  -10.346 1.00 32.02  ? 362 GLU A C   1 
ATOM   2612  O O   . GLU A 1 333 ? 9.569   18.617  -11.576 1.00 33.89  ? 362 GLU A O   1 
ATOM   2613  C CB  . GLU A 1 333 ? 10.516  20.478  -8.986  1.00 38.16  ? 362 GLU A CB  1 
ATOM   2614  C CG  . GLU A 1 333 ? 10.376  21.907  -8.488  1.00 40.94  ? 362 GLU A CG  1 
ATOM   2615  C CD  . GLU A 1 333 ? 11.509  22.377  -7.588  1.00 45.22  ? 362 GLU A CD  1 
ATOM   2616  O OE1 . GLU A 1 333 ? 12.478  21.596  -7.395  1.00 46.94  ? 362 GLU A OE1 1 
ATOM   2617  O OE2 . GLU A 1 333 ? 11.411  23.511  -7.060  1.00 41.97  ? 362 GLU A OE2 1 
ATOM   2618  N N   . PHE A 1 334 ? 9.573   17.500  -9.613  1.00 28.61  ? 363 PHE A N   1 
ATOM   2619  C CA  . PHE A 1 334 ? 9.871   16.231  -10.245 1.00 27.89  ? 363 PHE A CA  1 
ATOM   2620  C C   . PHE A 1 334 ? 8.746   15.870  -11.203 1.00 30.59  ? 363 PHE A C   1 
ATOM   2621  O O   . PHE A 1 334 ? 9.016   15.455  -12.328 1.00 34.75  ? 363 PHE A O   1 
ATOM   2622  C CB  . PHE A 1 334 ? 10.039  15.139  -9.190  1.00 27.53  ? 363 PHE A CB  1 
ATOM   2623  C CG  . PHE A 1 334 ? 10.407  13.782  -9.713  1.00 25.24  ? 363 PHE A CG  1 
ATOM   2624  C CD1 . PHE A 1 334 ? 9.447   12.907  -10.197 1.00 23.39  ? 363 PHE A CD1 1 
ATOM   2625  C CD2 . PHE A 1 334 ? 11.722  13.367  -9.667  1.00 25.23  ? 363 PHE A CD2 1 
ATOM   2626  C CE1 . PHE A 1 334 ? 9.801   11.651  -10.646 1.00 24.78  ? 363 PHE A CE1 1 
ATOM   2627  C CE2 . PHE A 1 334 ? 12.076  12.110  -10.128 1.00 27.26  ? 363 PHE A CE2 1 
ATOM   2628  C CZ  . PHE A 1 334 ? 11.119  11.266  -10.635 1.00 26.33  ? 363 PHE A CZ  1 
ATOM   2629  N N   . ALA A 1 335 ? 7.508   16.034  -10.720 1.00 29.96  ? 364 ALA A N   1 
ATOM   2630  C CA  . ALA A 1 335 ? 6.280   15.715  -11.438 1.00 33.82  ? 364 ALA A CA  1 
ATOM   2631  C C   . ALA A 1 335 ? 6.155   16.463  -12.766 1.00 33.68  ? 364 ALA A C   1 
ATOM   2632  O O   . ALA A 1 335 ? 5.642   15.906  -13.730 1.00 34.11  ? 364 ALA A O   1 
ATOM   2633  C CB  . ALA A 1 335 ? 5.093   16.055  -10.570 1.00 33.71  ? 364 ALA A CB  1 
ATOM   2634  N N   . LEU A 1 336 ? 6.533   17.745  -12.774 1.00 36.08  ? 365 LEU A N   1 
ATOM   2635  C CA  . LEU A 1 336 ? 6.209   18.613  -13.900 1.00 41.27  ? 365 LEU A CA  1 
ATOM   2636  C C   . LEU A 1 336 ? 7.315   18.561  -14.947 1.00 44.98  ? 365 LEU A C   1 
ATOM   2637  O O   . LEU A 1 336 ? 7.090   18.989  -16.081 1.00 41.76  ? 365 LEU A O   1 
ATOM   2638  C CB  . LEU A 1 336 ? 5.929   20.045  -13.433 1.00 45.66  ? 365 LEU A CB  1 
ATOM   2639  C CG  . LEU A 1 336 ? 7.031   20.759  -12.657 1.00 46.21  ? 365 LEU A CG  1 
ATOM   2640  C CD1 . LEU A 1 336 ? 8.069   21.352  -13.595 1.00 49.22  ? 365 LEU A CD1 1 
ATOM   2641  C CD2 . LEU A 1 336 ? 6.434   21.843  -11.765 1.00 49.05  ? 365 LEU A CD2 1 
ATOM   2642  N N   . LYS A 1 337 ? 8.477   17.994  -14.579 1.00 44.06  ? 366 LYS A N   1 
ATOM   2643  C CA  . LYS A 1 337 ? 9.526   17.761  -15.551 1.00 44.56  ? 366 LYS A CA  1 
ATOM   2644  C C   . LYS A 1 337 ? 9.566   16.284  -15.936 1.00 42.60  ? 366 LYS A C   1 
ATOM   2645  O O   . LYS A 1 337 ? 10.312  15.942  -16.845 1.00 51.12  ? 366 LYS A O   1 
ATOM   2646  C CB  . LYS A 1 337 ? 10.883  18.273  -15.054 1.00 49.54  ? 366 LYS A CB  1 
ATOM   2647  C CG  . LYS A 1 337 ? 11.747  17.275  -14.293 1.00 57.23  ? 366 LYS A CG  1 
ATOM   2648  C CD  . LYS A 1 337 ? 13.238  17.450  -14.531 1.00 58.97  ? 366 LYS A CD  1 
ATOM   2649  C CE  . LYS A 1 337 ? 13.686  16.976  -15.902 1.00 59.44  ? 366 LYS A CE  1 
ATOM   2650  N NZ  . LYS A 1 337 ? 15.162  16.849  -15.998 1.00 57.77  ? 366 LYS A NZ  1 
ATOM   2651  N N   . HIS A 1 338 ? 8.748   15.431  -15.293 1.00 41.45  ? 367 HIS A N   1 
ATOM   2652  C CA  . HIS A 1 338 ? 8.764   13.998  -15.570 1.00 38.94  ? 367 HIS A CA  1 
ATOM   2653  C C   . HIS A 1 338 ? 7.415   13.403  -15.978 1.00 36.92  ? 367 HIS A C   1 
ATOM   2654  O O   . HIS A 1 338 ? 7.430   12.461  -16.754 1.00 40.49  ? 367 HIS A O   1 
ATOM   2655  C CB  . HIS A 1 338 ? 9.377   13.191  -14.417 1.00 43.36  ? 367 HIS A CB  1 
ATOM   2656  C CG  . HIS A 1 338 ? 10.844  13.442  -14.271 1.00 43.71  ? 367 HIS A CG  1 
ATOM   2657  N ND1 . HIS A 1 338 ? 11.697  13.437  -15.354 1.00 43.23  ? 367 HIS A ND1 1 
ATOM   2658  C CD2 . HIS A 1 338 ? 11.588  13.755  -13.207 1.00 46.30  ? 367 HIS A CD2 1 
ATOM   2659  C CE1 . HIS A 1 338 ? 12.927  13.701  -14.938 1.00 49.95  ? 367 HIS A CE1 1 
ATOM   2660  N NE2 . HIS A 1 338 ? 12.884  13.897  -13.632 1.00 48.02  ? 367 HIS A NE2 1 
ATOM   2661  N N   . LEU A 1 339 ? 6.273   13.876  -15.458 1.00 34.79  ? 368 LEU A N   1 
ATOM   2662  C CA  . LEU A 1 339 ? 4.991   13.298  -15.835 1.00 34.90  ? 368 LEU A CA  1 
ATOM   2663  C C   . LEU A 1 339 ? 3.887   14.354  -15.867 1.00 35.92  ? 368 LEU A C   1 
ATOM   2664  O O   . LEU A 1 339 ? 2.776   14.132  -15.366 1.00 33.38  ? 368 LEU A O   1 
ATOM   2665  C CB  . LEU A 1 339 ? 4.628   12.156  -14.876 1.00 34.73  ? 368 LEU A CB  1 
ATOM   2666  C CG  . LEU A 1 339 ? 4.533   12.478  -13.383 1.00 32.72  ? 368 LEU A CG  1 
ATOM   2667  C CD1 . LEU A 1 339 ? 3.425   11.660  -12.722 1.00 32.27  ? 368 LEU A CD1 1 
ATOM   2668  C CD2 . LEU A 1 339 ? 5.866   12.224  -12.675 1.00 35.28  ? 368 LEU A CD2 1 
ATOM   2669  N N   . PRO A 1 340 ? 4.127   15.510  -16.527 1.00 40.51  ? 369 PRO A N   1 
ATOM   2670  C CA  . PRO A 1 340 ? 3.242   16.671  -16.407 1.00 41.35  ? 369 PRO A CA  1 
ATOM   2671  C C   . PRO A 1 340 ? 1.802   16.410  -16.848 1.00 41.14  ? 369 PRO A C   1 
ATOM   2672  O O   . PRO A 1 340 ? 0.893   17.060  -16.349 1.00 37.11  ? 369 PRO A O   1 
ATOM   2673  C CB  . PRO A 1 340 ? 3.909   17.728  -17.293 1.00 37.56  ? 369 PRO A CB  1 
ATOM   2674  C CG  . PRO A 1 340 ? 4.723   16.927  -18.276 1.00 37.81  ? 369 PRO A CG  1 
ATOM   2675  C CD  . PRO A 1 340 ? 5.229   15.754  -17.465 1.00 42.03  ? 369 PRO A CD  1 
ATOM   2676  N N   . ASN A 1 341 ? 1.615   15.428  -17.743 1.00 42.30  ? 370 ASN A N   1 
ATOM   2677  C CA  . ASN A 1 341 ? 0.321   15.144  -18.343 1.00 44.37  ? 370 ASN A CA  1 
ATOM   2678  C C   . ASN A 1 341 ? -0.334  13.925  -17.692 1.00 45.39  ? 370 ASN A C   1 
ATOM   2679  O O   . ASN A 1 341 ? -1.165  13.255  -18.312 1.00 47.18  ? 370 ASN A O   1 
ATOM   2680  C CB  . ASN A 1 341 ? 0.460   14.941  -19.855 1.00 46.57  ? 370 ASN A CB  1 
ATOM   2681  C CG  . ASN A 1 341 ? 1.103   16.128  -20.544 1.00 48.11  ? 370 ASN A CG  1 
ATOM   2682  O OD1 . ASN A 1 341 ? 0.726   17.270  -20.289 1.00 44.30  ? 370 ASN A OD1 1 
ATOM   2683  N ND2 . ASN A 1 341 ? 2.079   15.878  -21.403 1.00 50.53  ? 370 ASN A ND2 1 
ATOM   2684  N N   . ASP A 1 342 ? 0.023   13.632  -16.433 1.00 39.55  ? 371 ASP A N   1 
ATOM   2685  C CA  . ASP A 1 342 ? -0.639  12.546  -15.727 1.00 38.50  ? 371 ASP A CA  1 
ATOM   2686  C C   . ASP A 1 342 ? -1.975  13.098  -15.228 1.00 38.00  ? 371 ASP A C   1 
ATOM   2687  O O   . ASP A 1 342 ? -2.009  14.224  -14.749 1.00 36.72  ? 371 ASP A O   1 
ATOM   2688  C CB  . ASP A 1 342 ? 0.268   11.992  -14.622 1.00 35.75  ? 371 ASP A CB  1 
ATOM   2689  C CG  . ASP A 1 342 ? -0.372  10.958  -13.713 1.00 36.47  ? 371 ASP A CG  1 
ATOM   2690  O OD1 . ASP A 1 342 ? -0.482  9.787   -14.131 1.00 41.24  ? 371 ASP A OD1 1 
ATOM   2691  O OD2 . ASP A 1 342 ? -0.769  11.331  -12.602 1.00 37.12  ? 371 ASP A OD2 1 
ATOM   2692  N N   . PRO A 1 343 ? -3.119  12.393  -15.404 1.00 38.32  ? 372 PRO A N   1 
ATOM   2693  C CA  . PRO A 1 343 ? -4.400  12.847  -14.847 1.00 38.15  ? 372 PRO A CA  1 
ATOM   2694  C C   . PRO A 1 343 ? -4.407  13.143  -13.343 1.00 39.74  ? 372 PRO A C   1 
ATOM   2695  O O   . PRO A 1 343 ? -4.779  14.241  -12.918 1.00 38.08  ? 372 PRO A O   1 
ATOM   2696  C CB  . PRO A 1 343 ? -5.343  11.673  -15.156 1.00 38.99  ? 372 PRO A CB  1 
ATOM   2697  C CG  . PRO A 1 343 ? -4.763  11.041  -16.397 1.00 40.36  ? 372 PRO A CG  1 
ATOM   2698  C CD  . PRO A 1 343 ? -3.262  11.194  -16.247 1.00 39.86  ? 372 PRO A CD  1 
ATOM   2699  N N   . MET A 1 344 ? -3.978  12.163  -12.537 1.00 36.44  ? 373 MET A N   1 
ATOM   2700  C CA  . MET A 1 344 ? -3.968  12.301  -11.088 1.00 38.26  ? 373 MET A CA  1 
ATOM   2701  C C   . MET A 1 344 ? -3.053  13.455  -10.689 1.00 35.79  ? 373 MET A C   1 
ATOM   2702  O O   . MET A 1 344 ? -3.391  14.228  -9.803  1.00 34.93  ? 373 MET A O   1 
ATOM   2703  C CB  . MET A 1 344 ? -3.492  11.014  -10.405 1.00 40.45  ? 373 MET A CB  1 
ATOM   2704  C CG  . MET A 1 344 ? -4.516  9.889   -10.444 1.00 45.71  ? 373 MET A CG  1 
ATOM   2705  S SD  . MET A 1 344 ? -5.930  10.101  -9.310  1.00 57.07  ? 373 MET A SD  1 
ATOM   2706  C CE  . MET A 1 344 ? -5.098  10.258  -7.729  1.00 55.80  ? 373 MET A CE  1 
ATOM   2707  N N   . PHE A 1 345 ? -1.903  13.604  -11.352 1.00 34.42  ? 374 PHE A N   1 
ATOM   2708  C CA  . PHE A 1 345 ? -1.019  14.698  -10.989 1.00 32.72  ? 374 PHE A CA  1 
ATOM   2709  C C   . PHE A 1 345 ? -1.653  16.049  -11.334 1.00 35.95  ? 374 PHE A C   1 
ATOM   2710  O O   . PHE A 1 345 ? -1.368  17.041  -10.658 1.00 32.12  ? 374 PHE A O   1 
ATOM   2711  C CB  . PHE A 1 345 ? 0.360   14.587  -11.636 1.00 34.46  ? 374 PHE A CB  1 
ATOM   2712  C CG  . PHE A 1 345 ? 1.051   15.922  -11.681 1.00 36.17  ? 374 PHE A CG  1 
ATOM   2713  C CD1 . PHE A 1 345 ? 1.322   16.610  -10.511 1.00 40.19  ? 374 PHE A CD1 1 
ATOM   2714  C CD2 . PHE A 1 345 ? 1.341   16.538  -12.888 1.00 39.11  ? 374 PHE A CD2 1 
ATOM   2715  C CE1 . PHE A 1 345 ? 1.899   17.870  -10.550 1.00 40.98  ? 374 PHE A CE1 1 
ATOM   2716  C CE2 . PHE A 1 345 ? 1.910   17.800  -12.926 1.00 37.34  ? 374 PHE A CE2 1 
ATOM   2717  C CZ  . PHE A 1 345 ? 2.198   18.460  -11.757 1.00 41.69  ? 374 PHE A CZ  1 
ATOM   2718  N N   . LYS A 1 346 ? -2.459  16.102  -12.415 1.00 36.82  ? 375 LYS A N   1 
ATOM   2719  C CA  . LYS A 1 346 ? -3.078  17.358  -12.830 1.00 38.18  ? 375 LYS A CA  1 
ATOM   2720  C C   . LYS A 1 346 ? -4.024  17.848  -11.741 1.00 32.63  ? 375 LYS A C   1 
ATOM   2721  O O   . LYS A 1 346 ? -4.095  19.049  -11.488 1.00 31.55  ? 375 LYS A O   1 
ATOM   2722  C CB  . LYS A 1 346 ? -3.774  17.239  -14.192 1.00 43.99  ? 375 LYS A CB  1 
ATOM   2723  C CG  . LYS A 1 346 ? -2.872  17.560  -15.377 1.00 51.62  ? 375 LYS A CG  1 
ATOM   2724  C CD  . LYS A 1 346 ? -3.548  17.572  -16.737 1.00 53.48  ? 375 LYS A CD  1 
ATOM   2725  C CE  . LYS A 1 346 ? -3.467  16.246  -17.466 1.00 58.22  ? 375 LYS A CE  1 
ATOM   2726  N NZ  . LYS A 1 346 ? -3.812  16.386  -18.905 1.00 59.15  ? 375 LYS A NZ  1 
ATOM   2727  N N   . LEU A 1 347 ? -4.706  16.914  -11.071 1.00 30.42  ? 376 LEU A N   1 
ATOM   2728  C CA  . LEU A 1 347 ? -5.627  17.257  -10.001 1.00 33.26  ? 376 LEU A CA  1 
ATOM   2729  C C   . LEU A 1 347 ? -4.849  17.843  -8.818  1.00 31.10  ? 376 LEU A C   1 
ATOM   2730  O O   . LEU A 1 347 ? -5.191  18.903  -8.308  1.00 33.22  ? 376 LEU A O   1 
ATOM   2731  C CB  . LEU A 1 347 ? -6.412  16.001  -9.608  1.00 34.57  ? 376 LEU A CB  1 
ATOM   2732  C CG  . LEU A 1 347 ? -7.395  16.182  -8.456  1.00 36.28  ? 376 LEU A CG  1 
ATOM   2733  C CD1 . LEU A 1 347 ? -8.405  17.287  -8.767  1.00 38.15  ? 376 LEU A CD1 1 
ATOM   2734  C CD2 . LEU A 1 347 ? -8.109  14.879  -8.137  1.00 36.05  ? 376 LEU A CD2 1 
ATOM   2735  N N   . VAL A 1 348 ? -3.751  17.167  -8.435  1.00 29.10  ? 377 VAL A N   1 
ATOM   2736  C CA  . VAL A 1 348 ? -2.922  17.563  -7.313  1.00 24.92  ? 377 VAL A CA  1 
ATOM   2737  C C   . VAL A 1 348 ? -2.453  19.004  -7.502  1.00 25.67  ? 377 VAL A C   1 
ATOM   2738  O O   . VAL A 1 348 ? -2.466  19.797  -6.561  1.00 29.46  ? 377 VAL A O   1 
ATOM   2739  C CB  . VAL A 1 348 ? -1.757  16.560  -7.152  1.00 24.73  ? 377 VAL A CB  1 
ATOM   2740  C CG1 . VAL A 1 348 ? -0.736  17.017  -6.121  1.00 24.68  ? 377 VAL A CG1 1 
ATOM   2741  C CG2 . VAL A 1 348 ? -2.275  15.170  -6.807  1.00 24.91  ? 377 VAL A CG2 1 
ATOM   2742  N N   . ALA A 1 349 ? -2.070  19.330  -8.735  1.00 27.86  ? 378 ALA A N   1 
ATOM   2743  C CA  . ALA A 1 349 ? -1.602  20.659  -9.090  1.00 28.64  ? 378 ALA A CA  1 
ATOM   2744  C C   . ALA A 1 349 ? -2.768  21.630  -9.057  1.00 32.96  ? 378 ALA A C   1 
ATOM   2745  O O   . ALA A 1 349 ? -2.589  22.774  -8.662  1.00 29.92  ? 378 ALA A O   1 
ATOM   2746  C CB  . ALA A 1 349 ? -0.986  20.649  -10.463 1.00 28.87  ? 378 ALA A CB  1 
ATOM   2747  N N   . GLN A 1 350 ? -3.932  21.157  -9.525  1.00 36.68  ? 379 GLN A N   1 
ATOM   2748  C CA  . GLN A 1 350 ? -5.113  22.000  -9.632  1.00 37.05  ? 379 GLN A CA  1 
ATOM   2749  C C   . GLN A 1 350 ? -5.513  22.416  -8.220  1.00 34.22  ? 379 GLN A C   1 
ATOM   2750  O O   . GLN A 1 350 ? -5.815  23.581  -7.988  1.00 34.12  ? 379 GLN A O   1 
ATOM   2751  C CB  . GLN A 1 350 ? -6.222  21.296  -10.422 1.00 36.22  ? 379 GLN A CB  1 
ATOM   2752  C CG  . GLN A 1 350 ? -7.162  22.284  -11.117 1.00 37.06  ? 379 GLN A CG  1 
ATOM   2753  C CD  . GLN A 1 350 ? -8.449  21.707  -11.663 1.00 36.93  ? 379 GLN A CD  1 
ATOM   2754  O OE1 . GLN A 1 350 ? -8.628  20.496  -11.795 1.00 37.12  ? 379 GLN A OE1 1 
ATOM   2755  N NE2 . GLN A 1 350 ? -9.373  22.594  -12.001 1.00 37.78  ? 379 GLN A NE2 1 
ATOM   2756  N N   . LEU A 1 351 ? -5.401  21.492  -7.255  1.00 33.42  ? 380 LEU A N   1 
ATOM   2757  C CA  . LEU A 1 351 ? -5.639  21.813  -5.847  1.00 31.59  ? 380 LEU A CA  1 
ATOM   2758  C C   . LEU A 1 351 ? -4.570  22.772  -5.304  1.00 32.20  ? 380 LEU A C   1 
ATOM   2759  O O   . LEU A 1 351 ? -4.838  23.552  -4.390  1.00 28.19  ? 380 LEU A O   1 
ATOM   2760  C CB  . LEU A 1 351 ? -5.638  20.515  -5.043  1.00 32.32  ? 380 LEU A CB  1 
ATOM   2761  C CG  . LEU A 1 351 ? -6.719  19.514  -5.422  1.00 32.01  ? 380 LEU A CG  1 
ATOM   2762  C CD1 . LEU A 1 351 ? -6.384  18.134  -4.896  1.00 31.75  ? 380 LEU A CD1 1 
ATOM   2763  C CD2 . LEU A 1 351 ? -8.058  19.962  -4.892  1.00 34.77  ? 380 LEU A CD2 1 
ATOM   2764  N N   . TYR A 1 352 ? -3.343  22.679  -5.837  1.00 30.47  ? 381 TYR A N   1 
ATOM   2765  C CA  . TYR A 1 352 ? -2.263  23.542  -5.397  1.00 33.35  ? 381 TYR A CA  1 
ATOM   2766  C C   . TYR A 1 352 ? -2.615  25.016  -5.636  1.00 36.32  ? 381 TYR A C   1 
ATOM   2767  O O   . TYR A 1 352 ? -2.276  25.866  -4.811  1.00 34.05  ? 381 TYR A O   1 
ATOM   2768  C CB  . TYR A 1 352 ? -0.942  23.095  -6.029  1.00 34.63  ? 381 TYR A CB  1 
ATOM   2769  C CG  . TYR A 1 352 ? 0.270   23.866  -5.580  1.00 34.41  ? 381 TYR A CG  1 
ATOM   2770  C CD1 . TYR A 1 352 ? 0.388   24.314  -4.276  1.00 33.71  ? 381 TYR A CD1 1 
ATOM   2771  C CD2 . TYR A 1 352 ? 1.310   24.132  -6.455  1.00 34.28  ? 381 TYR A CD2 1 
ATOM   2772  C CE1 . TYR A 1 352 ? 1.484   25.047  -3.863  1.00 36.96  ? 381 TYR A CE1 1 
ATOM   2773  C CE2 . TYR A 1 352 ? 2.425   24.853  -6.053  1.00 36.23  ? 381 TYR A CE2 1 
ATOM   2774  C CZ  . TYR A 1 352 ? 2.514   25.306  -4.747  1.00 35.32  ? 381 TYR A CZ  1 
ATOM   2775  O OH  . TYR A 1 352 ? 3.601   26.018  -4.307  1.00 44.08  ? 381 TYR A OH  1 
ATOM   2776  N N   . LYS A 1 353 ? -3.308  25.309  -6.722  1.00 38.17  ? 382 LYS A N   1 
ATOM   2777  C CA  . LYS A 1 353 ? -3.583  26.741  -6.996  1.00 42.20  ? 382 LYS A CA  1 
ATOM   2778  C C   . LYS A 1 353 ? -4.840  27.197  -6.250  1.00 40.80  ? 382 LYS A C   1 
ATOM   2779  O O   . LYS A 1 353 ? -4.913  28.380  -5.889  1.00 41.69  ? 382 LYS A O   1 
ATOM   2780  C CB  . LYS A 1 353 ? -3.821  26.979  -8.491  1.00 49.45  ? 382 LYS A CB  1 
ATOM   2781  C CG  . LYS A 1 353 ? -3.833  25.771  -9.397  1.00 52.55  ? 382 LYS A CG  1 
ATOM   2782  C CD  . LYS A 1 353 ? -4.907  25.922  -10.466 1.00 58.35  ? 382 LYS A CD  1 
ATOM   2783  C CE  . LYS A 1 353 ? -5.243  27.353  -10.733 1.00 62.13  ? 382 LYS A CE  1 
ATOM   2784  N NZ  . LYS A 1 353 ? -5.263  27.662  -12.166 1.00 62.27  ? 382 LYS A NZ  1 
ATOM   2785  N N   . ILE A 1 354 ? -5.746  26.275  -5.962  1.00 36.86  ? 383 ILE A N   1 
ATOM   2786  C CA  . ILE A 1 354 ? -7.074  26.658  -5.409  1.00 36.17  ? 383 ILE A CA  1 
ATOM   2787  C C   . ILE A 1 354 ? -7.175  26.453  -3.892  1.00 36.99  ? 383 ILE A C   1 
ATOM   2788  O O   . ILE A 1 354 ? -7.718  27.334  -3.210  1.00 34.70  ? 383 ILE A O   1 
ATOM   2789  C CB  . ILE A 1 354 ? -8.126  25.825  -6.163  1.00 37.40  ? 383 ILE A CB  1 
ATOM   2790  C CG1 . ILE A 1 354 ? -8.330  26.346  -7.582  1.00 38.54  ? 383 ILE A CG1 1 
ATOM   2791  C CG2 . ILE A 1 354 ? -9.445  25.729  -5.396  1.00 42.06  ? 383 ILE A CG2 1 
ATOM   2792  C CD1 . ILE A 1 354 ? -8.580  25.257  -8.607  1.00 41.29  ? 383 ILE A CD1 1 
ATOM   2793  N N   . VAL A 1 355 ? -6.686  25.332  -3.380  1.00 34.25  ? 384 VAL A N   1 
ATOM   2794  C CA  . VAL A 1 355 ? -6.908  25.037  -1.935  1.00 34.24  ? 384 VAL A CA  1 
ATOM   2795  C C   . VAL A 1 355 ? -6.233  26.091  -1.038  1.00 36.51  ? 384 VAL A C   1 
ATOM   2796  O O   . VAL A 1 355 ? -6.862  26.483  -0.061  1.00 37.30  ? 384 VAL A O   1 
ATOM   2797  C CB  . VAL A 1 355 ? -6.522  23.589  -1.558  1.00 32.40  ? 384 VAL A CB  1 
ATOM   2798  C CG1 . VAL A 1 355 ? -6.735  23.308  -0.077  1.00 28.87  ? 384 VAL A CG1 1 
ATOM   2799  C CG2 . VAL A 1 355 ? -7.291  22.582  -2.398  1.00 35.96  ? 384 VAL A CG2 1 
ATOM   2800  N N   . PRO A 1 356 ? -4.993  26.561  -1.273  1.00 38.70  ? 385 PRO A N   1 
ATOM   2801  C CA  . PRO A 1 356 ? -4.433  27.555  -0.370  1.00 44.69  ? 385 PRO A CA  1 
ATOM   2802  C C   . PRO A 1 356 ? -5.274  28.825  -0.155  1.00 46.95  ? 385 PRO A C   1 
ATOM   2803  O O   . PRO A 1 356 ? -5.332  29.247  1.006   1.00 45.01  ? 385 PRO A O   1 
ATOM   2804  C CB  . PRO A 1 356 ? -3.072  27.821  -0.998  1.00 42.48  ? 385 PRO A CB  1 
ATOM   2805  C CG  . PRO A 1 356 ? -2.721  26.506  -1.642  1.00 40.15  ? 385 PRO A CG  1 
ATOM   2806  C CD  . PRO A 1 356 ? -4.041  26.096  -2.255  1.00 40.58  ? 385 PRO A CD  1 
ATOM   2807  N N   . ASN A 1 357 ? -5.872  29.400  -1.200  1.00 48.90  ? 386 ASN A N   1 
ATOM   2808  C CA  . ASN A 1 357 ? -6.760  30.598  -1.063  1.00 51.84  ? 386 ASN A CA  1 
ATOM   2809  C C   . ASN A 1 357 ? -7.973  30.204  -0.219  1.00 47.12  ? 386 ASN A C   1 
ATOM   2810  O O   . ASN A 1 357 ? -8.295  30.961  0.691   1.00 51.07  ? 386 ASN A O   1 
ATOM   2811  C CB  . ASN A 1 357 ? -7.044  31.241  -2.416  1.00 58.06  ? 386 ASN A CB  1 
ATOM   2812  C CG  . ASN A 1 357 ? -8.396  30.891  -2.995  1.00 70.01  ? 386 ASN A CG  1 
ATOM   2813  O OD1 . ASN A 1 357 ? -9.351  31.667  -2.869  1.00 69.97  ? 386 ASN A OD1 1 
ATOM   2814  N ND2 . ASN A 1 357 ? -8.497  29.753  -3.665  1.00 71.09  ? 386 ASN A ND2 1 
ATOM   2815  N N   . VAL A 1 358 ? -8.588  29.054  -0.478  1.00 41.47  ? 387 VAL A N   1 
ATOM   2816  C CA  . VAL A 1 358 ? -9.633  28.555  0.451   1.00 42.97  ? 387 VAL A CA  1 
ATOM   2817  C C   . VAL A 1 358 ? -8.857  28.192  1.737   1.00 53.12  ? 387 VAL A C   1 
ATOM   2818  O O   . VAL A 1 358 ? -7.638  28.304  1.701   1.00 55.19  ? 387 VAL A O   1 
ATOM   2819  C CB  . VAL A 1 358 ? -10.317 27.353  -0.218  1.00 43.42  ? 387 VAL A CB  1 
ATOM   2820  C CG1 . VAL A 1 358 ? -11.563 26.892  0.528   1.00 41.02  ? 387 VAL A CG1 1 
ATOM   2821  C CG2 . VAL A 1 358 ? -10.626 27.610  -1.685  1.00 42.94  ? 387 VAL A CG2 1 
ATOM   2822  N N   . LEU A 1 359 ? -9.484  27.813  2.847   1.00 55.56  ? 388 LEU A N   1 
ATOM   2823  C CA  . LEU A 1 359 ? -8.713  27.562  4.108   1.00 59.56  ? 388 LEU A CA  1 
ATOM   2824  C C   . LEU A 1 359 ? -8.307  28.922  4.710   1.00 48.84  ? 388 LEU A C   1 
ATOM   2825  O O   . LEU A 1 359 ? -8.650  29.175  5.861   1.00 42.46  ? 388 LEU A O   1 
ATOM   2826  C CB  . LEU A 1 359 ? -7.487  26.648  3.973   1.00 64.37  ? 388 LEU A CB  1 
ATOM   2827  C CG  . LEU A 1 359 ? -7.695  25.137  4.118   1.00 63.97  ? 388 LEU A CG  1 
ATOM   2828  C CD1 . LEU A 1 359 ? -8.828  24.586  3.285   1.00 63.30  ? 388 LEU A CD1 1 
ATOM   2829  C CD2 . LEU A 1 359 ? -6.407  24.426  3.753   1.00 66.09  ? 388 LEU A CD2 1 
ATOM   2830  N N   . LEU A 1 360 ? -7.559  29.724  3.963   1.00 49.38  ? 389 LEU A N   1 
ATOM   2831  C CA  . LEU A 1 360 ? -7.241  31.088  4.441   1.00 51.91  ? 389 LEU A CA  1 
ATOM   2832  C C   . LEU A 1 360 ? -8.568  31.759  4.794   1.00 54.86  ? 389 LEU A C   1 
ATOM   2833  O O   . LEU A 1 360 ? -8.759  32.113  5.967   1.00 60.99  ? 389 LEU A O   1 
ATOM   2834  C CB  . LEU A 1 360 ? -6.482  31.888  3.386   1.00 54.70  ? 389 LEU A CB  1 
ATOM   2835  C CG  . LEU A 1 360 ? -4.955  31.814  3.439   1.00 55.03  ? 389 LEU A CG  1 
ATOM   2836  C CD1 . LEU A 1 360 ? -4.368  32.149  2.083   1.00 53.91  ? 389 LEU A CD1 1 
ATOM   2837  C CD2 . LEU A 1 360 ? -4.434  32.777  4.485   1.00 55.72  ? 389 LEU A CD2 1 
ATOM   2838  N N   . GLU A 1 361 ? -9.466  31.880  3.817   1.00 57.85  ? 390 GLU A N   1 
ATOM   2839  C CA  . GLU A 1 361 ? -10.768 32.549  4.038   1.00 58.36  ? 390 GLU A CA  1 
ATOM   2840  C C   . GLU A 1 361 ? -11.579 31.790  5.096   1.00 57.41  ? 390 GLU A C   1 
ATOM   2841  O O   . GLU A 1 361 ? -12.320 32.449  5.833   1.00 62.60  ? 390 GLU A O   1 
ATOM   2842  C CB  . GLU A 1 361 ? -11.609 32.624  2.763   1.00 59.48  ? 390 GLU A CB  1 
ATOM   2843  C CG  . GLU A 1 361 ? -11.073 31.755  1.634   1.00 58.76  ? 390 GLU A CG  1 
ATOM   2844  C CD  . GLU A 1 361 ? -10.962 32.523  0.333   1.00 60.88  ? 390 GLU A CD  1 
ATOM   2845  O OE1 . GLU A 1 361 ? -9.971  33.263  0.159   1.00 54.03  ? 390 GLU A OE1 1 
ATOM   2846  O OE2 . GLU A 1 361 ? -11.882 32.383  -0.497  1.00 56.68  ? 390 GLU A OE2 1 
ATOM   2847  N N   . GLN A 1 362 ? -11.476 30.467  5.145   1.00 53.79  ? 391 GLN A N   1 
ATOM   2848  C CA  . GLN A 1 362 ? -12.203 29.738  6.216   1.00 54.20  ? 391 GLN A CA  1 
ATOM   2849  C C   . GLN A 1 362 ? -11.628 30.201  7.559   1.00 55.38  ? 391 GLN A C   1 
ATOM   2850  O O   . GLN A 1 362 ? -12.406 30.469  8.482   1.00 59.12  ? 391 GLN A O   1 
ATOM   2851  C CB  . GLN A 1 362 ? -12.126 28.224  6.034   1.00 51.40  ? 391 GLN A CB  1 
ATOM   2852  C CG  . GLN A 1 362 ? -12.650 27.411  7.208   1.00 49.83  ? 391 GLN A CG  1 
ATOM   2853  C CD  . GLN A 1 362 ? -12.080 26.013  7.220   1.00 52.22  ? 391 GLN A CD  1 
ATOM   2854  O OE1 . GLN A 1 362 ? -10.912 25.796  6.881   1.00 56.83  ? 391 GLN A OE1 1 
ATOM   2855  N NE2 . GLN A 1 362 ? -12.907 25.049  7.594   1.00 50.13  ? 391 GLN A NE2 1 
ATOM   2856  N N   . GLY A 1 363 ? -10.303 30.352  7.629   1.00 54.77  ? 392 GLY A N   1 
ATOM   2857  C CA  . GLY A 1 363 ? -9.657  30.819  8.871   1.00 59.63  ? 392 GLY A CA  1 
ATOM   2858  C C   . GLY A 1 363 ? -9.093  29.650  9.648   1.00 66.60  ? 392 GLY A C   1 
ATOM   2859  O O   . GLY A 1 363 ? -7.885  29.679  9.961   1.00 62.63  ? 392 GLY A O   1 
ATOM   2860  N N   . LYS A 1 364 ? -9.995  28.571  9.840   1.00 73.40  ? 393 LYS A N   1 
ATOM   2861  C CA  . LYS A 1 364 ? -9.385  27.561  10.740  1.00 75.00  ? 393 LYS A CA  1 
ATOM   2862  C C   . LYS A 1 364 ? -8.393  26.730  9.920   1.00 75.42  ? 393 LYS A C   1 
ATOM   2863  O O   . LYS A 1 364 ? -8.802  25.686  9.391   1.00 84.01  ? 393 LYS A O   1 
ATOM   2864  C CB  . LYS A 1 364 ? -10.474 26.661  11.326  1.00 73.61  ? 393 LYS A CB  1 
ATOM   2865  C CG  . LYS A 1 364 ? -10.338 26.327  12.799  1.00 75.50  ? 393 LYS A CG  1 
ATOM   2866  C CD  . LYS A 1 364 ? -11.229 25.165  13.224  1.00 73.08  ? 393 LYS A CD  1 
ATOM   2867  C CE  . LYS A 1 364 ? -12.689 25.463  13.087  1.00 70.54  ? 393 LYS A CE  1 
ATOM   2868  N NZ  . LYS A 1 364 ? -13.014 26.819  13.533  1.00 71.45  ? 393 LYS A NZ  1 
ATOM   2869  N N   . ALA A 1 365 ? -7.112  27.334  9.678   1.00 68.86  ? 394 ALA A N   1 
ATOM   2870  C CA  . ALA A 1 365 ? -6.138  26.407  9.054   1.00 67.87  ? 394 ALA A CA  1 
ATOM   2871  C C   . ALA A 1 365 ? -4.779  26.507  9.749   1.00 65.54  ? 394 ALA A C   1 
ATOM   2872  O O   . ALA A 1 365 ? -4.265  25.427  10.117  1.00 73.25  ? 394 ALA A O   1 
ATOM   2873  C CB  . ALA A 1 365 ? -6.014  26.714  7.577   1.00 71.81  ? 394 ALA A CB  1 
ATOM   2874  N N   . LYS A 1 366 ? -4.367  27.819  10.039  1.00 60.89  ? 395 LYS A N   1 
ATOM   2875  C CA  . LYS A 1 366 ? -2.986  28.049  10.551  1.00 57.25  ? 395 LYS A CA  1 
ATOM   2876  C C   . LYS A 1 366 ? -2.032  27.766  9.385   1.00 50.96  ? 395 LYS A C   1 
ATOM   2877  O O   . LYS A 1 366 ? -1.328  28.705  8.955   1.00 50.76  ? 395 LYS A O   1 
ATOM   2878  C CB  . LYS A 1 366 ? -2.638  27.191  11.774  1.00 61.03  ? 395 LYS A CB  1 
ATOM   2879  C CG  . LYS A 1 366 ? -3.294  27.618  13.077  1.00 61.08  ? 395 LYS A CG  1 
ATOM   2880  C CD  . LYS A 1 366 ? -2.290  27.765  14.214  1.00 61.52  ? 395 LYS A CD  1 
ATOM   2881  C CE  . LYS A 1 366 ? -1.284  28.838  13.944  1.00 64.81  ? 395 LYS A CE  1 
ATOM   2882  N NZ  . LYS A 1 366 ? -0.207  28.831  14.937  1.00 65.67  ? 395 LYS A NZ  1 
ATOM   2883  N N   . ASN A 1 367 ? -2.007  26.523  8.907   1.00 44.04  ? 396 ASN A N   1 
ATOM   2884  C CA  . ASN A 1 367 ? -1.214  26.172  7.705   1.00 39.50  ? 396 ASN A CA  1 
ATOM   2885  C C   . ASN A 1 367 ? -2.166  25.822  6.561   1.00 37.39  ? 396 ASN A C   1 
ATOM   2886  O O   . ASN A 1 367 ? -2.554  24.656  6.448   1.00 33.22  ? 396 ASN A O   1 
ATOM   2887  C CB  . ASN A 1 367 ? -0.192  25.080  8.019   1.00 43.48  ? 396 ASN A CB  1 
ATOM   2888  C CG  . ASN A 1 367 ? 0.600   24.654  6.811   1.00 42.94  ? 396 ASN A CG  1 
ATOM   2889  O OD1 . ASN A 1 367 ? 0.674   25.389  5.823   1.00 47.44  ? 396 ASN A OD1 1 
ATOM   2890  N ND2 . ASN A 1 367 ? 1.204   23.480  6.876   1.00 41.16  ? 396 ASN A ND2 1 
ATOM   2891  N N   . PRO A 1 368 ? -2.553  26.784  5.703   1.00 34.13  ? 397 PRO A N   1 
ATOM   2892  C CA  . PRO A 1 368 ? -3.371  26.480  4.523   1.00 33.33  ? 397 PRO A CA  1 
ATOM   2893  C C   . PRO A 1 368 ? -2.595  25.904  3.341   1.00 32.06  ? 397 PRO A C   1 
ATOM   2894  O O   . PRO A 1 368 ? -3.101  25.831  2.222   1.00 39.82  ? 397 PRO A O   1 
ATOM   2895  C CB  . PRO A 1 368 ? -3.902  27.874  4.162   1.00 36.15  ? 397 PRO A CB  1 
ATOM   2896  C CG  . PRO A 1 368 ? -2.722  28.775  4.455   1.00 35.23  ? 397 PRO A CG  1 
ATOM   2897  C CD  . PRO A 1 368 ? -2.185  28.215  5.755   1.00 36.22  ? 397 PRO A CD  1 
ATOM   2898  N N   . TRP A 1 369 ? -1.356  25.478  3.591   1.00 28.53  ? 398 TRP A N   1 
ATOM   2899  C CA  . TRP A 1 369 ? -0.480  25.041  2.519   1.00 26.11  ? 398 TRP A CA  1 
ATOM   2900  C C   . TRP A 1 369 ? -0.339  23.522  2.570   1.00 26.11  ? 398 TRP A C   1 
ATOM   2901  O O   . TRP A 1 369 ? -0.658  22.916  3.593   1.00 26.70  ? 398 TRP A O   1 
ATOM   2902  C CB  . TRP A 1 369 ? 0.858   25.754  2.654   1.00 27.18  ? 398 TRP A CB  1 
ATOM   2903  C CG  . TRP A 1 369 ? 0.692   27.242  2.693   1.00 33.13  ? 398 TRP A CG  1 
ATOM   2904  C CD1 . TRP A 1 369 ? 0.723   28.061  3.782   1.00 35.62  ? 398 TRP A CD1 1 
ATOM   2905  C CD2 . TRP A 1 369 ? 0.424   28.081  1.564   1.00 37.30  ? 398 TRP A CD2 1 
ATOM   2906  N NE1 . TRP A 1 369 ? 0.516   29.360  3.404   1.00 35.64  ? 398 TRP A NE1 1 
ATOM   2907  C CE2 . TRP A 1 369 ? 0.333   29.403  2.049   1.00 40.07  ? 398 TRP A CE2 1 
ATOM   2908  C CE3 . TRP A 1 369 ? 0.255   27.839  0.197   1.00 42.43  ? 398 TRP A CE3 1 
ATOM   2909  C CZ2 . TRP A 1 369 ? 0.066   30.482  1.207   1.00 42.25  ? 398 TRP A CZ2 1 
ATOM   2910  C CZ3 . TRP A 1 369 ? 0.002   28.904  -0.638  1.00 42.12  ? 398 TRP A CZ3 1 
ATOM   2911  C CH2 . TRP A 1 369 ? -0.101  30.204  -0.132  1.00 43.28  ? 398 TRP A CH2 1 
ATOM   2912  N N   . PRO A 1 370 ? 0.133   22.885  1.477   1.00 25.05  ? 399 PRO A N   1 
ATOM   2913  C CA  . PRO A 1 370 ? 0.309   21.435  1.425   1.00 23.72  ? 399 PRO A CA  1 
ATOM   2914  C C   . PRO A 1 370 ? 1.550   20.936  2.153   1.00 25.54  ? 399 PRO A C   1 
ATOM   2915  O O   . PRO A 1 370 ? 2.540   21.642  2.301   1.00 25.67  ? 399 PRO A O   1 
ATOM   2916  C CB  . PRO A 1 370 ? 0.448   21.144  -0.073  1.00 22.41  ? 399 PRO A CB  1 
ATOM   2917  C CG  . PRO A 1 370 ? 1.057   22.402  -0.635  1.00 24.35  ? 399 PRO A CG  1 
ATOM   2918  C CD  . PRO A 1 370 ? 0.525   23.527  0.221   1.00 23.34  ? 399 PRO A CD  1 
ATOM   2919  N N   . ASN A 1 371 ? 1.446   19.700  2.635   1.00 26.96  ? 400 ASN A N   1 
ATOM   2920  C CA  . ASN A 1 371 ? 2.570   18.966  3.185   1.00 28.39  ? 400 ASN A CA  1 
ATOM   2921  C C   . ASN A 1 371 ? 2.990   17.912  2.156   1.00 27.88  ? 400 ASN A C   1 
ATOM   2922  O O   . ASN A 1 371 ? 2.334   17.751  1.131   1.00 26.16  ? 400 ASN A O   1 
ATOM   2923  C CB  . ASN A 1 371 ? 2.168   18.374  4.533   1.00 27.47  ? 400 ASN A CB  1 
ATOM   2924  C CG  . ASN A 1 371 ? 1.081   17.329  4.406   1.00 29.62  ? 400 ASN A CG  1 
ATOM   2925  O OD1 . ASN A 1 371 ? 1.242   16.344  3.692   1.00 38.03  ? 400 ASN A OD1 1 
ATOM   2926  N ND2 . ASN A 1 371 ? -0.016  17.504  5.120   1.00 33.26  ? 400 ASN A ND2 1 
ATOM   2927  N N   . VAL A 1 372 ? 4.101   17.221  2.436   1.00 29.60  ? 401 VAL A N   1 
ATOM   2928  C CA  . VAL A 1 372 ? 4.691   16.234  1.543   1.00 26.06  ? 401 VAL A CA  1 
ATOM   2929  C C   . VAL A 1 372 ? 3.650   15.224  1.047   1.00 24.23  ? 401 VAL A C   1 
ATOM   2930  O O   . VAL A 1 372 ? 3.713   14.785  -0.099  1.00 23.68  ? 401 VAL A O   1 
ATOM   2931  C CB  . VAL A 1 372 ? 5.849   15.504  2.249   1.00 29.83  ? 401 VAL A CB  1 
ATOM   2932  C CG1 . VAL A 1 372 ? 5.396   14.731  3.484   1.00 26.75  ? 401 VAL A CG1 1 
ATOM   2933  C CG2 . VAL A 1 372 ? 6.598   14.590  1.297   1.00 34.39  ? 401 VAL A CG2 1 
ATOM   2934  N N   . ASP A 1 373 ? 2.713   14.837  1.921   1.00 26.44  ? 402 ASP A N   1 
ATOM   2935  C CA  . ASP A 1 373 ? 1.797   13.730  1.666   1.00 25.90  ? 402 ASP A CA  1 
ATOM   2936  C C   . ASP A 1 373 ? 0.700   14.058  0.646   1.00 25.19  ? 402 ASP A C   1 
ATOM   2937  O O   . ASP A 1 373 ? -0.041  13.171  0.204   1.00 23.22  ? 402 ASP A O   1 
ATOM   2938  C CB  . ASP A 1 373 ? 1.111   13.289  2.952   1.00 32.13  ? 402 ASP A CB  1 
ATOM   2939  C CG  . ASP A 1 373 ? 2.090   12.827  4.016   1.00 35.01  ? 402 ASP A CG  1 
ATOM   2940  O OD1 . ASP A 1 373 ? 3.028   12.061  3.660   1.00 36.55  ? 402 ASP A OD1 1 
ATOM   2941  O OD2 . ASP A 1 373 ? 1.866   13.178  5.188   1.00 38.84  ? 402 ASP A OD2 1 
ATOM   2942  N N   . ALA A 1 374 ? 0.545   15.342  0.327   1.00 24.41  ? 403 ALA A N   1 
ATOM   2943  C CA  . ALA A 1 374 ? -0.389  15.778  -0.698  1.00 23.66  ? 403 ALA A CA  1 
ATOM   2944  C C   . ALA A 1 374 ? 0.086   15.302  -2.075  1.00 24.57  ? 403 ALA A C   1 
ATOM   2945  O O   . ALA A 1 374 ? -0.728  15.096  -2.972  1.00 23.81  ? 403 ALA A O   1 
ATOM   2946  C CB  . ALA A 1 374 ? -0.545  17.280  -0.650  1.00 21.50  ? 403 ALA A CB  1 
ATOM   2947  N N   . HIS A 1 375 ? 1.396   15.039  -2.212  1.00 25.18  ? 404 HIS A N   1 
ATOM   2948  C CA  . HIS A 1 375 ? 1.959   14.854  -3.539  1.00 25.49  ? 404 HIS A CA  1 
ATOM   2949  C C   . HIS A 1 375 ? 2.532   13.458  -3.754  1.00 26.24  ? 404 HIS A C   1 
ATOM   2950  O O   . HIS A 1 375 ? 2.629   13.013  -4.898  1.00 26.30  ? 404 HIS A O   1 
ATOM   2951  C CB  . HIS A 1 375 ? 3.056   15.887  -3.796  1.00 26.82  ? 404 HIS A CB  1 
ATOM   2952  C CG  . HIS A 1 375 ? 3.084   16.289  -5.218  1.00 28.66  ? 404 HIS A CG  1 
ATOM   2953  N ND1 . HIS A 1 375 ? 3.181   17.596  -5.656  1.00 28.50  ? 404 HIS A ND1 1 
ATOM   2954  C CD2 . HIS A 1 375 ? 2.981   15.524  -6.308  1.00 27.52  ? 404 HIS A CD2 1 
ATOM   2955  C CE1 . HIS A 1 375 ? 3.148   17.599  -6.979  1.00 27.54  ? 404 HIS A CE1 1 
ATOM   2956  N NE2 . HIS A 1 375 ? 3.014   16.358  -7.399  1.00 30.35  ? 404 HIS A NE2 1 
ATOM   2957  N N   . SER A 1 376 ? 2.933   12.778  -2.672  1.00 26.62  ? 405 SER A N   1 
ATOM   2958  C CA  . SER A 1 376 ? 3.781   11.604  -2.835  1.00 25.07  ? 405 SER A CA  1 
ATOM   2959  C C   . SER A 1 376 ? 3.023   10.427  -3.460  1.00 26.16  ? 405 SER A C   1 
ATOM   2960  O O   . SER A 1 376 ? 3.556   9.706   -4.329  1.00 24.98  ? 405 SER A O   1 
ATOM   2961  C CB  . SER A 1 376 ? 4.456   11.275  -1.514  1.00 25.08  ? 405 SER A CB  1 
ATOM   2962  O OG  . SER A 1 376 ? 3.513   10.971  -0.499  1.00 27.15  ? 405 SER A OG  1 
ATOM   2963  N N   . GLY A 1 377 ? 1.777   10.209  -3.028  1.00 27.59  ? 406 GLY A N   1 
ATOM   2964  C CA  . GLY A 1 377 ? 0.978   9.101   -3.527  1.00 28.91  ? 406 GLY A CA  1 
ATOM   2965  C C   . GLY A 1 377 ? 0.865   9.045   -5.057  1.00 27.80  ? 406 GLY A C   1 
ATOM   2966  O O   . GLY A 1 377 ? 0.955   7.972   -5.655  1.00 24.31  ? 406 GLY A O   1 
ATOM   2967  N N   . VAL A 1 378 ? 0.592   10.182  -5.699  1.00 24.87  ? 407 VAL A N   1 
ATOM   2968  C CA  . VAL A 1 378 ? 0.310   10.165  -7.133  1.00 26.05  ? 407 VAL A CA  1 
ATOM   2969  C C   . VAL A 1 378 ? 1.567   9.763   -7.905  1.00 25.52  ? 407 VAL A C   1 
ATOM   2970  O O   . VAL A 1 378 ? 1.457   9.179   -8.992  1.00 23.11  ? 407 VAL A O   1 
ATOM   2971  C CB  . VAL A 1 378 ? -0.267  11.503  -7.636  1.00 27.28  ? 407 VAL A CB  1 
ATOM   2972  C CG1 . VAL A 1 378 ? -1.636  11.784  -7.046  1.00 29.59  ? 407 VAL A CG1 1 
ATOM   2973  C CG2 . VAL A 1 378 ? 0.663   12.667  -7.375  1.00 26.95  ? 407 VAL A CG2 1 
ATOM   2974  N N   . LEU A 1 379 ? 2.747   10.102  -7.354  1.00 26.15  ? 408 LEU A N   1 
ATOM   2975  C CA  . LEU A 1 379 ? 4.009   9.832   -8.028  1.00 27.70  ? 408 LEU A CA  1 
ATOM   2976  C C   . LEU A 1 379 ? 4.264   8.336   -7.996  1.00 27.58  ? 408 LEU A C   1 
ATOM   2977  O O   . LEU A 1 379 ? 4.645   7.720   -8.996  1.00 31.65  ? 408 LEU A O   1 
ATOM   2978  C CB  . LEU A 1 379 ? 5.165   10.536  -7.325  1.00 29.32  ? 408 LEU A CB  1 
ATOM   2979  C CG  . LEU A 1 379 ? 5.261   12.047  -7.497  1.00 31.01  ? 408 LEU A CG  1 
ATOM   2980  C CD1 . LEU A 1 379 ? 6.383   12.598  -6.622  1.00 32.23  ? 408 LEU A CD1 1 
ATOM   2981  C CD2 . LEU A 1 379 ? 5.476   12.419  -8.953  1.00 37.06  ? 408 LEU A CD2 1 
ATOM   2982  N N   . LEU A 1 380 ? 4.096   7.756   -6.807  1.00 24.37  ? 409 LEU A N   1 
ATOM   2983  C CA  . LEU A 1 380 ? 4.313   6.323   -6.700  1.00 24.83  ? 409 LEU A CA  1 
ATOM   2984  C C   . LEU A 1 380 ? 3.343   5.587   -7.625  1.00 25.20  ? 409 LEU A C   1 
ATOM   2985  O O   . LEU A 1 380 ? 3.707   4.637   -8.308  1.00 26.41  ? 409 LEU A O   1 
ATOM   2986  C CB  . LEU A 1 380 ? 4.137   5.913   -5.238  1.00 23.55  ? 409 LEU A CB  1 
ATOM   2987  C CG  . LEU A 1 380 ? 5.155   6.497   -4.260  1.00 23.61  ? 409 LEU A CG  1 
ATOM   2988  C CD1 . LEU A 1 380 ? 4.782   6.165   -2.810  1.00 23.74  ? 409 LEU A CD1 1 
ATOM   2989  C CD2 . LEU A 1 380 ? 6.573   6.011   -4.561  1.00 22.85  ? 409 LEU A CD2 1 
ATOM   2990  N N   . GLN A 1 381 ? 2.075   6.008   -7.648  1.00 26.07  ? 410 GLN A N   1 
ATOM   2991  C CA  . GLN A 1 381 ? 1.066   5.311   -8.415  1.00 25.26  ? 410 GLN A CA  1 
ATOM   2992  C C   . GLN A 1 381 ? 1.417   5.379   -9.899  1.00 24.52  ? 410 GLN A C   1 
ATOM   2993  O O   . GLN A 1 381 ? 1.208   4.412   -10.622 1.00 25.57  ? 410 GLN A O   1 
ATOM   2994  C CB  . GLN A 1 381 ? -0.326  5.899   -8.157  1.00 26.52  ? 410 GLN A CB  1 
ATOM   2995  C CG  . GLN A 1 381 ? -1.427  5.088   -8.817  1.00 33.50  ? 410 GLN A CG  1 
ATOM   2996  C CD  . GLN A 1 381 ? -2.624  4.848   -7.938  1.00 38.88  ? 410 GLN A CD  1 
ATOM   2997  O OE1 . GLN A 1 381 ? -3.315  5.780   -7.534  1.00 48.10  ? 410 GLN A OE1 1 
ATOM   2998  N NE2 . GLN A 1 381 ? -2.890  3.583   -7.658  1.00 41.33  ? 410 GLN A NE2 1 
ATOM   2999  N N   . TYR A 1 382 ? 1.965   6.519   -10.326 1.00 23.43  ? 411 TYR A N   1 
ATOM   3000  C CA  . TYR A 1 382 ? 2.341   6.734   -11.719 1.00 25.90  ? 411 TYR A CA  1 
ATOM   3001  C C   . TYR A 1 382 ? 3.375   5.716   -12.216 1.00 27.35  ? 411 TYR A C   1 
ATOM   3002  O O   . TYR A 1 382 ? 3.331   5.289   -13.374 1.00 29.25  ? 411 TYR A O   1 
ATOM   3003  C CB  . TYR A 1 382 ? 2.906   8.137   -11.905 1.00 28.00  ? 411 TYR A CB  1 
ATOM   3004  C CG  . TYR A 1 382 ? 3.382   8.345   -13.309 1.00 35.12  ? 411 TYR A CG  1 
ATOM   3005  C CD1 . TYR A 1 382 ? 2.474   8.312   -14.356 1.00 35.90  ? 411 TYR A CD1 1 
ATOM   3006  C CD2 . TYR A 1 382 ? 4.735   8.423   -13.603 1.00 38.69  ? 411 TYR A CD2 1 
ATOM   3007  C CE1 . TYR A 1 382 ? 2.892   8.436   -15.667 1.00 37.78  ? 411 TYR A CE1 1 
ATOM   3008  C CE2 . TYR A 1 382 ? 5.172   8.552   -14.911 1.00 42.28  ? 411 TYR A CE2 1 
ATOM   3009  C CZ  . TYR A 1 382 ? 4.242   8.541   -15.938 1.00 40.12  ? 411 TYR A CZ  1 
ATOM   3010  O OH  . TYR A 1 382 ? 4.615   8.654   -17.238 1.00 44.81  ? 411 TYR A OH  1 
ATOM   3011  N N   . TYR A 1 383 ? 4.298   5.295   -11.345 1.00 29.34  ? 412 TYR A N   1 
ATOM   3012  C CA  . TYR A 1 383 ? 5.372   4.392   -11.753 1.00 26.82  ? 412 TYR A CA  1 
ATOM   3013  C C   . TYR A 1 383 ? 5.015   2.922   -11.539 1.00 24.85  ? 412 TYR A C   1 
ATOM   3014  O O   . TYR A 1 383 ? 5.837   2.047   -11.811 1.00 27.32  ? 412 TYR A O   1 
ATOM   3015  C CB  . TYR A 1 383 ? 6.674   4.784   -11.054 1.00 25.95  ? 412 TYR A CB  1 
ATOM   3016  C CG  . TYR A 1 383 ? 7.288   6.026   -11.624 1.00 25.48  ? 412 TYR A CG  1 
ATOM   3017  C CD1 . TYR A 1 383 ? 7.834   6.036   -12.899 1.00 24.04  ? 412 TYR A CD1 1 
ATOM   3018  C CD2 . TYR A 1 383 ? 7.188   7.232   -10.963 1.00 26.41  ? 412 TYR A CD2 1 
ATOM   3019  C CE1 . TYR A 1 383 ? 8.393   7.188   -13.443 1.00 24.05  ? 412 TYR A CE1 1 
ATOM   3020  C CE2 . TYR A 1 383 ? 7.712   8.392   -11.502 1.00 25.77  ? 412 TYR A CE2 1 
ATOM   3021  C CZ  . TYR A 1 383 ? 8.304   8.378   -12.754 1.00 23.23  ? 412 TYR A CZ  1 
ATOM   3022  O OH  . TYR A 1 383 ? 8.821   9.560   -13.224 1.00 26.12  ? 412 TYR A OH  1 
ATOM   3023  N N   . GLY A 1 384 ? 3.808   2.632   -11.055 1.00 24.11  ? 413 GLY A N   1 
ATOM   3024  C CA  . GLY A 1 384 ? 3.309   1.263   -11.030 1.00 25.21  ? 413 GLY A CA  1 
ATOM   3025  C C   . GLY A 1 384 ? 3.042   0.746   -9.624  1.00 26.69  ? 413 GLY A C   1 
ATOM   3026  O O   . GLY A 1 384 ? 2.474   -0.318  -9.445  1.00 26.87  ? 413 GLY A O   1 
ATOM   3027  N N   . MET A 1 385 ? 3.495   1.527   -8.645  1.00 30.08  ? 414 MET A N   1 
ATOM   3028  C CA  . MET A 1 385 ? 3.477   1.210   -7.227  1.00 29.43  ? 414 MET A CA  1 
ATOM   3029  C C   . MET A 1 385 ? 2.079   1.562   -6.718  1.00 30.53  ? 414 MET A C   1 
ATOM   3030  O O   . MET A 1 385 ? 1.830   2.640   -6.169  1.00 28.59  ? 414 MET A O   1 
ATOM   3031  C CB  . MET A 1 385 ? 4.615   2.030   -6.600  1.00 30.38  ? 414 MET A CB  1 
ATOM   3032  C CG  . MET A 1 385 ? 4.552   2.340   -5.124  1.00 36.96  ? 414 MET A CG  1 
ATOM   3033  S SD  . MET A 1 385 ? 5.293   1.093   -4.060  1.00 34.85  ? 414 MET A SD  1 
ATOM   3034  C CE  . MET A 1 385 ? 6.984   1.018   -4.645  1.00 37.05  ? 414 MET A CE  1 
ATOM   3035  N N   . THR A 1 386 ? 1.157   0.629   -6.966  1.00 28.07  ? 415 THR A N   1 
ATOM   3036  C CA  . THR A 1 386 ? -0.265  0.834   -6.763  1.00 31.54  ? 415 THR A CA  1 
ATOM   3037  C C   . THR A 1 386 ? -0.724  0.373   -5.373  1.00 32.65  ? 415 THR A C   1 
ATOM   3038  O O   . THR A 1 386 ? -1.837  0.711   -4.964  1.00 32.99  ? 415 THR A O   1 
ATOM   3039  C CB  . THR A 1 386 ? -1.055  0.103   -7.850  1.00 33.98  ? 415 THR A CB  1 
ATOM   3040  O OG1 . THR A 1 386 ? -0.503  -1.213  -7.921  1.00 31.38  ? 415 THR A OG1 1 
ATOM   3041  C CG2 . THR A 1 386 ? -1.005  0.781   -9.204  1.00 36.97  ? 415 THR A CG2 1 
ATOM   3042  N N   . GLU A 1 387 ? 0.101   -0.412  -4.658  1.00 28.78  ? 416 GLU A N   1 
ATOM   3043  C CA  . GLU A 1 387 ? -0.313  -1.007  -3.384  1.00 27.05  ? 416 GLU A CA  1 
ATOM   3044  C C   . GLU A 1 387 ? -0.182  0.017   -2.251  1.00 26.76  ? 416 GLU A C   1 
ATOM   3045  O O   . GLU A 1 387 ? 0.905   0.209   -1.711  1.00 25.48  ? 416 GLU A O   1 
ATOM   3046  C CB  . GLU A 1 387 ? 0.559   -2.215  -3.042  1.00 23.42  ? 416 GLU A CB  1 
ATOM   3047  C CG  . GLU A 1 387 ? 0.683   -3.227  -4.157  1.00 25.50  ? 416 GLU A CG  1 
ATOM   3048  C CD  . GLU A 1 387 ? 1.650   -2.972  -5.301  1.00 26.70  ? 416 GLU A CD  1 
ATOM   3049  O OE1 . GLU A 1 387 ? 2.289   -1.897  -5.376  1.00 26.48  ? 416 GLU A OE1 1 
ATOM   3050  O OE2 . GLU A 1 387 ? 1.739   -3.870  -6.140  1.00 27.45  ? 416 GLU A OE2 1 
ATOM   3051  N N   . MET A 1 388 ? -1.279  0.704   -1.910  1.00 24.66  ? 417 MET A N   1 
ATOM   3052  C CA  . MET A 1 388 ? -1.218  1.884   -1.048  1.00 28.83  ? 417 MET A CA  1 
ATOM   3053  C C   . MET A 1 388 ? -0.838  1.559   0.401   1.00 25.48  ? 417 MET A C   1 
ATOM   3054  O O   . MET A 1 388 ? -0.248  2.387   1.073   1.00 25.47  ? 417 MET A O   1 
ATOM   3055  C CB  . MET A 1 388 ? -2.583  2.575   -1.015  1.00 31.64  ? 417 MET A CB  1 
ATOM   3056  C CG  . MET A 1 388 ? -2.906  3.217   -2.343  1.00 38.03  ? 417 MET A CG  1 
ATOM   3057  S SD  . MET A 1 388 ? -4.476  4.090   -2.356  1.00 42.15  ? 417 MET A SD  1 
ATOM   3058  C CE  . MET A 1 388 ? -5.502  2.954   -1.418  1.00 39.25  ? 417 MET A CE  1 
ATOM   3059  N N   . ASN A 1 389 ? -1.207  0.369   0.887   1.00 25.03  ? 418 ASN A N   1 
ATOM   3060  C CA  . ASN A 1 389 ? -0.881  -0.025  2.241   1.00 25.24  ? 418 ASN A CA  1 
ATOM   3061  C C   . ASN A 1 389 ? 0.628   -0.128  2.444   1.00 23.77  ? 418 ASN A C   1 
ATOM   3062  O O   . ASN A 1 389 ? 1.066   -0.183  3.591   1.00 23.86  ? 418 ASN A O   1 
ATOM   3063  C CB  . ASN A 1 389 ? -1.503  -1.369  2.622   1.00 28.59  ? 418 ASN A CB  1 
ATOM   3064  C CG  . ASN A 1 389 ? -2.879  -1.226  3.227   1.00 33.07  ? 418 ASN A CG  1 
ATOM   3065  O OD1 . ASN A 1 389 ? -3.458  -0.137  3.225   1.00 30.56  ? 418 ASN A OD1 1 
ATOM   3066  N ND2 . ASN A 1 389 ? -3.386  -2.323  3.770   1.00 40.10  ? 418 ASN A ND2 1 
ATOM   3067  N N   . TYR A 1 390 ? 1.404   -0.174  1.348   1.00 22.36  ? 419 TYR A N   1 
ATOM   3068  C CA  . TYR A 1 390 ? 2.839   -0.366  1.450   1.00 22.91  ? 419 TYR A CA  1 
ATOM   3069  C C   . TYR A 1 390 ? 3.555   0.973   1.533   1.00 20.56  ? 419 TYR A C   1 
ATOM   3070  O O   . TYR A 1 390 ? 4.719   1.010   1.888   1.00 20.61  ? 419 TYR A O   1 
ATOM   3071  C CB  . TYR A 1 390 ? 3.349   -1.187  0.262   1.00 23.76  ? 419 TYR A CB  1 
ATOM   3072  C CG  . TYR A 1 390 ? 4.830   -1.461  0.289   1.00 21.62  ? 419 TYR A CG  1 
ATOM   3073  C CD1 . TYR A 1 390 ? 5.351   -2.464  1.084   1.00 21.69  ? 419 TYR A CD1 1 
ATOM   3074  C CD2 . TYR A 1 390 ? 5.709   -0.708  -0.467  1.00 23.49  ? 419 TYR A CD2 1 
ATOM   3075  C CE1 . TYR A 1 390 ? 6.715   -2.703  1.139   1.00 20.44  ? 419 TYR A CE1 1 
ATOM   3076  C CE2 . TYR A 1 390 ? 7.078   -0.942  -0.433  1.00 23.62  ? 419 TYR A CE2 1 
ATOM   3077  C CZ  . TYR A 1 390 ? 7.582   -1.953  0.371   1.00 21.81  ? 419 TYR A CZ  1 
ATOM   3078  O OH  . TYR A 1 390 ? 8.943   -2.207  0.414   1.00 21.53  ? 419 TYR A OH  1 
ATOM   3079  N N   . TYR A 1 391 ? 2.871   2.079   1.190   1.00 22.44  ? 420 TYR A N   1 
ATOM   3080  C CA  . TYR A 1 391 ? 3.530   3.365   1.025   1.00 22.10  ? 420 TYR A CA  1 
ATOM   3081  C C   . TYR A 1 391 ? 4.332   3.798   2.262   1.00 20.95  ? 420 TYR A C   1 
ATOM   3082  O O   . TYR A 1 391 ? 5.412   4.373   2.140   1.00 21.84  ? 420 TYR A O   1 
ATOM   3083  C CB  . TYR A 1 391 ? 2.511   4.459   0.680   1.00 23.12  ? 420 TYR A CB  1 
ATOM   3084  C CG  . TYR A 1 391 ? 1.971   4.441   -0.734  1.00 24.63  ? 420 TYR A CG  1 
ATOM   3085  C CD1 . TYR A 1 391 ? 2.266   3.412   -1.622  1.00 22.42  ? 420 TYR A CD1 1 
ATOM   3086  C CD2 . TYR A 1 391 ? 1.068   5.410   -1.156  1.00 25.42  ? 420 TYR A CD2 1 
ATOM   3087  C CE1 . TYR A 1 391 ? 1.755   3.396   -2.906  1.00 24.24  ? 420 TYR A CE1 1 
ATOM   3088  C CE2 . TYR A 1 391 ? 0.545   5.410   -2.444  1.00 25.44  ? 420 TYR A CE2 1 
ATOM   3089  C CZ  . TYR A 1 391 ? 0.877   4.390   -3.316  1.00 25.53  ? 420 TYR A CZ  1 
ATOM   3090  O OH  . TYR A 1 391 ? 0.450   4.374   -4.616  1.00 27.25  ? 420 TYR A OH  1 
ATOM   3091  N N   . THR A 1 392 ? 3.828   3.523   3.461   1.00 19.94  ? 421 THR A N   1 
ATOM   3092  C CA  . THR A 1 392 ? 4.506   3.983   4.652   1.00 20.50  ? 421 THR A CA  1 
ATOM   3093  C C   . THR A 1 392 ? 5.821   3.234   4.857   1.00 19.28  ? 421 THR A C   1 
ATOM   3094  O O   . THR A 1 392 ? 6.727   3.747   5.495   1.00 21.08  ? 421 THR A O   1 
ATOM   3095  C CB  . THR A 1 392 ? 3.604   3.884   5.879   1.00 19.99  ? 421 THR A CB  1 
ATOM   3096  O OG1 . THR A 1 392 ? 2.324   4.363   5.445   1.00 23.90  ? 421 THR A OG1 1 
ATOM   3097  C CG2 . THR A 1 392 ? 4.123   4.723   7.024   1.00 19.96  ? 421 THR A CG2 1 
ATOM   3098  N N   . VAL A 1 393 ? 5.914   2.027   4.309   1.00 18.66  ? 422 VAL A N   1 
ATOM   3099  C CA  . VAL A 1 393 ? 7.152   1.271   4.399   1.00 18.06  ? 422 VAL A CA  1 
ATOM   3100  C C   . VAL A 1 393 ? 8.300   2.047   3.738   1.00 20.35  ? 422 VAL A C   1 
ATOM   3101  O O   . VAL A 1 393 ? 9.418   2.099   4.259   1.00 19.23  ? 422 VAL A O   1 
ATOM   3102  C CB  . VAL A 1 393 ? 7.018   -0.155  3.831   1.00 18.02  ? 422 VAL A CB  1 
ATOM   3103  C CG1 . VAL A 1 393 ? 8.379   -0.833  3.758   1.00 19.02  ? 422 VAL A CG1 1 
ATOM   3104  C CG2 . VAL A 1 393 ? 6.067   -1.029  4.631   1.00 18.46  ? 422 VAL A CG2 1 
ATOM   3105  N N   . LEU A 1 394 ? 8.028   2.688   2.594   1.00 22.69  ? 423 LEU A N   1 
ATOM   3106  C CA  . LEU A 1 394 ? 9.014   3.545   1.951   1.00 22.83  ? 423 LEU A CA  1 
ATOM   3107  C C   . LEU A 1 394 ? 9.394   4.708   2.868   1.00 23.29  ? 423 LEU A C   1 
ATOM   3108  O O   . LEU A 1 394 ? 10.565  5.066   2.973   1.00 23.02  ? 423 LEU A O   1 
ATOM   3109  C CB  . LEU A 1 394 ? 8.433   4.077   0.634   1.00 22.14  ? 423 LEU A CB  1 
ATOM   3110  C CG  . LEU A 1 394 ? 8.134   3.073   -0.488  1.00 24.68  ? 423 LEU A CG  1 
ATOM   3111  C CD1 . LEU A 1 394 ? 7.912   3.846   -1.787  1.00 26.00  ? 423 LEU A CD1 1 
ATOM   3112  C CD2 . LEU A 1 394 ? 9.242   2.061   -0.691  1.00 27.04  ? 423 LEU A CD2 1 
ATOM   3113  N N   . PHE A 1 395 ? 8.387   5.324   3.493   1.00 22.94  ? 424 PHE A N   1 
ATOM   3114  C CA  . PHE A 1 395 ? 8.605   6.397   4.452   1.00 22.22  ? 424 PHE A CA  1 
ATOM   3115  C C   . PHE A 1 395 ? 9.501   5.897   5.601   1.00 20.78  ? 424 PHE A C   1 
ATOM   3116  O O   . PHE A 1 395 ? 10.437  6.578   6.016   1.00 22.28  ? 424 PHE A O   1 
ATOM   3117  C CB  . PHE A 1 395 ? 7.241   7.009   4.828   1.00 20.98  ? 424 PHE A CB  1 
ATOM   3118  C CG  . PHE A 1 395 ? 7.242   8.280   5.656   1.00 21.06  ? 424 PHE A CG  1 
ATOM   3119  C CD1 . PHE A 1 395 ? 8.373   8.775   6.289   1.00 24.20  ? 424 PHE A CD1 1 
ATOM   3120  C CD2 . PHE A 1 395 ? 6.076   9.018   5.774   1.00 22.60  ? 424 PHE A CD2 1 
ATOM   3121  C CE1 . PHE A 1 395 ? 8.344   9.965   7.004   1.00 24.81  ? 424 PHE A CE1 1 
ATOM   3122  C CE2 . PHE A 1 395 ? 6.048   10.203  6.490   1.00 23.10  ? 424 PHE A CE2 1 
ATOM   3123  C CZ  . PHE A 1 395 ? 7.179   10.684  7.096   1.00 23.12  ? 424 PHE A CZ  1 
ATOM   3124  N N   . GLY A 1 396 ? 9.255   4.670   6.084   1.00 20.05  ? 425 GLY A N   1 
ATOM   3125  C CA  . GLY A 1 396 ? 10.035  4.095   7.169   1.00 18.95  ? 425 GLY A CA  1 
ATOM   3126  C C   . GLY A 1 396 ? 11.517  3.949   6.817   1.00 17.10  ? 425 GLY A C   1 
ATOM   3127  O O   . GLY A 1 396 ? 12.392  4.350   7.577   1.00 19.51  ? 425 GLY A O   1 
ATOM   3128  N N   . VAL A 1 397 ? 11.789  3.362   5.647   1.00 19.37  ? 426 VAL A N   1 
ATOM   3129  C CA  . VAL A 1 397 ? 13.152  3.087   5.240   1.00 19.26  ? 426 VAL A CA  1 
ATOM   3130  C C   . VAL A 1 397 ? 13.892  4.407   5.182   1.00 18.88  ? 426 VAL A C   1 
ATOM   3131  O O   . VAL A 1 397 ? 15.054  4.487   5.516   1.00 20.73  ? 426 VAL A O   1 
ATOM   3132  C CB  . VAL A 1 397 ? 13.181  2.370   3.880   1.00 19.62  ? 426 VAL A CB  1 
ATOM   3133  C CG1 . VAL A 1 397 ? 14.585  2.320   3.313   1.00 19.92  ? 426 VAL A CG1 1 
ATOM   3134  C CG2 . VAL A 1 397 ? 12.575  0.980   3.953   1.00 19.81  ? 426 VAL A CG2 1 
ATOM   3135  N N   . SER A 1 398 ? 13.206  5.445   4.700   1.00 19.07  ? 427 SER A N   1 
ATOM   3136  C CA  . SER A 1 398 ? 13.793  6.760   4.574   1.00 18.25  ? 427 SER A CA  1 
ATOM   3137  C C   . SER A 1 398 ? 14.138  7.355   5.936   1.00 17.26  ? 427 SER A C   1 
ATOM   3138  O O   . SER A 1 398 ? 15.241  7.883   6.124   1.00 15.65  ? 427 SER A O   1 
ATOM   3139  C CB  . SER A 1 398 ? 12.818  7.658   3.899   1.00 18.43  ? 427 SER A CB  1 
ATOM   3140  O OG  . SER A 1 398 ? 13.338  8.981   3.854   1.00 19.44  ? 427 SER A OG  1 
ATOM   3141  N N   . ARG A 1 399 ? 13.155  7.286   6.848   1.00 17.68  ? 428 ARG A N   1 
ATOM   3142  C CA  . ARG A 1 399 ? 13.243  7.920   8.160   1.00 17.86  ? 428 ARG A CA  1 
ATOM   3143  C C   . ARG A 1 399 ? 14.361  7.281   8.994   1.00 16.15  ? 428 ARG A C   1 
ATOM   3144  O O   . ARG A 1 399 ? 14.882  7.891   9.897   1.00 17.06  ? 428 ARG A O   1 
ATOM   3145  C CB  . ARG A 1 399 ? 11.864  7.909   8.820   1.00 16.34  ? 428 ARG A CB  1 
ATOM   3146  C CG  . ARG A 1 399 ? 11.777  8.563   10.188  1.00 17.12  ? 428 ARG A CG  1 
ATOM   3147  C CD  . ARG A 1 399 ? 12.248  10.025  10.125  1.00 19.35  ? 428 ARG A CD  1 
ATOM   3148  N NE  . ARG A 1 399 ? 11.629  10.817  9.053   1.00 19.83  ? 428 ARG A NE  1 
ATOM   3149  C CZ  . ARG A 1 399 ? 10.671  11.727  9.226   1.00 23.91  ? 428 ARG A CZ  1 
ATOM   3150  N NH1 . ARG A 1 399 ? 10.004  11.776  10.369  1.00 23.75  ? 428 ARG A NH1 1 
ATOM   3151  N NH2 . ARG A 1 399 ? 10.339  12.553  8.242   1.00 23.88  ? 428 ARG A NH2 1 
ATOM   3152  N N   . ALA A 1 400 ? 14.695  6.008   8.759   1.00 16.87  ? 429 ALA A N   1 
ATOM   3153  C CA  . ALA A 1 400 ? 15.829  5.403   9.440   1.00 17.58  ? 429 ALA A CA  1 
ATOM   3154  C C   . ALA A 1 400 ? 17.064  6.275   9.314   1.00 17.95  ? 429 ALA A C   1 
ATOM   3155  O O   . ALA A 1 400 ? 17.798  6.406   10.257  1.00 18.98  ? 429 ALA A O   1 
ATOM   3156  C CB  . ALA A 1 400 ? 16.128  4.013   8.928   1.00 18.34  ? 429 ALA A CB  1 
ATOM   3157  N N   . LEU A 1 401 ? 17.266  6.914   8.150   1.00 18.81  ? 430 LEU A N   1 
ATOM   3158  C CA  . LEU A 1 401 ? 18.447  7.741   7.982   1.00 21.00  ? 430 LEU A CA  1 
ATOM   3159  C C   . LEU A 1 401 ? 18.561  8.818   9.067   1.00 20.00  ? 430 LEU A C   1 
ATOM   3160  O O   . LEU A 1 401 ? 19.611  8.991   9.691   1.00 18.15  ? 430 LEU A O   1 
ATOM   3161  C CB  . LEU A 1 401 ? 18.443  8.347   6.581   1.00 20.27  ? 430 LEU A CB  1 
ATOM   3162  C CG  . LEU A 1 401 ? 18.456  7.339   5.439   1.00 22.90  ? 430 LEU A CG  1 
ATOM   3163  C CD1 . LEU A 1 401 ? 18.344  8.015   4.090   1.00 24.44  ? 430 LEU A CD1 1 
ATOM   3164  C CD2 . LEU A 1 401 ? 19.724  6.494   5.487   1.00 25.57  ? 430 LEU A CD2 1 
ATOM   3165  N N   . GLY A 1 402 ? 17.485  9.572   9.275   1.00 17.89  ? 431 GLY A N   1 
ATOM   3166  C CA  . GLY A 1 402 ? 17.570  10.699  10.173  1.00 18.41  ? 431 GLY A CA  1 
ATOM   3167  C C   . GLY A 1 402 ? 17.646  10.270  11.636  1.00 17.93  ? 431 GLY A C   1 
ATOM   3168  O O   . GLY A 1 402 ? 18.478  10.757  12.405  1.00 19.77  ? 431 GLY A O   1 
ATOM   3169  N N   . VAL A 1 403 ? 16.814  9.299   11.984  1.00 17.21  ? 432 VAL A N   1 
ATOM   3170  C CA  . VAL A 1 403 ? 16.597  8.982   13.391  1.00 18.22  ? 432 VAL A CA  1 
ATOM   3171  C C   . VAL A 1 403 ? 17.801  8.199   13.934  1.00 16.58  ? 432 VAL A C   1 
ATOM   3172  O O   . VAL A 1 403 ? 18.142  8.291   15.120  1.00 20.05  ? 432 VAL A O   1 
ATOM   3173  C CB  . VAL A 1 403 ? 15.249  8.279   13.583  1.00 18.60  ? 432 VAL A CB  1 
ATOM   3174  C CG1 . VAL A 1 403 ? 14.137  9.092   12.938  1.00 18.72  ? 432 VAL A CG1 1 
ATOM   3175  C CG2 . VAL A 1 403 ? 15.252  6.837   13.092  1.00 18.21  ? 432 VAL A CG2 1 
ATOM   3176  N N   . LEU A 1 404 ? 18.501  7.508   13.031  1.00 17.56  ? 433 LEU A N   1 
ATOM   3177  C CA  . LEU A 1 404 ? 19.653  6.720   13.423  1.00 17.33  ? 433 LEU A CA  1 
ATOM   3178  C C   . LEU A 1 404 ? 20.907  7.585   13.399  1.00 19.21  ? 433 LEU A C   1 
ATOM   3179  O O   . LEU A 1 404 ? 21.820  7.377   14.213  1.00 18.66  ? 433 LEU A O   1 
ATOM   3180  C CB  . LEU A 1 404 ? 19.768  5.507   12.501  1.00 17.59  ? 433 LEU A CB  1 
ATOM   3181  C CG  . LEU A 1 404 ? 18.686  4.430   12.645  1.00 17.74  ? 433 LEU A CG  1 
ATOM   3182  C CD1 . LEU A 1 404 ? 18.981  3.249   11.765  1.00 16.60  ? 433 LEU A CD1 1 
ATOM   3183  C CD2 . LEU A 1 404 ? 18.507  3.945   14.086  1.00 17.86  ? 433 LEU A CD2 1 
ATOM   3184  N N   . ALA A 1 405 ? 20.930  8.599   12.507  1.00 19.99  ? 434 ALA A N   1 
ATOM   3185  C CA  . ALA A 1 405 ? 22.008  9.572   12.531  1.00 21.70  ? 434 ALA A CA  1 
ATOM   3186  C C   . ALA A 1 405 ? 22.019  10.284  13.878  1.00 22.72  ? 434 ALA A C   1 
ATOM   3187  O O   . ALA A 1 405 ? 23.073  10.540  14.450  1.00 21.02  ? 434 ALA A O   1 
ATOM   3188  C CB  . ALA A 1 405 ? 21.844  10.592  11.425  1.00 22.26  ? 434 ALA A CB  1 
ATOM   3189  N N   . GLN A 1 406 ? 20.820  10.673  14.338  1.00 21.18  ? 435 GLN A N   1 
ATOM   3190  C CA  . GLN A 1 406 ? 20.681  11.375  15.595  1.00 21.47  ? 435 GLN A CA  1 
ATOM   3191  C C   . GLN A 1 406 ? 20.923  10.435  16.764  1.00 18.79  ? 435 GLN A C   1 
ATOM   3192  O O   . GLN A 1 406 ? 21.513  10.864  17.732  1.00 19.91  ? 435 GLN A O   1 
ATOM   3193  C CB  . GLN A 1 406 ? 19.275  11.948  15.797  1.00 22.16  ? 435 GLN A CB  1 
ATOM   3194  C CG  . GLN A 1 406 ? 19.067  12.522  17.196  1.00 23.59  ? 435 GLN A CG  1 
ATOM   3195  C CD  . GLN A 1 406 ? 20.008  13.664  17.456  1.00 24.93  ? 435 GLN A CD  1 
ATOM   3196  O OE1 . GLN A 1 406 ? 20.229  14.511  16.600  1.00 26.69  ? 435 GLN A OE1 1 
ATOM   3197  N NE2 . GLN A 1 406 ? 20.617  13.676  18.627  1.00 24.34  ? 435 GLN A NE2 1 
ATOM   3198  N N   . LEU A 1 407 ? 20.447  9.179   16.678  1.00 18.07  ? 436 LEU A N   1 
ATOM   3199  C CA  . LEU A 1 407 ? 20.662  8.230   17.759  1.00 18.61  ? 436 LEU A CA  1 
ATOM   3200  C C   . LEU A 1 407 ? 22.162  8.108   18.052  1.00 17.30  ? 436 LEU A C   1 
ATOM   3201  O O   . LEU A 1 407 ? 22.580  8.059   19.212  1.00 15.78  ? 436 LEU A O   1 
ATOM   3202  C CB  . LEU A 1 407 ? 20.053  6.864   17.414  1.00 17.74  ? 436 LEU A CB  1 
ATOM   3203  C CG  . LEU A 1 407 ? 20.106  5.814   18.527  1.00 19.77  ? 436 LEU A CG  1 
ATOM   3204  C CD1 . LEU A 1 407 ? 19.369  6.306   19.786  1.00 17.52  ? 436 LEU A CD1 1 
ATOM   3205  C CD2 . LEU A 1 407 ? 19.556  4.473   18.062  1.00 20.88  ? 436 LEU A CD2 1 
ATOM   3206  N N   . ILE A 1 408 ? 22.971  8.085   16.989  1.00 16.46  ? 437 ILE A N   1 
ATOM   3207  C CA  . ILE A 1 408 ? 24.412  7.989   17.160  1.00 16.27  ? 437 ILE A CA  1 
ATOM   3208  C C   . ILE A 1 408 ? 24.931  9.184   17.945  1.00 17.58  ? 437 ILE A C   1 
ATOM   3209  O O   . ILE A 1 408 ? 25.710  9.010   18.872  1.00 18.66  ? 437 ILE A O   1 
ATOM   3210  C CB  . ILE A 1 408 ? 25.086  7.879   15.791  1.00 16.53  ? 437 ILE A CB  1 
ATOM   3211  C CG1 . ILE A 1 408 ? 24.710  6.574   15.083  1.00 14.97  ? 437 ILE A CG1 1 
ATOM   3212  C CG2 . ILE A 1 408 ? 26.591  8.071   15.962  1.00 16.64  ? 437 ILE A CG2 1 
ATOM   3213  C CD1 . ILE A 1 408 ? 25.038  6.593   13.616  1.00 16.31  ? 437 ILE A CD1 1 
ATOM   3214  N N   . TRP A 1 409 ? 24.427  10.379  17.611  1.00 17.92  ? 438 TRP A N   1 
ATOM   3215  C CA  . TRP A 1 409 ? 24.790  11.604  18.289  1.00 16.97  ? 438 TRP A CA  1 
ATOM   3216  C C   . TRP A 1 409 ? 24.296  11.686  19.735  1.00 16.04  ? 438 TRP A C   1 
ATOM   3217  O O   . TRP A 1 409 ? 25.080  12.015  20.610  1.00 17.62  ? 438 TRP A O   1 
ATOM   3218  C CB  . TRP A 1 409 ? 24.413  12.837  17.469  1.00 18.95  ? 438 TRP A CB  1 
ATOM   3219  C CG  . TRP A 1 409 ? 25.464  13.113  16.437  1.00 20.58  ? 438 TRP A CG  1 
ATOM   3220  C CD1 . TRP A 1 409 ? 25.449  12.752  15.127  1.00 22.04  ? 438 TRP A CD1 1 
ATOM   3221  C CD2 . TRP A 1 409 ? 26.743  13.730  16.655  1.00 21.42  ? 438 TRP A CD2 1 
ATOM   3222  N NE1 . TRP A 1 409 ? 26.611  13.125  14.517  1.00 22.77  ? 438 TRP A NE1 1 
ATOM   3223  C CE2 . TRP A 1 409 ? 27.394  13.798  15.407  1.00 21.28  ? 438 TRP A CE2 1 
ATOM   3224  C CE3 . TRP A 1 409 ? 27.348  14.324  17.754  1.00 20.17  ? 438 TRP A CE3 1 
ATOM   3225  C CZ2 . TRP A 1 409 ? 28.689  14.319  15.266  1.00 20.20  ? 438 TRP A CZ2 1 
ATOM   3226  C CZ3 . TRP A 1 409 ? 28.594  14.887  17.610  1.00 21.52  ? 438 TRP A CZ3 1 
ATOM   3227  C CH2 . TRP A 1 409 ? 29.255  14.881  16.383  1.00 20.78  ? 438 TRP A CH2 1 
ATOM   3228  N N   . SER A 1 410 ? 23.024  11.404  20.000  1.00 14.11  ? 439 SER A N   1 
ATOM   3229  C CA  . SER A 1 410 ? 22.500  11.292  21.357  1.00 16.41  ? 439 SER A CA  1 
ATOM   3230  C C   . SER A 1 410 ? 23.388  10.472  22.297  1.00 16.71  ? 439 SER A C   1 
ATOM   3231  O O   . SER A 1 410 ? 23.556  10.834  23.463  1.00 19.49  ? 439 SER A O   1 
ATOM   3232  C CB  . SER A 1 410 ? 21.114  10.683  21.331  1.00 17.07  ? 439 SER A CB  1 
ATOM   3233  O OG  . SER A 1 410 ? 20.204  11.514  20.660  1.00 16.17  ? 439 SER A OG  1 
ATOM   3234  N N   . ARG A 1 411 ? 23.865  9.306   21.843  1.00 18.44  ? 440 ARG A N   1 
ATOM   3235  C CA  . ARG A 1 411 ? 24.691  8.461   22.690  1.00 18.42  ? 440 ARG A CA  1 
ATOM   3236  C C   . ARG A 1 411 ? 26.142  8.950   22.774  1.00 19.05  ? 440 ARG A C   1 
ATOM   3237  O O   . ARG A 1 411 ? 26.753  8.849   23.839  1.00 22.32  ? 440 ARG A O   1 
ATOM   3238  C CB  . ARG A 1 411 ? 24.598  7.031   22.181  1.00 20.93  ? 440 ARG A CB  1 
ATOM   3239  C CG  . ARG A 1 411 ? 23.164  6.546   22.113  1.00 24.30  ? 440 ARG A CG  1 
ATOM   3240  C CD  . ARG A 1 411 ? 22.572  6.419   23.507  1.00 29.73  ? 440 ARG A CD  1 
ATOM   3241  N NE  . ARG A 1 411 ? 21.341  5.654   23.381  1.00 38.01  ? 440 ARG A NE  1 
ATOM   3242  C CZ  . ARG A 1 411 ? 21.277  4.400   22.932  1.00 33.71  ? 440 ARG A CZ  1 
ATOM   3243  N NH1 . ARG A 1 411 ? 22.345  3.623   22.984  1.00 42.19  ? 440 ARG A NH1 1 
ATOM   3244  N NH2 . ARG A 1 411 ? 20.133  3.898   22.502  1.00 24.67  ? 440 ARG A NH2 1 
ATOM   3245  N N   . ALA A 1 412 ? 26.674  9.521   21.690  1.00 19.89  ? 441 ALA A N   1 
ATOM   3246  C CA  . ALA A 1 412 ? 27.994  10.153  21.671  1.00 21.29  ? 441 ALA A CA  1 
ATOM   3247  C C   . ALA A 1 412 ? 28.048  11.337  22.634  1.00 21.40  ? 441 ALA A C   1 
ATOM   3248  O O   . ALA A 1 412 ? 29.071  11.556  23.264  1.00 26.84  ? 441 ALA A O   1 
ATOM   3249  C CB  . ALA A 1 412 ? 28.354  10.583  20.261  1.00 20.61  ? 441 ALA A CB  1 
ATOM   3250  N N   . LEU A 1 413 ? 26.947  12.086  22.735  1.00 19.64  ? 442 LEU A N   1 
ATOM   3251  C CA  . LEU A 1 413 ? 26.852  13.263  23.580  1.00 21.69  ? 442 LEU A CA  1 
ATOM   3252  C C   . LEU A 1 413 ? 26.372  12.942  25.003  1.00 22.26  ? 442 LEU A C   1 
ATOM   3253  O O   . LEU A 1 413 ? 26.277  13.825  25.837  1.00 21.92  ? 442 LEU A O   1 
ATOM   3254  C CB  . LEU A 1 413 ? 25.906  14.243  22.891  1.00 21.97  ? 442 LEU A CB  1 
ATOM   3255  C CG  . LEU A 1 413 ? 26.397  14.778  21.548  1.00 24.54  ? 442 LEU A CG  1 
ATOM   3256  C CD1 . LEU A 1 413 ? 25.415  15.775  20.955  1.00 23.63  ? 442 LEU A CD1 1 
ATOM   3257  C CD2 . LEU A 1 413 ? 27.785  15.393  21.709  1.00 22.54  ? 442 LEU A CD2 1 
ATOM   3258  N N   . GLY A 1 414 ? 26.054  11.682  25.285  1.00 20.80  ? 443 GLY A N   1 
ATOM   3259  C CA  . GLY A 1 414 ? 25.657  11.257  26.611  1.00 23.96  ? 443 GLY A CA  1 
ATOM   3260  C C   . GLY A 1 414 ? 24.296  11.796  27.060  1.00 22.28  ? 443 GLY A C   1 
ATOM   3261  O O   . GLY A 1 414 ? 24.104  11.994  28.252  1.00 19.56  ? 443 GLY A O   1 
ATOM   3262  N N   . PHE A 1 415 ? 23.345  11.986  26.120  1.00 23.95  ? 444 PHE A N   1 
ATOM   3263  C CA  . PHE A 1 415 ? 22.001  12.458  26.471  1.00 21.40  ? 444 PHE A CA  1 
ATOM   3264  C C   . PHE A 1 415 ? 21.369  11.414  27.378  1.00 19.63  ? 444 PHE A C   1 
ATOM   3265  O O   . PHE A 1 415 ? 21.501  10.232  27.096  1.00 18.65  ? 444 PHE A O   1 
ATOM   3266  C CB  . PHE A 1 415 ? 21.104  12.690  25.249  1.00 21.84  ? 444 PHE A CB  1 
ATOM   3267  C CG  . PHE A 1 415 ? 21.429  13.874  24.364  1.00 22.12  ? 444 PHE A CG  1 
ATOM   3268  C CD1 . PHE A 1 415 ? 22.470  14.746  24.647  1.00 21.51  ? 444 PHE A CD1 1 
ATOM   3269  C CD2 . PHE A 1 415 ? 20.698  14.093  23.207  1.00 21.69  ? 444 PHE A CD2 1 
ATOM   3270  C CE1 . PHE A 1 415 ? 22.762  15.818  23.812  1.00 23.27  ? 444 PHE A CE1 1 
ATOM   3271  C CE2 . PHE A 1 415 ? 20.989  15.167  22.376  1.00 23.20  ? 444 PHE A CE2 1 
ATOM   3272  C CZ  . PHE A 1 415 ? 22.034  16.013  22.665  1.00 21.58  ? 444 PHE A CZ  1 
ATOM   3273  N N   . PRO A 1 416 ? 20.734  11.817  28.504  1.00 19.97  ? 445 PRO A N   1 
ATOM   3274  C CA  . PRO A 1 416 ? 20.135  10.875  29.448  1.00 20.07  ? 445 PRO A CA  1 
ATOM   3275  C C   . PRO A 1 416 ? 18.723  10.398  29.121  1.00 18.21  ? 445 PRO A C   1 
ATOM   3276  O O   . PRO A 1 416 ? 18.110  10.802  28.148  1.00 17.19  ? 445 PRO A O   1 
ATOM   3277  C CB  . PRO A 1 416 ? 20.073  11.674  30.751  1.00 19.86  ? 445 PRO A CB  1 
ATOM   3278  C CG  . PRO A 1 416 ? 19.904  13.104  30.306  1.00 21.40  ? 445 PRO A CG  1 
ATOM   3279  C CD  . PRO A 1 416 ? 20.599  13.222  28.958  1.00 20.32  ? 445 PRO A CD  1 
ATOM   3280  N N   . LEU A 1 417 ? 18.209  9.551   30.009  1.00 20.20  ? 446 LEU A N   1 
ATOM   3281  C CA  . LEU A 1 417 ? 16.842  9.088   29.956  1.00 19.02  ? 446 LEU A CA  1 
ATOM   3282  C C   . LEU A 1 417 ? 15.934  10.294  29.747  1.00 19.93  ? 446 LEU A C   1 
ATOM   3283  O O   . LEU A 1 417 ? 16.068  11.301  30.455  1.00 20.42  ? 446 LEU A O   1 
ATOM   3284  C CB  . LEU A 1 417 ? 16.506  8.394   31.275  1.00 22.68  ? 446 LEU A CB  1 
ATOM   3285  C CG  . LEU A 1 417 ? 15.263  7.520   31.266  1.00 22.97  ? 446 LEU A CG  1 
ATOM   3286  C CD1 . LEU A 1 417 ? 15.598  6.173   30.679  1.00 22.42  ? 446 LEU A CD1 1 
ATOM   3287  C CD2 . LEU A 1 417 ? 14.692  7.361   32.670  1.00 25.81  ? 446 LEU A CD2 1 
ATOM   3288  N N   . GLU A 1 418 ? 15.075  10.183  28.732  1.00 17.76  ? 447 GLU A N   1 
ATOM   3289  C CA  . GLU A 1 418 ? 13.958  11.108  28.576  1.00 20.09  ? 447 GLU A CA  1 
ATOM   3290  C C   . GLU A 1 418 ? 12.857  10.689  29.535  1.00 20.91  ? 447 GLU A C   1 
ATOM   3291  O O   . GLU A 1 418 ? 12.310  9.586   29.477  1.00 21.64  ? 447 GLU A O   1 
ATOM   3292  C CB  . GLU A 1 418 ? 13.392  11.177  27.163  1.00 21.88  ? 447 GLU A CB  1 
ATOM   3293  C CG  . GLU A 1 418 ? 12.342  12.271  27.036  1.00 21.22  ? 447 GLU A CG  1 
ATOM   3294  C CD  . GLU A 1 418 ? 11.771  12.389  25.634  1.00 23.71  ? 447 GLU A CD  1 
ATOM   3295  O OE1 . GLU A 1 418 ? 12.595  12.608  24.699  1.00 21.94  ? 447 GLU A OE1 1 
ATOM   3296  O OE2 . GLU A 1 418 ? 10.487  12.209  25.478  1.00 19.31  ? 447 GLU A OE2 1 
ATOM   3297  N N   . ARG A 1 419 ? 12.507  11.613  30.413  1.00 20.29  ? 448 ARG A N   1 
ATOM   3298  C CA  . ARG A 1 419 ? 11.640  11.276  31.509  1.00 20.49  ? 448 ARG A CA  1 
ATOM   3299  C C   . ARG A 1 419 ? 11.078  12.578  32.054  1.00 20.59  ? 448 ARG A C   1 
ATOM   3300  O O   . ARG A 1 419 ? 11.598  13.122  33.031  1.00 21.89  ? 448 ARG A O   1 
ATOM   3301  C CB  . ARG A 1 419 ? 12.423  10.471  32.540  1.00 21.47  ? 448 ARG A CB  1 
ATOM   3302  C CG  . ARG A 1 419 ? 11.560  9.546   33.376  1.00 19.88  ? 448 ARG A CG  1 
ATOM   3303  C CD  . ARG A 1 419 ? 10.436  10.254  34.131  1.00 19.07  ? 448 ARG A CD  1 
ATOM   3304  N NE  . ARG A 1 419 ? 9.640   9.260   34.847  1.00 20.94  ? 448 ARG A NE  1 
ATOM   3305  C CZ  . ARG A 1 419 ? 8.392   9.414   35.279  1.00 20.74  ? 448 ARG A CZ  1 
ATOM   3306  N NH1 . ARG A 1 419 ? 7.805   8.413   35.917  1.00 22.09  ? 448 ARG A NH1 1 
ATOM   3307  N NH2 . ARG A 1 419 ? 7.708   10.528  35.035  1.00 20.68  ? 448 ARG A NH2 1 
ATOM   3308  N N   . PRO A 1 420 ? 9.997   13.093  31.422  1.00 20.58  ? 449 PRO A N   1 
ATOM   3309  C CA  . PRO A 1 420 ? 9.310   14.268  31.946  1.00 22.71  ? 449 PRO A CA  1 
ATOM   3310  C C   . PRO A 1 420 ? 8.415   13.882  33.112  1.00 21.76  ? 449 PRO A C   1 
ATOM   3311  O O   . PRO A 1 420 ? 8.258   12.714  33.436  1.00 20.20  ? 449 PRO A O   1 
ATOM   3312  C CB  . PRO A 1 420 ? 8.495   14.748  30.722  1.00 19.29  ? 449 PRO A CB  1 
ATOM   3313  C CG  . PRO A 1 420 ? 8.083   13.430  30.065  1.00 20.02  ? 449 PRO A CG  1 
ATOM   3314  C CD  . PRO A 1 420 ? 9.355   12.603  30.181  1.00 21.19  ? 449 PRO A CD  1 
ATOM   3315  N N   . LYS A 1 421 ? 7.858   14.895  33.759  1.00 22.57  ? 450 LYS A N   1 
ATOM   3316  C CA  . LYS A 1 421 ? 6.876   14.734  34.823  1.00 21.98  ? 450 LYS A CA  1 
ATOM   3317  C C   . LYS A 1 421 ? 5.462   14.867  34.255  1.00 20.93  ? 450 LYS A C   1 
ATOM   3318  O O   . LYS A 1 421 ? 5.217   15.768  33.468  1.00 23.62  ? 450 LYS A O   1 
ATOM   3319  C CB  . LYS A 1 421 ? 7.054   15.881  35.827  1.00 23.45  ? 450 LYS A CB  1 
ATOM   3320  C CG  . LYS A 1 421 ? 6.031   15.899  36.946  1.00 25.86  ? 450 LYS A CG  1 
ATOM   3321  C CD  . LYS A 1 421 ? 6.184   14.734  37.934  1.00 29.00  ? 450 LYS A CD  1 
ATOM   3322  C CE  . LYS A 1 421 ? 4.988   14.601  38.856  1.00 31.29  ? 450 LYS A CE  1 
ATOM   3323  N NZ  . LYS A 1 421 ? 5.405   14.235  40.233  1.00 35.25  ? 450 LYS A NZ  1 
ATOM   3324  N N   . SER A 1 422 ? 4.560   13.952  34.619  1.00 19.30  ? 451 SER A N   1 
ATOM   3325  C CA  . SER A 1 422 ? 3.157   14.033  34.248  1.00 20.10  ? 451 SER A CA  1 
ATOM   3326  C C   . SER A 1 422 ? 2.315   14.548  35.414  1.00 20.54  ? 451 SER A C   1 
ATOM   3327  O O   . SER A 1 422 ? 2.777   14.613  36.558  1.00 20.57  ? 451 SER A O   1 
ATOM   3328  C CB  . SER A 1 422 ? 2.665   12.708  33.758  1.00 20.19  ? 451 SER A CB  1 
ATOM   3329  O OG  . SER A 1 422 ? 2.608   11.784  34.809  1.00 18.22  ? 451 SER A OG  1 
ATOM   3330  N N   . MET A 1 423 ? 1.074   14.933  35.097  1.00 21.99  ? 452 MET A N   1 
ATOM   3331  C CA  . MET A 1 423 ? 0.095   15.304  36.092  1.00 22.95  ? 452 MET A CA  1 
ATOM   3332  C C   . MET A 1 423 ? -1.282  14.791  35.671  1.00 20.84  ? 452 MET A C   1 
ATOM   3333  O O   . MET A 1 423 ? -1.565  14.677  34.492  1.00 19.84  ? 452 MET A O   1 
ATOM   3334  C CB  . MET A 1 423 ? 0.086   16.828  36.230  1.00 26.95  ? 452 MET A CB  1 
ATOM   3335  C CG  . MET A 1 423 ? 1.385   17.363  36.787  1.00 31.23  ? 452 MET A CG  1 
ATOM   3336  S SD  . MET A 1 423 ? 1.412   17.394  38.592  1.00 45.82  ? 452 MET A SD  1 
ATOM   3337  C CE  . MET A 1 423 ? 0.476   18.903  38.872  1.00 36.73  ? 452 MET A CE  1 
ATOM   3338  N N   . SER A 1 424 ? -2.157  14.511  36.640  1.00 20.57  ? 453 SER A N   1 
ATOM   3339  C CA  . SER A 1 424 ? -3.542  14.209  36.328  1.00 22.56  ? 453 SER A CA  1 
ATOM   3340  C C   . SER A 1 424 ? -4.323  15.524  36.263  1.00 23.32  ? 453 SER A C   1 
ATOM   3341  O O   . SER A 1 424 ? -3.790  16.583  36.606  1.00 28.79  ? 453 SER A O   1 
ATOM   3342  C CB  . SER A 1 424 ? -4.165  13.248  37.297  1.00 23.71  ? 453 SER A CB  1 
ATOM   3343  O OG  . SER A 1 424 ? -4.157  13.762  38.615  1.00 24.90  ? 453 SER A OG  1 
ATOM   3344  N N   . THR A 1 425 ? -5.562  15.434  35.807  1.00 24.00  ? 454 THR A N   1 
ATOM   3345  C CA  . THR A 1 425 ? -6.455  16.588  35.785  1.00 25.24  ? 454 THR A CA  1 
ATOM   3346  C C   . THR A 1 425 ? -6.691  17.042  37.226  1.00 26.80  ? 454 THR A C   1 
ATOM   3347  O O   . THR A 1 425 ? -6.496  18.205  37.590  1.00 26.72  ? 454 THR A O   1 
ATOM   3348  C CB  . THR A 1 425 ? -7.766  16.262  35.057  1.00 27.19  ? 454 THR A CB  1 
ATOM   3349  O OG1 . THR A 1 425 ? -7.597  16.068  33.643  1.00 23.81  ? 454 THR A OG1 1 
ATOM   3350  C CG2 . THR A 1 425 ? -8.783  17.372  35.239  1.00 27.27  ? 454 THR A CG2 1 
ATOM   3351  N N   . GLU A 1 426 ? -7.120  16.097  38.046  1.00 23.16  ? 455 GLU A N   1 
ATOM   3352  C CA  . GLU A 1 426 ? -7.325  16.327  39.470  1.00 27.31  ? 455 GLU A CA  1 
ATOM   3353  C C   . GLU A 1 426 ? -6.154  17.101  40.085  1.00 26.54  ? 455 GLU A C   1 
ATOM   3354  O O   . GLU A 1 426 ? -6.372  18.122  40.733  1.00 28.19  ? 455 GLU A O   1 
ATOM   3355  C CB  . GLU A 1 426 ? -7.536  14.971  40.140  1.00 32.10  ? 455 GLU A CB  1 
ATOM   3356  C CG  . GLU A 1 426 ? -7.543  15.014  41.653  1.00 41.62  ? 455 GLU A CG  1 
ATOM   3357  C CD  . GLU A 1 426 ? -7.985  13.680  42.228  1.00 51.45  ? 455 GLU A CD  1 
ATOM   3358  O OE1 . GLU A 1 426 ? -9.031  13.169  41.778  1.00 55.42  ? 455 GLU A OE1 1 
ATOM   3359  O OE2 . GLU A 1 426 ? -7.268  13.141  43.098  1.00 63.68  ? 455 GLU A OE2 1 
ATOM   3360  N N   . GLY A 1 427 ? -4.922  16.584  39.888  1.00 24.16  ? 456 GLY A N   1 
ATOM   3361  C CA  . GLY A 1 427 ? -3.706  17.146  40.438  1.00 23.93  ? 456 GLY A CA  1 
ATOM   3362  C C   . GLY A 1 427 ? -3.416  18.532  39.886  1.00 27.84  ? 456 GLY A C   1 
ATOM   3363  O O   . GLY A 1 427 ? -2.963  19.416  40.618  1.00 31.26  ? 456 GLY A O   1 
ATOM   3364  N N   . LEU A 1 428 ? -3.692  18.706  38.585  1.00 28.26  ? 457 LEU A N   1 
ATOM   3365  C CA  . LEU A 1 428 ? -3.331  19.928  37.892  1.00 31.49  ? 457 LEU A CA  1 
ATOM   3366  C C   . LEU A 1 428 ? -4.259  21.042  38.369  1.00 31.91  ? 457 LEU A C   1 
ATOM   3367  O O   . LEU A 1 428 ? -3.865  22.196  38.490  1.00 33.31  ? 457 LEU A O   1 
ATOM   3368  C CB  . LEU A 1 428 ? -3.442  19.619  36.397  1.00 34.57  ? 457 LEU A CB  1 
ATOM   3369  C CG  . LEU A 1 428 ? -2.939  20.655  35.406  1.00 35.49  ? 457 LEU A CG  1 
ATOM   3370  C CD1 . LEU A 1 428 ? -1.504  21.075  35.709  1.00 36.77  ? 457 LEU A CD1 1 
ATOM   3371  C CD2 . LEU A 1 428 ? -3.064  20.074  34.001  1.00 34.37  ? 457 LEU A CD2 1 
ATOM   3372  N N   . MET A 1 429 ? -5.496  20.683  38.697  1.00 33.63  ? 458 MET A N   1 
ATOM   3373  C CA  . MET A 1 429 ? -6.408  21.659  39.268  1.00 35.76  ? 458 MET A CA  1 
ATOM   3374  C C   . MET A 1 429 ? -5.902  22.098  40.640  1.00 39.99  ? 458 MET A C   1 
ATOM   3375  O O   . MET A 1 429 ? -5.866  23.296  40.930  1.00 37.69  ? 458 MET A O   1 
ATOM   3376  C CB  . MET A 1 429 ? -7.811  21.069  39.400  1.00 37.20  ? 458 MET A CB  1 
ATOM   3377  C CG  . MET A 1 429 ? -8.521  20.931  38.068  1.00 38.45  ? 458 MET A CG  1 
ATOM   3378  S SD  . MET A 1 429 ? -9.908  19.805  38.236  1.00 41.94  ? 458 MET A SD  1 
ATOM   3379  C CE  . MET A 1 429 ? -11.162 20.974  38.762  1.00 49.86  ? 458 MET A CE  1 
ATOM   3380  N N   . LYS A 1 430 ? -5.465  21.133  41.458  1.00 42.41  ? 459 LYS A N   1 
ATOM   3381  C CA  . LYS A 1 430 ? -4.979  21.424  42.800  1.00 46.43  ? 459 LYS A CA  1 
ATOM   3382  C C   . LYS A 1 430 ? -3.723  22.300  42.748  1.00 49.11  ? 459 LYS A C   1 
ATOM   3383  O O   . LYS A 1 430 ? -3.606  23.242  43.529  1.00 51.48  ? 459 LYS A O   1 
ATOM   3384  C CB  . LYS A 1 430 ? -4.725  20.132  43.584  1.00 45.23  ? 459 LYS A CB  1 
ATOM   3385  C CG  . LYS A 1 430 ? -5.979  19.476  44.138  1.00 48.81  ? 459 LYS A CG  1 
ATOM   3386  C CD  . LYS A 1 430 ? -5.702  18.500  45.259  1.00 52.30  ? 459 LYS A CD  1 
ATOM   3387  C CE  . LYS A 1 430 ? -5.074  17.213  44.774  1.00 52.29  ? 459 LYS A CE  1 
ATOM   3388  N NZ  . LYS A 1 430 ? -6.073  16.126  44.630  1.00 55.02  ? 459 LYS A NZ  1 
ATOM   3389  N N   . PHE A 1 431 ? -2.792  21.974  41.845  1.00 45.86  ? 460 PHE A N   1 
ATOM   3390  C CA  . PHE A 1 431 ? -1.543  22.703  41.688  1.00 48.31  ? 460 PHE A CA  1 
ATOM   3391  C C   . PHE A 1 431 ? -1.840  24.165  41.360  1.00 57.55  ? 460 PHE A C   1 
ATOM   3392  O O   . PHE A 1 431 ? -1.208  25.077  41.894  1.00 53.81  ? 460 PHE A O   1 
ATOM   3393  C CB  . PHE A 1 431 ? -0.710  22.070  40.570  1.00 46.65  ? 460 PHE A CB  1 
ATOM   3394  C CG  . PHE A 1 431 ? 0.701   22.591  40.411  1.00 49.08  ? 460 PHE A CG  1 
ATOM   3395  C CD1 . PHE A 1 431 ? 1.725   22.149  41.247  1.00 52.05  ? 460 PHE A CD1 1 
ATOM   3396  C CD2 . PHE A 1 431 ? 1.022   23.486  39.397  1.00 45.25  ? 460 PHE A CD2 1 
ATOM   3397  C CE1 . PHE A 1 431 ? 3.028   22.597  41.081  1.00 49.36  ? 460 PHE A CE1 1 
ATOM   3398  C CE2 . PHE A 1 431 ? 2.326   23.935  39.235  1.00 47.66  ? 460 PHE A CE2 1 
ATOM   3399  C CZ  . PHE A 1 431 ? 3.325   23.494  40.078  1.00 48.16  ? 460 PHE A CZ  1 
ATOM   3400  N N   . VAL A 1 432 ? -2.805  24.350  40.452  1.00 63.46  ? 461 VAL A N   1 
ATOM   3401  C CA  . VAL A 1 432 ? -3.267  25.655  40.009  1.00 65.63  ? 461 VAL A CA  1 
ATOM   3402  C C   . VAL A 1 432 ? -3.761  26.478  41.205  1.00 69.26  ? 461 VAL A C   1 
ATOM   3403  O O   . VAL A 1 432 ? -3.484  27.677  41.285  1.00 74.17  ? 461 VAL A O   1 
ATOM   3404  C CB  . VAL A 1 432 ? -4.340  25.475  38.911  1.00 66.37  ? 461 VAL A CB  1 
ATOM   3405  C CG1 . VAL A 1 432 ? -5.621  26.238  39.195  1.00 66.72  ? 461 VAL A CG1 1 
ATOM   3406  C CG2 . VAL A 1 432 ? -3.800  25.802  37.525  1.00 67.76  ? 461 VAL A CG2 1 
ATOM   3407  N N   . ASP A 1 433 ? -4.485  25.832  42.133  1.00 65.64  ? 462 ASP A N   1 
ATOM   3408  C CA  . ASP A 1 433 ? -5.042  26.505  43.299  1.00 65.73  ? 462 ASP A CA  1 
ATOM   3409  C C   . ASP A 1 433 ? -3.944  26.941  44.267  1.00 65.71  ? 462 ASP A C   1 
ATOM   3410  O O   . ASP A 1 433 ? -4.028  28.025  44.840  1.00 64.08  ? 462 ASP A O   1 
ATOM   3411  C CB  . ASP A 1 433 ? -6.055  25.626  44.036  1.00 65.44  ? 462 ASP A CB  1 
ATOM   3412  C CG  . ASP A 1 433 ? -7.450  25.701  43.446  1.00 64.62  ? 462 ASP A CG  1 
ATOM   3413  O OD1 . ASP A 1 433 ? -7.587  26.245  42.338  1.00 69.02  ? 462 ASP A OD1 1 
ATOM   3414  O OD2 . ASP A 1 433 ? -8.389  25.244  44.113  1.00 71.69  ? 462 ASP A OD2 1 
ATOM   3415  N N   . SER A 1 434 ? -2.949  26.070  44.471  1.00 59.55  ? 463 SER A N   1 
ATOM   3416  C CA  . SER A 1 434 ? -1.816  26.365  45.334  1.00 55.39  ? 463 SER A CA  1 
ATOM   3417  C C   . SER A 1 434 ? -0.722  27.089  44.536  1.00 55.74  ? 463 SER A C   1 
ATOM   3418  O O   . SER A 1 434 ? -0.966  28.248  44.136  1.00 54.78  ? 463 SER A O   1 
ATOM   3419  C CB  . SER A 1 434 ? -1.291  25.098  45.950  1.00 51.68  ? 463 SER A CB  1 
ATOM   3420  O OG  . SER A 1 434 ? -0.630  24.312  44.970  1.00 52.41  ? 463 SER A OG  1 
ATOM   3421  N N   . SER B 1 1   ? -25.585 -6.926  37.091  1.00 43.78  ? 30  SER B N   1 
ATOM   3422  C CA  . SER B 1 1   ? -24.648 -7.400  36.037  1.00 42.14  ? 30  SER B CA  1 
ATOM   3423  C C   . SER B 1 1   ? -23.566 -6.344  35.841  1.00 38.46  ? 30  SER B C   1 
ATOM   3424  O O   . SER B 1 1   ? -23.877 -5.174  35.621  1.00 36.51  ? 30  SER B O   1 
ATOM   3425  C CB  . SER B 1 1   ? -25.374 -7.707  34.738  1.00 43.65  ? 30  SER B CB  1 
ATOM   3426  O OG  . SER B 1 1   ? -24.519 -8.347  33.795  1.00 42.63  ? 30  SER B OG  1 
ATOM   3427  N N   . THR B 1 2   ? -22.304 -6.772  35.953  1.00 33.51  ? 31  THR B N   1 
ATOM   3428  C CA  . THR B 1 2   ? -21.170 -5.860  35.898  1.00 32.74  ? 31  THR B CA  1 
ATOM   3429  C C   . THR B 1 2   ? -20.703 -5.737  34.443  1.00 30.45  ? 31  THR B C   1 
ATOM   3430  O O   . THR B 1 2   ? -20.694 -6.706  33.684  1.00 29.26  ? 31  THR B O   1 
ATOM   3431  C CB  . THR B 1 2   ? -20.106 -6.297  36.922  1.00 34.74  ? 31  THR B CB  1 
ATOM   3432  O OG1 . THR B 1 2   ? -19.712 -7.633  36.631  1.00 46.30  ? 31  THR B OG1 1 
ATOM   3433  C CG2 . THR B 1 2   ? -20.618 -6.314  38.344  1.00 34.83  ? 31  THR B CG2 1 
ATOM   3434  N N   . ASN B 1 3   ? -20.374 -4.511  34.034  1.00 27.64  ? 32  ASN B N   1 
ATOM   3435  C CA  . ASN B 1 3   ? -19.769 -4.278  32.733  1.00 25.89  ? 32  ASN B CA  1 
ATOM   3436  C C   . ASN B 1 3   ? -18.990 -2.984  32.849  1.00 25.58  ? 32  ASN B C   1 
ATOM   3437  O O   . ASN B 1 3   ? -19.566 -1.920  33.027  1.00 25.59  ? 32  ASN B O   1 
ATOM   3438  C CB  . ASN B 1 3   ? -20.763 -4.220  31.567  1.00 25.26  ? 32  ASN B CB  1 
ATOM   3439  C CG  . ASN B 1 3   ? -20.126 -4.208  30.183  1.00 26.51  ? 32  ASN B CG  1 
ATOM   3440  O OD1 . ASN B 1 3   ? -18.929 -3.967  29.996  1.00 25.09  ? 32  ASN B OD1 1 
ATOM   3441  N ND2 . ASN B 1 3   ? -20.929 -4.512  29.186  1.00 28.66  ? 32  ASN B ND2 1 
ATOM   3442  N N   . LEU B 1 4   ? -17.669 -3.123  32.808  1.00 22.93  ? 33  LEU B N   1 
ATOM   3443  C CA  . LEU B 1 4   ? -16.763 -1.998  32.938  1.00 21.36  ? 33  LEU B CA  1 
ATOM   3444  C C   . LEU B 1 4   ? -16.984 -0.988  31.818  1.00 20.56  ? 33  LEU B C   1 
ATOM   3445  O O   . LEU B 1 4   ? -16.890 0.220   32.070  1.00 21.99  ? 33  LEU B O   1 
ATOM   3446  C CB  . LEU B 1 4   ? -15.329 -2.540  32.916  1.00 21.93  ? 33  LEU B CB  1 
ATOM   3447  C CG  . LEU B 1 4   ? -14.241 -1.485  33.023  1.00 19.82  ? 33  LEU B CG  1 
ATOM   3448  C CD1 . LEU B 1 4   ? -14.435 -0.638  34.249  1.00 21.39  ? 33  LEU B CD1 1 
ATOM   3449  C CD2 . LEU B 1 4   ? -12.866 -2.150  33.038  1.00 20.79  ? 33  LEU B CD2 1 
ATOM   3450  N N   . LYS B 1 5   ? -17.314 -1.458  30.606  1.00 22.02  ? 34  LYS B N   1 
ATOM   3451  C CA  . LYS B 1 5   ? -17.592 -0.551  29.499  1.00 21.75  ? 34  LYS B CA  1 
ATOM   3452  C C   . LYS B 1 5   ? -18.780 0.370   29.814  1.00 22.43  ? 34  LYS B C   1 
ATOM   3453  O O   . LYS B 1 5   ? -18.778 1.542   29.427  1.00 22.48  ? 34  LYS B O   1 
ATOM   3454  C CB  . LYS B 1 5   ? -17.816 -1.304  28.189  1.00 24.54  ? 34  LYS B CB  1 
ATOM   3455  C CG  . LYS B 1 5   ? -17.591 -0.476  26.941  1.00 25.77  ? 34  LYS B CG  1 
ATOM   3456  C CD  . LYS B 1 5   ? -17.764 -1.320  25.736  1.00 26.95  ? 34  LYS B CD  1 
ATOM   3457  C CE  . LYS B 1 5   ? -17.488 -0.620  24.428  1.00 27.00  ? 34  LYS B CE  1 
ATOM   3458  N NZ  . LYS B 1 5   ? -17.558 -1.591  23.323  1.00 26.96  ? 34  LYS B NZ  1 
ATOM   3459  N N   . ASP B 1 6   ? -19.762 -0.105  30.576  1.00 24.61  ? 35  ASP B N   1 
ATOM   3460  C CA  . ASP B 1 6   ? -20.899 0.751   30.894  1.00 26.47  ? 35  ASP B CA  1 
ATOM   3461  C C   . ASP B 1 6   ? -20.528 1.805   31.930  1.00 25.74  ? 35  ASP B C   1 
ATOM   3462  O O   . ASP B 1 6   ? -21.000 2.946   31.857  1.00 24.14  ? 35  ASP B O   1 
ATOM   3463  C CB  . ASP B 1 6   ? -22.086 -0.065  31.391  1.00 28.75  ? 35  ASP B CB  1 
ATOM   3464  C CG  . ASP B 1 6   ? -22.798 -0.866  30.324  1.00 32.12  ? 35  ASP B CG  1 
ATOM   3465  O OD1 . ASP B 1 6   ? -22.622 -0.560  29.122  1.00 34.35  ? 35  ASP B OD1 1 
ATOM   3466  O OD2 . ASP B 1 6   ? -23.511 -1.811  30.711  1.00 33.97  ? 35  ASP B OD2 1 
ATOM   3467  N N   . ILE B 1 7   ? -19.734 1.424   32.942  1.00 23.89  ? 36  ILE B N   1 
ATOM   3468  C CA  . ILE B 1 7   ? -19.262 2.397   33.909  1.00 26.56  ? 36  ILE B CA  1 
ATOM   3469  C C   . ILE B 1 7   ? -18.476 3.492   33.196  1.00 25.66  ? 36  ILE B C   1 
ATOM   3470  O O   . ILE B 1 7   ? -18.554 4.669   33.587  1.00 22.65  ? 36  ILE B O   1 
ATOM   3471  C CB  . ILE B 1 7   ? -18.428 1.725   35.018  1.00 29.96  ? 36  ILE B CB  1 
ATOM   3472  C CG1 . ILE B 1 7   ? -19.321 0.999   36.029  1.00 31.40  ? 36  ILE B CG1 1 
ATOM   3473  C CG2 . ILE B 1 7   ? -17.542 2.746   35.715  1.00 29.48  ? 36  ILE B CG2 1 
ATOM   3474  C CD1 . ILE B 1 7   ? -18.846 -0.374  36.369  1.00 34.63  ? 36  ILE B CD1 1 
ATOM   3475  N N   . LEU B 1 8   ? -17.664 3.084   32.205  1.00 26.13  ? 37  LEU B N   1 
ATOM   3476  C CA  . LEU B 1 8   ? -16.809 4.035   31.507  1.00 26.90  ? 37  LEU B CA  1 
ATOM   3477  C C   . LEU B 1 8   ? -17.695 5.040   30.777  1.00 27.63  ? 37  LEU B C   1 
ATOM   3478  O O   . LEU B 1 8   ? -17.469 6.260   30.820  1.00 26.07  ? 37  LEU B O   1 
ATOM   3479  C CB  . LEU B 1 8   ? -15.957 3.228   30.526  1.00 30.46  ? 37  LEU B CB  1 
ATOM   3480  C CG  . LEU B 1 8   ? -14.441 3.383   30.599  1.00 31.49  ? 37  LEU B CG  1 
ATOM   3481  C CD1 . LEU B 1 8   ? -13.951 3.715   31.996  1.00 33.09  ? 37  LEU B CD1 1 
ATOM   3482  C CD2 . LEU B 1 8   ? -13.803 2.094   30.084  1.00 29.96  ? 37  LEU B CD2 1 
ATOM   3483  N N   . ALA B 1 9   ? -18.718 4.492   30.107  1.00 29.12  ? 38  ALA B N   1 
ATOM   3484  C CA  . ALA B 1 9   ? -19.686 5.282   29.359  1.00 29.21  ? 38  ALA B CA  1 
ATOM   3485  C C   . ALA B 1 9   ? -20.254 6.393   30.237  1.00 28.70  ? 38  ALA B C   1 
ATOM   3486  O O   . ALA B 1 9   ? -20.390 7.526   29.792  1.00 30.91  ? 38  ALA B O   1 
ATOM   3487  C CB  . ALA B 1 9   ? -20.756 4.378   28.804  1.00 32.37  ? 38  ALA B CB  1 
ATOM   3488  N N   . ASP B 1 10  ? -20.571 6.087   31.497  1.00 30.55  ? 39  ASP B N   1 
ATOM   3489  C CA  . ASP B 1 10  ? -21.055 7.103   32.421  1.00 31.13  ? 39  ASP B CA  1 
ATOM   3490  C C   . ASP B 1 10  ? -19.989 8.126   32.766  1.00 29.76  ? 39  ASP B C   1 
ATOM   3491  O O   . ASP B 1 10  ? -20.294 9.308   32.898  1.00 28.13  ? 39  ASP B O   1 
ATOM   3492  C CB  . ASP B 1 10  ? -21.466 6.530   33.777  1.00 36.07  ? 39  ASP B CB  1 
ATOM   3493  C CG  . ASP B 1 10  ? -22.894 6.050   33.815  1.00 39.17  ? 39  ASP B CG  1 
ATOM   3494  O OD1 . ASP B 1 10  ? -23.137 4.918   33.386  1.00 44.26  ? 39  ASP B OD1 1 
ATOM   3495  O OD2 . ASP B 1 10  ? -23.734 6.821   34.277  1.00 35.24  ? 39  ASP B OD2 1 
ATOM   3496  N N   . LEU B 1 11  ? -18.753 7.660   33.003  1.00 25.82  ? 40  LEU B N   1 
ATOM   3497  C CA  . LEU B 1 11  ? -17.739 8.493   33.630  1.00 26.24  ? 40  LEU B CA  1 
ATOM   3498  C C   . LEU B 1 11  ? -17.174 9.498   32.631  1.00 25.33  ? 40  LEU B C   1 
ATOM   3499  O O   . LEU B 1 11  ? -16.871 10.627  33.013  1.00 28.19  ? 40  LEU B O   1 
ATOM   3500  C CB  . LEU B 1 11  ? -16.633 7.587   34.192  1.00 28.39  ? 40  LEU B CB  1 
ATOM   3501  C CG  . LEU B 1 11  ? -16.895 6.939   35.554  1.00 30.83  ? 40  LEU B CG  1 
ATOM   3502  C CD1 . LEU B 1 11  ? -15.736 6.035   35.932  1.00 32.04  ? 40  LEU B CD1 1 
ATOM   3503  C CD2 . LEU B 1 11  ? -17.112 7.976   36.653  1.00 30.22  ? 40  LEU B CD2 1 
ATOM   3504  N N   . ILE B 1 12  ? -17.087 9.111   31.353  1.00 24.45  ? 41  ILE B N   1 
ATOM   3505  C CA  . ILE B 1 12  ? -16.348 9.868   30.350  1.00 22.44  ? 41  ILE B CA  1 
ATOM   3506  C C   . ILE B 1 12  ? -16.954 11.254  30.145  1.00 23.16  ? 41  ILE B C   1 
ATOM   3507  O O   . ILE B 1 12  ? -16.219 12.240  30.211  1.00 22.44  ? 41  ILE B O   1 
ATOM   3508  C CB  . ILE B 1 12  ? -16.223 9.032   29.062  1.00 23.75  ? 41  ILE B CB  1 
ATOM   3509  C CG1 . ILE B 1 12  ? -15.118 7.989   29.239  1.00 22.55  ? 41  ILE B CG1 1 
ATOM   3510  C CG2 . ILE B 1 12  ? -15.995 9.899   27.829  1.00 25.82  ? 41  ILE B CG2 1 
ATOM   3511  C CD1 . ILE B 1 12  ? -15.183 6.839   28.285  1.00 20.33  ? 41  ILE B CD1 1 
ATOM   3512  N N   . PRO B 1 13  ? -18.276 11.380  29.871  1.00 24.36  ? 42  PRO B N   1 
ATOM   3513  C CA  . PRO B 1 13  ? -18.879 12.708  29.655  1.00 26.76  ? 42  PRO B CA  1 
ATOM   3514  C C   . PRO B 1 13  ? -18.663 13.667  30.824  1.00 25.05  ? 42  PRO B C   1 
ATOM   3515  O O   . PRO B 1 13  ? -18.567 14.886  30.631  1.00 25.83  ? 42  PRO B O   1 
ATOM   3516  C CB  . PRO B 1 13  ? -20.378 12.433  29.434  1.00 25.22  ? 42  PRO B CB  1 
ATOM   3517  C CG  . PRO B 1 13  ? -20.442 10.970  29.022  1.00 27.82  ? 42  PRO B CG  1 
ATOM   3518  C CD  . PRO B 1 13  ? -19.245 10.292  29.663  1.00 26.48  ? 42  PRO B CD  1 
ATOM   3519  N N   . LYS B 1 14  ? -18.600 13.132  32.044  1.00 26.77  ? 43  LYS B N   1 
ATOM   3520  C CA  . LYS B 1 14  ? -18.432 13.958  33.231  1.00 28.66  ? 43  LYS B CA  1 
ATOM   3521  C C   . LYS B 1 14  ? -17.036 14.578  33.214  1.00 29.08  ? 43  LYS B C   1 
ATOM   3522  O O   . LYS B 1 14  ? -16.894 15.785  33.410  1.00 31.33  ? 43  LYS B O   1 
ATOM   3523  C CB  . LYS B 1 14  ? -18.668 13.145  34.508  1.00 29.28  ? 43  LYS B CB  1 
ATOM   3524  C CG  . LYS B 1 14  ? -19.899 12.257  34.451  1.00 32.24  ? 43  LYS B CG  1 
ATOM   3525  C CD  . LYS B 1 14  ? -20.652 12.052  35.752  1.00 34.71  ? 43  LYS B CD  1 
ATOM   3526  C CE  . LYS B 1 14  ? -20.434 10.701  36.384  1.00 37.38  ? 43  LYS B CE  1 
ATOM   3527  N NZ  . LYS B 1 14  ? -21.663 10.237  37.064  1.00 41.27  ? 43  LYS B NZ  1 
ATOM   3528  N N   . GLU B 1 15  ? -16.013 13.747  32.971  1.00 26.23  ? 44  GLU B N   1 
ATOM   3529  C CA  . GLU B 1 15  ? -14.640 14.220  32.897  1.00 26.44  ? 44  GLU B CA  1 
ATOM   3530  C C   . GLU B 1 15  ? -14.413 15.133  31.690  1.00 24.27  ? 44  GLU B C   1 
ATOM   3531  O O   . GLU B 1 15  ? -13.581 16.047  31.779  1.00 28.76  ? 44  GLU B O   1 
ATOM   3532  C CB  . GLU B 1 15  ? -13.638 13.064  32.838  1.00 30.30  ? 44  GLU B CB  1 
ATOM   3533  C CG  . GLU B 1 15  ? -13.451 12.354  34.169  1.00 34.46  ? 44  GLU B CG  1 
ATOM   3534  C CD  . GLU B 1 15  ? -13.128 13.242  35.357  1.00 34.57  ? 44  GLU B CD  1 
ATOM   3535  O OE1 . GLU B 1 15  ? -12.060 13.873  35.350  1.00 36.97  ? 44  GLU B OE1 1 
ATOM   3536  O OE2 . GLU B 1 15  ? -13.958 13.318  36.270  1.00 41.71  ? 44  GLU B OE2 1 
ATOM   3537  N N   . GLN B 1 16  ? -15.128 14.908  30.580  1.00 23.66  ? 45  GLN B N   1 
ATOM   3538  C CA  . GLN B 1 16  ? -14.928 15.761  29.409  1.00 26.01  ? 45  GLN B CA  1 
ATOM   3539  C C   . GLN B 1 16  ? -15.367 17.189  29.763  1.00 26.16  ? 45  GLN B C   1 
ATOM   3540  O O   . GLN B 1 16  ? -14.622 18.143  29.544  1.00 27.03  ? 45  GLN B O   1 
ATOM   3541  C CB  . GLN B 1 16  ? -15.679 15.285  28.162  1.00 26.37  ? 45  GLN B CB  1 
ATOM   3542  C CG  . GLN B 1 16  ? -15.241 13.936  27.597  1.00 27.58  ? 45  GLN B CG  1 
ATOM   3543  C CD  . GLN B 1 16  ? -16.190 13.432  26.530  1.00 30.83  ? 45  GLN B CD  1 
ATOM   3544  O OE1 . GLN B 1 16  ? -17.400 13.620  26.603  1.00 31.78  ? 45  GLN B OE1 1 
ATOM   3545  N NE2 . GLN B 1 16  ? -15.660 12.792  25.495  1.00 33.33  ? 45  GLN B NE2 1 
ATOM   3546  N N   . ALA B 1 17  ? -16.561 17.296  30.340  1.00 28.76  ? 46  ALA B N   1 
ATOM   3547  C CA  . ALA B 1 17  ? -17.116 18.569  30.772  1.00 29.84  ? 46  ALA B CA  1 
ATOM   3548  C C   . ALA B 1 17  ? -16.150 19.269  31.716  1.00 30.63  ? 46  ALA B C   1 
ATOM   3549  O O   . ALA B 1 17  ? -15.829 20.436  31.524  1.00 33.03  ? 46  ALA B O   1 
ATOM   3550  C CB  . ALA B 1 17  ? -18.451 18.335  31.431  1.00 31.24  ? 46  ALA B CB  1 
ATOM   3551  N N   . ARG B 1 18  ? -15.673 18.543  32.727  1.00 29.73  ? 47  ARG B N   1 
ATOM   3552  C CA  . ARG B 1 18  ? -14.808 19.118  33.750  1.00 34.97  ? 47  ARG B CA  1 
ATOM   3553  C C   . ARG B 1 18  ? -13.542 19.711  33.127  1.00 33.78  ? 47  ARG B C   1 
ATOM   3554  O O   . ARG B 1 18  ? -13.107 20.803  33.489  1.00 34.83  ? 47  ARG B O   1 
ATOM   3555  C CB  . ARG B 1 18  ? -14.493 18.033  34.780  1.00 37.77  ? 47  ARG B CB  1 
ATOM   3556  C CG  . ARG B 1 18  ? -13.314 18.316  35.695  1.00 42.42  ? 47  ARG B CG  1 
ATOM   3557  C CD  . ARG B 1 18  ? -13.650 18.486  37.167  1.00 51.44  ? 47  ARG B CD  1 
ATOM   3558  N NE  . ARG B 1 18  ? -12.493 18.090  37.969  1.00 54.73  ? 47  ARG B NE  1 
ATOM   3559  C CZ  . ARG B 1 18  ? -12.363 16.930  38.606  1.00 57.65  ? 47  ARG B CZ  1 
ATOM   3560  N NH1 . ARG B 1 18  ? -11.172 16.552  39.045  1.00 57.19  ? 47  ARG B NH1 1 
ATOM   3561  N NH2 . ARG B 1 18  ? -13.398 16.115  38.725  1.00 55.77  ? 47  ARG B NH2 1 
ATOM   3562  N N   . ILE B 1 19  ? -12.917 18.958  32.220  1.00 32.73  ? 48  ILE B N   1 
ATOM   3563  C CA  . ILE B 1 19  ? -11.682 19.400  31.606  1.00 29.06  ? 48  ILE B CA  1 
ATOM   3564  C C   . ILE B 1 19  ? -11.985 20.563  30.664  1.00 28.66  ? 48  ILE B C   1 
ATOM   3565  O O   . ILE B 1 19  ? -11.149 21.426  30.465  1.00 28.52  ? 48  ILE B O   1 
ATOM   3566  C CB  . ILE B 1 19  ? -10.964 18.224  30.911  1.00 28.26  ? 48  ILE B CB  1 
ATOM   3567  C CG1 . ILE B 1 19  ? -10.403 17.267  31.966  1.00 27.03  ? 48  ILE B CG1 1 
ATOM   3568  C CG2 . ILE B 1 19  ? -9.887  18.721  29.966  1.00 26.64  ? 48  ILE B CG2 1 
ATOM   3569  C CD1 . ILE B 1 19  ? -10.107 15.884  31.464  1.00 24.61  ? 48  ILE B CD1 1 
ATOM   3570  N N   . LYS B 1 20  ? -13.169 20.589  30.068  1.00 30.25  ? 49  LYS B N   1 
ATOM   3571  C CA  . LYS B 1 20  ? -13.491 21.710  29.203  1.00 32.84  ? 49  LYS B CA  1 
ATOM   3572  C C   . LYS B 1 20  ? -13.555 22.988  30.040  1.00 31.31  ? 49  LYS B C   1 
ATOM   3573  O O   . LYS B 1 20  ? -12.883 23.972  29.719  1.00 25.84  ? 49  LYS B O   1 
ATOM   3574  C CB  . LYS B 1 20  ? -14.763 21.421  28.418  1.00 33.68  ? 49  LYS B CB  1 
ATOM   3575  C CG  . LYS B 1 20  ? -15.185 22.543  27.484  1.00 38.49  ? 49  LYS B CG  1 
ATOM   3576  C CD  . LYS B 1 20  ? -16.262 22.123  26.535  1.00 38.36  ? 49  LYS B CD  1 
ATOM   3577  C CE  . LYS B 1 20  ? -16.662 23.211  25.558  1.00 46.04  ? 49  LYS B CE  1 
ATOM   3578  N NZ  . LYS B 1 20  ? -17.690 24.121  26.118  1.00 47.83  ? 49  LYS B NZ  1 
ATOM   3579  N N   . THR B 1 21  ? -14.284 22.917  31.161  1.00 31.94  ? 50  THR B N   1 
ATOM   3580  C CA  . THR B 1 21  ? -14.441 24.028  32.093  1.00 32.79  ? 50  THR B CA  1 
ATOM   3581  C C   . THR B 1 21  ? -13.098 24.479  32.651  1.00 32.56  ? 50  THR B C   1 
ATOM   3582  O O   . THR B 1 21  ? -12.824 25.676  32.744  1.00 30.05  ? 50  THR B O   1 
ATOM   3583  C CB  . THR B 1 21  ? -15.280 23.617  33.310  1.00 35.62  ? 50  THR B CB  1 
ATOM   3584  O OG1 . THR B 1 21  ? -16.584 23.255  32.852  1.00 36.99  ? 50  THR B OG1 1 
ATOM   3585  C CG2 . THR B 1 21  ? -15.357 24.695  34.368  1.00 35.66  ? 50  THR B CG2 1 
ATOM   3586  N N   . PHE B 1 22  ? -12.292 23.498  33.069  1.00 35.31  ? 51  PHE B N   1 
ATOM   3587  C CA  . PHE B 1 22  ? -10.990 23.771  33.644  1.00 33.17  ? 51  PHE B CA  1 
ATOM   3588  C C   . PHE B 1 22  ? -10.119 24.504  32.626  1.00 29.43  ? 51  PHE B C   1 
ATOM   3589  O O   . PHE B 1 22  ? -9.482  25.496  32.969  1.00 32.98  ? 51  PHE B O   1 
ATOM   3590  C CB  . PHE B 1 22  ? -10.354 22.482  34.180  1.00 34.41  ? 51  PHE B CB  1 
ATOM   3591  C CG  . PHE B 1 22  ? -8.946  22.642  34.697  1.00 35.08  ? 51  PHE B CG  1 
ATOM   3592  C CD1 . PHE B 1 22  ? -8.605  23.690  35.539  1.00 32.62  ? 51  PHE B CD1 1 
ATOM   3593  C CD2 . PHE B 1 22  ? -7.950  21.739  34.350  1.00 33.76  ? 51  PHE B CD2 1 
ATOM   3594  C CE1 . PHE B 1 22  ? -7.303  23.841  36.000  1.00 33.70  ? 51  PHE B CE1 1 
ATOM   3595  C CE2 . PHE B 1 22  ? -6.653  21.879  34.835  1.00 33.41  ? 51  PHE B CE2 1 
ATOM   3596  C CZ  . PHE B 1 22  ? -6.325  22.940  35.647  1.00 34.01  ? 51  PHE B CZ  1 
ATOM   3597  N N   . ARG B 1 23  ? -10.092 24.042  31.369  1.00 28.20  ? 52  ARG B N   1 
ATOM   3598  C CA  . ARG B 1 23  ? -9.253  24.682  30.365  1.00 26.61  ? 52  ARG B CA  1 
ATOM   3599  C C   . ARG B 1 23  ? -9.793  26.070  30.015  1.00 27.04  ? 52  ARG B C   1 
ATOM   3600  O O   . ARG B 1 23  ? -9.009  26.971  29.727  1.00 25.19  ? 52  ARG B O   1 
ATOM   3601  C CB  . ARG B 1 23  ? -9.121  23.816  29.114  1.00 28.68  ? 52  ARG B CB  1 
ATOM   3602  C CG  . ARG B 1 23  ? -8.358  22.522  29.362  1.00 29.26  ? 52  ARG B CG  1 
ATOM   3603  C CD  . ARG B 1 23  ? -8.333  21.598  28.170  1.00 25.89  ? 52  ARG B CD  1 
ATOM   3604  N NE  . ARG B 1 23  ? -7.479  22.107  27.116  1.00 30.32  ? 52  ARG B NE  1 
ATOM   3605  C CZ  . ARG B 1 23  ? -7.295  21.523  25.932  1.00 27.25  ? 52  ARG B CZ  1 
ATOM   3606  N NH1 . ARG B 1 23  ? -7.830  20.343  25.663  1.00 26.80  ? 52  ARG B NH1 1 
ATOM   3607  N NH2 . ARG B 1 23  ? -6.531  22.110  25.035  1.00 33.33  ? 52  ARG B NH2 1 
ATOM   3608  N N   . GLN B 1 24  ? -11.126 26.185  30.004  1.00 30.54  ? 53  GLN B N   1 
ATOM   3609  C CA  . GLN B 1 24  ? -11.828 27.453  29.842  1.00 36.36  ? 53  GLN B CA  1 
ATOM   3610  C C   . GLN B 1 24  ? -11.251 28.474  30.826  1.00 34.64  ? 53  GLN B C   1 
ATOM   3611  O O   . GLN B 1 24  ? -10.959 29.607  30.448  1.00 41.33  ? 53  GLN B O   1 
ATOM   3612  C CB  . GLN B 1 24  ? -13.338 27.213  30.016  1.00 42.18  ? 53  GLN B CB  1 
ATOM   3613  C CG  . GLN B 1 24  ? -14.224 27.871  28.956  1.00 49.09  ? 53  GLN B CG  1 
ATOM   3614  C CD  . GLN B 1 24  ? -14.336 27.150  27.629  1.00 55.28  ? 53  GLN B CD  1 
ATOM   3615  O OE1 . GLN B 1 24  ? -14.056 27.704  26.564  1.00 60.83  ? 53  GLN B OE1 1 
ATOM   3616  N NE2 . GLN B 1 24  ? -14.801 25.914  27.665  1.00 59.93  ? 53  GLN B NE2 1 
ATOM   3617  N N   . GLN B 1 25  ? -11.038 28.068  32.087  1.00 35.35  ? 54  GLN B N   1 
ATOM   3618  C CA  . GLN B 1 25  ? -10.643 29.006  33.126  1.00 37.18  ? 54  GLN B CA  1 
ATOM   3619  C C   . GLN B 1 25  ? -9.123  29.045  33.303  1.00 35.63  ? 54  GLN B C   1 
ATOM   3620  O O   . GLN B 1 25  ? -8.592  30.105  33.601  1.00 38.34  ? 54  GLN B O   1 
ATOM   3621  C CB  . GLN B 1 25  ? -11.395 28.749  34.441  1.00 40.41  ? 54  GLN B CB  1 
ATOM   3622  C CG  . GLN B 1 25  ? -11.091 27.445  35.168  1.00 45.06  ? 54  GLN B CG  1 
ATOM   3623  C CD  . GLN B 1 25  ? -11.675 27.454  36.568  1.00 49.20  ? 54  GLN B CD  1 
ATOM   3624  O OE1 . GLN B 1 25  ? -11.199 28.157  37.458  1.00 49.42  ? 54  GLN B OE1 1 
ATOM   3625  N NE2 . GLN B 1 25  ? -12.734 26.687  36.782  1.00 52.10  ? 54  GLN B NE2 1 
ATOM   3626  N N   . HIS B 1 26  ? -8.414  27.920  33.113  1.00 32.76  ? 55  HIS B N   1 
ATOM   3627  C CA  . HIS B 1 26  ? -7.004  27.864  33.477  1.00 33.13  ? 55  HIS B CA  1 
ATOM   3628  C C   . HIS B 1 26  ? -6.073  27.491  32.322  1.00 30.57  ? 55  HIS B C   1 
ATOM   3629  O O   . HIS B 1 26  ? -4.873  27.363  32.543  1.00 28.83  ? 55  HIS B O   1 
ATOM   3630  C CB  . HIS B 1 26  ? -6.822  26.902  34.656  1.00 36.32  ? 55  HIS B CB  1 
ATOM   3631  C CG  . HIS B 1 26  ? -7.053  27.515  35.998  1.00 42.09  ? 55  HIS B CG  1 
ATOM   3632  N ND1 . HIS B 1 26  ? -6.287  28.548  36.497  1.00 43.21  ? 55  HIS B ND1 1 
ATOM   3633  C CD2 . HIS B 1 26  ? -7.948  27.217  36.951  1.00 42.63  ? 55  HIS B CD2 1 
ATOM   3634  C CE1 . HIS B 1 26  ? -6.727  28.867  37.709  1.00 43.15  ? 55  HIS B CE1 1 
ATOM   3635  N NE2 . HIS B 1 26  ? -7.729  28.070  38.002  1.00 44.24  ? 55  HIS B NE2 1 
ATOM   3636  N N   . GLY B 1 27  ? -6.594  27.365  31.096  1.00 30.57  ? 56  GLY B N   1 
ATOM   3637  C CA  . GLY B 1 27  ? -5.834  26.851  29.965  1.00 29.19  ? 56  GLY B CA  1 
ATOM   3638  C C   . GLY B 1 27  ? -4.542  27.624  29.727  1.00 30.56  ? 56  GLY B C   1 
ATOM   3639  O O   . GLY B 1 27  ? -3.506  27.054  29.376  1.00 28.76  ? 56  GLY B O   1 
ATOM   3640  N N   . LYS B 1 28  ? -4.612  28.938  29.930  1.00 28.19  ? 57  LYS B N   1 
ATOM   3641  C CA  . LYS B 1 28  ? -3.486  29.828  29.715  1.00 30.69  ? 57  LYS B CA  1 
ATOM   3642  C C   . LYS B 1 28  ? -2.556  29.925  30.932  1.00 30.41  ? 57  LYS B C   1 
ATOM   3643  O O   . LYS B 1 28  ? -1.519  30.585  30.838  1.00 31.05  ? 57  LYS B O   1 
ATOM   3644  C CB  . LYS B 1 28  ? -4.010  31.230  29.383  1.00 31.87  ? 57  LYS B CB  1 
ATOM   3645  C CG  . LYS B 1 28  ? -4.881  31.320  28.140  1.00 35.98  ? 57  LYS B CG  1 
ATOM   3646  C CD  . LYS B 1 28  ? -5.204  32.751  27.790  1.00 38.19  ? 57  LYS B CD  1 
ATOM   3647  C CE  . LYS B 1 28  ? -5.194  33.011  26.300  1.00 39.91  ? 57  LYS B CE  1 
ATOM   3648  N NZ  . LYS B 1 28  ? -5.349  34.456  25.999  1.00 40.06  ? 57  LYS B NZ  1 
ATOM   3649  N N   . THR B 1 29  ? -2.930  29.324  32.076  1.00 30.23  ? 58  THR B N   1 
ATOM   3650  C CA  . THR B 1 29  ? -2.124  29.399  33.285  1.00 30.46  ? 58  THR B CA  1 
ATOM   3651  C C   . THR B 1 29  ? -0.797  28.683  33.074  1.00 33.56  ? 58  THR B C   1 
ATOM   3652  O O   . THR B 1 29  ? -0.753  27.559  32.575  1.00 32.60  ? 58  THR B O   1 
ATOM   3653  C CB  . THR B 1 29  ? -2.827  28.816  34.518  1.00 32.99  ? 58  THR B CB  1 
ATOM   3654  O OG1 . THR B 1 29  ? -4.015  29.553  34.773  1.00 32.95  ? 58  THR B OG1 1 
ATOM   3655  C CG2 . THR B 1 29  ? -1.990  28.873  35.778  1.00 31.07  ? 58  THR B CG2 1 
ATOM   3656  N N   . VAL B 1 30  ? 0.279   29.369  33.449  1.00 36.39  ? 59  VAL B N   1 
ATOM   3657  C CA  . VAL B 1 30  ? 1.611   28.800  33.374  1.00 36.35  ? 59  VAL B CA  1 
ATOM   3658  C C   . VAL B 1 30  ? 1.763   27.826  34.535  1.00 36.41  ? 59  VAL B C   1 
ATOM   3659  O O   . VAL B 1 30  ? 1.397   28.155  35.653  1.00 35.47  ? 59  VAL B O   1 
ATOM   3660  C CB  . VAL B 1 30  ? 2.671   29.917  33.384  1.00 37.50  ? 59  VAL B CB  1 
ATOM   3661  C CG1 . VAL B 1 30  ? 4.064   29.391  33.686  1.00 36.98  ? 59  VAL B CG1 1 
ATOM   3662  C CG2 . VAL B 1 30  ? 2.652   30.695  32.078  1.00 36.21  ? 59  VAL B CG2 1 
ATOM   3663  N N   . VAL B 1 31  ? 2.295   26.632  34.244  1.00 37.10  ? 60  VAL B N   1 
ATOM   3664  C CA  . VAL B 1 31  ? 2.520   25.607  35.249  1.00 35.77  ? 60  VAL B CA  1 
ATOM   3665  C C   . VAL B 1 31  ? 4.012   25.282  35.381  1.00 36.96  ? 60  VAL B C   1 
ATOM   3666  O O   . VAL B 1 31  ? 4.409   24.541  36.286  1.00 34.56  ? 60  VAL B O   1 
ATOM   3667  C CB  . VAL B 1 31  ? 1.676   24.361  34.924  1.00 38.52  ? 60  VAL B CB  1 
ATOM   3668  C CG1 . VAL B 1 31  ? 0.201   24.615  35.178  1.00 40.69  ? 60  VAL B CG1 1 
ATOM   3669  C CG2 . VAL B 1 31  ? 1.879   23.887  33.501  1.00 40.99  ? 60  VAL B CG2 1 
ATOM   3670  N N   . GLY B 1 32  ? 4.849   25.835  34.494  1.00 34.50  ? 61  GLY B N   1 
ATOM   3671  C CA  . GLY B 1 32  ? 6.285   25.702  34.664  1.00 36.28  ? 61  GLY B CA  1 
ATOM   3672  C C   . GLY B 1 32  ? 7.068   26.323  33.518  1.00 38.64  ? 61  GLY B C   1 
ATOM   3673  O O   . GLY B 1 32  ? 6.508   26.938  32.615  1.00 34.89  ? 61  GLY B O   1 
ATOM   3674  N N   . GLN B 1 33  ? 8.393   26.184  33.589  1.00 43.32  ? 62  GLN B N   1 
ATOM   3675  C CA  . GLN B 1 33  ? 9.272   26.762  32.587  1.00 39.68  ? 62  GLN B CA  1 
ATOM   3676  C C   . GLN B 1 33  ? 9.973   25.622  31.846  1.00 37.56  ? 62  GLN B C   1 
ATOM   3677  O O   . GLN B 1 33  ? 9.867   24.460  32.223  1.00 37.41  ? 62  GLN B O   1 
ATOM   3678  C CB  . GLN B 1 33  ? 10.286  27.711  33.234  1.00 48.02  ? 62  GLN B CB  1 
ATOM   3679  C CG  . GLN B 1 33  ? 9.810   28.422  34.498  1.00 54.30  ? 62  GLN B CG  1 
ATOM   3680  C CD  . GLN B 1 33  ? 9.015   29.684  34.260  1.00 56.25  ? 62  GLN B CD  1 
ATOM   3681  O OE1 . GLN B 1 33  ? 7.917   29.848  34.790  1.00 60.84  ? 62  GLN B OE1 1 
ATOM   3682  N NE2 . GLN B 1 33  ? 9.585   30.610  33.501  1.00 52.45  ? 62  GLN B NE2 1 
ATOM   3683  N N   . ILE B 1 34  ? 10.677  25.967  30.768  1.00 37.10  ? 63  ILE B N   1 
ATOM   3684  C CA  . ILE B 1 34  ? 11.622  25.067  30.135  1.00 34.69  ? 63  ILE B CA  1 
ATOM   3685  C C   . ILE B 1 34  ? 12.987  25.753  30.145  1.00 32.65  ? 63  ILE B C   1 
ATOM   3686  O O   . ILE B 1 34  ? 13.097  26.891  29.695  1.00 33.85  ? 63  ILE B O   1 
ATOM   3687  C CB  . ILE B 1 34  ? 11.164  24.718  28.707  1.00 31.28  ? 63  ILE B CB  1 
ATOM   3688  C CG1 . ILE B 1 34  ? 9.809   24.000  28.711  1.00 35.01  ? 63  ILE B CG1 1 
ATOM   3689  C CG2 . ILE B 1 34  ? 12.236  23.901  28.009  1.00 35.71  ? 63  ILE B CG2 1 
ATOM   3690  C CD1 . ILE B 1 34  ? 9.120   23.904  27.346  1.00 34.73  ? 63  ILE B CD1 1 
ATOM   3691  N N   . THR B 1 35  ? 14.017  25.048  30.629  1.00 33.44  ? 64  THR B N   1 
ATOM   3692  C CA  . THR B 1 35  ? 15.391  25.538  30.598  1.00 36.24  ? 64  THR B CA  1 
ATOM   3693  C C   . THR B 1 35  ? 16.203  24.805  29.529  1.00 35.04  ? 64  THR B C   1 
ATOM   3694  O O   . THR B 1 35  ? 15.815  23.730  29.085  1.00 30.13  ? 64  THR B O   1 
ATOM   3695  C CB  . THR B 1 35  ? 16.113  25.346  31.937  1.00 35.31  ? 64  THR B CB  1 
ATOM   3696  O OG1 . THR B 1 35  ? 16.185  23.941  32.189  1.00 38.91  ? 64  THR B OG1 1 
ATOM   3697  C CG2 . THR B 1 35  ? 15.421  26.042  33.091  1.00 36.34  ? 64  THR B CG2 1 
ATOM   3698  N N   . VAL B 1 36  ? 17.347  25.393  29.155  1.00 33.83  ? 65  VAL B N   1 
ATOM   3699  C CA  . VAL B 1 36  ? 18.318  24.735  28.292  1.00 33.13  ? 65  VAL B CA  1 
ATOM   3700  C C   . VAL B 1 36  ? 18.656  23.387  28.924  1.00 32.36  ? 65  VAL B C   1 
ATOM   3701  O O   . VAL B 1 36  ? 18.548  22.348  28.283  1.00 31.12  ? 65  VAL B O   1 
ATOM   3702  C CB  . VAL B 1 36  ? 19.573  25.604  28.107  1.00 34.56  ? 65  VAL B CB  1 
ATOM   3703  C CG1 . VAL B 1 36  ? 20.671  24.910  27.304  1.00 36.09  ? 65  VAL B CG1 1 
ATOM   3704  C CG2 . VAL B 1 36  ? 19.225  26.945  27.479  1.00 35.00  ? 65  VAL B CG2 1 
ATOM   3705  N N   . ASP B 1 37  ? 19.008  23.420  30.210  1.00 32.47  ? 66  ASP B N   1 
ATOM   3706  C CA  . ASP B 1 37  ? 19.394  22.215  30.931  1.00 35.02  ? 66  ASP B CA  1 
ATOM   3707  C C   . ASP B 1 37  ? 18.332  21.130  30.785  1.00 31.66  ? 66  ASP B C   1 
ATOM   3708  O O   . ASP B 1 37  ? 18.678  19.967  30.585  1.00 26.32  ? 66  ASP B O   1 
ATOM   3709  C CB  . ASP B 1 37  ? 19.669  22.508  32.411  1.00 37.83  ? 66  ASP B CB  1 
ATOM   3710  C CG  . ASP B 1 37  ? 21.109  22.901  32.673  1.00 42.26  ? 66  ASP B CG  1 
ATOM   3711  O OD1 . ASP B 1 37  ? 21.907  22.826  31.715  1.00 46.85  ? 66  ASP B OD1 1 
ATOM   3712  O OD2 . ASP B 1 37  ? 21.422  23.276  33.825  1.00 47.62  ? 66  ASP B OD2 1 
ATOM   3713  N N   . MET B 1 38  ? 17.055  21.498  30.919  1.00 28.03  ? 67  MET B N   1 
ATOM   3714  C CA  . MET B 1 38  ? 15.969  20.542  30.714  1.00 28.52  ? 67  MET B CA  1 
ATOM   3715  C C   . MET B 1 38  ? 15.997  19.923  29.318  1.00 25.75  ? 67  MET B C   1 
ATOM   3716  O O   . MET B 1 38  ? 15.676  18.741  29.138  1.00 24.53  ? 67  MET B O   1 
ATOM   3717  C CB  . MET B 1 38  ? 14.606  21.214  30.888  1.00 31.61  ? 67  MET B CB  1 
ATOM   3718  C CG  . MET B 1 38  ? 13.997  21.003  32.261  1.00 36.56  ? 67  MET B CG  1 
ATOM   3719  S SD  . MET B 1 38  ? 12.648  22.182  32.588  1.00 41.31  ? 67  MET B SD  1 
ATOM   3720  C CE  . MET B 1 38  ? 12.752  22.348  34.369  1.00 42.85  ? 67  MET B CE  1 
ATOM   3721  N N   . MET B 1 39  ? 16.253  20.755  28.309  1.00 22.54  ? 68  MET B N   1 
ATOM   3722  C CA  . MET B 1 39  ? 16.215  20.290  26.936  1.00 23.47  ? 68  MET B CA  1 
ATOM   3723  C C   . MET B 1 39  ? 17.341  19.286  26.701  1.00 23.02  ? 68  MET B C   1 
ATOM   3724  O O   . MET B 1 39  ? 17.103  18.253  26.071  1.00 20.70  ? 68  MET B O   1 
ATOM   3725  C CB  . MET B 1 39  ? 16.328  21.465  25.973  1.00 26.08  ? 68  MET B CB  1 
ATOM   3726  C CG  . MET B 1 39  ? 15.010  22.221  25.870  1.00 25.03  ? 68  MET B CG  1 
ATOM   3727  S SD  . MET B 1 39  ? 15.221  23.558  24.721  1.00 27.68  ? 68  MET B SD  1 
ATOM   3728  C CE  . MET B 1 39  ? 15.263  22.622  23.190  1.00 28.51  ? 68  MET B CE  1 
ATOM   3729  N N   . TYR B 1 40  ? 18.533  19.575  27.256  1.00 21.66  ? 69  TYR B N   1 
ATOM   3730  C CA  . TYR B 1 40  ? 19.649  18.644  27.145  1.00 24.07  ? 69  TYR B CA  1 
ATOM   3731  C C   . TYR B 1 40  ? 19.441  17.417  28.025  1.00 24.60  ? 69  TYR B C   1 
ATOM   3732  O O   . TYR B 1 40  ? 19.945  16.349  27.698  1.00 25.25  ? 69  TYR B O   1 
ATOM   3733  C CB  . TYR B 1 40  ? 20.980  19.332  27.463  1.00 24.97  ? 69  TYR B CB  1 
ATOM   3734  C CG  . TYR B 1 40  ? 21.544  20.127  26.318  1.00 25.78  ? 69  TYR B CG  1 
ATOM   3735  C CD1 . TYR B 1 40  ? 22.169  19.500  25.248  1.00 22.85  ? 69  TYR B CD1 1 
ATOM   3736  C CD2 . TYR B 1 40  ? 21.388  21.500  26.267  1.00 26.82  ? 69  TYR B CD2 1 
ATOM   3737  C CE1 . TYR B 1 40  ? 22.696  20.222  24.193  1.00 25.00  ? 69  TYR B CE1 1 
ATOM   3738  C CE2 . TYR B 1 40  ? 21.897  22.232  25.214  1.00 27.22  ? 69  TYR B CE2 1 
ATOM   3739  C CZ  . TYR B 1 40  ? 22.541  21.591  24.177  1.00 24.54  ? 69  TYR B CZ  1 
ATOM   3740  O OH  . TYR B 1 40  ? 23.017  22.324  23.138  1.00 34.13  ? 69  TYR B OH  1 
ATOM   3741  N N   . GLY B 1 41  ? 18.735  17.576  29.150  1.00 25.75  ? 70  GLY B N   1 
ATOM   3742  C CA  . GLY B 1 41  ? 18.636  16.533  30.166  1.00 24.70  ? 70  GLY B CA  1 
ATOM   3743  C C   . GLY B 1 41  ? 17.324  15.733  30.148  1.00 22.50  ? 70  GLY B C   1 
ATOM   3744  O O   . GLY B 1 41  ? 16.740  15.463  31.200  1.00 21.11  ? 70  GLY B O   1 
ATOM   3745  N N   . GLY B 1 42  ? 16.911  15.265  28.964  1.00 22.07  ? 71  GLY B N   1 
ATOM   3746  C CA  . GLY B 1 42  ? 15.721  14.435  28.821  1.00 20.09  ? 71  GLY B CA  1 
ATOM   3747  C C   . GLY B 1 42  ? 14.475  14.931  29.555  1.00 21.32  ? 71  GLY B C   1 
ATOM   3748  O O   . GLY B 1 42  ? 13.690  14.128  30.063  1.00 22.47  ? 71  GLY B O   1 
ATOM   3749  N N   . MET B 1 43  ? 14.256  16.249  29.542  1.00 20.96  ? 72  MET B N   1 
ATOM   3750  C CA  . MET B 1 43  ? 13.003  16.841  29.993  1.00 24.81  ? 72  MET B CA  1 
ATOM   3751  C C   . MET B 1 43  ? 12.838  16.690  31.504  1.00 26.10  ? 72  MET B C   1 
ATOM   3752  O O   . MET B 1 43  ? 11.714  16.580  31.975  1.00 26.09  ? 72  MET B O   1 
ATOM   3753  C CB  . MET B 1 43  ? 11.795  16.160  29.355  1.00 24.60  ? 72  MET B CB  1 
ATOM   3754  C CG  . MET B 1 43  ? 11.716  16.253  27.851  1.00 24.68  ? 72  MET B CG  1 
ATOM   3755  S SD  . MET B 1 43  ? 10.193  15.454  27.291  1.00 28.24  ? 72  MET B SD  1 
ATOM   3756  C CE  . MET B 1 43  ? 10.306  15.762  25.526  1.00 28.91  ? 72  MET B CE  1 
ATOM   3757  N N   . ARG B 1 44  ? 13.944  16.643  32.248  1.00 27.24  ? 73  ARG B N   1 
ATOM   3758  C CA  . ARG B 1 44  ? 13.871  16.295  33.657  1.00 29.38  ? 73  ARG B CA  1 
ATOM   3759  C C   . ARG B 1 44  ? 13.127  17.408  34.396  1.00 28.13  ? 73  ARG B C   1 
ATOM   3760  O O   . ARG B 1 44  ? 13.526  18.572  34.320  1.00 30.76  ? 73  ARG B O   1 
ATOM   3761  C CB  . ARG B 1 44  ? 15.271  16.097  34.239  1.00 32.13  ? 73  ARG B CB  1 
ATOM   3762  C CG  . ARG B 1 44  ? 15.322  15.181  35.451  1.00 36.92  ? 73  ARG B CG  1 
ATOM   3763  C CD  . ARG B 1 44  ? 16.735  14.657  35.605  1.00 44.30  ? 73  ARG B CD  1 
ATOM   3764  N NE  . ARG B 1 44  ? 16.925  13.808  36.775  1.00 55.06  ? 73  ARG B NE  1 
ATOM   3765  C CZ  . ARG B 1 44  ? 17.081  12.489  36.729  1.00 56.02  ? 73  ARG B CZ  1 
ATOM   3766  N NH1 . ARG B 1 44  ? 16.734  11.823  35.641  1.00 61.56  ? 73  ARG B NH1 1 
ATOM   3767  N NH2 . ARG B 1 44  ? 17.539  11.836  37.785  1.00 56.30  ? 73  ARG B NH2 1 
ATOM   3768  N N   . GLY B 1 45  ? 12.030  17.031  35.061  1.00 28.22  ? 74  GLY B N   1 
ATOM   3769  C CA  . GLY B 1 45  ? 11.195  17.949  35.818  1.00 28.11  ? 74  GLY B CA  1 
ATOM   3770  C C   . GLY B 1 45  ? 10.429  18.937  34.943  1.00 28.18  ? 74  GLY B C   1 
ATOM   3771  O O   . GLY B 1 45  ? 9.963   19.967  35.419  1.00 29.78  ? 74  GLY B O   1 
ATOM   3772  N N   . MET B 1 46  ? 10.288  18.634  33.653  1.00 28.43  ? 75  MET B N   1 
ATOM   3773  C CA  . MET B 1 46  ? 9.430   19.419  32.792  1.00 26.77  ? 75  MET B CA  1 
ATOM   3774  C C   . MET B 1 46  ? 8.043   18.772  32.798  1.00 26.26  ? 75  MET B C   1 
ATOM   3775  O O   . MET B 1 46  ? 7.914   17.554  32.651  1.00 23.12  ? 75  MET B O   1 
ATOM   3776  C CB  . MET B 1 46  ? 10.066  19.482  31.401  1.00 29.33  ? 75  MET B CB  1 
ATOM   3777  C CG  . MET B 1 46  ? 9.239   20.091  30.334  1.00 34.62  ? 75  MET B CG  1 
ATOM   3778  S SD  . MET B 1 46  ? 9.917   19.710  28.689  1.00 39.35  ? 75  MET B SD  1 
ATOM   3779  C CE  . MET B 1 46  ? 11.446  20.634  28.760  1.00 36.40  ? 75  MET B CE  1 
ATOM   3780  N N   . LYS B 1 47  ? 6.991   19.584  32.967  1.00 26.58  ? 76  LYS B N   1 
ATOM   3781  C CA  . LYS B 1 47  ? 5.649   19.041  33.141  1.00 31.35  ? 76  LYS B CA  1 
ATOM   3782  C C   . LYS B 1 47  ? 5.002   18.905  31.762  1.00 30.70  ? 76  LYS B C   1 
ATOM   3783  O O   . LYS B 1 47  ? 4.383   19.829  31.239  1.00 34.43  ? 76  LYS B O   1 
ATOM   3784  C CB  . LYS B 1 47  ? 4.870   19.881  34.162  1.00 35.64  ? 76  LYS B CB  1 
ATOM   3785  C CG  . LYS B 1 47  ? 5.258   19.589  35.611  1.00 37.65  ? 76  LYS B CG  1 
ATOM   3786  C CD  . LYS B 1 47  ? 5.155   20.757  36.564  1.00 44.70  ? 76  LYS B CD  1 
ATOM   3787  C CE  . LYS B 1 47  ? 3.809   20.904  37.245  1.00 47.25  ? 76  LYS B CE  1 
ATOM   3788  N NZ  . LYS B 1 47  ? 2.681   20.749  36.293  1.00 49.72  ? 76  LYS B NZ  1 
ATOM   3789  N N   . GLY B 1 48  ? 5.155   17.723  31.164  1.00 26.91  ? 77  GLY B N   1 
ATOM   3790  C CA  . GLY B 1 48  ? 5.017   17.587  29.719  1.00 27.02  ? 77  GLY B CA  1 
ATOM   3791  C C   . GLY B 1 48  ? 3.669   17.042  29.273  1.00 24.52  ? 77  GLY B C   1 
ATOM   3792  O O   . GLY B 1 48  ? 3.290   17.206  28.120  1.00 22.59  ? 77  GLY B O   1 
ATOM   3793  N N   . LEU B 1 49  ? 2.948   16.358  30.165  1.00 23.03  ? 78  LEU B N   1 
ATOM   3794  C CA  . LEU B 1 49  ? 1.730   15.718  29.722  1.00 24.46  ? 78  LEU B CA  1 
ATOM   3795  C C   . LEU B 1 49  ? 0.796   15.439  30.889  1.00 20.61  ? 78  LEU B C   1 
ATOM   3796  O O   . LEU B 1 49  ? 1.204   15.292  32.041  1.00 21.80  ? 78  LEU B O   1 
ATOM   3797  C CB  . LEU B 1 49  ? 2.043   14.399  29.006  1.00 27.38  ? 78  LEU B CB  1 
ATOM   3798  C CG  . LEU B 1 49  ? 2.651   13.290  29.862  1.00 29.10  ? 78  LEU B CG  1 
ATOM   3799  C CD1 . LEU B 1 49  ? 2.232   11.928  29.349  1.00 33.95  ? 78  LEU B CD1 1 
ATOM   3800  C CD2 . LEU B 1 49  ? 4.164   13.388  29.881  1.00 32.26  ? 78  LEU B CD2 1 
ATOM   3801  N N   . VAL B 1 50  ? -0.477  15.323  30.505  1.00 21.86  ? 79  VAL B N   1 
ATOM   3802  C CA  . VAL B 1 50  ? -1.534  14.913  31.390  1.00 18.97  ? 79  VAL B CA  1 
ATOM   3803  C C   . VAL B 1 50  ? -1.672  13.398  31.231  1.00 18.88  ? 79  VAL B C   1 
ATOM   3804  O O   . VAL B 1 50  ? -1.710  12.858  30.123  1.00 17.54  ? 79  VAL B O   1 
ATOM   3805  C CB  . VAL B 1 50  ? -2.828  15.688  31.063  1.00 20.40  ? 79  VAL B CB  1 
ATOM   3806  C CG1 . VAL B 1 50  ? -3.936  15.402  32.064  1.00 21.09  ? 79  VAL B CG1 1 
ATOM   3807  C CG2 . VAL B 1 50  ? -2.572  17.187  30.971  1.00 22.25  ? 79  VAL B CG2 1 
ATOM   3808  N N   . TYR B 1 51  ? -1.724  12.735  32.373  1.00 18.08  ? 80  TYR B N   1 
ATOM   3809  C CA  . TYR B 1 51  ? -1.831  11.284  32.470  1.00 19.75  ? 80  TYR B CA  1 
ATOM   3810  C C   . TYR B 1 51  ? -2.627  11.008  33.738  1.00 19.61  ? 80  TYR B C   1 
ATOM   3811  O O   . TYR B 1 51  ? -2.241  11.483  34.802  1.00 22.01  ? 80  TYR B O   1 
ATOM   3812  C CB  . TYR B 1 51  ? -0.410  10.721  32.452  1.00 19.42  ? 80  TYR B CB  1 
ATOM   3813  C CG  . TYR B 1 51  ? -0.273  9.230   32.278  1.00 19.77  ? 80  TYR B CG  1 
ATOM   3814  C CD1 . TYR B 1 51  ? -0.352  8.389   33.364  1.00 19.70  ? 80  TYR B CD1 1 
ATOM   3815  C CD2 . TYR B 1 51  ? 0.011   8.683   31.046  1.00 19.78  ? 80  TYR B CD2 1 
ATOM   3816  C CE1 . TYR B 1 51  ? -0.221  7.015   33.217  1.00 21.99  ? 80  TYR B CE1 1 
ATOM   3817  C CE2 . TYR B 1 51  ? 0.145   7.309   30.880  1.00 18.96  ? 80  TYR B CE2 1 
ATOM   3818  C CZ  . TYR B 1 51  ? 0.021   6.474   31.972  1.00 18.56  ? 80  TYR B CZ  1 
ATOM   3819  O OH  . TYR B 1 51  ? 0.153   5.084   31.798  1.00 17.51  ? 80  TYR B OH  1 
ATOM   3820  N N   . GLU B 1 52  ? -3.744  10.277  33.614  1.00 22.57  ? 81  GLU B N   1 
ATOM   3821  C CA  . GLU B 1 52  ? -4.835  10.352  34.586  1.00 23.69  ? 81  GLU B CA  1 
ATOM   3822  C C   . GLU B 1 52  ? -4.721  9.231   35.624  1.00 23.10  ? 81  GLU B C   1 
ATOM   3823  O O   . GLU B 1 52  ? -5.164  9.371   36.763  1.00 21.36  ? 81  GLU B O   1 
ATOM   3824  C CB  . GLU B 1 52  ? -6.211  10.202  33.922  1.00 24.32  ? 81  GLU B CB  1 
ATOM   3825  C CG  . GLU B 1 52  ? -6.650  11.330  32.978  1.00 26.69  ? 81  GLU B CG  1 
ATOM   3826  C CD  . GLU B 1 52  ? -6.888  12.712  33.590  1.00 28.69  ? 81  GLU B CD  1 
ATOM   3827  O OE1 . GLU B 1 52  ? -6.557  12.911  34.787  1.00 28.43  ? 81  GLU B OE1 1 
ATOM   3828  O OE2 . GLU B 1 52  ? -7.354  13.609  32.851  1.00 31.38  ? 81  GLU B OE2 1 
ATOM   3829  N N   . THR B 1 53  ? -4.185  8.086   35.215  1.00 22.43  ? 82  THR B N   1 
ATOM   3830  C CA  . THR B 1 53  ? -4.362  6.855   35.977  1.00 20.69  ? 82  THR B CA  1 
ATOM   3831  C C   . THR B 1 53  ? -3.513  6.804   37.247  1.00 20.62  ? 82  THR B C   1 
ATOM   3832  O O   . THR B 1 53  ? -3.957  6.226   38.248  1.00 21.42  ? 82  THR B O   1 
ATOM   3833  C CB  . THR B 1 53  ? -4.073  5.632   35.108  1.00 21.53  ? 82  THR B CB  1 
ATOM   3834  O OG1 . THR B 1 53  ? -2.870  5.951   34.418  1.00 18.71  ? 82  THR B OG1 1 
ATOM   3835  C CG2 . THR B 1 53  ? -5.167  5.342   34.107  1.00 22.58  ? 82  THR B CG2 1 
ATOM   3836  N N   . SER B 1 54  ? -2.310  7.385   37.212  1.00 20.76  ? 83  SER B N   1 
ATOM   3837  C CA  . SER B 1 54  ? -1.430  7.393   38.363  1.00 20.05  ? 83  SER B CA  1 
ATOM   3838  C C   . SER B 1 54  ? -0.602  8.669   38.348  1.00 21.83  ? 83  SER B C   1 
ATOM   3839  O O   . SER B 1 54  ? -0.372  9.251   37.293  1.00 20.83  ? 83  SER B O   1 
ATOM   3840  C CB  . SER B 1 54  ? -0.557  6.141   38.410  1.00 20.83  ? 83  SER B CB  1 
ATOM   3841  O OG  . SER B 1 54  ? 0.411   6.154   37.360  1.00 21.48  ? 83  SER B OG  1 
ATOM   3842  N N   . VAL B 1 55  ? -0.198  9.107   39.541  1.00 23.53  ? 84  VAL B N   1 
ATOM   3843  C CA  . VAL B 1 55  ? 0.716   10.215  39.713  1.00 21.96  ? 84  VAL B CA  1 
ATOM   3844  C C   . VAL B 1 55  ? 1.812   9.859   40.721  1.00 22.60  ? 84  VAL B C   1 
ATOM   3845  O O   . VAL B 1 55  ? 1.546   9.309   41.787  1.00 20.86  ? 84  VAL B O   1 
ATOM   3846  C CB  . VAL B 1 55  ? -0.028  11.488  40.139  1.00 23.73  ? 84  VAL B CB  1 
ATOM   3847  C CG1 . VAL B 1 55  ? 0.964   12.626  40.324  1.00 24.42  ? 84  VAL B CG1 1 
ATOM   3848  C CG2 . VAL B 1 55  ? -1.118  11.857  39.138  1.00 22.12  ? 84  VAL B CG2 1 
ATOM   3849  N N   . LEU B 1 56  ? 3.052   10.217  40.371  1.00 23.65  ? 85  LEU B N   1 
ATOM   3850  C CA  . LEU B 1 56  ? 4.218   10.011  41.199  1.00 22.87  ? 85  LEU B CA  1 
ATOM   3851  C C   . LEU B 1 56  ? 4.563   11.326  41.900  1.00 23.62  ? 85  LEU B C   1 
ATOM   3852  O O   . LEU B 1 56  ? 4.916   12.282  41.217  1.00 24.24  ? 85  LEU B O   1 
ATOM   3853  C CB  . LEU B 1 56  ? 5.333   9.539   40.257  1.00 26.29  ? 85  LEU B CB  1 
ATOM   3854  C CG  . LEU B 1 56  ? 6.663   9.095   40.865  1.00 26.50  ? 85  LEU B CG  1 
ATOM   3855  C CD1 . LEU B 1 56  ? 6.473   8.065   41.972  1.00 28.28  ? 85  LEU B CD1 1 
ATOM   3856  C CD2 . LEU B 1 56  ? 7.565   8.546   39.780  1.00 25.81  ? 85  LEU B CD2 1 
ATOM   3857  N N   . ASP B 1 57  ? 4.417   11.361  43.241  1.00 24.07  ? 86  ASP B N   1 
ATOM   3858  C CA  . ASP B 1 57  ? 5.006   12.396  44.089  1.00 28.52  ? 86  ASP B CA  1 
ATOM   3859  C C   . ASP B 1 57  ? 6.482   12.058  44.341  1.00 28.48  ? 86  ASP B C   1 
ATOM   3860  O O   . ASP B 1 57  ? 6.817   10.902  44.641  1.00 26.27  ? 86  ASP B O   1 
ATOM   3861  C CB  . ASP B 1 57  ? 4.233   12.520  45.408  1.00 31.43  ? 86  ASP B CB  1 
ATOM   3862  C CG  . ASP B 1 57  ? 4.837   13.459  46.438  1.00 32.62  ? 86  ASP B CG  1 
ATOM   3863  O OD1 . ASP B 1 57  ? 5.315   14.549  46.058  1.00 33.58  ? 86  ASP B OD1 1 
ATOM   3864  O OD2 . ASP B 1 57  ? 4.760   13.118  47.638  1.00 41.19  ? 86  ASP B OD2 1 
ATOM   3865  N N   . PRO B 1 58  ? 7.433   13.004  44.160  1.00 29.11  ? 87  PRO B N   1 
ATOM   3866  C CA  . PRO B 1 58  ? 8.854   12.722  44.409  1.00 30.41  ? 87  PRO B CA  1 
ATOM   3867  C C   . PRO B 1 58  ? 9.158   12.270  45.838  1.00 34.56  ? 87  PRO B C   1 
ATOM   3868  O O   . PRO B 1 58  ? 10.072  11.474  46.086  1.00 31.30  ? 87  PRO B O   1 
ATOM   3869  C CB  . PRO B 1 58  ? 9.539   14.077  44.152  1.00 35.14  ? 87  PRO B CB  1 
ATOM   3870  C CG  . PRO B 1 58  ? 8.609   14.802  43.201  1.00 33.87  ? 87  PRO B CG  1 
ATOM   3871  C CD  . PRO B 1 58  ? 7.219   14.355  43.606  1.00 34.78  ? 87  PRO B CD  1 
ATOM   3872  N N   . ASP B 1 59  ? 8.344   12.801  46.759  1.00 35.61  ? 88  ASP B N   1 
ATOM   3873  C CA  . ASP B 1 59  ? 8.497   12.634  48.188  1.00 39.75  ? 88  ASP B CA  1 
ATOM   3874  C C   . ASP B 1 59  ? 7.786   11.365  48.654  1.00 38.67  ? 88  ASP B C   1 
ATOM   3875  O O   . ASP B 1 59  ? 8.343   10.634  49.466  1.00 39.34  ? 88  ASP B O   1 
ATOM   3876  C CB  . ASP B 1 59  ? 8.012   13.906  48.890  1.00 40.08  ? 88  ASP B CB  1 
ATOM   3877  C CG  . ASP B 1 59  ? 8.611   15.168  48.281  1.00 43.51  ? 88  ASP B CG  1 
ATOM   3878  O OD1 . ASP B 1 59  ? 9.853   15.329  48.342  1.00 45.26  ? 88  ASP B OD1 1 
ATOM   3879  O OD2 . ASP B 1 59  ? 7.842   15.964  47.718  1.00 45.14  ? 88  ASP B OD2 1 
ATOM   3880  N N   . GLU B 1 60  ? 6.594   11.067  48.123  1.00 35.14  ? 89  GLU B N   1 
ATOM   3881  C CA  . GLU B 1 60  ? 5.782   10.005  48.703  1.00 33.02  ? 89  GLU B CA  1 
ATOM   3882  C C   . GLU B 1 60  ? 5.690   8.751   47.845  1.00 32.20  ? 89  GLU B C   1 
ATOM   3883  O O   . GLU B 1 60  ? 5.298   7.701   48.364  1.00 32.21  ? 89  GLU B O   1 
ATOM   3884  C CB  . GLU B 1 60  ? 4.395   10.525  49.079  1.00 36.43  ? 89  GLU B CB  1 
ATOM   3885  C CG  . GLU B 1 60  ? 4.434   11.180  50.441  1.00 45.32  ? 89  GLU B CG  1 
ATOM   3886  C CD  . GLU B 1 60  ? 5.299   10.406  51.434  1.00 50.58  ? 89  GLU B CD  1 
ATOM   3887  O OE1 . GLU B 1 60  ? 5.478   9.178   51.255  1.00 57.40  ? 89  GLU B OE1 1 
ATOM   3888  O OE2 . GLU B 1 60  ? 5.828   11.012  52.370  1.00 55.25  ? 89  GLU B OE2 1 
ATOM   3889  N N   . GLY B 1 61  ? 6.076   8.850   46.567  1.00 27.69  ? 90  GLY B N   1 
ATOM   3890  C CA  . GLY B 1 61  ? 5.984   7.729   45.649  1.00 24.73  ? 90  GLY B CA  1 
ATOM   3891  C C   . GLY B 1 61  ? 4.651   7.713   44.912  1.00 24.82  ? 90  GLY B C   1 
ATOM   3892  O O   . GLY B 1 61  ? 3.952   8.711   44.871  1.00 22.45  ? 90  GLY B O   1 
ATOM   3893  N N   . ILE B 1 62  ? 4.347   6.575   44.294  1.00 25.89  ? 91  ILE B N   1 
ATOM   3894  C CA  . ILE B 1 62  ? 3.239   6.467   43.368  1.00 25.27  ? 91  ILE B CA  1 
ATOM   3895  C C   . ILE B 1 62  ? 1.932   6.443   44.142  1.00 24.86  ? 91  ILE B C   1 
ATOM   3896  O O   . ILE B 1 62  ? 1.842   5.834   45.198  1.00 21.88  ? 91  ILE B O   1 
ATOM   3897  C CB  . ILE B 1 62  ? 3.379   5.218   42.475  1.00 25.97  ? 91  ILE B CB  1 
ATOM   3898  C CG1 . ILE B 1 62  ? 2.465   5.284   41.247  1.00 25.44  ? 91  ILE B CG1 1 
ATOM   3899  C CG2 . ILE B 1 62  ? 3.128   3.934   43.259  1.00 25.64  ? 91  ILE B CG2 1 
ATOM   3900  C CD1 . ILE B 1 62  ? 2.799   6.373   40.262  1.00 23.80  ? 91  ILE B CD1 1 
ATOM   3901  N N   . ARG B 1 63  ? 0.945   7.142   43.581  1.00 24.29  ? 92  ARG B N   1 
ATOM   3902  C CA  . ARG B 1 63  ? -0.468  6.944   43.886  1.00 24.75  ? 92  ARG B CA  1 
ATOM   3903  C C   . ARG B 1 63  ? -1.199  6.562   42.601  1.00 22.87  ? 92  ARG B C   1 
ATOM   3904  O O   . ARG B 1 63  ? -0.923  7.128   41.549  1.00 19.10  ? 92  ARG B O   1 
ATOM   3905  C CB  . ARG B 1 63  ? -1.068  8.222   44.490  1.00 28.30  ? 92  ARG B CB  1 
ATOM   3906  C CG  . ARG B 1 63  ? -0.592  8.483   45.912  1.00 31.08  ? 92  ARG B CG  1 
ATOM   3907  C CD  . ARG B 1 63  ? -1.069  9.793   46.509  1.00 40.74  ? 92  ARG B CD  1 
ATOM   3908  N NE  . ARG B 1 63  ? -0.761  9.951   47.932  1.00 44.29  ? 92  ARG B NE  1 
ATOM   3909  C CZ  . ARG B 1 63  ? -1.339  9.280   48.926  1.00 48.64  ? 92  ARG B CZ  1 
ATOM   3910  N NH1 . ARG B 1 63  ? -2.159  8.275   48.676  1.00 47.82  ? 92  ARG B NH1 1 
ATOM   3911  N NH2 . ARG B 1 63  ? -1.084  9.615   50.183  1.00 50.68  ? 92  ARG B NH2 1 
ATOM   3912  N N   . PHE B 1 64  ? -2.065  5.540   42.711  1.00 21.99  ? 93  PHE B N   1 
ATOM   3913  C CA  . PHE B 1 64  ? -2.989  5.083   41.693  1.00 22.72  ? 93  PHE B CA  1 
ATOM   3914  C C   . PHE B 1 64  ? -4.343  5.732   41.960  1.00 22.40  ? 93  PHE B C   1 
ATOM   3915  O O   . PHE B 1 64  ? -5.021  5.377   42.931  1.00 21.61  ? 93  PHE B O   1 
ATOM   3916  C CB  . PHE B 1 64  ? -3.115  3.557   41.736  1.00 21.48  ? 93  PHE B CB  1 
ATOM   3917  C CG  . PHE B 1 64  ? -1.811  2.819   41.566  1.00 25.87  ? 93  PHE B CG  1 
ATOM   3918  C CD1 . PHE B 1 64  ? -1.105  2.881   40.376  1.00 24.89  ? 93  PHE B CD1 1 
ATOM   3919  C CD2 . PHE B 1 64  ? -1.281  2.064   42.604  1.00 27.80  ? 93  PHE B CD2 1 
ATOM   3920  C CE1 . PHE B 1 64  ? 0.099   2.206   40.229  1.00 26.61  ? 93  PHE B CE1 1 
ATOM   3921  C CE2 . PHE B 1 64  ? -0.070  1.402   42.459  1.00 29.34  ? 93  PHE B CE2 1 
ATOM   3922  C CZ  . PHE B 1 64  ? 0.613   1.461   41.263  1.00 28.52  ? 93  PHE B CZ  1 
ATOM   3923  N N   . ARG B 1 65  ? -4.703  6.725   41.139  1.00 19.39  ? 94  ARG B N   1 
ATOM   3924  C CA  . ARG B 1 65  ? -5.968  7.425   41.325  1.00 18.86  ? 94  ARG B CA  1 
ATOM   3925  C C   . ARG B 1 65  ? -6.103  7.904   42.785  1.00 19.20  ? 94  ARG B C   1 
ATOM   3926  O O   . ARG B 1 65  ? -7.191  7.842   43.369  1.00 21.77  ? 94  ARG B O   1 
ATOM   3927  C CB  . ARG B 1 65  ? -7.107  6.484   40.905  1.00 18.52  ? 94  ARG B CB  1 
ATOM   3928  C CG  . ARG B 1 65  ? -7.153  6.188   39.407  1.00 19.30  ? 94  ARG B CG  1 
ATOM   3929  C CD  . ARG B 1 65  ? -7.540  7.423   38.599  1.00 21.88  ? 94  ARG B CD  1 
ATOM   3930  N NE  . ARG B 1 65  ? -7.940  7.072   37.237  1.00 22.00  ? 94  ARG B NE  1 
ATOM   3931  C CZ  . ARG B 1 65  ? -8.482  7.904   36.356  1.00 26.58  ? 94  ARG B CZ  1 
ATOM   3932  N NH1 . ARG B 1 65  ? -8.575  9.194   36.639  1.00 25.97  ? 94  ARG B NH1 1 
ATOM   3933  N NH2 . ARG B 1 65  ? -8.895  7.449   35.184  1.00 27.53  ? 94  ARG B NH2 1 
ATOM   3934  N N   . GLY B 1 66  ? -5.000  8.375   43.359  1.00 21.64  ? 95  GLY B N   1 
ATOM   3935  C CA  . GLY B 1 66  ? -4.984  8.902   44.721  1.00 22.68  ? 95  GLY B CA  1 
ATOM   3936  C C   . GLY B 1 66  ? -4.572  7.885   45.793  1.00 21.55  ? 95  GLY B C   1 
ATOM   3937  O O   . GLY B 1 66  ? -4.271  8.276   46.929  1.00 20.08  ? 95  GLY B O   1 
ATOM   3938  N N   . PHE B 1 67  ? -4.589  6.585   45.468  1.00 20.86  ? 96  PHE B N   1 
ATOM   3939  C CA  . PHE B 1 67  ? -4.362  5.557   46.466  1.00 23.35  ? 96  PHE B CA  1 
ATOM   3940  C C   . PHE B 1 67  ? -2.908  5.067   46.461  1.00 25.40  ? 96  PHE B C   1 
ATOM   3941  O O   . PHE B 1 67  ? -2.371  4.721   45.401  1.00 22.52  ? 96  PHE B O   1 
ATOM   3942  C CB  . PHE B 1 67  ? -5.272  4.365   46.211  1.00 22.73  ? 96  PHE B CB  1 
ATOM   3943  C CG  . PHE B 1 67  ? -6.734  4.637   46.415  1.00 23.04  ? 96  PHE B CG  1 
ATOM   3944  C CD1 . PHE B 1 67  ? -7.303  4.537   47.680  1.00 25.82  ? 96  PHE B CD1 1 
ATOM   3945  C CD2 . PHE B 1 67  ? -7.529  5.008   45.346  1.00 22.71  ? 96  PHE B CD2 1 
ATOM   3946  C CE1 . PHE B 1 67  ? -8.650  4.821   47.856  1.00 26.82  ? 96  PHE B CE1 1 
ATOM   3947  C CE2 . PHE B 1 67  ? -8.878  5.273   45.525  1.00 25.73  ? 96  PHE B CE2 1 
ATOM   3948  C CZ  . PHE B 1 67  ? -9.430  5.190   46.787  1.00 23.60  ? 96  PHE B CZ  1 
ATOM   3949  N N   . SER B 1 68  ? -2.321  4.976   47.667  1.00 24.80  ? 97  SER B N   1 
ATOM   3950  C CA  . SER B 1 68  ? -0.952  4.515   47.838  1.00 26.64  ? 97  SER B CA  1 
ATOM   3951  C C   . SER B 1 68  ? -0.936  3.005   47.690  1.00 25.07  ? 97  SER B C   1 
ATOM   3952  O O   . SER B 1 68  ? -1.993  2.373   47.672  1.00 25.17  ? 97  SER B O   1 
ATOM   3953  C CB  . SER B 1 68  ? -0.375  4.940   49.160  1.00 27.91  ? 97  SER B CB  1 
ATOM   3954  O OG  . SER B 1 68  ? -1.117  4.356   50.214  1.00 27.76  ? 97  SER B OG  1 
ATOM   3955  N N   . ILE B 1 69  ? 0.276   2.447   47.588  1.00 27.24  ? 98  ILE B N   1 
ATOM   3956  C CA  . ILE B 1 69  ? 0.420   1.007   47.493  1.00 26.90  ? 98  ILE B CA  1 
ATOM   3957  C C   . ILE B 1 69  ? -0.125  0.355   48.761  1.00 27.33  ? 98  ILE B C   1 
ATOM   3958  O O   . ILE B 1 69  ? -0.924  -0.573  48.647  1.00 28.91  ? 98  ILE B O   1 
ATOM   3959  C CB  . ILE B 1 69  ? 1.864   0.595   47.155  1.00 28.85  ? 98  ILE B CB  1 
ATOM   3960  C CG1 . ILE B 1 69  ? 2.152   0.939   45.692  1.00 28.77  ? 98  ILE B CG1 1 
ATOM   3961  C CG2 . ILE B 1 69  ? 2.091   -0.888  47.447  1.00 26.22  ? 98  ILE B CG2 1 
ATOM   3962  C CD1 . ILE B 1 69  ? 3.594   0.848   45.301  1.00 31.28  ? 98  ILE B CD1 1 
ATOM   3963  N N   . PRO B 1 70  ? 0.302   0.768   49.982  1.00 28.61  ? 99  PRO B N   1 
ATOM   3964  C CA  . PRO B 1 70  ? -0.306  0.263   51.222  1.00 30.24  ? 99  PRO B CA  1 
ATOM   3965  C C   . PRO B 1 70  ? -1.833  0.312   51.259  1.00 29.21  ? 99  PRO B C   1 
ATOM   3966  O O   . PRO B 1 70  ? -2.461  -0.682  51.612  1.00 32.61  ? 99  PRO B O   1 
ATOM   3967  C CB  . PRO B 1 70  ? 0.294   1.158   52.308  1.00 27.77  ? 99  PRO B CB  1 
ATOM   3968  C CG  . PRO B 1 70  ? 1.659   1.519   51.761  1.00 28.47  ? 99  PRO B CG  1 
ATOM   3969  C CD  . PRO B 1 70  ? 1.467   1.637   50.256  1.00 25.07  ? 99  PRO B CD  1 
ATOM   3970  N N   . GLU B 1 71  ? -2.409  1.458   50.877  1.00 30.15  ? 100 GLU B N   1 
ATOM   3971  C CA  . GLU B 1 71  ? -3.854  1.596   50.739  1.00 29.07  ? 100 GLU B CA  1 
ATOM   3972  C C   . GLU B 1 71  ? -4.441  0.568   49.767  1.00 29.90  ? 100 GLU B C   1 
ATOM   3973  O O   . GLU B 1 71  ? -5.504  0.026   50.032  1.00 33.60  ? 100 GLU B O   1 
ATOM   3974  C CB  . GLU B 1 71  ? -4.200  3.017   50.302  1.00 29.87  ? 100 GLU B CB  1 
ATOM   3975  C CG  . GLU B 1 71  ? -4.074  4.040   51.410  1.00 35.02  ? 100 GLU B CG  1 
ATOM   3976  C CD  . GLU B 1 71  ? -4.038  5.501   50.987  1.00 38.52  ? 100 GLU B CD  1 
ATOM   3977  O OE1 . GLU B 1 71  ? -3.732  5.776   49.816  1.00 41.62  ? 100 GLU B OE1 1 
ATOM   3978  O OE2 . GLU B 1 71  ? -4.333  6.371   51.829  1.00 45.39  ? 100 GLU B OE2 1 
ATOM   3979  N N   . CYS B 1 72  ? -3.803  0.345   48.606  1.00 27.43  ? 101 CYS B N   1 
ATOM   3980  C CA  . CYS B 1 72  ? -4.256  -0.657  47.652  1.00 25.17  ? 101 CYS B CA  1 
ATOM   3981  C C   . CYS B 1 72  ? -4.105  -2.068  48.216  1.00 27.59  ? 101 CYS B C   1 
ATOM   3982  O O   . CYS B 1 72  ? -4.901  -2.937  47.930  1.00 28.54  ? 101 CYS B O   1 
ATOM   3983  C CB  . CYS B 1 72  ? -3.468  -0.586  46.346  1.00 25.90  ? 101 CYS B CB  1 
ATOM   3984  S SG  . CYS B 1 72  ? -3.816  0.912   45.390  1.00 26.34  ? 101 CYS B SG  1 
ATOM   3985  N N   . GLN B 1 73  ? -3.076  -2.298  49.022  1.00 33.70  ? 102 GLN B N   1 
ATOM   3986  C CA  . GLN B 1 73  ? -2.865  -3.612  49.611  1.00 38.30  ? 102 GLN B CA  1 
ATOM   3987  C C   . GLN B 1 73  ? -4.006  -3.958  50.565  1.00 38.08  ? 102 GLN B C   1 
ATOM   3988  O O   . GLN B 1 73  ? -4.382  -5.124  50.671  1.00 38.66  ? 102 GLN B O   1 
ATOM   3989  C CB  . GLN B 1 73  ? -1.494  -3.660  50.280  1.00 39.16  ? 102 GLN B CB  1 
ATOM   3990  C CG  . GLN B 1 73  ? -0.377  -3.811  49.261  1.00 42.54  ? 102 GLN B CG  1 
ATOM   3991  C CD  . GLN B 1 73  ? 0.988   -3.834  49.894  1.00 44.02  ? 102 GLN B CD  1 
ATOM   3992  O OE1 . GLN B 1 73  ? 1.499   -2.809  50.331  1.00 42.32  ? 102 GLN B OE1 1 
ATOM   3993  N NE2 . GLN B 1 73  ? 1.596   -5.008  49.921  1.00 49.39  ? 102 GLN B NE2 1 
ATOM   3994  N N   . LYS B 1 74  ? -4.557  -2.934  51.226  1.00 38.67  ? 103 LYS B N   1 
ATOM   3995  C CA  . LYS B 1 74  ? -5.643  -3.110  52.179  1.00 43.61  ? 103 LYS B CA  1 
ATOM   3996  C C   . LYS B 1 74  ? -6.993  -3.122  51.467  1.00 35.53  ? 103 LYS B C   1 
ATOM   3997  O O   . LYS B 1 74  ? -7.828  -3.984  51.735  1.00 32.24  ? 103 LYS B O   1 
ATOM   3998  C CB  . LYS B 1 74  ? -5.616  -1.997  53.236  1.00 49.57  ? 103 LYS B CB  1 
ATOM   3999  C CG  . LYS B 1 74  ? -4.510  -2.124  54.274  1.00 59.87  ? 103 LYS B CG  1 
ATOM   4000  C CD  . LYS B 1 74  ? -4.583  -3.397  55.111  1.00 69.16  ? 103 LYS B CD  1 
ATOM   4001  C CE  . LYS B 1 74  ? -5.793  -3.466  56.024  1.00 75.18  ? 103 LYS B CE  1 
ATOM   4002  N NZ  . LYS B 1 74  ? -5.788  -4.693  56.859  1.00 78.93  ? 103 LYS B NZ  1 
ATOM   4003  N N   . LEU B 1 75  ? -7.211  -2.140  50.585  1.00 31.60  ? 104 LEU B N   1 
ATOM   4004  C CA  . LEU B 1 75  ? -8.531  -1.901  50.015  1.00 28.63  ? 104 LEU B CA  1 
ATOM   4005  C C   . LEU B 1 75  ? -8.855  -2.812  48.829  1.00 26.76  ? 104 LEU B C   1 
ATOM   4006  O O   . LEU B 1 75  ? -10.023 -3.155  48.609  1.00 24.37  ? 104 LEU B O   1 
ATOM   4007  C CB  . LEU B 1 75  ? -8.620  -0.439  49.586  1.00 30.41  ? 104 LEU B CB  1 
ATOM   4008  C CG  . LEU B 1 75  ? -8.927  0.580   50.683  1.00 33.84  ? 104 LEU B CG  1 
ATOM   4009  C CD1 . LEU B 1 75  ? -9.298  1.910   50.054  1.00 36.74  ? 104 LEU B CD1 1 
ATOM   4010  C CD2 . LEU B 1 75  ? -10.053 0.107   51.599  1.00 35.58  ? 104 LEU B CD2 1 
ATOM   4011  N N   . LEU B 1 76  ? -7.864  -3.160  48.008  1.00 25.02  ? 105 LEU B N   1 
ATOM   4012  C CA  . LEU B 1 76  ? -8.166  -3.895  46.794  1.00 26.61  ? 105 LEU B CA  1 
ATOM   4013  C C   . LEU B 1 76  ? -8.508  -5.338  47.113  1.00 29.20  ? 105 LEU B C   1 
ATOM   4014  O O   . LEU B 1 76  ? -7.876  -5.958  47.969  1.00 29.79  ? 105 LEU B O   1 
ATOM   4015  C CB  . LEU B 1 76  ? -6.972  -3.870  45.848  1.00 23.51  ? 105 LEU B CB  1 
ATOM   4016  C CG  . LEU B 1 76  ? -6.691  -2.520  45.205  1.00 25.32  ? 105 LEU B CG  1 
ATOM   4017  C CD1 . LEU B 1 76  ? -5.521  -2.657  44.246  1.00 24.58  ? 105 LEU B CD1 1 
ATOM   4018  C CD2 . LEU B 1 76  ? -7.927  -1.990  44.482  1.00 26.81  ? 105 LEU B CD2 1 
ATOM   4019  N N   . PRO B 1 77  ? -9.532  -5.902  46.444  1.00 26.80  ? 106 PRO B N   1 
ATOM   4020  C CA  . PRO B 1 77  ? -9.867  -7.301  46.630  1.00 27.68  ? 106 PRO B CA  1 
ATOM   4021  C C   . PRO B 1 77  ? -8.693  -8.221  46.338  1.00 26.24  ? 106 PRO B C   1 
ATOM   4022  O O   . PRO B 1 77  ? -7.773  -7.875  45.616  1.00 24.48  ? 106 PRO B O   1 
ATOM   4023  C CB  . PRO B 1 77  ? -10.974 -7.566  45.608  1.00 29.57  ? 106 PRO B CB  1 
ATOM   4024  C CG  . PRO B 1 77  ? -11.610 -6.201  45.414  1.00 28.67  ? 106 PRO B CG  1 
ATOM   4025  C CD  . PRO B 1 77  ? -10.450 -5.224  45.520  1.00 27.48  ? 106 PRO B CD  1 
ATOM   4026  N N   . LYS B 1 78  ? -8.834  -9.436  46.855  1.00 28.15  ? 107 LYS B N   1 
ATOM   4027  C CA  . LYS B 1 78  ? -7.790  -10.433 46.918  1.00 28.40  ? 107 LYS B CA  1 
ATOM   4028  C C   . LYS B 1 78  ? -8.407  -11.736 46.434  1.00 27.75  ? 107 LYS B C   1 
ATOM   4029  O O   . LYS B 1 78  ? -9.631  -11.846 46.365  1.00 29.17  ? 107 LYS B O   1 
ATOM   4030  C CB  . LYS B 1 78  ? -7.300  -10.529 48.371  1.00 29.42  ? 107 LYS B CB  1 
ATOM   4031  C CG  . LYS B 1 78  ? -6.417  -9.378  48.818  1.00 32.40  ? 107 LYS B CG  1 
ATOM   4032  C CD  . LYS B 1 78  ? -6.534  -9.048  50.277  1.00 36.29  ? 107 LYS B CD  1 
ATOM   4033  C CE  . LYS B 1 78  ? -5.689  -7.843  50.629  1.00 34.73  ? 107 LYS B CE  1 
ATOM   4034  N NZ  . LYS B 1 78  ? -6.353  -6.564  50.310  1.00 36.36  ? 107 LYS B NZ  1 
ATOM   4035  N N   . ALA B 1 79  ? -7.569  -12.705 46.077  1.00 26.13  ? 108 ALA B N   1 
ATOM   4036  C CA  . ALA B 1 79  ? -8.046  -14.062 45.910  1.00 27.06  ? 108 ALA B CA  1 
ATOM   4037  C C   . ALA B 1 79  ? -8.493  -14.601 47.268  1.00 31.54  ? 108 ALA B C   1 
ATOM   4038  O O   . ALA B 1 79  ? -8.019  -14.175 48.328  1.00 28.09  ? 108 ALA B O   1 
ATOM   4039  C CB  . ALA B 1 79  ? -6.987  -14.934 45.300  1.00 26.79  ? 108 ALA B CB  1 
ATOM   4040  N N   . LYS B 1 80  ? -9.404  -15.575 47.224  1.00 38.78  ? 109 LYS B N   1 
ATOM   4041  C CA  . LYS B 1 80  ? -10.103 -16.024 48.423  1.00 42.39  ? 109 LYS B CA  1 
ATOM   4042  C C   . LYS B 1 80  ? -9.121  -16.505 49.493  1.00 44.82  ? 109 LYS B C   1 
ATOM   4043  O O   . LYS B 1 80  ? -9.195  -16.074 50.639  1.00 48.71  ? 109 LYS B O   1 
ATOM   4044  C CB  . LYS B 1 80  ? -11.124 -17.111 48.078  1.00 43.03  ? 109 LYS B CB  1 
ATOM   4045  C CG  . LYS B 1 80  ? -12.236 -16.669 47.130  1.00 46.10  ? 109 LYS B CG  1 
ATOM   4046  C CD  . LYS B 1 80  ? -12.017 -17.038 45.660  1.00 49.55  ? 109 LYS B CD  1 
ATOM   4047  C CE  . LYS B 1 80  ? -11.613 -18.485 45.433  1.00 48.70  ? 109 LYS B CE  1 
ATOM   4048  N NZ  . LYS B 1 80  ? -11.630 -18.861 43.998  1.00 47.62  ? 109 LYS B NZ  1 
ATOM   4049  N N   . GLY B 1 81  ? -8.221  -17.419 49.134  1.00 42.06  ? 110 GLY B N   1 
ATOM   4050  C CA  . GLY B 1 81  ? -7.235  -17.902 50.086  1.00 40.19  ? 110 GLY B CA  1 
ATOM   4051  C C   . GLY B 1 81  ? -5.909  -17.186 49.867  1.00 40.68  ? 110 GLY B C   1 
ATOM   4052  O O   . GLY B 1 81  ? -4.861  -17.816 49.729  1.00 43.96  ? 110 GLY B O   1 
ATOM   4053  N N   . GLY B 1 82  ? -5.992  -15.854 49.803  1.00 34.67  ? 111 GLY B N   1 
ATOM   4054  C CA  . GLY B 1 82  ? -4.875  -15.048 49.364  1.00 31.23  ? 111 GLY B CA  1 
ATOM   4055  C C   . GLY B 1 82  ? -4.802  -13.756 50.153  1.00 28.80  ? 111 GLY B C   1 
ATOM   4056  O O   . GLY B 1 82  ? -5.754  -13.368 50.833  1.00 31.93  ? 111 GLY B O   1 
ATOM   4057  N N   . GLU B 1 83  ? -3.636  -13.124 50.076  1.00 29.98  ? 112 GLU B N   1 
ATOM   4058  C CA  . GLU B 1 83  ? -3.321  -11.955 50.881  1.00 32.80  ? 112 GLU B CA  1 
ATOM   4059  C C   . GLU B 1 83  ? -2.976  -10.767 49.983  1.00 29.67  ? 112 GLU B C   1 
ATOM   4060  O O   . GLU B 1 83  ? -3.187  -9.624  50.368  1.00 33.49  ? 112 GLU B O   1 
ATOM   4061  C CB  . GLU B 1 83  ? -2.172  -12.320 51.827  1.00 37.01  ? 112 GLU B CB  1 
ATOM   4062  C CG  . GLU B 1 83  ? -2.588  -13.320 52.903  1.00 40.54  ? 112 GLU B CG  1 
ATOM   4063  C CD  . GLU B 1 83  ? -3.432  -12.724 54.020  1.00 48.40  ? 112 GLU B CD  1 
ATOM   4064  O OE1 . GLU B 1 83  ? -3.605  -11.487 54.027  1.00 56.67  ? 112 GLU B OE1 1 
ATOM   4065  O OE2 . GLU B 1 83  ? -3.920  -13.494 54.888  1.00 53.18  ? 112 GLU B OE2 1 
ATOM   4066  N N   . GLU B 1 84  ? -2.428  -11.035 48.795  1.00 27.80  ? 113 GLU B N   1 
ATOM   4067  C CA  . GLU B 1 84  ? -1.937  -9.973  47.918  1.00 26.01  ? 113 GLU B CA  1 
ATOM   4068  C C   . GLU B 1 84  ? -3.070  -9.436  47.030  1.00 25.07  ? 113 GLU B C   1 
ATOM   4069  O O   . GLU B 1 84  ? -4.035  -10.135 46.723  1.00 25.68  ? 113 GLU B O   1 
ATOM   4070  C CB  . GLU B 1 84  ? -0.756  -10.498 47.092  1.00 31.35  ? 113 GLU B CB  1 
ATOM   4071  C CG  . GLU B 1 84  ? 0.499   -10.818 47.909  1.00 32.20  ? 113 GLU B CG  1 
ATOM   4072  C CD  . GLU B 1 84  ? 0.947   -9.709  48.841  1.00 34.17  ? 113 GLU B CD  1 
ATOM   4073  O OE1 . GLU B 1 84  ? 0.885   -8.533  48.435  1.00 42.43  ? 113 GLU B OE1 1 
ATOM   4074  O OE2 . GLU B 1 84  ? 1.374   -10.020 49.961  1.00 36.48  ? 113 GLU B OE2 1 
ATOM   4075  N N   . PRO B 1 85  ? -2.992  -8.168  46.575  1.00 24.09  ? 114 PRO B N   1 
ATOM   4076  C CA  . PRO B 1 85  ? -4.045  -7.566  45.754  1.00 21.56  ? 114 PRO B CA  1 
ATOM   4077  C C   . PRO B 1 85  ? -4.084  -8.152  44.337  1.00 22.26  ? 114 PRO B C   1 
ATOM   4078  O O   . PRO B 1 85  ? -3.045  -8.379  43.699  1.00 22.55  ? 114 PRO B O   1 
ATOM   4079  C CB  . PRO B 1 85  ? -3.668  -6.067  45.763  1.00 21.05  ? 114 PRO B CB  1 
ATOM   4080  C CG  . PRO B 1 85  ? -2.161  -6.084  45.862  1.00 22.85  ? 114 PRO B CG  1 
ATOM   4081  C CD  . PRO B 1 85  ? -1.843  -7.275  46.748  1.00 25.14  ? 114 PRO B CD  1 
ATOM   4082  N N   . LEU B 1 86  ? -5.299  -8.418  43.844  1.00 20.37  ? 115 LEU B N   1 
ATOM   4083  C CA  . LEU B 1 86  ? -5.475  -8.920  42.486  1.00 20.90  ? 115 LEU B CA  1 
ATOM   4084  C C   . LEU B 1 86  ? -5.217  -7.792  41.491  1.00 21.74  ? 115 LEU B C   1 
ATOM   4085  O O   . LEU B 1 86  ? -5.767  -6.690  41.676  1.00 18.00  ? 115 LEU B O   1 
ATOM   4086  C CB  . LEU B 1 86  ? -6.898  -9.477  42.334  1.00 21.85  ? 115 LEU B CB  1 
ATOM   4087  C CG  . LEU B 1 86  ? -7.199  -10.802 43.057  1.00 22.50  ? 115 LEU B CG  1 
ATOM   4088  C CD1 . LEU B 1 86  ? -8.615  -11.301 42.757  1.00 25.48  ? 115 LEU B CD1 1 
ATOM   4089  C CD2 . LEU B 1 86  ? -6.199  -11.872 42.691  1.00 22.58  ? 115 LEU B CD2 1 
ATOM   4090  N N   . PRO B 1 87  ? -4.357  -7.990  40.461  1.00 19.42  ? 116 PRO B N   1 
ATOM   4091  C CA  . PRO B 1 87  ? -4.116  -6.948  39.457  1.00 20.44  ? 116 PRO B CA  1 
ATOM   4092  C C   . PRO B 1 87  ? -5.387  -6.541  38.698  1.00 19.86  ? 116 PRO B C   1 
ATOM   4093  O O   . PRO B 1 87  ? -5.560  -5.379  38.385  1.00 22.47  ? 116 PRO B O   1 
ATOM   4094  C CB  . PRO B 1 87  ? -3.044  -7.504  38.517  1.00 19.85  ? 116 PRO B CB  1 
ATOM   4095  C CG  . PRO B 1 87  ? -3.060  -9.002  38.781  1.00 19.76  ? 116 PRO B CG  1 
ATOM   4096  C CD  . PRO B 1 87  ? -3.525  -9.186  40.223  1.00 19.79  ? 116 PRO B CD  1 
ATOM   4097  N N   . GLU B 1 88  ? -6.310  -7.475  38.457  1.00 19.87  ? 117 GLU B N   1 
ATOM   4098  C CA  . GLU B 1 88  ? -7.645  -7.115  37.996  1.00 21.74  ? 117 GLU B CA  1 
ATOM   4099  C C   . GLU B 1 88  ? -8.190  -5.901  38.731  1.00 21.29  ? 117 GLU B C   1 
ATOM   4100  O O   . GLU B 1 88  ? -8.656  -4.963  38.090  1.00 21.92  ? 117 GLU B O   1 
ATOM   4101  C CB  . GLU B 1 88  ? -8.681  -8.209  38.241  1.00 22.52  ? 117 GLU B CB  1 
ATOM   4102  C CG  . GLU B 1 88  ? -8.542  -9.429  37.339  1.00 25.75  ? 117 GLU B CG  1 
ATOM   4103  C CD  . GLU B 1 88  ? -7.610  -10.529 37.803  1.00 26.77  ? 117 GLU B CD  1 
ATOM   4104  O OE1 . GLU B 1 88  ? -6.624  -10.186 38.470  1.00 26.11  ? 117 GLU B OE1 1 
ATOM   4105  O OE2 . GLU B 1 88  ? -7.856  -11.719 37.409  1.00 24.19  ? 117 GLU B OE2 1 
ATOM   4106  N N   . GLY B 1 89  ? -8.202  -5.911  40.077  1.00 19.24  ? 118 GLY B N   1 
ATOM   4107  C CA  . GLY B 1 89  ? -8.794  -4.792  40.781  1.00 20.18  ? 118 GLY B CA  1 
ATOM   4108  C C   . GLY B 1 89  ? -8.052  -3.476  40.593  1.00 20.74  ? 118 GLY B C   1 
ATOM   4109  O O   . GLY B 1 89  ? -8.669  -2.410  40.621  1.00 22.35  ? 118 GLY B O   1 
ATOM   4110  N N   . LEU B 1 90  ? -6.728  -3.529  40.435  1.00 18.88  ? 119 LEU B N   1 
ATOM   4111  C CA  . LEU B 1 90  ? -5.970  -2.303  40.223  1.00 22.57  ? 119 LEU B CA  1 
ATOM   4112  C C   . LEU B 1 90  ? -6.350  -1.676  38.884  1.00 21.59  ? 119 LEU B C   1 
ATOM   4113  O O   . LEU B 1 90  ? -6.551  -0.455  38.735  1.00 20.71  ? 119 LEU B O   1 
ATOM   4114  C CB  . LEU B 1 90  ? -4.477  -2.611  40.251  1.00 27.14  ? 119 LEU B CB  1 
ATOM   4115  C CG  . LEU B 1 90  ? -3.612  -1.422  39.848  1.00 33.00  ? 119 LEU B CG  1 
ATOM   4116  C CD1 . LEU B 1 90  ? -2.608  -1.056  40.937  1.00 38.29  ? 119 LEU B CD1 1 
ATOM   4117  C CD2 . LEU B 1 90  ? -2.956  -1.715  38.510  1.00 31.29  ? 119 LEU B CD2 1 
ATOM   4118  N N   . PHE B 1 91  ? -6.452  -2.533  37.885  1.00 20.22  ? 120 PHE B N   1 
ATOM   4119  C CA  . PHE B 1 91  ? -6.913  -2.080  36.580  1.00 20.02  ? 120 PHE B CA  1 
ATOM   4120  C C   . PHE B 1 91  ? -8.259  -1.384  36.704  1.00 21.09  ? 120 PHE B C   1 
ATOM   4121  O O   . PHE B 1 91  ? -8.416  -0.236  36.287  1.00 19.91  ? 120 PHE B O   1 
ATOM   4122  C CB  . PHE B 1 91  ? -7.054  -3.248  35.618  1.00 20.61  ? 120 PHE B CB  1 
ATOM   4123  C CG  . PHE B 1 91  ? -7.380  -2.823  34.213  1.00 16.83  ? 120 PHE B CG  1 
ATOM   4124  C CD1 . PHE B 1 91  ? -6.444  -2.156  33.434  1.00 18.54  ? 120 PHE B CD1 1 
ATOM   4125  C CD2 . PHE B 1 91  ? -8.635  -3.029  33.681  1.00 19.02  ? 120 PHE B CD2 1 
ATOM   4126  C CE1 . PHE B 1 91  ? -6.735  -1.786  32.132  1.00 18.75  ? 120 PHE B CE1 1 
ATOM   4127  C CE2 . PHE B 1 91  ? -8.919  -2.665  32.369  1.00 19.69  ? 120 PHE B CE2 1 
ATOM   4128  C CZ  . PHE B 1 91  ? -7.980  -2.005  31.612  1.00 19.44  ? 120 PHE B CZ  1 
ATOM   4129  N N   . TRP B 1 92  ? -9.200  -2.037  37.386  1.00 21.50  ? 121 TRP B N   1 
ATOM   4130  C CA  . TRP B 1 92  ? -10.488 -1.412  37.635  1.00 19.58  ? 121 TRP B CA  1 
ATOM   4131  C C   . TRP B 1 92  ? -10.304 -0.004  38.192  1.00 19.34  ? 121 TRP B C   1 
ATOM   4132  O O   . TRP B 1 92  ? -10.984 0.940   37.754  1.00 22.66  ? 121 TRP B O   1 
ATOM   4133  C CB  . TRP B 1 92  ? -11.362 -2.245  38.563  1.00 20.23  ? 121 TRP B CB  1 
ATOM   4134  C CG  . TRP B 1 92  ? -12.776 -1.746  38.616  1.00 19.16  ? 121 TRP B CG  1 
ATOM   4135  C CD1 . TRP B 1 92  ? -13.227 -0.635  39.272  1.00 20.03  ? 121 TRP B CD1 1 
ATOM   4136  C CD2 . TRP B 1 92  ? -13.932 -2.324  37.984  1.00 21.92  ? 121 TRP B CD2 1 
ATOM   4137  N NE1 . TRP B 1 92  ? -14.578 -0.502  39.116  1.00 18.14  ? 121 TRP B NE1 1 
ATOM   4138  C CE2 . TRP B 1 92  ? -15.043 -1.520  38.330  1.00 19.83  ? 121 TRP B CE2 1 
ATOM   4139  C CE3 . TRP B 1 92  ? -14.146 -3.418  37.135  1.00 22.39  ? 121 TRP B CE3 1 
ATOM   4140  C CZ2 . TRP B 1 92  ? -16.327 -1.789  37.849  1.00 21.17  ? 121 TRP B CZ2 1 
ATOM   4141  C CZ3 . TRP B 1 92  ? -15.417 -3.688  36.667  1.00 23.90  ? 121 TRP B CZ3 1 
ATOM   4142  C CH2 . TRP B 1 92  ? -16.500 -2.891  37.042  1.00 22.45  ? 121 TRP B CH2 1 
ATOM   4143  N N   . LEU B 1 93  ? -9.457  0.100   39.213  1.00 20.33  ? 122 LEU B N   1 
ATOM   4144  C CA  . LEU B 1 93  ? -9.261  1.362   39.911  1.00 19.92  ? 122 LEU B CA  1 
ATOM   4145  C C   . LEU B 1 93  ? -8.692  2.394   38.943  1.00 21.64  ? 122 LEU B C   1 
ATOM   4146  O O   . LEU B 1 93  ? -9.173  3.545   38.930  1.00 20.65  ? 122 LEU B O   1 
ATOM   4147  C CB  . LEU B 1 93  ? -8.346  1.135   41.119  1.00 20.87  ? 122 LEU B CB  1 
ATOM   4148  C CG  . LEU B 1 93  ? -7.696  2.377   41.718  1.00 21.37  ? 122 LEU B CG  1 
ATOM   4149  C CD1 . LEU B 1 93  ? -8.732  3.213   42.462  1.00 21.66  ? 122 LEU B CD1 1 
ATOM   4150  C CD2 . LEU B 1 93  ? -6.551  1.983   42.626  1.00 20.80  ? 122 LEU B CD2 1 
ATOM   4151  N N   . LEU B 1 94  ? -7.632  2.003   38.199  1.00 19.04  ? 123 LEU B N   1 
ATOM   4152  C CA  . LEU B 1 94  ? -6.962  2.893   37.251  1.00 20.72  ? 123 LEU B CA  1 
ATOM   4153  C C   . LEU B 1 94  ? -7.970  3.454   36.242  1.00 22.61  ? 123 LEU B C   1 
ATOM   4154  O O   . LEU B 1 94  ? -7.959  4.647   35.914  1.00 23.10  ? 123 LEU B O   1 
ATOM   4155  C CB  . LEU B 1 94  ? -5.841  2.124   36.537  1.00 21.94  ? 123 LEU B CB  1 
ATOM   4156  C CG  . LEU B 1 94  ? -4.647  1.707   37.399  1.00 21.51  ? 123 LEU B CG  1 
ATOM   4157  C CD1 . LEU B 1 94  ? -3.471  1.283   36.529  1.00 20.34  ? 123 LEU B CD1 1 
ATOM   4158  C CD2 . LEU B 1 94  ? -4.233  2.815   38.365  1.00 21.14  ? 123 LEU B CD2 1 
ATOM   4159  N N   . VAL B 1 95  ? -8.856  2.587   35.778  1.00 22.21  ? 124 VAL B N   1 
ATOM   4160  C CA  . VAL B 1 95  ? -9.793  2.889   34.709  1.00 25.19  ? 124 VAL B CA  1 
ATOM   4161  C C   . VAL B 1 95  ? -10.934 3.753   35.226  1.00 24.26  ? 124 VAL B C   1 
ATOM   4162  O O   . VAL B 1 95  ? -11.329 4.682   34.543  1.00 22.63  ? 124 VAL B O   1 
ATOM   4163  C CB  . VAL B 1 95  ? -10.307 1.574   34.103  1.00 25.51  ? 124 VAL B CB  1 
ATOM   4164  C CG1 . VAL B 1 95  ? -11.564 1.736   33.262  1.00 25.73  ? 124 VAL B CG1 1 
ATOM   4165  C CG2 . VAL B 1 95  ? -9.194  0.903   33.317  1.00 24.12  ? 124 VAL B CG2 1 
ATOM   4166  N N   . THR B 1 96  ? -11.472 3.421   36.404  1.00 24.57  ? 125 THR B N   1 
ATOM   4167  C CA  . THR B 1 96  ? -12.691 4.065   36.876  1.00 22.52  ? 125 THR B CA  1 
ATOM   4168  C C   . THR B 1 96  ? -12.414 5.126   37.927  1.00 23.85  ? 125 THR B C   1 
ATOM   4169  O O   . THR B 1 96  ? -13.252 6.007   38.139  1.00 24.43  ? 125 THR B O   1 
ATOM   4170  C CB  . THR B 1 96  ? -13.683 3.102   37.532  1.00 24.66  ? 125 THR B CB  1 
ATOM   4171  O OG1 . THR B 1 96  ? -13.067 2.587   38.716  1.00 20.71  ? 125 THR B OG1 1 
ATOM   4172  C CG2 . THR B 1 96  ? -14.170 2.012   36.613  1.00 22.92  ? 125 THR B CG2 1 
ATOM   4173  N N   . GLY B 1 97  ? -11.258 5.060   38.595  1.00 23.35  ? 126 GLY B N   1 
ATOM   4174  C CA  . GLY B 1 97  ? -10.980 5.927   39.732  1.00 25.80  ? 126 GLY B CA  1 
ATOM   4175  C C   . GLY B 1 97  ? -11.622 5.433   41.033  1.00 25.75  ? 126 GLY B C   1 
ATOM   4176  O O   . GLY B 1 97  ? -11.467 6.092   42.063  1.00 22.92  ? 126 GLY B O   1 
ATOM   4177  N N   . HIS B 1 98  ? -12.336 4.288   40.959  1.00 25.19  ? 127 HIS B N   1 
ATOM   4178  C CA  . HIS B 1 98  ? -13.098 3.712   42.058  1.00 25.27  ? 127 HIS B CA  1 
ATOM   4179  C C   . HIS B 1 98  ? -12.490 2.371   42.442  1.00 25.30  ? 127 HIS B C   1 
ATOM   4180  O O   . HIS B 1 98  ? -12.149 1.576   41.562  1.00 23.04  ? 127 HIS B O   1 
ATOM   4181  C CB  . HIS B 1 98  ? -14.552 3.417   41.669  1.00 26.81  ? 127 HIS B CB  1 
ATOM   4182  C CG  . HIS B 1 98  ? -15.344 4.631   41.324  1.00 29.69  ? 127 HIS B CG  1 
ATOM   4183  N ND1 . HIS B 1 98  ? -14.830 5.901   41.490  1.00 33.08  ? 127 HIS B ND1 1 
ATOM   4184  C CD2 . HIS B 1 98  ? -16.578 4.785   40.844  1.00 32.20  ? 127 HIS B CD2 1 
ATOM   4185  C CE1 . HIS B 1 98  ? -15.724 6.792   41.088  1.00 33.10  ? 127 HIS B CE1 1 
ATOM   4186  N NE2 . HIS B 1 98  ? -16.801 6.137   40.697  1.00 34.28  ? 127 HIS B NE2 1 
ATOM   4187  N N   . ILE B 1 99  ? -12.385 2.121   43.757  1.00 25.66  ? 128 ILE B N   1 
ATOM   4188  C CA  . ILE B 1 99  ? -11.965 0.814   44.234  1.00 23.56  ? 128 ILE B CA  1 
ATOM   4189  C C   . ILE B 1 99  ? -13.060 -0.158  43.805  1.00 23.33  ? 128 ILE B C   1 
ATOM   4190  O O   . ILE B 1 99  ? -14.218 0.087   44.108  1.00 24.23  ? 128 ILE B O   1 
ATOM   4191  C CB  . ILE B 1 99  ? -11.797 0.813   45.774  1.00 22.74  ? 128 ILE B CB  1 
ATOM   4192  C CG1 . ILE B 1 99  ? -10.674 1.723   46.275  1.00 22.29  ? 128 ILE B CG1 1 
ATOM   4193  C CG2 . ILE B 1 99  ? -11.643 -0.608  46.275  1.00 22.64  ? 128 ILE B CG2 1 
ATOM   4194  C CD1 . ILE B 1 99  ? -9.292  1.299   45.816  1.00 21.64  ? 128 ILE B CD1 1 
ATOM   4195  N N   . PRO B 1 100 ? -12.751 -1.332  43.213  1.00 22.91  ? 129 PRO B N   1 
ATOM   4196  C CA  . PRO B 1 100 ? -13.782 -2.285  42.825  1.00 23.52  ? 129 PRO B CA  1 
ATOM   4197  C C   . PRO B 1 100 ? -14.307 -3.128  43.975  1.00 27.01  ? 129 PRO B C   1 
ATOM   4198  O O   . PRO B 1 100 ? -13.665 -3.231  45.021  1.00 24.13  ? 129 PRO B O   1 
ATOM   4199  C CB  . PRO B 1 100 ? -13.042 -3.222  41.868  1.00 26.47  ? 129 PRO B CB  1 
ATOM   4200  C CG  . PRO B 1 100 ? -11.652 -3.257  42.459  1.00 25.60  ? 129 PRO B CG  1 
ATOM   4201  C CD  . PRO B 1 100 ? -11.397 -1.819  42.895  1.00 24.65  ? 129 PRO B CD  1 
ATOM   4202  N N   . THR B 1 101 ? -15.477 -3.727  43.747  1.00 27.07  ? 130 THR B N   1 
ATOM   4203  C CA  . THR B 1 101 ? -16.036 -4.700  44.669  1.00 28.22  ? 130 THR B CA  1 
ATOM   4204  C C   . THR B 1 101 ? -15.402 -6.042  44.338  1.00 30.47  ? 130 THR B C   1 
ATOM   4205  O O   . THR B 1 101 ? -14.764 -6.195  43.296  1.00 24.54  ? 130 THR B O   1 
ATOM   4206  C CB  . THR B 1 101 ? -17.570 -4.791  44.584  1.00 30.76  ? 130 THR B CB  1 
ATOM   4207  O OG1 . THR B 1 101 ? -17.952 -5.310  43.307  1.00 29.11  ? 130 THR B OG1 1 
ATOM   4208  C CG2 . THR B 1 101 ? -18.248 -3.463  44.848  1.00 30.37  ? 130 THR B CG2 1 
ATOM   4209  N N   . GLU B 1 102 ? -15.598 -7.005  45.242  1.00 30.02  ? 131 GLU B N   1 
ATOM   4210  C CA  . GLU B 1 102 ? -15.222 -8.388  44.979  1.00 32.26  ? 131 GLU B CA  1 
ATOM   4211  C C   . GLU B 1 102 ? -15.898 -8.887  43.697  1.00 27.46  ? 131 GLU B C   1 
ATOM   4212  O O   . GLU B 1 102 ? -15.315 -9.669  42.951  1.00 24.31  ? 131 GLU B O   1 
ATOM   4213  C CB  . GLU B 1 102 ? -15.586 -9.269  46.184  1.00 34.98  ? 131 GLU B CB  1 
ATOM   4214  C CG  . GLU B 1 102 ? -14.956 -8.807  47.511  1.00 40.40  ? 131 GLU B CG  1 
ATOM   4215  C CD  . GLU B 1 102 ? -13.943 -9.702  48.230  1.00 47.01  ? 131 GLU B CD  1 
ATOM   4216  O OE1 . GLU B 1 102 ? -13.985 -10.940 48.043  1.00 52.85  ? 131 GLU B OE1 1 
ATOM   4217  O OE2 . GLU B 1 102 ? -13.109 -9.158  49.014  1.00 44.04  ? 131 GLU B OE2 1 
ATOM   4218  N N   . GLU B 1 103 ? -17.147 -8.461  43.470  1.00 23.24  ? 132 GLU B N   1 
ATOM   4219  C CA  . GLU B 1 103 ? -17.951 -8.903  42.345  1.00 26.31  ? 132 GLU B CA  1 
ATOM   4220  C C   . GLU B 1 103 ? -17.408 -8.350  41.031  1.00 21.93  ? 132 GLU B C   1 
ATOM   4221  O O   . GLU B 1 103 ? -17.422 -9.015  39.997  1.00 25.56  ? 132 GLU B O   1 
ATOM   4222  C CB  . GLU B 1 103 ? -19.391 -8.435  42.553  1.00 28.45  ? 132 GLU B CB  1 
ATOM   4223  C CG  . GLU B 1 103 ? -20.098 -9.201  43.647  1.00 30.65  ? 132 GLU B CG  1 
ATOM   4224  C CD  . GLU B 1 103 ? -19.596 -8.993  45.064  1.00 31.56  ? 132 GLU B CD  1 
ATOM   4225  O OE1 . GLU B 1 103 ? -19.077 -7.903  45.380  1.00 31.69  ? 132 GLU B OE1 1 
ATOM   4226  O OE2 . GLU B 1 103 ? -19.708 -9.944  45.835  1.00 35.25  ? 132 GLU B OE2 1 
ATOM   4227  N N   . GLN B 1 104 ? -17.014 -7.080  41.054  1.00 20.99  ? 133 GLN B N   1 
ATOM   4228  C CA  . GLN B 1 104 ? -16.506 -6.428  39.859  1.00 21.65  ? 133 GLN B CA  1 
ATOM   4229  C C   . GLN B 1 104 ? -15.216 -7.124  39.411  1.00 22.91  ? 133 GLN B C   1 
ATOM   4230  O O   . GLN B 1 104 ? -15.050 -7.396  38.224  1.00 26.85  ? 133 GLN B O   1 
ATOM   4231  C CB  . GLN B 1 104 ? -16.357 -4.940  40.169  1.00 21.61  ? 133 GLN B CB  1 
ATOM   4232  C CG  . GLN B 1 104 ? -17.716 -4.274  40.211  1.00 23.09  ? 133 GLN B CG  1 
ATOM   4233  C CD  . GLN B 1 104 ? -17.713 -2.841  40.680  1.00 25.64  ? 133 GLN B CD  1 
ATOM   4234  O OE1 . GLN B 1 104 ? -16.887 -2.399  41.481  1.00 25.25  ? 133 GLN B OE1 1 
ATOM   4235  N NE2 . GLN B 1 104 ? -18.715 -2.113  40.218  1.00 25.93  ? 133 GLN B NE2 1 
ATOM   4236  N N   . VAL B 1 105 ? -14.344 -7.437  40.376  1.00 23.59  ? 134 VAL B N   1 
ATOM   4237  C CA  . VAL B 1 105 ? -13.071 -8.088  40.095  1.00 24.16  ? 134 VAL B CA  1 
ATOM   4238  C C   . VAL B 1 105 ? -13.346 -9.475  39.541  1.00 23.86  ? 134 VAL B C   1 
ATOM   4239  O O   . VAL B 1 105 ? -12.711 -9.883  38.579  1.00 26.25  ? 134 VAL B O   1 
ATOM   4240  C CB  . VAL B 1 105 ? -12.145 -8.136  41.328  1.00 22.95  ? 134 VAL B CB  1 
ATOM   4241  C CG1 . VAL B 1 105 ? -11.020 -9.149  41.192  1.00 23.04  ? 134 VAL B CG1 1 
ATOM   4242  C CG2 . VAL B 1 105 ? -11.546 -6.773  41.629  1.00 21.48  ? 134 VAL B CG2 1 
ATOM   4243  N N   . SER B 1 106 ? -14.291 -10.192 40.153  1.00 23.69  ? 135 SER B N   1 
ATOM   4244  C CA  A SER B 1 106 ? -14.648 -11.519 39.688  0.50 22.33  ? 135 SER B CA  1 
ATOM   4245  C CA  B SER B 1 106 ? -14.637 -11.523 39.681  0.50 23.25  ? 135 SER B CA  1 
ATOM   4246  C C   . SER B 1 106 ? -15.043 -11.457 38.207  1.00 24.39  ? 135 SER B C   1 
ATOM   4247  O O   . SER B 1 106 ? -14.591 -12.261 37.393  1.00 23.70  ? 135 SER B O   1 
ATOM   4248  C CB  A SER B 1 106 ? -15.736 -12.080 40.550  0.50 21.53  ? 135 SER B CB  1 
ATOM   4249  C CB  B SER B 1 106 ? -15.710 -12.147 40.521  0.50 23.51  ? 135 SER B CB  1 
ATOM   4250  O OG  A SER B 1 106 ? -15.841 -13.480 40.396  0.50 21.75  ? 135 SER B OG  1 
ATOM   4251  O OG  B SER B 1 106 ? -15.244 -12.389 41.838  0.50 26.35  ? 135 SER B OG  1 
ATOM   4252  N N   . TRP B 1 107 ? -15.888 -10.471 37.856  1.00 21.80  ? 136 TRP B N   1 
ATOM   4253  C CA  . TRP B 1 107 ? -16.296 -10.253 36.483  1.00 25.73  ? 136 TRP B CA  1 
ATOM   4254  C C   . TRP B 1 107 ? -15.085 -10.041 35.580  1.00 20.64  ? 136 TRP B C   1 
ATOM   4255  O O   . TRP B 1 107 ? -15.064 -10.545 34.481  1.00 21.71  ? 136 TRP B O   1 
ATOM   4256  C CB  . TRP B 1 107 ? -17.247 -9.041  36.385  1.00 25.53  ? 136 TRP B CB  1 
ATOM   4257  C CG  . TRP B 1 107 ? -17.604 -8.728  34.967  1.00 27.82  ? 136 TRP B CG  1 
ATOM   4258  C CD1 . TRP B 1 107 ? -18.541 -9.365  34.202  1.00 29.48  ? 136 TRP B CD1 1 
ATOM   4259  C CD2 . TRP B 1 107 ? -16.952 -7.786  34.096  1.00 27.65  ? 136 TRP B CD2 1 
ATOM   4260  N NE1 . TRP B 1 107 ? -18.558 -8.839  32.941  1.00 29.53  ? 136 TRP B NE1 1 
ATOM   4261  C CE2 . TRP B 1 107 ? -17.605 -7.868  32.847  1.00 31.31  ? 136 TRP B CE2 1 
ATOM   4262  C CE3 . TRP B 1 107 ? -15.932 -6.840  34.258  1.00 29.95  ? 136 TRP B CE3 1 
ATOM   4263  C CZ2 . TRP B 1 107 ? -17.270 -7.048  31.769  1.00 28.17  ? 136 TRP B CZ2 1 
ATOM   4264  C CZ3 . TRP B 1 107 ? -15.576 -6.055  33.188  1.00 28.81  ? 136 TRP B CZ3 1 
ATOM   4265  C CH2 . TRP B 1 107 ? -16.232 -6.164  31.961  1.00 29.39  ? 136 TRP B CH2 1 
ATOM   4266  N N   . LEU B 1 108 ? -14.134 -9.201  36.012  1.00 20.83  ? 137 LEU B N   1 
ATOM   4267  C CA  . LEU B 1 108 ? -13.002 -8.853  35.187  1.00 22.18  ? 137 LEU B CA  1 
ATOM   4268  C C   . LEU B 1 108 ? -12.141 -10.099 34.942  1.00 22.80  ? 137 LEU B C   1 
ATOM   4269  O O   . LEU B 1 108 ? -11.716 -10.351 33.809  1.00 24.16  ? 137 LEU B O   1 
ATOM   4270  C CB  . LEU B 1 108 ? -12.297 -7.688  35.891  1.00 23.79  ? 137 LEU B CB  1 
ATOM   4271  C CG  . LEU B 1 108 ? -11.342 -6.823  35.084  1.00 25.44  ? 137 LEU B CG  1 
ATOM   4272  C CD1 . LEU B 1 108 ? -11.869 -6.506  33.697  1.00 23.67  ? 137 LEU B CD1 1 
ATOM   4273  C CD2 . LEU B 1 108 ? -11.074 -5.519  35.832  1.00 25.26  ? 137 LEU B CD2 1 
ATOM   4274  N N   . SER B 1 109 ? -11.934 -10.911 35.984  1.00 22.40  ? 138 SER B N   1 
ATOM   4275  C CA  . SER B 1 109 ? -11.177 -12.156 35.848  1.00 22.73  ? 138 SER B CA  1 
ATOM   4276  C C   . SER B 1 109 ? -11.832 -13.023 34.776  1.00 23.04  ? 138 SER B C   1 
ATOM   4277  O O   . SER B 1 109 ? -11.181 -13.578 33.893  1.00 21.06  ? 138 SER B O   1 
ATOM   4278  C CB  . SER B 1 109 ? -11.105 -12.919 37.152  1.00 23.31  ? 138 SER B CB  1 
ATOM   4279  O OG  . SER B 1 109 ? -10.536 -12.144 38.186  1.00 22.00  ? 138 SER B OG  1 
ATOM   4280  N N   . LYS B 1 110 ? -13.167 -13.138 34.860  1.00 21.55  ? 139 LYS B N   1 
ATOM   4281  C CA  . LYS B 1 110 ? -13.904 -13.934 33.902  1.00 23.60  ? 139 LYS B CA  1 
ATOM   4282  C C   . LYS B 1 110 ? -13.792 -13.336 32.503  1.00 21.78  ? 139 LYS B C   1 
ATOM   4283  O O   . LYS B 1 110 ? -13.696 -14.046 31.532  1.00 20.48  ? 139 LYS B O   1 
ATOM   4284  C CB  . LYS B 1 110 ? -15.345 -14.089 34.390  1.00 30.53  ? 139 LYS B CB  1 
ATOM   4285  C CG  . LYS B 1 110 ? -15.470 -14.796 35.729  1.00 34.88  ? 139 LYS B CG  1 
ATOM   4286  C CD  . LYS B 1 110 ? -16.769 -14.489 36.413  1.00 38.44  ? 139 LYS B CD  1 
ATOM   4287  C CE  . LYS B 1 110 ? -16.855 -15.062 37.805  1.00 38.45  ? 139 LYS B CE  1 
ATOM   4288  N NZ  . LYS B 1 110 ? -17.078 -16.522 37.771  1.00 43.38  ? 139 LYS B NZ  1 
ATOM   4289  N N   . GLU B 1 111 ? -13.807 -12.007 32.394  1.00 21.74  ? 140 GLU B N   1 
ATOM   4290  C CA  . GLU B 1 111 ? -13.736 -11.373 31.093  1.00 22.74  ? 140 GLU B CA  1 
ATOM   4291  C C   . GLU B 1 111 ? -12.402 -11.699 30.442  1.00 22.46  ? 140 GLU B C   1 
ATOM   4292  O O   . GLU B 1 111 ? -12.402 -12.004 29.256  1.00 20.46  ? 140 GLU B O   1 
ATOM   4293  C CB  . GLU B 1 111 ? -13.823 -9.845  31.156  1.00 26.15  ? 140 GLU B CB  1 
ATOM   4294  C CG  . GLU B 1 111 ? -15.143 -9.243  30.695  1.00 30.39  ? 140 GLU B CG  1 
ATOM   4295  C CD  . GLU B 1 111 ? -15.807 -9.829  29.465  1.00 26.03  ? 140 GLU B CD  1 
ATOM   4296  O OE1 . GLU B 1 111 ? -15.344 -9.580  28.312  1.00 22.73  ? 140 GLU B OE1 1 
ATOM   4297  O OE2 . GLU B 1 111 ? -16.767 -10.563 29.666  1.00 23.53  ? 140 GLU B OE2 1 
ATOM   4298  N N   . TRP B 1 112 ? -11.287 -11.625 31.205  1.00 21.43  ? 141 TRP B N   1 
ATOM   4299  C CA  . TRP B 1 112 ? -9.971  -11.839 30.618  1.00 22.51  ? 141 TRP B CA  1 
ATOM   4300  C C   . TRP B 1 112 ? -9.701  -13.313 30.299  1.00 24.59  ? 141 TRP B C   1 
ATOM   4301  O O   . TRP B 1 112 ? -9.000  -13.605 29.335  1.00 28.47  ? 141 TRP B O   1 
ATOM   4302  C CB  . TRP B 1 112 ? -8.842  -11.267 31.472  1.00 25.28  ? 141 TRP B CB  1 
ATOM   4303  C CG  . TRP B 1 112 ? -8.801  -9.775  31.510  1.00 25.76  ? 141 TRP B CG  1 
ATOM   4304  C CD1 . TRP B 1 112 ? -9.399  -8.894  30.663  1.00 27.18  ? 141 TRP B CD1 1 
ATOM   4305  C CD2 . TRP B 1 112 ? -8.127  -8.989  32.498  1.00 25.94  ? 141 TRP B CD2 1 
ATOM   4306  N NE1 . TRP B 1 112 ? -9.155  -7.612  31.061  1.00 24.97  ? 141 TRP B NE1 1 
ATOM   4307  C CE2 . TRP B 1 112 ? -8.382  -7.636  32.186  1.00 24.39  ? 141 TRP B CE2 1 
ATOM   4308  C CE3 . TRP B 1 112 ? -7.335  -9.291  33.605  1.00 22.73  ? 141 TRP B CE3 1 
ATOM   4309  C CZ2 . TRP B 1 112 ? -7.865  -6.594  32.949  1.00 23.51  ? 141 TRP B CZ2 1 
ATOM   4310  C CZ3 . TRP B 1 112 ? -6.846  -8.265  34.371  1.00 23.12  ? 141 TRP B CZ3 1 
ATOM   4311  C CH2 . TRP B 1 112 ? -7.115  -6.930  34.052  1.00 21.50  ? 141 TRP B CH2 1 
ATOM   4312  N N   . ALA B 1 113 ? -10.282 -14.232 31.075  1.00 25.47  ? 142 ALA B N   1 
ATOM   4313  C CA  . ALA B 1 113 ? -10.315 -15.646 30.708  1.00 24.06  ? 142 ALA B CA  1 
ATOM   4314  C C   . ALA B 1 113 ? -10.921 -15.841 29.317  1.00 25.04  ? 142 ALA B C   1 
ATOM   4315  O O   . ALA B 1 113 ? -10.300 -16.424 28.441  1.00 27.80  ? 142 ALA B O   1 
ATOM   4316  C CB  . ALA B 1 113 ? -11.115 -16.429 31.726  1.00 25.10  ? 142 ALA B CB  1 
ATOM   4317  N N   . LYS B 1 114 ? -12.127 -15.288 29.092  1.00 26.20  ? 143 LYS B N   1 
ATOM   4318  C CA  . LYS B 1 114 ? -12.875 -15.499 27.858  1.00 26.21  ? 143 LYS B CA  1 
ATOM   4319  C C   . LYS B 1 114 ? -12.182 -14.953 26.610  1.00 25.01  ? 143 LYS B C   1 
ATOM   4320  O O   . LYS B 1 114 ? -12.335 -15.507 25.526  1.00 25.79  ? 143 LYS B O   1 
ATOM   4321  C CB  . LYS B 1 114 ? -14.285 -14.905 27.973  1.00 29.38  ? 143 LYS B CB  1 
ATOM   4322  C CG  . LYS B 1 114 ? -15.340 -15.887 28.460  1.00 35.06  ? 143 LYS B CG  1 
ATOM   4323  C CD  . LYS B 1 114 ? -16.749 -15.497 28.088  1.00 39.31  ? 143 LYS B CD  1 
ATOM   4324  C CE  . LYS B 1 114 ? -17.051 -14.041 28.357  1.00 41.65  ? 143 LYS B CE  1 
ATOM   4325  N NZ  . LYS B 1 114 ? -18.500 -13.769 28.215  1.00 46.27  ? 143 LYS B NZ  1 
ATOM   4326  N N   . ARG B 1 115 ? -11.438 -13.853 26.724  1.00 24.06  ? 144 ARG B N   1 
ATOM   4327  C CA  . ARG B 1 115 ? -10.839 -13.253 25.547  1.00 23.96  ? 144 ARG B CA  1 
ATOM   4328  C C   . ARG B 1 115 ? -9.420  -13.781 25.345  1.00 25.38  ? 144 ARG B C   1 
ATOM   4329  O O   . ARG B 1 115 ? -8.707  -13.271 24.488  1.00 30.94  ? 144 ARG B O   1 
ATOM   4330  C CB  . ARG B 1 115 ? -10.818 -11.730 25.707  1.00 24.30  ? 144 ARG B CB  1 
ATOM   4331  C CG  . ARG B 1 115 ? -12.158 -11.131 26.105  1.00 24.31  ? 144 ARG B CG  1 
ATOM   4332  C CD  . ARG B 1 115 ? -12.010 -9.699  26.549  1.00 26.51  ? 144 ARG B CD  1 
ATOM   4333  N NE  . ARG B 1 115 ? -13.296 -8.985  26.523  1.00 27.64  ? 144 ARG B NE  1 
ATOM   4334  C CZ  . ARG B 1 115 ? -13.594 -7.972  25.718  1.00 26.88  ? 144 ARG B CZ  1 
ATOM   4335  N NH1 . ARG B 1 115 ? -12.804 -7.665  24.700  1.00 25.61  ? 144 ARG B NH1 1 
ATOM   4336  N NH2 . ARG B 1 115 ? -14.731 -7.305  25.901  1.00 25.03  ? 144 ARG B NH2 1 
ATOM   4337  N N   . ALA B 1 116 ? -9.031  -14.769 26.151  1.00 30.12  ? 145 ALA B N   1 
ATOM   4338  C CA  . ALA B 1 116 ? -7.665  -15.321 26.057  1.00 32.20  ? 145 ALA B CA  1 
ATOM   4339  C C   . ALA B 1 116 ? -7.646  -16.361 24.956  1.00 34.79  ? 145 ALA B C   1 
ATOM   4340  O O   . ALA B 1 116 ? -8.243  -17.430 25.147  1.00 39.63  ? 145 ALA B O   1 
ATOM   4341  C CB  . ALA B 1 116 ? -7.187  -15.888 27.355  1.00 30.08  ? 145 ALA B CB  1 
ATOM   4342  N N   . ALA B 1 117 ? -6.945  -16.044 23.878  1.00 32.52  ? 146 ALA B N   1 
ATOM   4343  C CA  . ALA B 1 117 ? -6.879  -16.928 22.707  1.00 33.78  ? 146 ALA B CA  1 
ATOM   4344  C C   . ALA B 1 117 ? -5.904  -16.284 21.728  1.00 32.68  ? 146 ALA B C   1 
ATOM   4345  O O   . ALA B 1 117 ? -6.059  -15.113 21.403  1.00 30.92  ? 146 ALA B O   1 
ATOM   4346  C CB  . ALA B 1 117 ? -8.249  -17.048 22.109  1.00 36.25  ? 146 ALA B CB  1 
ATOM   4347  N N   . LEU B 1 118 ? -4.921  -17.050 21.281  1.00 27.66  ? 147 LEU B N   1 
ATOM   4348  C CA  . LEU B 1 118 ? -3.963  -16.512 20.297  1.00 28.51  ? 147 LEU B CA  1 
ATOM   4349  C C   . LEU B 1 118 ? -4.251  -17.036 18.887  1.00 26.92  ? 147 LEU B C   1 
ATOM   4350  O O   . LEU B 1 118 ? -4.605  -18.206 18.742  1.00 25.22  ? 147 LEU B O   1 
ATOM   4351  C CB  . LEU B 1 118 ? -2.534  -16.869 20.701  1.00 28.54  ? 147 LEU B CB  1 
ATOM   4352  C CG  . LEU B 1 118 ? -1.998  -16.172 21.953  1.00 28.78  ? 147 LEU B CG  1 
ATOM   4353  C CD1 . LEU B 1 118 ? -0.502  -16.393 22.077  1.00 29.38  ? 147 LEU B CD1 1 
ATOM   4354  C CD2 . LEU B 1 118 ? -2.320  -14.693 21.925  1.00 27.91  ? 147 LEU B CD2 1 
ATOM   4355  N N   . PRO B 1 119 ? -4.157  -16.181 17.863  1.00 25.84  ? 148 PRO B N   1 
ATOM   4356  C CA  . PRO B 1 119 ? -4.201  -16.626 16.471  1.00 28.13  ? 148 PRO B CA  1 
ATOM   4357  C C   . PRO B 1 119 ? -2.994  -17.460 16.058  1.00 30.88  ? 148 PRO B C   1 
ATOM   4358  O O   . PRO B 1 119 ? -1.891  -17.263 16.584  1.00 31.35  ? 148 PRO B O   1 
ATOM   4359  C CB  . PRO B 1 119 ? -4.175  -15.331 15.655  1.00 26.77  ? 148 PRO B CB  1 
ATOM   4360  C CG  . PRO B 1 119 ? -3.578  -14.305 16.592  1.00 28.72  ? 148 PRO B CG  1 
ATOM   4361  C CD  . PRO B 1 119 ? -3.984  -14.726 17.980  1.00 25.64  ? 148 PRO B CD  1 
ATOM   4362  N N   . SER B 1 120 ? -3.206  -18.345 15.071  1.00 30.54  ? 149 SER B N   1 
ATOM   4363  C CA  . SER B 1 120 ? -2.208  -19.342 14.740  1.00 32.04  ? 149 SER B CA  1 
ATOM   4364  C C   . SER B 1 120 ? -0.950  -18.699 14.156  1.00 30.47  ? 149 SER B C   1 
ATOM   4365  O O   . SER B 1 120 ? 0.134   -19.233 14.353  1.00 29.34  ? 149 SER B O   1 
ATOM   4366  C CB  . SER B 1 120 ? -2.779  -20.413 13.848  1.00 32.77  ? 149 SER B CB  1 
ATOM   4367  O OG  . SER B 1 120 ? -3.279  -19.869 12.648  1.00 35.13  ? 149 SER B OG  1 
ATOM   4368  N N   . HIS B 1 121 ? -1.057  -17.545 13.477  1.00 29.98  ? 150 HIS B N   1 
ATOM   4369  C CA  . HIS B 1 121 ? 0.142   -16.893 12.965  1.00 28.32  ? 150 HIS B CA  1 
ATOM   4370  C C   . HIS B 1 121 ? 1.064   -16.438 14.092  1.00 28.93  ? 150 HIS B C   1 
ATOM   4371  O O   . HIS B 1 121 ? 2.280   -16.495 13.934  1.00 27.26  ? 150 HIS B O   1 
ATOM   4372  C CB  . HIS B 1 121 ? -0.154  -15.738 12.005  1.00 29.85  ? 150 HIS B CB  1 
ATOM   4373  C CG  . HIS B 1 121 ? -0.664  -14.476 12.611  1.00 29.23  ? 150 HIS B CG  1 
ATOM   4374  N ND1 . HIS B 1 121 ? -1.974  -14.323 13.016  1.00 32.05  ? 150 HIS B ND1 1 
ATOM   4375  C CD2 . HIS B 1 121 ? -0.090  -13.286 12.765  1.00 28.07  ? 150 HIS B CD2 1 
ATOM   4376  C CE1 . HIS B 1 121 ? -2.157  -13.078 13.445  1.00 29.02  ? 150 HIS B CE1 1 
ATOM   4377  N NE2 . HIS B 1 121 ? -1.037  -12.426 13.285  1.00 29.06  ? 150 HIS B NE2 1 
ATOM   4378  N N   . VAL B 1 122 ? 0.502   -15.995 15.223  1.00 27.29  ? 151 VAL B N   1 
ATOM   4379  C CA  . VAL B 1 122 ? 1.329   -15.567 16.342  1.00 25.14  ? 151 VAL B CA  1 
ATOM   4380  C C   . VAL B 1 122 ? 1.930   -16.795 17.030  1.00 25.01  ? 151 VAL B C   1 
ATOM   4381  O O   . VAL B 1 122 ? 3.104   -16.794 17.424  1.00 22.30  ? 151 VAL B O   1 
ATOM   4382  C CB  . VAL B 1 122 ? 0.552   -14.631 17.293  1.00 26.07  ? 151 VAL B CB  1 
ATOM   4383  C CG1 . VAL B 1 122 ? 1.369   -14.265 18.522  1.00 24.92  ? 151 VAL B CG1 1 
ATOM   4384  C CG2 . VAL B 1 122 ? 0.116   -13.380 16.556  1.00 24.80  ? 151 VAL B CG2 1 
ATOM   4385  N N   . VAL B 1 123 ? 1.134   -17.861 17.140  1.00 27.40  ? 152 VAL B N   1 
ATOM   4386  C CA  . VAL B 1 123 ? 1.615   -19.153 17.610  1.00 28.44  ? 152 VAL B CA  1 
ATOM   4387  C C   . VAL B 1 123 ? 2.783   -19.600 16.730  1.00 26.27  ? 152 VAL B C   1 
ATOM   4388  O O   . VAL B 1 123 ? 3.852   -19.901 17.250  1.00 27.87  ? 152 VAL B O   1 
ATOM   4389  C CB  . VAL B 1 123 ? 0.465   -20.179 17.656  1.00 26.77  ? 152 VAL B CB  1 
ATOM   4390  C CG1 . VAL B 1 123 ? 0.958   -21.592 17.936  1.00 30.49  ? 152 VAL B CG1 1 
ATOM   4391  C CG2 . VAL B 1 123 ? -0.604  -19.780 18.663  1.00 27.82  ? 152 VAL B CG2 1 
ATOM   4392  N N   . THR B 1 124 ? 2.593   -19.574 15.400  1.00 25.95  ? 153 THR B N   1 
ATOM   4393  C CA  . THR B 1 124 ? 3.610   -19.964 14.443  1.00 26.93  ? 153 THR B CA  1 
ATOM   4394  C C   . THR B 1 124 ? 4.871   -19.146 14.695  1.00 25.31  ? 153 THR B C   1 
ATOM   4395  O O   . THR B 1 124 ? 5.951   -19.707 14.791  1.00 25.16  ? 153 THR B O   1 
ATOM   4396  C CB  . THR B 1 124 ? 3.095   -19.847 12.991  1.00 29.23  ? 153 THR B CB  1 
ATOM   4397  O OG1 . THR B 1 124 ? 2.013   -20.769 12.819  1.00 29.82  ? 153 THR B OG1 1 
ATOM   4398  C CG2 . THR B 1 124 ? 4.130   -20.126 11.926  1.00 29.93  ? 153 THR B CG2 1 
ATOM   4399  N N   . MET B 1 125 ? 4.720   -17.823 14.827  1.00 22.36  ? 154 MET B N   1 
ATOM   4400  C CA  . MET B 1 125 ? 5.877   -16.945 14.895  1.00 26.04  ? 154 MET B CA  1 
ATOM   4401  C C   . MET B 1 125 ? 6.693   -17.258 16.152  1.00 23.62  ? 154 MET B C   1 
ATOM   4402  O O   . MET B 1 125 ? 7.919   -17.406 16.103  1.00 22.93  ? 154 MET B O   1 
ATOM   4403  C CB  . MET B 1 125 ? 5.382   -15.495 14.902  1.00 24.06  ? 154 MET B CB  1 
ATOM   4404  C CG  . MET B 1 125 ? 6.465   -14.450 14.867  1.00 26.91  ? 154 MET B CG  1 
ATOM   4405  S SD  . MET B 1 125 ? 5.850   -12.758 15.176  1.00 32.29  ? 154 MET B SD  1 
ATOM   4406  C CE  . MET B 1 125 ? 4.099   -13.109 15.156  1.00 24.65  ? 154 MET B CE  1 
ATOM   4407  N N   . LEU B 1 126 ? 5.999   -17.413 17.288  1.00 23.34  ? 155 LEU B N   1 
ATOM   4408  C CA  . LEU B 1 126 ? 6.675   -17.651 18.554  1.00 23.46  ? 155 LEU B CA  1 
ATOM   4409  C C   . LEU B 1 126 ? 7.381   -18.995 18.509  1.00 24.72  ? 155 LEU B C   1 
ATOM   4410  O O   . LEU B 1 126 ? 8.550   -19.076 18.839  1.00 26.28  ? 155 LEU B O   1 
ATOM   4411  C CB  . LEU B 1 126 ? 5.664   -17.620 19.702  1.00 24.52  ? 155 LEU B CB  1 
ATOM   4412  C CG  . LEU B 1 126 ? 5.113   -16.232 20.028  1.00 24.78  ? 155 LEU B CG  1 
ATOM   4413  C CD1 . LEU B 1 126 ? 3.995   -16.341 21.033  1.00 24.48  ? 155 LEU B CD1 1 
ATOM   4414  C CD2 . LEU B 1 126 ? 6.237   -15.342 20.541  1.00 24.81  ? 155 LEU B CD2 1 
ATOM   4415  N N   . ASP B 1 127 ? 6.676   -20.035 18.071  1.00 24.73  ? 156 ASP B N   1 
ATOM   4416  C CA  . ASP B 1 127 ? 7.276   -21.367 18.014  1.00 27.32  ? 156 ASP B CA  1 
ATOM   4417  C C   . ASP B 1 127 ? 8.554   -21.378 17.158  1.00 27.30  ? 156 ASP B C   1 
ATOM   4418  O O   . ASP B 1 127 ? 9.454   -22.169 17.439  1.00 24.20  ? 156 ASP B O   1 
ATOM   4419  C CB  . ASP B 1 127 ? 6.240   -22.412 17.593  1.00 27.57  ? 156 ASP B CB  1 
ATOM   4420  C CG  . ASP B 1 127 ? 5.166   -22.683 18.642  1.00 31.88  ? 156 ASP B CG  1 
ATOM   4421  O OD1 . ASP B 1 127 ? 5.314   -22.189 19.773  1.00 31.86  ? 156 ASP B OD1 1 
ATOM   4422  O OD2 . ASP B 1 127 ? 4.146   -23.378 18.312  1.00 32.13  ? 156 ASP B OD2 1 
ATOM   4423  N N   . ASN B 1 128 ? 8.675   -20.496 16.152  1.00 28.65  ? 157 ASN B N   1 
ATOM   4424  C CA  . ASN B 1 128 ? 9.803   -20.541 15.224  1.00 29.37  ? 157 ASN B CA  1 
ATOM   4425  C C   . ASN B 1 128 ? 10.946  -19.611 15.630  1.00 27.93  ? 157 ASN B C   1 
ATOM   4426  O O   . ASN B 1 128 ? 11.978  -19.592 14.962  1.00 27.95  ? 157 ASN B O   1 
ATOM   4427  C CB  . ASN B 1 128 ? 9.422   -20.145 13.798  1.00 31.15  ? 157 ASN B CB  1 
ATOM   4428  C CG  . ASN B 1 128 ? 8.673   -21.226 13.055  1.00 31.86  ? 157 ASN B CG  1 
ATOM   4429  O OD1 . ASN B 1 128 ? 8.959   -22.403 13.241  1.00 31.86  ? 157 ASN B OD1 1 
ATOM   4430  N ND2 . ASN B 1 128 ? 7.711   -20.839 12.229  1.00 32.80  ? 157 ASN B ND2 1 
ATOM   4431  N N   . PHE B 1 129 ? 10.761  -18.803 16.681  1.00 28.31  ? 158 PHE B N   1 
ATOM   4432  C CA  . PHE B 1 129 ? 11.796  -17.869 17.099  1.00 26.87  ? 158 PHE B CA  1 
ATOM   4433  C C   . PHE B 1 129 ? 13.002  -18.618 17.667  1.00 29.26  ? 158 PHE B C   1 
ATOM   4434  O O   . PHE B 1 129 ? 12.856  -19.579 18.422  1.00 28.87  ? 158 PHE B O   1 
ATOM   4435  C CB  . PHE B 1 129 ? 11.247  -16.903 18.148  1.00 30.67  ? 158 PHE B CB  1 
ATOM   4436  C CG  . PHE B 1 129 ? 10.490  -15.716 17.603  1.00 28.46  ? 158 PHE B CG  1 
ATOM   4437  C CD1 . PHE B 1 129 ? 10.697  -15.262 16.307  1.00 27.78  ? 158 PHE B CD1 1 
ATOM   4438  C CD2 . PHE B 1 129 ? 9.569   -15.051 18.399  1.00 29.46  ? 158 PHE B CD2 1 
ATOM   4439  C CE1 . PHE B 1 129 ? 9.994   -14.173 15.820  1.00 27.92  ? 158 PHE B CE1 1 
ATOM   4440  C CE2 . PHE B 1 129 ? 8.866   -13.957 17.908  1.00 27.13  ? 158 PHE B CE2 1 
ATOM   4441  C CZ  . PHE B 1 129 ? 9.080   -13.525 16.616  1.00 27.18  ? 158 PHE B CZ  1 
ATOM   4442  N N   . PRO B 1 130 ? 14.242  -18.165 17.393  1.00 28.18  ? 159 PRO B N   1 
ATOM   4443  C CA  . PRO B 1 130 ? 15.422  -18.838 17.929  1.00 28.47  ? 159 PRO B CA  1 
ATOM   4444  C C   . PRO B 1 130 ? 15.613  -18.517 19.409  1.00 30.72  ? 159 PRO B C   1 
ATOM   4445  O O   . PRO B 1 130 ? 15.182  -17.476 19.925  1.00 25.92  ? 159 PRO B O   1 
ATOM   4446  C CB  . PRO B 1 130 ? 16.548  -18.267 17.078  1.00 27.81  ? 159 PRO B CB  1 
ATOM   4447  C CG  . PRO B 1 130 ? 16.091  -16.836 16.868  1.00 27.30  ? 159 PRO B CG  1 
ATOM   4448  C CD  . PRO B 1 130 ? 14.594  -16.949 16.646  1.00 27.45  ? 159 PRO B CD  1 
ATOM   4449  N N   . THR B 1 131 ? 16.325  -19.420 20.075  1.00 29.45  ? 160 THR B N   1 
ATOM   4450  C CA  . THR B 1 131 ? 16.537  -19.337 21.497  1.00 30.17  ? 160 THR B CA  1 
ATOM   4451  C C   . THR B 1 131 ? 17.376  -18.111 21.854  1.00 27.89  ? 160 THR B C   1 
ATOM   4452  O O   . THR B 1 131 ? 17.419  -17.730 23.018  1.00 29.42  ? 160 THR B O   1 
ATOM   4453  C CB  . THR B 1 131 ? 17.180  -20.635 21.991  1.00 31.77  ? 160 THR B CB  1 
ATOM   4454  O OG1 . THR B 1 131 ? 18.519  -20.613 21.502  1.00 34.20  ? 160 THR B OG1 1 
ATOM   4455  C CG2 . THR B 1 131 ? 16.427  -21.859 21.526  1.00 33.12  ? 160 THR B CG2 1 
ATOM   4456  N N   . ASN B 1 132 ? 18.025  -17.469 20.877  1.00 26.15  ? 161 ASN B N   1 
ATOM   4457  C CA  . ASN B 1 132 ? 18.877  -16.342 21.234  1.00 26.40  ? 161 ASN B CA  1 
ATOM   4458  C C   . ASN B 1 132 ? 18.180  -15.032 20.880  1.00 23.83  ? 161 ASN B C   1 
ATOM   4459  O O   . ASN B 1 132 ? 18.825  -14.002 20.887  1.00 27.41  ? 161 ASN B O   1 
ATOM   4460  C CB  . ASN B 1 132 ? 20.279  -16.418 20.623  1.00 31.18  ? 161 ASN B CB  1 
ATOM   4461  C CG  . ASN B 1 132 ? 20.314  -16.075 19.150  1.00 31.72  ? 161 ASN B CG  1 
ATOM   4462  O OD1 . ASN B 1 132 ? 21.253  -15.434 18.679  1.00 39.75  ? 161 ASN B OD1 1 
ATOM   4463  N ND2 . ASN B 1 132 ? 19.301  -16.504 18.415  1.00 27.96  ? 161 ASN B ND2 1 
ATOM   4464  N N   . LEU B 1 133 ? 16.889  -15.070 20.556  1.00 21.96  ? 162 LEU B N   1 
ATOM   4465  C CA  . LEU B 1 133 ? 16.141  -13.823 20.460  1.00 21.26  ? 162 LEU B CA  1 
ATOM   4466  C C   . LEU B 1 133 ? 15.558  -13.557 21.842  1.00 20.06  ? 162 LEU B C   1 
ATOM   4467  O O   . LEU B 1 133 ? 14.842  -14.397 22.399  1.00 19.70  ? 162 LEU B O   1 
ATOM   4468  C CB  . LEU B 1 133 ? 15.068  -13.923 19.374  1.00 22.00  ? 162 LEU B CB  1 
ATOM   4469  C CG  . LEU B 1 133 ? 14.180  -12.690 19.213  1.00 21.96  ? 162 LEU B CG  1 
ATOM   4470  C CD1 . LEU B 1 133 ? 15.042  -11.490 18.954  1.00 21.57  ? 162 LEU B CD1 1 
ATOM   4471  C CD2 . LEU B 1 133 ? 13.179  -12.901 18.091  1.00 24.67  ? 162 LEU B CD2 1 
ATOM   4472  N N   . HIS B 1 134 ? 15.900  -12.377 22.376  1.00 20.65  ? 163 HIS B N   1 
ATOM   4473  C CA  . HIS B 1 134 ? 15.657  -12.015 23.759  1.00 19.49  ? 163 HIS B CA  1 
ATOM   4474  C C   . HIS B 1 134 ? 14.161  -12.084 24.033  1.00 19.39  ? 163 HIS B C   1 
ATOM   4475  O O   . HIS B 1 134 ? 13.379  -11.638 23.212  1.00 21.81  ? 163 HIS B O   1 
ATOM   4476  C CB  . HIS B 1 134 ? 16.188  -10.596 24.029  1.00 19.88  ? 163 HIS B CB  1 
ATOM   4477  C CG  . HIS B 1 134 ? 16.108  -10.211 25.483  1.00 20.87  ? 163 HIS B CG  1 
ATOM   4478  N ND1 . HIS B 1 134 ? 14.954  -9.822  26.152  1.00 19.09  ? 163 HIS B ND1 1 
ATOM   4479  C CD2 . HIS B 1 134 ? 17.076  -10.232 26.404  1.00 20.82  ? 163 HIS B CD2 1 
ATOM   4480  C CE1 . HIS B 1 134 ? 15.248  -9.612  27.425  1.00 20.75  ? 163 HIS B CE1 1 
ATOM   4481  N NE2 . HIS B 1 134 ? 16.535  -9.849  27.598  1.00 21.59  ? 163 HIS B NE2 1 
ATOM   4482  N N   . PRO B 1 135 ? 13.691  -12.630 25.175  1.00 20.67  ? 164 PRO B N   1 
ATOM   4483  C CA  . PRO B 1 135 ? 12.260  -12.649 25.481  1.00 18.75  ? 164 PRO B CA  1 
ATOM   4484  C C   . PRO B 1 135 ? 11.496  -11.358 25.209  1.00 18.04  ? 164 PRO B C   1 
ATOM   4485  O O   . PRO B 1 135 ? 10.358  -11.427 24.718  1.00 21.53  ? 164 PRO B O   1 
ATOM   4486  C CB  . PRO B 1 135 ? 12.224  -13.007 26.973  1.00 19.02  ? 164 PRO B CB  1 
ATOM   4487  C CG  . PRO B 1 135 ? 13.394  -13.918 27.109  1.00 20.60  ? 164 PRO B CG  1 
ATOM   4488  C CD  . PRO B 1 135 ? 14.473  -13.266 26.249  1.00 20.21  ? 164 PRO B CD  1 
ATOM   4489  N N   . MET B 1 136 ? 12.113  -10.207 25.477  1.00 19.68  ? 165 MET B N   1 
ATOM   4490  C CA  . MET B 1 136 ? 11.385  -8.955  25.305  1.00 18.25  ? 165 MET B CA  1 
ATOM   4491  C C   . MET B 1 136 ? 11.121  -8.697  23.813  1.00 19.71  ? 165 MET B C   1 
ATOM   4492  O O   . MET B 1 136 ? 10.094  -8.115  23.433  1.00 17.93  ? 165 MET B O   1 
ATOM   4493  C CB  . MET B 1 136 ? 12.122  -7.760  25.929  1.00 15.60  ? 165 MET B CB  1 
ATOM   4494  C CG  . MET B 1 136 ? 11.915  -7.664  27.445  1.00 17.53  ? 165 MET B CG  1 
ATOM   4495  S SD  . MET B 1 136 ? 10.186  -7.415  27.933  1.00 17.88  ? 165 MET B SD  1 
ATOM   4496  C CE  . MET B 1 136 ? 10.085  -5.647  27.618  1.00 12.34  ? 165 MET B CE  1 
ATOM   4497  N N   . SER B 1 137 ? 12.024  -9.194  22.972  1.00 17.71  ? 166 SER B N   1 
ATOM   4498  C CA  . SER B 1 137 ? 11.920  -9.003  21.538  1.00 18.65  ? 166 SER B CA  1 
ATOM   4499  C C   . SER B 1 137 ? 10.796  -9.886  21.012  1.00 17.54  ? 166 SER B C   1 
ATOM   4500  O O   . SER B 1 137 ? 10.031  -9.487  20.157  1.00 19.88  ? 166 SER B O   1 
ATOM   4501  C CB  . SER B 1 137 ? 13.220  -9.295  20.874  1.00 18.55  ? 166 SER B CB  1 
ATOM   4502  O OG  . SER B 1 137 ? 14.149  -8.251  21.119  1.00 21.02  ? 166 SER B OG  1 
ATOM   4503  N N   . GLN B 1 138 ? 10.763  -11.132 21.491  1.00 17.35  ? 167 GLN B N   1 
ATOM   4504  C CA  . GLN B 1 138 ? 9.701   -12.039 21.147  1.00 19.34  ? 167 GLN B CA  1 
ATOM   4505  C C   . GLN B 1 138 ? 8.351   -11.450 21.540  1.00 17.97  ? 167 GLN B C   1 
ATOM   4506  O O   . GLN B 1 138 ? 7.414   -11.560 20.776  1.00 19.12  ? 167 GLN B O   1 
ATOM   4507  C CB  . GLN B 1 138 ? 9.929   -13.383 21.836  1.00 18.21  ? 167 GLN B CB  1 
ATOM   4508  C CG  . GLN B 1 138 ? 11.237  -14.028 21.383  1.00 19.24  ? 167 GLN B CG  1 
ATOM   4509  C CD  . GLN B 1 138 ? 11.253  -15.513 21.637  1.00 19.78  ? 167 GLN B CD  1 
ATOM   4510  O OE1 . GLN B 1 138 ? 10.214  -16.150 21.772  1.00 19.41  ? 167 GLN B OE1 1 
ATOM   4511  N NE2 . GLN B 1 138 ? 12.459  -16.055 21.700  1.00 23.39  ? 167 GLN B NE2 1 
ATOM   4512  N N   . LEU B 1 139 ? 8.287   -10.826 22.727  1.00 18.57  ? 168 LEU B N   1 
ATOM   4513  C CA  . LEU B 1 139 ? 7.050   -10.254 23.230  1.00 19.19  ? 168 LEU B CA  1 
ATOM   4514  C C   . LEU B 1 139 ? 6.586   -9.088  22.354  1.00 17.80  ? 168 LEU B C   1 
ATOM   4515  O O   . LEU B 1 139 ? 5.449   -9.073  21.908  1.00 15.30  ? 168 LEU B O   1 
ATOM   4516  C CB  . LEU B 1 139 ? 7.275   -9.773  24.659  1.00 19.80  ? 168 LEU B CB  1 
ATOM   4517  C CG  . LEU B 1 139 ? 6.085   -9.075  25.308  1.00 20.61  ? 168 LEU B CG  1 
ATOM   4518  C CD1 . LEU B 1 139 ? 4.912   -10.031 25.472  1.00 21.84  ? 168 LEU B CD1 1 
ATOM   4519  C CD2 . LEU B 1 139 ? 6.496   -8.469  26.627  1.00 20.35  ? 168 LEU B CD2 1 
ATOM   4520  N N   . SER B 1 140 ? 7.481   -8.129  22.139  1.00 19.43  ? 169 SER B N   1 
ATOM   4521  C CA  . SER B 1 140 ? 7.199   -6.964  21.318  1.00 21.54  ? 169 SER B CA  1 
ATOM   4522  C C   . SER B 1 140 ? 6.813   -7.413  19.905  1.00 19.60  ? 169 SER B C   1 
ATOM   4523  O O   . SER B 1 140 ? 5.802   -6.996  19.353  1.00 20.62  ? 169 SER B O   1 
ATOM   4524  C CB  . SER B 1 140 ? 8.364   -6.000  21.297  1.00 22.79  ? 169 SER B CB  1 
ATOM   4525  O OG  . SER B 1 140 ? 8.202   -5.028  20.282  1.00 21.86  ? 169 SER B OG  1 
ATOM   4526  N N   . ALA B 1 141 ? 7.594   -8.306  19.316  1.00 19.00  ? 170 ALA B N   1 
ATOM   4527  C CA  . ALA B 1 141 ? 7.320   -8.746  17.970  1.00 18.32  ? 170 ALA B CA  1 
ATOM   4528  C C   . ALA B 1 141 ? 5.924   -9.352  17.882  1.00 17.37  ? 170 ALA B C   1 
ATOM   4529  O O   . ALA B 1 141 ? 5.234   -9.114  16.906  1.00 17.76  ? 170 ALA B O   1 
ATOM   4530  C CB  . ALA B 1 141 ? 8.390   -9.723  17.518  1.00 18.83  ? 170 ALA B CB  1 
ATOM   4531  N N   . ALA B 1 142 ? 5.585   -10.216 18.854  1.00 18.78  ? 171 ALA B N   1 
ATOM   4532  C CA  . ALA B 1 142 ? 4.345   -10.979 18.845  1.00 19.42  ? 171 ALA B CA  1 
ATOM   4533  C C   . ALA B 1 142 ? 3.135   -10.060 19.004  1.00 21.45  ? 171 ALA B C   1 
ATOM   4534  O O   . ALA B 1 142 ? 2.061   -10.324 18.453  1.00 24.09  ? 171 ALA B O   1 
ATOM   4535  C CB  . ALA B 1 142 ? 4.356   -12.015 19.942  1.00 20.37  ? 171 ALA B CB  1 
ATOM   4536  N N   . VAL B 1 143 ? 3.310   -9.027  19.821  1.00 20.54  ? 172 VAL B N   1 
ATOM   4537  C CA  . VAL B 1 143 ? 2.257   -8.060  20.067  1.00 21.77  ? 172 VAL B CA  1 
ATOM   4538  C C   . VAL B 1 143 ? 2.022   -7.170  18.844  1.00 18.08  ? 172 VAL B C   1 
ATOM   4539  O O   . VAL B 1 143 ? 0.860   -6.936  18.511  1.00 18.64  ? 172 VAL B O   1 
ATOM   4540  C CB  . VAL B 1 143 ? 2.519   -7.242  21.343  1.00 20.51  ? 172 VAL B CB  1 
ATOM   4541  C CG1 . VAL B 1 143 ? 1.558   -6.075  21.456  1.00 19.91  ? 172 VAL B CG1 1 
ATOM   4542  C CG2 . VAL B 1 143 ? 2.413   -8.137  22.576  1.00 21.17  ? 172 VAL B CG2 1 
ATOM   4543  N N   . THR B 1 144 ? 3.093   -6.762  18.153  1.00 19.82  ? 173 THR B N   1 
ATOM   4544  C CA  . THR B 1 144 ? 3.000   -6.065  16.876  1.00 20.15  ? 173 THR B CA  1 
ATOM   4545  C C   . THR B 1 144 ? 2.189   -6.910  15.892  1.00 23.47  ? 173 THR B C   1 
ATOM   4546  O O   . THR B 1 144 ? 1.198   -6.446  15.355  1.00 24.56  ? 173 THR B O   1 
ATOM   4547  C CB  . THR B 1 144 ? 4.399   -5.675  16.380  1.00 21.07  ? 173 THR B CB  1 
ATOM   4548  O OG1 . THR B 1 144 ? 4.892   -4.742  17.334  1.00 21.27  ? 173 THR B OG1 1 
ATOM   4549  C CG2 . THR B 1 144 ? 4.428   -5.092  14.985  1.00 19.64  ? 173 THR B CG2 1 
ATOM   4550  N N   . ALA B 1 145 ? 2.504   -8.202  15.775  1.00 21.02  ? 174 ALA B N   1 
ATOM   4551  C CA  . ALA B 1 145 ? 1.795   -9.064  14.851  1.00 21.20  ? 174 ALA B CA  1 
ATOM   4552  C C   . ALA B 1 145 ? 0.344   -9.327  15.282  1.00 18.83  ? 174 ALA B C   1 
ATOM   4553  O O   . ALA B 1 145 ? -0.473  -9.702  14.443  1.00 19.26  ? 174 ALA B O   1 
ATOM   4554  C CB  . ALA B 1 145 ? 2.569   -10.347 14.673  1.00 19.99  ? 174 ALA B CB  1 
ATOM   4555  N N   . LEU B 1 146 ? -0.009  -9.145  16.572  1.00 18.87  ? 175 LEU B N   1 
ATOM   4556  C CA  . LEU B 1 146 ? -1.399  -9.307  16.995  1.00 21.61  ? 175 LEU B CA  1 
ATOM   4557  C C   . LEU B 1 146 ? -2.264  -8.169  16.457  1.00 22.51  ? 175 LEU B C   1 
ATOM   4558  O O   . LEU B 1 146 ? -3.494  -8.231  16.502  1.00 24.29  ? 175 LEU B O   1 
ATOM   4559  C CB  . LEU B 1 146 ? -1.488  -9.367  18.533  1.00 22.29  ? 175 LEU B CB  1 
ATOM   4560  C CG  . LEU B 1 146 ? -1.164  -10.708 19.189  1.00 23.95  ? 175 LEU B CG  1 
ATOM   4561  C CD1 . LEU B 1 146 ? -0.973  -10.531 20.686  1.00 23.58  ? 175 LEU B CD1 1 
ATOM   4562  C CD2 . LEU B 1 146 ? -2.260  -11.745 18.948  1.00 26.45  ? 175 LEU B CD2 1 
ATOM   4563  N N   . ASN B 1 147 ? -1.640  -7.098  15.969  1.00 23.07  ? 176 ASN B N   1 
ATOM   4564  C CA  . ASN B 1 147 ? -2.425  -5.952  15.533  1.00 23.87  ? 176 ASN B CA  1 
ATOM   4565  C C   . ASN B 1 147 ? -3.318  -6.316  14.341  1.00 23.79  ? 176 ASN B C   1 
ATOM   4566  O O   . ASN B 1 147 ? -4.253  -5.595  14.012  1.00 25.86  ? 176 ASN B O   1 
ATOM   4567  C CB  . ASN B 1 147 ? -1.511  -4.768  15.260  1.00 23.02  ? 176 ASN B CB  1 
ATOM   4568  C CG  . ASN B 1 147 ? -1.536  -4.346  13.819  1.00 24.79  ? 176 ASN B CG  1 
ATOM   4569  O OD1 . ASN B 1 147 ? -1.240  -5.136  12.933  1.00 28.78  ? 176 ASN B OD1 1 
ATOM   4570  N ND2 . ASN B 1 147 ? -1.889  -3.098  13.577  1.00 25.34  ? 176 ASN B ND2 1 
ATOM   4571  N N   . SER B 1 148 ? -3.086  -7.483  13.727  1.00 25.65  ? 177 SER B N   1 
ATOM   4572  C CA  . SER B 1 148 ? -3.989  -8.014  12.732  1.00 25.49  ? 177 SER B CA  1 
ATOM   4573  C C   . SER B 1 148 ? -5.385  -8.195  13.338  1.00 26.94  ? 177 SER B C   1 
ATOM   4574  O O   . SER B 1 148 ? -6.370  -8.117  12.621  1.00 30.63  ? 177 SER B O   1 
ATOM   4575  C CB  . SER B 1 148 ? -3.427  -9.277  12.091  1.00 24.73  ? 177 SER B CB  1 
ATOM   4576  O OG  . SER B 1 148 ? -3.367  -10.342 13.004  1.00 27.96  ? 177 SER B OG  1 
ATOM   4577  N N   . GLU B 1 149 ? -5.471  -8.339  14.665  1.00 26.10  ? 178 GLU B N   1 
ATOM   4578  C CA  . GLU B 1 149 ? -6.726  -8.582  15.351  1.00 29.89  ? 178 GLU B CA  1 
ATOM   4579  C C   . GLU B 1 149 ? -7.351  -7.278  15.852  1.00 28.19  ? 178 GLU B C   1 
ATOM   4580  O O   . GLU B 1 149 ? -8.357  -7.319  16.558  1.00 27.38  ? 178 GLU B O   1 
ATOM   4581  C CB  . GLU B 1 149 ? -6.517  -9.497  16.558  1.00 32.84  ? 178 GLU B CB  1 
ATOM   4582  C CG  . GLU B 1 149 ? -5.847  -10.819 16.214  1.00 37.24  ? 178 GLU B CG  1 
ATOM   4583  C CD  . GLU B 1 149 ? -6.447  -11.558 15.033  1.00 42.02  ? 178 GLU B CD  1 
ATOM   4584  O OE1 . GLU B 1 149 ? -7.619  -11.991 15.154  1.00 48.37  ? 178 GLU B OE1 1 
ATOM   4585  O OE2 . GLU B 1 149 ? -5.752  -11.677 13.985  1.00 43.65  ? 178 GLU B OE2 1 
ATOM   4586  N N   . SER B 1 150 ? -6.766  -6.134  15.489  1.00 24.37  ? 179 SER B N   1 
ATOM   4587  C CA  . SER B 1 150 ? -7.170  -4.867  16.075  1.00 25.35  ? 179 SER B CA  1 
ATOM   4588  C C   . SER B 1 150 ? -8.473  -4.349  15.467  1.00 26.53  ? 179 SER B C   1 
ATOM   4589  O O   . SER B 1 150 ? -8.583  -4.145  14.255  1.00 27.36  ? 179 SER B O   1 
ATOM   4590  C CB  . SER B 1 150 ? -6.108  -3.831  15.919  1.00 23.78  ? 179 SER B CB  1 
ATOM   4591  O OG  . SER B 1 150 ? -6.600  -2.592  16.398  1.00 21.04  ? 179 SER B OG  1 
ATOM   4592  N N   . ASN B 1 151 ? -9.427  -4.084  16.360  1.00 25.70  ? 180 ASN B N   1 
ATOM   4593  C CA  . ASN B 1 151 ? -10.732 -3.555  16.010  1.00 27.30  ? 180 ASN B CA  1 
ATOM   4594  C C   . ASN B 1 151 ? -10.629 -2.066  15.754  1.00 26.51  ? 180 ASN B C   1 
ATOM   4595  O O   . ASN B 1 151 ? -11.406 -1.509  14.982  1.00 27.66  ? 180 ASN B O   1 
ATOM   4596  C CB  . ASN B 1 151 ? -11.731 -3.781  17.141  1.00 31.19  ? 180 ASN B CB  1 
ATOM   4597  C CG  . ASN B 1 151 ? -11.971 -5.243  17.412  1.00 35.31  ? 180 ASN B CG  1 
ATOM   4598  O OD1 . ASN B 1 151 ? -12.451 -5.950  16.531  1.00 43.18  ? 180 ASN B OD1 1 
ATOM   4599  N ND2 . ASN B 1 151 ? -11.638 -5.693  18.614  1.00 42.02  ? 180 ASN B ND2 1 
ATOM   4600  N N   . PHE B 1 152 ? -9.708  -1.417  16.464  1.00 21.68  ? 181 PHE B N   1 
ATOM   4601  C CA  . PHE B 1 152 ? -9.524  0.003   16.252  1.00 23.09  ? 181 PHE B CA  1 
ATOM   4602  C C   . PHE B 1 152 ? -8.936  0.265   14.870  1.00 22.43  ? 181 PHE B C   1 
ATOM   4603  O O   . PHE B 1 152 ? -9.391  1.167   14.192  1.00 23.43  ? 181 PHE B O   1 
ATOM   4604  C CB  . PHE B 1 152 ? -8.653  0.628   17.331  1.00 24.05  ? 181 PHE B CB  1 
ATOM   4605  C CG  . PHE B 1 152 ? -8.505  2.112   17.158  1.00 25.06  ? 181 PHE B CG  1 
ATOM   4606  C CD1 . PHE B 1 152 ? -9.578  2.947   17.400  1.00 27.53  ? 181 PHE B CD1 1 
ATOM   4607  C CD2 . PHE B 1 152 ? -7.335  2.656   16.651  1.00 26.54  ? 181 PHE B CD2 1 
ATOM   4608  C CE1 . PHE B 1 152 ? -9.466  4.310   17.188  1.00 27.76  ? 181 PHE B CE1 1 
ATOM   4609  C CE2 . PHE B 1 152 ? -7.217  4.023   16.471  1.00 28.42  ? 181 PHE B CE2 1 
ATOM   4610  C CZ  . PHE B 1 152 ? -8.283  4.845   16.743  1.00 29.94  ? 181 PHE B CZ  1 
ATOM   4611  N N   . ALA B 1 153 ? -7.860  -0.437  14.485  1.00 23.16  ? 182 ALA B N   1 
ATOM   4612  C CA  . ALA B 1 153 ? -7.287  -0.200  13.168  1.00 26.11  ? 182 ALA B CA  1 
ATOM   4613  C C   . ALA B 1 153 ? -8.365  -0.370  12.098  1.00 26.43  ? 182 ALA B C   1 
ATOM   4614  O O   . ALA B 1 153 ? -8.476  0.440   11.182  1.00 28.25  ? 182 ALA B O   1 
ATOM   4615  C CB  . ALA B 1 153 ? -6.128  -1.122  12.901  1.00 24.06  ? 182 ALA B CB  1 
ATOM   4616  N N   . ARG B 1 154 ? -9.159  -1.433  12.239  1.00 27.62  ? 183 ARG B N   1 
ATOM   4617  C CA  . ARG B 1 154 ? -10.161 -1.809  11.256  1.00 31.16  ? 183 ARG B CA  1 
ATOM   4618  C C   . ARG B 1 154 ? -11.247 -0.735  11.127  1.00 31.09  ? 183 ARG B C   1 
ATOM   4619  O O   . ARG B 1 154 ? -11.675 -0.408  10.015  1.00 28.77  ? 183 ARG B O   1 
ATOM   4620  C CB  . ARG B 1 154 ? -10.780 -3.153  11.645  1.00 35.54  ? 183 ARG B CB  1 
ATOM   4621  C CG  . ARG B 1 154 ? -12.031 -3.491  10.849  1.00 40.06  ? 183 ARG B CG  1 
ATOM   4622  C CD  . ARG B 1 154 ? -12.580 -4.876  11.121  1.00 46.17  ? 183 ARG B CD  1 
ATOM   4623  N NE  . ARG B 1 154 ? -11.807 -5.966  10.537  1.00 53.39  ? 183 ARG B NE  1 
ATOM   4624  C CZ  . ARG B 1 154 ? -11.529 -6.102  9.238   1.00 54.33  ? 183 ARG B CZ  1 
ATOM   4625  N NH1 . ARG B 1 154 ? -11.030 -7.237  8.780   1.00 55.03  ? 183 ARG B NH1 1 
ATOM   4626  N NH2 . ARG B 1 154 ? -11.780 -5.117  8.390   1.00 56.11  ? 183 ARG B NH2 1 
ATOM   4627  N N   . ALA B 1 155 ? -11.696 -0.212  12.274  1.00 30.18  ? 184 ALA B N   1 
ATOM   4628  C CA  . ALA B 1 155 ? -12.802 0.729   12.325  1.00 26.49  ? 184 ALA B CA  1 
ATOM   4629  C C   . ALA B 1 155 ? -12.350 2.106   11.851  1.00 26.66  ? 184 ALA B C   1 
ATOM   4630  O O   . ALA B 1 155 ? -13.111 2.828   11.193  1.00 28.23  ? 184 ALA B O   1 
ATOM   4631  C CB  . ALA B 1 155 ? -13.344 0.778   13.734  1.00 28.31  ? 184 ALA B CB  1 
ATOM   4632  N N   . TYR B 1 156 ? -11.107 2.466   12.176  1.00 25.65  ? 185 TYR B N   1 
ATOM   4633  C CA  . TYR B 1 156 ? -10.537 3.751   11.785  1.00 27.17  ? 185 TYR B CA  1 
ATOM   4634  C C   . TYR B 1 156 ? -10.429 3.858   10.264  1.00 29.61  ? 185 TYR B C   1 
ATOM   4635  O O   . TYR B 1 156 ? -10.645 4.934   9.711   1.00 34.40  ? 185 TYR B O   1 
ATOM   4636  C CB  . TYR B 1 156 ? -9.135  4.009   12.364  1.00 26.86  ? 185 TYR B CB  1 
ATOM   4637  C CG  . TYR B 1 156 ? -8.607  5.384   12.009  1.00 24.40  ? 185 TYR B CG  1 
ATOM   4638  C CD1 . TYR B 1 156 ? -8.895  6.488   12.791  1.00 25.95  ? 185 TYR B CD1 1 
ATOM   4639  C CD2 . TYR B 1 156 ? -7.952  5.605   10.810  1.00 25.91  ? 185 TYR B CD2 1 
ATOM   4640  C CE1 . TYR B 1 156 ? -8.471  7.761   12.420  1.00 26.75  ? 185 TYR B CE1 1 
ATOM   4641  C CE2 . TYR B 1 156 ? -7.547  6.870   10.410  1.00 24.06  ? 185 TYR B CE2 1 
ATOM   4642  C CZ  . TYR B 1 156 ? -7.813  7.952   11.219  1.00 26.47  ? 185 TYR B CZ  1 
ATOM   4643  O OH  . TYR B 1 156 ? -7.380  9.194   10.814  1.00 29.99  ? 185 TYR B OH  1 
ATOM   4644  N N   . ALA B 1 157 ? -10.065 2.758   9.597   1.00 33.56  ? 186 ALA B N   1 
ATOM   4645  C CA  . ALA B 1 157 ? -10.016 2.715   8.137   1.00 35.61  ? 186 ALA B CA  1 
ATOM   4646  C C   . ALA B 1 157 ? -11.395 3.043   7.546   1.00 37.17  ? 186 ALA B C   1 
ATOM   4647  O O   . ALA B 1 157 ? -11.505 3.702   6.514   1.00 35.55  ? 186 ALA B O   1 
ATOM   4648  C CB  . ALA B 1 157 ? -9.528  1.358   7.677   1.00 32.79  ? 186 ALA B CB  1 
ATOM   4649  N N   . GLN B 1 158 ? -12.447 2.608   8.245   1.00 38.15  ? 187 GLN B N   1 
ATOM   4650  C CA  . GLN B 1 158 ? -13.817 2.739   7.785   1.00 34.15  ? 187 GLN B CA  1 
ATOM   4651  C C   . GLN B 1 158 ? -14.448 4.058   8.218   1.00 31.81  ? 187 GLN B C   1 
ATOM   4652  O O   . GLN B 1 158 ? -15.612 4.289   7.900   1.00 29.99  ? 187 GLN B O   1 
ATOM   4653  C CB  . GLN B 1 158 ? -14.641 1.553   8.288   1.00 36.50  ? 187 GLN B CB  1 
ATOM   4654  C CG  . GLN B 1 158 ? -14.238 0.266   7.591   1.00 39.15  ? 187 GLN B CG  1 
ATOM   4655  C CD  . GLN B 1 158 ? -14.953 -0.940  8.133   1.00 40.94  ? 187 GLN B CD  1 
ATOM   4656  O OE1 . GLN B 1 158 ? -15.248 -1.031  9.326   1.00 42.89  ? 187 GLN B OE1 1 
ATOM   4657  N NE2 . GLN B 1 158 ? -15.231 -1.873  7.239   1.00 42.87  ? 187 GLN B NE2 1 
ATOM   4658  N N   . GLY B 1 159 ? -13.698 4.912   8.924   1.00 26.02  ? 188 GLY B N   1 
ATOM   4659  C CA  . GLY B 1 159 ? -14.095 6.301   9.128   1.00 25.83  ? 188 GLY B CA  1 
ATOM   4660  C C   . GLY B 1 159 ? -14.926 6.499   10.397  1.00 26.40  ? 188 GLY B C   1 
ATOM   4661  O O   . GLY B 1 159 ? -15.712 7.440   10.474  1.00 25.38  ? 188 GLY B O   1 
ATOM   4662  N N   . ILE B 1 160 ? -14.699 5.649   11.402  1.00 27.89  ? 189 ILE B N   1 
ATOM   4663  C CA  . ILE B 1 160 ? -15.478 5.644   12.629  1.00 28.08  ? 189 ILE B CA  1 
ATOM   4664  C C   . ILE B 1 160 ? -15.384 7.000   13.322  1.00 25.88  ? 189 ILE B C   1 
ATOM   4665  O O   . ILE B 1 160 ? -14.378 7.706   13.229  1.00 22.86  ? 189 ILE B O   1 
ATOM   4666  C CB  . ILE B 1 160 ? -15.054 4.468   13.530  1.00 32.89  ? 189 ILE B CB  1 
ATOM   4667  C CG1 . ILE B 1 160 ? -16.200 4.027   14.441  1.00 32.92  ? 189 ILE B CG1 1 
ATOM   4668  C CG2 . ILE B 1 160 ? -13.767 4.781   14.290  1.00 35.65  ? 189 ILE B CG2 1 
ATOM   4669  C CD1 . ILE B 1 160 ? -17.263 3.237   13.718  1.00 35.18  ? 189 ILE B CD1 1 
ATOM   4670  N N   . SER B 1 161 ? -16.477 7.412   13.973  1.00 26.13  ? 190 SER B N   1 
ATOM   4671  C CA  . SER B 1 161 ? -16.494 8.710   14.638  1.00 24.53  ? 190 SER B CA  1 
ATOM   4672  C C   . SER B 1 161 ? -15.448 8.765   15.762  1.00 22.38  ? 190 SER B C   1 
ATOM   4673  O O   . SER B 1 161 ? -15.267 7.807   16.479  1.00 21.13  ? 190 SER B O   1 
ATOM   4674  C CB  . SER B 1 161 ? -17.877 9.032   15.137  1.00 21.63  ? 190 SER B CB  1 
ATOM   4675  O OG  . SER B 1 161 ? -17.852 10.032  16.146  1.00 22.15  ? 190 SER B OG  1 
ATOM   4676  N N   . ARG B 1 162 ? -14.805 9.925   15.962  1.00 22.73  ? 191 ARG B N   1 
ATOM   4677  C CA  . ARG B 1 162 ? -13.901 10.152  17.085  1.00 28.79  ? 191 ARG B CA  1 
ATOM   4678  C C   . ARG B 1 162 ? -14.576 9.897   18.440  1.00 26.17  ? 191 ARG B C   1 
ATOM   4679  O O   . ARG B 1 162 ? -13.883 9.690   19.433  1.00 22.78  ? 191 ARG B O   1 
ATOM   4680  C CB  . ARG B 1 162 ? -13.373 11.593  17.084  1.00 33.37  ? 191 ARG B CB  1 
ATOM   4681  C CG  . ARG B 1 162 ? -12.556 11.980  15.859  1.00 41.06  ? 191 ARG B CG  1 
ATOM   4682  C CD  . ARG B 1 162 ? -12.185 13.449  15.826  1.00 45.53  ? 191 ARG B CD  1 
ATOM   4683  N NE  . ARG B 1 162 ? -11.187 13.798  16.834  1.00 54.36  ? 191 ARG B NE  1 
ATOM   4684  C CZ  . ARG B 1 162 ? -11.432 14.530  17.923  1.00 61.12  ? 191 ARG B CZ  1 
ATOM   4685  N NH1 . ARG B 1 162 ? -12.634 15.053  18.112  1.00 63.63  ? 191 ARG B NH1 1 
ATOM   4686  N NH2 . ARG B 1 162 ? -10.477 14.742  18.818  1.00 54.89  ? 191 ARG B NH2 1 
ATOM   4687  N N   . THR B 1 163 ? -15.920 9.952   18.506  1.00 24.33  ? 192 THR B N   1 
ATOM   4688  C CA  . THR B 1 163 ? -16.618 9.742   19.764  1.00 22.98  ? 192 THR B CA  1 
ATOM   4689  C C   . THR B 1 163 ? -16.622 8.254   20.122  1.00 23.34  ? 192 THR B C   1 
ATOM   4690  O O   . THR B 1 163 ? -16.941 7.916   21.248  1.00 25.22  ? 192 THR B O   1 
ATOM   4691  C CB  . THR B 1 163 ? -18.052 10.280  19.695  1.00 25.46  ? 192 THR B CB  1 
ATOM   4692  O OG1 . THR B 1 163 ? -18.765 9.446   18.775  1.00 23.70  ? 192 THR B OG1 1 
ATOM   4693  C CG2 . THR B 1 163 ? -18.118 11.740  19.293  1.00 24.35  ? 192 THR B CG2 1 
ATOM   4694  N N   . LYS B 1 164 ? -16.281 7.384   19.161  1.00 24.08  ? 193 LYS B N   1 
ATOM   4695  C CA  . LYS B 1 164 ? -16.299 5.936   19.357  1.00 25.64  ? 193 LYS B CA  1 
ATOM   4696  C C   . LYS B 1 164 ? -14.897 5.366   19.613  1.00 22.80  ? 193 LYS B C   1 
ATOM   4697  O O   . LYS B 1 164 ? -14.751 4.166   19.859  1.00 23.40  ? 193 LYS B O   1 
ATOM   4698  C CB  . LYS B 1 164 ? -16.895 5.235   18.126  1.00 28.49  ? 193 LYS B CB  1 
ATOM   4699  C CG  . LYS B 1 164 ? -18.204 5.819   17.591  1.00 34.52  ? 193 LYS B CG  1 
ATOM   4700  C CD  . LYS B 1 164 ? -19.456 4.982   17.778  1.00 38.16  ? 193 LYS B CD  1 
ATOM   4701  C CE  . LYS B 1 164 ? -19.618 4.345   19.145  1.00 36.13  ? 193 LYS B CE  1 
ATOM   4702  N NZ  . LYS B 1 164 ? -19.458 2.870   19.087  1.00 37.78  ? 193 LYS B NZ  1 
ATOM   4703  N N   . TYR B 1 165 ? -13.852 6.183   19.489  1.00 20.59  ? 194 TYR B N   1 
ATOM   4704  C CA  . TYR B 1 165 ? -12.479 5.706   19.597  1.00 21.38  ? 194 TYR B CA  1 
ATOM   4705  C C   . TYR B 1 165 ? -12.270 4.954   20.913  1.00 22.62  ? 194 TYR B C   1 
ATOM   4706  O O   . TYR B 1 165 ? -11.665 3.884   20.924  1.00 24.87  ? 194 TYR B O   1 
ATOM   4707  C CB  . TYR B 1 165 ? -11.480 6.860   19.489  1.00 20.36  ? 194 TYR B CB  1 
ATOM   4708  C CG  . TYR B 1 165 ? -11.214 7.409   18.111  1.00 20.58  ? 194 TYR B CG  1 
ATOM   4709  C CD1 . TYR B 1 165 ? -11.719 6.812   16.974  1.00 19.77  ? 194 TYR B CD1 1 
ATOM   4710  C CD2 . TYR B 1 165 ? -10.481 8.571   17.945  1.00 20.48  ? 194 TYR B CD2 1 
ATOM   4711  C CE1 . TYR B 1 165 ? -11.471 7.317   15.708  1.00 20.13  ? 194 TYR B CE1 1 
ATOM   4712  C CE2 . TYR B 1 165 ? -10.234 9.101   16.687  1.00 20.12  ? 194 TYR B CE2 1 
ATOM   4713  C CZ  . TYR B 1 165 ? -10.729 8.475   15.563  1.00 19.96  ? 194 TYR B CZ  1 
ATOM   4714  O OH  . TYR B 1 165 ? -10.518 8.925   14.268  1.00 20.81  ? 194 TYR B OH  1 
ATOM   4715  N N   . TRP B 1 166 ? -12.786 5.474   22.025  1.00 20.79  ? 195 TRP B N   1 
ATOM   4716  C CA  . TRP B 1 166 ? -12.468 4.894   23.329  1.00 19.18  ? 195 TRP B CA  1 
ATOM   4717  C C   . TRP B 1 166 ? -13.032 3.486   23.463  1.00 18.66  ? 195 TRP B C   1 
ATOM   4718  O O   . TRP B 1 166 ? -12.376 2.661   24.081  1.00 18.34  ? 195 TRP B O   1 
ATOM   4719  C CB  . TRP B 1 166 ? -12.890 5.805   24.480  1.00 20.78  ? 195 TRP B CB  1 
ATOM   4720  C CG  . TRP B 1 166 ? -14.355 5.869   24.772  1.00 21.34  ? 195 TRP B CG  1 
ATOM   4721  C CD1 . TRP B 1 166 ? -15.209 6.895   24.487  1.00 26.01  ? 195 TRP B CD1 1 
ATOM   4722  C CD2 . TRP B 1 166 ? -15.136 4.890   25.475  1.00 20.98  ? 195 TRP B CD2 1 
ATOM   4723  N NE1 . TRP B 1 166 ? -16.473 6.596   24.918  1.00 25.86  ? 195 TRP B NE1 1 
ATOM   4724  C CE2 . TRP B 1 166 ? -16.462 5.378   25.539  1.00 23.35  ? 195 TRP B CE2 1 
ATOM   4725  C CE3 . TRP B 1 166 ? -14.857 3.651   26.053  1.00 21.54  ? 195 TRP B CE3 1 
ATOM   4726  C CZ2 . TRP B 1 166 ? -17.485 4.689   26.182  1.00 23.44  ? 195 TRP B CZ2 1 
ATOM   4727  C CZ3 . TRP B 1 166 ? -15.870 2.966   26.681  1.00 21.15  ? 195 TRP B CZ3 1 
ATOM   4728  C CH2 . TRP B 1 166 ? -17.171 3.460   26.726  1.00 23.07  ? 195 TRP B CH2 1 
ATOM   4729  N N   . GLU B 1 167 ? -14.228 3.240   22.924  1.00 17.12  ? 196 GLU B N   1 
ATOM   4730  C CA  . GLU B 1 167 ? -14.845 1.919   22.987  1.00 20.84  ? 196 GLU B CA  1 
ATOM   4731  C C   . GLU B 1 167 ? -13.973 0.889   22.261  1.00 22.34  ? 196 GLU B C   1 
ATOM   4732  O O   . GLU B 1 167 ? -13.927 -0.282  22.627  1.00 20.62  ? 196 GLU B O   1 
ATOM   4733  C CB  . GLU B 1 167 ? -16.259 1.983   22.384  1.00 25.31  ? 196 GLU B CB  1 
ATOM   4734  C CG  . GLU B 1 167 ? -17.041 3.229   22.783  1.00 26.50  ? 196 GLU B CG  1 
ATOM   4735  C CD  . GLU B 1 167 ? -18.552 3.144   22.680  1.00 31.30  ? 196 GLU B CD  1 
ATOM   4736  O OE1 . GLU B 1 167 ? -19.097 2.034   22.828  1.00 35.52  ? 196 GLU B OE1 1 
ATOM   4737  O OE2 . GLU B 1 167 ? -19.182 4.195   22.500  1.00 41.21  ? 196 GLU B OE2 1 
ATOM   4738  N N   . LEU B 1 168 ? -13.317 1.307   21.179  1.00 24.70  ? 197 LEU B N   1 
ATOM   4739  C CA  . LEU B 1 168 ? -12.549 0.388   20.357  1.00 23.48  ? 197 LEU B CA  1 
ATOM   4740  C C   . LEU B 1 168 ? -11.230 0.094   21.059  1.00 23.92  ? 197 LEU B C   1 
ATOM   4741  O O   . LEU B 1 168 ? -10.765 -1.052  21.092  1.00 23.03  ? 197 LEU B O   1 
ATOM   4742  C CB  . LEU B 1 168 ? -12.291 1.041   18.992  1.00 26.11  ? 197 LEU B CB  1 
ATOM   4743  C CG  . LEU B 1 168 ? -13.531 1.384   18.169  1.00 29.96  ? 197 LEU B CG  1 
ATOM   4744  C CD1 . LEU B 1 168 ? -13.150 2.250   16.970  1.00 29.57  ? 197 LEU B CD1 1 
ATOM   4745  C CD2 . LEU B 1 168 ? -14.259 0.122   17.714  1.00 29.73  ? 197 LEU B CD2 1 
ATOM   4746  N N   . ILE B 1 169 ? -10.618 1.148   21.590  1.00 22.00  ? 198 ILE B N   1 
ATOM   4747  C CA  . ILE B 1 169 ? -9.415  0.998   22.391  1.00 21.31  ? 198 ILE B CA  1 
ATOM   4748  C C   . ILE B 1 169 ? -9.726  0.056   23.558  1.00 19.91  ? 198 ILE B C   1 
ATOM   4749  O O   . ILE B 1 169 ? -8.944  -0.844  23.876  1.00 19.33  ? 198 ILE B O   1 
ATOM   4750  C CB  . ILE B 1 169 ? -8.914  2.372   22.869  1.00 23.52  ? 198 ILE B CB  1 
ATOM   4751  C CG1 . ILE B 1 169 ? -8.594  3.299   21.696  1.00 23.71  ? 198 ILE B CG1 1 
ATOM   4752  C CG2 . ILE B 1 169 ? -7.742  2.249   23.820  1.00 24.13  ? 198 ILE B CG2 1 
ATOM   4753  C CD1 . ILE B 1 169 ? -7.526  2.792   20.754  1.00 23.00  ? 198 ILE B CD1 1 
ATOM   4754  N N   . TYR B 1 170 ? -10.882 0.261   24.180  1.00 21.53  ? 199 TYR B N   1 
ATOM   4755  C CA  . TYR B 1 170 ? -11.276 -0.564  25.309  1.00 22.16  ? 199 TYR B CA  1 
ATOM   4756  C C   . TYR B 1 170 ? -11.287 -2.026  24.869  1.00 22.77  ? 199 TYR B C   1 
ATOM   4757  O O   . TYR B 1 170 ? -10.650 -2.875  25.495  1.00 21.91  ? 199 TYR B O   1 
ATOM   4758  C CB  . TYR B 1 170 ? -12.635 -0.117  25.859  1.00 23.31  ? 199 TYR B CB  1 
ATOM   4759  C CG  . TYR B 1 170 ? -13.276 -1.117  26.790  1.00 21.56  ? 199 TYR B CG  1 
ATOM   4760  C CD1 . TYR B 1 170 ? -14.090 -2.141  26.315  1.00 20.32  ? 199 TYR B CD1 1 
ATOM   4761  C CD2 . TYR B 1 170 ? -13.056 -1.046  28.155  1.00 20.22  ? 199 TYR B CD2 1 
ATOM   4762  C CE1 . TYR B 1 170 ? -14.668 -3.057  27.183  1.00 19.43  ? 199 TYR B CE1 1 
ATOM   4763  C CE2 . TYR B 1 170 ? -13.610 -1.959  29.026  1.00 19.98  ? 199 TYR B CE2 1 
ATOM   4764  C CZ  . TYR B 1 170 ? -14.420 -2.959  28.544  1.00 19.70  ? 199 TYR B CZ  1 
ATOM   4765  O OH  . TYR B 1 170 ? -14.934 -3.807  29.491  1.00 21.37  ? 199 TYR B OH  1 
ATOM   4766  N N   . GLU B 1 171 ? -12.007 -2.311  23.790  1.00 21.37  ? 200 GLU B N   1 
ATOM   4767  C CA  . GLU B 1 171 ? -12.129 -3.689  23.337  1.00 21.09  ? 200 GLU B CA  1 
ATOM   4768  C C   . GLU B 1 171 ? -10.758 -4.276  22.992  1.00 20.01  ? 200 GLU B C   1 
ATOM   4769  O O   . GLU B 1 171 ? -10.480 -5.414  23.352  1.00 20.82  ? 200 GLU B O   1 
ATOM   4770  C CB  . GLU B 1 171 ? -13.057 -3.780  22.137  1.00 21.81  ? 200 GLU B CB  1 
ATOM   4771  C CG  . GLU B 1 171 ? -14.506 -3.461  22.485  1.00 23.25  ? 200 GLU B CG  1 
ATOM   4772  C CD  . GLU B 1 171 ? -15.154 -4.407  23.480  1.00 25.76  ? 200 GLU B CD  1 
ATOM   4773  O OE1 . GLU B 1 171 ? -14.602 -5.517  23.702  1.00 28.44  ? 200 GLU B OE1 1 
ATOM   4774  O OE2 . GLU B 1 171 ? -16.197 -4.038  24.041  1.00 25.26  ? 200 GLU B OE2 1 
ATOM   4775  N N   . ASP B 1 172 ? -9.913  -3.546  22.257  1.00 18.16  ? 201 ASP B N   1 
ATOM   4776  C CA  . ASP B 1 172 ? -8.570  -4.049  21.927  1.00 18.63  ? 201 ASP B CA  1 
ATOM   4777  C C   . ASP B 1 172 ? -7.721  -4.223  23.195  1.00 20.67  ? 201 ASP B C   1 
ATOM   4778  O O   . ASP B 1 172 ? -6.959  -5.188  23.285  1.00 20.71  ? 201 ASP B O   1 
ATOM   4779  C CB  . ASP B 1 172 ? -7.861  -3.124  20.927  1.00 19.48  ? 201 ASP B CB  1 
ATOM   4780  C CG  . ASP B 1 172 ? -8.311  -3.261  19.471  1.00 21.02  ? 201 ASP B CG  1 
ATOM   4781  O OD1 . ASP B 1 172 ? -9.039  -4.238  19.138  1.00 22.79  ? 201 ASP B OD1 1 
ATOM   4782  O OD2 . ASP B 1 172 ? -7.944  -2.390  18.644  1.00 19.68  ? 201 ASP B OD2 1 
ATOM   4783  N N   . SER B 1 173 ? -7.807  -3.271  24.148  1.00 18.77  ? 202 SER B N   1 
ATOM   4784  C CA  . SER B 1 173 ? -7.038  -3.313  25.404  1.00 18.49  ? 202 SER B CA  1 
ATOM   4785  C C   . SER B 1 173 ? -7.387  -4.517  26.279  1.00 20.43  ? 202 SER B C   1 
ATOM   4786  O O   . SER B 1 173 ? -6.508  -5.207  26.790  1.00 18.47  ? 202 SER B O   1 
ATOM   4787  C CB  . SER B 1 173 ? -7.196  -2.077  26.176  1.00 19.40  ? 202 SER B CB  1 
ATOM   4788  O OG  . SER B 1 173 ? -6.574  -1.024  25.488  1.00 19.14  ? 202 SER B OG  1 
ATOM   4789  N N   . MET B 1 174 ? -8.698  -4.759  26.433  1.00 21.44  ? 203 MET B N   1 
ATOM   4790  C CA  . MET B 1 174 ? -9.187  -5.948  27.107  1.00 20.70  ? 203 MET B CA  1 
ATOM   4791  C C   . MET B 1 174 ? -8.667  -7.209  26.440  1.00 19.44  ? 203 MET B C   1 
ATOM   4792  O O   . MET B 1 174 ? -8.312  -8.131  27.171  1.00 22.61  ? 203 MET B O   1 
ATOM   4793  C CB  . MET B 1 174 ? -10.712 -5.985  27.105  1.00 20.07  ? 203 MET B CB  1 
ATOM   4794  C CG  . MET B 1 174 ? -11.327 -4.857  27.958  1.00 19.48  ? 203 MET B CG  1 
ATOM   4795  S SD  . MET B 1 174 ? -11.126 -5.022  29.760  1.00 23.14  ? 203 MET B SD  1 
ATOM   4796  C CE  . MET B 1 174 ? -12.292 -6.331  30.111  1.00 20.56  ? 203 MET B CE  1 
ATOM   4797  N N   . ASP B 1 175 ? -8.655  -7.253  25.096  1.00 18.50  ? 204 ASP B N   1 
ATOM   4798  C CA  . ASP B 1 175 ? -8.217  -8.461  24.378  1.00 19.24  ? 204 ASP B CA  1 
ATOM   4799  C C   . ASP B 1 175 ? -6.713  -8.693  24.630  1.00 20.35  ? 204 ASP B C   1 
ATOM   4800  O O   . ASP B 1 175 ? -6.250  -9.823  24.867  1.00 20.55  ? 204 ASP B O   1 
ATOM   4801  C CB  . ASP B 1 175 ? -8.530  -8.381  22.865  1.00 21.11  ? 204 ASP B CB  1 
ATOM   4802  C CG  . ASP B 1 175 ? -10.009 -8.543  22.477  1.00 23.88  ? 204 ASP B CG  1 
ATOM   4803  O OD1 . ASP B 1 175 ? -10.796 -9.006  23.319  1.00 26.32  ? 204 ASP B OD1 1 
ATOM   4804  O OD2 . ASP B 1 175 ? -10.380 -8.220  21.321  1.00 28.20  ? 204 ASP B OD2 1 
ATOM   4805  N N   . LEU B 1 176 ? -5.932  -7.622  24.534  1.00 19.54  ? 205 LEU B N   1 
ATOM   4806  C CA  . LEU B 1 176 ? -4.482  -7.703  24.618  1.00 19.03  ? 205 LEU B CA  1 
ATOM   4807  C C   . LEU B 1 176 ? -4.071  -8.111  26.034  1.00 19.26  ? 205 LEU B C   1 
ATOM   4808  O O   . LEU B 1 176 ? -3.295  -9.049  26.220  1.00 18.92  ? 205 LEU B O   1 
ATOM   4809  C CB  . LEU B 1 176 ? -3.894  -6.343  24.240  1.00 17.95  ? 205 LEU B CB  1 
ATOM   4810  C CG  . LEU B 1 176 ? -2.386  -6.174  24.439  1.00 16.86  ? 205 LEU B CG  1 
ATOM   4811  C CD1 . LEU B 1 176 ? -1.573  -7.279  23.774  1.00 18.79  ? 205 LEU B CD1 1 
ATOM   4812  C CD2 . LEU B 1 176 ? -1.953  -4.808  23.935  1.00 19.07  ? 205 LEU B CD2 1 
ATOM   4813  N N   . ILE B 1 177 ? -4.684  -7.477  27.029  1.00 19.37  ? 206 ILE B N   1 
ATOM   4814  C CA  . ILE B 1 177 ? -4.460  -7.822  28.426  1.00 18.54  ? 206 ILE B CA  1 
ATOM   4815  C C   . ILE B 1 177 ? -4.744  -9.290  28.656  1.00 19.52  ? 206 ILE B C   1 
ATOM   4816  O O   . ILE B 1 177 ? -3.912  -9.969  29.261  1.00 19.05  ? 206 ILE B O   1 
ATOM   4817  C CB  . ILE B 1 177 ? -5.256  -6.905  29.356  1.00 19.61  ? 206 ILE B CB  1 
ATOM   4818  C CG1 . ILE B 1 177 ? -4.670  -5.502  29.232  1.00 20.19  ? 206 ILE B CG1 1 
ATOM   4819  C CG2 . ILE B 1 177 ? -5.211  -7.441  30.792  1.00 20.95  ? 206 ILE B CG2 1 
ATOM   4820  C CD1 . ILE B 1 177 ? -5.568  -4.401  29.704  1.00 20.74  ? 206 ILE B CD1 1 
ATOM   4821  N N   . ALA B 1 178 ? -5.858  -9.758  28.095  1.00 17.70  ? 207 ALA B N   1 
ATOM   4822  C CA  . ALA B 1 178 ? -6.257  -11.159 28.188  1.00 19.68  ? 207 ALA B CA  1 
ATOM   4823  C C   . ALA B 1 178 ? -5.250  -12.081 27.527  1.00 21.09  ? 207 ALA B C   1 
ATOM   4824  O O   . ALA B 1 178 ? -5.089  -13.222 27.951  1.00 23.58  ? 207 ALA B O   1 
ATOM   4825  C CB  . ALA B 1 178 ? -7.607  -11.371 27.569  1.00 19.32  ? 207 ALA B CB  1 
ATOM   4826  N N   . LYS B 1 179 ? -4.622  -11.606 26.452  1.00 20.92  ? 208 LYS B N   1 
ATOM   4827  C CA  . LYS B 1 179 ? -3.806  -12.465 25.615  1.00 23.77  ? 208 LYS B CA  1 
ATOM   4828  C C   . LYS B 1 179 ? -2.390  -12.509 26.166  1.00 23.64  ? 208 LYS B C   1 
ATOM   4829  O O   . LYS B 1 179 ? -1.618  -13.395 25.808  1.00 24.91  ? 208 LYS B O   1 
ATOM   4830  C CB  . LYS B 1 179 ? -3.771  -11.935 24.181  1.00 25.52  ? 208 LYS B CB  1 
ATOM   4831  C CG  . LYS B 1 179 ? -4.984  -12.293 23.339  1.00 26.45  ? 208 LYS B CG  1 
ATOM   4832  C CD  . LYS B 1 179 ? -5.015  -11.584 22.012  1.00 29.85  ? 208 LYS B CD  1 
ATOM   4833  C CE  . LYS B 1 179 ? -6.171  -11.982 21.118  1.00 36.01  ? 208 LYS B CE  1 
ATOM   4834  N NZ  . LYS B 1 179 ? -7.398  -12.325 21.871  1.00 36.12  ? 208 LYS B NZ  1 
ATOM   4835  N N   . LEU B 1 180 ? -2.037  -11.505 26.971  1.00 21.75  ? 209 LEU B N   1 
ATOM   4836  C CA  . LEU B 1 180 ? -0.633  -11.230 27.220  1.00 22.05  ? 209 LEU B CA  1 
ATOM   4837  C C   . LEU B 1 180 ? 0.024   -12.428 27.901  1.00 21.53  ? 209 LEU B C   1 
ATOM   4838  O O   . LEU B 1 180 ? 1.019   -12.918 27.358  1.00 22.17  ? 209 LEU B O   1 
ATOM   4839  C CB  . LEU B 1 180 ? -0.479  -9.899  27.969  1.00 23.27  ? 209 LEU B CB  1 
ATOM   4840  C CG  . LEU B 1 180 ? -0.240  -8.701  27.048  1.00 22.40  ? 209 LEU B CG  1 
ATOM   4841  C CD1 . LEU B 1 180 ? -0.321  -7.384  27.808  1.00 23.20  ? 209 LEU B CD1 1 
ATOM   4842  C CD2 . LEU B 1 180 ? 1.114   -8.804  26.347  1.00 22.82  ? 209 LEU B CD2 1 
ATOM   4843  N N   . PRO B 1 181 ? -0.514  -12.952 29.036  1.00 22.71  ? 210 PRO B N   1 
ATOM   4844  C CA  . PRO B 1 181 ? 0.052   -14.137 29.689  1.00 23.28  ? 210 PRO B CA  1 
ATOM   4845  C C   . PRO B 1 181 ? 0.206   -15.299 28.706  1.00 22.90  ? 210 PRO B C   1 
ATOM   4846  O O   . PRO B 1 181 ? 1.143   -16.086 28.822  1.00 21.34  ? 210 PRO B O   1 
ATOM   4847  C CB  . PRO B 1 181 ? -0.944  -14.470 30.828  1.00 22.49  ? 210 PRO B CB  1 
ATOM   4848  C CG  . PRO B 1 181 ? -1.658  -13.140 31.111  1.00 22.24  ? 210 PRO B CG  1 
ATOM   4849  C CD  . PRO B 1 181 ? -1.678  -12.442 29.772  1.00 22.48  ? 210 PRO B CD  1 
ATOM   4850  N N   . CYS B 1 182 ? -0.713  -15.420 27.752  1.00 23.22  ? 211 CYS B N   1 
ATOM   4851  C CA  . CYS B 1 182 ? -0.609  -16.489 26.764  1.00 25.80  ? 211 CYS B CA  1 
ATOM   4852  C C   . CYS B 1 182 ? 0.691   -16.377 25.979  1.00 22.45  ? 211 CYS B C   1 
ATOM   4853  O O   . CYS B 1 182 ? 1.401   -17.358 25.843  1.00 22.10  ? 211 CYS B O   1 
ATOM   4854  C CB  . CYS B 1 182 ? -1.779  -16.535 25.788  1.00 27.31  ? 211 CYS B CB  1 
ATOM   4855  S SG  . CYS B 1 182 ? -3.349  -16.950 26.588  1.00 30.71  ? 211 CYS B SG  1 
ATOM   4856  N N   . VAL B 1 183 ? 0.990   -15.176 25.476  1.00 20.46  ? 212 VAL B N   1 
ATOM   4857  C CA  . VAL B 1 183 ? 2.226   -14.896 24.765  1.00 21.50  ? 212 VAL B CA  1 
ATOM   4858  C C   . VAL B 1 183 ? 3.419   -15.124 25.689  1.00 21.21  ? 212 VAL B C   1 
ATOM   4859  O O   . VAL B 1 183 ? 4.354   -15.864 25.362  1.00 20.81  ? 212 VAL B O   1 
ATOM   4860  C CB  . VAL B 1 183 ? 2.210   -13.431 24.273  1.00 20.28  ? 212 VAL B CB  1 
ATOM   4861  C CG1 . VAL B 1 183 ? 3.542   -13.003 23.701  1.00 20.90  ? 212 VAL B CG1 1 
ATOM   4862  C CG2 . VAL B 1 183 ? 1.081   -13.176 23.283  1.00 21.65  ? 212 VAL B CG2 1 
ATOM   4863  N N   . ALA B 1 184 ? 3.364   -14.496 26.868  1.00 19.52  ? 213 ALA B N   1 
ATOM   4864  C CA  . ALA B 1 184 ? 4.492   -14.517 27.788  1.00 19.08  ? 213 ALA B CA  1 
ATOM   4865  C C   . ALA B 1 184 ? 4.843   -15.955 28.180  1.00 18.50  ? 213 ALA B C   1 
ATOM   4866  O O   . ALA B 1 184 ? 6.027   -16.293 28.262  1.00 18.65  ? 213 ALA B O   1 
ATOM   4867  C CB  . ALA B 1 184 ? 4.186   -13.665 28.995  1.00 19.29  ? 213 ALA B CB  1 
ATOM   4868  N N   . ALA B 1 185 ? 3.825   -16.782 28.405  1.00 21.72  ? 214 ALA B N   1 
ATOM   4869  C CA  . ALA B 1 185 ? 4.069   -18.140 28.877  1.00 23.37  ? 214 ALA B CA  1 
ATOM   4870  C C   . ALA B 1 185 ? 4.615   -19.015 27.756  1.00 22.00  ? 214 ALA B C   1 
ATOM   4871  O O   . ALA B 1 185 ? 5.443   -19.893 28.022  1.00 21.39  ? 214 ALA B O   1 
ATOM   4872  C CB  . ALA B 1 185 ? 2.824   -18.721 29.514  1.00 22.12  ? 214 ALA B CB  1 
ATOM   4873  N N   . LYS B 1 186 ? 4.158   -18.804 26.515  1.00 24.43  ? 215 LYS B N   1 
ATOM   4874  C CA  . LYS B 1 186 ? 4.690   -19.553 25.384  1.00 22.83  ? 215 LYS B CA  1 
ATOM   4875  C C   . LYS B 1 186 ? 6.172   -19.228 25.197  1.00 22.72  ? 215 LYS B C   1 
ATOM   4876  O O   . LYS B 1 186 ? 6.978   -20.081 24.825  1.00 23.28  ? 215 LYS B O   1 
ATOM   4877  C CB  . LYS B 1 186 ? 3.914   -19.273 24.088  1.00 24.27  ? 215 LYS B CB  1 
ATOM   4878  C CG  . LYS B 1 186 ? 4.374   -20.071 22.870  1.00 26.57  ? 215 LYS B CG  1 
ATOM   4879  C CD  . LYS B 1 186 ? 3.262   -20.728 22.037  1.00 26.95  ? 215 LYS B CD  1 
ATOM   4880  C CE  . LYS B 1 186 ? 3.239   -22.249 22.080  1.00 25.02  ? 215 LYS B CE  1 
ATOM   4881  N N   . ILE B 1 187 ? 6.524   -17.958 25.367  1.00 23.46  ? 216 ILE B N   1 
ATOM   4882  C CA  . ILE B 1 187 ? 7.915   -17.584 25.283  1.00 21.41  ? 216 ILE B CA  1 
ATOM   4883  C C   . ILE B 1 187 ? 8.682   -18.338 26.374  1.00 24.18  ? 216 ILE B C   1 
ATOM   4884  O O   . ILE B 1 187 ? 9.759   -18.852 26.119  1.00 23.86  ? 216 ILE B O   1 
ATOM   4885  C CB  . ILE B 1 187 ? 8.064   -16.053 25.377  1.00 21.24  ? 216 ILE B CB  1 
ATOM   4886  C CG1 . ILE B 1 187 ? 7.482   -15.385 24.130  1.00 17.33  ? 216 ILE B CG1 1 
ATOM   4887  C CG2 . ILE B 1 187 ? 9.528   -15.698 25.571  1.00 20.62  ? 216 ILE B CG2 1 
ATOM   4888  C CD1 . ILE B 1 187 ? 7.447   -13.882 24.201  1.00 18.62  ? 216 ILE B CD1 1 
ATOM   4889  N N   . TYR B 1 188 ? 8.127   -18.375 27.585  1.00 26.13  ? 217 TYR B N   1 
ATOM   4890  C CA  . TYR B 1 188 ? 8.804   -18.998 28.713  1.00 26.56  ? 217 TYR B CA  1 
ATOM   4891  C C   . TYR B 1 188 ? 8.988   -20.480 28.432  1.00 24.16  ? 217 TYR B C   1 
ATOM   4892  O O   . TYR B 1 188 ? 10.089  -20.982 28.561  1.00 26.69  ? 217 TYR B O   1 
ATOM   4893  C CB  . TYR B 1 188 ? 8.039   -18.863 30.026  1.00 24.23  ? 217 TYR B CB  1 
ATOM   4894  C CG  . TYR B 1 188 ? 8.846   -19.244 31.253  1.00 26.64  ? 217 TYR B CG  1 
ATOM   4895  C CD1 . TYR B 1 188 ? 9.860   -18.440 31.746  1.00 24.92  ? 217 TYR B CD1 1 
ATOM   4896  C CD2 . TYR B 1 188 ? 8.667   -20.475 31.864  1.00 27.08  ? 217 TYR B CD2 1 
ATOM   4897  C CE1 . TYR B 1 188 ? 10.589  -18.794 32.875  1.00 27.53  ? 217 TYR B CE1 1 
ATOM   4898  C CE2 . TYR B 1 188 ? 9.392   -20.852 32.984  1.00 26.43  ? 217 TYR B CE2 1 
ATOM   4899  C CZ  . TYR B 1 188 ? 10.371  -20.021 33.488  1.00 28.73  ? 217 TYR B CZ  1 
ATOM   4900  O OH  . TYR B 1 188 ? 11.081  -20.412 34.606  1.00 27.86  ? 217 TYR B OH  1 
ATOM   4901  N N   . ARG B 1 189 ? 7.905   -21.136 28.027  1.00 24.69  ? 218 ARG B N   1 
ATOM   4902  C CA  . ARG B 1 189 ? 7.966   -22.573 27.838  1.00 27.93  ? 218 ARG B CA  1 
ATOM   4903  C C   . ARG B 1 189 ? 8.911   -22.902 26.685  1.00 28.22  ? 218 ARG B C   1 
ATOM   4904  O O   . ARG B 1 189 ? 9.670   -23.876 26.765  1.00 29.56  ? 218 ARG B O   1 
ATOM   4905  C CB  . ARG B 1 189 ? 6.572   -23.137 27.597  1.00 29.65  ? 218 ARG B CB  1 
ATOM   4906  C CG  . ARG B 1 189 ? 5.701   -23.136 28.840  1.00 36.47  ? 218 ARG B CG  1 
ATOM   4907  C CD  . ARG B 1 189 ? 5.084   -24.505 29.042  1.00 45.93  ? 218 ARG B CD  1 
ATOM   4908  N NE  . ARG B 1 189 ? 4.130   -24.540 30.145  1.00 49.04  ? 218 ARG B NE  1 
ATOM   4909  C CZ  . ARG B 1 189 ? 3.872   -25.606 30.892  1.00 49.94  ? 218 ARG B CZ  1 
ATOM   4910  N NH1 . ARG B 1 189 ? 4.400   -26.780 30.580  1.00 48.14  ? 218 ARG B NH1 1 
ATOM   4911  N NH2 . ARG B 1 189 ? 3.054   -25.495 31.927  1.00 47.62  ? 218 ARG B NH2 1 
ATOM   4912  N N   . ASN B 1 190 ? 8.872   -22.090 25.626  1.00 22.80  ? 219 ASN B N   1 
ATOM   4913  C CA  . ASN B 1 190 ? 9.658   -22.381 24.439  1.00 23.74  ? 219 ASN B CA  1 
ATOM   4914  C C   . ASN B 1 190 ? 11.142  -22.219 24.738  1.00 26.20  ? 219 ASN B C   1 
ATOM   4915  O O   . ASN B 1 190 ? 11.944  -23.041 24.308  1.00 27.17  ? 219 ASN B O   1 
ATOM   4916  C CB  . ASN B 1 190 ? 9.267   -21.538 23.228  1.00 25.64  ? 219 ASN B CB  1 
ATOM   4917  C CG  . ASN B 1 190 ? 7.945   -21.955 22.625  1.00 24.95  ? 219 ASN B CG  1 
ATOM   4918  O OD1 . ASN B 1 190 ? 7.391   -22.991 22.984  1.00 26.01  ? 219 ASN B OD1 1 
ATOM   4919  N ND2 . ASN B 1 190 ? 7.464   -21.192 21.669  1.00 25.07  ? 219 ASN B ND2 1 
ATOM   4920  N N   . LEU B 1 191 ? 11.506  -21.164 25.468  1.00 28.62  ? 220 LEU B N   1 
ATOM   4921  C CA  . LEU B 1 191 ? 12.913  -20.904 25.742  1.00 27.70  ? 220 LEU B CA  1 
ATOM   4922  C C   . LEU B 1 191 ? 13.487  -21.848 26.806  1.00 27.13  ? 220 LEU B C   1 
ATOM   4923  O O   . LEU B 1 191 ? 14.664  -22.220 26.747  1.00 25.94  ? 220 LEU B O   1 
ATOM   4924  C CB  . LEU B 1 191 ? 13.053  -19.439 26.162  1.00 30.22  ? 220 LEU B CB  1 
ATOM   4925  C CG  . LEU B 1 191 ? 13.105  -18.438 25.011  1.00 31.17  ? 220 LEU B CG  1 
ATOM   4926  C CD1 . LEU B 1 191 ? 13.290  -17.029 25.543  1.00 30.12  ? 220 LEU B CD1 1 
ATOM   4927  C CD2 . LEU B 1 191 ? 14.228  -18.781 24.045  1.00 30.61  ? 220 LEU B CD2 1 
ATOM   4928  N N   . TYR B 1 192 ? 12.681  -22.187 27.809  1.00 27.35  ? 221 TYR B N   1 
ATOM   4929  C CA  . TYR B 1 192 ? 13.236  -22.687 29.055  1.00 28.51  ? 221 TYR B CA  1 
ATOM   4930  C C   . TYR B 1 192 ? 12.601  -24.000 29.503  1.00 30.64  ? 221 TYR B C   1 
ATOM   4931  O O   . TYR B 1 192 ? 13.023  -24.533 30.518  1.00 31.24  ? 221 TYR B O   1 
ATOM   4932  C CB  . TYR B 1 192 ? 13.084  -21.641 30.154  1.00 28.29  ? 221 TYR B CB  1 
ATOM   4933  C CG  . TYR B 1 192 ? 13.628  -20.284 29.783  1.00 27.87  ? 221 TYR B CG  1 
ATOM   4934  C CD1 . TYR B 1 192 ? 14.917  -20.131 29.290  1.00 28.31  ? 221 TYR B CD1 1 
ATOM   4935  C CD2 . TYR B 1 192 ? 12.845  -19.149 29.895  1.00 29.38  ? 221 TYR B CD2 1 
ATOM   4936  C CE1 . TYR B 1 192 ? 15.415  -18.887 28.936  1.00 27.76  ? 221 TYR B CE1 1 
ATOM   4937  C CE2 . TYR B 1 192 ? 13.331  -17.899 29.557  1.00 26.24  ? 221 TYR B CE2 1 
ATOM   4938  C CZ  . TYR B 1 192 ? 14.620  -17.765 29.078  1.00 27.09  ? 221 TYR B CZ  1 
ATOM   4939  O OH  . TYR B 1 192 ? 15.115  -16.524 28.748  1.00 26.50  ? 221 TYR B OH  1 
ATOM   4940  N N   . ARG B 1 193 ? 11.572  -24.455 28.796  1.00 30.77  ? 222 ARG B N   1 
ATOM   4941  C CA  . ARG B 1 193 ? 10.923  -25.746 29.134  1.00 33.05  ? 222 ARG B CA  1 
ATOM   4942  C C   . ARG B 1 193 ? 10.779  -26.607 27.869  1.00 34.32  ? 222 ARG B C   1 
ATOM   4943  O O   . ARG B 1 193 ? 9.803   -27.364 27.793  1.00 39.38  ? 222 ARG B O   1 
ATOM   4944  C CB  . ARG B 1 193 ? 9.573   -25.560 29.838  1.00 33.11  ? 222 ARG B CB  1 
ATOM   4945  C CG  . ARG B 1 193 ? 9.549   -24.601 31.018  1.00 37.69  ? 222 ARG B CG  1 
ATOM   4946  C CD  . ARG B 1 193 ? 10.197  -25.198 32.245  1.00 47.23  ? 222 ARG B CD  1 
ATOM   4947  N NE  . ARG B 1 193 ? 11.194  -24.305 32.846  1.00 52.78  ? 222 ARG B NE  1 
ATOM   4948  C CZ  . ARG B 1 193 ? 11.158  -23.918 34.105  1.00 59.40  ? 222 ARG B CZ  1 
ATOM   4949  N NH1 . ARG B 1 193 ? 12.072  -23.096 34.575  1.00 48.70  ? 222 ARG B NH1 1 
ATOM   4950  N NH2 . ARG B 1 193 ? 10.196  -24.352 34.889  1.00 58.93  ? 222 ARG B NH2 1 
ATOM   4951  N N   . GLU B 1 194 ? 11.702  -26.483 26.920  1.00 35.94  ? 223 GLU B N   1 
ATOM   4952  C CA  . GLU B 1 194 ? 11.702  -27.353 25.718  1.00 41.43  ? 223 GLU B CA  1 
ATOM   4953  C C   . GLU B 1 194 ? 10.353  -27.323 24.974  1.00 45.21  ? 223 GLU B C   1 
ATOM   4954  O O   . GLU B 1 194 ? 10.080  -28.261 24.211  1.00 42.82  ? 223 GLU B O   1 
ATOM   4955  C CB  . GLU B 1 194 ? 12.065  -28.793 26.094  1.00 45.26  ? 223 GLU B CB  1 
ATOM   4956  C CG  . GLU B 1 194 ? 13.493  -28.950 26.603  1.00 49.99  ? 223 GLU B CG  1 
ATOM   4957  C CD  . GLU B 1 194 ? 13.875  -30.411 26.733  1.00 59.95  ? 223 GLU B CD  1 
ATOM   4958  O OE1 . GLU B 1 194 ? 12.971  -31.259 26.598  1.00 66.70  ? 223 GLU B OE1 1 
ATOM   4959  O OE2 . GLU B 1 194 ? 15.061  -30.703 26.977  1.00 65.04  ? 223 GLU B OE2 1 
ATOM   4960  N N   . GLY B 1 195 ? 9.561   -26.269 25.195  1.00 46.26  ? 224 GLY B N   1 
ATOM   4961  C CA  . GLY B 1 195 ? 8.246   -26.149 24.536  1.00 47.92  ? 224 GLY B CA  1 
ATOM   4962  C C   . GLY B 1 195 ? 7.285   -27.204 25.045  1.00 47.16  ? 224 GLY B C   1 
ATOM   4963  O O   . GLY B 1 195 ? 6.766   -27.979 24.215  1.00 51.66  ? 224 GLY B O   1 
ATOM   4964  N N   . SER B 1 196 ? 7.044   -27.230 26.337  1.00 51.12  ? 225 SER B N   1 
ATOM   4965  C CA  . SER B 1 196 ? 5.932   -28.055 26.840  1.00 56.06  ? 225 SER B CA  1 
ATOM   4966  C C   . SER B 1 196 ? 4.690   -27.256 26.429  1.00 70.18  ? 225 SER B C   1 
ATOM   4967  O O   . SER B 1 196 ? 4.854   -26.055 26.100  1.00 76.38  ? 225 SER B O   1 
ATOM   4968  C CB  . SER B 1 196 ? 6.014   -28.168 28.303  1.00 54.04  ? 225 SER B CB  1 
ATOM   4969  O OG  . SER B 1 196 ? 6.873   -27.175 28.837  1.00 48.52  ? 225 SER B OG  1 
ATOM   4970  N N   . GLY B 1 197 ? 3.497   -27.850 26.436  1.00 77.51  ? 226 GLY B N   1 
ATOM   4971  C CA  . GLY B 1 197 ? 2.313   -27.129 25.927  1.00 73.95  ? 226 GLY B CA  1 
ATOM   4972  C C   . GLY B 1 197 ? 1.309   -26.928 27.035  1.00 79.14  ? 226 GLY B C   1 
ATOM   4973  O O   . GLY B 1 197 ? 0.220   -26.375 26.788  1.00 70.44  ? 226 GLY B O   1 
ATOM   4974  N N   . ILE B 1 198 ? 1.660   -27.386 28.228  1.00 88.12  ? 227 ILE B N   1 
ATOM   4975  C CA  . ILE B 1 198 ? 0.730   -27.114 29.356  1.00 88.75  ? 227 ILE B CA  1 
ATOM   4976  C C   . ILE B 1 198 ? 0.507   -25.593 29.397  1.00 83.44  ? 227 ILE B C   1 
ATOM   4977  O O   . ILE B 1 198 ? 1.483   -24.840 29.520  1.00 85.29  ? 227 ILE B O   1 
ATOM   4978  C CB  . ILE B 1 198 ? 1.245   -27.707 30.684  1.00 87.43  ? 227 ILE B CB  1 
ATOM   4979  C CG1 . ILE B 1 198 ? 1.899   -29.076 30.471  1.00 90.04  ? 227 ILE B CG1 1 
ATOM   4980  C CG2 . ILE B 1 198 ? 0.130   -27.765 31.729  1.00 80.29  ? 227 ILE B CG2 1 
ATOM   4981  C CD1 . ILE B 1 198 ? 1.027   -30.086 29.743  1.00 86.79  ? 227 ILE B CD1 1 
ATOM   4982  N N   . GLY B 1 199 ? -0.740  -25.166 29.245  1.00 69.62  ? 228 GLY B N   1 
ATOM   4983  C CA  . GLY B 1 199 ? -1.014  -23.733 29.352  1.00 58.89  ? 228 GLY B CA  1 
ATOM   4984  C C   . GLY B 1 199 ? -2.463  -23.403 29.109  1.00 49.11  ? 228 GLY B C   1 
ATOM   4985  O O   . GLY B 1 199 ? -2.713  -22.542 28.264  1.00 48.49  ? 228 GLY B O   1 
ATOM   4986  N N   . ALA B 1 200 ? -3.392  -23.990 29.848  1.00 41.36  ? 229 ALA B N   1 
ATOM   4987  C CA  . ALA B 1 200 ? -4.783  -23.626 29.519  1.00 42.24  ? 229 ALA B CA  1 
ATOM   4988  C C   . ALA B 1 200 ? -5.291  -22.534 30.451  1.00 34.73  ? 229 ALA B C   1 
ATOM   4989  O O   . ALA B 1 200 ? -4.584  -22.171 31.396  1.00 36.39  ? 229 ALA B O   1 
ATOM   4990  C CB  . ALA B 1 200 ? -5.687  -24.831 29.534  1.00 43.26  ? 229 ALA B CB  1 
ATOM   4991  N N   . ILE B 1 201 ? -6.496  -22.045 30.168  1.00 35.75  ? 230 ILE B N   1 
ATOM   4992  C CA  . ILE B 1 201 ? -7.105  -21.025 30.975  1.00 32.60  ? 230 ILE B CA  1 
ATOM   4993  C C   . ILE B 1 201 ? -8.260  -21.685 31.719  1.00 31.07  ? 230 ILE B C   1 
ATOM   4994  O O   . ILE B 1 201 ? -9.100  -22.326 31.104  1.00 35.17  ? 230 ILE B O   1 
ATOM   4995  C CB  . ILE B 1 201 ? -7.521  -19.878 30.033  1.00 29.58  ? 230 ILE B CB  1 
ATOM   4996  C CG1 . ILE B 1 201 ? -6.319  -19.224 29.348  1.00 28.37  ? 230 ILE B CG1 1 
ATOM   4997  C CG2 . ILE B 1 201 ? -8.392  -18.858 30.738  1.00 28.40  ? 230 ILE B CG2 1 
ATOM   4998  C CD1 . ILE B 1 201 ? -5.285  -18.624 30.279  1.00 28.39  ? 230 ILE B CD1 1 
ATOM   4999  N N   . ASP B 1 202 ? -8.236  -21.593 33.049  1.00 30.19  ? 231 ASP B N   1 
ATOM   5000  C CA  . ASP B 1 202 ? -9.383  -21.916 33.879  1.00 31.84  ? 231 ASP B CA  1 
ATOM   5001  C C   . ASP B 1 202 ? -10.247 -20.661 33.956  1.00 30.41  ? 231 ASP B C   1 
ATOM   5002  O O   . ASP B 1 202 ? -9.766  -19.591 34.356  1.00 32.66  ? 231 ASP B O   1 
ATOM   5003  C CB  . ASP B 1 202 ? -8.927  -22.437 35.248  1.00 32.01  ? 231 ASP B CB  1 
ATOM   5004  C CG  . ASP B 1 202 ? -10.005 -22.980 36.175  1.00 35.72  ? 231 ASP B CG  1 
ATOM   5005  O OD1 . ASP B 1 202 ? -11.068 -22.323 36.319  1.00 39.39  ? 231 ASP B OD1 1 
ATOM   5006  O OD2 . ASP B 1 202 ? -9.759  -24.045 36.803  1.00 32.98  ? 231 ASP B OD2 1 
ATOM   5007  N N   . SER B 1 203 ? -11.530 -20.813 33.601  1.00 29.01  ? 232 SER B N   1 
ATOM   5008  C CA  . SER B 1 203 ? -12.432 -19.679 33.492  1.00 32.00  ? 232 SER B CA  1 
ATOM   5009  C C   . SER B 1 203 ? -12.818 -19.117 34.857  1.00 31.81  ? 232 SER B C   1 
ATOM   5010  O O   . SER B 1 203 ? -13.299 -17.989 34.934  1.00 33.18  ? 232 SER B O   1 
ATOM   5011  C CB  . SER B 1 203 ? -13.652 -20.043 32.681  1.00 33.85  ? 232 SER B CB  1 
ATOM   5012  O OG  . SER B 1 203 ? -14.337 -21.140 33.267  1.00 39.01  ? 232 SER B OG  1 
ATOM   5013  N N   . ASN B 1 204 ? -12.599 -19.882 35.932  1.00 33.63  ? 233 ASN B N   1 
ATOM   5014  C CA  . ASN B 1 204 ? -12.928 -19.422 37.276  1.00 37.73  ? 233 ASN B CA  1 
ATOM   5015  C C   . ASN B 1 204 ? -11.700 -18.978 38.075  1.00 34.78  ? 233 ASN B C   1 
ATOM   5016  O O   . ASN B 1 204 ? -11.831 -18.740 39.274  1.00 35.46  ? 233 ASN B O   1 
ATOM   5017  C CB  . ASN B 1 204 ? -13.654 -20.514 38.064  1.00 42.29  ? 233 ASN B CB  1 
ATOM   5018  C CG  . ASN B 1 204 ? -15.057 -20.750 37.563  1.00 41.63  ? 233 ASN B CG  1 
ATOM   5019  O OD1 . ASN B 1 204 ? -15.478 -21.897 37.424  1.00 49.64  ? 233 ASN B OD1 1 
ATOM   5020  N ND2 . ASN B 1 204 ? -15.779 -19.671 37.313  1.00 41.71  ? 233 ASN B ND2 1 
ATOM   5021  N N   . LEU B 1 205 ? -10.532 -18.864 37.424  1.00 29.08  ? 234 LEU B N   1 
ATOM   5022  C CA  . LEU B 1 205 ? -9.319  -18.408 38.082  1.00 29.86  ? 234 LEU B CA  1 
ATOM   5023  C C   . LEU B 1 205 ? -9.065  -16.959 37.685  1.00 27.28  ? 234 LEU B C   1 
ATOM   5024  O O   . LEU B 1 205 ? -9.540  -16.488 36.652  1.00 31.39  ? 234 LEU B O   1 
ATOM   5025  C CB  . LEU B 1 205 ? -8.110  -19.290 37.735  1.00 29.97  ? 234 LEU B CB  1 
ATOM   5026  C CG  . LEU B 1 205 ? -8.197  -20.736 38.240  1.00 29.75  ? 234 LEU B CG  1 
ATOM   5027  C CD1 . LEU B 1 205 ? -6.924  -21.522 37.938  1.00 33.88  ? 234 LEU B CD1 1 
ATOM   5028  C CD2 . LEU B 1 205 ? -8.503  -20.780 39.730  1.00 29.47  ? 234 LEU B CD2 1 
ATOM   5029  N N   . ASP B 1 206 ? -8.358  -16.274 38.581  1.00 27.25  ? 235 ASP B N   1 
ATOM   5030  C CA  . ASP B 1 206 ? -7.850  -14.939 38.326  1.00 24.44  ? 235 ASP B CA  1 
ATOM   5031  C C   . ASP B 1 206 ? -6.648  -15.041 37.381  1.00 23.76  ? 235 ASP B C   1 
ATOM   5032  O O   . ASP B 1 206 ? -6.030  -16.087 37.237  1.00 22.84  ? 235 ASP B O   1 
ATOM   5033  C CB  . ASP B 1 206 ? -7.544  -14.208 39.634  1.00 26.04  ? 235 ASP B CB  1 
ATOM   5034  C CG  . ASP B 1 206 ? -6.389  -14.804 40.418  1.00 26.02  ? 235 ASP B CG  1 
ATOM   5035  O OD1 . ASP B 1 206 ? -6.560  -15.898 40.975  1.00 24.39  ? 235 ASP B OD1 1 
ATOM   5036  O OD2 . ASP B 1 206 ? -5.325  -14.207 40.401  1.00 23.82  ? 235 ASP B OD2 1 
ATOM   5037  N N   . TRP B 1 207 ? -6.315  -13.890 36.783  1.00 19.94  ? 236 TRP B N   1 
ATOM   5038  C CA  . TRP B 1 207 ? -5.393  -13.704 35.666  1.00 18.34  ? 236 TRP B CA  1 
ATOM   5039  C C   . TRP B 1 207 ? -3.973  -14.154 36.030  1.00 19.60  ? 236 TRP B C   1 
ATOM   5040  O O   . TRP B 1 207 ? -3.313  -14.798 35.227  1.00 17.40  ? 236 TRP B O   1 
ATOM   5041  C CB  . TRP B 1 207 ? -5.435  -12.205 35.342  1.00 17.68  ? 236 TRP B CB  1 
ATOM   5042  C CG  . TRP B 1 207 ? -4.739  -11.688 34.123  1.00 19.78  ? 236 TRP B CG  1 
ATOM   5043  C CD1 . TRP B 1 207 ? -5.004  -11.967 32.815  1.00 21.37  ? 236 TRP B CD1 1 
ATOM   5044  C CD2 . TRP B 1 207 ? -3.746  -10.643 34.122  1.00 19.53  ? 236 TRP B CD2 1 
ATOM   5045  N NE1 . TRP B 1 207 ? -4.204  -11.204 32.002  1.00 23.59  ? 236 TRP B NE1 1 
ATOM   5046  C CE2 . TRP B 1 207 ? -3.431  -10.378 32.777  1.00 19.66  ? 236 TRP B CE2 1 
ATOM   5047  C CE3 . TRP B 1 207 ? -3.086  -9.923  35.128  1.00 22.09  ? 236 TRP B CE3 1 
ATOM   5048  C CZ2 . TRP B 1 207 ? -2.467  -9.436  32.426  1.00 20.72  ? 236 TRP B CZ2 1 
ATOM   5049  C CZ3 . TRP B 1 207 ? -2.134  -8.982  34.782  1.00 18.66  ? 236 TRP B CZ3 1 
ATOM   5050  C CH2 . TRP B 1 207 ? -1.844  -8.741  33.441  1.00 19.65  ? 236 TRP B CH2 1 
ATOM   5051  N N   . SER B 1 208 ? -3.550  -13.799 37.246  1.00 19.15  ? 237 SER B N   1 
ATOM   5052  C CA  . SER B 1 208 ? -2.225  -14.094 37.766  1.00 19.25  ? 237 SER B CA  1 
ATOM   5053  C C   . SER B 1 208 ? -2.046  -15.598 37.911  1.00 19.46  ? 237 SER B C   1 
ATOM   5054  O O   . SER B 1 208 ? -1.027  -16.128 37.493  1.00 25.26  ? 237 SER B O   1 
ATOM   5055  C CB  . SER B 1 208 ? -2.010  -13.398 39.046  1.00 20.92  ? 237 SER B CB  1 
ATOM   5056  O OG  . SER B 1 208 ? -2.126  -11.994 38.900  1.00 18.93  ? 237 SER B OG  1 
ATOM   5057  N N   . HIS B 1 209 ? -3.060  -16.278 38.458  1.00 21.77  ? 238 HIS B N   1 
ATOM   5058  C CA  . HIS B 1 209 ? -2.959  -17.714 38.743  1.00 22.05  ? 238 HIS B CA  1 
ATOM   5059  C C   . HIS B 1 209 ? -2.930  -18.509 37.433  1.00 24.52  ? 238 HIS B C   1 
ATOM   5060  O O   . HIS B 1 209 ? -2.107  -19.430 37.292  1.00 19.81  ? 238 HIS B O   1 
ATOM   5061  C CB  . HIS B 1 209 ? -4.026  -18.091 39.785  1.00 22.80  ? 238 HIS B CB  1 
ATOM   5062  C CG  . HIS B 1 209 ? -4.083  -19.520 40.210  1.00 23.27  ? 238 HIS B CG  1 
ATOM   5063  N ND1 . HIS B 1 209 ? -5.038  -19.968 41.091  1.00 26.60  ? 238 HIS B ND1 1 
ATOM   5064  C CD2 . HIS B 1 209 ? -3.355  -20.582 39.878  1.00 26.75  ? 238 HIS B CD2 1 
ATOM   5065  C CE1 . HIS B 1 209 ? -4.889  -21.279 41.267  1.00 26.34  ? 238 HIS B CE1 1 
ATOM   5066  N NE2 . HIS B 1 209 ? -3.877  -21.673 40.536  1.00 26.57  ? 238 HIS B NE2 1 
ATOM   5067  N N   . ASN B 1 210 ? -3.795  -18.125 36.460  1.00 24.51  ? 239 ASN B N   1 
ATOM   5068  C CA  . ASN B 1 210 ? -3.755  -18.660 35.104  1.00 23.71  ? 239 ASN B CA  1 
ATOM   5069  C C   . ASN B 1 210 ? -2.375  -18.460 34.481  1.00 23.69  ? 239 ASN B C   1 
ATOM   5070  O O   . ASN B 1 210 ? -1.881  -19.349 33.794  1.00 24.85  ? 239 ASN B O   1 
ATOM   5071  C CB  . ASN B 1 210 ? -4.856  -18.088 34.193  1.00 26.22  ? 239 ASN B CB  1 
ATOM   5072  C CG  . ASN B 1 210 ? -6.162  -18.847 34.294  1.00 27.71  ? 239 ASN B CG  1 
ATOM   5073  O OD1 . ASN B 1 210 ? -6.138  -20.071 34.428  1.00 28.40  ? 239 ASN B OD1 1 
ATOM   5074  N ND2 . ASN B 1 210 ? -7.290  -18.150 34.183  1.00 28.21  ? 239 ASN B ND2 1 
ATOM   5075  N N   . PHE B 1 211 ? -1.753  -17.302 34.744  1.00 23.02  ? 240 PHE B N   1 
ATOM   5076  C CA  . PHE B 1 211 ? -0.408  -17.043 34.262  1.00 22.13  ? 240 PHE B CA  1 
ATOM   5077  C C   . PHE B 1 211 ? 0.579   -18.037 34.878  1.00 21.94  ? 240 PHE B C   1 
ATOM   5078  O O   . PHE B 1 211 ? 1.376   -18.585 34.148  1.00 21.22  ? 240 PHE B O   1 
ATOM   5079  C CB  . PHE B 1 211 ? -0.063  -15.573 34.506  1.00 23.21  ? 240 PHE B CB  1 
ATOM   5080  C CG  . PHE B 1 211 ? 1.207   -15.073 33.881  1.00 23.26  ? 240 PHE B CG  1 
ATOM   5081  C CD1 . PHE B 1 211 ? 1.821   -15.734 32.833  1.00 24.09  ? 240 PHE B CD1 1 
ATOM   5082  C CD2 . PHE B 1 211 ? 1.775   -13.900 34.349  1.00 27.03  ? 240 PHE B CD2 1 
ATOM   5083  C CE1 . PHE B 1 211 ? 2.980   -15.239 32.262  1.00 23.56  ? 240 PHE B CE1 1 
ATOM   5084  C CE2 . PHE B 1 211 ? 2.957   -13.424 33.811  1.00 25.35  ? 240 PHE B CE2 1 
ATOM   5085  C CZ  . PHE B 1 211 ? 3.549   -14.090 32.754  1.00 25.18  ? 240 PHE B CZ  1 
ATOM   5086  N N   . THR B 1 212 ? 0.513   -18.271 36.197  1.00 21.69  ? 241 THR B N   1 
ATOM   5087  C CA  . THR B 1 212 ? 1.542   -19.061 36.866  1.00 24.29  ? 241 THR B CA  1 
ATOM   5088  C C   . THR B 1 212 ? 1.317   -20.523 36.496  1.00 26.24  ? 241 THR B C   1 
ATOM   5089  O O   . THR B 1 212 ? 2.285   -21.274 36.369  1.00 25.50  ? 241 THR B O   1 
ATOM   5090  C CB  . THR B 1 212 ? 1.614   -18.839 38.390  1.00 24.03  ? 241 THR B CB  1 
ATOM   5091  O OG1 . THR B 1 212 ? 0.350   -19.086 39.005  1.00 24.23  ? 241 THR B OG1 1 
ATOM   5092  C CG2 . THR B 1 212 ? 2.058   -17.441 38.776  1.00 26.12  ? 241 THR B CG2 1 
ATOM   5093  N N   . ASN B 1 213 ? 0.046   -20.901 36.251  1.00 27.44  ? 242 ASN B N   1 
ATOM   5094  C CA  . ASN B 1 213 ? -0.261  -22.258 35.806  1.00 26.17  ? 242 ASN B CA  1 
ATOM   5095  C C   . ASN B 1 213 ? 0.412   -22.537 34.462  1.00 24.94  ? 242 ASN B C   1 
ATOM   5096  O O   . ASN B 1 213 ? 0.978   -23.601 34.247  1.00 26.65  ? 242 ASN B O   1 
ATOM   5097  C CB  . ASN B 1 213 ? -1.764  -22.544 35.703  1.00 26.65  ? 242 ASN B CB  1 
ATOM   5098  C CG  . ASN B 1 213 ? -2.478  -22.912 36.995  1.00 24.68  ? 242 ASN B CG  1 
ATOM   5099  O OD1 . ASN B 1 213 ? -1.891  -23.079 38.051  1.00 28.15  ? 242 ASN B OD1 1 
ATOM   5100  N ND2 . ASN B 1 213 ? -3.787  -23.045 36.924  1.00 27.68  ? 242 ASN B ND2 1 
ATOM   5101  N N   . MET B 1 214 ? 0.339   -21.577 33.539  1.00 25.44  ? 243 MET B N   1 
ATOM   5102  C CA  . MET B 1 214 ? 0.889   -21.724 32.201  1.00 24.04  ? 243 MET B CA  1 
ATOM   5103  C C   . MET B 1 214 ? 2.416   -21.658 32.221  1.00 25.65  ? 243 MET B C   1 
ATOM   5104  O O   . MET B 1 214 ? 3.053   -22.103 31.270  1.00 27.11  ? 243 MET B O   1 
ATOM   5105  C CB  . MET B 1 214 ? 0.352   -20.619 31.287  1.00 24.50  ? 243 MET B CB  1 
ATOM   5106  C CG  . MET B 1 214 ? -1.121  -20.804 31.012  1.00 25.72  ? 243 MET B CG  1 
ATOM   5107  S SD  . MET B 1 214 ? -1.704  -19.830 29.628  1.00 28.17  ? 243 MET B SD  1 
ATOM   5108  C CE  . MET B 1 214 ? -1.205  -18.195 30.174  1.00 27.67  ? 243 MET B CE  1 
ATOM   5109  N N   . LEU B 1 215 ? 2.988   -21.041 33.264  1.00 23.84  ? 244 LEU B N   1 
ATOM   5110  C CA  . LEU B 1 215 ? 4.435   -20.954 33.387  1.00 24.81  ? 244 LEU B CA  1 
ATOM   5111  C C   . LEU B 1 215 ? 4.991   -22.265 33.927  1.00 26.73  ? 244 LEU B C   1 
ATOM   5112  O O   . LEU B 1 215 ? 6.203   -22.486 33.882  1.00 29.64  ? 244 LEU B O   1 
ATOM   5113  C CB  . LEU B 1 215 ? 4.792   -19.798 34.311  1.00 24.68  ? 244 LEU B CB  1 
ATOM   5114  C CG  . LEU B 1 215 ? 4.610   -18.399 33.726  1.00 24.61  ? 244 LEU B CG  1 
ATOM   5115  C CD1 . LEU B 1 215 ? 4.845   -17.350 34.794  1.00 24.47  ? 244 LEU B CD1 1 
ATOM   5116  C CD2 . LEU B 1 215 ? 5.544   -18.152 32.549  1.00 22.54  ? 244 LEU B CD2 1 
ATOM   5117  N N   . GLY B 1 216 ? 4.110   -23.089 34.491  1.00 30.11  ? 245 GLY B N   1 
ATOM   5118  C CA  . GLY B 1 216 ? 4.482   -24.394 35.015  1.00 30.48  ? 245 GLY B CA  1 
ATOM   5119  C C   . GLY B 1 216 ? 4.826   -24.394 36.503  1.00 31.35  ? 245 GLY B C   1 
ATOM   5120  O O   . GLY B 1 216 ? 5.476   -25.318 36.959  1.00 30.32  ? 245 GLY B O   1 
ATOM   5121  N N   . TYR B 1 217 ? 4.349   -23.406 37.263  1.00 28.36  ? 246 TYR B N   1 
ATOM   5122  C CA  . TYR B 1 217 ? 4.631   -23.298 38.690  1.00 25.47  ? 246 TYR B CA  1 
ATOM   5123  C C   . TYR B 1 217 ? 3.403   -23.757 39.479  1.00 27.44  ? 246 TYR B C   1 
ATOM   5124  O O   . TYR B 1 217 ? 2.285   -23.681 38.982  1.00 32.72  ? 246 TYR B O   1 
ATOM   5125  C CB  . TYR B 1 217 ? 5.044   -21.863 39.043  1.00 24.34  ? 246 TYR B CB  1 
ATOM   5126  C CG  . TYR B 1 217 ? 6.416   -21.475 38.528  1.00 23.53  ? 246 TYR B CG  1 
ATOM   5127  C CD1 . TYR B 1 217 ? 6.656   -21.311 37.166  1.00 23.10  ? 246 TYR B CD1 1 
ATOM   5128  C CD2 . TYR B 1 217 ? 7.497   -21.339 39.381  1.00 22.92  ? 246 TYR B CD2 1 
ATOM   5129  C CE1 . TYR B 1 217 ? 7.923   -21.035 36.677  1.00 22.11  ? 246 TYR B CE1 1 
ATOM   5130  C CE2 . TYR B 1 217 ? 8.772   -21.059 38.911  1.00 24.29  ? 246 TYR B CE2 1 
ATOM   5131  C CZ  . TYR B 1 217 ? 8.984   -20.902 37.550  1.00 23.71  ? 246 TYR B CZ  1 
ATOM   5132  O OH  . TYR B 1 217 ? 10.229  -20.593 37.073  1.00 24.89  ? 246 TYR B OH  1 
ATOM   5133  N N   . THR B 1 218 ? 3.601   -24.185 40.728  1.00 28.50  ? 247 THR B N   1 
ATOM   5134  C CA  . THR B 1 218 ? 2.497   -24.711 41.515  1.00 31.57  ? 247 THR B CA  1 
ATOM   5135  C C   . THR B 1 218 ? 2.409   -24.049 42.889  1.00 35.20  ? 247 THR B C   1 
ATOM   5136  O O   . THR B 1 218 ? 1.330   -24.023 43.482  1.00 38.85  ? 247 THR B O   1 
ATOM   5137  C CB  . THR B 1 218 ? 2.598   -26.240 41.598  1.00 29.92  ? 247 THR B CB  1 
ATOM   5138  O OG1 . THR B 1 218 ? 3.956   -26.581 41.882  1.00 34.87  ? 247 THR B OG1 1 
ATOM   5139  C CG2 . THR B 1 218 ? 2.175   -26.920 40.314  1.00 29.79  ? 247 THR B CG2 1 
ATOM   5140  N N   . ASP B 1 219 ? 3.528   -23.524 43.391  1.00 31.41  ? 248 ASP B N   1 
ATOM   5141  C CA  . ASP B 1 219 ? 3.598   -22.940 44.720  1.00 31.73  ? 248 ASP B CA  1 
ATOM   5142  C C   . ASP B 1 219 ? 2.595   -21.801 44.864  1.00 32.42  ? 248 ASP B C   1 
ATOM   5143  O O   . ASP B 1 219 ? 2.650   -20.838 44.104  1.00 29.13  ? 248 ASP B O   1 
ATOM   5144  C CB  . ASP B 1 219 ? 4.995   -22.387 44.991  1.00 33.56  ? 248 ASP B CB  1 
ATOM   5145  C CG  . ASP B 1 219 ? 5.218   -21.996 46.437  1.00 33.82  ? 248 ASP B CG  1 
ATOM   5146  O OD1 . ASP B 1 219 ? 4.258   -21.482 47.060  1.00 36.25  ? 248 ASP B OD1 1 
ATOM   5147  O OD2 . ASP B 1 219 ? 6.360   -22.207 46.929  1.00 34.90  ? 248 ASP B OD2 1 
ATOM   5148  N N   . HIS B 1 220 ? 1.738   -21.882 45.894  1.00 30.61  ? 249 HIS B N   1 
ATOM   5149  C CA  . HIS B 1 220 ? 0.733   -20.866 46.152  1.00 28.87  ? 249 HIS B CA  1 
ATOM   5150  C C   . HIS B 1 220 ? 1.367   -19.502 46.387  1.00 29.15  ? 249 HIS B C   1 
ATOM   5151  O O   . HIS B 1 220 ? 0.732   -18.493 46.082  1.00 27.65  ? 249 HIS B O   1 
ATOM   5152  C CB  . HIS B 1 220 ? -0.155  -21.237 47.350  1.00 32.88  ? 249 HIS B CB  1 
ATOM   5153  C CG  . HIS B 1 220 ? -0.966  -20.128 47.945  1.00 33.93  ? 249 HIS B CG  1 
ATOM   5154  N ND1 . HIS B 1 220 ? -0.555  -19.505 49.104  1.00 34.06  ? 249 HIS B ND1 1 
ATOM   5155  C CD2 . HIS B 1 220 ? -2.138  -19.536 47.616  1.00 35.84  ? 249 HIS B CD2 1 
ATOM   5156  C CE1 . HIS B 1 220 ? -1.435  -18.560 49.454  1.00 35.21  ? 249 HIS B CE1 1 
ATOM   5157  N NE2 . HIS B 1 220 ? -2.414  -18.575 48.582  1.00 35.27  ? 249 HIS B NE2 1 
ATOM   5158  N N   . GLN B 1 221 ? 2.593   -19.464 46.935  1.00 28.02  ? 250 GLN B N   1 
ATOM   5159  C CA  . GLN B 1 221 ? 3.195   -18.189 47.288  1.00 30.06  ? 250 GLN B CA  1 
ATOM   5160  C C   . GLN B 1 221 ? 3.863   -17.533 46.079  1.00 25.48  ? 250 GLN B C   1 
ATOM   5161  O O   . GLN B 1 221 ? 4.103   -16.322 46.110  1.00 24.06  ? 250 GLN B O   1 
ATOM   5162  C CB  . GLN B 1 221 ? 4.144   -18.365 48.471  1.00 33.52  ? 250 GLN B CB  1 
ATOM   5163  C CG  . GLN B 1 221 ? 3.401   -18.729 49.751  1.00 36.67  ? 250 GLN B CG  1 
ATOM   5164  C CD  . GLN B 1 221 ? 2.460   -17.650 50.249  1.00 40.79  ? 250 GLN B CD  1 
ATOM   5165  O OE1 . GLN B 1 221 ? 2.529   -16.477 49.869  1.00 36.13  ? 250 GLN B OE1 1 
ATOM   5166  N NE2 . GLN B 1 221 ? 1.581   -18.039 51.160  1.00 39.33  ? 250 GLN B NE2 1 
ATOM   5167  N N   . PHE B 1 222 ? 4.171   -18.317 45.038  1.00 22.96  ? 251 PHE B N   1 
ATOM   5168  C CA  . PHE B 1 222 ? 4.620   -17.760 43.759  1.00 23.48  ? 251 PHE B CA  1 
ATOM   5169  C C   . PHE B 1 222 ? 3.469   -17.033 43.067  1.00 20.93  ? 251 PHE B C   1 
ATOM   5170  O O   . PHE B 1 222 ? 3.636   -15.946 42.522  1.00 24.52  ? 251 PHE B O   1 
ATOM   5171  C CB  . PHE B 1 222 ? 5.168   -18.838 42.820  1.00 22.67  ? 251 PHE B CB  1 
ATOM   5172  C CG  . PHE B 1 222 ? 5.661   -18.290 41.502  1.00 22.79  ? 251 PHE B CG  1 
ATOM   5173  C CD1 . PHE B 1 222 ? 6.707   -17.378 41.480  1.00 23.65  ? 251 PHE B CD1 1 
ATOM   5174  C CD2 . PHE B 1 222 ? 5.086   -18.661 40.305  1.00 21.81  ? 251 PHE B CD2 1 
ATOM   5175  C CE1 . PHE B 1 222 ? 7.161   -16.853 40.280  1.00 23.30  ? 251 PHE B CE1 1 
ATOM   5176  C CE2 . PHE B 1 222 ? 5.555   -18.149 39.102  1.00 25.30  ? 251 PHE B CE2 1 
ATOM   5177  C CZ  . PHE B 1 222 ? 6.588   -17.242 39.092  1.00 22.69  ? 251 PHE B CZ  1 
ATOM   5178  N N   . THR B 1 223 ? 2.283   -17.607 43.166  1.00 21.93  ? 252 THR B N   1 
ATOM   5179  C CA  . THR B 1 223 ? 1.098   -17.023 42.579  1.00 21.55  ? 252 THR B CA  1 
ATOM   5180  C C   . THR B 1 223 ? 0.772   -15.715 43.288  1.00 20.40  ? 252 THR B C   1 
ATOM   5181  O O   . THR B 1 223 ? 0.420   -14.752 42.628  1.00 24.29  ? 252 THR B O   1 
ATOM   5182  C CB  . THR B 1 223 ? -0.083  -17.993 42.606  1.00 23.63  ? 252 THR B CB  1 
ATOM   5183  O OG1 . THR B 1 223 ? 0.217   -19.178 41.860  1.00 20.60  ? 252 THR B OG1 1 
ATOM   5184  C CG2 . THR B 1 223 ? -1.323  -17.327 42.064  1.00 24.26  ? 252 THR B CG2 1 
ATOM   5185  N N   . GLU B 1 224 ? 0.864   -15.700 44.617  1.00 20.33  ? 253 GLU B N   1 
ATOM   5186  C CA  . GLU B 1 224 ? 0.710   -14.484 45.397  1.00 22.91  ? 253 GLU B CA  1 
ATOM   5187  C C   . GLU B 1 224 ? 1.788   -13.461 45.045  1.00 21.40  ? 253 GLU B C   1 
ATOM   5188  O O   . GLU B 1 224 ? 1.516   -12.263 45.006  1.00 22.02  ? 253 GLU B O   1 
ATOM   5189  C CB  . GLU B 1 224 ? 0.726   -14.843 46.889  1.00 25.02  ? 253 GLU B CB  1 
ATOM   5190  C CG  . GLU B 1 224 ? -0.562  -15.517 47.336  1.00 26.35  ? 253 GLU B CG  1 
ATOM   5191  C CD  . GLU B 1 224 ? -1.643  -14.501 47.631  1.00 26.49  ? 253 GLU B CD  1 
ATOM   5192  O OE1 . GLU B 1 224 ? -1.503  -13.784 48.633  1.00 25.60  ? 253 GLU B OE1 1 
ATOM   5193  O OE2 . GLU B 1 224 ? -2.592  -14.402 46.851  1.00 31.58  ? 253 GLU B OE2 1 
ATOM   5194  N N   . LEU B 1 225 ? 3.031   -13.899 44.857  1.00 22.61  ? 254 LEU B N   1 
ATOM   5195  C CA  . LEU B 1 225 ? 4.079   -12.978 44.451  1.00 23.24  ? 254 LEU B CA  1 
ATOM   5196  C C   . LEU B 1 225 ? 3.690   -12.360 43.105  1.00 21.71  ? 254 LEU B C   1 
ATOM   5197  O O   . LEU B 1 225 ? 3.813   -11.151 42.901  1.00 21.31  ? 254 LEU B O   1 
ATOM   5198  C CB  . LEU B 1 225 ? 5.431   -13.704 44.342  1.00 22.80  ? 254 LEU B CB  1 
ATOM   5199  C CG  . LEU B 1 225 ? 6.586   -12.882 43.759  1.00 24.05  ? 254 LEU B CG  1 
ATOM   5200  C CD1 . LEU B 1 225 ? 6.944   -11.671 44.626  1.00 25.66  ? 254 LEU B CD1 1 
ATOM   5201  C CD2 . LEU B 1 225 ? 7.806   -13.764 43.566  1.00 25.80  ? 254 LEU B CD2 1 
ATOM   5202  N N   . THR B 1 226 ? 3.219   -13.210 42.203  1.00 20.56  ? 255 THR B N   1 
ATOM   5203  C CA  . THR B 1 226 ? 2.874   -12.806 40.852  1.00 20.15  ? 255 THR B CA  1 
ATOM   5204  C C   . THR B 1 226 ? 1.759   -11.757 40.933  1.00 22.59  ? 255 THR B C   1 
ATOM   5205  O O   . THR B 1 226 ? 1.849   -10.754 40.234  1.00 20.35  ? 255 THR B O   1 
ATOM   5206  C CB  . THR B 1 226 ? 2.570   -14.039 40.000  1.00 22.14  ? 255 THR B CB  1 
ATOM   5207  O OG1 . THR B 1 226 ? 3.768   -14.831 39.989  1.00 20.71  ? 255 THR B OG1 1 
ATOM   5208  C CG2 . THR B 1 226 ? 2.134   -13.692 38.598  1.00 21.07  ? 255 THR B CG2 1 
ATOM   5209  N N   . ARG B 1 227 ? 0.781   -11.950 41.846  1.00 23.42  ? 256 ARG B N   1 
ATOM   5210  C CA  . ARG B 1 227 ? -0.370  -11.051 41.923  1.00 21.92  ? 256 ARG B CA  1 
ATOM   5211  C C   . ARG B 1 227 ? 0.138   -9.676  42.343  1.00 24.21  ? 256 ARG B C   1 
ATOM   5212  O O   . ARG B 1 227 ? -0.161  -8.666  41.705  1.00 24.92  ? 256 ARG B O   1 
ATOM   5213  C CB  . ARG B 1 227 ? -1.418  -11.544 42.936  1.00 23.31  ? 256 ARG B CB  1 
ATOM   5214  C CG  . ARG B 1 227 ? -2.238  -12.743 42.492  1.00 21.83  ? 256 ARG B CG  1 
ATOM   5215  C CD  . ARG B 1 227 ? -2.985  -13.439 43.636  1.00 22.39  ? 256 ARG B CD  1 
ATOM   5216  N NE  . ARG B 1 227 ? -3.696  -14.596 43.098  1.00 20.69  ? 256 ARG B NE  1 
ATOM   5217  C CZ  . ARG B 1 227 ? -3.869  -15.767 43.718  1.00 28.58  ? 256 ARG B CZ  1 
ATOM   5218  N NH1 . ARG B 1 227 ? -3.384  -15.968 44.924  1.00 28.82  ? 256 ARG B NH1 1 
ATOM   5219  N NH2 . ARG B 1 227 ? -4.496  -16.756 43.101  1.00 28.42  ? 256 ARG B NH2 1 
ATOM   5220  N N   . LEU B 1 228 ? 0.956   -9.661  43.407  1.00 23.61  ? 257 LEU B N   1 
ATOM   5221  C CA  . LEU B 1 228 ? 1.569   -8.435  43.889  1.00 23.69  ? 257 LEU B CA  1 
ATOM   5222  C C   . LEU B 1 228 ? 2.448   -7.826  42.800  1.00 20.84  ? 257 LEU B C   1 
ATOM   5223  O O   . LEU B 1 228 ? 2.405   -6.616  42.596  1.00 20.66  ? 257 LEU B O   1 
ATOM   5224  C CB  . LEU B 1 228 ? 2.407   -8.742  45.138  1.00 23.91  ? 257 LEU B CB  1 
ATOM   5225  C CG  . LEU B 1 228 ? 3.104   -7.547  45.774  1.00 24.95  ? 257 LEU B CG  1 
ATOM   5226  C CD1 . LEU B 1 228 ? 2.080   -6.555  46.329  1.00 26.66  ? 257 LEU B CD1 1 
ATOM   5227  C CD2 . LEU B 1 228 ? 4.053   -8.020  46.872  1.00 26.14  ? 257 LEU B CD2 1 
ATOM   5228  N N   . TYR B 1 229 ? 3.343   -8.640  42.217  1.00 18.58  ? 258 TYR B N   1 
ATOM   5229  C CA  . TYR B 1 229 ? 4.267   -8.168  41.181  1.00 19.47  ? 258 TYR B CA  1 
ATOM   5230  C C   . TYR B 1 229 ? 3.490   -7.419  40.094  1.00 21.41  ? 258 TYR B C   1 
ATOM   5231  O O   . TYR B 1 229 ? 3.823   -6.273  39.760  1.00 19.94  ? 258 TYR B O   1 
ATOM   5232  C CB  . TYR B 1 229 ? 5.087   -9.348  40.631  1.00 19.01  ? 258 TYR B CB  1 
ATOM   5233  C CG  . TYR B 1 229 ? 6.182   -9.000  39.653  1.00 20.82  ? 258 TYR B CG  1 
ATOM   5234  C CD1 . TYR B 1 229 ? 5.904   -8.384  38.448  1.00 21.78  ? 258 TYR B CD1 1 
ATOM   5235  C CD2 . TYR B 1 229 ? 7.511   -9.281  39.930  1.00 23.70  ? 258 TYR B CD2 1 
ATOM   5236  C CE1 . TYR B 1 229 ? 6.896   -8.077  37.535  1.00 22.12  ? 258 TYR B CE1 1 
ATOM   5237  C CE2 . TYR B 1 229 ? 8.519   -9.000  39.020  1.00 23.27  ? 258 TYR B CE2 1 
ATOM   5238  C CZ  . TYR B 1 229 ? 8.211   -8.388  37.820  1.00 23.46  ? 258 TYR B CZ  1 
ATOM   5239  O OH  . TYR B 1 229 ? 9.232   -8.093  36.962  1.00 25.33  ? 258 TYR B OH  1 
ATOM   5240  N N   . LEU B 1 230 ? 2.401   -8.021  39.595  1.00 19.42  ? 259 LEU B N   1 
ATOM   5241  C CA  . LEU B 1 230 ? 1.687   -7.457  38.459  1.00 20.11  ? 259 LEU B CA  1 
ATOM   5242  C C   . LEU B 1 230 ? 0.911   -6.214  38.901  1.00 20.64  ? 259 LEU B C   1 
ATOM   5243  O O   . LEU B 1 230 ? 0.662   -5.335  38.084  1.00 21.04  ? 259 LEU B O   1 
ATOM   5244  C CB  . LEU B 1 230 ? 0.772   -8.517  37.821  1.00 20.51  ? 259 LEU B CB  1 
ATOM   5245  C CG  . LEU B 1 230 ? 1.477   -9.712  37.180  1.00 20.12  ? 259 LEU B CG  1 
ATOM   5246  C CD1 . LEU B 1 230 ? 0.478   -10.758 36.754  1.00 19.63  ? 259 LEU B CD1 1 
ATOM   5247  C CD2 . LEU B 1 230 ? 2.337   -9.349  35.977  1.00 20.92  ? 259 LEU B CD2 1 
ATOM   5248  N N   . THR B 1 231 ? 0.473   -6.184  40.174  1.00 19.14  ? 260 THR B N   1 
ATOM   5249  C CA  . THR B 1 231 ? -0.253  -5.045  40.708  1.00 19.79  ? 260 THR B CA  1 
ATOM   5250  C C   . THR B 1 231 ? 0.693   -3.850  40.797  1.00 20.27  ? 260 THR B C   1 
ATOM   5251  O O   . THR B 1 231 ? 0.302   -2.754  40.399  1.00 19.31  ? 260 THR B O   1 
ATOM   5252  C CB  . THR B 1 231 ? -0.904  -5.362  42.066  1.00 18.85  ? 260 THR B CB  1 
ATOM   5253  O OG1 . THR B 1 231 ? -2.001  -6.254  41.867  1.00 21.02  ? 260 THR B OG1 1 
ATOM   5254  C CG2 . THR B 1 231 ? -1.379  -4.133  42.792  1.00 20.19  ? 260 THR B CG2 1 
ATOM   5255  N N   . ILE B 1 232 ? 1.893   -4.032  41.390  1.00 18.15  ? 261 ILE B N   1 
ATOM   5256  C CA  . ILE B 1 232 ? 2.739   -2.881  41.697  1.00 19.37  ? 261 ILE B CA  1 
ATOM   5257  C C   . ILE B 1 232 ? 3.502   -2.375  40.478  1.00 17.55  ? 261 ILE B C   1 
ATOM   5258  O O   . ILE B 1 232 ? 3.920   -1.225  40.460  1.00 18.27  ? 261 ILE B O   1 
ATOM   5259  C CB  . ILE B 1 232 ? 3.700   -3.156  42.870  1.00 21.69  ? 261 ILE B CB  1 
ATOM   5260  C CG1 . ILE B 1 232 ? 4.719   -4.232  42.491  1.00 22.50  ? 261 ILE B CG1 1 
ATOM   5261  C CG2 . ILE B 1 232 ? 2.923   -3.500  44.131  1.00 22.80  ? 261 ILE B CG2 1 
ATOM   5262  C CD1 . ILE B 1 232 ? 5.387   -4.880  43.664  1.00 25.00  ? 261 ILE B CD1 1 
ATOM   5263  N N   . HIS B 1 233 ? 3.702   -3.203  39.471  1.00 17.79  ? 262 HIS B N   1 
ATOM   5264  C CA  . HIS B 1 233 ? 4.421   -2.761  38.283  1.00 20.04  ? 262 HIS B CA  1 
ATOM   5265  C C   . HIS B 1 233 ? 3.506   -2.044  37.283  1.00 20.22  ? 262 HIS B C   1 
ATOM   5266  O O   . HIS B 1 233 ? 3.961   -1.666  36.189  1.00 19.69  ? 262 HIS B O   1 
ATOM   5267  C CB  . HIS B 1 233 ? 5.153   -3.955  37.670  1.00 20.67  ? 262 HIS B CB  1 
ATOM   5268  C CG  . HIS B 1 233 ? 6.381   -4.344  38.409  1.00 22.20  ? 262 HIS B CG  1 
ATOM   5269  N ND1 . HIS B 1 233 ? 6.316   -5.015  39.613  1.00 22.54  ? 262 HIS B ND1 1 
ATOM   5270  C CD2 . HIS B 1 233 ? 7.689   -4.193  38.117  1.00 22.17  ? 262 HIS B CD2 1 
ATOM   5271  C CE1 . HIS B 1 233 ? 7.552   -5.245  40.032  1.00 26.74  ? 262 HIS B CE1 1 
ATOM   5272  N NE2 . HIS B 1 233 ? 8.410   -4.772  39.135  1.00 23.12  ? 262 HIS B NE2 1 
ATOM   5273  N N   . SER B 1 234 ? 2.216   -1.876  37.642  1.00 21.13  ? 263 SER B N   1 
ATOM   5274  C CA  . SER B 1 234 ? 1.167   -1.680  36.658  1.00 19.27  ? 263 SER B CA  1 
ATOM   5275  C C   . SER B 1 234 ? 1.298   -0.335  35.966  1.00 18.64  ? 263 SER B C   1 
ATOM   5276  O O   . SER B 1 234 ? 1.014   -0.232  34.774  1.00 15.95  ? 263 SER B O   1 
ATOM   5277  C CB  . SER B 1 234 ? -0.178  -1.800  37.278  1.00 19.74  ? 263 SER B CB  1 
ATOM   5278  O OG  . SER B 1 234 ? -0.262  -0.991  38.443  1.00 20.72  ? 263 SER B OG  1 
ATOM   5279  N N   . ASP B 1 235 ? 1.648   0.685   36.758  1.00 18.09  ? 264 ASP B N   1 
ATOM   5280  C CA  . ASP B 1 235 ? 1.654   2.059   36.290  1.00 19.83  ? 264 ASP B CA  1 
ATOM   5281  C C   . ASP B 1 235 ? 2.583   2.887   37.173  1.00 19.65  ? 264 ASP B C   1 
ATOM   5282  O O   . ASP B 1 235 ? 2.715   2.579   38.347  1.00 20.61  ? 264 ASP B O   1 
ATOM   5283  C CB  . ASP B 1 235 ? 0.200   2.561   36.326  1.00 19.79  ? 264 ASP B CB  1 
ATOM   5284  C CG  . ASP B 1 235 ? -0.115  3.638   35.311  1.00 19.77  ? 264 ASP B CG  1 
ATOM   5285  O OD1 . ASP B 1 235 ? 0.341   3.519   34.152  1.00 19.41  ? 264 ASP B OD1 1 
ATOM   5286  O OD2 . ASP B 1 235 ? -0.894  4.578   35.660  1.00 23.52  ? 264 ASP B OD2 1 
ATOM   5287  N N   . HIS B 1 236 ? 3.230   3.895   36.595  1.00 18.81  ? 265 HIS B N   1 
ATOM   5288  C CA  . HIS B 1 236 ? 4.166   4.770   37.335  1.00 19.88  ? 265 HIS B CA  1 
ATOM   5289  C C   . HIS B 1 236 ? 4.121   6.131   36.654  1.00 19.41  ? 265 HIS B C   1 
ATOM   5290  O O   . HIS B 1 236 ? 5.168   6.616   36.202  1.00 18.37  ? 265 HIS B O   1 
ATOM   5291  C CB  . HIS B 1 236 ? 5.576   4.179   37.390  1.00 19.92  ? 265 HIS B CB  1 
ATOM   5292  C CG  . HIS B 1 236 ? 6.351   4.543   38.598  1.00 21.01  ? 265 HIS B CG  1 
ATOM   5293  N ND1 . HIS B 1 236 ? 5.864   4.366   39.870  1.00 23.44  ? 265 HIS B ND1 1 
ATOM   5294  C CD2 . HIS B 1 236 ? 7.565   5.067   38.736  1.00 20.22  ? 265 HIS B CD2 1 
ATOM   5295  C CE1 . HIS B 1 236 ? 6.775   4.776   40.732  1.00 21.74  ? 265 HIS B CE1 1 
ATOM   5296  N NE2 . HIS B 1 236 ? 7.814   5.205   40.069  1.00 23.60  ? 265 HIS B NE2 1 
ATOM   5297  N N   . GLU B 1 237 ? 2.912   6.673   36.553  1.00 17.78  ? 266 GLU B N   1 
ATOM   5298  C CA  . GLU B 1 237 ? 2.700   7.990   35.894  1.00 18.26  ? 266 GLU B CA  1 
ATOM   5299  C C   . GLU B 1 237 ? 3.041   7.899   34.383  1.00 17.88  ? 266 GLU B C   1 
ATOM   5300  O O   . GLU B 1 237 ? 3.289   6.797   33.882  1.00 19.59  ? 266 GLU B O   1 
ATOM   5301  C CB  . GLU B 1 237 ? 3.278   9.120   36.762  1.00 17.89  ? 266 GLU B CB  1 
ATOM   5302  C CG  . GLU B 1 237 ? 4.640   9.679   36.372  1.00 19.45  ? 266 GLU B CG  1 
ATOM   5303  C CD  . GLU B 1 237 ? 4.769   11.100  36.891  1.00 21.04  ? 266 GLU B CD  1 
ATOM   5304  O OE1 . GLU B 1 237 ? 4.100   11.435  37.887  1.00 21.46  ? 266 GLU B OE1 1 
ATOM   5305  O OE2 . GLU B 1 237 ? 5.536   11.865  36.295  1.00 19.65  ? 266 GLU B OE2 1 
ATOM   5306  N N   . GLY B 1 238 ? 2.969   9.020   33.677  1.00 18.69  ? 267 GLY B N   1 
ATOM   5307  C CA  . GLY B 1 238 ? 3.098   8.947   32.206  1.00 19.42  ? 267 GLY B CA  1 
ATOM   5308  C C   . GLY B 1 238 ? 4.450   9.298   31.661  1.00 16.48  ? 267 GLY B C   1 
ATOM   5309  O O   . GLY B 1 238 ? 4.642   9.142   30.464  1.00 17.45  ? 267 GLY B O   1 
ATOM   5310  N N   . GLY B 1 239 ? 5.333   9.758   32.529  1.00 21.00  ? 268 GLY B N   1 
ATOM   5311  C CA  . GLY B 1 239 ? 6.628   10.233  32.078  1.00 18.03  ? 268 GLY B CA  1 
ATOM   5312  C C   . GLY B 1 239 ? 7.738   9.182   32.082  1.00 17.48  ? 268 GLY B C   1 
ATOM   5313  O O   . GLY B 1 239 ? 8.843   9.466   31.670  1.00 16.74  ? 268 GLY B O   1 
ATOM   5314  N N   . ASN B 1 240 ? 7.452   7.957   32.513  1.00 17.44  ? 269 ASN B N   1 
ATOM   5315  C CA  . ASN B 1 240 ? 8.420   6.886   32.343  1.00 18.65  ? 269 ASN B CA  1 
ATOM   5316  C C   . ASN B 1 240 ? 8.454   6.439   30.872  1.00 19.12  ? 269 ASN B C   1 
ATOM   5317  O O   . ASN B 1 240 ? 7.489   6.637   30.121  1.00 14.83  ? 269 ASN B O   1 
ATOM   5318  C CB  . ASN B 1 240 ? 8.117   5.687   33.243  1.00 17.96  ? 269 ASN B CB  1 
ATOM   5319  C CG  . ASN B 1 240 ? 6.831   4.964   32.920  1.00 18.68  ? 269 ASN B CG  1 
ATOM   5320  O OD1 . ASN B 1 240 ? 6.798   4.109   32.047  1.00 18.42  ? 269 ASN B OD1 1 
ATOM   5321  N ND2 . ASN B 1 240 ? 5.793   5.205   33.696  1.00 17.97  ? 269 ASN B ND2 1 
ATOM   5322  N N   . VAL B 1 241 ? 9.596   5.857   30.459  1.00 17.25  ? 270 VAL B N   1 
ATOM   5323  C CA  . VAL B 1 241 ? 9.823   5.627   29.042  1.00 16.13  ? 270 VAL B CA  1 
ATOM   5324  C C   . VAL B 1 241 ? 8.707   4.757   28.458  1.00 16.09  ? 270 VAL B C   1 
ATOM   5325  O O   . VAL B 1 241 ? 8.225   5.034   27.384  1.00 16.67  ? 270 VAL B O   1 
ATOM   5326  C CB  . VAL B 1 241 ? 11.234  5.069   28.749  1.00 15.80  ? 270 VAL B CB  1 
ATOM   5327  C CG1 . VAL B 1 241 ? 11.379  4.678   27.284  1.00 16.16  ? 270 VAL B CG1 1 
ATOM   5328  C CG2 . VAL B 1 241 ? 12.328  6.060   29.154  1.00 15.34  ? 270 VAL B CG2 1 
ATOM   5329  N N   . SER B 1 242 ? 8.263   3.708   29.147  1.00 16.67  ? 271 SER B N   1 
ATOM   5330  C CA  . SER B 1 242 ? 7.318   2.797   28.531  1.00 16.33  ? 271 SER B CA  1 
ATOM   5331  C C   . SER B 1 242 ? 5.941   3.444   28.450  1.00 15.32  ? 271 SER B C   1 
ATOM   5332  O O   . SER B 1 242 ? 5.283   3.373   27.426  1.00 16.84  ? 271 SER B O   1 
ATOM   5333  C CB  . SER B 1 242 ? 7.283   1.436   29.223  1.00 17.17  ? 271 SER B CB  1 
ATOM   5334  O OG  . SER B 1 242 ? 7.074   1.564   30.625  1.00 19.15  ? 271 SER B OG  1 
ATOM   5335  N N   . ALA B 1 243 ? 5.539   4.128   29.512  1.00 15.50  ? 272 ALA B N   1 
ATOM   5336  C CA  . ALA B 1 243 ? 4.239   4.765   29.528  1.00 16.62  ? 272 ALA B CA  1 
ATOM   5337  C C   . ALA B 1 243 ? 4.210   5.890   28.479  1.00 17.61  ? 272 ALA B C   1 
ATOM   5338  O O   . ALA B 1 243 ? 3.234   6.083   27.768  1.00 16.57  ? 272 ALA B O   1 
ATOM   5339  C CB  . ALA B 1 243 ? 4.007   5.287   30.918  1.00 14.71  ? 272 ALA B CB  1 
ATOM   5340  N N   . HIS B 1 244 ? 5.283   6.676   28.442  1.00 15.83  ? 273 HIS B N   1 
ATOM   5341  C CA  . HIS B 1 244 ? 5.366   7.792   27.539  1.00 16.03  ? 273 HIS B CA  1 
ATOM   5342  C C   . HIS B 1 244 ? 5.424   7.311   26.095  1.00 17.61  ? 273 HIS B C   1 
ATOM   5343  O O   . HIS B 1 244 ? 4.823   7.899   25.224  1.00 17.89  ? 273 HIS B O   1 
ATOM   5344  C CB  . HIS B 1 244 ? 6.606   8.610   27.846  1.00 15.75  ? 273 HIS B CB  1 
ATOM   5345  C CG  . HIS B 1 244 ? 6.681   9.892   27.112  1.00 15.96  ? 273 HIS B CG  1 
ATOM   5346  N ND1 . HIS B 1 244 ? 7.835   10.600  27.129  1.00 15.96  ? 273 HIS B ND1 1 
ATOM   5347  C CD2 . HIS B 1 244 ? 5.797   10.585  26.385  1.00 18.32  ? 273 HIS B CD2 1 
ATOM   5348  C CE1 . HIS B 1 244 ? 7.640   11.732  26.438  1.00 16.84  ? 273 HIS B CE1 1 
ATOM   5349  N NE2 . HIS B 1 244 ? 6.430   11.728  25.959  1.00 16.18  ? 273 HIS B NE2 1 
ATOM   5350  N N   . THR B 1 245 ? 6.115   6.200   25.830  1.00 17.07  ? 274 THR B N   1 
ATOM   5351  C CA  . THR B 1 245 ? 6.181   5.676   24.477  1.00 16.79  ? 274 THR B CA  1 
ATOM   5352  C C   . THR B 1 245 ? 4.753   5.308   24.041  1.00 17.04  ? 274 THR B C   1 
ATOM   5353  O O   . THR B 1 245 ? 4.302   5.656   22.939  1.00 13.63  ? 274 THR B O   1 
ATOM   5354  C CB  . THR B 1 245 ? 7.195   4.519   24.404  1.00 16.40  ? 274 THR B CB  1 
ATOM   5355  O OG1 . THR B 1 245 ? 8.459   5.059   24.790  1.00 18.17  ? 274 THR B OG1 1 
ATOM   5356  C CG2 . THR B 1 245 ? 7.310   3.929   23.019  1.00 19.05  ? 274 THR B CG2 1 
ATOM   5357  N N   . SER B 1 246 ? 4.028   4.616   24.935  1.00 16.73  ? 275 SER B N   1 
ATOM   5358  C CA  . SER B 1 246 ? 2.671   4.180   24.635  1.00 19.09  ? 275 SER B CA  1 
ATOM   5359  C C   . SER B 1 246 ? 1.806   5.386   24.292  1.00 18.28  ? 275 SER B C   1 
ATOM   5360  O O   . SER B 1 246 ? 0.998   5.322   23.372  1.00 17.78  ? 275 SER B O   1 
ATOM   5361  C CB  . SER B 1 246 ? 2.069   3.397   25.767  1.00 21.20  ? 275 SER B CB  1 
ATOM   5362  O OG  . SER B 1 246 ? 1.641   4.215   26.858  1.00 23.66  ? 275 SER B OG  1 
ATOM   5363  N N   . HIS B 1 247 ? 1.988   6.433   25.109  1.00 18.53  ? 276 HIS B N   1 
ATOM   5364  C CA  . HIS B 1 247 ? 1.223   7.670   24.999  1.00 17.28  ? 276 HIS B CA  1 
ATOM   5365  C C   . HIS B 1 247 ? 1.516   8.350   23.657  1.00 18.34  ? 276 HIS B C   1 
ATOM   5366  O O   . HIS B 1 247 ? 0.630   8.798   22.931  1.00 16.71  ? 276 HIS B O   1 
ATOM   5367  C CB  . HIS B 1 247 ? 1.570   8.576   26.167  1.00 17.45  ? 276 HIS B CB  1 
ATOM   5368  C CG  . HIS B 1 247 ? 0.645   9.729   26.324  1.00 18.72  ? 276 HIS B CG  1 
ATOM   5369  N ND1 . HIS B 1 247 ? 1.049   11.048  26.234  1.00 21.46  ? 276 HIS B ND1 1 
ATOM   5370  C CD2 . HIS B 1 247 ? -0.646  9.751   26.634  1.00 19.19  ? 276 HIS B CD2 1 
ATOM   5371  C CE1 . HIS B 1 247 ? 0.009   11.840  26.486  1.00 19.65  ? 276 HIS B CE1 1 
ATOM   5372  N NE2 . HIS B 1 247 ? -1.031  11.079  26.741  1.00 23.73  ? 276 HIS B NE2 1 
ATOM   5373  N N   . LEU B 1 248 ? 2.800   8.412   23.323  1.00 17.32  ? 277 LEU B N   1 
ATOM   5374  C CA  . LEU B 1 248 ? 3.254   9.089   22.117  1.00 17.62  ? 277 LEU B CA  1 
ATOM   5375  C C   . LEU B 1 248 ? 2.741   8.379   20.861  1.00 17.36  ? 277 LEU B C   1 
ATOM   5376  O O   . LEU B 1 248 ? 2.126   8.985   19.990  1.00 20.00  ? 277 LEU B O   1 
ATOM   5377  C CB  . LEU B 1 248 ? 4.773   9.138   22.212  1.00 16.67  ? 277 LEU B CB  1 
ATOM   5378  C CG  . LEU B 1 248 ? 5.547   9.574   20.979  1.00 15.77  ? 277 LEU B CG  1 
ATOM   5379  C CD1 . LEU B 1 248 ? 5.101   10.969  20.581  1.00 18.12  ? 277 LEU B CD1 1 
ATOM   5380  C CD2 . LEU B 1 248 ? 7.046   9.586   21.284  1.00 16.53  ? 277 LEU B CD2 1 
ATOM   5381  N N   . VAL B 1 249 ? 2.968   7.057   20.786  1.00 16.24  ? 278 VAL B N   1 
ATOM   5382  C CA  . VAL B 1 249 ? 2.569   6.246   19.651  1.00 16.28  ? 278 VAL B CA  1 
ATOM   5383  C C   . VAL B 1 249 ? 1.037   6.223   19.545  1.00 16.06  ? 278 VAL B C   1 
ATOM   5384  O O   . VAL B 1 249 ? 0.469   6.288   18.471  1.00 18.48  ? 278 VAL B O   1 
ATOM   5385  C CB  . VAL B 1 249 ? 3.202   4.844   19.776  1.00 16.02  ? 278 VAL B CB  1 
ATOM   5386  C CG1 . VAL B 1 249 ? 2.628   3.804   18.832  1.00 17.81  ? 278 VAL B CG1 1 
ATOM   5387  C CG2 . VAL B 1 249 ? 4.691   4.955   19.601  1.00 17.55  ? 278 VAL B CG2 1 
ATOM   5388  N N   . GLY B 1 250 ? 0.353   6.123   20.678  1.00 16.01  ? 279 GLY B N   1 
ATOM   5389  C CA  . GLY B 1 250 ? -1.085  6.114   20.614  1.00 15.51  ? 279 GLY B CA  1 
ATOM   5390  C C   . GLY B 1 250 ? -1.668  7.478   20.251  1.00 15.33  ? 279 GLY B C   1 
ATOM   5391  O O   . GLY B 1 250 ? -2.786  7.538   19.800  1.00 17.04  ? 279 GLY B O   1 
ATOM   5392  N N   . SER B 1 251 ? -0.945  8.562   20.499  1.00 17.43  ? 280 SER B N   1 
ATOM   5393  C CA  . SER B 1 251 ? -1.447  9.876   20.111  1.00 17.66  ? 280 SER B CA  1 
ATOM   5394  C C   . SER B 1 251 ? -1.515  10.010  18.586  1.00 17.19  ? 280 SER B C   1 
ATOM   5395  O O   . SER B 1 251 ? -2.202  10.883  18.096  1.00 16.98  ? 280 SER B O   1 
ATOM   5396  C CB  . SER B 1 251 ? -0.629  10.975  20.698  1.00 16.51  ? 280 SER B CB  1 
ATOM   5397  O OG  . SER B 1 251 ? 0.591   11.196  20.006  1.00 17.31  ? 280 SER B OG  1 
ATOM   5398  N N   . ALA B 1 252 ? -0.784  9.152   17.858  1.00 17.57  ? 281 ALA B N   1 
ATOM   5399  C CA  . ALA B 1 252 ? -0.840  9.101   16.402  1.00 18.12  ? 281 ALA B CA  1 
ATOM   5400  C C   . ALA B 1 252 ? -2.001  8.238   15.894  1.00 17.52  ? 281 ALA B C   1 
ATOM   5401  O O   . ALA B 1 252 ? -2.155  8.053   14.689  1.00 19.49  ? 281 ALA B O   1 
ATOM   5402  C CB  . ALA B 1 252 ? 0.485   8.610   15.874  1.00 20.45  ? 281 ALA B CB  1 
ATOM   5403  N N   . LEU B 1 253 ? -2.759  7.681   16.848  1.00 19.18  ? 282 LEU B N   1 
ATOM   5404  C CA  . LEU B 1 253 ? -3.923  6.837   16.659  1.00 19.42  ? 282 LEU B CA  1 
ATOM   5405  C C   . LEU B 1 253 ? -3.465  5.460   16.189  1.00 18.90  ? 282 LEU B C   1 
ATOM   5406  O O   . LEU B 1 253 ? -4.269  4.697   15.714  1.00 19.45  ? 282 LEU B O   1 
ATOM   5407  C CB  . LEU B 1 253 ? -4.956  7.469   15.720  1.00 18.41  ? 282 LEU B CB  1 
ATOM   5408  C CG  . LEU B 1 253 ? -5.556  8.792   16.189  1.00 19.48  ? 282 LEU B CG  1 
ATOM   5409  C CD1 . LEU B 1 253 ? -6.624  9.282   15.236  1.00 21.35  ? 282 LEU B CD1 1 
ATOM   5410  C CD2 . LEU B 1 253 ? -6.118  8.677   17.585  1.00 17.65  ? 282 LEU B CD2 1 
ATOM   5411  N N   . SER B 1 254 ? -2.187  5.111   16.396  1.00 20.23  ? 283 SER B N   1 
ATOM   5412  C CA  . SER B 1 254 ? -1.840  3.697   16.367  1.00 19.44  ? 283 SER B CA  1 
ATOM   5413  C C   . SER B 1 254 ? -2.672  2.936   17.403  1.00 20.95  ? 283 SER B C   1 
ATOM   5414  O O   . SER B 1 254 ? -2.992  3.441   18.465  1.00 21.22  ? 283 SER B O   1 
ATOM   5415  C CB  . SER B 1 254 ? -0.374  3.484   16.578  1.00 19.87  ? 283 SER B CB  1 
ATOM   5416  O OG  . SER B 1 254 ? 0.387   4.286   15.711  1.00 20.06  ? 283 SER B OG  1 
ATOM   5417  N N   . ASP B 1 255 ? -3.012  1.688   17.080  1.00 21.21  ? 284 ASP B N   1 
ATOM   5418  C CA  . ASP B 1 255 ? -3.901  0.896   17.903  1.00 22.17  ? 284 ASP B CA  1 
ATOM   5419  C C   . ASP B 1 255 ? -3.180  0.428   19.164  1.00 17.18  ? 284 ASP B C   1 
ATOM   5420  O O   . ASP B 1 255 ? -1.965  0.587   19.303  1.00 18.47  ? 284 ASP B O   1 
ATOM   5421  C CB  . ASP B 1 255 ? -4.471  -0.292  17.134  1.00 21.19  ? 284 ASP B CB  1 
ATOM   5422  C CG  . ASP B 1 255 ? -3.423  -1.295  16.666  1.00 23.85  ? 284 ASP B CG  1 
ATOM   5423  O OD1 . ASP B 1 255 ? -2.751  -1.896  17.537  1.00 24.31  ? 284 ASP B OD1 1 
ATOM   5424  O OD2 . ASP B 1 255 ? -3.261  -1.415  15.435  1.00 26.73  ? 284 ASP B OD2 1 
ATOM   5425  N N   . PRO B 1 256 ? -3.890  -0.151  20.149  1.00 16.98  ? 285 PRO B N   1 
ATOM   5426  C CA  . PRO B 1 256 ? -3.235  -0.537  21.394  1.00 19.01  ? 285 PRO B CA  1 
ATOM   5427  C C   . PRO B 1 256 ? -2.116  -1.581  21.275  1.00 19.56  ? 285 PRO B C   1 
ATOM   5428  O O   . PRO B 1 256 ? -1.218  -1.593  22.115  1.00 19.88  ? 285 PRO B O   1 
ATOM   5429  C CB  . PRO B 1 256 ? -4.362  -1.138  22.212  1.00 18.81  ? 285 PRO B CB  1 
ATOM   5430  C CG  . PRO B 1 256 ? -5.569  -0.361  21.705  1.00 18.42  ? 285 PRO B CG  1 
ATOM   5431  C CD  . PRO B 1 256 ? -5.346  -0.334  20.215  1.00 16.69  ? 285 PRO B CD  1 
ATOM   5432  N N   . TYR B 1 257 ? -2.214  -2.473  20.280  1.00 18.95  ? 286 TYR B N   1 
ATOM   5433  C CA  . TYR B 1 257 ? -1.156  -3.453  20.079  1.00 20.24  ? 286 TYR B CA  1 
ATOM   5434  C C   . TYR B 1 257 ? 0.143   -2.739  19.674  1.00 21.62  ? 286 TYR B C   1 
ATOM   5435  O O   . TYR B 1 257 ? 1.170   -2.897  20.325  1.00 18.14  ? 286 TYR B O   1 
ATOM   5436  C CB  . TYR B 1 257 ? -1.564  -4.514  19.059  1.00 21.62  ? 286 TYR B CB  1 
ATOM   5437  C CG  . TYR B 1 257 ? -2.776  -5.329  19.425  1.00 23.13  ? 286 TYR B CG  1 
ATOM   5438  C CD1 . TYR B 1 257 ? -2.648  -6.417  20.257  1.00 22.76  ? 286 TYR B CD1 1 
ATOM   5439  C CD2 . TYR B 1 257 ? -4.044  -4.983  18.986  1.00 24.11  ? 286 TYR B CD2 1 
ATOM   5440  C CE1 . TYR B 1 257 ? -3.730  -7.216  20.569  1.00 22.61  ? 286 TYR B CE1 1 
ATOM   5441  C CE2 . TYR B 1 257 ? -5.150  -5.748  19.310  1.00 23.28  ? 286 TYR B CE2 1 
ATOM   5442  C CZ  . TYR B 1 257 ? -4.990  -6.879  20.096  1.00 24.65  ? 286 TYR B CZ  1 
ATOM   5443  O OH  . TYR B 1 257 ? -6.071  -7.661  20.426  1.00 23.07  ? 286 TYR B OH  1 
ATOM   5444  N N   . LEU B 1 258 ? 0.082   -1.849  18.673  1.00 21.14  ? 287 LEU B N   1 
ATOM   5445  C CA  . LEU B 1 258 ? 1.267   -1.122  18.234  1.00 19.33  ? 287 LEU B CA  1 
ATOM   5446  C C   . LEU B 1 258 ? 1.852   -0.222  19.334  1.00 21.75  ? 287 LEU B C   1 
ATOM   5447  O O   . LEU B 1 258 ? 3.077   -0.087  19.470  1.00 18.71  ? 287 LEU B O   1 
ATOM   5448  C CB  . LEU B 1 258 ? 0.891   -0.281  17.005  1.00 20.86  ? 287 LEU B CB  1 
ATOM   5449  C CG  . LEU B 1 258 ? 0.497   -1.031  15.734  1.00 22.14  ? 287 LEU B CG  1 
ATOM   5450  C CD1 . LEU B 1 258 ? 0.507   -0.060  14.556  1.00 23.17  ? 287 LEU B CD1 1 
ATOM   5451  C CD2 . LEU B 1 258 ? 1.421   -2.204  15.434  1.00 24.06  ? 287 LEU B CD2 1 
ATOM   5452  N N   . SER B 1 259 ? 0.962   0.417   20.115  1.00 21.70  ? 288 SER B N   1 
ATOM   5453  C CA  . SER B 1 259 ? 1.355   1.320   21.183  1.00 22.38  ? 288 SER B CA  1 
ATOM   5454  C C   . SER B 1 259 ? 2.018   0.540   22.313  1.00 19.46  ? 288 SER B C   1 
ATOM   5455  O O   . SER B 1 259 ? 3.074   0.932   22.797  1.00 20.08  ? 288 SER B O   1 
ATOM   5456  C CB  . SER B 1 259 ? 0.146   2.109   21.614  1.00 22.32  ? 288 SER B CB  1 
ATOM   5457  O OG  . SER B 1 259 ? -0.403  2.749   20.471  1.00 26.44  ? 288 SER B OG  1 
ATOM   5458  N N   . PHE B 1 260 ? 1.474   -0.639  22.624  1.00 17.71  ? 289 PHE B N   1 
ATOM   5459  C CA  . PHE B 1 260 ? 2.040   -1.472  23.675  1.00 19.19  ? 289 PHE B CA  1 
ATOM   5460  C C   . PHE B 1 260 ? 3.376   -2.065  23.212  1.00 17.47  ? 289 PHE B C   1 
ATOM   5461  O O   . PHE B 1 260 ? 4.346   -1.979  23.951  1.00 15.98  ? 289 PHE B O   1 
ATOM   5462  C CB  . PHE B 1 260 ? 1.100   -2.586  24.124  1.00 18.73  ? 289 PHE B CB  1 
ATOM   5463  C CG  . PHE B 1 260 ? 1.650   -3.453  25.236  1.00 20.03  ? 289 PHE B CG  1 
ATOM   5464  C CD1 . PHE B 1 260 ? 1.713   -3.000  26.551  1.00 20.77  ? 289 PHE B CD1 1 
ATOM   5465  C CD2 . PHE B 1 260 ? 2.091   -4.744  24.982  1.00 20.03  ? 289 PHE B CD2 1 
ATOM   5466  C CE1 . PHE B 1 260 ? 2.247   -3.794  27.559  1.00 20.25  ? 289 PHE B CE1 1 
ATOM   5467  C CE2 . PHE B 1 260 ? 2.603   -5.542  25.997  1.00 19.42  ? 289 PHE B CE2 1 
ATOM   5468  C CZ  . PHE B 1 260 ? 2.666   -5.083  27.282  1.00 19.38  ? 289 PHE B CZ  1 
ATOM   5469  N N   . ALA B 1 261 ? 3.444   -2.575  21.964  1.00 15.78  ? 290 ALA B N   1 
ATOM   5470  C CA  . ALA B 1 261 ? 4.686   -3.160  21.466  1.00 16.81  ? 290 ALA B CA  1 
ATOM   5471  C C   . ALA B 1 261 ? 5.821   -2.131  21.463  1.00 16.11  ? 290 ALA B C   1 
ATOM   5472  O O   . ALA B 1 261 ? 6.945   -2.436  21.802  1.00 16.92  ? 290 ALA B O   1 
ATOM   5473  C CB  . ALA B 1 261 ? 4.480   -3.751  20.091  1.00 14.97  ? 290 ALA B CB  1 
ATOM   5474  N N   . ALA B 1 262 ? 5.539   -0.869  21.085  1.00 13.95  ? 291 ALA B N   1 
ATOM   5475  C CA  . ALA B 1 262 ? 6.543   0.159   21.188  1.00 17.48  ? 291 ALA B CA  1 
ATOM   5476  C C   . ALA B 1 262 ? 6.929   0.424   22.644  1.00 15.61  ? 291 ALA B C   1 
ATOM   5477  O O   . ALA B 1 262 ? 8.097   0.673   22.918  1.00 14.07  ? 291 ALA B O   1 
ATOM   5478  C CB  . ALA B 1 262 ? 6.065   1.421   20.555  1.00 15.41  ? 291 ALA B CB  1 
ATOM   5479  N N   . ALA B 1 263 ? 5.940   0.411   23.539  1.00 15.88  ? 292 ALA B N   1 
ATOM   5480  C CA  . ALA B 1 263 ? 6.200   0.568   24.963  1.00 15.59  ? 292 ALA B CA  1 
ATOM   5481  C C   . ALA B 1 263 ? 7.198   -0.483  25.469  1.00 14.78  ? 292 ALA B C   1 
ATOM   5482  O O   . ALA B 1 263 ? 8.132   -0.179  26.189  1.00 16.22  ? 292 ALA B O   1 
ATOM   5483  C CB  . ALA B 1 263 ? 4.908   0.525   25.713  1.00 16.62  ? 292 ALA B CB  1 
ATOM   5484  N N   . MET B 1 264 ? 6.983   -1.727  25.060  1.00 16.82  ? 293 MET B N   1 
ATOM   5485  C CA  . MET B 1 264 ? 7.863   -2.817  25.415  1.00 17.10  ? 293 MET B CA  1 
ATOM   5486  C C   . MET B 1 264 ? 9.276   -2.609  24.853  1.00 19.71  ? 293 MET B C   1 
ATOM   5487  O O   . MET B 1 264 ? 10.252  -2.979  25.518  1.00 18.57  ? 293 MET B O   1 
ATOM   5488  C CB  . MET B 1 264 ? 7.305   -4.141  24.885  1.00 17.01  ? 293 MET B CB  1 
ATOM   5489  C CG  . MET B 1 264 ? 6.026   -4.613  25.554  1.00 16.77  ? 293 MET B CG  1 
ATOM   5490  S SD  . MET B 1 264 ? 6.072   -4.593  27.333  1.00 18.78  ? 293 MET B SD  1 
ATOM   5491  C CE  . MET B 1 264 ? 5.721   -2.863  27.678  1.00 14.56  ? 293 MET B CE  1 
ATOM   5492  N N   . ASN B 1 265 ? 9.418   -2.042  23.648  1.00 18.63  ? 294 ASN B N   1 
ATOM   5493  C CA  . ASN B 1 265 ? 10.749  -1.764  23.143  1.00 20.89  ? 294 ASN B CA  1 
ATOM   5494  C C   . ASN B 1 265 ? 11.472  -0.785  24.067  1.00 21.93  ? 294 ASN B C   1 
ATOM   5495  O O   . ASN B 1 265 ? 12.697  -0.871  24.251  1.00 19.81  ? 294 ASN B O   1 
ATOM   5496  C CB  . ASN B 1 265 ? 10.745  -1.347  21.668  1.00 22.02  ? 294 ASN B CB  1 
ATOM   5497  C CG  . ASN B 1 265 ? 10.653  -2.526  20.732  1.00 21.06  ? 294 ASN B CG  1 
ATOM   5498  O OD1 . ASN B 1 265 ? 10.283  -3.621  21.141  1.00 24.26  ? 294 ASN B OD1 1 
ATOM   5499  N ND2 . ASN B 1 265 ? 10.985  -2.321  19.476  1.00 25.33  ? 294 ASN B ND2 1 
ATOM   5500  N N   . GLY B 1 266 ? 10.722  0.153   24.658  1.00 21.87  ? 295 GLY B N   1 
ATOM   5501  C CA  . GLY B 1 266 ? 11.307  1.064   25.615  1.00 21.10  ? 295 GLY B CA  1 
ATOM   5502  C C   . GLY B 1 266 ? 11.578  0.440   26.985  1.00 19.88  ? 295 GLY B C   1 
ATOM   5503  O O   . GLY B 1 266 ? 12.571  0.774   27.618  1.00 19.67  ? 295 GLY B O   1 
ATOM   5504  N N   . LEU B 1 267 ? 10.646  -0.406  27.445  1.00 18.09  ? 296 LEU B N   1 
ATOM   5505  C CA  . LEU B 1 267 ? 10.774  -1.115  28.696  1.00 17.54  ? 296 LEU B CA  1 
ATOM   5506  C C   . LEU B 1 267 ? 12.012  -2.015  28.664  1.00 16.54  ? 296 LEU B C   1 
ATOM   5507  O O   . LEU B 1 267 ? 12.608  -2.196  29.718  1.00 15.88  ? 296 LEU B O   1 
ATOM   5508  C CB  . LEU B 1 267 ? 9.497   -1.915  28.962  1.00 17.71  ? 296 LEU B CB  1 
ATOM   5509  C CG  . LEU B 1 267 ? 9.383   -2.537  30.349  1.00 19.67  ? 296 LEU B CG  1 
ATOM   5510  C CD1 . LEU B 1 267 ? 9.413   -1.472  31.439  1.00 19.78  ? 296 LEU B CD1 1 
ATOM   5511  C CD2 . LEU B 1 267 ? 8.127   -3.383  30.452  1.00 20.71  ? 296 LEU B CD2 1 
ATOM   5512  N N   . ALA B 1 268 ? 12.441  -2.437  27.460  1.00 16.75  ? 297 ALA B N   1 
ATOM   5513  C CA  . ALA B 1 268 ? 13.550  -3.372  27.309  1.00 16.32  ? 297 ALA B CA  1 
ATOM   5514  C C   . ALA B 1 268 ? 14.894  -2.660  27.406  1.00 17.77  ? 297 ALA B C   1 
ATOM   5515  O O   . ALA B 1 268 ? 15.952  -3.284  27.359  1.00 21.23  ? 297 ALA B O   1 
ATOM   5516  C CB  . ALA B 1 268 ? 13.435  -4.118  26.017  1.00 18.22  ? 297 ALA B CB  1 
ATOM   5517  N N   . GLY B 1 269 ? 14.882  -1.337  27.565  1.00 16.38  ? 298 GLY B N   1 
ATOM   5518  C CA  . GLY B 1 269 ? 16.121  -0.600  27.654  1.00 16.49  ? 298 GLY B CA  1 
ATOM   5519  C C   . GLY B 1 269 ? 16.781  -0.815  29.018  1.00 16.93  ? 298 GLY B C   1 
ATOM   5520  O O   . GLY B 1 269 ? 16.127  -0.787  30.059  1.00 16.25  ? 298 GLY B O   1 
ATOM   5521  N N   . PRO B 1 270 ? 18.108  -1.055  29.052  1.00 19.16  ? 299 PRO B N   1 
ATOM   5522  C CA  . PRO B 1 270 ? 18.837  -1.146  30.317  1.00 21.50  ? 299 PRO B CA  1 
ATOM   5523  C C   . PRO B 1 270 ? 18.477  -0.102  31.368  1.00 20.62  ? 299 PRO B C   1 
ATOM   5524  O O   . PRO B 1 270 ? 18.380  -0.419  32.530  1.00 23.28  ? 299 PRO B O   1 
ATOM   5525  C CB  . PRO B 1 270 ? 20.300  -0.944  29.893  1.00 22.49  ? 299 PRO B CB  1 
ATOM   5526  C CG  . PRO B 1 270 ? 20.355  -1.514  28.487  1.00 23.93  ? 299 PRO B CG  1 
ATOM   5527  C CD  . PRO B 1 270 ? 18.973  -1.278  27.892  1.00 21.32  ? 299 PRO B CD  1 
ATOM   5528  N N   . LEU B 1 271 ? 18.287  1.165   30.986  1.00 21.73  ? 300 LEU B N   1 
ATOM   5529  C CA  . LEU B 1 271 ? 17.960  2.154   31.998  1.00 20.15  ? 300 LEU B CA  1 
ATOM   5530  C C   . LEU B 1 271 ? 16.477  2.140   32.367  1.00 21.88  ? 300 LEU B C   1 
ATOM   5531  O O   . LEU B 1 271 ? 16.002  3.027   33.079  1.00 23.72  ? 300 LEU B O   1 
ATOM   5532  C CB  . LEU B 1 271 ? 18.324  3.551   31.511  1.00 21.59  ? 300 LEU B CB  1 
ATOM   5533  C CG  . LEU B 1 271 ? 19.776  3.760   31.092  1.00 22.18  ? 300 LEU B CG  1 
ATOM   5534  C CD1 . LEU B 1 271 ? 20.030  5.233   30.737  1.00 21.38  ? 300 LEU B CD1 1 
ATOM   5535  C CD2 . LEU B 1 271 ? 20.716  3.289   32.187  1.00 21.74  ? 300 LEU B CD2 1 
ATOM   5536  N N   . HIS B 1 272 ? 15.725  1.175   31.881  1.00 20.94  ? 301 HIS B N   1 
ATOM   5537  C CA  . HIS B 1 272 ? 14.324  1.112   32.233  1.00 20.92  ? 301 HIS B CA  1 
ATOM   5538  C C   . HIS B 1 272 ? 14.124  -0.279  32.809  1.00 21.90  ? 301 HIS B C   1 
ATOM   5539  O O   . HIS B 1 272 ? 14.952  -0.704  33.603  1.00 23.62  ? 301 HIS B O   1 
ATOM   5540  C CB  . HIS B 1 272 ? 13.420  1.482   31.048  1.00 20.54  ? 301 HIS B CB  1 
ATOM   5541  C CG  . HIS B 1 272 ? 12.012  1.772   31.460  1.00 18.63  ? 301 HIS B CG  1 
ATOM   5542  N ND1 . HIS B 1 272 ? 10.954  1.925   30.587  1.00 21.08  ? 301 HIS B ND1 1 
ATOM   5543  C CD2 . HIS B 1 272 ? 11.507  1.948   32.688  1.00 16.54  ? 301 HIS B CD2 1 
ATOM   5544  C CE1 . HIS B 1 272 ? 9.873   2.226   31.288  1.00 17.19  ? 301 HIS B CE1 1 
ATOM   5545  N NE2 . HIS B 1 272 ? 10.169  2.253   32.534  1.00 19.20  ? 301 HIS B NE2 1 
ATOM   5546  N N   . GLY B 1 273 ? 13.107  -0.975  32.298  1.00 22.04  ? 302 GLY B N   1 
ATOM   5547  C CA  . GLY B 1 273 ? 12.652  -2.271  32.771  1.00 20.63  ? 302 GLY B CA  1 
ATOM   5548  C C   . GLY B 1 273 ? 13.731  -3.348  32.751  1.00 20.44  ? 302 GLY B C   1 
ATOM   5549  O O   . GLY B 1 273 ? 13.750  -4.190  33.642  1.00 19.32  ? 302 GLY B O   1 
ATOM   5550  N N   . LEU B 1 274 ? 14.648  -3.299  31.787  1.00 18.60  ? 303 LEU B N   1 
ATOM   5551  C CA  . LEU B 1 274 ? 15.636  -4.365  31.696  1.00 20.48  ? 303 LEU B CA  1 
ATOM   5552  C C   . LEU B 1 274 ? 16.555  -4.360  32.925  1.00 22.06  ? 303 LEU B C   1 
ATOM   5553  O O   . LEU B 1 274 ? 17.230  -5.346  33.208  1.00 22.24  ? 303 LEU B O   1 
ATOM   5554  C CB  . LEU B 1 274 ? 16.432  -4.225  30.397  1.00 20.78  ? 303 LEU B CB  1 
ATOM   5555  C CG  . LEU B 1 274 ? 17.111  -5.509  29.947  1.00 22.27  ? 303 LEU B CG  1 
ATOM   5556  C CD1 . LEU B 1 274 ? 16.142  -6.343  29.126  1.00 24.50  ? 303 LEU B CD1 1 
ATOM   5557  C CD2 . LEU B 1 274 ? 18.373  -5.192  29.173  1.00 23.27  ? 303 LEU B CD2 1 
ATOM   5558  N N   . ALA B 1 275 ? 16.581  -3.251  33.672  1.00 21.32  ? 304 ALA B N   1 
ATOM   5559  C CA  . ALA B 1 275 ? 17.304  -3.191  34.934  1.00 22.46  ? 304 ALA B CA  1 
ATOM   5560  C C   . ALA B 1 275 ? 16.986  -4.364  35.865  1.00 22.63  ? 304 ALA B C   1 
ATOM   5561  O O   . ALA B 1 275 ? 17.896  -4.791  36.576  1.00 22.42  ? 304 ALA B O   1 
ATOM   5562  C CB  . ALA B 1 275 ? 17.070  -1.861  35.596  1.00 21.63  ? 304 ALA B CB  1 
ATOM   5563  N N   . ASN B 1 276 ? 15.750  -4.920  35.847  1.00 23.19  ? 305 ASN B N   1 
ATOM   5564  C CA  . ASN B 1 276 ? 15.405  -6.021  36.744  1.00 21.85  ? 305 ASN B CA  1 
ATOM   5565  C C   . ASN B 1 276 ? 16.140  -7.298  36.344  1.00 21.53  ? 305 ASN B C   1 
ATOM   5566  O O   . ASN B 1 276 ? 16.379  -8.130  37.200  1.00 20.48  ? 305 ASN B O   1 
ATOM   5567  C CB  . ASN B 1 276 ? 13.894  -6.235  36.931  1.00 24.91  ? 305 ASN B CB  1 
ATOM   5568  C CG  . ASN B 1 276 ? 13.041  -6.671  35.745  1.00 27.04  ? 305 ASN B CG  1 
ATOM   5569  O OD1 . ASN B 1 276 ? 11.813  -6.710  35.893  1.00 31.91  ? 305 ASN B OD1 1 
ATOM   5570  N ND2 . ASN B 1 276 ? 13.616  -7.009  34.595  1.00 23.01  ? 305 ASN B ND2 1 
ATOM   5571  N N   . GLN B 1 277 ? 16.531  -7.430  35.077  1.00 21.62  ? 306 GLN B N   1 
ATOM   5572  C CA  . GLN B 1 277 ? 17.420  -8.511  34.641  1.00 21.72  ? 306 GLN B CA  1 
ATOM   5573  C C   . GLN B 1 277 ? 18.878  -8.198  34.996  1.00 23.90  ? 306 GLN B C   1 
ATOM   5574  O O   . GLN B 1 277 ? 19.637  -9.075  35.403  1.00 23.72  ? 306 GLN B O   1 
ATOM   5575  C CB  . GLN B 1 277 ? 17.286  -8.683  33.125  1.00 21.79  ? 306 GLN B CB  1 
ATOM   5576  C CG  . GLN B 1 277 ? 18.438  -9.402  32.446  1.00 23.66  ? 306 GLN B CG  1 
ATOM   5577  C CD  . GLN B 1 277 ? 18.366  -9.241  30.947  1.00 23.34  ? 306 GLN B CD  1 
ATOM   5578  O OE1 . GLN B 1 277 ? 17.353  -9.569  30.327  1.00 22.29  ? 306 GLN B OE1 1 
ATOM   5579  N NE2 . GLN B 1 277 ? 19.397  -8.619  30.390  1.00 23.66  ? 306 GLN B NE2 1 
ATOM   5580  N N   . GLU B 1 278 ? 19.286  -6.943  34.778  1.00 23.60  ? 307 GLU B N   1 
ATOM   5581  C CA  . GLU B 1 278 ? 20.663  -6.537  34.948  1.00 25.79  ? 307 GLU B CA  1 
ATOM   5582  C C   . GLU B 1 278 ? 21.092  -6.638  36.412  1.00 26.55  ? 307 GLU B C   1 
ATOM   5583  O O   . GLU B 1 278 ? 22.241  -6.962  36.685  1.00 25.87  ? 307 GLU B O   1 
ATOM   5584  C CB  . GLU B 1 278 ? 20.865  -5.107  34.455  1.00 30.98  ? 307 GLU B CB  1 
ATOM   5585  C CG  . GLU B 1 278 ? 20.206  -4.861  33.122  1.00 37.04  ? 307 GLU B CG  1 
ATOM   5586  C CD  . GLU B 1 278 ? 20.830  -3.755  32.309  1.00 45.62  ? 307 GLU B CD  1 
ATOM   5587  O OE1 . GLU B 1 278 ? 21.231  -2.730  32.915  1.00 50.38  ? 307 GLU B OE1 1 
ATOM   5588  O OE2 . GLU B 1 278 ? 20.881  -3.918  31.068  1.00 56.23  ? 307 GLU B OE2 1 
ATOM   5589  N N   . VAL B 1 279 ? 20.155  -6.377  37.335  1.00 24.49  ? 308 VAL B N   1 
ATOM   5590  C CA  . VAL B 1 279 ? 20.397  -6.521  38.757  1.00 22.68  ? 308 VAL B CA  1 
ATOM   5591  C C   . VAL B 1 279 ? 20.890  -7.937  39.060  1.00 23.64  ? 308 VAL B C   1 
ATOM   5592  O O   . VAL B 1 279 ? 21.846  -8.122  39.813  1.00 26.29  ? 308 VAL B O   1 
ATOM   5593  C CB  . VAL B 1 279 ? 19.132  -6.163  39.555  1.00 23.30  ? 308 VAL B CB  1 
ATOM   5594  C CG1 . VAL B 1 279 ? 19.166  -6.684  40.986  1.00 24.12  ? 308 VAL B CG1 1 
ATOM   5595  C CG2 . VAL B 1 279 ? 18.927  -4.658  39.552  1.00 22.15  ? 308 VAL B CG2 1 
ATOM   5596  N N   . LEU B 1 280 ? 20.219  -8.945  38.507  1.00 24.99  ? 309 LEU B N   1 
ATOM   5597  C CA  . LEU B 1 280 ? 20.569  -10.303 38.881  1.00 26.12  ? 309 LEU B CA  1 
ATOM   5598  C C   . LEU B 1 280 ? 21.814  -10.786 38.152  1.00 27.36  ? 309 LEU B C   1 
ATOM   5599  O O   . LEU B 1 280 ? 22.493  -11.658 38.685  1.00 25.00  ? 309 LEU B O   1 
ATOM   5600  C CB  . LEU B 1 280 ? 19.392  -11.267 38.739  1.00 29.85  ? 309 LEU B CB  1 
ATOM   5601  C CG  . LEU B 1 280 ? 18.815  -11.662 40.100  1.00 32.16  ? 309 LEU B CG  1 
ATOM   5602  C CD1 . LEU B 1 280 ? 18.074  -10.502 40.737  1.00 34.09  ? 309 LEU B CD1 1 
ATOM   5603  C CD2 . LEU B 1 280 ? 17.941  -12.893 40.023  1.00 33.78  ? 309 LEU B CD2 1 
ATOM   5604  N N   . VAL B 1 281 ? 22.111  -10.234 36.972  1.00 25.27  ? 310 VAL B N   1 
ATOM   5605  C CA  . VAL B 1 281 ? 23.392  -10.489 36.335  1.00 24.83  ? 310 VAL B CA  1 
ATOM   5606  C C   . VAL B 1 281 ? 24.520  -9.937  37.211  1.00 27.78  ? 310 VAL B C   1 
ATOM   5607  O O   . VAL B 1 281 ? 25.535  -10.588 37.435  1.00 25.84  ? 310 VAL B O   1 
ATOM   5608  C CB  . VAL B 1 281 ? 23.458  -9.864  34.930  1.00 25.22  ? 310 VAL B CB  1 
ATOM   5609  C CG1 . VAL B 1 281 ? 24.891  -9.877  34.401  1.00 23.85  ? 310 VAL B CG1 1 
ATOM   5610  C CG2 . VAL B 1 281 ? 22.492  -10.548 33.973  1.00 26.69  ? 310 VAL B CG2 1 
ATOM   5611  N N   . TRP B 1 282 ? 24.351  -8.683  37.639  1.00 25.84  ? 311 TRP B N   1 
ATOM   5612  C CA  . TRP B 1 282 ? 25.307  -7.977  38.468  1.00 26.84  ? 311 TRP B CA  1 
ATOM   5613  C C   . TRP B 1 282 ? 25.469  -8.664  39.830  1.00 28.37  ? 311 TRP B C   1 
ATOM   5614  O O   . TRP B 1 282 ? 26.577  -8.698  40.361  1.00 27.49  ? 311 TRP B O   1 
ATOM   5615  C CB  . TRP B 1 282 ? 24.821  -6.533  38.555  1.00 25.25  ? 311 TRP B CB  1 
ATOM   5616  C CG  . TRP B 1 282 ? 25.743  -5.547  39.192  1.00 29.76  ? 311 TRP B CG  1 
ATOM   5617  C CD1 . TRP B 1 282 ? 26.873  -4.994  38.658  1.00 28.48  ? 311 TRP B CD1 1 
ATOM   5618  C CD2 . TRP B 1 282 ? 25.564  -4.935  40.479  1.00 30.50  ? 311 TRP B CD2 1 
ATOM   5619  N NE1 . TRP B 1 282 ? 27.411  -4.085  39.529  1.00 29.22  ? 311 TRP B NE1 1 
ATOM   5620  C CE2 . TRP B 1 282 ? 26.645  -4.041  40.662  1.00 31.05  ? 311 TRP B CE2 1 
ATOM   5621  C CE3 . TRP B 1 282 ? 24.609  -5.059  41.499  1.00 31.33  ? 311 TRP B CE3 1 
ATOM   5622  C CZ2 . TRP B 1 282 ? 26.795  -3.286  41.825  1.00 30.98  ? 311 TRP B CZ2 1 
ATOM   5623  C CZ3 . TRP B 1 282 ? 24.758  -4.304  42.640  1.00 32.50  ? 311 TRP B CZ3 1 
ATOM   5624  C CH2 . TRP B 1 282 ? 25.824  -3.419  42.791  1.00 34.01  ? 311 TRP B CH2 1 
ATOM   5625  N N   . LEU B 1 283 ? 24.390  -9.250  40.377  1.00 27.31  ? 312 LEU B N   1 
ATOM   5626  C CA  . LEU B 1 283 ? 24.481  -9.996  41.627  1.00 29.78  ? 312 LEU B CA  1 
ATOM   5627  C C   . LEU B 1 283 ? 25.254  -11.291 41.440  1.00 30.57  ? 312 LEU B C   1 
ATOM   5628  O O   . LEU B 1 283 ? 26.026  -11.682 42.317  1.00 28.33  ? 312 LEU B O   1 
ATOM   5629  C CB  . LEU B 1 283 ? 23.084  -10.341 42.150  1.00 28.73  ? 312 LEU B CB  1 
ATOM   5630  C CG  . LEU B 1 283 ? 22.354  -9.161  42.777  1.00 32.17  ? 312 LEU B CG  1 
ATOM   5631  C CD1 . LEU B 1 283 ? 20.948  -9.555  43.223  1.00 32.56  ? 312 LEU B CD1 1 
ATOM   5632  C CD2 . LEU B 1 283 ? 23.196  -8.564  43.899  1.00 37.49  ? 312 LEU B CD2 1 
ATOM   5633  N N   . THR B 1 284 ? 24.952  -11.983 40.342  1.00 31.41  ? 313 THR B N   1 
ATOM   5634  C CA  . THR B 1 284 ? 25.602  -13.239 40.009  1.00 33.58  ? 313 THR B CA  1 
ATOM   5635  C C   . THR B 1 284 ? 27.103  -12.997 39.872  1.00 38.15  ? 313 THR B C   1 
ATOM   5636  O O   . THR B 1 284 ? 27.911  -13.754 40.409  1.00 35.35  ? 313 THR B O   1 
ATOM   5637  C CB  . THR B 1 284 ? 25.035  -13.842 38.714  1.00 36.75  ? 313 THR B CB  1 
ATOM   5638  O OG1 . THR B 1 284 ? 23.612  -13.965 38.848  1.00 34.79  ? 313 THR B OG1 1 
ATOM   5639  C CG2 . THR B 1 284 ? 25.657  -15.185 38.388  1.00 37.32  ? 313 THR B CG2 1 
ATOM   5640  N N   . GLN B 1 285 ? 27.453  -11.898 39.200  1.00 39.30  ? 314 GLN B N   1 
ATOM   5641  C CA  . GLN B 1 285 ? 28.842  -11.538 38.972  1.00 44.28  ? 314 GLN B CA  1 
ATOM   5642  C C   . GLN B 1 285 ? 29.546  -11.265 40.307  1.00 42.63  ? 314 GLN B C   1 
ATOM   5643  O O   . GLN B 1 285 ? 30.687  -11.684 40.483  1.00 41.29  ? 314 GLN B O   1 
ATOM   5644  C CB  . GLN B 1 285 ? 28.934  -10.316 38.049  1.00 46.82  ? 314 GLN B CB  1 
ATOM   5645  C CG  . GLN B 1 285 ? 30.021  -10.399 36.985  1.00 52.88  ? 314 GLN B CG  1 
ATOM   5646  C CD  . GLN B 1 285 ? 31.320  -11.006 37.456  1.00 61.01  ? 314 GLN B CD  1 
ATOM   5647  O OE1 . GLN B 1 285 ? 31.641  -12.150 37.131  1.00 62.53  ? 314 GLN B OE1 1 
ATOM   5648  N NE2 . GLN B 1 285 ? 32.081  -10.242 38.226  1.00 68.26  ? 314 GLN B NE2 1 
ATOM   5649  N N   . LEU B 1 286 ? 28.879  -10.570 41.245  1.00 45.01  ? 315 LEU B N   1 
ATOM   5650  C CA  . LEU B 1 286 ? 29.542  -10.166 42.481  1.00 43.52  ? 315 LEU B CA  1 
ATOM   5651  C C   . LEU B 1 286 ? 29.706  -11.385 43.389  1.00 43.68  ? 315 LEU B C   1 
ATOM   5652  O O   . LEU B 1 286 ? 30.710  -11.496 44.090  1.00 42.34  ? 315 LEU B O   1 
ATOM   5653  C CB  . LEU B 1 286 ? 28.790  -9.010  43.163  1.00 45.15  ? 315 LEU B CB  1 
ATOM   5654  C CG  . LEU B 1 286 ? 28.105  -9.301  44.500  1.00 48.12  ? 315 LEU B CG  1 
ATOM   5655  C CD1 . LEU B 1 286 ? 29.083  -9.163  45.658  1.00 47.62  ? 315 LEU B CD1 1 
ATOM   5656  C CD2 . LEU B 1 286 ? 26.913  -8.376  44.717  1.00 49.70  ? 315 LEU B CD2 1 
ATOM   5657  N N   . GLN B 1 287 ? 28.752  -12.321 43.335  1.00 40.46  ? 316 GLN B N   1 
ATOM   5658  C CA  . GLN B 1 287 ? 28.846  -13.530 44.133  1.00 44.71  ? 316 GLN B CA  1 
ATOM   5659  C C   . GLN B 1 287 ? 29.993  -14.401 43.629  1.00 49.29  ? 316 GLN B C   1 
ATOM   5660  O O   . GLN B 1 287 ? 30.703  -14.989 44.443  1.00 51.07  ? 316 GLN B O   1 
ATOM   5661  C CB  . GLN B 1 287 ? 27.508  -14.263 44.170  1.00 40.43  ? 316 GLN B CB  1 
ATOM   5662  C CG  . GLN B 1 287 ? 26.511  -13.553 45.069  1.00 41.33  ? 316 GLN B CG  1 
ATOM   5663  C CD  . GLN B 1 287 ? 25.307  -14.409 45.357  1.00 45.31  ? 316 GLN B CD  1 
ATOM   5664  O OE1 . GLN B 1 287 ? 24.597  -14.823 44.450  1.00 51.88  ? 316 GLN B OE1 1 
ATOM   5665  N NE2 . GLN B 1 287 ? 25.065  -14.680 46.630  1.00 49.01  ? 316 GLN B NE2 1 
ATOM   5666  N N   . LYS B 1 288 ? 30.189  -14.416 42.313  1.00 50.52  ? 317 LYS B N   1 
ATOM   5667  C CA  . LYS B 1 288 ? 31.284  -15.229 41.722  1.00 53.63  ? 317 LYS B CA  1 
ATOM   5668  C C   . LYS B 1 288 ? 32.625  -14.656 42.195  1.00 57.74  ? 317 LYS B C   1 
ATOM   5669  O O   . LYS B 1 288 ? 33.507  -15.448 42.563  1.00 57.19  ? 317 LYS B O   1 
ATOM   5670  C CB  . LYS B 1 288 ? 31.227  -15.238 40.195  1.00 53.14  ? 317 LYS B CB  1 
ATOM   5671  C CG  . LYS B 1 288 ? 29.980  -15.783 39.526  1.00 52.38  ? 317 LYS B CG  1 
ATOM   5672  C CD  . LYS B 1 288 ? 29.472  -17.099 40.094  1.00 53.54  ? 317 LYS B CD  1 
ATOM   5673  C CE  . LYS B 1 288 ? 27.982  -17.206 40.062  1.00 52.64  ? 317 LYS B CE  1 
ATOM   5674  N NZ  . LYS B 1 288 ? 27.353  -16.404 41.115  1.00 49.12  ? 317 LYS B NZ  1 
ATOM   5675  N N   . GLU B 1 289 ? 32.758  -13.334 42.188  1.00 61.36  ? 318 GLU B N   1 
ATOM   5676  C CA  . GLU B 1 289 ? 34.011  -12.676 42.629  1.00 68.55  ? 318 GLU B CA  1 
ATOM   5677  C C   . GLU B 1 289 ? 33.924  -12.296 44.119  1.00 74.66  ? 318 GLU B C   1 
ATOM   5678  O O   . GLU B 1 289 ? 34.641  -11.365 44.517  1.00 68.91  ? 318 GLU B O   1 
ATOM   5679  C CB  . GLU B 1 289 ? 34.305  -11.461 41.760  1.00 71.04  ? 318 GLU B CB  1 
ATOM   5680  C CG  . GLU B 1 289 ? 34.309  -11.795 40.274  1.00 81.92  ? 318 GLU B CG  1 
ATOM   5681  C CD  . GLU B 1 289 ? 35.238  -12.950 39.954  1.00 93.91  ? 318 GLU B CD  1 
ATOM   5682  O OE1 . GLU B 1 289 ? 34.749  -14.088 39.776  1.00 102.42 ? 318 GLU B OE1 1 
ATOM   5683  O OE2 . GLU B 1 289 ? 36.459  -12.700 39.886  1.00 103.97 ? 318 GLU B OE2 1 
ATOM   5684  N N   . VAL B 1 290 ? 33.096  -12.975 44.910  1.00 79.55  ? 319 VAL B N   1 
ATOM   5685  C CA  . VAL B 1 290 ? 33.105  -12.750 46.392  1.00 80.07  ? 319 VAL B CA  1 
ATOM   5686  C C   . VAL B 1 290 ? 32.725  -14.100 47.009  1.00 81.41  ? 319 VAL B C   1 
ATOM   5687  O O   . VAL B 1 290 ? 32.810  -15.115 46.298  1.00 84.36  ? 319 VAL B O   1 
ATOM   5688  C CB  . VAL B 1 290 ? 32.211  -11.636 46.980  1.00 80.77  ? 319 VAL B CB  1 
ATOM   5689  C CG1 . VAL B 1 290 ? 32.474  -10.251 46.404  1.00 78.95  ? 319 VAL B CG1 1 
ATOM   5690  C CG2 . VAL B 1 290 ? 30.725  -11.972 47.027  1.00 81.86  ? 319 VAL B CG2 1 
ATOM   5691  N N   . GLY B 1 291 ? 32.388  -14.131 48.296  1.00 79.27  ? 320 GLY B N   1 
ATOM   5692  C CA  . GLY B 1 291 ? 31.837  -15.379 48.844  1.00 78.72  ? 320 GLY B CA  1 
ATOM   5693  C C   . GLY B 1 291 ? 30.361  -15.398 48.505  1.00 76.29  ? 320 GLY B C   1 
ATOM   5694  O O   . GLY B 1 291 ? 30.015  -15.111 47.348  1.00 68.52  ? 320 GLY B O   1 
ATOM   5695  N N   . LYS B 1 292 ? 29.508  -15.726 49.464  1.00 73.19  ? 321 LYS B N   1 
ATOM   5696  C CA  . LYS B 1 292 ? 28.057  -15.625 49.226  1.00 66.74  ? 321 LYS B CA  1 
ATOM   5697  C C   . LYS B 1 292 ? 27.578  -14.551 50.184  1.00 71.28  ? 321 LYS B C   1 
ATOM   5698  O O   . LYS B 1 292 ? 26.438  -14.076 50.011  1.00 79.70  ? 321 LYS B O   1 
ATOM   5699  C CB  . LYS B 1 292 ? 27.392  -16.952 49.579  1.00 69.97  ? 321 LYS B CB  1 
ATOM   5700  C CG  . LYS B 1 292 ? 26.940  -17.748 48.366  1.00 69.17  ? 321 LYS B CG  1 
ATOM   5701  C CD  . LYS B 1 292 ? 27.843  -17.548 47.156  1.00 66.68  ? 321 LYS B CD  1 
ATOM   5702  C CE  . LYS B 1 292 ? 27.133  -17.843 45.880  1.00 68.11  ? 321 LYS B CE  1 
ATOM   5703  N NZ  . LYS B 1 292 ? 25.688  -17.930 46.092  1.00 67.81  ? 321 LYS B NZ  1 
ATOM   5704  N N   . ASP B 1 293 ? 28.443  -14.195 51.145  1.00 72.97  ? 322 ASP B N   1 
ATOM   5705  C CA  . ASP B 1 293 ? 28.092  -13.250 52.240  1.00 68.61  ? 322 ASP B CA  1 
ATOM   5706  C C   . ASP B 1 293 ? 29.331  -12.385 52.499  1.00 67.31  ? 322 ASP B C   1 
ATOM   5707  O O   . ASP B 1 293 ? 30.079  -12.692 53.446  1.00 66.63  ? 322 ASP B O   1 
ATOM   5708  C CB  . ASP B 1 293 ? 27.588  -14.051 53.433  1.00 66.18  ? 322 ASP B CB  1 
ATOM   5709  C CG  . ASP B 1 293 ? 26.785  -13.267 54.454  1.00 63.76  ? 322 ASP B CG  1 
ATOM   5710  O OD1 . ASP B 1 293 ? 27.129  -12.092 54.688  1.00 69.95  ? 322 ASP B OD1 1 
ATOM   5711  O OD2 . ASP B 1 293 ? 25.824  -13.842 54.998  1.00 65.21  ? 322 ASP B OD2 1 
ATOM   5712  N N   . VAL B 1 294 ? 29.530  -11.323 51.715  1.00 61.55  ? 323 VAL B N   1 
ATOM   5713  C CA  . VAL B 1 294 ? 30.800  -10.544 51.802  1.00 56.57  ? 323 VAL B CA  1 
ATOM   5714  C C   . VAL B 1 294 ? 30.763  -9.420  52.843  1.00 54.39  ? 323 VAL B C   1 
ATOM   5715  O O   . VAL B 1 294 ? 29.663  -9.062  53.298  1.00 51.46  ? 323 VAL B O   1 
ATOM   5716  C CB  . VAL B 1 294 ? 31.066  -10.015 50.383  1.00 60.77  ? 323 VAL B CB  1 
ATOM   5717  C CG1 . VAL B 1 294 ? 30.421  -8.667  50.101  1.00 61.75  ? 323 VAL B CG1 1 
ATOM   5718  C CG2 . VAL B 1 294 ? 32.544  -10.038 50.039  1.00 60.58  ? 323 VAL B CG2 1 
ATOM   5719  N N   . SER B 1 295 ? 31.936  -8.895  53.189  1.00 48.47  ? 324 SER B N   1 
ATOM   5720  C CA  . SER B 1 295 ? 32.038  -7.771  54.144  1.00 47.95  ? 324 SER B CA  1 
ATOM   5721  C C   . SER B 1 295 ? 31.443  -6.509  53.510  1.00 50.42  ? 324 SER B C   1 
ATOM   5722  O O   . SER B 1 295 ? 31.232  -6.495  52.280  1.00 55.43  ? 324 SER B O   1 
ATOM   5723  C CB  . SER B 1 295 ? 33.465  -7.532  54.469  1.00 45.72  ? 324 SER B CB  1 
ATOM   5724  O OG  . SER B 1 295 ? 34.102  -6.847  53.401  1.00 47.67  ? 324 SER B OG  1 
ATOM   5725  N N   . ASP B 1 296 ? 31.306  -5.451  54.297  1.00 49.44  ? 325 ASP B N   1 
ATOM   5726  C CA  . ASP B 1 296 ? 30.696  -4.217  53.755  1.00 45.01  ? 325 ASP B CA  1 
ATOM   5727  C C   . ASP B 1 296 ? 31.741  -3.494  52.904  1.00 42.69  ? 325 ASP B C   1 
ATOM   5728  O O   . ASP B 1 296 ? 31.343  -2.887  51.907  1.00 45.79  ? 325 ASP B O   1 
ATOM   5729  C CB  . ASP B 1 296 ? 30.166  -3.356  54.884  1.00 46.81  ? 325 ASP B CB  1 
ATOM   5730  C CG  . ASP B 1 296 ? 28.830  -3.785  55.469  1.00 46.02  ? 325 ASP B CG  1 
ATOM   5731  O OD1 . ASP B 1 296 ? 28.250  -4.764  54.957  1.00 39.56  ? 325 ASP B OD1 1 
ATOM   5732  O OD2 . ASP B 1 296 ? 28.389  -3.134  56.435  1.00 40.41  ? 325 ASP B OD2 1 
ATOM   5733  N N   . GLU B 1 297 ? 33.018  -3.626  53.242  1.00 44.86  ? 326 GLU B N   1 
ATOM   5734  C CA  . GLU B 1 297 ? 34.093  -2.941  52.481  1.00 42.41  ? 326 GLU B CA  1 
ATOM   5735  C C   . GLU B 1 297 ? 34.299  -3.653  51.131  1.00 43.57  ? 326 GLU B C   1 
ATOM   5736  O O   . GLU B 1 297 ? 34.639  -2.979  50.151  1.00 38.94  ? 326 GLU B O   1 
ATOM   5737  C CB  . GLU B 1 297 ? 35.335  -2.860  53.369  1.00 44.54  ? 326 GLU B CB  1 
ATOM   5738  C CG  . GLU B 1 297 ? 35.434  -1.532  54.117  1.00 48.53  ? 326 GLU B CG  1 
ATOM   5739  C CD  . GLU B 1 297 ? 36.324  -1.452  55.348  1.00 50.63  ? 326 GLU B CD  1 
ATOM   5740  O OE1 . GLU B 1 297 ? 37.561  -1.430  55.191  1.00 51.29  ? 326 GLU B OE1 1 
ATOM   5741  O OE2 . GLU B 1 297 ? 35.781  -1.401  56.472  1.00 51.98  ? 326 GLU B OE2 1 
ATOM   5742  N N   . LYS B 1 298 ? 34.038  -4.961  51.080  1.00 41.59  ? 327 LYS B N   1 
ATOM   5743  C CA  . LYS B 1 298 ? 34.163  -5.708  49.806  1.00 44.77  ? 327 LYS B CA  1 
ATOM   5744  C C   . LYS B 1 298 ? 32.985  -5.390  48.879  1.00 47.83  ? 327 LYS B C   1 
ATOM   5745  O O   . LYS B 1 298 ? 33.170  -5.476  47.647  1.00 52.75  ? 327 LYS B O   1 
ATOM   5746  C CB  . LYS B 1 298 ? 34.228  -7.222  49.982  1.00 47.80  ? 327 LYS B CB  1 
ATOM   5747  C CG  . LYS B 1 298 ? 35.637  -7.794  49.901  1.00 50.94  ? 327 LYS B CG  1 
ATOM   5748  C CD  . LYS B 1 298 ? 36.558  -7.350  51.033  1.00 50.46  ? 327 LYS B CD  1 
ATOM   5749  C CE  . LYS B 1 298 ? 37.022  -8.496  51.878  1.00 51.57  ? 327 LYS B CE  1 
ATOM   5750  N NZ  . LYS B 1 298 ? 36.579  -8.381  53.271  1.00 51.93  ? 327 LYS B NZ  1 
ATOM   5751  N N   . LEU B 1 299 ? 31.819  -5.109  49.438  1.00 46.97  ? 328 LEU B N   1 
ATOM   5752  C CA  . LEU B 1 299 ? 30.674  -4.687  48.594  1.00 44.59  ? 328 LEU B CA  1 
ATOM   5753  C C   . LEU B 1 299 ? 31.006  -3.307  48.029  1.00 37.61  ? 328 LEU B C   1 
ATOM   5754  O O   . LEU B 1 299 ? 30.783  -3.092  46.839  1.00 31.08  ? 328 LEU B O   1 
ATOM   5755  C CB  . LEU B 1 299 ? 29.417  -4.636  49.460  1.00 49.38  ? 328 LEU B CB  1 
ATOM   5756  C CG  . LEU B 1 299 ? 28.093  -4.815  48.722  1.00 53.32  ? 328 LEU B CG  1 
ATOM   5757  C CD1 . LEU B 1 299 ? 28.274  -5.868  47.645  1.00 58.05  ? 328 LEU B CD1 1 
ATOM   5758  C CD2 . LEU B 1 299 ? 27.031  -5.226  49.722  1.00 54.56  ? 328 LEU B CD2 1 
ATOM   5759  N N   . ARG B 1 300 ? 31.525  -2.433  48.885  1.00 37.70  ? 329 ARG B N   1 
ATOM   5760  C CA  . ARG B 1 300 ? 31.868  -1.056  48.462  1.00 36.77  ? 329 ARG B CA  1 
ATOM   5761  C C   . ARG B 1 300 ? 32.880  -1.145  47.321  1.00 34.44  ? 329 ARG B C   1 
ATOM   5762  O O   . ARG B 1 300 ? 32.819  -0.347  46.398  1.00 32.00  ? 329 ARG B O   1 
ATOM   5763  C CB  . ARG B 1 300 ? 32.418  -0.226  49.619  1.00 39.33  ? 329 ARG B CB  1 
ATOM   5764  C CG  . ARG B 1 300 ? 31.374  0.370   50.547  1.00 39.56  ? 329 ARG B CG  1 
ATOM   5765  C CD  . ARG B 1 300 ? 32.048  0.860   51.808  1.00 43.35  ? 329 ARG B CD  1 
ATOM   5766  N NE  . ARG B 1 300 ? 31.096  1.422   52.769  1.00 41.12  ? 329 ARG B NE  1 
ATOM   5767  C CZ  . ARG B 1 300 ? 30.663  0.750   53.818  1.00 37.44  ? 329 ARG B CZ  1 
ATOM   5768  N NH1 . ARG B 1 300 ? 31.146  -0.451  54.056  1.00 36.99  ? 329 ARG B NH1 1 
ATOM   5769  N NH2 . ARG B 1 300 ? 29.756  1.275   54.617  1.00 34.98  ? 329 ARG B NH2 1 
ATOM   5770  N N   . ASP B 1 301 ? 33.758  -2.125  47.403  1.00 35.58  ? 330 ASP B N   1 
ATOM   5771  C CA  . ASP B 1 301 ? 34.760  -2.309  46.330  1.00 35.92  ? 330 ASP B CA  1 
ATOM   5772  C C   . ASP B 1 301 ? 34.064  -2.661  45.021  1.00 33.36  ? 330 ASP B C   1 
ATOM   5773  O O   . ASP B 1 301 ? 34.352  -2.016  44.011  1.00 29.80  ? 330 ASP B O   1 
ATOM   5774  C CB  . ASP B 1 301 ? 35.724  -3.419  46.695  1.00 36.62  ? 330 ASP B CB  1 
ATOM   5775  C CG  . ASP B 1 301 ? 36.861  -3.018  47.625  1.00 39.35  ? 330 ASP B CG  1 
ATOM   5776  O OD1 . ASP B 1 301 ? 36.989  -1.813  47.908  1.00 33.34  ? 330 ASP B OD1 1 
ATOM   5777  O OD2 . ASP B 1 301 ? 37.607  -3.918  48.059  1.00 39.13  ? 330 ASP B OD2 1 
ATOM   5778  N N   . TYR B 1 302 ? 33.187  -3.662  45.064  1.00 32.64  ? 331 TYR B N   1 
ATOM   5779  C CA  . TYR B 1 302 ? 32.543  -4.102  43.842  1.00 32.02  ? 331 TYR B CA  1 
ATOM   5780  C C   . TYR B 1 302 ? 31.722  -2.958  43.239  1.00 30.10  ? 331 TYR B C   1 
ATOM   5781  O O   . TYR B 1 302 ? 31.719  -2.760  42.024  1.00 25.63  ? 331 TYR B O   1 
ATOM   5782  C CB  . TYR B 1 302 ? 31.699  -5.347  44.116  1.00 34.10  ? 331 TYR B CB  1 
ATOM   5783  C CG  . TYR B 1 302 ? 31.000  -5.922  42.911  1.00 34.39  ? 331 TYR B CG  1 
ATOM   5784  C CD1 . TYR B 1 302 ? 31.653  -6.776  42.030  1.00 37.89  ? 331 TYR B CD1 1 
ATOM   5785  C CD2 . TYR B 1 302 ? 29.666  -5.628  42.658  1.00 34.12  ? 331 TYR B CD2 1 
ATOM   5786  C CE1 . TYR B 1 302 ? 31.000  -7.331  40.938  1.00 33.44  ? 331 TYR B CE1 1 
ATOM   5787  C CE2 . TYR B 1 302 ? 29.012  -6.157  41.558  1.00 31.39  ? 331 TYR B CE2 1 
ATOM   5788  C CZ  . TYR B 1 302 ? 29.670  -7.018  40.701  1.00 30.97  ? 331 TYR B CZ  1 
ATOM   5789  O OH  . TYR B 1 302 ? 28.969  -7.529  39.632  1.00 32.37  ? 331 TYR B OH  1 
ATOM   5790  N N   . ILE B 1 303 ? 31.029  -2.195  44.089  1.00 29.57  ? 332 ILE B N   1 
ATOM   5791  C CA  . ILE B 1 303 ? 30.205  -1.115  43.575  1.00 30.87  ? 332 ILE B CA  1 
ATOM   5792  C C   . ILE B 1 303 ? 31.120  -0.078  42.930  1.00 29.33  ? 332 ILE B C   1 
ATOM   5793  O O   . ILE B 1 303 ? 30.791  0.455   41.881  1.00 26.53  ? 332 ILE B O   1 
ATOM   5794  C CB  . ILE B 1 303 ? 29.293  -0.485  44.645  1.00 32.24  ? 332 ILE B CB  1 
ATOM   5795  C CG1 . ILE B 1 303 ? 30.064  0.398   45.618  1.00 35.80  ? 332 ILE B CG1 1 
ATOM   5796  C CG2 . ILE B 1 303 ? 28.451  -1.533  45.360  1.00 26.12  ? 332 ILE B CG2 1 
ATOM   5797  C CD1 . ILE B 1 303 ? 30.259  1.815   45.123  1.00 39.48  ? 332 ILE B CD1 1 
ATOM   5798  N N   . TRP B 1 304 ? 32.275  0.178   43.558  1.00 26.83  ? 333 TRP B N   1 
ATOM   5799  C CA  . TRP B 1 304 ? 33.172  1.216   43.088  1.00 30.62  ? 333 TRP B CA  1 
ATOM   5800  C C   . TRP B 1 304 ? 33.751  0.820   41.732  1.00 29.31  ? 333 TRP B C   1 
ATOM   5801  O O   . TRP B 1 304 ? 33.818  1.652   40.826  1.00 30.92  ? 333 TRP B O   1 
ATOM   5802  C CB  . TRP B 1 304 ? 34.220  1.532   44.151  1.00 29.51  ? 333 TRP B CB  1 
ATOM   5803  C CG  . TRP B 1 304 ? 33.835  2.689   45.027  1.00 32.01  ? 333 TRP B CG  1 
ATOM   5804  C CD1 . TRP B 1 304 ? 33.679  2.673   46.385  1.00 29.40  ? 333 TRP B CD1 1 
ATOM   5805  C CD2 . TRP B 1 304 ? 33.566  4.043   44.614  1.00 30.67  ? 333 TRP B CD2 1 
ATOM   5806  N NE1 . TRP B 1 304 ? 33.336  3.918   46.842  1.00 29.76  ? 333 TRP B NE1 1 
ATOM   5807  C CE2 . TRP B 1 304 ? 33.270  4.780   45.780  1.00 30.40  ? 333 TRP B CE2 1 
ATOM   5808  C CE3 . TRP B 1 304 ? 33.532  4.704   43.380  1.00 30.49  ? 333 TRP B CE3 1 
ATOM   5809  C CZ2 . TRP B 1 304 ? 32.955  6.141   45.744  1.00 31.62  ? 333 TRP B CZ2 1 
ATOM   5810  C CZ3 . TRP B 1 304 ? 33.244  6.050   43.353  1.00 29.97  ? 333 TRP B CZ3 1 
ATOM   5811  C CH2 . TRP B 1 304 ? 32.942  6.754   44.518  1.00 31.29  ? 333 TRP B CH2 1 
ATOM   5812  N N   . ASN B 1 305 ? 34.038  -0.476  41.549  1.00 30.40  ? 334 ASN B N   1 
ATOM   5813  C CA  . ASN B 1 305 ? 34.569  -0.955  40.273  1.00 34.64  ? 334 ASN B CA  1 
ATOM   5814  C C   . ASN B 1 305 ? 33.529  -0.751  39.159  1.00 30.26  ? 334 ASN B C   1 
ATOM   5815  O O   . ASN B 1 305 ? 33.850  -0.392  38.030  1.00 29.18  ? 334 ASN B O   1 
ATOM   5816  C CB  . ASN B 1 305 ? 35.096  -2.391  40.400  1.00 38.44  ? 334 ASN B CB  1 
ATOM   5817  C CG  . ASN B 1 305 ? 34.340  -3.465  39.640  1.00 44.74  ? 334 ASN B CG  1 
ATOM   5818  O OD1 . ASN B 1 305 ? 34.440  -3.568  38.421  1.00 36.48  ? 334 ASN B OD1 1 
ATOM   5819  N ND2 . ASN B 1 305 ? 33.663  -4.346  40.365  1.00 51.90  ? 334 ASN B ND2 1 
ATOM   5820  N N   . THR B 1 306 ? 32.259  -0.949  39.494  1.00 27.69  ? 335 THR B N   1 
ATOM   5821  C CA  . THR B 1 306 ? 31.174  -0.688  38.559  1.00 26.57  ? 335 THR B CA  1 
ATOM   5822  C C   . THR B 1 306 ? 31.153  0.783   38.153  1.00 23.02  ? 335 THR B C   1 
ATOM   5823  O O   . THR B 1 306 ? 31.108  1.092   36.965  1.00 22.84  ? 335 THR B O   1 
ATOM   5824  C CB  . THR B 1 306 ? 29.858  -1.161  39.180  1.00 26.52  ? 335 THR B CB  1 
ATOM   5825  O OG1 . THR B 1 306 ? 30.003  -2.584  39.183  1.00 25.66  ? 335 THR B OG1 1 
ATOM   5826  C CG2 . THR B 1 306 ? 28.623  -0.707  38.432  1.00 27.99  ? 335 THR B CG2 1 
ATOM   5827  N N   . LEU B 1 307 ? 31.160  1.669   39.136  1.00 21.71  ? 336 LEU B N   1 
ATOM   5828  C CA  . LEU B 1 307 ? 30.979  3.093   38.893  1.00 21.19  ? 336 LEU B CA  1 
ATOM   5829  C C   . LEU B 1 307 ? 32.203  3.689   38.188  1.00 24.13  ? 336 LEU B C   1 
ATOM   5830  O O   . LEU B 1 307 ? 32.049  4.557   37.334  1.00 22.90  ? 336 LEU B O   1 
ATOM   5831  C CB  . LEU B 1 307 ? 30.734  3.803   40.227  1.00 21.89  ? 336 LEU B CB  1 
ATOM   5832  C CG  . LEU B 1 307 ? 29.422  3.479   40.951  1.00 22.25  ? 336 LEU B CG  1 
ATOM   5833  C CD1 . LEU B 1 307 ? 29.299  4.279   42.244  1.00 23.88  ? 336 LEU B CD1 1 
ATOM   5834  C CD2 . LEU B 1 307 ? 28.205  3.716   40.075  1.00 22.58  ? 336 LEU B CD2 1 
ATOM   5835  N N   . ASN B 1 308 ? 33.418  3.224   38.514  1.00 24.46  ? 337 ASN B N   1 
ATOM   5836  C CA  . ASN B 1 308 ? 34.617  3.771   37.874  1.00 27.87  ? 337 ASN B CA  1 
ATOM   5837  C C   . ASN B 1 308 ? 34.814  3.212   36.457  1.00 26.10  ? 337 ASN B C   1 
ATOM   5838  O O   . ASN B 1 308 ? 35.659  3.704   35.704  1.00 27.40  ? 337 ASN B O   1 
ATOM   5839  C CB  . ASN B 1 308 ? 35.880  3.555   38.717  1.00 29.85  ? 337 ASN B CB  1 
ATOM   5840  C CG  . ASN B 1 308 ? 35.863  4.300   40.040  1.00 35.50  ? 337 ASN B CG  1 
ATOM   5841  O OD1 . ASN B 1 308 ? 35.402  5.440   40.135  1.00 35.04  ? 337 ASN B OD1 1 
ATOM   5842  N ND2 . ASN B 1 308 ? 36.346  3.654   41.088  1.00 36.61  ? 337 ASN B ND2 1 
ATOM   5843  N N   . SER B 1 309 ? 34.031  2.201   36.071  1.00 25.17  ? 338 SER B N   1 
ATOM   5844  C CA  . SER B 1 309 ? 34.078  1.656   34.720  1.00 24.82  ? 338 SER B CA  1 
ATOM   5845  C C   . SER B 1 309 ? 33.100  2.348   33.759  1.00 26.55  ? 338 SER B C   1 
ATOM   5846  O O   . SER B 1 309 ? 32.966  1.919   32.597  1.00 25.60  ? 338 SER B O   1 
ATOM   5847  C CB  . SER B 1 309 ? 33.804  0.178   34.759  1.00 24.10  ? 338 SER B CB  1 
ATOM   5848  O OG  . SER B 1 309 ? 34.749  -0.487  35.560  1.00 28.94  ? 338 SER B OG  1 
ATOM   5849  N N   . GLY B 1 310 ? 32.422  3.412   34.231  1.00 21.66  ? 339 GLY B N   1 
ATOM   5850  C CA  . GLY B 1 310 ? 31.457  4.140   33.411  1.00 23.13  ? 339 GLY B CA  1 
ATOM   5851  C C   . GLY B 1 310 ? 30.152  3.368   33.226  1.00 23.14  ? 339 GLY B C   1 
ATOM   5852  O O   . GLY B 1 310 ? 29.499  3.461   32.188  1.00 22.29  ? 339 GLY B O   1 
ATOM   5853  N N   . ARG B 1 311 ? 29.838  2.538   34.230  1.00 23.63  ? 340 ARG B N   1 
ATOM   5854  C CA  . ARG B 1 311 ? 28.608  1.771   34.274  1.00 24.66  ? 340 ARG B CA  1 
ATOM   5855  C C   . ARG B 1 311 ? 27.748  2.286   35.426  1.00 25.55  ? 340 ARG B C   1 
ATOM   5856  O O   . ARG B 1 311 ? 28.268  2.899   36.352  1.00 21.96  ? 340 ARG B O   1 
ATOM   5857  C CB  . ARG B 1 311 ? 28.940  0.286   34.456  1.00 26.10  ? 340 ARG B CB  1 
ATOM   5858  C CG  . ARG B 1 311 ? 29.966  -0.254  33.476  1.00 32.27  ? 340 ARG B CG  1 
ATOM   5859  C CD  . ARG B 1 311 ? 30.131  -1.769  33.514  1.00 36.25  ? 340 ARG B CD  1 
ATOM   5860  N NE  . ARG B 1 311 ? 30.641  -2.277  34.781  1.00 46.04  ? 340 ARG B NE  1 
ATOM   5861  C CZ  . ARG B 1 311 ? 30.054  -3.230  35.509  1.00 54.31  ? 340 ARG B CZ  1 
ATOM   5862  N NH1 . ARG B 1 311 ? 28.993  -3.867  35.039  1.00 56.20  ? 340 ARG B NH1 1 
ATOM   5863  N NH2 . ARG B 1 311 ? 30.540  -3.562  36.695  1.00 55.74  ? 340 ARG B NH2 1 
ATOM   5864  N N   . VAL B 1 312 ? 26.433  2.029   35.366  1.00 27.11  ? 341 VAL B N   1 
ATOM   5865  C CA  . VAL B 1 312 ? 25.537  2.383   36.463  1.00 26.08  ? 341 VAL B CA  1 
ATOM   5866  C C   . VAL B 1 312 ? 25.371  1.158   37.359  1.00 24.64  ? 341 VAL B C   1 
ATOM   5867  O O   . VAL B 1 312 ? 25.642  0.029   36.940  1.00 23.25  ? 341 VAL B O   1 
ATOM   5868  C CB  . VAL B 1 312 ? 24.198  2.946   35.929  1.00 29.43  ? 341 VAL B CB  1 
ATOM   5869  C CG1 . VAL B 1 312 ? 24.406  4.216   35.115  1.00 26.91  ? 341 VAL B CG1 1 
ATOM   5870  C CG2 . VAL B 1 312 ? 23.442  1.923   35.112  1.00 28.17  ? 341 VAL B CG2 1 
ATOM   5871  N N   . VAL B 1 313 ? 25.000  1.395   38.631  1.00 25.22  ? 342 VAL B N   1 
ATOM   5872  C CA  . VAL B 1 313 ? 24.495  0.336   39.506  1.00 25.19  ? 342 VAL B CA  1 
ATOM   5873  C C   . VAL B 1 313 ? 23.048  0.080   39.091  1.00 25.02  ? 342 VAL B C   1 
ATOM   5874  O O   . VAL B 1 313 ? 22.245  1.003   39.104  1.00 23.44  ? 342 VAL B O   1 
ATOM   5875  C CB  . VAL B 1 313 ? 24.581  0.711   40.998  1.00 25.07  ? 342 VAL B CB  1 
ATOM   5876  C CG1 . VAL B 1 313 ? 24.098  -0.411  41.916  1.00 24.84  ? 342 VAL B CG1 1 
ATOM   5877  C CG2 . VAL B 1 313 ? 25.992  1.134   41.369  1.00 27.76  ? 342 VAL B CG2 1 
ATOM   5878  N N   . PRO B 1 314 ? 22.695  -1.138  38.622  1.00 21.70  ? 343 PRO B N   1 
ATOM   5879  C CA  . PRO B 1 314 ? 21.318  -1.446  38.227  1.00 22.76  ? 343 PRO B CA  1 
ATOM   5880  C C   . PRO B 1 314 ? 20.351  -1.383  39.407  1.00 22.95  ? 343 PRO B C   1 
ATOM   5881  O O   . PRO B 1 314 ? 20.682  -1.822  40.511  1.00 23.87  ? 343 PRO B O   1 
ATOM   5882  C CB  . PRO B 1 314 ? 21.418  -2.862  37.638  1.00 23.89  ? 343 PRO B CB  1 
ATOM   5883  C CG  . PRO B 1 314 ? 22.698  -3.435  38.211  1.00 23.45  ? 343 PRO B CG  1 
ATOM   5884  C CD  . PRO B 1 314 ? 23.629  -2.253  38.376  1.00 23.09  ? 343 PRO B CD  1 
ATOM   5885  N N   . GLY B 1 315 ? 19.179  -0.799  39.153  1.00 23.37  ? 344 GLY B N   1 
ATOM   5886  C CA  . GLY B 1 315 ? 18.087  -0.801  40.095  1.00 24.27  ? 344 GLY B CA  1 
ATOM   5887  C C   . GLY B 1 315 ? 18.163  0.347   41.085  1.00 23.68  ? 344 GLY B C   1 
ATOM   5888  O O   . GLY B 1 315 ? 17.418  0.356   42.053  1.00 25.72  ? 344 GLY B O   1 
ATOM   5889  N N   . TYR B 1 316 ? 19.050  1.306   40.837  1.00 22.96  ? 345 TYR B N   1 
ATOM   5890  C CA  . TYR B 1 316 ? 19.299  2.365   41.798  1.00 23.31  ? 345 TYR B CA  1 
ATOM   5891  C C   . TYR B 1 316 ? 19.152  3.692   41.062  1.00 24.59  ? 345 TYR B C   1 
ATOM   5892  O O   . TYR B 1 316 ? 19.487  3.781   39.891  1.00 23.98  ? 345 TYR B O   1 
ATOM   5893  C CB  . TYR B 1 316 ? 20.658  2.158   42.493  1.00 23.18  ? 345 TYR B CB  1 
ATOM   5894  C CG  . TYR B 1 316 ? 20.568  1.358   43.776  1.00 24.33  ? 345 TYR B CG  1 
ATOM   5895  C CD1 . TYR B 1 316 ? 20.405  -0.018  43.748  1.00 21.46  ? 345 TYR B CD1 1 
ATOM   5896  C CD2 . TYR B 1 316 ? 20.596  1.972   45.021  1.00 24.61  ? 345 TYR B CD2 1 
ATOM   5897  C CE1 . TYR B 1 316 ? 20.312  -0.763  44.910  1.00 24.27  ? 345 TYR B CE1 1 
ATOM   5898  C CE2 . TYR B 1 316 ? 20.472  1.235   46.196  1.00 24.77  ? 345 TYR B CE2 1 
ATOM   5899  C CZ  . TYR B 1 316 ? 20.350  -0.142  46.140  1.00 23.75  ? 345 TYR B CZ  1 
ATOM   5900  O OH  . TYR B 1 316 ? 20.207  -0.941  47.259  1.00 24.42  ? 345 TYR B OH  1 
ATOM   5901  N N   . GLY B 1 317 ? 18.630  4.714   41.740  1.00 23.52  ? 346 GLY B N   1 
ATOM   5902  C CA  . GLY B 1 317 ? 18.373  5.986   41.076  1.00 22.93  ? 346 GLY B CA  1 
ATOM   5903  C C   . GLY B 1 317 ? 16.981  6.040   40.449  1.00 23.68  ? 346 GLY B C   1 
ATOM   5904  O O   . GLY B 1 317 ? 16.315  5.018   40.257  1.00 23.35  ? 346 GLY B O   1 
ATOM   5905  N N   . HIS B 1 318 ? 16.527  7.262   40.146  1.00 21.62  ? 347 HIS B N   1 
ATOM   5906  C CA  . HIS B 1 318 ? 15.238  7.446   39.526  1.00 21.26  ? 347 HIS B CA  1 
ATOM   5907  C C   . HIS B 1 318 ? 15.186  8.892   39.043  1.00 23.82  ? 347 HIS B C   1 
ATOM   5908  O O   . HIS B 1 318 ? 15.834  9.734   39.652  1.00 21.20  ? 347 HIS B O   1 
ATOM   5909  C CB  . HIS B 1 318 ? 14.124  7.058   40.510  1.00 21.49  ? 347 HIS B CB  1 
ATOM   5910  C CG  . HIS B 1 318 ? 12.823  6.832   39.848  1.00 20.87  ? 347 HIS B CG  1 
ATOM   5911  N ND1 . HIS B 1 318 ? 12.345  5.610   39.460  1.00 21.67  ? 347 HIS B ND1 1 
ATOM   5912  C CD2 . HIS B 1 318 ? 11.911  7.713   39.432  1.00 18.02  ? 347 HIS B CD2 1 
ATOM   5913  C CE1 . HIS B 1 318 ? 11.170  5.776   38.860  1.00 20.82  ? 347 HIS B CE1 1 
ATOM   5914  N NE2 . HIS B 1 318 ? 10.905  7.053   38.832  1.00 21.17  ? 347 HIS B NE2 1 
ATOM   5915  N N   . ALA B 1 319 ? 14.419  9.159   37.970  1.00 24.44  ? 348 ALA B N   1 
ATOM   5916  C CA  . ALA B 1 319 ? 14.334  10.496  37.396  1.00 26.42  ? 348 ALA B CA  1 
ATOM   5917  C C   . ALA B 1 319 ? 13.542  11.443  38.291  1.00 26.85  ? 348 ALA B C   1 
ATOM   5918  O O   . ALA B 1 319 ? 13.729  12.666  38.211  1.00 23.60  ? 348 ALA B O   1 
ATOM   5919  C CB  . ALA B 1 319 ? 13.736  10.441  35.995  1.00 29.80  ? 348 ALA B CB  1 
ATOM   5920  N N   . VAL B 1 320 ? 12.663  10.897  39.146  1.00 27.85  ? 349 VAL B N   1 
ATOM   5921  C CA  . VAL B 1 320 ? 11.668  11.705  39.844  1.00 26.62  ? 349 VAL B CA  1 
ATOM   5922  C C   . VAL B 1 320 ? 11.583  11.374  41.341  1.00 26.69  ? 349 VAL B C   1 
ATOM   5923  O O   . VAL B 1 320 ? 11.448  12.283  42.155  1.00 26.58  ? 349 VAL B O   1 
ATOM   5924  C CB  . VAL B 1 320 ? 10.293  11.643  39.146  1.00 27.88  ? 349 VAL B CB  1 
ATOM   5925  C CG1 . VAL B 1 320 ? 10.014  10.295  38.510  1.00 34.12  ? 349 VAL B CG1 1 
ATOM   5926  C CG2 . VAL B 1 320 ? 9.157   12.049  40.076  1.00 26.95  ? 349 VAL B CG2 1 
ATOM   5927  N N   . LEU B 1 321 ? 11.565  10.093  41.714  1.00 25.11  ? 350 LEU B N   1 
ATOM   5928  C CA  . LEU B 1 321 ? 11.616  9.656   43.110  1.00 28.35  ? 350 LEU B CA  1 
ATOM   5929  C C   . LEU B 1 321 ? 12.851  10.245  43.800  1.00 26.39  ? 350 LEU B C   1 
ATOM   5930  O O   . LEU B 1 321 ? 13.940  10.191  43.240  1.00 25.56  ? 350 LEU B O   1 
ATOM   5931  C CB  . LEU B 1 321 ? 11.673  8.118   43.069  1.00 31.71  ? 350 LEU B CB  1 
ATOM   5932  C CG  . LEU B 1 321 ? 10.861  7.302   44.075  1.00 35.50  ? 350 LEU B CG  1 
ATOM   5933  C CD1 . LEU B 1 321 ? 9.602   8.008   44.547  1.00 33.35  ? 350 LEU B CD1 1 
ATOM   5934  C CD2 . LEU B 1 321 ? 10.507  5.955   43.454  1.00 36.32  ? 350 LEU B CD2 1 
ATOM   5935  N N   . ARG B 1 322 ? 12.679  10.817  45.003  1.00 27.51  ? 351 ARG B N   1 
ATOM   5936  C CA  . ARG B 1 322 ? 13.796  11.359  45.768  1.00 33.28  ? 351 ARG B CA  1 
ATOM   5937  C C   . ARG B 1 322 ? 13.965  10.644  47.117  1.00 34.90  ? 351 ARG B C   1 
ATOM   5938  O O   . ARG B 1 322 ? 14.716  11.111  47.973  1.00 33.36  ? 351 ARG B O   1 
ATOM   5939  C CB  . ARG B 1 322 ? 13.622  12.873  45.940  1.00 33.27  ? 351 ARG B CB  1 
ATOM   5940  C CG  . ARG B 1 322 ? 13.771  13.660  44.646  1.00 36.44  ? 351 ARG B CG  1 
ATOM   5941  C CD  . ARG B 1 322 ? 15.094  13.403  43.942  1.00 42.40  ? 351 ARG B CD  1 
ATOM   5942  N NE  . ARG B 1 322 ? 15.123  13.938  42.583  1.00 43.22  ? 351 ARG B NE  1 
ATOM   5943  C CZ  . ARG B 1 322 ? 15.313  13.210  41.482  1.00 43.16  ? 351 ARG B CZ  1 
ATOM   5944  N NH1 . ARG B 1 322 ? 15.275  13.788  40.293  1.00 37.36  ? 351 ARG B NH1 1 
ATOM   5945  N NH2 . ARG B 1 322 ? 15.531  11.906  41.569  1.00 38.56  ? 351 ARG B NH2 1 
ATOM   5946  N N   . LYS B 1 323 ? 13.299  9.492   47.278  1.00 36.58  ? 352 LYS B N   1 
ATOM   5947  C CA  . LYS B 1 323 ? 13.507  8.588   48.398  1.00 33.79  ? 352 LYS B CA  1 
ATOM   5948  C C   . LYS B 1 323 ? 13.399  7.170   47.863  1.00 28.11  ? 352 LYS B C   1 
ATOM   5949  O O   . LYS B 1 323 ? 13.214  6.963   46.669  1.00 26.28  ? 352 LYS B O   1 
ATOM   5950  C CB  . LYS B 1 323 ? 12.422  8.698   49.479  1.00 37.99  ? 352 LYS B CB  1 
ATOM   5951  C CG  . LYS B 1 323 ? 11.868  10.088  49.749  1.00 48.80  ? 352 LYS B CG  1 
ATOM   5952  C CD  . LYS B 1 323 ? 11.140  10.199  51.091  1.00 56.58  ? 352 LYS B CD  1 
ATOM   5953  C CE  . LYS B 1 323 ? 10.242  9.019   51.434  1.00 60.26  ? 352 LYS B CE  1 
ATOM   5954  N NZ  . LYS B 1 323 ? 9.386   9.270   52.628  1.00 60.35  ? 352 LYS B NZ  1 
ATOM   5955  N N   . THR B 1 324 ? 13.370  6.217   48.788  1.00 24.42  ? 353 THR B N   1 
ATOM   5956  C CA  . THR B 1 324 ? 13.193  4.831   48.435  1.00 22.69  ? 353 THR B CA  1 
ATOM   5957  C C   . THR B 1 324 ? 11.828  4.652   47.772  1.00 23.79  ? 353 THR B C   1 
ATOM   5958  O O   . THR B 1 324 ? 10.837  5.209   48.234  1.00 22.52  ? 353 THR B O   1 
ATOM   5959  C CB  . THR B 1 324 ? 13.384  3.968   49.687  1.00 21.81  ? 353 THR B CB  1 
ATOM   5960  O OG1 . THR B 1 324 ? 14.706  4.181   50.205  1.00 24.37  ? 353 THR B OG1 1 
ATOM   5961  C CG2 . THR B 1 324 ? 13.215  2.494   49.403  1.00 22.57  ? 353 THR B CG2 1 
ATOM   5962  N N   . ASP B 1 325 ? 11.801  3.842   46.696  1.00 22.50  ? 354 ASP B N   1 
ATOM   5963  C CA  . ASP B 1 325 ? 10.582  3.508   45.981  1.00 23.90  ? 354 ASP B CA  1 
ATOM   5964  C C   . ASP B 1 325 ? 9.688   2.681   46.893  1.00 23.20  ? 354 ASP B C   1 
ATOM   5965  O O   . ASP B 1 325 ? 10.150  1.681   47.423  1.00 22.84  ? 354 ASP B O   1 
ATOM   5966  C CB  . ASP B 1 325 ? 10.904  2.669   44.740  1.00 23.59  ? 354 ASP B CB  1 
ATOM   5967  C CG  . ASP B 1 325 ? 9.827   2.567   43.670  1.00 25.72  ? 354 ASP B CG  1 
ATOM   5968  O OD1 . ASP B 1 325 ? 8.593   2.567   44.005  1.00 24.63  ? 354 ASP B OD1 1 
ATOM   5969  O OD2 . ASP B 1 325 ? 10.235  2.411   42.491  1.00 26.68  ? 354 ASP B OD2 1 
ATOM   5970  N N   . PRO B 1 326 ? 8.395   3.026   47.102  1.00 22.35  ? 355 PRO B N   1 
ATOM   5971  C CA  . PRO B 1 326 ? 7.513   2.139   47.859  1.00 22.78  ? 355 PRO B CA  1 
ATOM   5972  C C   . PRO B 1 326 ? 7.366   0.768   47.208  1.00 20.37  ? 355 PRO B C   1 
ATOM   5973  O O   . PRO B 1 326 ? 7.052   -0.210  47.878  1.00 20.75  ? 355 PRO B O   1 
ATOM   5974  C CB  . PRO B 1 326 ? 6.193   2.921   47.968  1.00 23.86  ? 355 PRO B CB  1 
ATOM   5975  C CG  . PRO B 1 326 ? 6.270   3.931   46.831  1.00 26.20  ? 355 PRO B CG  1 
ATOM   5976  C CD  . PRO B 1 326 ? 7.742   4.281   46.708  1.00 24.00  ? 355 PRO B CD  1 
ATOM   5977  N N   . ARG B 1 327 ? 7.549   0.674   45.890  1.00 19.81  ? 356 ARG B N   1 
ATOM   5978  C CA  . ARG B 1 327 ? 7.468   -0.626  45.246  1.00 19.12  ? 356 ARG B CA  1 
ATOM   5979  C C   . ARG B 1 327 ? 8.658   -1.462  45.707  1.00 20.09  ? 356 ARG B C   1 
ATOM   5980  O O   . ARG B 1 327 ? 8.570   -2.680  45.749  1.00 21.42  ? 356 ARG B O   1 
ATOM   5981  C CB  . ARG B 1 327 ? 7.480   -0.516  43.715  1.00 19.34  ? 356 ARG B CB  1 
ATOM   5982  C CG  . ARG B 1 327 ? 6.227   0.095   43.111  1.00 20.61  ? 356 ARG B CG  1 
ATOM   5983  C CD  . ARG B 1 327 ? 6.369   0.428   41.638  1.00 21.17  ? 356 ARG B CD  1 
ATOM   5984  N NE  . ARG B 1 327 ? 7.463   1.342   41.408  1.00 22.05  ? 356 ARG B NE  1 
ATOM   5985  C CZ  . ARG B 1 327 ? 8.035   1.534   40.221  1.00 21.78  ? 356 ARG B CZ  1 
ATOM   5986  N NH1 . ARG B 1 327 ? 7.478   1.048   39.124  1.00 21.93  ? 356 ARG B NH1 1 
ATOM   5987  N NH2 . ARG B 1 327 ? 9.171   2.200   40.143  1.00 23.93  ? 356 ARG B NH2 1 
ATOM   5988  N N   . TYR B 1 328 ? 9.768   -0.820  46.056  1.00 20.80  ? 357 TYR B N   1 
ATOM   5989  C CA  . TYR B 1 328 ? 10.880  -1.546  46.687  1.00 22.41  ? 357 TYR B CA  1 
ATOM   5990  C C   . TYR B 1 328 ? 10.496  -2.022  48.091  1.00 24.51  ? 357 TYR B C   1 
ATOM   5991  O O   . TYR B 1 328 ? 10.744  -3.168  48.450  1.00 25.98  ? 357 TYR B O   1 
ATOM   5992  C CB  . TYR B 1 328 ? 12.136  -0.679  46.805  1.00 23.33  ? 357 TYR B CB  1 
ATOM   5993  C CG  . TYR B 1 328 ? 13.385  -1.366  47.300  1.00 25.36  ? 357 TYR B CG  1 
ATOM   5994  C CD1 . TYR B 1 328 ? 14.269  -1.978  46.417  1.00 25.32  ? 357 TYR B CD1 1 
ATOM   5995  C CD2 . TYR B 1 328 ? 13.754  -1.299  48.639  1.00 27.35  ? 357 TYR B CD2 1 
ATOM   5996  C CE1 . TYR B 1 328 ? 15.442  -2.580  46.873  1.00 26.89  ? 357 TYR B CE1 1 
ATOM   5997  C CE2 . TYR B 1 328 ? 14.926  -1.876  49.109  1.00 26.70  ? 357 TYR B CE2 1 
ATOM   5998  C CZ  . TYR B 1 328 ? 15.770  -2.528  48.221  1.00 26.65  ? 357 TYR B CZ  1 
ATOM   5999  O OH  . TYR B 1 328 ? 16.933  -3.107  48.670  1.00 29.05  ? 357 TYR B OH  1 
ATOM   6000  N N   . THR B 1 329 ? 9.958   -1.118  48.913  1.00 25.47  ? 358 THR B N   1 
ATOM   6001  C CA  . THR B 1 329 ? 9.632   -1.438  50.295  1.00 28.10  ? 358 THR B CA  1 
ATOM   6002  C C   . THR B 1 329 ? 8.644   -2.598  50.336  1.00 27.60  ? 358 THR B C   1 
ATOM   6003  O O   . THR B 1 329 ? 8.821   -3.562  51.074  1.00 29.53  ? 358 THR B O   1 
ATOM   6004  C CB  . THR B 1 329 ? 9.074   -0.197  51.006  1.00 31.15  ? 358 THR B CB  1 
ATOM   6005  O OG1 . THR B 1 329 ? 10.020  0.857   50.876  1.00 33.60  ? 358 THR B OG1 1 
ATOM   6006  C CG2 . THR B 1 329 ? 8.772   -0.425  52.468  1.00 29.40  ? 358 THR B CG2 1 
ATOM   6007  N N   . CYS B 1 330 ? 7.595   -2.500  49.515  1.00 28.62  ? 359 CYS B N   1 
ATOM   6008  C CA  . CYS B 1 330 ? 6.547   -3.500  49.466  1.00 28.83  ? 359 CYS B CA  1 
ATOM   6009  C C   . CYS B 1 330 ? 7.115   -4.866  49.071  1.00 27.63  ? 359 CYS B C   1 
ATOM   6010  O O   . CYS B 1 330 ? 6.658   -5.891  49.570  1.00 24.86  ? 359 CYS B O   1 
ATOM   6011  C CB  . CYS B 1 330 ? 5.438   -2.994  48.542  1.00 33.12  ? 359 CYS B CB  1 
ATOM   6012  S SG  . CYS B 1 330 ? 4.314   -4.278  47.933  1.00 38.59  ? 359 CYS B SG  1 
ATOM   6013  N N   . GLN B 1 331 ? 8.118   -4.897  48.180  1.00 25.78  ? 360 GLN B N   1 
ATOM   6014  C CA  . GLN B 1 331 ? 8.780   -6.150  47.840  1.00 24.72  ? 360 GLN B CA  1 
ATOM   6015  C C   . GLN B 1 331 ? 9.663   -6.626  48.987  1.00 25.64  ? 360 GLN B C   1 
ATOM   6016  O O   . GLN B 1 331 ? 9.784   -7.828  49.218  1.00 26.24  ? 360 GLN B O   1 
ATOM   6017  C CB  . GLN B 1 331 ? 9.610   -5.995  46.572  1.00 25.57  ? 360 GLN B CB  1 
ATOM   6018  C CG  . GLN B 1 331 ? 8.762   -5.952  45.315  1.00 25.54  ? 360 GLN B CG  1 
ATOM   6019  C CD  . GLN B 1 331 ? 9.573   -5.629  44.088  1.00 25.96  ? 360 GLN B CD  1 
ATOM   6020  O OE1 . GLN B 1 331 ? 10.310  -4.643  44.024  1.00 26.55  ? 360 GLN B OE1 1 
ATOM   6021  N NE2 . GLN B 1 331 ? 9.421   -6.468  43.091  1.00 24.48  ? 360 GLN B NE2 1 
ATOM   6022  N N   . ARG B 1 332 ? 10.308  -5.687  49.686  1.00 30.77  ? 361 ARG B N   1 
ATOM   6023  C CA  . ARG B 1 332 ? 10.993  -6.040  50.920  1.00 35.28  ? 361 ARG B CA  1 
ATOM   6024  C C   . ARG B 1 332 ? 10.017  -6.699  51.896  1.00 31.22  ? 361 ARG B C   1 
ATOM   6025  O O   . ARG B 1 332 ? 10.371  -7.677  52.557  1.00 34.19  ? 361 ARG B O   1 
ATOM   6026  C CB  . ARG B 1 332 ? 11.637  -4.815  51.573  1.00 41.21  ? 361 ARG B CB  1 
ATOM   6027  C CG  . ARG B 1 332 ? 12.052  -5.023  53.027  1.00 51.64  ? 361 ARG B CG  1 
ATOM   6028  C CD  . ARG B 1 332 ? 13.307  -5.856  53.253  1.00 61.40  ? 361 ARG B CD  1 
ATOM   6029  N NE  . ARG B 1 332 ? 13.534  -6.167  54.669  1.00 68.89  ? 361 ARG B NE  1 
ATOM   6030  C CZ  . ARG B 1 332 ? 14.707  -6.510  55.209  1.00 67.99  ? 361 ARG B CZ  1 
ATOM   6031  N NH1 . ARG B 1 332 ? 15.802  -6.548  54.470  1.00 65.40  ? 361 ARG B NH1 1 
ATOM   6032  N NH2 . ARG B 1 332 ? 14.788  -6.800  56.499  1.00 63.99  ? 361 ARG B NH2 1 
ATOM   6033  N N   . GLU B 1 333 ? 8.798   -6.161  51.991  1.00 28.19  ? 362 GLU B N   1 
ATOM   6034  C CA  . GLU B 1 333 ? 7.801   -6.705  52.911  1.00 30.83  ? 362 GLU B CA  1 
ATOM   6035  C C   . GLU B 1 333 ? 7.493   -8.161  52.603  1.00 28.04  ? 362 GLU B C   1 
ATOM   6036  O O   . GLU B 1 333 ? 7.360   -8.994  53.505  1.00 29.04  ? 362 GLU B O   1 
ATOM   6037  C CB  . GLU B 1 333 ? 6.466   -5.979  52.817  1.00 34.62  ? 362 GLU B CB  1 
ATOM   6038  C CG  . GLU B 1 333 ? 6.568   -4.525  53.197  1.00 41.94  ? 362 GLU B CG  1 
ATOM   6039  C CD  . GLU B 1 333 ? 5.223   -3.836  53.319  1.00 46.94  ? 362 GLU B CD  1 
ATOM   6040  O OE1 . GLU B 1 333 ? 4.357   -4.021  52.403  1.00 48.49  ? 362 GLU B OE1 1 
ATOM   6041  O OE2 . GLU B 1 333 ? 5.050   -3.105  54.314  1.00 48.95  ? 362 GLU B OE2 1 
ATOM   6042  N N   . PHE B 1 334 ? 7.367   -8.449  51.314  1.00 26.81  ? 363 PHE B N   1 
ATOM   6043  C CA  . PHE B 1 334 ? 7.044   -9.794  50.877  1.00 26.34  ? 363 PHE B CA  1 
ATOM   6044  C C   . PHE B 1 334 ? 8.196   -10.732 51.241  1.00 25.67  ? 363 PHE B C   1 
ATOM   6045  O O   . PHE B 1 334 ? 7.961   -11.813 51.782  1.00 30.84  ? 363 PHE B O   1 
ATOM   6046  C CB  . PHE B 1 334 ? 6.732   -9.781  49.377  1.00 25.78  ? 363 PHE B CB  1 
ATOM   6047  C CG  . PHE B 1 334 ? 6.186   -11.069 48.825  1.00 24.10  ? 363 PHE B CG  1 
ATOM   6048  C CD1 . PHE B 1 334 ? 7.034   -12.113 48.502  1.00 24.37  ? 363 PHE B CD1 1 
ATOM   6049  C CD2 . PHE B 1 334 ? 4.826   -11.250 48.678  1.00 25.86  ? 363 PHE B CD2 1 
ATOM   6050  C CE1 . PHE B 1 334 ? 6.530   -13.307 48.029  1.00 22.79  ? 363 PHE B CE1 1 
ATOM   6051  C CE2 . PHE B 1 334 ? 4.324   -12.445 48.189  1.00 27.51  ? 363 PHE B CE2 1 
ATOM   6052  C CZ  . PHE B 1 334 ? 5.183   -13.474 47.875  1.00 25.65  ? 363 PHE B CZ  1 
ATOM   6053  N N   . ALA B 1 335 ? 9.430   -10.320 50.939  1.00 25.91  ? 364 ALA B N   1 
ATOM   6054  C CA  . ALA B 1 335 ? 10.578  -11.194 51.153  1.00 26.68  ? 364 ALA B CA  1 
ATOM   6055  C C   . ALA B 1 335 ? 10.707  -11.498 52.643  1.00 28.03  ? 364 ALA B C   1 
ATOM   6056  O O   . ALA B 1 335 ? 10.995  -12.637 53.020  1.00 32.26  ? 364 ALA B O   1 
ATOM   6057  C CB  . ALA B 1 335 ? 11.851  -10.582 50.612  1.00 26.85  ? 364 ALA B CB  1 
ATOM   6058  N N   . LEU B 1 336 ? 10.514  -10.490 53.504  1.00 31.50  ? 365 LEU B N   1 
ATOM   6059  C CA  . LEU B 1 336 ? 10.746  -10.707 54.932  1.00 37.20  ? 365 LEU B CA  1 
ATOM   6060  C C   . LEU B 1 336 ? 9.661   -11.617 55.505  1.00 34.20  ? 365 LEU B C   1 
ATOM   6061  O O   . LEU B 1 336 ? 9.870   -12.234 56.542  1.00 40.96  ? 365 LEU B O   1 
ATOM   6062  C CB  . LEU B 1 336 ? 10.814  -9.371  55.680  1.00 38.04  ? 365 LEU B CB  1 
ATOM   6063  C CG  . LEU B 1 336 ? 9.493   -8.889  56.276  1.00 44.71  ? 365 LEU B CG  1 
ATOM   6064  C CD1 . LEU B 1 336 ? 9.393   -9.270  57.758  1.00 45.82  ? 365 LEU B CD1 1 
ATOM   6065  C CD2 . LEU B 1 336 ? 9.315   -7.388  56.067  1.00 46.92  ? 365 LEU B CD2 1 
ATOM   6066  N N   . LYS B 1 337 ? 8.482   -11.668 54.870  1.00 33.84  ? 366 LYS B N   1 
ATOM   6067  C CA  . LYS B 1 337 ? 7.432   -12.591 55.280  1.00 34.23  ? 366 LYS B CA  1 
ATOM   6068  C C   . LYS B 1 337 ? 7.776   -13.996 54.799  1.00 34.79  ? 366 LYS B C   1 
ATOM   6069  O O   . LYS B 1 337 ? 7.648   -14.960 55.551  1.00 35.05  ? 366 LYS B O   1 
ATOM   6070  C CB  . LYS B 1 337 ? 6.073   -12.188 54.693  1.00 38.90  ? 366 LYS B CB  1 
ATOM   6071  C CG  . LYS B 1 337 ? 4.857   -12.858 55.317  1.00 43.57  ? 366 LYS B CG  1 
ATOM   6072  C CD  . LYS B 1 337 ? 3.548   -12.202 54.927  1.00 41.61  ? 366 LYS B CD  1 
ATOM   6073  C CE  . LYS B 1 337 ? 2.359   -12.698 55.723  1.00 42.44  ? 366 LYS B CE  1 
ATOM   6074  N NZ  . LYS B 1 337 ? 2.453   -12.349 57.164  1.00 39.33  ? 366 LYS B NZ  1 
ATOM   6075  N N   . HIS B 1 338 ? 8.217   -14.112 53.539  1.00 30.78  ? 367 HIS B N   1 
ATOM   6076  C CA  . HIS B 1 338 ? 8.157   -15.392 52.852  1.00 31.33  ? 367 HIS B CA  1 
ATOM   6077  C C   . HIS B 1 338 ? 9.524   -16.029 52.647  1.00 27.76  ? 367 HIS B C   1 
ATOM   6078  O O   . HIS B 1 338 ? 9.596   -17.248 52.629  1.00 28.12  ? 367 HIS B O   1 
ATOM   6079  C CB  . HIS B 1 338 ? 7.343   -15.250 51.565  1.00 34.36  ? 367 HIS B CB  1 
ATOM   6080  C CG  . HIS B 1 338 ? 5.915   -14.959 51.887  1.00 36.85  ? 367 HIS B CG  1 
ATOM   6081  N ND1 . HIS B 1 338 ? 5.111   -15.885 52.508  1.00 34.75  ? 367 HIS B ND1 1 
ATOM   6082  C CD2 . HIS B 1 338 ? 5.160   -13.850 51.738  1.00 40.73  ? 367 HIS B CD2 1 
ATOM   6083  C CE1 . HIS B 1 338 ? 3.903   -15.364 52.682  1.00 41.82  ? 367 HIS B CE1 1 
ATOM   6084  N NE2 . HIS B 1 338 ? 3.906   -14.131 52.219  1.00 39.91  ? 367 HIS B NE2 1 
ATOM   6085  N N   . LEU B 1 339 ? 10.587  -15.233 52.503  1.00 26.54  ? 368 LEU B N   1 
ATOM   6086  C CA  . LEU B 1 339 ? 11.914  -15.763 52.204  1.00 30.20  ? 368 LEU B CA  1 
ATOM   6087  C C   . LEU B 1 339 ? 12.990  -14.915 52.876  1.00 28.27  ? 368 LEU B C   1 
ATOM   6088  O O   . LEU B 1 339 ? 13.983  -14.552 52.246  1.00 29.54  ? 368 LEU B O   1 
ATOM   6089  C CB  . LEU B 1 339 ? 12.109  -15.783 50.681  1.00 30.09  ? 368 LEU B CB  1 
ATOM   6090  C CG  . LEU B 1 339 ? 11.813  -14.466 49.958  1.00 29.27  ? 368 LEU B CG  1 
ATOM   6091  C CD1 . LEU B 1 339 ? 13.015  -14.006 49.140  1.00 29.84  ? 368 LEU B CD1 1 
ATOM   6092  C CD2 . LEU B 1 339 ? 10.572  -14.614 49.083  1.00 27.34  ? 368 LEU B CD2 1 
ATOM   6093  N N   . PRO B 1 340 ? 12.868  -14.633 54.193  1.00 28.24  ? 369 PRO B N   1 
ATOM   6094  C CA  . PRO B 1 340 ? 13.712  -13.634 54.855  1.00 29.46  ? 369 PRO B CA  1 
ATOM   6095  C C   . PRO B 1 340 ? 15.198  -13.987 54.870  1.00 31.13  ? 369 PRO B C   1 
ATOM   6096  O O   . PRO B 1 340 ? 16.037  -13.099 55.007  1.00 32.18  ? 369 PRO B O   1 
ATOM   6097  C CB  . PRO B 1 340 ? 13.166  -13.620 56.299  1.00 29.95  ? 369 PRO B CB  1 
ATOM   6098  C CG  . PRO B 1 340 ? 12.581  -14.997 56.457  1.00 31.05  ? 369 PRO B CG  1 
ATOM   6099  C CD  . PRO B 1 340 ? 11.921  -15.268 55.123  1.00 29.97  ? 369 PRO B CD  1 
ATOM   6100  N N   . ASN B 1 341 ? 15.510  -15.287 54.737  1.00 32.82  ? 370 ASN B N   1 
ATOM   6101  C CA  . ASN B 1 341 ? 16.862  -15.773 54.962  1.00 33.83  ? 370 ASN B CA  1 
ATOM   6102  C C   . ASN B 1 341 ? 17.577  -16.109 53.658  1.00 35.20  ? 370 ASN B C   1 
ATOM   6103  O O   . ASN B 1 341 ? 18.763  -16.410 53.697  1.00 40.64  ? 370 ASN B O   1 
ATOM   6104  C CB  . ASN B 1 341 ? 16.831  -16.962 55.924  1.00 34.43  ? 370 ASN B CB  1 
ATOM   6105  C CG  . ASN B 1 341 ? 16.300  -16.540 57.276  1.00 36.10  ? 370 ASN B CG  1 
ATOM   6106  O OD1 . ASN B 1 341 ? 16.665  -15.475 57.766  1.00 40.27  ? 370 ASN B OD1 1 
ATOM   6107  N ND2 . ASN B 1 341 ? 15.378  -17.294 57.847  1.00 40.00  ? 370 ASN B ND2 1 
ATOM   6108  N N   . ASP B 1 342 ? 16.883  -16.035 52.516  1.00 32.92  ? 371 ASP B N   1 
ATOM   6109  C CA  . ASP B 1 342 ? 17.469  -16.366 51.227  1.00 31.97  ? 371 ASP B CA  1 
ATOM   6110  C C   . ASP B 1 342 ? 18.752  -15.566 51.024  1.00 30.62  ? 371 ASP B C   1 
ATOM   6111  O O   . ASP B 1 342 ? 18.797  -14.369 51.303  1.00 30.32  ? 371 ASP B O   1 
ATOM   6112  C CB  . ASP B 1 342 ? 16.497  -16.090 50.077  1.00 30.72  ? 371 ASP B CB  1 
ATOM   6113  C CG  . ASP B 1 342 ? 17.142  -16.251 48.713  1.00 31.44  ? 371 ASP B CG  1 
ATOM   6114  O OD1 . ASP B 1 342 ? 17.282  -17.406 48.258  1.00 35.89  ? 371 ASP B OD1 1 
ATOM   6115  O OD2 . ASP B 1 342 ? 17.601  -15.236 48.168  1.00 31.34  ? 371 ASP B OD2 1 
ATOM   6116  N N   . PRO B 1 343 ? 19.832  -16.195 50.512  1.00 29.46  ? 372 PRO B N   1 
ATOM   6117  C CA  . PRO B 1 343 ? 21.146  -15.554 50.454  1.00 31.02  ? 372 PRO B CA  1 
ATOM   6118  C C   . PRO B 1 343 ? 21.225  -14.317 49.562  1.00 30.78  ? 372 PRO B C   1 
ATOM   6119  O O   . PRO B 1 343 ? 21.921  -13.344 49.903  1.00 29.39  ? 372 PRO B O   1 
ATOM   6120  C CB  . PRO B 1 343 ? 22.070  -16.666 49.915  1.00 33.11  ? 372 PRO B CB  1 
ATOM   6121  C CG  . PRO B 1 343 ? 21.329  -17.947 50.214  1.00 31.71  ? 372 PRO B CG  1 
ATOM   6122  C CD  . PRO B 1 343 ? 19.872  -17.588 50.045  1.00 32.19  ? 372 PRO B CD  1 
ATOM   6123  N N   . MET B 1 344 ? 20.501  -14.358 48.434  1.00 32.83  ? 373 MET B N   1 
ATOM   6124  C CA  . MET B 1 344 ? 20.554  -13.260 47.477  1.00 33.21  ? 373 MET B CA  1 
ATOM   6125  C C   . MET B 1 344 ? 19.753  -12.088 48.046  1.00 29.90  ? 373 MET B C   1 
ATOM   6126  O O   . MET B 1 344 ? 20.070  -10.926 47.808  1.00 34.25  ? 373 MET B O   1 
ATOM   6127  C CB  . MET B 1 344 ? 20.017  -13.681 46.103  1.00 38.06  ? 373 MET B CB  1 
ATOM   6128  C CG  . MET B 1 344 ? 20.685  -14.944 45.552  1.00 39.90  ? 373 MET B CG  1 
ATOM   6129  S SD  . MET B 1 344 ? 20.471  -15.196 43.763  1.00 43.39  ? 373 MET B SD  1 
ATOM   6130  C CE  . MET B 1 344 ? 21.480  -13.829 43.189  1.00 40.30  ? 373 MET B CE  1 
ATOM   6131  N N   . PHE B 1 345 ? 18.722  -12.401 48.827  1.00 27.48  ? 374 PHE B N   1 
ATOM   6132  C CA  . PHE B 1 345 ? 17.943  -11.375 49.506  1.00 27.83  ? 374 PHE B CA  1 
ATOM   6133  C C   . PHE B 1 345 ? 18.760  -10.639 50.575  1.00 27.87  ? 374 PHE B C   1 
ATOM   6134  O O   . PHE B 1 345 ? 18.685  -9.415  50.694  1.00 24.94  ? 374 PHE B O   1 
ATOM   6135  C CB  . PHE B 1 345 ? 16.682  -11.994 50.102  1.00 26.37  ? 374 PHE B CB  1 
ATOM   6136  C CG  . PHE B 1 345 ? 15.963  -11.075 51.050  1.00 26.80  ? 374 PHE B CG  1 
ATOM   6137  C CD1 . PHE B 1 345 ? 15.673  -9.770  50.678  1.00 27.45  ? 374 PHE B CD1 1 
ATOM   6138  C CD2 . PHE B 1 345 ? 15.601  -11.508 52.315  1.00 28.81  ? 374 PHE B CD2 1 
ATOM   6139  C CE1 . PHE B 1 345 ? 15.037  -8.925  51.565  1.00 28.19  ? 374 PHE B CE1 1 
ATOM   6140  C CE2 . PHE B 1 345 ? 14.948  -10.666 53.193  1.00 28.37  ? 374 PHE B CE2 1 
ATOM   6141  C CZ  . PHE B 1 345 ? 14.666  -9.375  52.814  1.00 29.06  ? 374 PHE B CZ  1 
ATOM   6142  N N   . LYS B 1 346 ? 19.555  -11.386 51.338  1.00 30.73  ? 375 LYS B N   1 
ATOM   6143  C CA  . LYS B 1 346 ? 20.470  -10.754 52.321  1.00 31.01  ? 375 LYS B CA  1 
ATOM   6144  C C   . LYS B 1 346 ? 21.402  -9.809  51.559  1.00 27.59  ? 375 LYS B C   1 
ATOM   6145  O O   . LYS B 1 346 ? 21.626  -8.699  52.035  1.00 25.29  ? 375 LYS B O   1 
ATOM   6146  C CB  . LYS B 1 346 ? 21.246  -11.862 53.035  1.00 36.34  ? 375 LYS B CB  1 
ATOM   6147  C CG  . LYS B 1 346 ? 21.658  -11.620 54.464  1.00 44.33  ? 375 LYS B CG  1 
ATOM   6148  C CD  . LYS B 1 346 ? 23.068  -12.149 54.687  1.00 47.51  ? 375 LYS B CD  1 
ATOM   6149  C CE  . LYS B 1 346 ? 24.095  -11.076 54.544  1.00 49.40  ? 375 LYS B CE  1 
ATOM   6150  N NZ  . LYS B 1 346 ? 24.284  -10.653 53.155  1.00 49.27  ? 375 LYS B NZ  1 
ATOM   6151  N N   . LEU B 1 347 ? 21.870  -10.237 50.383  1.00 27.73  ? 376 LEU B N   1 
ATOM   6152  C CA  . LEU B 1 347 ? 22.759  -9.389  49.599  1.00 29.50  ? 376 LEU B CA  1 
ATOM   6153  C C   . LEU B 1 347 ? 22.015  -8.102  49.209  1.00 28.67  ? 376 LEU B C   1 
ATOM   6154  O O   . LEU B 1 347 ? 22.509  -6.994  49.466  1.00 27.62  ? 376 LEU B O   1 
ATOM   6155  C CB  . LEU B 1 347 ? 23.266  -10.191 48.393  1.00 33.50  ? 376 LEU B CB  1 
ATOM   6156  C CG  . LEU B 1 347 ? 24.514  -9.670  47.682  1.00 39.05  ? 376 LEU B CG  1 
ATOM   6157  C CD1 . LEU B 1 347 ? 25.629  -9.342  48.677  1.00 41.07  ? 376 LEU B CD1 1 
ATOM   6158  C CD2 . LEU B 1 347 ? 25.015  -10.701 46.673  1.00 38.49  ? 376 LEU B CD2 1 
ATOM   6159  N N   . VAL B 1 348 ? 20.802  -8.252  48.633  1.00 27.02  ? 377 VAL B N   1 
ATOM   6160  C CA  . VAL B 1 348 ? 19.970  -7.123  48.212  1.00 24.88  ? 377 VAL B CA  1 
ATOM   6161  C C   . VAL B 1 348 ? 19.756  -6.193  49.394  1.00 24.05  ? 377 VAL B C   1 
ATOM   6162  O O   . VAL B 1 348 ? 19.882  -4.971  49.259  1.00 22.55  ? 377 VAL B O   1 
ATOM   6163  C CB  . VAL B 1 348 ? 18.625  -7.578  47.620  1.00 23.61  ? 377 VAL B CB  1 
ATOM   6164  C CG1 . VAL B 1 348 ? 17.579  -6.476  47.627  1.00 23.02  ? 377 VAL B CG1 1 
ATOM   6165  C CG2 . VAL B 1 348 ? 18.797  -8.155  46.225  1.00 25.73  ? 377 VAL B CG2 1 
ATOM   6166  N N   . ALA B 1 349 ? 19.477  -6.789  50.572  1.00 24.26  ? 378 ALA B N   1 
ATOM   6167  C CA  . ALA B 1 349 ? 19.274  -5.990  51.764  1.00 23.65  ? 378 ALA B CA  1 
ATOM   6168  C C   . ALA B 1 349 ? 20.599  -5.325  52.110  1.00 25.42  ? 378 ALA B C   1 
ATOM   6169  O O   . ALA B 1 349 ? 20.643  -4.174  52.522  1.00 25.52  ? 378 ALA B O   1 
ATOM   6170  C CB  . ALA B 1 349 ? 18.770  -6.843  52.911  1.00 24.61  ? 378 ALA B CB  1 
ATOM   6171  N N   . GLN B 1 350 ? 21.675  -6.106  52.010  1.00 24.91  ? 379 GLN B N   1 
ATOM   6172  C CA  . GLN B 1 350 ? 23.020  -5.627  52.285  1.00 31.63  ? 379 GLN B CA  1 
ATOM   6173  C C   . GLN B 1 350 ? 23.341  -4.391  51.448  1.00 27.88  ? 379 GLN B C   1 
ATOM   6174  O O   . GLN B 1 350 ? 23.885  -3.413  51.947  1.00 26.35  ? 379 GLN B O   1 
ATOM   6175  C CB  . GLN B 1 350 ? 23.998  -6.771  52.015  1.00 39.86  ? 379 GLN B CB  1 
ATOM   6176  C CG  . GLN B 1 350 ? 24.220  -7.654  53.232  1.00 47.46  ? 379 GLN B CG  1 
ATOM   6177  C CD  . GLN B 1 350 ? 25.511  -7.349  53.952  1.00 55.45  ? 379 GLN B CD  1 
ATOM   6178  O OE1 . GLN B 1 350 ? 25.536  -7.199  55.172  1.00 62.46  ? 379 GLN B OE1 1 
ATOM   6179  N NE2 . GLN B 1 350 ? 26.603  -7.297  53.200  1.00 54.54  ? 379 GLN B NE2 1 
ATOM   6180  N N   . LEU B 1 351 ? 22.982  -4.438  50.167  1.00 27.57  ? 380 LEU B N   1 
ATOM   6181  C CA  . LEU B 1 351 ? 23.311  -3.351  49.264  1.00 29.47  ? 380 LEU B CA  1 
ATOM   6182  C C   . LEU B 1 351 ? 22.525  -2.087  49.641  1.00 27.73  ? 380 LEU B C   1 
ATOM   6183  O O   . LEU B 1 351 ? 23.027  -0.974  49.528  1.00 26.03  ? 380 LEU B O   1 
ATOM   6184  C CB  . LEU B 1 351 ? 23.014  -3.851  47.850  1.00 31.91  ? 380 LEU B CB  1 
ATOM   6185  C CG  . LEU B 1 351 ? 23.951  -4.962  47.372  1.00 34.05  ? 380 LEU B CG  1 
ATOM   6186  C CD1 . LEU B 1 351 ? 23.250  -5.892  46.401  1.00 38.61  ? 380 LEU B CD1 1 
ATOM   6187  C CD2 . LEU B 1 351 ? 25.180  -4.383  46.703  1.00 35.56  ? 380 LEU B CD2 1 
ATOM   6188  N N   . TYR B 1 352 ? 21.319  -2.262  50.186  1.00 30.42  ? 381 TYR B N   1 
ATOM   6189  C CA  . TYR B 1 352 ? 20.511  -1.134  50.639  1.00 28.23  ? 381 TYR B CA  1 
ATOM   6190  C C   . TYR B 1 352 ? 21.261  -0.299  51.671  1.00 29.07  ? 381 TYR B C   1 
ATOM   6191  O O   . TYR B 1 352 ? 21.097  0.917   51.739  1.00 26.52  ? 381 TYR B O   1 
ATOM   6192  C CB  . TYR B 1 352 ? 19.186  -1.604  51.236  1.00 28.35  ? 381 TYR B CB  1 
ATOM   6193  C CG  . TYR B 1 352 ? 18.216  -0.488  51.524  1.00 26.99  ? 381 TYR B CG  1 
ATOM   6194  C CD1 . TYR B 1 352 ? 17.535  0.129   50.491  1.00 28.39  ? 381 TYR B CD1 1 
ATOM   6195  C CD2 . TYR B 1 352 ? 17.971  -0.045  52.821  1.00 30.78  ? 381 TYR B CD2 1 
ATOM   6196  C CE1 . TYR B 1 352 ? 16.630  1.152   50.724  1.00 25.61  ? 381 TYR B CE1 1 
ATOM   6197  C CE2 . TYR B 1 352 ? 17.063  0.979   53.077  1.00 29.80  ? 381 TYR B CE2 1 
ATOM   6198  C CZ  . TYR B 1 352 ? 16.406  1.594   52.019  1.00 28.94  ? 381 TYR B CZ  1 
ATOM   6199  O OH  . TYR B 1 352 ? 15.497  2.616   52.232  1.00 25.92  ? 381 TYR B OH  1 
ATOM   6200  N N   . LYS B 1 353 ? 22.088  -0.949  52.486  1.00 30.77  ? 382 LYS B N   1 
ATOM   6201  C CA  . LYS B 1 353 ? 22.772  -0.223  53.540  1.00 34.21  ? 382 LYS B CA  1 
ATOM   6202  C C   . LYS B 1 353 ? 24.033  0.459   53.013  1.00 31.03  ? 382 LYS B C   1 
ATOM   6203  O O   . LYS B 1 353 ? 24.559  1.346   53.680  1.00 33.26  ? 382 LYS B O   1 
ATOM   6204  C CB  . LYS B 1 353 ? 23.091  -1.161  54.706  1.00 37.26  ? 382 LYS B CB  1 
ATOM   6205  C CG  . LYS B 1 353 ? 21.885  -1.835  55.345  1.00 43.66  ? 382 LYS B CG  1 
ATOM   6206  C CD  . LYS B 1 353 ? 22.257  -2.924  56.338  1.00 49.02  ? 382 LYS B CD  1 
ATOM   6207  C CE  . LYS B 1 353 ? 21.369  -4.147  56.244  1.00 52.44  ? 382 LYS B CE  1 
ATOM   6208  N NZ  . LYS B 1 353 ? 22.161  -5.397  56.337  1.00 55.83  ? 382 LYS B NZ  1 
ATOM   6209  N N   . ILE B 1 354 ? 24.512  0.048   51.829  1.00 29.15  ? 383 ILE B N   1 
ATOM   6210  C CA  . ILE B 1 354 ? 25.814  0.440   51.323  1.00 28.65  ? 383 ILE B CA  1 
ATOM   6211  C C   . ILE B 1 354 ? 25.736  1.347   50.101  1.00 26.61  ? 383 ILE B C   1 
ATOM   6212  O O   . ILE B 1 354 ? 26.465  2.347   50.059  1.00 25.00  ? 383 ILE B O   1 
ATOM   6213  C CB  . ILE B 1 354 ? 26.630  -0.817  51.000  1.00 30.92  ? 383 ILE B CB  1 
ATOM   6214  C CG1 . ILE B 1 354 ? 26.846  -1.642  52.268  1.00 31.80  ? 383 ILE B CG1 1 
ATOM   6215  C CG2 . ILE B 1 354 ? 27.938  -0.450  50.307  1.00 30.23  ? 383 ILE B CG2 1 
ATOM   6216  C CD1 . ILE B 1 354 ? 27.618  -0.918  53.343  1.00 35.23  ? 383 ILE B CD1 1 
ATOM   6217  N N   . VAL B 1 355 ? 24.975  0.890   49.111  1.00 24.63  ? 384 VAL B N   1 
ATOM   6218  C CA  . VAL B 1 355 ? 24.937  1.585   47.793  1.00 24.99  ? 384 VAL B CA  1 
ATOM   6219  C C   . VAL B 1 355 ? 24.553  3.055   47.978  1.00 22.69  ? 384 VAL B C   1 
ATOM   6220  O O   . VAL B 1 355 ? 25.234  3.884   47.448  1.00 23.79  ? 384 VAL B O   1 
ATOM   6221  C CB  . VAL B 1 355 ? 24.057  0.875   46.740  1.00 24.80  ? 384 VAL B CB  1 
ATOM   6222  C CG1 . VAL B 1 355 ? 24.059  1.609   45.407  1.00 26.85  ? 384 VAL B CG1 1 
ATOM   6223  C CG2 . VAL B 1 355 ? 24.471  -0.574  46.535  1.00 28.20  ? 384 VAL B CG2 1 
ATOM   6224  N N   . PRO B 1 356 ? 23.480  3.416   48.691  1.00 25.74  ? 385 PRO B N   1 
ATOM   6225  C CA  . PRO B 1 356 ? 23.155  4.827   48.788  1.00 27.76  ? 385 PRO B CA  1 
ATOM   6226  C C   . PRO B 1 356 ? 24.221  5.789   49.334  1.00 31.09  ? 385 PRO B C   1 
ATOM   6227  O O   . PRO B 1 356 ? 24.206  6.933   48.877  1.00 42.03  ? 385 PRO B O   1 
ATOM   6228  C CB  . PRO B 1 356 ? 21.903  4.752   49.659  1.00 27.18  ? 385 PRO B CB  1 
ATOM   6229  C CG  . PRO B 1 356 ? 21.294  3.433   49.298  1.00 24.28  ? 385 PRO B CG  1 
ATOM   6230  C CD  . PRO B 1 356 ? 22.507  2.543   49.317  1.00 24.38  ? 385 PRO B CD  1 
ATOM   6231  N N   . ASN B 1 357 ? 25.106  5.366   50.235  1.00 34.55  ? 386 ASN B N   1 
ATOM   6232  C CA  . ASN B 1 357 ? 26.196  6.287   50.697  1.00 34.64  ? 386 ASN B CA  1 
ATOM   6233  C C   . ASN B 1 357 ? 27.240  6.386   49.589  1.00 31.62  ? 386 ASN B C   1 
ATOM   6234  O O   . ASN B 1 357 ? 27.878  7.446   49.425  1.00 28.53  ? 386 ASN B O   1 
ATOM   6235  C CB  . ASN B 1 357 ? 26.752  5.903   52.055  1.00 36.12  ? 386 ASN B CB  1 
ATOM   6236  C CG  . ASN B 1 357 ? 25.888  6.463   53.151  1.00 35.28  ? 386 ASN B CG  1 
ATOM   6237  O OD1 . ASN B 1 357 ? 25.499  7.633   53.088  1.00 36.12  ? 386 ASN B OD1 1 
ATOM   6238  N ND2 . ASN B 1 357 ? 25.561  5.641   54.133  1.00 33.29  ? 386 ASN B ND2 1 
ATOM   6239  N N   . VAL B 1 358 ? 27.439  5.286   48.874  1.00 33.56  ? 387 VAL B N   1 
ATOM   6240  C CA  . VAL B 1 358 ? 28.226  5.439   47.627  1.00 35.27  ? 387 VAL B CA  1 
ATOM   6241  C C   . VAL B 1 358 ? 27.167  6.068   46.712  1.00 35.83  ? 387 VAL B C   1 
ATOM   6242  O O   . VAL B 1 358 ? 26.082  6.286   47.184  1.00 44.14  ? 387 VAL B O   1 
ATOM   6243  C CB  . VAL B 1 358 ? 28.873  4.154   47.088  1.00 35.66  ? 387 VAL B CB  1 
ATOM   6244  C CG1 . VAL B 1 358 ? 30.027  3.717   47.982  1.00 36.33  ? 387 VAL B CG1 1 
ATOM   6245  C CG2 . VAL B 1 358 ? 27.889  3.012   46.954  1.00 37.50  ? 387 VAL B CG2 1 
ATOM   6246  N N   . LEU B 1 359 ? 27.455  6.414   45.482  1.00 40.83  ? 388 LEU B N   1 
ATOM   6247  C CA  . LEU B 1 359 ? 26.424  7.138   44.688  1.00 35.45  ? 388 LEU B CA  1 
ATOM   6248  C C   . LEU B 1 359 ? 26.344  8.578   45.242  1.00 32.87  ? 388 LEU B C   1 
ATOM   6249  O O   . LEU B 1 359 ? 26.643  9.498   44.475  1.00 34.62  ? 388 LEU B O   1 
ATOM   6250  C CB  . LEU B 1 359 ? 25.046  6.466   44.616  1.00 36.34  ? 388 LEU B CB  1 
ATOM   6251  C CG  . LEU B 1 359 ? 24.743  5.605   43.388  1.00 38.18  ? 388 LEU B CG  1 
ATOM   6252  C CD1 . LEU B 1 359 ? 25.891  4.689   43.048  1.00 40.29  ? 388 LEU B CD1 1 
ATOM   6253  C CD2 . LEU B 1 359 ? 23.471  4.806   43.621  1.00 37.04  ? 388 LEU B CD2 1 
ATOM   6254  N N   . LEU B 1 360 ? 25.989  8.773   46.512  1.00 32.06  ? 389 LEU B N   1 
ATOM   6255  C CA  . LEU B 1 360 ? 25.973  10.164  47.020  1.00 35.46  ? 389 LEU B CA  1 
ATOM   6256  C C   . LEU B 1 360 ? 27.378  10.750  46.872  1.00 39.58  ? 389 LEU B C   1 
ATOM   6257  O O   . LEU B 1 360 ? 27.524  11.833  46.298  1.00 40.73  ? 389 LEU B O   1 
ATOM   6258  C CB  . LEU B 1 360 ? 25.514  10.222  48.471  1.00 36.81  ? 389 LEU B CB  1 
ATOM   6259  C CG  . LEU B 1 360 ? 24.005  10.317  48.702  1.00 39.24  ? 389 LEU B CG  1 
ATOM   6260  C CD1 . LEU B 1 360 ? 23.613  9.894   50.102  1.00 38.26  ? 389 LEU B CD1 1 
ATOM   6261  C CD2 . LEU B 1 360 ? 23.512  11.715  48.401  1.00 37.05  ? 389 LEU B CD2 1 
ATOM   6262  N N   . GLU B 1 361 ? 28.370  9.997   47.326  1.00 41.10  ? 390 GLU B N   1 
ATOM   6263  C CA  . GLU B 1 361 ? 29.763  10.472  47.265  1.00 42.50  ? 390 GLU B CA  1 
ATOM   6264  C C   . GLU B 1 361 ? 30.295  10.426  45.831  1.00 37.76  ? 390 GLU B C   1 
ATOM   6265  O O   . GLU B 1 361 ? 31.209  11.200  45.525  1.00 38.12  ? 390 GLU B O   1 
ATOM   6266  C CB  . GLU B 1 361 ? 30.420  9.533   48.256  1.00 48.46  ? 390 GLU B CB  1 
ATOM   6267  C CG  . GLU B 1 361 ? 30.513  10.139  49.654  1.00 58.11  ? 390 GLU B CG  1 
ATOM   6268  C CD  . GLU B 1 361 ? 29.214  10.293  50.423  1.00 63.19  ? 390 GLU B CD  1 
ATOM   6269  O OE1 . GLU B 1 361 ? 28.873  9.383   51.208  1.00 56.89  ? 390 GLU B OE1 1 
ATOM   6270  O OE2 . GLU B 1 361 ? 28.543  11.332  50.249  1.00 63.24  ? 390 GLU B OE2 1 
ATOM   6271  N N   . GLN B 1 362 ? 29.759  9.555   44.989  1.00 36.60  ? 391 GLN B N   1 
ATOM   6272  C CA  . GLN B 1 362 ? 30.162  9.578   43.557  1.00 41.23  ? 391 GLN B CA  1 
ATOM   6273  C C   . GLN B 1 362 ? 29.623  10.874  42.926  1.00 43.07  ? 391 GLN B C   1 
ATOM   6274  O O   . GLN B 1 362 ? 30.308  11.421  42.050  1.00 41.89  ? 391 GLN B O   1 
ATOM   6275  C CB  . GLN B 1 362 ? 29.724  8.313   42.820  1.00 42.10  ? 391 GLN B CB  1 
ATOM   6276  C CG  . GLN B 1 362 ? 30.397  8.128   41.466  1.00 47.62  ? 391 GLN B CG  1 
ATOM   6277  C CD  . GLN B 1 362 ? 29.426  7.749   40.374  1.00 43.93  ? 391 GLN B CD  1 
ATOM   6278  O OE1 . GLN B 1 362 ? 28.205  7.784   40.557  1.00 43.19  ? 391 GLN B OE1 1 
ATOM   6279  N NE2 . GLN B 1 362 ? 29.964  7.363   39.230  1.00 46.77  ? 391 GLN B NE2 1 
ATOM   6280  N N   . GLY B 1 363 ? 28.434  11.327  43.336  1.00 42.19  ? 392 GLY B N   1 
ATOM   6281  C CA  . GLY B 1 363 ? 27.912  12.633  42.878  1.00 43.59  ? 392 GLY B CA  1 
ATOM   6282  C C   . GLY B 1 363 ? 26.989  12.573  41.682  1.00 44.76  ? 392 GLY B C   1 
ATOM   6283  O O   . GLY B 1 363 ? 26.160  13.482  41.539  1.00 56.40  ? 392 GLY B O   1 
ATOM   6284  N N   . LYS B 1 364 ? 27.079  11.540  40.863  1.00 46.26  ? 393 LYS B N   1 
ATOM   6285  C CA  . LYS B 1 364 ? 26.299  11.524  39.606  1.00 51.94  ? 393 LYS B CA  1 
ATOM   6286  C C   . LYS B 1 364 ? 24.918  10.897  39.849  1.00 54.85  ? 393 LYS B C   1 
ATOM   6287  O O   . LYS B 1 364 ? 24.424  10.166  38.974  1.00 55.00  ? 393 LYS B O   1 
ATOM   6288  C CB  . LYS B 1 364 ? 27.137  10.790  38.555  1.00 52.11  ? 393 LYS B CB  1 
ATOM   6289  C CG  . LYS B 1 364 ? 27.942  11.689  37.642  1.00 51.56  ? 393 LYS B CG  1 
ATOM   6290  C CD  . LYS B 1 364 ? 28.460  10.911  36.443  1.00 50.16  ? 393 LYS B CD  1 
ATOM   6291  C CE  . LYS B 1 364 ? 29.054  9.618   36.874  1.00 48.92  ? 393 LYS B CE  1 
ATOM   6292  N NZ  . LYS B 1 364 ? 30.513  9.730   36.903  1.00 47.29  ? 393 LYS B NZ  1 
ATOM   6293  N N   . ALA B 1 365 ? 24.321  11.193  40.994  1.00 56.55  ? 394 ALA B N   1 
ATOM   6294  C CA  . ALA B 1 365 ? 22.985  10.640  41.277  1.00 58.93  ? 394 ALA B CA  1 
ATOM   6295  C C   . ALA B 1 365 ? 22.208  11.621  42.126  1.00 59.48  ? 394 ALA B C   1 
ATOM   6296  O O   . ALA B 1 365 ? 22.606  11.852  43.277  1.00 68.29  ? 394 ALA B O   1 
ATOM   6297  C CB  . ALA B 1 365 ? 23.062  9.313   41.976  1.00 60.70  ? 394 ALA B CB  1 
ATOM   6298  N N   . LYS B 1 366 ? 21.131  12.150  41.557  1.00 57.60  ? 395 LYS B N   1 
ATOM   6299  C CA  . LYS B 1 366 ? 20.259  13.062  42.321  1.00 51.11  ? 395 LYS B CA  1 
ATOM   6300  C C   . LYS B 1 366 ? 19.555  12.204  43.376  1.00 43.17  ? 395 LYS B C   1 
ATOM   6301  O O   . LYS B 1 366 ? 19.303  12.683  44.483  1.00 38.88  ? 395 LYS B O   1 
ATOM   6302  C CB  . LYS B 1 366 ? 19.362  13.663  41.241  1.00 48.23  ? 395 LYS B CB  1 
ATOM   6303  C CG  . LYS B 1 366 ? 19.268  15.178  41.277  1.00 51.54  ? 395 LYS B CG  1 
ATOM   6304  C CD  . LYS B 1 366 ? 17.840  15.644  41.518  1.00 52.07  ? 395 LYS B CD  1 
ATOM   6305  C CE  . LYS B 1 366 ? 17.706  16.885  42.333  1.00 53.55  ? 395 LYS B CE  1 
ATOM   6306  N NZ  . LYS B 1 366 ? 16.324  17.063  42.776  1.00 49.34  ? 395 LYS B NZ  1 
ATOM   6307  N N   . ASN B 1 367 ? 19.274  10.964  43.009  1.00 40.79  ? 396 ASN B N   1 
ATOM   6308  C CA  . ASN B 1 367 ? 18.594  10.048  43.913  1.00 36.88  ? 396 ASN B CA  1 
ATOM   6309  C C   . ASN B 1 367 ? 19.438  8.790   44.107  1.00 34.18  ? 396 ASN B C   1 
ATOM   6310  O O   . ASN B 1 367 ? 19.605  8.031   43.153  1.00 32.80  ? 396 ASN B O   1 
ATOM   6311  C CB  . ASN B 1 367 ? 17.214  9.652   43.379  1.00 38.06  ? 396 ASN B CB  1 
ATOM   6312  C CG  . ASN B 1 367 ? 16.560  8.553   44.189  1.00 42.12  ? 396 ASN B CG  1 
ATOM   6313  O OD1 . ASN B 1 367 ? 16.365  8.695   45.398  1.00 39.12  ? 396 ASN B OD1 1 
ATOM   6314  N ND2 . ASN B 1 367 ? 16.231  7.455   43.526  1.00 39.93  ? 396 ASN B ND2 1 
ATOM   6315  N N   . PRO B 1 368 ? 19.971  8.522   45.327  1.00 28.83  ? 397 PRO B N   1 
ATOM   6316  C CA  . PRO B 1 368 ? 20.785  7.327   45.587  1.00 27.55  ? 397 PRO B CA  1 
ATOM   6317  C C   . PRO B 1 368 ? 20.009  6.082   46.001  1.00 28.34  ? 397 PRO B C   1 
ATOM   6318  O O   . PRO B 1 368 ? 20.607  5.066   46.335  1.00 28.88  ? 397 PRO B O   1 
ATOM   6319  C CB  . PRO B 1 368 ? 21.641  7.736   46.786  1.00 28.78  ? 397 PRO B CB  1 
ATOM   6320  C CG  . PRO B 1 368 ? 20.724  8.674   47.567  1.00 31.11  ? 397 PRO B CG  1 
ATOM   6321  C CD  . PRO B 1 368 ? 19.837  9.352   46.535  1.00 31.95  ? 397 PRO B CD  1 
ATOM   6322  N N   . TRP B 1 369 ? 18.678  6.182   45.990  1.00 27.51  ? 398 TRP B N   1 
ATOM   6323  C CA  . TRP B 1 369 ? 17.837  5.167   46.581  1.00 25.70  ? 398 TRP B CA  1 
ATOM   6324  C C   . TRP B 1 369 ? 17.436  4.160   45.514  1.00 24.14  ? 398 TRP B C   1 
ATOM   6325  O O   . TRP B 1 369 ? 17.486  4.438   44.311  1.00 26.87  ? 398 TRP B O   1 
ATOM   6326  C CB  . TRP B 1 369 ? 16.664  5.847   47.297  1.00 28.14  ? 398 TRP B CB  1 
ATOM   6327  C CG  . TRP B 1 369 ? 17.146  6.723   48.416  1.00 29.90  ? 398 TRP B CG  1 
ATOM   6328  C CD1 . TRP B 1 369 ? 17.031  8.081   48.506  1.00 31.10  ? 398 TRP B CD1 1 
ATOM   6329  C CD2 . TRP B 1 369 ? 17.862  6.314   49.597  1.00 32.52  ? 398 TRP B CD2 1 
ATOM   6330  N NE1 . TRP B 1 369 ? 17.605  8.543   49.660  1.00 32.59  ? 398 TRP B NE1 1 
ATOM   6331  C CE2 . TRP B 1 369 ? 18.135  7.482   50.346  1.00 32.62  ? 398 TRP B CE2 1 
ATOM   6332  C CE3 . TRP B 1 369 ? 18.323  5.085   50.087  1.00 32.91  ? 398 TRP B CE3 1 
ATOM   6333  C CZ2 . TRP B 1 369 ? 18.810  7.446   51.563  1.00 29.99  ? 398 TRP B CZ2 1 
ATOM   6334  C CZ3 . TRP B 1 369 ? 18.980  5.057   51.298  1.00 31.16  ? 398 TRP B CZ3 1 
ATOM   6335  C CH2 . TRP B 1 369 ? 19.221  6.218   52.013  1.00 29.74  ? 398 TRP B CH2 1 
ATOM   6336  N N   . PRO B 1 370 ? 17.077  2.927   45.913  1.00 23.30  ? 399 PRO B N   1 
ATOM   6337  C CA  . PRO B 1 370 ? 16.690  1.917   44.944  1.00 25.18  ? 399 PRO B CA  1 
ATOM   6338  C C   . PRO B 1 370 ? 15.277  2.130   44.386  1.00 25.12  ? 399 PRO B C   1 
ATOM   6339  O O   . PRO B 1 370 ? 14.429  2.823   44.979  1.00 26.30  ? 399 PRO B O   1 
ATOM   6340  C CB  . PRO B 1 370 ? 16.825  0.628   45.749  1.00 22.94  ? 399 PRO B CB  1 
ATOM   6341  C CG  . PRO B 1 370 ? 16.516  1.027   47.180  1.00 25.45  ? 399 PRO B CG  1 
ATOM   6342  C CD  . PRO B 1 370 ? 16.925  2.471   47.312  1.00 24.83  ? 399 PRO B CD  1 
ATOM   6343  N N   . ASN B 1 371 ? 15.077  1.547   43.202  1.00 23.71  ? 400 ASN B N   1 
ATOM   6344  C CA  . ASN B 1 371 ? 13.794  1.510   42.534  1.00 23.70  ? 400 ASN B CA  1 
ATOM   6345  C C   . ASN B 1 371 ? 13.302  0.069   42.609  1.00 24.07  ? 400 ASN B C   1 
ATOM   6346  O O   . ASN B 1 371 ? 13.974  -0.821  43.143  1.00 21.64  ? 400 ASN B O   1 
ATOM   6347  C CB  . ASN B 1 371 ? 13.861  2.090   41.107  1.00 25.00  ? 400 ASN B CB  1 
ATOM   6348  C CG  . ASN B 1 371 ? 14.799  1.321   40.199  1.00 24.15  ? 400 ASN B CG  1 
ATOM   6349  O OD1 . ASN B 1 371 ? 14.618  0.121   40.024  1.00 23.18  ? 400 ASN B OD1 1 
ATOM   6350  N ND2 . ASN B 1 371 ? 15.810  1.976   39.642  1.00 23.03  ? 400 ASN B ND2 1 
ATOM   6351  N N   . VAL B 1 372 ? 12.127  -0.156  42.029  1.00 22.82  ? 401 VAL B N   1 
ATOM   6352  C CA  . VAL B 1 372 ? 11.494  -1.458  42.075  1.00 23.30  ? 401 VAL B CA  1 
ATOM   6353  C C   . VAL B 1 372 ? 12.390  -2.535  41.460  1.00 24.25  ? 401 VAL B C   1 
ATOM   6354  O O   . VAL B 1 372 ? 12.221  -3.710  41.775  1.00 21.80  ? 401 VAL B O   1 
ATOM   6355  C CB  . VAL B 1 372 ? 10.148  -1.404  41.332  1.00 25.07  ? 401 VAL B CB  1 
ATOM   6356  C CG1 . VAL B 1 372 ? 10.370  -1.187  39.846  1.00 25.45  ? 401 VAL B CG1 1 
ATOM   6357  C CG2 . VAL B 1 372 ? 9.340   -2.661  41.587  1.00 26.77  ? 401 VAL B CG2 1 
ATOM   6358  N N   . ASP B 1 373 ? 13.291  -2.173  40.529  1.00 23.65  ? 402 ASP B N   1 
ATOM   6359  C CA  . ASP B 1 373 ? 14.026  -3.200  39.796  1.00 27.49  ? 402 ASP B CA  1 
ATOM   6360  C C   . ASP B 1 373 ? 15.139  -3.791  40.672  1.00 26.95  ? 402 ASP B C   1 
ATOM   6361  O O   . ASP B 1 373 ? 15.635  -4.894  40.407  1.00 24.64  ? 402 ASP B O   1 
ATOM   6362  C CB  . ASP B 1 373 ? 14.535  -2.683  38.435  1.00 25.11  ? 402 ASP B CB  1 
ATOM   6363  C CG  . ASP B 1 373 ? 13.388  -2.370  37.480  1.00 27.65  ? 402 ASP B CG  1 
ATOM   6364  O OD1 . ASP B 1 373 ? 12.422  -3.146  37.479  1.00 28.92  ? 402 ASP B OD1 1 
ATOM   6365  O OD2 . ASP B 1 373 ? 13.465  -1.359  36.734  1.00 33.86  ? 402 ASP B OD2 1 
ATOM   6366  N N   . ALA B 1 374 ? 15.509  -3.088  41.748  1.00 26.21  ? 403 ALA B N   1 
ATOM   6367  C CA  . ALA B 1 374 ? 16.537  -3.594  42.638  1.00 24.56  ? 403 ALA B CA  1 
ATOM   6368  C C   . ALA B 1 374 ? 16.051  -4.855  43.354  1.00 25.20  ? 403 ALA B C   1 
ATOM   6369  O O   . ALA B 1 374 ? 16.859  -5.620  43.873  1.00 22.51  ? 403 ALA B O   1 
ATOM   6370  C CB  . ALA B 1 374 ? 16.980  -2.522  43.594  1.00 22.97  ? 403 ALA B CB  1 
ATOM   6371  N N   . HIS B 1 375 ? 14.738  -5.125  43.365  1.00 24.34  ? 404 HIS B N   1 
ATOM   6372  C CA  . HIS B 1 375 ? 14.266  -6.104  44.327  1.00 25.06  ? 404 HIS B CA  1 
ATOM   6373  C C   . HIS B 1 375 ? 13.442  -7.211  43.687  1.00 28.00  ? 404 HIS B C   1 
ATOM   6374  O O   . HIS B 1 375 ? 13.298  -8.273  44.287  1.00 26.81  ? 404 HIS B O   1 
ATOM   6375  C CB  . HIS B 1 375 ? 13.526  -5.417  45.476  1.00 27.05  ? 404 HIS B CB  1 
ATOM   6376  C CG  . HIS B 1 375 ? 13.613  -6.193  46.742  1.00 28.02  ? 404 HIS B CG  1 
ATOM   6377  N ND1 . HIS B 1 375 ? 13.867  -5.568  47.937  1.00 28.89  ? 404 HIS B ND1 1 
ATOM   6378  C CD2 . HIS B 1 375 ? 13.482  -7.490  47.019  1.00 27.79  ? 404 HIS B CD2 1 
ATOM   6379  C CE1 . HIS B 1 375 ? 13.885  -6.476  48.900  1.00 29.45  ? 404 HIS B CE1 1 
ATOM   6380  N NE2 . HIS B 1 375 ? 13.670  -7.649  48.363  1.00 30.93  ? 404 HIS B NE2 1 
ATOM   6381  N N   . SER B 1 376 ? 12.886  -6.960  42.498  1.00 27.49  ? 405 SER B N   1 
ATOM   6382  C CA  . SER B 1 376 ? 11.971  -7.903  41.876  1.00 24.31  ? 405 SER B CA  1 
ATOM   6383  C C   . SER B 1 376 ? 12.656  -9.245  41.653  1.00 25.02  ? 405 SER B C   1 
ATOM   6384  O O   . SER B 1 376 ? 12.083  -10.278 41.987  1.00 24.46  ? 405 SER B O   1 
ATOM   6385  C CB  . SER B 1 376 ? 11.403  -7.342  40.581  1.00 24.41  ? 405 SER B CB  1 
ATOM   6386  O OG  . SER B 1 376 ? 12.412  -6.945  39.664  1.00 23.27  ? 405 SER B OG  1 
ATOM   6387  N N   . GLY B 1 377 ? 13.890  -9.192  41.130  1.00 26.72  ? 406 GLY B N   1 
ATOM   6388  C CA  . GLY B 1 377 ? 14.574  -10.367 40.611  1.00 26.28  ? 406 GLY B CA  1 
ATOM   6389  C C   . GLY B 1 377 ? 14.827  -11.418 41.694  1.00 23.91  ? 406 GLY B C   1 
ATOM   6390  O O   . GLY B 1 377 ? 14.696  -12.606 41.412  1.00 26.21  ? 406 GLY B O   1 
ATOM   6391  N N   . VAL B 1 378 ? 15.148  -10.981 42.924  1.00 24.67  ? 407 VAL B N   1 
ATOM   6392  C CA  . VAL B 1 378 ? 15.516  -11.912 43.988  1.00 27.27  ? 407 VAL B CA  1 
ATOM   6393  C C   . VAL B 1 378 ? 14.300  -12.705 44.438  1.00 28.27  ? 407 VAL B C   1 
ATOM   6394  O O   . VAL B 1 378 ? 14.457  -13.827 44.915  1.00 26.11  ? 407 VAL B O   1 
ATOM   6395  C CB  . VAL B 1 378 ? 16.211  -11.278 45.213  1.00 27.35  ? 407 VAL B CB  1 
ATOM   6396  C CG1 . VAL B 1 378 ? 17.690  -11.079 44.949  1.00 29.37  ? 407 VAL B CG1 1 
ATOM   6397  C CG2 . VAL B 1 378 ? 15.542  -9.997  45.700  1.00 26.05  ? 407 VAL B CG2 1 
ATOM   6398  N N   . LEU B 1 379 ? 13.106  -12.109 44.343  1.00 26.58  ? 408 LEU B N   1 
ATOM   6399  C CA  . LEU B 1 379 ? 11.903  -12.811 44.758  1.00 24.52  ? 408 LEU B CA  1 
ATOM   6400  C C   . LEU B 1 379 ? 11.626  -13.930 43.762  1.00 24.16  ? 408 LEU B C   1 
ATOM   6401  O O   . LEU B 1 379 ? 11.264  -15.037 44.142  1.00 28.93  ? 408 LEU B O   1 
ATOM   6402  C CB  . LEU B 1 379 ? 10.746  -11.811 44.817  1.00 24.48  ? 408 LEU B CB  1 
ATOM   6403  C CG  . LEU B 1 379 ? 10.903  -10.704 45.849  1.00 23.72  ? 408 LEU B CG  1 
ATOM   6404  C CD1 . LEU B 1 379 ? 9.910   -9.578  45.627  1.00 23.77  ? 408 LEU B CD1 1 
ATOM   6405  C CD2 . LEU B 1 379 ? 10.756  -11.257 47.270  1.00 25.45  ? 408 LEU B CD2 1 
ATOM   6406  N N   . LEU B 1 380 ? 11.746  -13.608 42.472  1.00 26.73  ? 409 LEU B N   1 
ATOM   6407  C CA  . LEU B 1 380 ? 11.534  -14.558 41.398  1.00 25.58  ? 409 LEU B CA  1 
ATOM   6408  C C   . LEU B 1 380 ? 12.527  -15.714 41.534  1.00 21.53  ? 409 LEU B C   1 
ATOM   6409  O O   . LEU B 1 380 ? 12.113  -16.861 41.585  1.00 22.80  ? 409 LEU B O   1 
ATOM   6410  C CB  . LEU B 1 380 ? 11.688  -13.817 40.064  1.00 23.15  ? 409 LEU B CB  1 
ATOM   6411  C CG  . LEU B 1 380 ? 10.700  -12.663 39.853  1.00 25.78  ? 409 LEU B CG  1 
ATOM   6412  C CD1 . LEU B 1 380 ? 10.793  -12.161 38.428  1.00 25.13  ? 409 LEU B CD1 1 
ATOM   6413  C CD2 . LEU B 1 380 ? 9.269   -13.072 40.177  1.00 27.22  ? 409 LEU B CD2 1 
ATOM   6414  N N   . GLN B 1 381 ? 13.830  -15.400 41.564  1.00 25.30  ? 410 GLN B N   1 
ATOM   6415  C CA  . GLN B 1 381 ? 14.903  -16.383 41.758  1.00 26.09  ? 410 GLN B CA  1 
ATOM   6416  C C   . GLN B 1 381 ? 14.572  -17.396 42.868  1.00 25.21  ? 410 GLN B C   1 
ATOM   6417  O O   . GLN B 1 381 ? 14.747  -18.611 42.696  1.00 26.63  ? 410 GLN B O   1 
ATOM   6418  C CB  . GLN B 1 381 ? 16.191  -15.633 42.108  1.00 33.09  ? 410 GLN B CB  1 
ATOM   6419  C CG  . GLN B 1 381 ? 17.473  -16.449 42.000  1.00 38.73  ? 410 GLN B CG  1 
ATOM   6420  C CD  . GLN B 1 381 ? 18.208  -16.318 40.679  1.00 43.14  ? 410 GLN B CD  1 
ATOM   6421  O OE1 . GLN B 1 381 ? 19.413  -16.556 40.582  1.00 39.25  ? 410 GLN B OE1 1 
ATOM   6422  N NE2 . GLN B 1 381 ? 17.505  -15.884 39.643  1.00 52.67  ? 410 GLN B NE2 1 
ATOM   6423  N N   . TYR B 1 382 ? 14.073  -16.910 44.001  1.00 22.94  ? 411 TYR B N   1 
ATOM   6424  C CA  . TYR B 1 382 ? 13.717  -17.746 45.141  1.00 24.78  ? 411 TYR B CA  1 
ATOM   6425  C C   . TYR B 1 382 ? 12.762  -18.867 44.754  1.00 26.76  ? 411 TYR B C   1 
ATOM   6426  O O   . TYR B 1 382 ? 12.984  -20.022 45.110  1.00 29.61  ? 411 TYR B O   1 
ATOM   6427  C CB  . TYR B 1 382 ? 13.087  -16.930 46.266  1.00 27.30  ? 411 TYR B CB  1 
ATOM   6428  C CG  . TYR B 1 382 ? 12.712  -17.765 47.462  1.00 28.13  ? 411 TYR B CG  1 
ATOM   6429  C CD1 . TYR B 1 382 ? 13.694  -18.386 48.217  1.00 28.81  ? 411 TYR B CD1 1 
ATOM   6430  C CD2 . TYR B 1 382 ? 11.385  -17.985 47.804  1.00 29.97  ? 411 TYR B CD2 1 
ATOM   6431  C CE1 . TYR B 1 382 ? 13.370  -19.185 49.299  1.00 29.01  ? 411 TYR B CE1 1 
ATOM   6432  C CE2 . TYR B 1 382 ? 11.043  -18.763 48.905  1.00 29.37  ? 411 TYR B CE2 1 
ATOM   6433  C CZ  . TYR B 1 382 ? 12.045  -19.372 49.646  1.00 30.38  ? 411 TYR B CZ  1 
ATOM   6434  O OH  . TYR B 1 382 ? 11.762  -20.160 50.738  1.00 29.35  ? 411 TYR B OH  1 
ATOM   6435  N N   . TYR B 1 383 ? 11.718  -18.546 43.982  1.00 27.74  ? 412 TYR B N   1 
ATOM   6436  C CA  . TYR B 1 383 ? 10.711  -19.543 43.649  1.00 27.06  ? 412 TYR B CA  1 
ATOM   6437  C C   . TYR B 1 383 ? 11.143  -20.459 42.504  1.00 25.53  ? 412 TYR B C   1 
ATOM   6438  O O   . TYR B 1 383 ? 10.369  -21.289 42.047  1.00 28.19  ? 412 TYR B O   1 
ATOM   6439  C CB  . TYR B 1 383 ? 9.389   -18.811 43.422  1.00 24.90  ? 412 TYR B CB  1 
ATOM   6440  C CG  . TYR B 1 383 ? 8.822   -18.292 44.714  1.00 22.93  ? 412 TYR B CG  1 
ATOM   6441  C CD1 . TYR B 1 383 ? 8.328   -19.160 45.668  1.00 24.15  ? 412 TYR B CD1 1 
ATOM   6442  C CD2 . TYR B 1 383 ? 8.847   -16.949 45.036  1.00 22.68  ? 412 TYR B CD2 1 
ATOM   6443  C CE1 . TYR B 1 383 ? 7.874   -18.723 46.903  1.00 20.95  ? 412 TYR B CE1 1 
ATOM   6444  C CE2 . TYR B 1 383 ? 8.362   -16.492 46.243  1.00 21.13  ? 412 TYR B CE2 1 
ATOM   6445  C CZ  . TYR B 1 383 ? 7.860   -17.375 47.177  1.00 21.88  ? 412 TYR B CZ  1 
ATOM   6446  O OH  . TYR B 1 383 ? 7.374   -16.942 48.370  1.00 22.34  ? 412 TYR B OH  1 
ATOM   6447  N N   . GLY B 1 384 ? 12.384  -20.346 42.040  1.00 25.53  ? 413 GLY B N   1 
ATOM   6448  C CA  . GLY B 1 384 ? 12.847  -21.203 40.961  1.00 25.11  ? 413 GLY B CA  1 
ATOM   6449  C C   . GLY B 1 384 ? 12.810  -20.519 39.598  1.00 23.87  ? 413 GLY B C   1 
ATOM   6450  O O   . GLY B 1 384 ? 13.251  -21.081 38.595  1.00 23.09  ? 413 GLY B O   1 
ATOM   6451  N N   . MET B 1 385 ? 12.317  -19.278 39.524  1.00 22.38  ? 414 MET B N   1 
ATOM   6452  C CA  . MET B 1 385 ? 12.367  -18.615 38.222  1.00 23.18  ? 414 MET B CA  1 
ATOM   6453  C C   . MET B 1 385 ? 13.698  -17.886 38.093  1.00 24.57  ? 414 MET B C   1 
ATOM   6454  O O   . MET B 1 385 ? 13.803  -16.693 38.392  1.00 24.36  ? 414 MET B O   1 
ATOM   6455  C CB  . MET B 1 385 ? 11.215  -17.631 37.989  1.00 26.17  ? 414 MET B CB  1 
ATOM   6456  C CG  . MET B 1 385 ? 11.372  -16.843 36.683  1.00 26.28  ? 414 MET B CG  1 
ATOM   6457  S SD  . MET B 1 385 ? 9.869   -15.950 36.252  1.00 26.88  ? 414 MET B SD  1 
ATOM   6458  C CE  . MET B 1 385 ? 8.678   -17.262 36.030  1.00 24.84  ? 414 MET B CE  1 
ATOM   6459  N N   . THR B 1 386 ? 14.693  -18.659 37.642  1.00 23.57  ? 415 THR B N   1 
ATOM   6460  C CA  . THR B 1 386 ? 16.102  -18.305 37.616  1.00 26.91  ? 415 THR B CA  1 
ATOM   6461  C C   . THR B 1 386 ? 16.498  -17.641 36.295  1.00 22.37  ? 415 THR B C   1 
ATOM   6462  O O   . THR B 1 386 ? 17.641  -17.219 36.148  1.00 21.88  ? 415 THR B O   1 
ATOM   6463  C CB  . THR B 1 386 ? 16.944  -19.577 37.809  1.00 29.52  ? 415 THR B CB  1 
ATOM   6464  O OG1 . THR B 1 386 ? 16.567  -20.508 36.799  1.00 32.45  ? 415 THR B OG1 1 
ATOM   6465  C CG2 . THR B 1 386 ? 16.764  -20.223 39.167  1.00 31.57  ? 415 THR B CG2 1 
ATOM   6466  N N   . GLU B 1 387 ? 15.554  -17.598 35.343  1.00 24.21  ? 416 GLU B N   1 
ATOM   6467  C CA  . GLU B 1 387 ? 15.826  -17.148 33.985  1.00 23.86  ? 416 GLU B CA  1 
ATOM   6468  C C   . GLU B 1 387 ? 15.749  -15.625 33.946  1.00 23.44  ? 416 GLU B C   1 
ATOM   6469  O O   . GLU B 1 387 ? 14.697  -15.085 33.602  1.00 24.95  ? 416 GLU B O   1 
ATOM   6470  C CB  . GLU B 1 387 ? 14.816  -17.709 32.985  1.00 24.86  ? 416 GLU B CB  1 
ATOM   6471  C CG  . GLU B 1 387 ? 14.820  -19.234 32.875  1.00 24.51  ? 416 GLU B CG  1 
ATOM   6472  C CD  . GLU B 1 387 ? 13.948  -19.978 33.868  1.00 25.55  ? 416 GLU B CD  1 
ATOM   6473  O OE1 . GLU B 1 387 ? 13.241  -19.330 34.666  1.00 27.91  ? 416 GLU B OE1 1 
ATOM   6474  O OE2 . GLU B 1 387 ? 13.989  -21.218 33.861  1.00 24.90  ? 416 GLU B OE2 1 
ATOM   6475  N N   . MET B 1 388 ? 16.877  -14.974 34.237  1.00 22.82  ? 417 MET B N   1 
ATOM   6476  C CA  . MET B 1 388 ? 16.945  -13.532 34.473  1.00 26.77  ? 417 MET B CA  1 
ATOM   6477  C C   . MET B 1 388 ? 16.581  -12.770 33.201  1.00 23.99  ? 417 MET B C   1 
ATOM   6478  O O   . MET B 1 388 ? 16.060  -11.652 33.246  1.00 25.41  ? 417 MET B O   1 
ATOM   6479  C CB  . MET B 1 388 ? 18.364  -13.081 34.857  1.00 30.84  ? 417 MET B CB  1 
ATOM   6480  C CG  . MET B 1 388 ? 18.931  -13.754 36.098  1.00 40.97  ? 417 MET B CG  1 
ATOM   6481  S SD  . MET B 1 388 ? 20.763  -13.708 36.195  1.00 46.06  ? 417 MET B SD  1 
ATOM   6482  C CE  . MET B 1 388 ? 21.295  -14.044 34.515  1.00 44.71  ? 417 MET B CE  1 
ATOM   6483  N N   . ASN B 1 389 ? 16.832  -13.388 32.057  1.00 25.15  ? 418 ASN B N   1 
ATOM   6484  C CA  . ASN B 1 389 ? 16.552  -12.747 30.784  1.00 25.24  ? 418 ASN B CA  1 
ATOM   6485  C C   . ASN B 1 389 ? 15.051  -12.710 30.512  1.00 24.10  ? 418 ASN B C   1 
ATOM   6486  O O   . ASN B 1 389 ? 14.665  -12.160 29.488  1.00 25.00  ? 418 ASN B O   1 
ATOM   6487  C CB  . ASN B 1 389 ? 17.363  -13.383 29.654  1.00 27.80  ? 418 ASN B CB  1 
ATOM   6488  C CG  . ASN B 1 389 ? 18.693  -12.670 29.488  1.00 32.37  ? 418 ASN B CG  1 
ATOM   6489  O OD1 . ASN B 1 389 ? 19.297  -12.235 30.470  1.00 30.63  ? 418 ASN B OD1 1 
ATOM   6490  N ND2 . ASN B 1 389 ? 19.108  -12.472 28.252  1.00 37.13  ? 418 ASN B ND2 1 
ATOM   6491  N N   . TYR B 1 390 ? 14.226  -13.283 31.410  1.00 20.99  ? 419 TYR B N   1 
ATOM   6492  C CA  . TYR B 1 390 ? 12.789  -13.345 31.206  1.00 20.72  ? 419 TYR B CA  1 
ATOM   6493  C C   . TYR B 1 390 ? 12.062  -12.293 32.030  1.00 23.75  ? 419 TYR B C   1 
ATOM   6494  O O   . TYR B 1 390 ? 10.853  -12.047 31.826  1.00 24.93  ? 419 TYR B O   1 
ATOM   6495  C CB  . TYR B 1 390 ? 12.261  -14.735 31.570  1.00 19.48  ? 419 TYR B CB  1 
ATOM   6496  C CG  . TYR B 1 390 ? 10.772  -14.886 31.332  1.00 17.13  ? 419 TYR B CG  1 
ATOM   6497  C CD1 . TYR B 1 390 ? 10.267  -15.132 30.057  1.00 15.23  ? 419 TYR B CD1 1 
ATOM   6498  C CD2 . TYR B 1 390 ? 9.871   -14.774 32.377  1.00 14.72  ? 419 TYR B CD2 1 
ATOM   6499  C CE1 . TYR B 1 390 ? 8.901   -15.261 29.825  1.00 13.87  ? 419 TYR B CE1 1 
ATOM   6500  C CE2 . TYR B 1 390 ? 8.506   -14.881 32.159  1.00 13.66  ? 419 TYR B CE2 1 
ATOM   6501  C CZ  . TYR B 1 390 ? 8.022   -15.111 30.889  1.00 14.82  ? 419 TYR B CZ  1 
ATOM   6502  O OH  . TYR B 1 390 ? 6.655   -15.233 30.703  1.00 18.38  ? 419 TYR B OH  1 
ATOM   6503  N N   . TYR B 1 391 ? 12.814  -11.677 32.951  1.00 24.07  ? 420 TYR B N   1 
ATOM   6504  C CA  . TYR B 1 391 ? 12.224  -10.947 34.053  1.00 22.70  ? 420 TYR B CA  1 
ATOM   6505  C C   . TYR B 1 391 ? 11.483  -9.723  33.534  1.00 21.42  ? 420 TYR B C   1 
ATOM   6506  O O   . TYR B 1 391 ? 10.463  -9.350  34.102  1.00 20.36  ? 420 TYR B O   1 
ATOM   6507  C CB  . TYR B 1 391 ? 13.304  -10.505 35.035  1.00 23.20  ? 420 TYR B CB  1 
ATOM   6508  C CG  . TYR B 1 391 ? 13.820  -11.588 35.954  1.00 22.26  ? 420 TYR B CG  1 
ATOM   6509  C CD1 . TYR B 1 391 ? 13.323  -12.882 35.923  1.00 24.49  ? 420 TYR B CD1 1 
ATOM   6510  C CD2 . TYR B 1 391 ? 14.808  -11.299 36.865  1.00 24.65  ? 420 TYR B CD2 1 
ATOM   6511  C CE1 . TYR B 1 391 ? 13.818  -13.857 36.780  1.00 25.24  ? 420 TYR B CE1 1 
ATOM   6512  C CE2 . TYR B 1 391 ? 15.333  -12.264 37.707  1.00 24.04  ? 420 TYR B CE2 1 
ATOM   6513  C CZ  . TYR B 1 391 ? 14.826  -13.548 37.672  1.00 25.72  ? 420 TYR B CZ  1 
ATOM   6514  O OH  . TYR B 1 391 ? 15.369  -14.488 38.528  1.00 25.15  ? 420 TYR B OH  1 
ATOM   6515  N N   . THR B 1 392 ? 11.989  -9.105  32.463  1.00 21.58  ? 421 THR B N   1 
ATOM   6516  C CA  . THR B 1 392 ? 11.338  -7.882  32.027  1.00 20.67  ? 421 THR B CA  1 
ATOM   6517  C C   . THR B 1 392 ? 9.998   -8.216  31.368  1.00 21.21  ? 421 THR B C   1 
ATOM   6518  O O   . THR B 1 392 ? 9.109   -7.372  31.345  1.00 24.27  ? 421 THR B O   1 
ATOM   6519  C CB  . THR B 1 392 ? 12.247  -7.022  31.159  1.00 19.81  ? 421 THR B CB  1 
ATOM   6520  O OG1 . THR B 1 392 ? 13.551  -7.064  31.734  1.00 18.82  ? 421 THR B OG1 1 
ATOM   6521  C CG2 . THR B 1 392 ? 11.753  -5.592  31.036  1.00 21.32  ? 421 THR B CG2 1 
ATOM   6522  N N   . VAL B 1 393 ? 9.836   -9.435  30.835  1.00 18.92  ? 422 VAL B N   1 
ATOM   6523  C CA  . VAL B 1 393 ? 8.542   -9.850  30.302  1.00 19.24  ? 422 VAL B CA  1 
ATOM   6524  C C   . VAL B 1 393 ? 7.450   -9.747  31.366  1.00 19.10  ? 422 VAL B C   1 
ATOM   6525  O O   . VAL B 1 393 ? 6.351   -9.261  31.049  1.00 20.39  ? 422 VAL B O   1 
ATOM   6526  C CB  . VAL B 1 393 ? 8.597   -11.269 29.711  1.00 18.65  ? 422 VAL B CB  1 
ATOM   6527  C CG1 . VAL B 1 393 ? 7.244   -11.699 29.189  1.00 18.77  ? 422 VAL B CG1 1 
ATOM   6528  C CG2 . VAL B 1 393 ? 9.673   -11.364 28.650  1.00 18.90  ? 422 VAL B CG2 1 
ATOM   6529  N N   . LEU B 1 394 ? 7.713   -10.178 32.611  1.00 18.24  ? 423 LEU B N   1 
ATOM   6530  C CA  . LEU B 1 394 ? 6.711   -10.052 33.662  1.00 18.95  ? 423 LEU B CA  1 
ATOM   6531  C C   . LEU B 1 394 ? 6.385   -8.573  33.888  1.00 18.04  ? 423 LEU B C   1 
ATOM   6532  O O   . LEU B 1 394 ? 5.234   -8.217  34.033  1.00 20.73  ? 423 LEU B O   1 
ATOM   6533  C CB  . LEU B 1 394 ? 7.182   -10.723 34.954  1.00 18.66  ? 423 LEU B CB  1 
ATOM   6534  C CG  . LEU B 1 394 ? 7.505   -12.224 34.858  1.00 21.74  ? 423 LEU B CG  1 
ATOM   6535  C CD1 . LEU B 1 394 ? 8.306   -12.671 36.061  1.00 23.30  ? 423 LEU B CD1 1 
ATOM   6536  C CD2 . LEU B 1 394 ? 6.259   -13.072 34.743  1.00 22.09  ? 423 LEU B CD2 1 
ATOM   6537  N N   . PHE B 1 395 ? 7.411   -7.730  33.927  1.00 21.01  ? 424 PHE B N   1 
ATOM   6538  C CA  . PHE B 1 395 ? 7.215   -6.299  34.076  1.00 18.41  ? 424 PHE B CA  1 
ATOM   6539  C C   . PHE B 1 395 ? 6.296   -5.829  32.949  1.00 19.03  ? 424 PHE B C   1 
ATOM   6540  O O   . PHE B 1 395 ? 5.344   -5.091  33.208  1.00 18.53  ? 424 PHE B O   1 
ATOM   6541  C CB  . PHE B 1 395 ? 8.553   -5.560  34.154  1.00 17.55  ? 424 PHE B CB  1 
ATOM   6542  C CG  . PHE B 1 395 ? 8.517   -4.117  34.589  1.00 17.39  ? 424 PHE B CG  1 
ATOM   6543  C CD1 . PHE B 1 395 ? 7.327   -3.412  34.696  1.00 17.88  ? 424 PHE B CD1 1 
ATOM   6544  C CD2 . PHE B 1 395 ? 9.693   -3.461  34.903  1.00 18.49  ? 424 PHE B CD2 1 
ATOM   6545  C CE1 . PHE B 1 395 ? 7.327   -2.083  35.097  1.00 18.82  ? 424 PHE B CE1 1 
ATOM   6546  C CE2 . PHE B 1 395 ? 9.697   -2.127  35.298  1.00 20.45  ? 424 PHE B CE2 1 
ATOM   6547  C CZ  . PHE B 1 395 ? 8.508   -1.445  35.402  1.00 19.20  ? 424 PHE B CZ  1 
ATOM   6548  N N   . GLY B 1 396 ? 6.584   -6.252  31.707  1.00 18.51  ? 425 GLY B N   1 
ATOM   6549  C CA  . GLY B 1 396 ? 5.817   -5.820  30.549  1.00 20.12  ? 425 GLY B CA  1 
ATOM   6550  C C   . GLY B 1 396 ? 4.357   -6.204  30.700  1.00 17.35  ? 425 GLY B C   1 
ATOM   6551  O O   . GLY B 1 396 ? 3.456   -5.422  30.445  1.00 18.22  ? 425 GLY B O   1 
ATOM   6552  N N   . VAL B 1 397 ? 4.109   -7.445  31.114  1.00 16.73  ? 426 VAL B N   1 
ATOM   6553  C CA  . VAL B 1 397 ? 2.745   -7.891  31.288  1.00 18.91  ? 426 VAL B CA  1 
ATOM   6554  C C   . VAL B 1 397 ? 1.987   -7.020  32.284  1.00 18.70  ? 426 VAL B C   1 
ATOM   6555  O O   . VAL B 1 397 ? 0.805   -6.749  32.059  1.00 17.63  ? 426 VAL B O   1 
ATOM   6556  C CB  . VAL B 1 397 ? 2.730   -9.365  31.691  1.00 21.39  ? 426 VAL B CB  1 
ATOM   6557  C CG1 . VAL B 1 397 ? 1.354   -9.845  32.117  1.00 24.05  ? 426 VAL B CG1 1 
ATOM   6558  C CG2 . VAL B 1 397 ? 3.288   -10.195 30.544  1.00 22.18  ? 426 VAL B CG2 1 
ATOM   6559  N N   . SER B 1 398 ? 2.645   -6.617  33.376  1.00 18.42  ? 427 SER B N   1 
ATOM   6560  C CA  . SER B 1 398 ? 2.043   -5.771  34.388  1.00 19.96  ? 427 SER B CA  1 
ATOM   6561  C C   . SER B 1 398 ? 1.788   -4.369  33.835  1.00 18.97  ? 427 SER B C   1 
ATOM   6562  O O   . SER B 1 398 ? 0.708   -3.801  34.056  1.00 17.94  ? 427 SER B O   1 
ATOM   6563  C CB  . SER B 1 398 ? 2.932   -5.708  35.584  1.00 19.12  ? 427 SER B CB  1 
ATOM   6564  O OG  . SER B 1 398 ? 2.551   -4.687  36.482  1.00 19.77  ? 427 SER B OG  1 
ATOM   6565  N N   . ARG B 1 399 ? 2.776   -3.835  33.121  1.00 19.98  ? 428 ARG B N   1 
ATOM   6566  C CA  . ARG B 1 399 ? 2.729   -2.429  32.696  1.00 21.09  ? 428 ARG B CA  1 
ATOM   6567  C C   . ARG B 1 399 ? 1.668   -2.186  31.600  1.00 19.37  ? 428 ARG B C   1 
ATOM   6568  O O   . ARG B 1 399 ? 1.211   -1.066  31.411  1.00 16.70  ? 428 ARG B O   1 
ATOM   6569  C CB  . ARG B 1 399 ? 4.120   -1.979  32.250  1.00 20.25  ? 428 ARG B CB  1 
ATOM   6570  C CG  . ARG B 1 399 ? 4.196   -0.559  31.713  1.00 18.79  ? 428 ARG B CG  1 
ATOM   6571  C CD  . ARG B 1 399 ? 3.747   0.456   32.759  1.00 19.74  ? 428 ARG B CD  1 
ATOM   6572  N NE  . ARG B 1 399 ? 4.304   0.307   34.086  1.00 19.28  ? 428 ARG B NE  1 
ATOM   6573  C CZ  . ARG B 1 399 ? 5.375   0.938   34.544  1.00 21.22  ? 428 ARG B CZ  1 
ATOM   6574  N NH1 . ARG B 1 399 ? 6.142   1.621   33.705  1.00 22.27  ? 428 ARG B NH1 1 
ATOM   6575  N NH2 . ARG B 1 399 ? 5.678   0.890   35.836  1.00 23.12  ? 428 ARG B NH2 1 
ATOM   6576  N N   . ALA B 1 400 ? 1.194   -3.236  30.950  1.00 16.49  ? 429 ALA B N   1 
ATOM   6577  C CA  . ALA B 1 400 ? 0.042   -3.201  30.067  1.00 18.00  ? 429 ALA B CA  1 
ATOM   6578  C C   . ALA B 1 400 ? -1.186  -2.591  30.750  1.00 17.24  ? 429 ALA B C   1 
ATOM   6579  O O   . ALA B 1 400 ? -1.916  -1.781  30.158  1.00 16.49  ? 429 ALA B O   1 
ATOM   6580  C CB  . ALA B 1 400 ? -0.231  -4.625  29.650  1.00 18.77  ? 429 ALA B CB  1 
ATOM   6581  N N   . LEU B 1 401 ? -1.416  -2.992  32.014  1.00 16.19  ? 430 LEU B N   1 
ATOM   6582  C CA  . LEU B 1 401 ? -2.562  -2.556  32.774  1.00 16.79  ? 430 LEU B CA  1 
ATOM   6583  C C   . LEU B 1 401 ? -2.617  -1.032  32.817  1.00 17.70  ? 430 LEU B C   1 
ATOM   6584  O O   . LEU B 1 401 ? -3.677  -0.474  32.598  1.00 18.13  ? 430 LEU B O   1 
ATOM   6585  C CB  . LEU B 1 401 ? -2.481  -3.149  34.182  1.00 18.42  ? 430 LEU B CB  1 
ATOM   6586  C CG  . LEU B 1 401 ? -2.488  -4.687  34.230  1.00 18.02  ? 430 LEU B CG  1 
ATOM   6587  C CD1 . LEU B 1 401 ? -2.119  -5.201  35.615  1.00 19.65  ? 430 LEU B CD1 1 
ATOM   6588  C CD2 . LEU B 1 401 ? -3.830  -5.235  33.773  1.00 18.80  ? 430 LEU B CD2 1 
ATOM   6589  N N   . GLY B 1 402 ? -1.514  -0.393  33.197  1.00 18.04  ? 431 GLY B N   1 
ATOM   6590  C CA  . GLY B 1 402 ? -1.518  1.048   33.388  1.00 18.47  ? 431 GLY B CA  1 
ATOM   6591  C C   . GLY B 1 402 ? -1.629  1.802   32.064  1.00 20.34  ? 431 GLY B C   1 
ATOM   6592  O O   . GLY B 1 402 ? -2.495  2.681   31.901  1.00 16.87  ? 431 GLY B O   1 
ATOM   6593  N N   . VAL B 1 403 ? -0.783  1.427   31.108  1.00 19.73  ? 432 VAL B N   1 
ATOM   6594  C CA  . VAL B 1 403 ? -0.667  2.177   29.866  1.00 19.74  ? 432 VAL B CA  1 
ATOM   6595  C C   . VAL B 1 403 ? -1.960  2.049   29.067  1.00 19.75  ? 432 VAL B C   1 
ATOM   6596  O O   . VAL B 1 403 ? -2.382  3.010   28.436  1.00 21.94  ? 432 VAL B O   1 
ATOM   6597  C CB  . VAL B 1 403 ? 0.565   1.771   29.031  1.00 20.19  ? 432 VAL B CB  1 
ATOM   6598  C CG1 . VAL B 1 403 ? 1.866   2.000   29.796  1.00 21.64  ? 432 VAL B CG1 1 
ATOM   6599  C CG2 . VAL B 1 403 ? 0.464   0.332   28.548  1.00 20.91  ? 432 VAL B CG2 1 
ATOM   6600  N N   . LEU B 1 404 ? -2.608  0.874   29.095  1.00 18.89  ? 433 LEU B N   1 
ATOM   6601  C CA  . LEU B 1 404 ? -3.853  0.675   28.390  1.00 18.22  ? 433 LEU B CA  1 
ATOM   6602  C C   . LEU B 1 404 ? -5.031  1.345   29.108  1.00 17.53  ? 433 LEU B C   1 
ATOM   6603  O O   . LEU B 1 404 ? -5.941  1.800   28.447  1.00 18.07  ? 433 LEU B O   1 
ATOM   6604  C CB  . LEU B 1 404 ? -4.047  -0.825  28.159  1.00 17.97  ? 433 LEU B CB  1 
ATOM   6605  C CG  . LEU B 1 404 ? -2.994  -1.400  27.193  1.00 18.65  ? 433 LEU B CG  1 
ATOM   6606  C CD1 . LEU B 1 404 ? -3.199  -2.892  26.928  1.00 18.49  ? 433 LEU B CD1 1 
ATOM   6607  C CD2 . LEU B 1 404 ? -2.912  -0.613  25.888  1.00 18.49  ? 433 LEU B CD2 1 
ATOM   6608  N N   . ALA B 1 405 ? -5.014  1.396   30.451  1.00 18.49  ? 434 ALA B N   1 
ATOM   6609  C CA  . ALA B 1 405 ? -6.001  2.154   31.188  1.00 17.27  ? 434 ALA B CA  1 
ATOM   6610  C C   . ALA B 1 405 ? -5.955  3.602   30.729  1.00 18.32  ? 434 ALA B C   1 
ATOM   6611  O O   . ALA B 1 405 ? -7.002  4.186   30.435  1.00 17.32  ? 434 ALA B O   1 
ATOM   6612  C CB  . ALA B 1 405 ? -5.780  2.040   32.672  1.00 17.59  ? 434 ALA B CB  1 
ATOM   6613  N N   . GLN B 1 406 ? -4.749  4.147   30.599  1.00 17.63  ? 435 GLN B N   1 
ATOM   6614  C CA  . GLN B 1 406 ? -4.653  5.544   30.218  1.00 17.54  ? 435 GLN B CA  1 
ATOM   6615  C C   . GLN B 1 406 ? -5.058  5.723   28.756  1.00 17.03  ? 435 GLN B C   1 
ATOM   6616  O O   . GLN B 1 406 ? -5.566  6.767   28.371  1.00 14.50  ? 435 GLN B O   1 
ATOM   6617  C CB  . GLN B 1 406 ? -3.242  6.092   30.367  1.00 17.88  ? 435 GLN B CB  1 
ATOM   6618  C CG  . GLN B 1 406 ? -3.085  7.542   29.884  1.00 17.61  ? 435 GLN B CG  1 
ATOM   6619  C CD  . GLN B 1 406 ? -4.086  8.488   30.505  1.00 19.45  ? 435 GLN B CD  1 
ATOM   6620  O OE1 . GLN B 1 406 ? -4.432  8.382   31.679  1.00 19.88  ? 435 GLN B OE1 1 
ATOM   6621  N NE2 . GLN B 1 406 ? -4.508  9.482   29.736  1.00 18.76  ? 435 GLN B NE2 1 
ATOM   6622  N N   . LEU B 1 407 ? -4.612  4.801   27.897  1.00 16.13  ? 436 LEU B N   1 
ATOM   6623  C CA  . LEU B 1 407 ? -4.881  4.928   26.473  1.00 16.93  ? 436 LEU B CA  1 
ATOM   6624  C C   . LEU B 1 407 ? -6.384  5.082   26.235  1.00 18.28  ? 436 LEU B C   1 
ATOM   6625  O O   . LEU B 1 407 ? -6.814  5.857   25.389  1.00 21.38  ? 436 LEU B O   1 
ATOM   6626  C CB  . LEU B 1 407 ? -4.345  3.688   25.751  1.00 18.42  ? 436 LEU B CB  1 
ATOM   6627  C CG  . LEU B 1 407 ? -4.253  3.827   24.236  1.00 20.59  ? 436 LEU B CG  1 
ATOM   6628  C CD1 . LEU B 1 407 ? -3.260  4.898   23.886  1.00 21.43  ? 436 LEU B CD1 1 
ATOM   6629  C CD2 . LEU B 1 407 ? -3.868  2.507   23.595  1.00 21.94  ? 436 LEU B CD2 1 
ATOM   6630  N N   . ILE B 1 408 ? -7.178  4.350   27.016  1.00 19.66  ? 437 ILE B N   1 
ATOM   6631  C CA  . ILE B 1 408 ? -8.621  4.403   26.885  1.00 19.68  ? 437 ILE B CA  1 
ATOM   6632  C C   . ILE B 1 408 ? -9.027  5.846   27.165  1.00 20.14  ? 437 ILE B C   1 
ATOM   6633  O O   . ILE B 1 408 ? -9.835  6.399   26.413  1.00 21.68  ? 437 ILE B O   1 
ATOM   6634  C CB  . ILE B 1 408 ? -9.291  3.426   27.863  1.00 21.02  ? 437 ILE B CB  1 
ATOM   6635  C CG1 . ILE B 1 408 ? -9.030  1.969   27.493  1.00 20.66  ? 437 ILE B CG1 1 
ATOM   6636  C CG2 . ILE B 1 408 ? -10.777 3.716   27.972  1.00 22.55  ? 437 ILE B CG2 1 
ATOM   6637  C CD1 . ILE B 1 408 ? -9.365  1.024   28.617  1.00 21.20  ? 437 ILE B CD1 1 
ATOM   6638  N N   . TRP B 1 409 ? -8.445  6.426   28.221  1.00 20.16  ? 438 TRP B N   1 
ATOM   6639  C CA  . TRP B 1 409 ? -8.789  7.782   28.628  1.00 20.50  ? 438 TRP B CA  1 
ATOM   6640  C C   . TRP B 1 409 ? -8.248  8.824   27.654  1.00 20.47  ? 438 TRP B C   1 
ATOM   6641  O O   . TRP B 1 409 ? -8.916  9.818   27.358  1.00 15.98  ? 438 TRP B O   1 
ATOM   6642  C CB  . TRP B 1 409 ? -8.354  8.059   30.077  1.00 21.56  ? 438 TRP B CB  1 
ATOM   6643  C CG  . TRP B 1 409 ? -9.346  7.510   31.049  1.00 20.88  ? 438 TRP B CG  1 
ATOM   6644  C CD1 . TRP B 1 409 ? -9.308  6.302   31.672  1.00 22.81  ? 438 TRP B CD1 1 
ATOM   6645  C CD2 . TRP B 1 409 ? -10.604 8.103   31.416  1.00 21.82  ? 438 TRP B CD2 1 
ATOM   6646  N NE1 . TRP B 1 409 ? -10.451 6.094   32.397  1.00 21.71  ? 438 TRP B NE1 1 
ATOM   6647  C CE2 . TRP B 1 409 ? -11.260 7.194   32.267  1.00 21.50  ? 438 TRP B CE2 1 
ATOM   6648  C CE3 . TRP B 1 409 ? -11.231 9.316   31.111  1.00 23.93  ? 438 TRP B CE3 1 
ATOM   6649  C CZ2 . TRP B 1 409 ? -12.518 7.447   32.796  1.00 23.45  ? 438 TRP B CZ2 1 
ATOM   6650  C CZ3 . TRP B 1 409 ? -12.488 9.567   31.625  1.00 20.23  ? 438 TRP B CZ3 1 
ATOM   6651  C CH2 . TRP B 1 409 ? -13.087 8.666   32.506  1.00 23.18  ? 438 TRP B CH2 1 
ATOM   6652  N N   . SER B 1 410 ? -7.009  8.649   27.192  1.00 17.24  ? 439 SER B N   1 
ATOM   6653  C CA  . SER B 1 410 ? -6.450  9.564   26.197  1.00 18.35  ? 439 SER B CA  1 
ATOM   6654  C C   . SER B 1 410 ? -7.394  9.730   25.005  1.00 17.64  ? 439 SER B C   1 
ATOM   6655  O O   . SER B 1 410 ? -7.605  10.837  24.492  1.00 19.02  ? 439 SER B O   1 
ATOM   6656  C CB  . SER B 1 410 ? -5.083  9.105   25.756  1.00 17.27  ? 439 SER B CB  1 
ATOM   6657  O OG  . SER B 1 410 ? -4.222  8.941   26.863  1.00 18.33  ? 439 SER B OG  1 
ATOM   6658  N N   . ARG B 1 411 ? -7.954  8.611   24.536  1.00 17.17  ? 440 ARG B N   1 
ATOM   6659  C CA  . ARG B 1 411 ? -8.812  8.606   23.372  1.00 20.48  ? 440 ARG B CA  1 
ATOM   6660  C C   . ARG B 1 411 ? -10.177 9.146   23.790  1.00 20.40  ? 440 ARG B C   1 
ATOM   6661  O O   . ARG B 1 411 ? -10.790 9.875   23.019  1.00 20.52  ? 440 ARG B O   1 
ATOM   6662  C CB  . ARG B 1 411 ? -8.903  7.210   22.746  1.00 21.48  ? 440 ARG B CB  1 
ATOM   6663  C CG  . ARG B 1 411 ? -7.609  6.779   22.068  1.00 23.71  ? 440 ARG B CG  1 
ATOM   6664  C CD  . ARG B 1 411 ? -7.135  7.746   20.972  1.00 29.01  ? 440 ARG B CD  1 
ATOM   6665  N NE  . ARG B 1 411 ? -5.796  7.379   20.535  1.00 36.13  ? 440 ARG B NE  1 
ATOM   6666  C CZ  . ARG B 1 411 ? -5.453  6.161   20.127  1.00 35.87  ? 440 ARG B CZ  1 
ATOM   6667  N NH1 . ARG B 1 411 ? -6.326  5.395   19.496  1.00 44.05  ? 440 ARG B NH1 1 
ATOM   6668  N NH2 . ARG B 1 411 ? -4.209  5.743   20.256  1.00 27.95  ? 440 ARG B NH2 1 
ATOM   6669  N N   . ALA B 1 412 ? -10.609 8.816   25.018  1.00 18.14  ? 441 ALA B N   1 
ATOM   6670  C CA  . ALA B 1 412 ? -11.931 9.254   25.474  1.00 18.04  ? 441 ALA B CA  1 
ATOM   6671  C C   . ALA B 1 412 ? -11.982 10.770  25.568  1.00 18.99  ? 441 ALA B C   1 
ATOM   6672  O O   . ALA B 1 412 ? -13.048 11.352  25.316  1.00 21.04  ? 441 ALA B O   1 
ATOM   6673  C CB  . ALA B 1 412 ? -12.272 8.600   26.793  1.00 16.88  ? 441 ALA B CB  1 
ATOM   6674  N N   . LEU B 1 413 ? -10.837 11.373  25.884  1.00 18.06  ? 442 LEU B N   1 
ATOM   6675  C CA  . LEU B 1 413 ? -10.725 12.805  26.145  1.00 19.45  ? 442 LEU B CA  1 
ATOM   6676  C C   . LEU B 1 413 ? -10.226 13.558  24.923  1.00 19.63  ? 442 LEU B C   1 
ATOM   6677  O O   . LEU B 1 413 ? -10.092 14.775  24.965  1.00 21.31  ? 442 LEU B O   1 
ATOM   6678  C CB  . LEU B 1 413 ? -9.804  13.034  27.351  1.00 20.54  ? 442 LEU B CB  1 
ATOM   6679  C CG  . LEU B 1 413 ? -10.298 12.437  28.664  1.00 21.73  ? 442 LEU B CG  1 
ATOM   6680  C CD1 . LEU B 1 413 ? -9.381  12.805  29.812  1.00 22.32  ? 442 LEU B CD1 1 
ATOM   6681  C CD2 . LEU B 1 413 ? -11.745 12.880  28.949  1.00 21.17  ? 442 LEU B CD2 1 
ATOM   6682  N N   . GLY B 1 414 ? -9.991  12.859  23.815  1.00 23.71  ? 443 GLY B N   1 
ATOM   6683  C CA  . GLY B 1 414 ? -9.580  13.523  22.586  1.00 22.77  ? 443 GLY B CA  1 
ATOM   6684  C C   . GLY B 1 414 ? -8.201  14.188  22.663  1.00 22.23  ? 443 GLY B C   1 
ATOM   6685  O O   . GLY B 1 414 ? -7.928  15.120  21.900  1.00 20.06  ? 443 GLY B O   1 
ATOM   6686  N N   . PHE B 1 415 ? -7.287  13.665  23.506  1.00 19.77  ? 444 PHE B N   1 
ATOM   6687  C CA  . PHE B 1 415 ? -5.922  14.163  23.543  1.00 18.01  ? 444 PHE B CA  1 
ATOM   6688  C C   . PHE B 1 415 ? -5.348  14.109  22.128  1.00 17.37  ? 444 PHE B C   1 
ATOM   6689  O O   . PHE B 1 415 ? -5.406  13.090  21.470  1.00 16.72  ? 444 PHE B O   1 
ATOM   6690  C CB  . PHE B 1 415 ? -5.011  13.320  24.442  1.00 19.74  ? 444 PHE B CB  1 
ATOM   6691  C CG  . PHE B 1 415 ? -5.254  13.405  25.929  1.00 19.33  ? 444 PHE B CG  1 
ATOM   6692  C CD1 . PHE B 1 415 ? -6.229  14.245  26.455  1.00 19.86  ? 444 PHE B CD1 1 
ATOM   6693  C CD2 . PHE B 1 415 ? -4.484  12.659  26.808  1.00 19.47  ? 444 PHE B CD2 1 
ATOM   6694  C CE1 . PHE B 1 415 ? -6.397  14.352  27.831  1.00 20.87  ? 444 PHE B CE1 1 
ATOM   6695  C CE2 . PHE B 1 415 ? -4.669  12.741  28.180  1.00 19.69  ? 444 PHE B CE2 1 
ATOM   6696  C CZ  . PHE B 1 415 ? -5.641  13.589  28.692  1.00 21.89  ? 444 PHE B CZ  1 
ATOM   6697  N N   . PRO B 1 416 ? -4.722  15.185  21.623  1.00 18.70  ? 445 PRO B N   1 
ATOM   6698  C CA  . PRO B 1 416 ? -4.204  15.185  20.257  1.00 18.40  ? 445 PRO B CA  1 
ATOM   6699  C C   . PRO B 1 416 ? -2.828  14.536  20.115  1.00 20.40  ? 445 PRO B C   1 
ATOM   6700  O O   . PRO B 1 416 ? -2.244  14.101  21.100  1.00 17.37  ? 445 PRO B O   1 
ATOM   6701  C CB  . PRO B 1 416 ? -4.104  16.691  19.976  1.00 19.37  ? 445 PRO B CB  1 
ATOM   6702  C CG  . PRO B 1 416 ? -3.812  17.307  21.303  1.00 19.47  ? 445 PRO B CG  1 
ATOM   6703  C CD  . PRO B 1 416 ? -4.511  16.450  22.330  1.00 19.71  ? 445 PRO B CD  1 
ATOM   6704  N N   . LEU B 1 417 ? -2.347  14.509  18.865  1.00 19.02  ? 446 LEU B N   1 
ATOM   6705  C CA  . LEU B 1 417 ? -0.981  14.139  18.533  1.00 20.68  ? 446 LEU B CA  1 
ATOM   6706  C C   . LEU B 1 417 ? -0.005  14.874  19.451  1.00 22.59  ? 446 LEU B C   1 
ATOM   6707  O O   . LEU B 1 417 ? -0.068  16.108  19.600  1.00 21.79  ? 446 LEU B O   1 
ATOM   6708  C CB  . LEU B 1 417 ? -0.750  14.478  17.049  1.00 19.63  ? 446 LEU B CB  1 
ATOM   6709  C CG  . LEU B 1 417 ? 0.538   13.980  16.389  1.00 20.88  ? 446 LEU B CG  1 
ATOM   6710  C CD1 . LEU B 1 417 ? 0.327   12.646  15.714  1.00 19.93  ? 446 LEU B CD1 1 
ATOM   6711  C CD2 . LEU B 1 417 ? 1.064   14.954  15.360  1.00 21.68  ? 446 LEU B CD2 1 
ATOM   6712  N N   . GLU B 1 418 ? 0.926   14.101  20.045  1.00 20.25  ? 447 GLU B N   1 
ATOM   6713  C CA  . GLU B 1 418 ? 2.040   14.657  20.791  1.00 20.29  ? 447 GLU B CA  1 
ATOM   6714  C C   . GLU B 1 418 ? 3.167   15.039  19.829  1.00 18.25  ? 447 GLU B C   1 
ATOM   6715  O O   . GLU B 1 418 ? 3.761   14.194  19.187  1.00 18.68  ? 447 GLU B O   1 
ATOM   6716  C CB  . GLU B 1 418 ? 2.550   13.690  21.867  1.00 20.26  ? 447 GLU B CB  1 
ATOM   6717  C CG  . GLU B 1 418 ? 3.815   14.177  22.561  1.00 20.82  ? 447 GLU B CG  1 
ATOM   6718  C CD  . GLU B 1 418 ? 4.307   13.327  23.726  1.00 23.22  ? 447 GLU B CD  1 
ATOM   6719  O OE1 . GLU B 1 418 ? 3.466   12.871  24.543  1.00 26.03  ? 447 GLU B OE1 1 
ATOM   6720  O OE2 . GLU B 1 418 ? 5.534   13.144  23.822  1.00 20.73  ? 447 GLU B OE2 1 
ATOM   6721  N N   . ARG B 1 419 ? 3.467   16.336  19.738  1.00 18.32  ? 448 ARG B N   1 
ATOM   6722  C CA  . ARG B 1 419 ? 4.399   16.869  18.763  1.00 18.79  ? 448 ARG B CA  1 
ATOM   6723  C C   . ARG B 1 419 ? 5.075   18.094  19.380  1.00 20.31  ? 448 ARG B C   1 
ATOM   6724  O O   . ARG B 1 419 ? 4.708   19.241  19.101  1.00 22.55  ? 448 ARG B O   1 
ATOM   6725  C CB  . ARG B 1 419 ? 3.654   17.216  17.460  1.00 21.27  ? 448 ARG B CB  1 
ATOM   6726  C CG  . ARG B 1 419 ? 4.483   17.164  16.177  1.00 19.62  ? 448 ARG B CG  1 
ATOM   6727  C CD  . ARG B 1 419 ? 5.723   18.023  16.164  1.00 19.25  ? 448 ARG B CD  1 
ATOM   6728  N NE  . ARG B 1 419 ? 6.375   17.845  14.888  1.00 18.45  ? 448 ARG B NE  1 
ATOM   6729  C CZ  . ARG B 1 419 ? 7.620   18.228  14.627  1.00 20.30  ? 448 ARG B CZ  1 
ATOM   6730  N NH1 . ARG B 1 419 ? 8.147   17.957  13.445  1.00 22.11  ? 448 ARG B NH1 1 
ATOM   6731  N NH2 . ARG B 1 419 ? 8.345   18.829  15.550  1.00 22.51  ? 448 ARG B NH2 1 
ATOM   6732  N N   . PRO B 1 420 ? 6.101   17.915  20.237  1.00 19.58  ? 449 PRO B N   1 
ATOM   6733  C CA  . PRO B 1 420 ? 6.907   19.032  20.709  1.00 19.96  ? 449 PRO B CA  1 
ATOM   6734  C C   . PRO B 1 420 ? 7.834   19.563  19.618  1.00 20.17  ? 449 PRO B C   1 
ATOM   6735  O O   . PRO B 1 420 ? 7.950   19.020  18.514  1.00 17.36  ? 449 PRO B O   1 
ATOM   6736  C CB  . PRO B 1 420 ? 7.677   18.434  21.893  1.00 19.82  ? 449 PRO B CB  1 
ATOM   6737  C CG  . PRO B 1 420 ? 7.902   17.000  21.454  1.00 20.64  ? 449 PRO B CG  1 
ATOM   6738  C CD  . PRO B 1 420 ? 6.600   16.640  20.773  1.00 19.98  ? 449 PRO B CD  1 
ATOM   6739  N N   . LYS B 1 421 ? 8.409   20.738  19.912  1.00 18.35  ? 450 LYS B N   1 
ATOM   6740  C CA  . LYS B 1 421 ? 9.417   21.332  19.082  1.00 20.38  ? 450 LYS B CA  1 
ATOM   6741  C C   . LYS B 1 421 ? 10.800  20.889  19.533  1.00 19.34  ? 450 LYS B C   1 
ATOM   6742  O O   . LYS B 1 421 ? 11.062  20.792  20.718  1.00 19.94  ? 450 LYS B O   1 
ATOM   6743  C CB  . LYS B 1 421 ? 9.378   22.856  19.222  1.00 20.68  ? 450 LYS B CB  1 
ATOM   6744  C CG  . LYS B 1 421 ? 10.286  23.583  18.251  1.00 25.70  ? 450 LYS B CG  1 
ATOM   6745  C CD  . LYS B 1 421 ? 9.823   23.458  16.818  1.00 27.44  ? 450 LYS B CD  1 
ATOM   6746  C CE  . LYS B 1 421 ? 10.698  24.164  15.819  1.00 31.10  ? 450 LYS B CE  1 
ATOM   6747  N NZ  . LYS B 1 421 ? 10.013  24.267  14.515  1.00 36.04  ? 450 LYS B NZ  1 
ATOM   6748  N N   . SER B 1 422 ? 11.699  20.662  18.579  1.00 20.82  ? 451 SER B N   1 
ATOM   6749  C CA  . SER B 1 422 ? 13.071  20.372  18.934  1.00 21.57  ? 451 SER B CA  1 
ATOM   6750  C C   . SER B 1 422 ? 13.959  21.522  18.463  1.00 23.81  ? 451 SER B C   1 
ATOM   6751  O O   . SER B 1 422 ? 13.583  22.309  17.590  1.00 22.34  ? 451 SER B O   1 
ATOM   6752  C CB  . SER B 1 422 ? 13.525  19.031  18.376  1.00 20.44  ? 451 SER B CB  1 
ATOM   6753  O OG  . SER B 1 422 ? 13.645  19.104  16.975  1.00 20.62  ? 451 SER B OG  1 
ATOM   6754  N N   . MET B 1 423 ? 15.161  21.601  19.020  1.00 23.77  ? 452 MET B N   1 
ATOM   6755  C CA  . MET B 1 423 ? 16.158  22.495  18.470  1.00 24.24  ? 452 MET B CA  1 
ATOM   6756  C C   . MET B 1 423 ? 17.484  21.767  18.410  1.00 25.54  ? 452 MET B C   1 
ATOM   6757  O O   . MET B 1 423 ? 17.653  20.757  19.097  1.00 30.91  ? 452 MET B O   1 
ATOM   6758  C CB  . MET B 1 423 ? 16.284  23.734  19.345  1.00 26.94  ? 452 MET B CB  1 
ATOM   6759  C CG  . MET B 1 423 ? 14.945  24.309  19.679  1.00 30.15  ? 452 MET B CG  1 
ATOM   6760  S SD  . MET B 1 423 ? 14.486  25.505  18.465  1.00 39.32  ? 452 MET B SD  1 
ATOM   6761  C CE  . MET B 1 423 ? 15.671  26.802  18.842  1.00 40.31  ? 452 MET B CE  1 
ATOM   6762  N N   . SER B 1 424 ? 18.371  22.263  17.541  1.00 23.90  ? 453 SER B N   1 
ATOM   6763  C CA  . SER B 1 424 ? 19.773  21.883  17.530  1.00 23.50  ? 453 SER B CA  1 
ATOM   6764  C C   . SER B 1 424 ? 20.508  22.745  18.546  1.00 25.82  ? 453 SER B C   1 
ATOM   6765  O O   . SER B 1 424 ? 19.978  23.752  19.006  1.00 26.39  ? 453 SER B O   1 
ATOM   6766  C CB  . SER B 1 424 ? 20.409  22.081  16.175  1.00 23.20  ? 453 SER B CB  1 
ATOM   6767  O OG  . SER B 1 424 ? 20.488  23.479  15.912  1.00 23.40  ? 453 SER B OG  1 
ATOM   6768  N N   . THR B 1 425 ? 21.737  22.329  18.847  1.00 26.86  ? 454 THR B N   1 
ATOM   6769  C CA  . THR B 1 425 ? 22.624  23.076  19.718  1.00 27.68  ? 454 THR B CA  1 
ATOM   6770  C C   . THR B 1 425 ? 22.907  24.431  19.082  1.00 29.80  ? 454 THR B C   1 
ATOM   6771  O O   . THR B 1 425 ? 22.827  25.463  19.743  1.00 29.92  ? 454 THR B O   1 
ATOM   6772  C CB  . THR B 1 425 ? 23.937  22.317  19.925  1.00 27.14  ? 454 THR B CB  1 
ATOM   6773  O OG1 . THR B 1 425 ? 23.638  21.141  20.674  1.00 24.12  ? 454 THR B OG1 1 
ATOM   6774  C CG2 . THR B 1 425 ? 24.982  23.149  20.631  1.00 29.31  ? 454 THR B CG2 1 
ATOM   6775  N N   . GLU B 1 426 ? 23.251  24.398  17.794  1.00 32.34  ? 455 GLU B N   1 
ATOM   6776  C CA  . GLU B 1 426 ? 23.509  25.601  17.027  1.00 36.08  ? 455 GLU B CA  1 
ATOM   6777  C C   . GLU B 1 426 ? 22.263  26.481  17.091  1.00 34.88  ? 455 GLU B C   1 
ATOM   6778  O O   . GLU B 1 426 ? 22.356  27.660  17.436  1.00 34.77  ? 455 GLU B O   1 
ATOM   6779  C CB  . GLU B 1 426 ? 23.942  25.196  15.616  1.00 41.25  ? 455 GLU B CB  1 
ATOM   6780  C CG  . GLU B 1 426 ? 24.462  26.346  14.765  1.00 49.68  ? 455 GLU B CG  1 
ATOM   6781  C CD  . GLU B 1 426 ? 25.419  25.936  13.653  1.00 57.00  ? 455 GLU B CD  1 
ATOM   6782  O OE1 . GLU B 1 426 ? 26.136  24.913  13.825  1.00 56.09  ? 455 GLU B OE1 1 
ATOM   6783  O OE2 . GLU B 1 426 ? 25.435  26.627  12.600  1.00 61.76  ? 455 GLU B OE2 1 
ATOM   6784  N N   . GLY B 1 427 ? 21.093  25.878  16.829  1.00 30.51  ? 456 GLY B N   1 
ATOM   6785  C CA  . GLY B 1 427 ? 19.842  26.612  16.833  1.00 32.00  ? 456 GLY B CA  1 
ATOM   6786  C C   . GLY B 1 427 ? 19.508  27.172  18.212  1.00 29.99  ? 456 GLY B C   1 
ATOM   6787  O O   . GLY B 1 427 ? 18.965  28.270  18.326  1.00 29.48  ? 456 GLY B O   1 
ATOM   6788  N N   . LEU B 1 428 ? 19.830  26.397  19.255  1.00 29.93  ? 457 LEU B N   1 
ATOM   6789  C CA  . LEU B 1 428 ? 19.598  26.817  20.629  1.00 27.58  ? 457 LEU B CA  1 
ATOM   6790  C C   . LEU B 1 428 ? 20.561  27.950  20.988  1.00 29.62  ? 457 LEU B C   1 
ATOM   6791  O O   . LEU B 1 428 ? 20.129  28.974  21.510  1.00 34.31  ? 457 LEU B O   1 
ATOM   6792  C CB  . LEU B 1 428 ? 19.714  25.585  21.533  1.00 27.02  ? 457 LEU B CB  1 
ATOM   6793  C CG  . LEU B 1 428 ? 19.048  25.668  22.909  1.00 25.86  ? 457 LEU B CG  1 
ATOM   6794  C CD1 . LEU B 1 428 ? 17.626  26.195  22.829  1.00 24.59  ? 457 LEU B CD1 1 
ATOM   6795  C CD2 . LEU B 1 428 ? 19.017  24.293  23.554  1.00 23.81  ? 457 LEU B CD2 1 
ATOM   6796  N N   . MET B 1 429 ? 21.841  27.855  20.598  1.00 30.98  ? 458 MET B N   1 
ATOM   6797  C CA  . MET B 1 429 ? 22.805  28.910  20.899  1.00 36.19  ? 458 MET B CA  1 
ATOM   6798  C C   . MET B 1 429 ? 22.344  30.258  20.331  1.00 36.47  ? 458 MET B C   1 
ATOM   6799  O O   . MET B 1 429 ? 22.607  31.309  20.913  1.00 37.03  ? 458 MET B O   1 
ATOM   6800  C CB  . MET B 1 429 ? 24.195  28.582  20.338  1.00 37.01  ? 458 MET B CB  1 
ATOM   6801  C CG  . MET B 1 429 ? 25.015  27.655  21.232  1.00 38.32  ? 458 MET B CG  1 
ATOM   6802  S SD  . MET B 1 429 ? 26.416  26.919  20.323  1.00 38.58  ? 458 MET B SD  1 
ATOM   6803  C CE  . MET B 1 429 ? 27.804  27.531  21.280  1.00 44.15  ? 458 MET B CE  1 
ATOM   6804  N N   . LYS B 1 430 ? 21.637  30.231  19.202  1.00 39.35  ? 459 LYS B N   1 
ATOM   6805  C CA  . LYS B 1 430 ? 21.186  31.451  18.551  1.00 41.75  ? 459 LYS B CA  1 
ATOM   6806  C C   . LYS B 1 430 ? 19.878  31.939  19.183  1.00 40.54  ? 459 LYS B C   1 
ATOM   6807  O O   . LYS B 1 430 ? 19.639  33.143  19.283  1.00 38.71  ? 459 LYS B O   1 
ATOM   6808  C CB  . LYS B 1 430 ? 21.140  31.195  17.040  1.00 46.04  ? 459 LYS B CB  1 
ATOM   6809  C CG  . LYS B 1 430 ? 22.521  31.037  16.414  1.00 51.40  ? 459 LYS B CG  1 
ATOM   6810  C CD  . LYS B 1 430 ? 22.551  30.883  14.908  1.00 56.14  ? 459 LYS B CD  1 
ATOM   6811  C CE  . LYS B 1 430 ? 22.358  29.456  14.437  1.00 59.69  ? 459 LYS B CE  1 
ATOM   6812  N NZ  . LYS B 1 430 ? 22.733  29.310  13.010  1.00 63.83  ? 459 LYS B NZ  1 
ATOM   6813  N N   . PHE B 1 431 ? 19.068  31.014  19.698  1.00 40.26  ? 460 PHE B N   1 
ATOM   6814  C CA  . PHE B 1 431 ? 17.797  31.364  20.317  1.00 42.42  ? 460 PHE B CA  1 
ATOM   6815  C C   . PHE B 1 431 ? 18.018  32.064  21.659  1.00 41.76  ? 460 PHE B C   1 
ATOM   6816  O O   . PHE B 1 431 ? 17.287  32.989  22.000  1.00 38.60  ? 460 PHE B O   1 
ATOM   6817  C CB  . PHE B 1 431 ? 16.927  30.116  20.474  1.00 44.79  ? 460 PHE B CB  1 
ATOM   6818  C CG  . PHE B 1 431 ? 15.520  30.392  20.946  1.00 49.58  ? 460 PHE B CG  1 
ATOM   6819  C CD1 . PHE B 1 431 ? 14.567  30.913  20.080  1.00 50.04  ? 460 PHE B CD1 1 
ATOM   6820  C CD2 . PHE B 1 431 ? 15.154  30.148  22.260  1.00 45.19  ? 460 PHE B CD2 1 
ATOM   6821  C CE1 . PHE B 1 431 ? 13.271  31.151  20.517  1.00 49.64  ? 460 PHE B CE1 1 
ATOM   6822  C CE2 . PHE B 1 431 ? 13.858  30.385  22.692  1.00 46.32  ? 460 PHE B CE2 1 
ATOM   6823  C CZ  . PHE B 1 431 ? 12.921  30.889  21.823  1.00 48.08  ? 460 PHE B CZ  1 
ATOM   6824  N N   . VAL B 1 432 ? 19.056  31.643  22.396  1.00 44.57  ? 461 VAL B N   1 
ATOM   6825  C CA  . VAL B 1 432 ? 19.421  32.258  23.665  1.00 45.09  ? 461 VAL B CA  1 
ATOM   6826  C C   . VAL B 1 432 ? 20.116  33.602  23.423  1.00 47.40  ? 461 VAL B C   1 
ATOM   6827  O O   . VAL B 1 432 ? 20.274  34.393  24.353  1.00 40.06  ? 461 VAL B O   1 
ATOM   6828  C CB  . VAL B 1 432 ? 20.301  31.312  24.500  1.00 44.79  ? 461 VAL B CB  1 
ATOM   6829  C CG1 . VAL B 1 432 ? 20.769  31.969  25.788  1.00 45.35  ? 461 VAL B CG1 1 
ATOM   6830  C CG2 . VAL B 1 432 ? 19.588  30.004  24.809  1.00 46.20  ? 461 VAL B CG2 1 
ATOM   6831  N N   . ASP B 1 433 ? 20.521  33.852  22.167  1.00 51.35  ? 462 ASP B N   1 
ATOM   6832  C CA  . ASP B 1 433 ? 21.097  35.123  21.756  1.00 57.68  ? 462 ASP B CA  1 
ATOM   6833  C C   . ASP B 1 433 ? 20.094  35.921  20.922  1.00 56.71  ? 462 ASP B C   1 
ATOM   6834  O O   . ASP B 1 433 ? 20.379  36.239  19.769  1.00 61.72  ? 462 ASP B O   1 
ATOM   6835  C CB  . ASP B 1 433 ? 22.384  34.905  20.950  1.00 57.36  ? 462 ASP B CB  1 
ATOM   6836  C CG  . ASP B 1 433 ? 23.545  34.333  21.747  1.00 60.64  ? 462 ASP B CG  1 
ATOM   6837  O OD1 . ASP B 1 433 ? 23.448  34.283  22.997  1.00 56.52  ? 462 ASP B OD1 1 
ATOM   6838  O OD2 . ASP B 1 433 ? 24.540  33.934  21.106  1.00 58.92  ? 462 ASP B OD2 1 
ATOM   6839  N N   . SER B 1 434 ? 18.934  36.247  21.511  1.00 58.87  ? 463 SER B N   1 
ATOM   6840  C CA  . SER B 1 434 ? 17.923  37.073  20.860  1.00 61.17  ? 463 SER B CA  1 
ATOM   6841  C C   . SER B 1 434 ? 16.596  36.973  21.618  1.00 57.45  ? 463 SER B C   1 
ATOM   6842  O O   . SER B 1 434 ? 15.595  37.503  21.082  1.00 49.39  ? 463 SER B O   1 
ATOM   6843  C CB  . SER B 1 434 ? 17.720  36.720  19.392  1.00 61.85  ? 463 SER B CB  1 
ATOM   6844  O OG  . SER B 1 434 ? 17.414  35.341  19.227  1.00 62.44  ? 463 SER B OG  1 
ATOM   6845  N N   . SER C 1 1   ? -13.065 49.869  41.941  1.00 30.00  ? 30  SER C N   1 
ATOM   6846  C CA  . SER C 1 1   ? -11.753 50.037  42.641  1.00 30.00  ? 30  SER C CA  1 
ATOM   6847  C C   . SER C 1 1   ? -10.615 50.101  41.615  1.00 30.00  ? 30  SER C C   1 
ATOM   6848  O O   . SER C 1 1   ? -10.123 49.033  41.233  1.00 30.00  ? 30  SER C O   1 
ATOM   6849  C CB  . SER C 1 1   ? -11.513 48.941  43.649  1.00 30.00  ? 30  SER C CB  1 
ATOM   6850  O OG  . SER C 1 1   ? -10.956 49.458  44.851  1.00 30.00  ? 30  SER C OG  1 
ATOM   6851  N N   . THR C 1 2   ? -10.171 51.304  41.232  1.00 63.24  ? 31  THR C N   1 
ATOM   6852  C CA  . THR C 1 2   ? -9.174  51.396  40.127  1.00 64.36  ? 31  THR C CA  1 
ATOM   6853  C C   . THR C 1 2   ? -7.908  52.130  40.529  1.00 55.22  ? 31  THR C C   1 
ATOM   6854  O O   . THR C 1 2   ? -6.828  51.672  40.145  1.00 64.44  ? 31  THR C O   1 
ATOM   6855  C CB  . THR C 1 2   ? -9.862  52.080  38.950  1.00 65.61  ? 31  THR C CB  1 
ATOM   6856  O OG1 . THR C 1 2   ? -10.865 51.158  38.535  1.00 67.42  ? 31  THR C OG1 1 
ATOM   6857  C CG2 . THR C 1 2   ? -8.921  52.365  37.793  1.00 63.33  ? 31  THR C CG2 1 
ATOM   6858  N N   . ASN C 1 3   ? -8.016  53.246  41.246  1.00 44.23  ? 32  ASN C N   1 
ATOM   6859  C CA  . ASN C 1 3   ? -6.828  53.974  41.762  1.00 33.04  ? 32  ASN C CA  1 
ATOM   6860  C C   . ASN C 1 3   ? -5.861  52.997  42.424  1.00 26.21  ? 32  ASN C C   1 
ATOM   6861  O O   . ASN C 1 3   ? -6.325  52.128  43.159  1.00 22.25  ? 32  ASN C O   1 
ATOM   6862  C CB  . ASN C 1 3   ? -7.258  55.033  42.766  1.00 34.89  ? 32  ASN C CB  1 
ATOM   6863  C CG  . ASN C 1 3   ? -6.188  56.052  43.063  1.00 31.92  ? 32  ASN C CG  1 
ATOM   6864  O OD1 . ASN C 1 3   ? -5.066  55.699  43.433  1.00 30.00  ? 32  ASN C OD1 1 
ATOM   6865  N ND2 . ASN C 1 3   ? -6.517  57.323  42.894  1.00 34.93  ? 32  ASN C ND2 1 
ATOM   6866  N N   . LEU C 1 4   ? -4.557  53.190  42.195  1.00 24.02  ? 33  LEU C N   1 
ATOM   6867  C CA  . LEU C 1 4   ? -3.544  52.328  42.854  1.00 23.72  ? 33  LEU C CA  1 
ATOM   6868  C C   . LEU C 1 4   ? -3.732  52.429  44.378  1.00 21.97  ? 33  LEU C C   1 
ATOM   6869  O O   . LEU C 1 4   ? -3.666  51.410  45.051  1.00 21.97  ? 33  LEU C O   1 
ATOM   6870  C CB  . LEU C 1 4   ? -2.136  52.747  42.432  1.00 23.87  ? 33  LEU C CB  1 
ATOM   6871  C CG  . LEU C 1 4   ? -0.965  52.044  43.118  1.00 25.26  ? 33  LEU C CG  1 
ATOM   6872  C CD1 . LEU C 1 4   ? -1.061  50.565  42.836  1.00 25.48  ? 33  LEU C CD1 1 
ATOM   6873  C CD2 . LEU C 1 4   ? 0.349   52.595  42.597  1.00 26.22  ? 33  LEU C CD2 1 
ATOM   6874  N N   . LYS C 1 5   ? -4.006  53.633  44.868  1.00 22.18  ? 34  LYS C N   1 
ATOM   6875  C CA  . LYS C 1 5   ? -4.092  53.809  46.309  1.00 23.75  ? 34  LYS C CA  1 
ATOM   6876  C C   . LYS C 1 5   ? -5.236  52.985  46.920  1.00 24.19  ? 34  LYS C C   1 
ATOM   6877  O O   . LYS C 1 5   ? -5.096  52.502  48.041  1.00 24.81  ? 34  LYS C O   1 
ATOM   6878  C CB  . LYS C 1 5   ? -4.167  55.307  46.608  1.00 23.50  ? 34  LYS C CB  1 
ATOM   6879  C CG  . LYS C 1 5   ? -3.994  55.666  48.073  1.00 24.19  ? 34  LYS C CG  1 
ATOM   6880  C CD  . LYS C 1 5   ? -4.058  57.158  48.284  1.00 23.32  ? 34  LYS C CD  1 
ATOM   6881  C CE  . LYS C 1 5   ? -4.078  57.533  49.749  1.00 24.33  ? 34  LYS C CE  1 
ATOM   6882  N NZ  . LYS C 1 5   ? -3.783  58.975  49.924  1.00 22.49  ? 34  LYS C NZ  1 
ATOM   6883  N N   . ASP C 1 6   ? -6.349  52.792  46.186  1.00 26.09  ? 35  ASP C N   1 
ATOM   6884  C CA  . ASP C 1 6   ? -7.498  52.043  46.693  1.00 27.18  ? 35  ASP C CA  1 
ATOM   6885  C C   . ASP C 1 6   ? -7.259  50.543  46.645  1.00 24.09  ? 35  ASP C C   1 
ATOM   6886  O O   . ASP C 1 6   ? -7.625  49.821  47.559  1.00 25.63  ? 35  ASP C O   1 
ATOM   6887  C CB  . ASP C 1 6   ? -8.781  52.402  45.944  1.00 28.55  ? 35  ASP C CB  1 
ATOM   6888  C CG  . ASP C 1 6   ? -9.207  53.807  46.310  1.00 31.34  ? 35  ASP C CG  1 
ATOM   6889  O OD1 . ASP C 1 6   ? -9.411  54.054  47.529  1.00 35.35  ? 35  ASP C OD1 1 
ATOM   6890  O OD2 . ASP C 1 6   ? -9.255  54.647  45.410  1.00 32.79  ? 35  ASP C OD2 1 
ATOM   6891  N N   . ILE C 1 7   ? -6.614  50.097  45.577  1.00 25.64  ? 36  ILE C N   1 
ATOM   6892  C CA  . ILE C 1 7   ? -6.185  48.716  45.454  1.00 25.04  ? 36  ILE C CA  1 
ATOM   6893  C C   . ILE C 1 7   ? -5.252  48.371  46.615  1.00 24.33  ? 36  ILE C C   1 
ATOM   6894  O O   . ILE C 1 7   ? -5.344  47.322  47.227  1.00 20.56  ? 36  ILE C O   1 
ATOM   6895  C CB  . ILE C 1 7   ? -5.509  48.548  44.078  1.00 27.86  ? 36  ILE C CB  1 
ATOM   6896  C CG1 . ILE C 1 7   ? -6.502  48.842  42.944  1.00 30.70  ? 36  ILE C CG1 1 
ATOM   6897  C CG2 . ILE C 1 7   ? -4.892  47.163  43.950  1.00 30.25  ? 36  ILE C CG2 1 
ATOM   6898  C CD1 . ILE C 1 7   ? -5.875  48.976  41.573  1.00 31.59  ? 36  ILE C CD1 1 
ATOM   6899  N N   . LEU C 1 8   ? -4.369  49.315  46.940  1.00 24.03  ? 37  LEU C N   1 
ATOM   6900  C CA  . LEU C 1 8   ? -3.385  49.114  47.976  1.00 26.17  ? 37  LEU C CA  1 
ATOM   6901  C C   . LEU C 1 8   ? -4.080  49.062  49.342  1.00 23.60  ? 37  LEU C C   1 
ATOM   6902  O O   . LEU C 1 8   ? -3.809  48.172  50.136  1.00 22.78  ? 37  LEU C O   1 
ATOM   6903  C CB  . LEU C 1 8   ? -2.384  50.269  47.851  1.00 26.45  ? 37  LEU C CB  1 
ATOM   6904  C CG  . LEU C 1 8   ? -1.264  50.291  48.871  1.00 26.10  ? 37  LEU C CG  1 
ATOM   6905  C CD1 . LEU C 1 8   ? -0.588  48.922  48.930  1.00 25.46  ? 37  LEU C CD1 1 
ATOM   6906  C CD2 . LEU C 1 8   ? -0.268  51.400  48.539  1.00 27.75  ? 37  LEU C CD2 1 
ATOM   6907  N N   . ALA C 1 9   ? -5.013  49.996  49.569  1.00 23.60  ? 38  ALA C N   1 
ATOM   6908  C CA  . ALA C 1 9   ? -5.818  50.032  50.789  1.00 24.63  ? 38  ALA C CA  1 
ATOM   6909  C C   . ALA C 1 9   ? -6.494  48.682  51.048  1.00 25.05  ? 38  ALA C C   1 
ATOM   6910  O O   . ALA C 1 9   ? -6.596  48.240  52.195  1.00 25.11  ? 38  ALA C O   1 
ATOM   6911  C CB  . ALA C 1 9   ? -6.862  51.119  50.679  1.00 24.14  ? 38  ALA C CB  1 
ATOM   6912  N N   . ASP C 1 10  ? -6.954  48.035  49.977  1.00 26.76  ? 39  ASP C N   1 
ATOM   6913  C CA  . ASP C 1 10  ? -7.674  46.777  50.124  1.00 29.45  ? 39  ASP C CA  1 
ATOM   6914  C C   . ASP C 1 10  ? -6.742  45.617  50.462  1.00 28.12  ? 39  ASP C C   1 
ATOM   6915  O O   . ASP C 1 10  ? -7.184  44.650  51.086  1.00 24.70  ? 39  ASP C O   1 
ATOM   6916  C CB  . ASP C 1 10  ? -8.478  46.444  48.865  1.00 32.66  ? 39  ASP C CB  1 
ATOM   6917  C CG  . ASP C 1 10  ? -9.659  47.368  48.659  1.00 33.18  ? 39  ASP C CG  1 
ATOM   6918  O OD1 . ASP C 1 10  ? -10.119 47.911  49.658  1.00 34.19  ? 39  ASP C OD1 1 
ATOM   6919  O OD2 . ASP C 1 10  ? -10.074 47.557  47.491  1.00 41.00  ? 39  ASP C OD2 1 
ATOM   6920  N N   . LEU C 1 11  ? -5.491  45.695  49.993  1.00 24.74  ? 40  LEU C N   1 
ATOM   6921  C CA  . LEU C 1 11  ? -4.535  44.612  50.167  1.00 24.79  ? 40  LEU C CA  1 
ATOM   6922  C C   . LEU C 1 11  ? -3.948  44.625  51.577  1.00 25.16  ? 40  LEU C C   1 
ATOM   6923  O O   . LEU C 1 11  ? -3.562  43.586  52.115  1.00 24.19  ? 40  LEU C O   1 
ATOM   6924  C CB  . LEU C 1 11  ? -3.420  44.795  49.143  1.00 25.37  ? 40  LEU C CB  1 
ATOM   6925  C CG  . LEU C 1 11  ? -3.777  44.476  47.691  1.00 24.17  ? 40  LEU C CG  1 
ATOM   6926  C CD1 . LEU C 1 11  ? -2.603  44.793  46.792  1.00 26.17  ? 40  LEU C CD1 1 
ATOM   6927  C CD2 . LEU C 1 11  ? -4.160  43.018  47.538  1.00 23.27  ? 40  LEU C CD2 1 
ATOM   6928  N N   . ILE C 1 12  ? -3.840  45.820  52.162  1.00 25.46  ? 41  ILE C N   1 
ATOM   6929  C CA  . ILE C 1 12  ? -3.096  45.992  53.393  1.00 26.30  ? 41  ILE C CA  1 
ATOM   6930  C C   . ILE C 1 12  ? -3.693  45.176  54.542  1.00 26.76  ? 41  ILE C C   1 
ATOM   6931  O O   . ILE C 1 12  ? -2.941  44.462  55.198  1.00 28.27  ? 41  ILE C O   1 
ATOM   6932  C CB  . ILE C 1 12  ? -2.960  47.482  53.718  1.00 25.75  ? 41  ILE C CB  1 
ATOM   6933  C CG1 . ILE C 1 12  ? -1.801  48.079  52.912  1.00 23.30  ? 41  ILE C CG1 1 
ATOM   6934  C CG2 . ILE C 1 12  ? -2.787  47.683  55.205  1.00 26.90  ? 41  ILE C CG2 1 
ATOM   6935  C CD1 . ILE C 1 12  ? -1.767  49.602  52.915  1.00 23.05  ? 41  ILE C CD1 1 
ATOM   6936  N N   . PRO C 1 13  ? -5.022  45.198  54.825  1.00 26.58  ? 42  PRO C N   1 
ATOM   6937  C CA  . PRO C 1 13  ? -5.582  44.422  55.936  1.00 26.81  ? 42  PRO C CA  1 
ATOM   6938  C C   . PRO C 1 13  ? -5.353  42.916  55.867  1.00 29.61  ? 42  PRO C C   1 
ATOM   6939  O O   . PRO C 1 13  ? -5.045  42.308  56.897  1.00 28.02  ? 42  PRO C O   1 
ATOM   6940  C CB  . PRO C 1 13  ? -7.095  44.700  55.879  1.00 27.87  ? 42  PRO C CB  1 
ATOM   6941  C CG  . PRO C 1 13  ? -7.204  46.013  55.155  1.00 26.36  ? 42  PRO C CG  1 
ATOM   6942  C CD  . PRO C 1 13  ? -6.065  45.993  54.147  1.00 27.80  ? 42  PRO C CD  1 
ATOM   6943  N N   . LYS C 1 14  ? -5.465  42.358  54.653  1.00 32.29  ? 43  LYS C N   1 
ATOM   6944  C CA  . LYS C 1 14  ? -5.189  40.952  54.373  1.00 33.34  ? 43  LYS C CA  1 
ATOM   6945  C C   . LYS C 1 14  ? -3.778  40.581  54.826  1.00 29.68  ? 43  LYS C C   1 
ATOM   6946  O O   . LYS C 1 14  ? -3.521  39.489  55.327  1.00 31.13  ? 43  LYS C O   1 
ATOM   6947  C CB  . LYS C 1 14  ? -5.181  40.632  52.872  1.00 41.50  ? 43  LYS C CB  1 
ATOM   6948  C CG  . LYS C 1 14  ? -6.227  41.299  51.988  1.00 45.43  ? 43  LYS C CG  1 
ATOM   6949  C CD  . LYS C 1 14  ? -7.566  40.594  51.937  1.00 50.29  ? 43  LYS C CD  1 
ATOM   6950  C CE  . LYS C 1 14  ? -8.464  41.165  50.855  1.00 53.35  ? 43  LYS C CE  1 
ATOM   6951  N NZ  . LYS C 1 14  ? -9.738  40.418  50.738  1.00 51.50  ? 43  LYS C NZ  1 
ATOM   6952  N N   . GLU C 1 15  ? -2.840  41.492  54.589  1.00 27.16  ? 44  GLU C N   1 
ATOM   6953  C CA  . GLU C 1 15  ? -1.438  41.201  54.814  1.00 28.12  ? 44  GLU C CA  1 
ATOM   6954  C C   . GLU C 1 15  ? -1.122  41.360  56.298  1.00 26.93  ? 44  GLU C C   1 
ATOM   6955  O O   . GLU C 1 15  ? -0.380  40.564  56.856  1.00 29.45  ? 44  GLU C O   1 
ATOM   6956  C CB  . GLU C 1 15  ? -0.577  42.093  53.917  1.00 33.87  ? 44  GLU C CB  1 
ATOM   6957  C CG  . GLU C 1 15  ? -0.491  41.617  52.477  1.00 36.49  ? 44  GLU C CG  1 
ATOM   6958  C CD  . GLU C 1 15  ? -0.065  40.167  52.293  1.00 38.87  ? 44  GLU C CD  1 
ATOM   6959  O OE1 . GLU C 1 15  ? 0.955   39.767  52.893  1.00 39.20  ? 44  GLU C OE1 1 
ATOM   6960  O OE2 . GLU C 1 15  ? -0.751  39.450  51.540  1.00 43.74  ? 44  GLU C OE2 1 
ATOM   6961  N N   . GLN C 1 16  ? -1.677  42.401  56.935  1.00 27.92  ? 45  GLN C N   1 
ATOM   6962  C CA  . GLN C 1 16  ? -1.588  42.543  58.376  1.00 27.85  ? 45  GLN C CA  1 
ATOM   6963  C C   . GLN C 1 16  ? -2.101  41.264  59.042  1.00 29.10  ? 45  GLN C C   1 
ATOM   6964  O O   . GLN C 1 16  ? -1.487  40.754  59.974  1.00 30.01  ? 45  GLN C O   1 
ATOM   6965  C CB  . GLN C 1 16  ? -2.408  43.747  58.825  1.00 28.29  ? 45  GLN C CB  1 
ATOM   6966  C CG  . GLN C 1 16  ? -1.819  45.067  58.400  1.00 27.12  ? 45  GLN C CG  1 
ATOM   6967  C CD  . GLN C 1 16  ? -2.723  46.210  58.763  1.00 29.23  ? 45  GLN C CD  1 
ATOM   6968  O OE1 . GLN C 1 16  ? -3.888  46.017  59.109  1.00 33.18  ? 45  GLN C OE1 1 
ATOM   6969  N NE2 . GLN C 1 16  ? -2.194  47.417  58.674  1.00 28.73  ? 45  GLN C NE2 1 
ATOM   6970  N N   . ALA C 1 17  ? -3.255  40.782  58.580  1.00 32.02  ? 46  ALA C N   1 
ATOM   6971  C CA  . ALA C 1 17  ? -3.859  39.585  59.131  1.00 33.39  ? 46  ALA C CA  1 
ATOM   6972  C C   . ALA C 1 17  ? -2.929  38.388  58.937  1.00 34.04  ? 46  ALA C C   1 
ATOM   6973  O O   . ALA C 1 17  ? -2.697  37.612  59.870  1.00 34.62  ? 46  ALA C O   1 
ATOM   6974  C CB  . ALA C 1 17  ? -5.208  39.352  58.494  1.00 36.90  ? 46  ALA C CB  1 
ATOM   6975  N N   . ARG C 1 18  ? -2.350  38.269  57.738  1.00 31.94  ? 47  ARG C N   1 
ATOM   6976  C CA  . ARG C 1 18  ? -1.525  37.123  57.405  1.00 30.94  ? 47  ARG C CA  1 
ATOM   6977  C C   . ARG C 1 18  ? -0.241  37.125  58.240  1.00 30.69  ? 47  ARG C C   1 
ATOM   6978  O O   . ARG C 1 18  ? 0.241   36.053  58.579  1.00 30.91  ? 47  ARG C O   1 
ATOM   6979  C CB  . ARG C 1 18  ? -1.232  37.093  55.906  1.00 35.12  ? 47  ARG C CB  1 
ATOM   6980  C CG  . ARG C 1 18  ? -0.086  36.189  55.479  1.00 43.15  ? 47  ARG C CG  1 
ATOM   6981  C CD  . ARG C 1 18  ? -0.175  35.896  53.993  1.00 49.72  ? 47  ARG C CD  1 
ATOM   6982  N NE  . ARG C 1 18  ? 1.123   35.955  53.331  1.00 62.22  ? 47  ARG C NE  1 
ATOM   6983  C CZ  . ARG C 1 18  ? 1.605   35.029  52.502  1.00 73.75  ? 47  ARG C CZ  1 
ATOM   6984  N NH1 . ARG C 1 18  ? 2.775   35.214  51.912  1.00 71.32  ? 47  ARG C NH1 1 
ATOM   6985  N NH2 . ARG C 1 18  ? 0.913   33.927  52.252  1.00 77.60  ? 47  ARG C NH2 1 
ATOM   6986  N N   . ILE C 1 19  ? 0.292   38.303  58.581  1.00 26.14  ? 48  ILE C N   1 
ATOM   6987  C CA  . ILE C 1 19  ? 1.530   38.386  59.345  1.00 29.44  ? 48  ILE C CA  1 
ATOM   6988  C C   . ILE C 1 19  ? 1.228   38.139  60.821  1.00 31.59  ? 48  ILE C C   1 
ATOM   6989  O O   . ILE C 1 19  ? 2.006   37.474  61.495  1.00 34.03  ? 48  ILE C O   1 
ATOM   6990  C CB  . ILE C 1 19  ? 2.235   39.739  59.126  1.00 29.90  ? 48  ILE C CB  1 
ATOM   6991  C CG1 . ILE C 1 19  ? 2.860   39.816  57.730  1.00 31.97  ? 48  ILE C CG1 1 
ATOM   6992  C CG2 . ILE C 1 19  ? 3.262   40.011  60.219  1.00 28.21  ? 48  ILE C CG2 1 
ATOM   6993  C CD1 . ILE C 1 19  ? 3.506   41.149  57.434  1.00 31.80  ? 48  ILE C CD1 1 
ATOM   6994  N N   . LYS C 1 20  ? 0.118   38.715  61.314  1.00 31.27  ? 49  LYS C N   1 
ATOM   6995  C CA  . LYS C 1 20  ? -0.300  38.539  62.700  1.00 34.50  ? 49  LYS C CA  1 
ATOM   6996  C C   . LYS C 1 20  ? -0.327  37.049  63.042  1.00 37.12  ? 49  LYS C C   1 
ATOM   6997  O O   . LYS C 1 20  ? 0.220   36.634  64.067  1.00 43.43  ? 49  LYS C O   1 
ATOM   6998  C CB  . LYS C 1 20  ? -1.671  39.196  62.911  1.00 37.87  ? 49  LYS C CB  1 
ATOM   6999  C CG  . LYS C 1 20  ? -2.263  39.123  64.314  1.00 39.74  ? 49  LYS C CG  1 
ATOM   7000  C CD  . LYS C 1 20  ? -3.612  39.829  64.395  1.00 41.55  ? 49  LYS C CD  1 
ATOM   7001  C CE  . LYS C 1 20  ? -4.298  39.714  65.743  1.00 45.01  ? 49  LYS C CE  1 
ATOM   7002  N NZ  . LYS C 1 20  ? -4.880  38.368  65.952  1.00 44.62  ? 49  LYS C NZ  1 
ATOM   7003  N N   . THR C 1 21  ? -0.945  36.264  62.153  1.00 37.38  ? 50  THR C N   1 
ATOM   7004  C CA  . THR C 1 21  ? -1.200  34.850  62.381  1.00 36.24  ? 50  THR C CA  1 
ATOM   7005  C C   . THR C 1 21  ? 0.119   34.078  62.370  1.00 35.40  ? 50  THR C C   1 
ATOM   7006  O O   . THR C 1 21  ? 0.362   33.244  63.232  1.00 31.57  ? 50  THR C O   1 
ATOM   7007  C CB  . THR C 1 21  ? -2.197  34.339  61.338  1.00 35.12  ? 50  THR C CB  1 
ATOM   7008  O OG1 . THR C 1 21  ? -3.401  35.078  61.541  1.00 37.27  ? 50  THR C OG1 1 
ATOM   7009  C CG2 . THR C 1 21  ? -2.471  32.850  61.415  1.00 34.41  ? 50  THR C CG2 1 
ATOM   7010  N N   . PHE C 1 22  ? 0.953   34.384  61.369  1.00 31.72  ? 51  PHE C N   1 
ATOM   7011  C CA  . PHE C 1 22  ? 2.282   33.821  61.221  1.00 29.41  ? 51  PHE C CA  1 
ATOM   7012  C C   . PHE C 1 22  ? 3.129   34.095  62.471  1.00 31.37  ? 51  PHE C C   1 
ATOM   7013  O O   . PHE C 1 22  ? 3.776   33.213  63.029  1.00 27.89  ? 51  PHE C O   1 
ATOM   7014  C CB  . PHE C 1 22  ? 2.852   34.410  59.931  1.00 29.14  ? 51  PHE C CB  1 
ATOM   7015  C CG  . PHE C 1 22  ? 4.201   33.893  59.523  1.00 29.19  ? 51  PHE C CG  1 
ATOM   7016  C CD1 . PHE C 1 22  ? 4.452   32.533  59.489  1.00 28.29  ? 51  PHE C CD1 1 
ATOM   7017  C CD2 . PHE C 1 22  ? 5.213   34.767  59.153  1.00 27.86  ? 51  PHE C CD2 1 
ATOM   7018  C CE1 . PHE C 1 22  ? 5.706   32.060  59.146  1.00 28.25  ? 51  PHE C CE1 1 
ATOM   7019  C CE2 . PHE C 1 22  ? 6.465   34.291  58.804  1.00 28.35  ? 51  PHE C CE2 1 
ATOM   7020  C CZ  . PHE C 1 22  ? 6.701   32.935  58.785  1.00 27.39  ? 51  PHE C CZ  1 
ATOM   7021  N N   . ARG C 1 23  ? 3.134   35.346  62.923  1.00 32.39  ? 52  ARG C N   1 
ATOM   7022  C CA  . ARG C 1 23  ? 3.913   35.711  64.083  1.00 34.68  ? 52  ARG C CA  1 
ATOM   7023  C C   . ARG C 1 23  ? 3.335   35.011  65.311  1.00 38.73  ? 52  ARG C C   1 
ATOM   7024  O O   . ARG C 1 23  ? 4.089   34.575  66.174  1.00 37.16  ? 52  ARG C O   1 
ATOM   7025  C CB  . ARG C 1 23  ? 3.960   37.234  64.212  1.00 35.55  ? 52  ARG C CB  1 
ATOM   7026  C CG  . ARG C 1 23  ? 4.851   37.881  63.165  1.00 34.74  ? 52  ARG C CG  1 
ATOM   7027  C CD  . ARG C 1 23  ? 5.038   39.357  63.444  1.00 32.89  ? 52  ARG C CD  1 
ATOM   7028  N NE  . ARG C 1 23  ? 5.929   39.614  64.556  1.00 30.66  ? 52  ARG C NE  1 
ATOM   7029  C CZ  . ARG C 1 23  ? 6.219   40.831  65.008  1.00 36.35  ? 52  ARG C CZ  1 
ATOM   7030  N NH1 . ARG C 1 23  ? 5.654   41.889  64.450  1.00 32.60  ? 52  ARG C NH1 1 
ATOM   7031  N NH2 . ARG C 1 23  ? 7.066   40.989  66.012  1.00 35.69  ? 52  ARG C NH2 1 
ATOM   7032  N N   . GLN C 1 24  ? 2.006   34.864  65.333  1.00 38.96  ? 53  GLN C N   1 
ATOM   7033  C CA  . GLN C 1 24  ? 1.324   34.167  66.404  1.00 38.82  ? 53  GLN C CA  1 
ATOM   7034  C C   . GLN C 1 24  ? 1.773   32.704  66.432  1.00 39.70  ? 53  GLN C C   1 
ATOM   7035  O O   . GLN C 1 24  ? 1.991   32.149  67.502  1.00 38.46  ? 53  GLN C O   1 
ATOM   7036  C CB  . GLN C 1 24  ? -0.187  34.282  66.201  1.00 39.83  ? 53  GLN C CB  1 
ATOM   7037  C CG  . GLN C 1 24  ? -0.987  34.219  67.493  1.00 42.04  ? 53  GLN C CG  1 
ATOM   7038  C CD  . GLN C 1 24  ? -0.857  35.485  68.311  1.00 53.71  ? 53  GLN C CD  1 
ATOM   7039  O OE1 . GLN C 1 24  ? -0.363  35.474  69.442  1.00 56.57  ? 53  GLN C OE1 1 
ATOM   7040  N NE2 . GLN C 1 24  ? -1.309  36.598  67.748  1.00 52.73  ? 53  GLN C NE2 1 
ATOM   7041  N N   . GLN C 1 25  ? 1.902   32.078  65.257  1.00 39.56  ? 54  GLN C N   1 
ATOM   7042  C CA  . GLN C 1 25  ? 2.285   30.675  65.174  1.00 43.18  ? 54  GLN C CA  1 
ATOM   7043  C C   . GLN C 1 25  ? 3.791   30.480  65.339  1.00 42.33  ? 54  GLN C C   1 
ATOM   7044  O O   . GLN C 1 25  ? 4.207   29.533  66.005  1.00 30.90  ? 54  GLN C O   1 
ATOM   7045  C CB  . GLN C 1 25  ? 1.860   30.058  63.838  1.00 46.23  ? 54  GLN C CB  1 
ATOM   7046  C CG  . GLN C 1 25  ? 0.358   30.146  63.600  1.00 53.45  ? 54  GLN C CG  1 
ATOM   7047  C CD  . GLN C 1 25  ? -0.237  28.946  62.909  1.00 56.98  ? 54  GLN C CD  1 
ATOM   7048  O OE1 . GLN C 1 25  ? 0.460   28.095  62.363  1.00 65.07  ? 54  GLN C OE1 1 
ATOM   7049  N NE2 . GLN C 1 25  ? -1.557  28.887  62.917  1.00 64.46  ? 54  GLN C NE2 1 
ATOM   7050  N N   . HIS C 1 26  ? 4.586   31.358  64.706  1.00 35.68  ? 55  HIS C N   1 
ATOM   7051  C CA  . HIS C 1 26  ? 5.963   31.043  64.371  1.00 36.28  ? 55  HIS C CA  1 
ATOM   7052  C C   . HIS C 1 26  ? 6.920   32.175  64.733  1.00 32.28  ? 55  HIS C C   1 
ATOM   7053  O O   . HIS C 1 26  ? 8.104   32.099  64.408  1.00 30.16  ? 55  HIS C O   1 
ATOM   7054  C CB  . HIS C 1 26  ? 6.064   30.704  62.881  1.00 39.25  ? 55  HIS C CB  1 
ATOM   7055  C CG  . HIS C 1 26  ? 5.427   29.399  62.528  1.00 41.91  ? 55  HIS C CG  1 
ATOM   7056  N ND1 . HIS C 1 26  ? 5.854   28.210  63.079  1.00 42.64  ? 55  HIS C ND1 1 
ATOM   7057  C CD2 . HIS C 1 26  ? 4.410   29.091  61.711  1.00 41.22  ? 55  HIS C CD2 1 
ATOM   7058  C CE1 . HIS C 1 26  ? 5.114   27.219  62.595  1.00 41.42  ? 55  HIS C CE1 1 
ATOM   7059  N NE2 . HIS C 1 26  ? 4.235   27.731  61.758  1.00 39.41  ? 55  HIS C NE2 1 
ATOM   7060  N N   . GLY C 1 27  ? 6.420   33.177  65.464  1.00 32.56  ? 56  GLY C N   1 
ATOM   7061  C CA  . GLY C 1 27  ? 7.225   34.317  65.877  1.00 36.78  ? 56  GLY C CA  1 
ATOM   7062  C C   . GLY C 1 27  ? 8.526   33.898  66.555  1.00 36.26  ? 56  GLY C C   1 
ATOM   7063  O O   . GLY C 1 27  ? 9.578   34.514  66.345  1.00 31.45  ? 56  GLY C O   1 
ATOM   7064  N N   . LYS C 1 28  ? 8.447   32.813  67.337  1.00 38.33  ? 57  LYS C N   1 
ATOM   7065  C CA  . LYS C 1 28  ? 9.574   32.413  68.161  1.00 43.93  ? 57  LYS C CA  1 
ATOM   7066  C C   . LYS C 1 28  ? 10.385  31.332  67.449  1.00 42.13  ? 57  LYS C C   1 
ATOM   7067  O O   . LYS C 1 28  ? 11.419  30.933  67.964  1.00 44.75  ? 57  LYS C O   1 
ATOM   7068  C CB  . LYS C 1 28  ? 9.092   32.053  69.573  1.00 46.97  ? 57  LYS C CB  1 
ATOM   7069  C CG  . LYS C 1 28  ? 8.465   33.219  70.332  1.00 50.62  ? 57  LYS C CG  1 
ATOM   7070  C CD  . LYS C 1 28  ? 8.419   33.046  71.843  1.00 53.50  ? 57  LYS C CD  1 
ATOM   7071  C CE  . LYS C 1 28  ? 8.194   34.351  72.580  1.00 53.72  ? 57  LYS C CE  1 
ATOM   7072  N NZ  . LYS C 1 28  ? 9.403   35.208  72.578  1.00 52.79  ? 57  LYS C NZ  1 
ATOM   7073  N N   . THR C 1 29  ? 9.968   30.938  66.235  1.00 42.26  ? 58  THR C N   1 
ATOM   7074  C CA  . THR C 1 29  ? 10.737  30.031  65.391  1.00 43.18  ? 58  THR C CA  1 
ATOM   7075  C C   . THR C 1 29  ? 12.094  30.650  65.047  1.00 41.03  ? 58  THR C C   1 
ATOM   7076  O O   . THR C 1 29  ? 12.168  31.785  64.570  1.00 37.28  ? 58  THR C O   1 
ATOM   7077  C CB  . THR C 1 29  ? 9.929   29.625  64.147  1.00 42.45  ? 58  THR C CB  1 
ATOM   7078  O OG1 . THR C 1 29  ? 8.866   28.777  64.574  1.00 42.64  ? 58  THR C OG1 1 
ATOM   7079  C CG2 . THR C 1 29  ? 10.731  28.887  63.101  1.00 40.16  ? 58  THR C CG2 1 
ATOM   7080  N N   . VAL C 1 30  ? 13.173  29.887  65.302  1.00 40.13  ? 59  VAL C N   1 
ATOM   7081  C CA  . VAL C 1 30  ? 14.530  30.364  65.080  1.00 39.41  ? 59  VAL C CA  1 
ATOM   7082  C C   . VAL C 1 30  ? 14.897  30.043  63.634  1.00 37.49  ? 59  VAL C C   1 
ATOM   7083  O O   . VAL C 1 30  ? 14.711  28.919  63.184  1.00 37.27  ? 59  VAL C O   1 
ATOM   7084  C CB  . VAL C 1 30  ? 15.540  29.770  66.086  1.00 42.10  ? 59  VAL C CB  1 
ATOM   7085  C CG1 . VAL C 1 30  ? 16.979  30.101  65.725  1.00 42.83  ? 59  VAL C CG1 1 
ATOM   7086  C CG2 . VAL C 1 30  ? 15.259  30.220  67.510  1.00 42.71  ? 59  VAL C CG2 1 
ATOM   7087  N N   . VAL C 1 31  ? 15.405  31.044  62.913  1.00 38.32  ? 60  VAL C N   1 
ATOM   7088  C CA  . VAL C 1 31  ? 15.635  30.911  61.483  1.00 39.24  ? 60  VAL C CA  1 
ATOM   7089  C C   . VAL C 1 31  ? 17.127  31.066  61.191  1.00 36.52  ? 60  VAL C C   1 
ATOM   7090  O O   . VAL C 1 31  ? 17.564  30.909  60.054  1.00 38.95  ? 60  VAL C O   1 
ATOM   7091  C CB  . VAL C 1 31  ? 14.776  31.916  60.691  1.00 40.34  ? 60  VAL C CB  1 
ATOM   7092  C CG1 . VAL C 1 31  ? 13.291  31.736  60.989  1.00 42.67  ? 60  VAL C CG1 1 
ATOM   7093  C CG2 . VAL C 1 31  ? 15.179  33.359  60.940  1.00 38.59  ? 60  VAL C CG2 1 
ATOM   7094  N N   . GLY C 1 32  ? 17.927  31.369  62.207  1.00 35.94  ? 61  GLY C N   1 
ATOM   7095  C CA  . GLY C 1 32  ? 19.345  31.532  61.947  1.00 37.34  ? 61  GLY C CA  1 
ATOM   7096  C C   . GLY C 1 32  ? 20.173  31.753  63.205  1.00 41.31  ? 61  GLY C C   1 
ATOM   7097  O O   . GLY C 1 32  ? 19.674  32.155  64.255  1.00 41.24  ? 61  GLY C O   1 
ATOM   7098  N N   . GLN C 1 33  ? 21.471  31.501  63.051  1.00 40.47  ? 62  GLN C N   1 
ATOM   7099  C CA  . GLN C 1 33  ? 22.410  31.612  64.146  1.00 40.70  ? 62  GLN C CA  1 
ATOM   7100  C C   . GLN C 1 33  ? 23.284  32.829  63.876  1.00 33.46  ? 62  GLN C C   1 
ATOM   7101  O O   . GLN C 1 33  ? 23.428  33.241  62.725  1.00 32.38  ? 62  GLN C O   1 
ATOM   7102  C CB  . GLN C 1 33  ? 23.189  30.300  64.236  1.00 48.01  ? 62  GLN C CB  1 
ATOM   7103  C CG  . GLN C 1 33  ? 22.285  29.082  64.397  1.00 54.84  ? 62  GLN C CG  1 
ATOM   7104  C CD  . GLN C 1 33  ? 21.886  28.840  65.832  1.00 62.20  ? 62  GLN C CD  1 
ATOM   7105  O OE1 . GLN C 1 33  ? 20.759  29.113  66.244  1.00 70.17  ? 62  GLN C OE1 1 
ATOM   7106  N NE2 . GLN C 1 33  ? 22.822  28.330  66.616  1.00 63.37  ? 62  GLN C NE2 1 
ATOM   7107  N N   . ILE C 1 34  ? 23.818  33.442  64.932  1.00 28.31  ? 63  ILE C N   1 
ATOM   7108  C CA  . ILE C 1 34  ? 24.738  34.545  64.723  1.00 26.92  ? 63  ILE C CA  1 
ATOM   7109  C C   . ILE C 1 34  ? 26.105  34.155  65.281  1.00 26.64  ? 63  ILE C C   1 
ATOM   7110  O O   . ILE C 1 34  ? 26.260  33.992  66.494  1.00 24.47  ? 63  ILE C O   1 
ATOM   7111  C CB  . ILE C 1 34  ? 24.225  35.831  65.393  1.00 26.74  ? 63  ILE C CB  1 
ATOM   7112  C CG1 . ILE C 1 34  ? 22.825  36.218  64.925  1.00 28.11  ? 63  ILE C CG1 1 
ATOM   7113  C CG2 . ILE C 1 34  ? 25.232  36.957  65.202  1.00 26.32  ? 63  ILE C CG2 1 
ATOM   7114  C CD1 . ILE C 1 34  ? 22.314  37.498  65.558  1.00 30.26  ? 63  ILE C CD1 1 
ATOM   7115  N N   . THR C 1 35  ? 27.099  34.059  64.398  1.00 25.89  ? 64  THR C N   1 
ATOM   7116  C CA  . THR C 1 35  ? 28.451  33.815  64.849  1.00 25.65  ? 64  THR C CA  1 
ATOM   7117  C C   . THR C 1 35  ? 29.180  35.132  65.022  1.00 26.22  ? 64  THR C C   1 
ATOM   7118  O O   . THR C 1 35  ? 28.770  36.159  64.498  1.00 23.31  ? 64  THR C O   1 
ATOM   7119  C CB  . THR C 1 35  ? 29.225  32.900  63.905  1.00 25.45  ? 64  THR C CB  1 
ATOM   7120  O OG1 . THR C 1 35  ? 29.421  33.617  62.687  1.00 28.38  ? 64  THR C OG1 1 
ATOM   7121  C CG2 . THR C 1 35  ? 28.520  31.577  63.703  1.00 25.76  ? 64  THR C CG2 1 
ATOM   7122  N N   . VAL C 1 36  ? 30.288  35.045  65.759  1.00 27.69  ? 65  VAL C N   1 
ATOM   7123  C CA  . VAL C 1 36  ? 31.261  36.111  65.861  1.00 26.08  ? 65  VAL C CA  1 
ATOM   7124  C C   . VAL C 1 36  ? 31.676  36.560  64.458  1.00 25.43  ? 65  VAL C C   1 
ATOM   7125  O O   . VAL C 1 36  ? 31.823  37.754  64.215  1.00 25.02  ? 65  VAL C O   1 
ATOM   7126  C CB  . VAL C 1 36  ? 32.465  35.626  66.692  1.00 26.18  ? 65  VAL C CB  1 
ATOM   7127  C CG1 . VAL C 1 36  ? 33.713  36.455  66.463  1.00 27.73  ? 65  VAL C CG1 1 
ATOM   7128  C CG2 . VAL C 1 36  ? 32.127  35.539  68.176  1.00 27.42  ? 65  VAL C CG2 1 
ATOM   7129  N N   . ASP C 1 37  ? 31.924  35.607  63.553  1.00 23.47  ? 66  ASP C N   1 
ATOM   7130  C CA  . ASP C 1 37  ? 32.442  35.935  62.235  1.00 27.93  ? 66  ASP C CA  1 
ATOM   7131  C C   . ASP C 1 37  ? 31.458  36.821  61.472  1.00 26.39  ? 66  ASP C C   1 
ATOM   7132  O O   . ASP C 1 37  ? 31.876  37.710  60.721  1.00 26.55  ? 66  ASP C O   1 
ATOM   7133  C CB  . ASP C 1 37  ? 32.796  34.666  61.450  1.00 30.71  ? 66  ASP C CB  1 
ATOM   7134  C CG  . ASP C 1 37  ? 34.276  34.304  61.530  1.00 33.48  ? 66  ASP C CG  1 
ATOM   7135  O OD1 . ASP C 1 37  ? 35.094  35.221  61.718  1.00 32.64  ? 66  ASP C OD1 1 
ATOM   7136  O OD2 . ASP C 1 37  ? 34.604  33.095  61.430  1.00 34.17  ? 66  ASP C OD2 1 
ATOM   7137  N N   . MET C 1 38  ? 30.164  36.524  61.640  1.00 29.61  ? 67  MET C N   1 
ATOM   7138  C CA  . MET C 1 38  ? 29.097  37.212  60.934  1.00 28.18  ? 67  MET C CA  1 
ATOM   7139  C C   . MET C 1 38  ? 29.021  38.655  61.430  1.00 28.75  ? 67  MET C C   1 
ATOM   7140  O O   . MET C 1 38  ? 28.670  39.534  60.646  1.00 24.52  ? 67  MET C O   1 
ATOM   7141  C CB  . MET C 1 38  ? 27.750  36.518  61.159  1.00 30.13  ? 67  MET C CB  1 
ATOM   7142  C CG  . MET C 1 38  ? 27.507  35.288  60.258  1.00 31.28  ? 67  MET C CG  1 
ATOM   7143  S SD  . MET C 1 38  ? 26.148  34.263  60.867  1.00 35.22  ? 67  MET C SD  1 
ATOM   7144  C CE  . MET C 1 38  ? 26.250  32.853  59.768  1.00 34.45  ? 67  MET C CE  1 
ATOM   7145  N N   . MET C 1 39  ? 29.323  38.866  62.730  1.00 25.68  ? 68  MET C N   1 
ATOM   7146  C CA  . MET C 1 39  ? 29.274  40.186  63.352  1.00 25.50  ? 68  MET C CA  1 
ATOM   7147  C C   . MET C 1 39  ? 30.415  41.067  62.840  1.00 26.91  ? 68  MET C C   1 
ATOM   7148  O O   . MET C 1 39  ? 30.226  42.274  62.626  1.00 28.00  ? 68  MET C O   1 
ATOM   7149  C CB  . MET C 1 39  ? 29.370  40.088  64.880  1.00 26.58  ? 68  MET C CB  1 
ATOM   7150  C CG  . MET C 1 39  ? 28.077  39.626  65.544  1.00 26.57  ? 68  MET C CG  1 
ATOM   7151  S SD  . MET C 1 39  ? 28.148  39.513  67.329  1.00 27.96  ? 68  MET C SD  1 
ATOM   7152  C CE  . MET C 1 39  ? 28.337  41.257  67.715  1.00 27.88  ? 68  MET C CE  1 
ATOM   7153  N N   . TYR C 1 40  ? 31.614  40.490  62.695  1.00 25.08  ? 69  TYR C N   1 
ATOM   7154  C CA  . TYR C 1 40  ? 32.743  41.213  62.141  1.00 24.20  ? 69  TYR C CA  1 
ATOM   7155  C C   . TYR C 1 40  ? 32.621  41.354  60.623  1.00 23.60  ? 69  TYR C C   1 
ATOM   7156  O O   . TYR C 1 40  ? 33.263  42.229  60.045  1.00 27.31  ? 69  TYR C O   1 
ATOM   7157  C CB  . TYR C 1 40  ? 34.083  40.528  62.454  1.00 25.84  ? 69  TYR C CB  1 
ATOM   7158  C CG  . TYR C 1 40  ? 34.618  40.767  63.841  1.00 24.53  ? 69  TYR C CG  1 
ATOM   7159  C CD1 . TYR C 1 40  ? 35.233  41.963  64.178  1.00 25.62  ? 69  TYR C CD1 1 
ATOM   7160  C CD2 . TYR C 1 40  ? 34.445  39.828  64.842  1.00 26.43  ? 69  TYR C CD2 1 
ATOM   7161  C CE1 . TYR C 1 40  ? 35.687  42.205  65.466  1.00 25.86  ? 69  TYR C CE1 1 
ATOM   7162  C CE2 . TYR C 1 40  ? 34.912  40.048  66.129  1.00 25.45  ? 69  TYR C CE2 1 
ATOM   7163  C CZ  . TYR C 1 40  ? 35.529  41.243  66.447  1.00 23.89  ? 69  TYR C CZ  1 
ATOM   7164  O OH  . TYR C 1 40  ? 36.005  41.459  67.725  1.00 26.41  ? 69  TYR C OH  1 
ATOM   7165  N N   . GLY C 1 41  ? 31.833  40.480  59.976  1.00 23.37  ? 70  GLY C N   1 
ATOM   7166  C CA  . GLY C 1 41  ? 31.813  40.389  58.516  1.00 23.30  ? 70  GLY C CA  1 
ATOM   7167  C C   . GLY C 1 41  ? 30.521  40.952  57.918  1.00 22.57  ? 70  GLY C C   1 
ATOM   7168  O O   . GLY C 1 41  ? 30.045  40.492  56.885  1.00 22.92  ? 70  GLY C O   1 
ATOM   7169  N N   . GLY C 1 42  ? 29.977  41.994  58.558  1.00 21.94  ? 71  GLY C N   1 
ATOM   7170  C CA  . GLY C 1 42  ? 28.915  42.799  57.970  1.00 22.70  ? 71  GLY C CA  1 
ATOM   7171  C C   . GLY C 1 42  ? 27.625  42.035  57.700  1.00 20.30  ? 71  GLY C C   1 
ATOM   7172  O O   . GLY C 1 42  ? 27.060  42.150  56.613  1.00 20.93  ? 71  GLY C O   1 
ATOM   7173  N N   . MET C 1 43  ? 27.229  41.216  58.679  1.00 21.66  ? 72  MET C N   1 
ATOM   7174  C CA  . MET C 1 43  ? 25.982  40.469  58.692  1.00 23.20  ? 72  MET C CA  1 
ATOM   7175  C C   . MET C 1 43  ? 25.892  39.478  57.529  1.00 26.57  ? 72  MET C C   1 
ATOM   7176  O O   . MET C 1 43  ? 24.812  39.034  57.161  1.00 28.21  ? 72  MET C O   1 
ATOM   7177  C CB  . MET C 1 43  ? 24.790  41.426  58.655  1.00 24.70  ? 72  MET C CB  1 
ATOM   7178  C CG  . MET C 1 43  ? 24.700  42.318  59.872  1.00 27.06  ? 72  MET C CG  1 
ATOM   7179  S SD  . MET C 1 43  ? 23.391  43.515  59.604  1.00 31.03  ? 72  MET C SD  1 
ATOM   7180  C CE  . MET C 1 43  ? 23.332  44.353  61.184  1.00 27.71  ? 72  MET C CE  1 
ATOM   7181  N N   . ARG C 1 44  ? 27.035  39.093  56.965  1.00 28.64  ? 73  ARG C N   1 
ATOM   7182  C CA  . ARG C 1 44  ? 27.060  38.208  55.816  1.00 33.77  ? 73  ARG C CA  1 
ATOM   7183  C C   . ARG C 1 44  ? 26.392  36.879  56.185  1.00 32.17  ? 73  ARG C C   1 
ATOM   7184  O O   . ARG C 1 44  ? 26.841  36.176  57.095  1.00 30.75  ? 73  ARG C O   1 
ATOM   7185  C CB  . ARG C 1 44  ? 28.511  38.016  55.363  1.00 41.20  ? 73  ARG C CB  1 
ATOM   7186  C CG  . ARG C 1 44  ? 28.675  37.317  54.022  1.00 47.63  ? 73  ARG C CG  1 
ATOM   7187  C CD  . ARG C 1 44  ? 30.098  36.822  53.797  1.00 57.35  ? 73  ARG C CD  1 
ATOM   7188  N NE  . ARG C 1 44  ? 30.297  36.390  52.415  1.00 64.06  ? 73  ARG C NE  1 
ATOM   7189  C CZ  . ARG C 1 44  ? 30.529  37.208  51.390  1.00 71.28  ? 73  ARG C CZ  1 
ATOM   7190  N NH1 . ARG C 1 44  ? 30.836  38.477  51.600  1.00 73.35  ? 73  ARG C NH1 1 
ATOM   7191  N NH2 . ARG C 1 44  ? 30.496  36.743  50.153  1.00 72.90  ? 73  ARG C NH2 1 
ATOM   7192  N N   . GLY C 1 45  ? 25.313  36.553  55.465  1.00 27.80  ? 74  GLY C N   1 
ATOM   7193  C CA  . GLY C 1 45  ? 24.598  35.296  55.647  1.00 30.22  ? 74  GLY C CA  1 
ATOM   7194  C C   . GLY C 1 45  ? 23.460  35.389  56.661  1.00 30.34  ? 74  GLY C C   1 
ATOM   7195  O O   . GLY C 1 45  ? 22.746  34.415  56.885  1.00 28.33  ? 74  GLY C O   1 
ATOM   7196  N N   . MET C 1 46  ? 23.271  36.569  57.259  1.00 28.34  ? 75  MET C N   1 
ATOM   7197  C CA  . MET C 1 46  ? 22.359  36.728  58.384  1.00 29.68  ? 75  MET C CA  1 
ATOM   7198  C C   . MET C 1 46  ? 20.992  37.196  57.879  1.00 30.21  ? 75  MET C C   1 
ATOM   7199  O O   . MET C 1 46  ? 20.914  38.142  57.097  1.00 26.61  ? 75  MET C O   1 
ATOM   7200  C CB  . MET C 1 46  ? 22.968  37.782  59.313  1.00 35.04  ? 75  MET C CB  1 
ATOM   7201  C CG  . MET C 1 46  ? 22.274  37.987  60.627  1.00 39.23  ? 75  MET C CG  1 
ATOM   7202  S SD  . MET C 1 46  ? 23.219  39.099  61.732  1.00 44.95  ? 75  MET C SD  1 
ATOM   7203  C CE  . MET C 1 46  ? 24.835  38.345  61.633  1.00 35.24  ? 75  MET C CE  1 
ATOM   7204  N N   . LYS C 1 47  ? 19.908  36.572  58.361  1.00 29.21  ? 76  LYS C N   1 
ATOM   7205  C CA  . LYS C 1 47  ? 18.572  36.843  57.855  1.00 28.28  ? 76  LYS C CA  1 
ATOM   7206  C C   . LYS C 1 47  ? 17.909  37.924  58.700  1.00 25.54  ? 76  LYS C C   1 
ATOM   7207  O O   . LYS C 1 47  ? 17.166  37.624  59.622  1.00 27.28  ? 76  LYS C O   1 
ATOM   7208  C CB  . LYS C 1 47  ? 17.751  35.562  57.871  1.00 31.40  ? 76  LYS C CB  1 
ATOM   7209  C CG  . LYS C 1 47  ? 18.351  34.436  57.049  1.00 37.09  ? 76  LYS C CG  1 
ATOM   7210  C CD  . LYS C 1 47  ? 17.707  33.120  57.379  1.00 42.61  ? 76  LYS C CD  1 
ATOM   7211  C CE  . LYS C 1 47  ? 16.197  33.207  57.396  1.00 49.05  ? 76  LYS C CE  1 
ATOM   7212  N NZ  . LYS C 1 47  ? 15.694  33.717  56.103  1.00 50.79  ? 76  LYS C NZ  1 
ATOM   7213  N N   . GLY C 1 48  ? 18.171  39.181  58.341  1.00 21.94  ? 77  GLY C N   1 
ATOM   7214  C CA  . GLY C 1 48  ? 18.041  40.291  59.267  1.00 23.63  ? 77  GLY C CA  1 
ATOM   7215  C C   . GLY C 1 48  ? 16.724  41.052  59.207  1.00 22.76  ? 77  GLY C C   1 
ATOM   7216  O O   . GLY C 1 48  ? 16.379  41.738  60.186  1.00 23.46  ? 77  GLY C O   1 
ATOM   7217  N N   . LEU C 1 49  ? 16.029  40.974  58.064  1.00 21.81  ? 78  LEU C N   1 
ATOM   7218  C CA  . LEU C 1 49  ? 14.917  41.880  57.822  1.00 22.92  ? 78  LEU C CA  1 
ATOM   7219  C C   . LEU C 1 49  ? 13.883  41.269  56.869  1.00 22.12  ? 78  LEU C C   1 
ATOM   7220  O O   . LEU C 1 49  ? 14.177  40.364  56.081  1.00 20.95  ? 78  LEU C O   1 
ATOM   7221  C CB  . LEU C 1 49  ? 15.440  43.257  57.361  1.00 24.39  ? 78  LEU C CB  1 
ATOM   7222  C CG  . LEU C 1 49  ? 15.926  43.449  55.915  1.00 24.99  ? 78  LEU C CG  1 
ATOM   7223  C CD1 . LEU C 1 49  ? 15.844  44.916  55.519  1.00 25.71  ? 78  LEU C CD1 1 
ATOM   7224  C CD2 . LEU C 1 49  ? 17.350  42.965  55.724  1.00 27.67  ? 78  LEU C CD2 1 
ATOM   7225  N N   . VAL C 1 50  ? 12.635  41.706  57.057  1.00 21.72  ? 79  VAL C N   1 
ATOM   7226  C CA  . VAL C 1 50  ? 11.530  41.346  56.179  1.00 22.53  ? 79  VAL C CA  1 
ATOM   7227  C C   . VAL C 1 50  ? 11.399  42.451  55.142  1.00 21.83  ? 79  VAL C C   1 
ATOM   7228  O O   . VAL C 1 50  ? 11.311  43.612  55.497  1.00 23.10  ? 79  VAL C O   1 
ATOM   7229  C CB  . VAL C 1 50  ? 10.214  41.141  56.947  1.00 25.26  ? 79  VAL C CB  1 
ATOM   7230  C CG1 . VAL C 1 50  ? 9.023   40.976  56.019  1.00 26.77  ? 79  VAL C CG1 1 
ATOM   7231  C CG2 . VAL C 1 50  ? 10.318  39.989  57.946  1.00 27.84  ? 79  VAL C CG2 1 
ATOM   7232  N N   . TYR C 1 51  ? 11.461  42.076  53.870  1.00 21.62  ? 80  TYR C N   1 
ATOM   7233  C CA  . TYR C 1 51  ? 11.426  43.005  52.756  1.00 21.49  ? 80  TYR C CA  1 
ATOM   7234  C C   . TYR C 1 51  ? 10.572  42.319  51.694  1.00 24.77  ? 80  TYR C C   1 
ATOM   7235  O O   . TYR C 1 51  ? 10.893  41.203  51.257  1.00 21.59  ? 80  TYR C O   1 
ATOM   7236  C CB  . TYR C 1 51  ? 12.842  43.341  52.301  1.00 21.77  ? 80  TYR C CB  1 
ATOM   7237  C CG  . TYR C 1 51  ? 13.038  44.510  51.379  1.00 20.73  ? 80  TYR C CG  1 
ATOM   7238  C CD1 . TYR C 1 51  ? 13.227  45.782  51.874  1.00 21.49  ? 80  TYR C CD1 1 
ATOM   7239  C CD2 . TYR C 1 51  ? 13.086  44.334  50.007  1.00 20.70  ? 80  TYR C CD2 1 
ATOM   7240  C CE1 . TYR C 1 51  ? 13.431  46.854  51.019  1.00 19.23  ? 80  TYR C CE1 1 
ATOM   7241  C CE2 . TYR C 1 51  ? 13.339  45.379  49.148  1.00 19.35  ? 80  TYR C CE2 1 
ATOM   7242  C CZ  . TYR C 1 51  ? 13.500  46.647  49.654  1.00 18.31  ? 80  TYR C CZ  1 
ATOM   7243  O OH  . TYR C 1 51  ? 13.746  47.668  48.776  1.00 21.99  ? 80  TYR C OH  1 
ATOM   7244  N N   . GLU C 1 52  ? 9.409   42.928  51.414  1.00 23.34  ? 81  GLU C N   1 
ATOM   7245  C CA  . GLU C 1 52  ? 8.336   42.203  50.766  1.00 23.28  ? 81  GLU C CA  1 
ATOM   7246  C C   . GLU C 1 52  ? 8.512   42.250  49.244  1.00 23.00  ? 81  GLU C C   1 
ATOM   7247  O O   . GLU C 1 52  ? 8.017   41.376  48.530  1.00 23.96  ? 81  GLU C O   1 
ATOM   7248  C CB  . GLU C 1 52  ? 6.982   42.803  51.163  1.00 25.38  ? 81  GLU C CB  1 
ATOM   7249  C CG  . GLU C 1 52  ? 6.691   42.753  52.659  1.00 23.25  ? 81  GLU C CG  1 
ATOM   7250  C CD  . GLU C 1 52  ? 6.425   41.360  53.214  1.00 26.01  ? 81  GLU C CD  1 
ATOM   7251  O OE1 . GLU C 1 52  ? 6.770   40.358  52.523  1.00 27.54  ? 81  GLU C OE1 1 
ATOM   7252  O OE2 . GLU C 1 52  ? 5.887   41.265  54.362  1.00 26.29  ? 81  GLU C OE2 1 
ATOM   7253  N N   . THR C 1 53  ? 9.124   43.321  48.730  1.00 21.46  ? 82  THR C N   1 
ATOM   7254  C CA  . THR C 1 53  ? 8.953   43.656  47.326  1.00 21.44  ? 82  THR C CA  1 
ATOM   7255  C C   . THR C 1 53  ? 9.713   42.700  46.418  1.00 22.89  ? 82  THR C C   1 
ATOM   7256  O O   . THR C 1 53  ? 9.288   42.434  45.298  1.00 24.73  ? 82  THR C O   1 
ATOM   7257  C CB  . THR C 1 53  ? 9.298   45.118  47.053  1.00 22.25  ? 82  THR C CB  1 
ATOM   7258  O OG1 . THR C 1 53  ? 10.595  45.370  47.583  1.00 22.24  ? 82  THR C OG1 1 
ATOM   7259  C CG2 . THR C 1 53  ? 8.252   46.050  47.627  1.00 23.22  ? 82  THR C CG2 1 
ATOM   7260  N N   . SER C 1 54  ? 10.885  42.264  46.858  1.00 25.49  ? 83  SER C N   1 
ATOM   7261  C CA  . SER C 1 54  ? 11.699  41.400  46.025  1.00 24.46  ? 83  SER C CA  1 
ATOM   7262  C C   . SER C 1 54  ? 12.566  40.496  46.888  1.00 24.85  ? 83  SER C C   1 
ATOM   7263  O O   . SER C 1 54  ? 12.944  40.845  48.007  1.00 19.82  ? 83  SER C O   1 
ATOM   7264  C CB  . SER C 1 54  ? 12.515  42.180  45.033  1.00 23.78  ? 83  SER C CB  1 
ATOM   7265  O OG  . SER C 1 54  ? 13.476  42.997  45.651  1.00 20.83  ? 83  SER C OG  1 
ATOM   7266  N N   . VAL C 1 55  ? 12.851  39.321  46.331  1.00 25.12  ? 84  VAL C N   1 
ATOM   7267  C CA  . VAL C 1 55  ? 13.674  38.337  47.004  1.00 28.33  ? 84  VAL C CA  1 
ATOM   7268  C C   . VAL C 1 55  ? 14.718  37.880  45.994  1.00 24.84  ? 84  VAL C C   1 
ATOM   7269  O O   . VAL C 1 55  ? 14.384  37.601  44.835  1.00 26.92  ? 84  VAL C O   1 
ATOM   7270  C CB  . VAL C 1 55  ? 12.845  37.146  47.527  1.00 27.74  ? 84  VAL C CB  1 
ATOM   7271  C CG1 . VAL C 1 55  ? 13.724  36.116  48.219  1.00 29.40  ? 84  VAL C CG1 1 
ATOM   7272  C CG2 . VAL C 1 55  ? 11.713  37.572  48.454  1.00 30.29  ? 84  VAL C CG2 1 
ATOM   7273  N N   . LEU C 1 56  ? 15.975  37.868  46.455  1.00 27.29  ? 85  LEU C N   1 
ATOM   7274  C CA  . LEU C 1 56  ? 17.097  37.399  45.676  1.00 28.14  ? 85  LEU C CA  1 
ATOM   7275  C C   . LEU C 1 56  ? 17.392  35.962  46.099  1.00 32.73  ? 85  LEU C C   1 
ATOM   7276  O O   . LEU C 1 56  ? 17.758  35.704  47.250  1.00 30.63  ? 85  LEU C O   1 
ATOM   7277  C CB  . LEU C 1 56  ? 18.287  38.332  45.924  1.00 28.77  ? 85  LEU C CB  1 
ATOM   7278  C CG  . LEU C 1 56  ? 19.594  37.938  45.236  1.00 27.26  ? 85  LEU C CG  1 
ATOM   7279  C CD1 . LEU C 1 56  ? 19.417  37.988  43.729  1.00 26.95  ? 85  LEU C CD1 1 
ATOM   7280  C CD2 . LEU C 1 56  ? 20.763  38.820  45.696  1.00 28.34  ? 85  LEU C CD2 1 
ATOM   7281  N N   . ASP C 1 57  ? 17.153  35.029  45.179  1.00 36.05  ? 86  ASP C N   1 
ATOM   7282  C CA  . ASP C 1 57  ? 17.661  33.679  45.313  1.00 38.12  ? 86  ASP C CA  1 
ATOM   7283  C C   . ASP C 1 57  ? 19.138  33.648  44.925  1.00 37.28  ? 86  ASP C C   1 
ATOM   7284  O O   . ASP C 1 57  ? 19.473  34.049  43.814  1.00 39.20  ? 86  ASP C O   1 
ATOM   7285  C CB  . ASP C 1 57  ? 16.950  32.694  44.386  1.00 38.04  ? 86  ASP C CB  1 
ATOM   7286  C CG  . ASP C 1 57  ? 17.499  31.291  44.569  1.00 37.97  ? 86  ASP C CG  1 
ATOM   7287  O OD1 . ASP C 1 57  ? 17.204  30.697  45.614  1.00 43.24  ? 86  ASP C OD1 1 
ATOM   7288  O OD2 . ASP C 1 57  ? 18.279  30.840  43.699  1.00 39.38  ? 86  ASP C OD2 1 
ATOM   7289  N N   . PRO C 1 58  ? 20.053  33.125  45.780  1.00 38.26  ? 87  PRO C N   1 
ATOM   7290  C CA  . PRO C 1 58  ? 21.475  33.015  45.427  1.00 37.43  ? 87  PRO C CA  1 
ATOM   7291  C C   . PRO C 1 58  ? 21.795  32.432  44.044  1.00 40.68  ? 87  PRO C C   1 
ATOM   7292  O O   . PRO C 1 58  ? 22.685  32.929  43.355  1.00 42.95  ? 87  PRO C O   1 
ATOM   7293  C CB  . PRO C 1 58  ? 22.004  32.073  46.518  1.00 37.53  ? 87  PRO C CB  1 
ATOM   7294  C CG  . PRO C 1 58  ? 21.158  32.407  47.720  1.00 39.17  ? 87  PRO C CG  1 
ATOM   7295  C CD  . PRO C 1 58  ? 19.776  32.630  47.143  1.00 37.94  ? 87  PRO C CD  1 
ATOM   7296  N N   . ASP C 1 59  ? 21.074  31.376  43.645  1.00 40.63  ? 88  ASP C N   1 
ATOM   7297  C CA  . ASP C 1 59  ? 21.359  30.683  42.396  1.00 44.44  ? 88  ASP C CA  1 
ATOM   7298  C C   . ASP C 1 59  ? 20.591  31.277  41.215  1.00 43.58  ? 88  ASP C C   1 
ATOM   7299  O O   . ASP C 1 59  ? 21.143  31.339  40.114  1.00 44.75  ? 88  ASP C O   1 
ATOM   7300  C CB  . ASP C 1 59  ? 21.089  29.185  42.538  1.00 46.92  ? 88  ASP C CB  1 
ATOM   7301  C CG  . ASP C 1 59  ? 22.305  28.408  43.004  1.00 47.35  ? 88  ASP C CG  1 
ATOM   7302  O OD1 . ASP C 1 59  ? 23.430  28.920  42.825  1.00 49.73  ? 88  ASP C OD1 1 
ATOM   7303  O OD2 . ASP C 1 59  ? 22.114  27.312  43.548  1.00 51.44  ? 88  ASP C OD2 1 
ATOM   7304  N N   . GLU C 1 60  ? 19.330  31.702  41.434  1.00 43.87  ? 89  GLU C N   1 
ATOM   7305  C CA  . GLU C 1 60  ? 18.418  32.040  40.344  1.00 41.93  ? 89  GLU C CA  1 
ATOM   7306  C C   . GLU C 1 60  ? 18.402  33.539  40.042  1.00 42.04  ? 89  GLU C C   1 
ATOM   7307  O O   . GLU C 1 60  ? 18.085  33.938  38.924  1.00 45.73  ? 89  GLU C O   1 
ATOM   7308  C CB  . GLU C 1 60  ? 16.998  31.563  40.665  1.00 47.33  ? 89  GLU C CB  1 
ATOM   7309  C CG  . GLU C 1 60  ? 16.896  30.068  40.924  1.00 52.78  ? 89  GLU C CG  1 
ATOM   7310  C CD  . GLU C 1 60  ? 17.826  29.198  40.090  1.00 58.77  ? 89  GLU C CD  1 
ATOM   7311  O OE1 . GLU C 1 60  ? 17.876  29.393  38.853  1.00 61.69  ? 89  GLU C OE1 1 
ATOM   7312  O OE2 . GLU C 1 60  ? 18.498  28.319  40.679  1.00 64.85  ? 89  GLU C OE2 1 
ATOM   7313  N N   . GLY C 1 61  ? 18.711  34.377  41.039  1.00 36.73  ? 90  GLY C N   1 
ATOM   7314  C CA  . GLY C 1 61  ? 18.696  35.820  40.857  1.00 31.90  ? 90  GLY C CA  1 
ATOM   7315  C C   . GLY C 1 61  ? 17.409  36.447  41.386  1.00 26.17  ? 90  GLY C C   1 
ATOM   7316  O O   . GLY C 1 61  ? 16.608  35.790  42.045  1.00 24.47  ? 90  GLY C O   1 
ATOM   7317  N N   . ILE C 1 62  ? 17.241  37.745  41.120  1.00 25.70  ? 91  ILE C N   1 
ATOM   7318  C CA  . ILE C 1 62  ? 16.173  38.517  41.730  1.00 24.74  ? 91  ILE C CA  1 
ATOM   7319  C C   . ILE C 1 62  ? 14.819  38.074  41.194  1.00 25.95  ? 91  ILE C C   1 
ATOM   7320  O O   . ILE C 1 62  ? 14.695  37.772  40.004  1.00 30.42  ? 91  ILE C O   1 
ATOM   7321  C CB  . ILE C 1 62  ? 16.398  40.025  41.483  1.00 23.76  ? 91  ILE C CB  1 
ATOM   7322  C CG1 . ILE C 1 62  ? 15.597  40.882  42.458  1.00 21.21  ? 91  ILE C CG1 1 
ATOM   7323  C CG2 . ILE C 1 62  ? 16.099  40.406  40.047  1.00 23.47  ? 91  ILE C CG2 1 
ATOM   7324  C CD1 . ILE C 1 62  ? 15.883  40.597  43.901  1.00 19.99  ? 91  ILE C CD1 1 
ATOM   7325  N N   . ARG C 1 63  ? 13.830  38.053  42.094  1.00 26.72  ? 92  ARG C N   1 
ATOM   7326  C CA  . ARG C 1 63  ? 12.421  37.936  41.758  1.00 29.18  ? 92  ARG C CA  1 
ATOM   7327  C C   . ARG C 1 63  ? 11.661  39.132  42.351  1.00 25.74  ? 92  ARG C C   1 
ATOM   7328  O O   . ARG C 1 63  ? 11.804  39.450  43.533  1.00 27.56  ? 92  ARG C O   1 
ATOM   7329  C CB  . ARG C 1 63  ? 11.855  36.610  42.260  1.00 33.70  ? 92  ARG C CB  1 
ATOM   7330  C CG  . ARG C 1 63  ? 12.364  35.411  41.469  1.00 37.86  ? 92  ARG C CG  1 
ATOM   7331  C CD  . ARG C 1 63  ? 11.554  34.157  41.729  1.00 41.48  ? 92  ARG C CD  1 
ATOM   7332  N NE  . ARG C 1 63  ? 12.014  33.071  40.868  1.00 48.51  ? 92  ARG C NE  1 
ATOM   7333  C CZ  . ARG C 1 63  ? 11.250  32.394  40.015  1.00 55.61  ? 92  ARG C CZ  1 
ATOM   7334  N NH1 . ARG C 1 63  ? 9.969   32.696  39.876  1.00 56.48  ? 92  ARG C NH1 1 
ATOM   7335  N NH2 . ARG C 1 63  ? 11.773  31.413  39.297  1.00 57.30  ? 92  ARG C NH2 1 
ATOM   7336  N N   . PHE C 1 64  ? 10.915  39.816  41.489  1.00 25.33  ? 93  PHE C N   1 
ATOM   7337  C CA  . PHE C 1 64  ? 10.018  40.902  41.871  1.00 23.82  ? 93  PHE C CA  1 
ATOM   7338  C C   . PHE C 1 64  ? 8.608   40.358  42.106  1.00 22.86  ? 93  PHE C C   1 
ATOM   7339  O O   . PHE C 1 64  ? 7.911   40.017  41.146  1.00 26.33  ? 93  PHE C O   1 
ATOM   7340  C CB  . PHE C 1 64  ? 9.963   41.959  40.767  1.00 25.57  ? 93  PHE C CB  1 
ATOM   7341  C CG  . PHE C 1 64  ? 11.293  42.526  40.342  1.00 23.79  ? 93  PHE C CG  1 
ATOM   7342  C CD1 . PHE C 1 64  ? 12.129  43.168  41.255  1.00 24.98  ? 93  PHE C CD1 1 
ATOM   7343  C CD2 . PHE C 1 64  ? 11.714  42.437  39.024  1.00 23.98  ? 93  PHE C CD2 1 
ATOM   7344  C CE1 . PHE C 1 64  ? 13.360  43.672  40.861  1.00 22.73  ? 93  PHE C CE1 1 
ATOM   7345  C CE2 . PHE C 1 64  ? 12.924  42.991  38.625  1.00 26.23  ? 93  PHE C CE2 1 
ATOM   7346  C CZ  . PHE C 1 64  ? 13.746  43.611  39.539  1.00 23.77  ? 93  PHE C CZ  1 
ATOM   7347  N N   . ARG C 1 65  ? 8.195   40.319  43.380  1.00 22.70  ? 94  ARG C N   1 
ATOM   7348  C CA  . ARG C 1 65  ? 6.961   39.699  43.855  1.00 21.26  ? 94  ARG C CA  1 
ATOM   7349  C C   . ARG C 1 65  ? 6.735   38.314  43.249  1.00 22.79  ? 94  ARG C C   1 
ATOM   7350  O O   . ARG C 1 65  ? 5.606   37.959  42.912  1.00 25.27  ? 94  ARG C O   1 
ATOM   7351  C CB  . ARG C 1 65  ? 5.758   40.606  43.595  1.00 22.27  ? 94  ARG C CB  1 
ATOM   7352  C CG  . ARG C 1 65  ? 5.805   41.897  44.397  1.00 21.40  ? 94  ARG C CG  1 
ATOM   7353  C CD  . ARG C 1 65  ? 5.497   41.712  45.865  1.00 21.31  ? 94  ARG C CD  1 
ATOM   7354  N NE  . ARG C 1 65  ? 5.154   42.947  46.552  1.00 20.69  ? 94  ARG C NE  1 
ATOM   7355  C CZ  . ARG C 1 65  ? 4.635   43.002  47.772  1.00 21.01  ? 94  ARG C CZ  1 
ATOM   7356  N NH1 . ARG C 1 65  ? 4.534   41.904  48.491  1.00 20.92  ? 94  ARG C NH1 1 
ATOM   7357  N NH2 . ARG C 1 65  ? 4.231   44.156  48.283  1.00 23.23  ? 94  ARG C NH2 1 
ATOM   7358  N N   . GLY C 1 66  ? 7.786   37.503  43.183  1.00 25.20  ? 95  GLY C N   1 
ATOM   7359  C CA  . GLY C 1 66  ? 7.667   36.161  42.621  1.00 23.33  ? 95  GLY C CA  1 
ATOM   7360  C C   . GLY C 1 66  ? 8.093   36.022  41.161  1.00 26.20  ? 95  GLY C C   1 
ATOM   7361  O O   . GLY C 1 66  ? 8.345   34.904  40.693  1.00 29.59  ? 95  GLY C O   1 
ATOM   7362  N N   . PHE C 1 67  ? 8.186   37.126  40.422  1.00 25.33  ? 96  PHE C N   1 
ATOM   7363  C CA  . PHE C 1 67  ? 8.401   37.054  38.981  1.00 28.13  ? 96  PHE C CA  1 
ATOM   7364  C C   . PHE C 1 67  ? 9.872   37.279  38.632  1.00 28.63  ? 96  PHE C C   1 
ATOM   7365  O O   . PHE C 1 67  ? 10.493  38.262  39.059  1.00 23.20  ? 96  PHE C O   1 
ATOM   7366  C CB  . PHE C 1 67  ? 7.495   38.066  38.271  1.00 28.86  ? 96  PHE C CB  1 
ATOM   7367  C CG  . PHE C 1 67  ? 6.023   37.740  38.324  1.00 31.84  ? 96  PHE C CG  1 
ATOM   7368  C CD1 . PHE C 1 67  ? 5.476   36.755  37.510  1.00 36.97  ? 96  PHE C CD1 1 
ATOM   7369  C CD2 . PHE C 1 67  ? 5.179   38.394  39.208  1.00 32.65  ? 96  PHE C CD2 1 
ATOM   7370  C CE1 . PHE C 1 67  ? 4.122   36.457  37.557  1.00 36.39  ? 96  PHE C CE1 1 
ATOM   7371  C CE2 . PHE C 1 67  ? 3.824   38.100  39.245  1.00 33.40  ? 96  PHE C CE2 1 
ATOM   7372  C CZ  . PHE C 1 67  ? 3.297   37.133  38.420  1.00 32.85  ? 96  PHE C CZ  1 
ATOM   7373  N N   . SER C 1 68  ? 10.404  36.369  37.794  1.00 28.98  ? 97  SER C N   1 
ATOM   7374  C CA  . SER C 1 68  ? 11.745  36.513  37.258  1.00 30.23  ? 97  SER C CA  1 
ATOM   7375  C C   . SER C 1 68  ? 11.761  37.714  36.319  1.00 26.98  ? 97  SER C C   1 
ATOM   7376  O O   . SER C 1 68  ? 10.702  38.196  35.944  1.00 26.52  ? 97  SER C O   1 
ATOM   7377  C CB  . SER C 1 68  ? 12.180  35.255  36.530  1.00 33.16  ? 97  SER C CB  1 
ATOM   7378  O OG  . SER C 1 68  ? 11.567  35.211  35.257  1.00 35.83  ? 97  SER C OG  1 
ATOM   7379  N N   . ILE C 1 69  ? 12.958  38.187  35.948  1.00 25.51  ? 98  ILE C N   1 
ATOM   7380  C CA  . ILE C 1 69  ? 13.083  39.272  34.994  1.00 28.19  ? 98  ILE C CA  1 
ATOM   7381  C C   . ILE C 1 69  ? 12.564  38.836  33.614  1.00 30.69  ? 98  ILE C C   1 
ATOM   7382  O O   . ILE C 1 69  ? 11.788  39.564  32.981  1.00 30.71  ? 98  ILE C O   1 
ATOM   7383  C CB  . ILE C 1 69  ? 14.520  39.846  34.960  1.00 26.07  ? 98  ILE C CB  1 
ATOM   7384  C CG1 . ILE C 1 69  ? 14.769  40.774  36.161  1.00 26.98  ? 98  ILE C CG1 1 
ATOM   7385  C CG2 . ILE C 1 69  ? 14.793  40.562  33.652  1.00 27.39  ? 98  ILE C CG2 1 
ATOM   7386  C CD1 . ILE C 1 69  ? 16.162  41.392  36.214  1.00 28.07  ? 98  ILE C CD1 1 
ATOM   7387  N N   . PRO C 1 70  ? 12.985  37.672  33.064  1.00 31.10  ? 99  PRO C N   1 
ATOM   7388  C CA  . PRO C 1 70  ? 12.352  37.137  31.851  1.00 32.53  ? 99  PRO C CA  1 
ATOM   7389  C C   . PRO C 1 70  ? 10.818  37.161  31.810  1.00 35.02  ? 99  PRO C C   1 
ATOM   7390  O O   . PRO C 1 70  ? 10.235  37.519  30.789  1.00 40.92  ? 99  PRO C O   1 
ATOM   7391  C CB  . PRO C 1 70  ? 12.896  35.702  31.840  1.00 30.55  ? 99  PRO C CB  1 
ATOM   7392  C CG  . PRO C 1 70  ? 14.300  35.866  32.379  1.00 32.52  ? 99  PRO C CG  1 
ATOM   7393  C CD  . PRO C 1 70  ? 14.141  36.868  33.510  1.00 31.73  ? 99  PRO C CD  1 
ATOM   7394  N N   . GLU C 1 71  ? 10.173  36.797  32.920  1.00 32.95  ? 100 GLU C N   1 
ATOM   7395  C CA  . GLU C 1 71  ? 8.725   36.878  33.056  1.00 38.06  ? 100 GLU C CA  1 
ATOM   7396  C C   . GLU C 1 71  ? 8.239   38.328  33.024  1.00 37.00  ? 100 GLU C C   1 
ATOM   7397  O O   . GLU C 1 71  ? 7.181   38.604  32.470  1.00 33.17  ? 100 GLU C O   1 
ATOM   7398  C CB  . GLU C 1 71  ? 8.268   36.184  34.342  1.00 40.48  ? 100 GLU C CB  1 
ATOM   7399  C CG  . GLU C 1 71  ? 8.420   34.684  34.267  1.00 40.96  ? 100 GLU C CG  1 
ATOM   7400  C CD  . GLU C 1 71  ? 8.130   33.908  35.533  1.00 42.55  ? 100 GLU C CD  1 
ATOM   7401  O OE1 . GLU C 1 71  ? 8.771   34.208  36.576  1.00 45.90  ? 100 GLU C OE1 1 
ATOM   7402  O OE2 . GLU C 1 71  ? 7.280   32.994  35.467  1.00 40.75  ? 100 GLU C OE2 1 
ATOM   7403  N N   . CYS C 1 72  ? 8.984   39.252  33.644  1.00 37.00  ? 101 CYS C N   1 
ATOM   7404  C CA  . CYS C 1 72  ? 8.585   40.651  33.642  1.00 34.38  ? 101 CYS C CA  1 
ATOM   7405  C C   . CYS C 1 72  ? 8.695   41.227  32.233  1.00 33.53  ? 101 CYS C C   1 
ATOM   7406  O O   . CYS C 1 72  ? 7.936   42.111  31.836  1.00 33.66  ? 101 CYS C O   1 
ATOM   7407  C CB  . CYS C 1 72  ? 9.440   41.479  34.592  1.00 34.64  ? 101 CYS C CB  1 
ATOM   7408  S SG  . CYS C 1 72  ? 9.028   41.200  36.331  1.00 36.37  ? 101 CYS C SG  1 
ATOM   7409  N N   . GLN C 1 73  ? 9.680   40.734  31.490  1.00 30.37  ? 102 GLN C N   1 
ATOM   7410  C CA  . GLN C 1 73  ? 9.883   41.188  30.129  1.00 32.57  ? 102 GLN C CA  1 
ATOM   7411  C C   . GLN C 1 73  ? 8.739   40.718  29.242  1.00 34.23  ? 102 GLN C C   1 
ATOM   7412  O O   . GLN C 1 73  ? 8.421   41.396  28.272  1.00 41.36  ? 102 GLN C O   1 
ATOM   7413  C CB  . GLN C 1 73  ? 11.236  40.707  29.624  1.00 31.63  ? 102 GLN C CB  1 
ATOM   7414  C CG  . GLN C 1 73  ? 12.369  41.548  30.180  1.00 30.84  ? 102 GLN C CG  1 
ATOM   7415  C CD  . GLN C 1 73  ? 13.673  41.130  29.568  1.00 33.57  ? 102 GLN C CD  1 
ATOM   7416  O OE1 . GLN C 1 73  ? 14.068  39.969  29.671  1.00 32.75  ? 102 GLN C OE1 1 
ATOM   7417  N NE2 . GLN C 1 73  ? 14.344  42.073  28.921  1.00 33.07  ? 102 GLN C NE2 1 
ATOM   7418  N N   . LYS C 1 74  ? 8.145   39.568  29.576  1.00 35.54  ? 103 LYS C N   1 
ATOM   7419  C CA  . LYS C 1 74  ? 7.010   39.041  28.842  1.00 41.06  ? 103 LYS C CA  1 
ATOM   7420  C C   . LYS C 1 74  ? 5.699   39.676  29.315  1.00 40.45  ? 103 LYS C C   1 
ATOM   7421  O O   . LYS C 1 74  ? 4.838   39.955  28.481  1.00 44.56  ? 103 LYS C O   1 
ATOM   7422  C CB  . LYS C 1 74  ? 6.954   37.514  28.975  1.00 47.22  ? 103 LYS C CB  1 
ATOM   7423  C CG  . LYS C 1 74  ? 8.096   36.756  28.299  1.00 55.42  ? 103 LYS C CG  1 
ATOM   7424  C CD  . LYS C 1 74  ? 8.200   36.963  26.791  1.00 61.91  ? 103 LYS C CD  1 
ATOM   7425  C CE  . LYS C 1 74  ? 7.073   36.310  26.016  1.00 65.97  ? 103 LYS C CE  1 
ATOM   7426  N NZ  . LYS C 1 74  ? 6.893   36.921  24.675  1.00 66.47  ? 103 LYS C NZ  1 
ATOM   7427  N N   . LEU C 1 75  ? 5.545   39.898  30.633  1.00 34.28  ? 104 LEU C N   1 
ATOM   7428  C CA  . LEU C 1 75  ? 4.236   40.129  31.240  1.00 31.40  ? 104 LEU C CA  1 
ATOM   7429  C C   . LEU C 1 75  ? 3.941   41.616  31.458  1.00 32.80  ? 104 LEU C C   1 
ATOM   7430  O O   . LEU C 1 75  ? 2.795   42.028  31.341  1.00 32.87  ? 104 LEU C O   1 
ATOM   7431  C CB  . LEU C 1 75  ? 4.172   39.366  32.567  1.00 34.46  ? 104 LEU C CB  1 
ATOM   7432  C CG  . LEU C 1 75  ? 4.021   37.852  32.468  1.00 34.47  ? 104 LEU C CG  1 
ATOM   7433  C CD1 . LEU C 1 75  ? 3.745   37.261  33.839  1.00 33.76  ? 104 LEU C CD1 1 
ATOM   7434  C CD2 . LEU C 1 75  ? 2.920   37.463  31.484  1.00 35.61  ? 104 LEU C CD2 1 
ATOM   7435  N N   . LEU C 1 76  ? 4.946   42.415  31.835  1.00 29.79  ? 105 LEU C N   1 
ATOM   7436  C CA  . LEU C 1 76  ? 4.713   43.825  32.117  1.00 28.38  ? 105 LEU C CA  1 
ATOM   7437  C C   . LEU C 1 76  ? 4.412   44.555  30.816  1.00 30.05  ? 105 LEU C C   1 
ATOM   7438  O O   . LEU C 1 76  ? 5.029   44.261  29.795  1.00 32.68  ? 105 LEU C O   1 
ATOM   7439  C CB  . LEU C 1 76  ? 5.944   44.437  32.800  1.00 25.74  ? 105 LEU C CB  1 
ATOM   7440  C CG  . LEU C 1 76  ? 6.184   44.009  34.246  1.00 25.91  ? 105 LEU C CG  1 
ATOM   7441  C CD1 . LEU C 1 76  ? 7.482   44.596  34.796  1.00 26.32  ? 105 LEU C CD1 1 
ATOM   7442  C CD2 . LEU C 1 76  ? 5.004   44.404  35.114  1.00 26.58  ? 105 LEU C CD2 1 
ATOM   7443  N N   . PRO C 1 77  ? 3.453   45.513  30.816  1.00 28.40  ? 106 PRO C N   1 
ATOM   7444  C CA  . PRO C 1 77  ? 3.220   46.391  29.668  1.00 30.90  ? 106 PRO C CA  1 
ATOM   7445  C C   . PRO C 1 77  ? 4.447   47.098  29.108  1.00 31.14  ? 106 PRO C C   1 
ATOM   7446  O O   . PRO C 1 77  ? 5.324   47.540  29.844  1.00 32.98  ? 106 PRO C O   1 
ATOM   7447  C CB  . PRO C 1 77  ? 2.239   47.435  30.231  1.00 29.78  ? 106 PRO C CB  1 
ATOM   7448  C CG  . PRO C 1 77  ? 1.410   46.605  31.197  1.00 31.74  ? 106 PRO C CG  1 
ATOM   7449  C CD  . PRO C 1 77  ? 2.432   45.694  31.854  1.00 28.70  ? 106 PRO C CD  1 
ATOM   7450  N N   . LYS C 1 78  ? 4.458   47.204  27.780  1.00 30.94  ? 107 LYS C N   1 
ATOM   7451  C CA  . LYS C 1 78  ? 5.471   47.922  27.024  1.00 34.36  ? 107 LYS C CA  1 
ATOM   7452  C C   . LYS C 1 78  ? 4.863   49.243  26.552  1.00 32.37  ? 107 LYS C C   1 
ATOM   7453  O O   . LYS C 1 78  ? 3.649   49.424  26.608  1.00 34.77  ? 107 LYS C O   1 
ATOM   7454  C CB  . LYS C 1 78  ? 5.947   46.985  25.901  1.00 35.41  ? 107 LYS C CB  1 
ATOM   7455  C CG  . LYS C 1 78  ? 6.611   45.717  26.427  1.00 35.67  ? 107 LYS C CG  1 
ATOM   7456  C CD  . LYS C 1 78  ? 6.351   44.471  25.624  1.00 39.70  ? 107 LYS C CD  1 
ATOM   7457  C CE  . LYS C 1 78  ? 6.816   43.213  26.326  1.00 41.82  ? 107 LYS C CE  1 
ATOM   7458  N NZ  . LYS C 1 78  ? 5.970   42.878  27.500  1.00 43.89  ? 107 LYS C NZ  1 
ATOM   7459  N N   . ALA C 1 79  ? 5.700   50.175  26.105  1.00 34.54  ? 108 ALA C N   1 
ATOM   7460  C CA  . ALA C 1 79  ? 5.197   51.321  25.365  1.00 35.63  ? 108 ALA C CA  1 
ATOM   7461  C C   . ALA C 1 79  ? 4.604   50.809  24.050  1.00 36.13  ? 108 ALA C C   1 
ATOM   7462  O O   . ALA C 1 79  ? 5.041   49.779  23.543  1.00 30.74  ? 108 ALA C O   1 
ATOM   7463  C CB  . ALA C 1 79  ? 6.297   52.319  25.136  1.00 38.37  ? 108 ALA C CB  1 
ATOM   7464  N N   . LYS C 1 80  ? 3.600   51.513  23.508  1.00 38.48  ? 109 LYS C N   1 
ATOM   7465  C CA  . LYS C 1 80  ? 2.836   50.978  22.386  1.00 44.83  ? 109 LYS C CA  1 
ATOM   7466  C C   . LYS C 1 80  ? 3.768   50.545  21.252  1.00 45.76  ? 109 LYS C C   1 
ATOM   7467  O O   . LYS C 1 80  ? 3.477   49.572  20.555  1.00 48.89  ? 109 LYS C O   1 
ATOM   7468  C CB  . LYS C 1 80  ? 1.810   51.967  21.822  1.00 47.57  ? 109 LYS C CB  1 
ATOM   7469  C CG  . LYS C 1 80  ? 0.896   52.657  22.829  1.00 51.25  ? 109 LYS C CG  1 
ATOM   7470  C CD  . LYS C 1 80  ? 1.410   54.001  23.346  1.00 55.57  ? 109 LYS C CD  1 
ATOM   7471  C CE  . LYS C 1 80  ? 1.986   54.888  22.259  1.00 55.21  ? 109 LYS C CE  1 
ATOM   7472  N NZ  . LYS C 1 80  ? 2.173   56.284  22.717  1.00 57.26  ? 109 LYS C NZ  1 
ATOM   7473  N N   . GLY C 1 81  ? 4.883   51.258  21.056  1.00 40.77  ? 110 GLY C N   1 
ATOM   7474  C CA  . GLY C 1 81  ? 5.816   50.855  20.014  1.00 46.02  ? 110 GLY C CA  1 
ATOM   7475  C C   . GLY C 1 81  ? 6.992   50.007  20.517  1.00 40.41  ? 110 GLY C C   1 
ATOM   7476  O O   . GLY C 1 81  ? 7.960   49.861  19.787  1.00 35.66  ? 110 GLY C O   1 
ATOM   7477  N N   . GLY C 1 82  ? 6.897   49.413  21.723  1.00 39.72  ? 111 GLY C N   1 
ATOM   7478  C CA  . GLY C 1 82  ? 8.085   49.059  22.497  1.00 35.31  ? 111 GLY C CA  1 
ATOM   7479  C C   . GLY C 1 82  ? 8.282   47.563  22.723  1.00 31.63  ? 111 GLY C C   1 
ATOM   7480  O O   . GLY C 1 82  ? 7.339   46.787  22.587  1.00 33.54  ? 111 GLY C O   1 
ATOM   7481  N N   . GLU C 1 83  ? 9.520   47.180  23.094  1.00 32.16  ? 112 GLU C N   1 
ATOM   7482  C CA  . GLU C 1 83  ? 9.861   45.805  23.452  1.00 31.58  ? 112 GLU C CA  1 
ATOM   7483  C C   . GLU C 1 83  ? 10.093  45.644  24.954  1.00 30.50  ? 112 GLU C C   1 
ATOM   7484  O O   . GLU C 1 83  ? 9.874   44.566  25.504  1.00 29.37  ? 112 GLU C O   1 
ATOM   7485  C CB  . GLU C 1 83  ? 11.180  45.366  22.809  1.00 36.16  ? 112 GLU C CB  1 
ATOM   7486  C CG  . GLU C 1 83  ? 11.268  45.677  21.324  1.00 41.11  ? 112 GLU C CG  1 
ATOM   7487  C CD  . GLU C 1 83  ? 10.017  45.314  20.549  1.00 42.68  ? 112 GLU C CD  1 
ATOM   7488  O OE1 . GLU C 1 83  ? 9.537   44.177  20.702  1.00 41.43  ? 112 GLU C OE1 1 
ATOM   7489  O OE2 . GLU C 1 83  ? 9.524   46.178  19.800  1.00 45.85  ? 112 GLU C OE2 1 
ATOM   7490  N N   . GLU C 1 84  ? 10.574  46.711  25.595  1.00 29.15  ? 113 GLU C N   1 
ATOM   7491  C CA  . GLU C 1 84  ? 11.150  46.630  26.927  1.00 31.87  ? 113 GLU C CA  1 
ATOM   7492  C C   . GLU C 1 84  ? 10.108  47.049  27.971  1.00 29.27  ? 113 GLU C C   1 
ATOM   7493  O O   . GLU C 1 84  ? 9.321   47.968  27.734  1.00 31.94  ? 113 GLU C O   1 
ATOM   7494  C CB  . GLU C 1 84  ? 12.421  47.486  26.984  1.00 32.17  ? 113 GLU C CB  1 
ATOM   7495  C CG  . GLU C 1 84  ? 13.556  47.002  26.082  1.00 38.18  ? 113 GLU C CG  1 
ATOM   7496  C CD  . GLU C 1 84  ? 14.067  45.590  26.357  1.00 39.39  ? 113 GLU C CD  1 
ATOM   7497  O OE1 . GLU C 1 84  ? 13.732  45.036  27.444  1.00 37.49  ? 113 GLU C OE1 1 
ATOM   7498  O OE2 . GLU C 1 84  ? 14.760  45.014  25.462  1.00 37.20  ? 113 GLU C OE2 1 
ATOM   7499  N N   . PRO C 1 85  ? 10.023  46.365  29.132  1.00 27.40  ? 114 PRO C N   1 
ATOM   7500  C CA  . PRO C 1 85  ? 8.959   46.654  30.108  1.00 26.08  ? 114 PRO C CA  1 
ATOM   7501  C C   . PRO C 1 85  ? 9.085   48.059  30.690  1.00 26.89  ? 114 PRO C C   1 
ATOM   7502  O O   . PRO C 1 85  ? 10.196  48.560  30.881  1.00 27.95  ? 114 PRO C O   1 
ATOM   7503  C CB  . PRO C 1 85  ? 9.091   45.523  31.139  1.00 29.20  ? 114 PRO C CB  1 
ATOM   7504  C CG  . PRO C 1 85  ? 10.538  45.008  31.000  1.00 27.22  ? 114 PRO C CG  1 
ATOM   7505  C CD  . PRO C 1 85  ? 10.895  45.241  29.545  1.00 27.69  ? 114 PRO C CD  1 
ATOM   7506  N N   . LEU C 1 86  ? 7.936   48.699  30.951  1.00 25.48  ? 115 LEU C N   1 
ATOM   7507  C CA  . LEU C 1 86  ? 7.920   50.047  31.502  1.00 24.53  ? 115 LEU C CA  1 
ATOM   7508  C C   . LEU C 1 86  ? 8.149   49.986  33.009  1.00 24.86  ? 115 LEU C C   1 
ATOM   7509  O O   . LEU C 1 86  ? 7.486   49.239  33.712  1.00 22.97  ? 115 LEU C O   1 
ATOM   7510  C CB  . LEU C 1 86  ? 6.585   50.733  31.195  1.00 28.79  ? 115 LEU C CB  1 
ATOM   7511  C CG  . LEU C 1 86  ? 6.338   51.089  29.728  1.00 28.67  ? 115 LEU C CG  1 
ATOM   7512  C CD1 . LEU C 1 86  ? 5.090   51.947  29.612  1.00 31.14  ? 115 LEU C CD1 1 
ATOM   7513  C CD2 . LEU C 1 86  ? 7.542   51.798  29.117  1.00 29.14  ? 115 LEU C CD2 1 
ATOM   7514  N N   . PRO C 1 87  ? 9.071   50.806  33.563  1.00 26.38  ? 116 PRO C N   1 
ATOM   7515  C CA  . PRO C 1 87  ? 9.261   50.862  35.014  1.00 24.43  ? 116 PRO C CA  1 
ATOM   7516  C C   . PRO C 1 87  ? 7.971   51.200  35.773  1.00 25.46  ? 116 PRO C C   1 
ATOM   7517  O O   . PRO C 1 87  ? 7.776   50.682  36.863  1.00 23.86  ? 116 PRO C O   1 
ATOM   7518  C CB  . PRO C 1 87  ? 10.422  51.853  35.193  1.00 25.28  ? 116 PRO C CB  1 
ATOM   7519  C CG  . PRO C 1 87  ? 10.405  52.680  33.943  1.00 29.13  ? 116 PRO C CG  1 
ATOM   7520  C CD  . PRO C 1 87  ? 9.966   51.721  32.846  1.00 26.14  ? 116 PRO C CD  1 
ATOM   7521  N N   . GLU C 1 88  ? 7.042   51.952  35.174  1.00 25.00  ? 117 GLU C N   1 
ATOM   7522  C CA  . GLU C 1 88  ? 5.697   52.061  35.738  1.00 24.05  ? 117 GLU C CA  1 
ATOM   7523  C C   . GLU C 1 88  ? 5.136   50.702  36.122  1.00 25.86  ? 117 GLU C C   1 
ATOM   7524  O O   . GLU C 1 88  ? 4.687   50.499  37.250  1.00 25.82  ? 117 GLU C O   1 
ATOM   7525  C CB  . GLU C 1 88  ? 4.682   52.667  34.770  1.00 23.68  ? 117 GLU C CB  1 
ATOM   7526  C CG  . GLU C 1 88  ? 4.882   54.156  34.558  1.00 25.48  ? 117 GLU C CG  1 
ATOM   7527  C CD  . GLU C 1 88  ? 5.892   54.494  33.477  1.00 27.93  ? 117 GLU C CD  1 
ATOM   7528  O OE1 . GLU C 1 88  ? 6.878   53.734  33.342  1.00 25.14  ? 117 GLU C OE1 1 
ATOM   7529  O OE2 . GLU C 1 88  ? 5.713   55.529  32.795  1.00 29.52  ? 117 GLU C OE2 1 
ATOM   7530  N N   . GLY C 1 89  ? 5.058   49.810  35.134  1.00 24.32  ? 118 GLY C N   1 
ATOM   7531  C CA  . GLY C 1 89  ? 4.448   48.514  35.370  1.00 24.37  ? 118 GLY C CA  1 
ATOM   7532  C C   . GLY C 1 89  ? 5.148   47.752  36.495  1.00 23.11  ? 118 GLY C C   1 
ATOM   7533  O O   . GLY C 1 89  ? 4.524   46.981  37.220  1.00 24.38  ? 118 GLY C O   1 
ATOM   7534  N N   . LEU C 1 90  ? 6.468   47.909  36.581  1.00 21.73  ? 119 LEU C N   1 
ATOM   7535  C CA  . LEU C 1 90  ? 7.218   47.261  37.638  1.00 23.36  ? 119 LEU C CA  1 
ATOM   7536  C C   . LEU C 1 90  ? 6.823   47.833  38.998  1.00 19.32  ? 119 LEU C C   1 
ATOM   7537  O O   . LEU C 1 90  ? 6.653   47.097  39.946  1.00 21.72  ? 119 LEU C O   1 
ATOM   7538  C CB  . LEU C 1 90  ? 8.716   47.453  37.437  1.00 26.53  ? 119 LEU C CB  1 
ATOM   7539  C CG  . LEU C 1 90  ? 9.515   46.949  38.640  1.00 30.26  ? 119 LEU C CG  1 
ATOM   7540  C CD1 . LEU C 1 90  ? 10.442  45.825  38.262  1.00 32.24  ? 119 LEU C CD1 1 
ATOM   7541  C CD2 . LEU C 1 90  ? 10.234  48.094  39.307  1.00 32.61  ? 119 LEU C CD2 1 
ATOM   7542  N N   . PHE C 1 91  ? 6.724   49.173  39.103  1.00 19.14  ? 120 PHE C N   1 
ATOM   7543  C CA  . PHE C 1 91  ? 6.340   49.748  40.382  1.00 17.94  ? 120 PHE C CA  1 
ATOM   7544  C C   . PHE C 1 91  ? 4.991   49.176  40.830  1.00 19.80  ? 120 PHE C C   1 
ATOM   7545  O O   . PHE C 1 91  ? 4.799   48.818  42.007  1.00 19.57  ? 120 PHE C O   1 
ATOM   7546  C CB  . PHE C 1 91  ? 6.380   51.276  40.281  1.00 18.51  ? 120 PHE C CB  1 
ATOM   7547  C CG  . PHE C 1 91  ? 6.003   51.937  41.584  1.00 19.59  ? 120 PHE C CG  1 
ATOM   7548  C CD1 . PHE C 1 91  ? 6.897   51.988  42.643  1.00 16.98  ? 120 PHE C CD1 1 
ATOM   7549  C CD2 . PHE C 1 91  ? 4.730   52.451  41.784  1.00 18.22  ? 120 PHE C CD2 1 
ATOM   7550  C CE1 . PHE C 1 91  ? 6.560   52.579  43.859  1.00 16.99  ? 120 PHE C CE1 1 
ATOM   7551  C CE2 . PHE C 1 91  ? 4.396   53.023  43.007  1.00 18.02  ? 120 PHE C CE2 1 
ATOM   7552  C CZ  . PHE C 1 91  ? 5.306   53.103  44.032  1.00 17.58  ? 120 PHE C CZ  1 
ATOM   7553  N N   . TRP C 1 92  ? 4.061   49.058  39.876  1.00 21.67  ? 121 TRP C N   1 
ATOM   7554  C CA  . TRP C 1 92  ? 2.729   48.570  40.190  1.00 21.98  ? 121 TRP C CA  1 
ATOM   7555  C C   . TRP C 1 92  ? 2.846   47.158  40.749  1.00 20.45  ? 121 TRP C C   1 
ATOM   7556  O O   . TRP C 1 92  ? 2.238   46.825  41.761  1.00 24.21  ? 121 TRP C O   1 
ATOM   7557  C CB  . TRP C 1 92  ? 1.843   48.617  38.941  1.00 24.64  ? 121 TRP C CB  1 
ATOM   7558  C CG  . TRP C 1 92  ? 0.395   48.367  39.199  1.00 23.22  ? 121 TRP C CG  1 
ATOM   7559  C CD1 . TRP C 1 92  ? -0.200  47.175  39.484  1.00 23.47  ? 121 TRP C CD1 1 
ATOM   7560  C CD2 . TRP C 1 92  ? -0.648  49.352  39.229  1.00 24.18  ? 121 TRP C CD2 1 
ATOM   7561  N NE1 . TRP C 1 92  ? -1.539  47.346  39.657  1.00 23.50  ? 121 TRP C NE1 1 
ATOM   7562  C CE2 . TRP C 1 92  ? -1.844  48.672  39.508  1.00 23.72  ? 121 TRP C CE2 1 
ATOM   7563  C CE3 . TRP C 1 92  ? -0.694  50.727  38.979  1.00 24.84  ? 121 TRP C CE3 1 
ATOM   7564  C CZ2 . TRP C 1 92  ? -3.074  49.323  39.576  1.00 26.53  ? 121 TRP C CZ2 1 
ATOM   7565  C CZ3 . TRP C 1 92  ? -1.910  51.377  39.055  1.00 25.86  ? 121 TRP C CZ3 1 
ATOM   7566  C CH2 . TRP C 1 92  ? -3.082  50.682  39.343  1.00 26.60  ? 121 TRP C CH2 1 
ATOM   7567  N N   . LEU C 1 93  ? 3.676   46.330  40.113  1.00 21.71  ? 122 LEU C N   1 
ATOM   7568  C CA  . LEU C 1 93  ? 3.838   44.974  40.600  1.00 21.27  ? 122 LEU C CA  1 
ATOM   7569  C C   . LEU C 1 93  ? 4.367   44.982  42.030  1.00 21.06  ? 122 LEU C C   1 
ATOM   7570  O O   . LEU C 1 93  ? 3.937   44.182  42.851  1.00 20.83  ? 122 LEU C O   1 
ATOM   7571  C CB  . LEU C 1 93  ? 4.811   44.225  39.699  1.00 22.45  ? 122 LEU C CB  1 
ATOM   7572  C CG  . LEU C 1 93  ? 5.225   42.842  40.181  1.00 24.67  ? 122 LEU C CG  1 
ATOM   7573  C CD1 . LEU C 1 93  ? 4.034   41.899  40.190  1.00 24.22  ? 122 LEU C CD1 1 
ATOM   7574  C CD2 . LEU C 1 93  ? 6.351   42.313  39.294  1.00 25.04  ? 122 LEU C CD2 1 
ATOM   7575  N N   . LEU C 1 94  ? 5.359   45.835  42.301  1.00 20.81  ? 123 LEU C N   1 
ATOM   7576  C CA  . LEU C 1 94  ? 6.039   45.830  43.580  1.00 21.33  ? 123 LEU C CA  1 
ATOM   7577  C C   . LEU C 1 94  ? 5.060   46.208  44.684  1.00 21.51  ? 123 LEU C C   1 
ATOM   7578  O O   . LEU C 1 94  ? 5.010   45.533  45.710  1.00 22.62  ? 123 LEU C O   1 
ATOM   7579  C CB  . LEU C 1 94  ? 7.231   46.793  43.532  1.00 22.10  ? 123 LEU C CB  1 
ATOM   7580  C CG  . LEU C 1 94  ? 8.397   46.406  42.622  1.00 21.31  ? 123 LEU C CG  1 
ATOM   7581  C CD1 . LEU C 1 94  ? 9.637   47.186  43.039  1.00 19.17  ? 123 LEU C CD1 1 
ATOM   7582  C CD2 . LEU C 1 94  ? 8.699   44.912  42.684  1.00 21.21  ? 123 LEU C CD2 1 
ATOM   7583  N N   . VAL C 1 95  ? 4.262   47.246  44.404  1.00 24.72  ? 124 VAL C N   1 
ATOM   7584  C CA  . VAL C 1 95  ? 3.272   47.796  45.313  1.00 24.87  ? 124 VAL C CA  1 
ATOM   7585  C C   . VAL C 1 95  ? 2.129   46.812  45.556  1.00 24.46  ? 124 VAL C C   1 
ATOM   7586  O O   . VAL C 1 95  ? 1.785   46.606  46.718  1.00 27.28  ? 124 VAL C O   1 
ATOM   7587  C CB  . VAL C 1 95  ? 2.774   49.168  44.809  1.00 24.39  ? 124 VAL C CB  1 
ATOM   7588  C CG1 . VAL C 1 95  ? 1.460   49.608  45.442  1.00 26.29  ? 124 VAL C CG1 1 
ATOM   7589  C CG2 . VAL C 1 95  ? 3.831   50.228  45.029  1.00 25.18  ? 124 VAL C CG2 1 
ATOM   7590  N N   . THR C 1 96  ? 1.558   46.193  44.501  1.00 23.76  ? 125 THR C N   1 
ATOM   7591  C CA  . THR C 1 96  ? 0.339   45.402  44.652  1.00 22.35  ? 125 THR C CA  1 
ATOM   7592  C C   . THR C 1 96  ? 0.576   43.899  44.638  1.00 23.12  ? 125 THR C C   1 
ATOM   7593  O O   . THR C 1 96  ? -0.319  43.135  44.984  1.00 28.50  ? 125 THR C O   1 
ATOM   7594  C CB  . THR C 1 96  ? -0.655  45.633  43.507  1.00 21.89  ? 125 THR C CB  1 
ATOM   7595  O OG1 . THR C 1 96  ? -0.096  45.058  42.323  1.00 22.50  ? 125 THR C OG1 1 
ATOM   7596  C CG2 . THR C 1 96  ? -0.946  47.100  43.289  1.00 23.12  ? 125 THR C CG2 1 
ATOM   7597  N N   . GLY C 1 97  ? 1.699   43.481  44.069  1.00 23.40  ? 126 GLY C N   1 
ATOM   7598  C CA  . GLY C 1 97  ? 1.974   42.069  43.904  1.00 25.82  ? 126 GLY C CA  1 
ATOM   7599  C C   . GLY C 1 97  ? 1.315   41.487  42.661  1.00 28.02  ? 126 GLY C C   1 
ATOM   7600  O O   . GLY C 1 97  ? 1.397   40.283  42.466  1.00 31.68  ? 126 GLY C O   1 
ATOM   7601  N N   . HIS C 1 98  ? 0.687   42.341  41.843  1.00 29.79  ? 127 HIS C N   1 
ATOM   7602  C CA  . HIS C 1 98  ? -0.058  41.896  40.676  1.00 32.64  ? 127 HIS C CA  1 
ATOM   7603  C C   . HIS C 1 98  ? 0.514   42.552  39.426  1.00 29.11  ? 127 HIS C C   1 
ATOM   7604  O O   . HIS C 1 98  ? 0.944   43.708  39.450  1.00 27.72  ? 127 HIS C O   1 
ATOM   7605  C CB  . HIS C 1 98  ? -1.548  42.238  40.799  1.00 32.65  ? 127 HIS C CB  1 
ATOM   7606  C CG  . HIS C 1 98  ? -2.223  41.626  41.978  1.00 36.39  ? 127 HIS C CG  1 
ATOM   7607  N ND1 . HIS C 1 98  ? -2.522  40.283  42.050  1.00 39.78  ? 127 HIS C ND1 1 
ATOM   7608  C CD2 . HIS C 1 98  ? -2.690  42.175  43.102  1.00 37.92  ? 127 HIS C CD2 1 
ATOM   7609  C CE1 . HIS C 1 98  ? -3.140  40.035  43.198  1.00 40.33  ? 127 HIS C CE1 1 
ATOM   7610  N NE2 . HIS C 1 98  ? -3.248  41.172  43.858  1.00 40.20  ? 127 HIS C NE2 1 
ATOM   7611  N N   . ILE C 1 99  ? 0.519   41.796  38.328  1.00 26.81  ? 128 ILE C N   1 
ATOM   7612  C CA  . ILE C 1 99  ? 0.901   42.337  37.039  1.00 27.21  ? 128 ILE C CA  1 
ATOM   7613  C C   . ILE C 1 99  ? -0.187  43.329  36.617  1.00 26.88  ? 128 ILE C C   1 
ATOM   7614  O O   . ILE C 1 99  ? -1.363  42.954  36.578  1.00 26.89  ? 128 ILE C O   1 
ATOM   7615  C CB  . ILE C 1 99  ? 1.071   41.204  36.002  1.00 27.81  ? 128 ILE C CB  1 
ATOM   7616  C CG1 . ILE C 1 99  ? 2.049   40.105  36.448  1.00 27.35  ? 128 ILE C CG1 1 
ATOM   7617  C CG2 . ILE C 1 99  ? 1.469   41.795  34.656  1.00 26.99  ? 128 ILE C CG2 1 
ATOM   7618  C CD1 . ILE C 1 99  ? 3.486   40.537  36.490  1.00 27.80  ? 128 ILE C CD1 1 
ATOM   7619  N N   . PRO C 1 100 ? 0.151   44.599  36.278  1.00 24.00  ? 129 PRO C N   1 
ATOM   7620  C CA  . PRO C 1 100 ? -0.851  45.569  35.884  1.00 26.09  ? 129 PRO C CA  1 
ATOM   7621  C C   . PRO C 1 100 ? -1.395  45.241  34.503  1.00 28.54  ? 129 PRO C C   1 
ATOM   7622  O O   . PRO C 1 100 ? -0.712  44.616  33.692  1.00 30.26  ? 129 PRO C O   1 
ATOM   7623  C CB  . PRO C 1 100 ? -0.103  46.900  35.860  1.00 24.63  ? 129 PRO C CB  1 
ATOM   7624  C CG  . PRO C 1 100 ? 1.339   46.522  35.586  1.00 24.35  ? 129 PRO C CG  1 
ATOM   7625  C CD  . PRO C 1 100 ? 1.501   45.172  36.258  1.00 25.22  ? 129 PRO C CD  1 
ATOM   7626  N N   . THR C 1 101 ? -2.638  45.671  34.269  1.00 29.95  ? 130 THR C N   1 
ATOM   7627  C CA  . THR C 1 101 ? -3.171  45.806  32.923  1.00 28.67  ? 130 THR C CA  1 
ATOM   7628  C C   . THR C 1 101 ? -2.526  47.004  32.230  1.00 29.40  ? 130 THR C C   1 
ATOM   7629  O O   . THR C 1 101 ? -1.847  47.807  32.852  1.00 27.39  ? 130 THR C O   1 
ATOM   7630  C CB  . THR C 1 101 ? -4.689  46.012  32.961  1.00 27.14  ? 130 THR C CB  1 
ATOM   7631  O OG1 . THR C 1 101 ? -4.917  47.264  33.606  1.00 27.66  ? 130 THR C OG1 1 
ATOM   7632  C CG2 . THR C 1 101 ? -5.410  44.900  33.688  1.00 27.44  ? 130 THR C CG2 1 
ATOM   7633  N N   . GLU C 1 102 ? -2.756  47.109  30.921  1.00 29.38  ? 131 GLU C N   1 
ATOM   7634  C CA  . GLU C 1 102 ? -2.260  48.202  30.111  1.00 28.52  ? 131 GLU C CA  1 
ATOM   7635  C C   . GLU C 1 102 ? -2.780  49.557  30.572  1.00 27.17  ? 131 GLU C C   1 
ATOM   7636  O O   . GLU C 1 102 ? -2.047  50.548  30.556  1.00 26.82  ? 131 GLU C O   1 
ATOM   7637  C CB  . GLU C 1 102 ? -2.748  47.973  28.686  1.00 31.12  ? 131 GLU C CB  1 
ATOM   7638  C CG  . GLU C 1 102 ? -2.072  46.803  28.021  1.00 34.09  ? 131 GLU C CG  1 
ATOM   7639  C CD  . GLU C 1 102 ? -0.942  47.232  27.115  1.00 32.71  ? 131 GLU C CD  1 
ATOM   7640  O OE1 . GLU C 1 102 ? -0.750  48.455  26.948  1.00 36.38  ? 131 GLU C OE1 1 
ATOM   7641  O OE2 . GLU C 1 102 ? -0.283  46.350  26.585  1.00 39.13  ? 131 GLU C OE2 1 
ATOM   7642  N N   . GLU C 1 103 ? -4.057  49.604  30.950  1.00 28.81  ? 132 GLU C N   1 
ATOM   7643  C CA  . GLU C 1 103 ? -4.680  50.866  31.317  1.00 30.83  ? 132 GLU C CA  1 
ATOM   7644  C C   . GLU C 1 103 ? -4.102  51.379  32.640  1.00 30.09  ? 132 GLU C C   1 
ATOM   7645  O O   . GLU C 1 103 ? -3.901  52.588  32.825  1.00 25.59  ? 132 GLU C O   1 
ATOM   7646  C CB  . GLU C 1 103 ? -6.201  50.676  31.367  1.00 39.74  ? 132 GLU C CB  1 
ATOM   7647  C CG  . GLU C 1 103 ? -6.841  50.414  30.001  1.00 42.53  ? 132 GLU C CG  1 
ATOM   7648  C CD  . GLU C 1 103 ? -6.756  49.008  29.403  1.00 48.27  ? 132 GLU C CD  1 
ATOM   7649  O OE1 . GLU C 1 103 ? -6.289  48.065  30.099  1.00 48.43  ? 132 GLU C OE1 1 
ATOM   7650  O OE2 . GLU C 1 103 ? -7.151  48.846  28.210  1.00 44.15  ? 132 GLU C OE2 1 
ATOM   7651  N N   . GLN C 1 104 ? -3.855  50.447  33.562  1.00 29.09  ? 133 GLN C N   1 
ATOM   7652  C CA  . GLN C 1 104 ? -3.263  50.732  34.872  1.00 27.17  ? 133 GLN C CA  1 
ATOM   7653  C C   . GLN C 1 104 ? -1.903  51.413  34.709  1.00 27.54  ? 133 GLN C C   1 
ATOM   7654  O O   . GLN C 1 104 ? -1.661  52.442  35.337  1.00 27.88  ? 133 GLN C O   1 
ATOM   7655  C CB  . GLN C 1 104 ? -3.194  49.435  35.679  1.00 29.00  ? 133 GLN C CB  1 
ATOM   7656  C CG  . GLN C 1 104 ? -4.587  48.929  36.018  1.00 31.33  ? 133 GLN C CG  1 
ATOM   7657  C CD  . GLN C 1 104 ? -4.619  47.695  36.881  1.00 32.60  ? 133 GLN C CD  1 
ATOM   7658  O OE1 . GLN C 1 104 ? -3.809  46.772  36.743  1.00 34.20  ? 133 GLN C OE1 1 
ATOM   7659  N NE2 . GLN C 1 104 ? -5.598  47.672  37.773  1.00 32.24  ? 133 GLN C NE2 1 
ATOM   7660  N N   . VAL C 1 105 ? -1.059  50.894  33.794  1.00 27.29  ? 134 VAL C N   1 
ATOM   7661  C CA  . VAL C 1 105 ? 0.242   51.487  33.538  1.00 27.92  ? 134 VAL C CA  1 
ATOM   7662  C C   . VAL C 1 105 ? 0.046   52.868  32.916  1.00 27.62  ? 134 VAL C C   1 
ATOM   7663  O O   . VAL C 1 105 ? 0.754   53.808  33.249  1.00 24.72  ? 134 VAL C O   1 
ATOM   7664  C CB  . VAL C 1 105 ? 1.152   50.576  32.683  1.00 29.53  ? 134 VAL C CB  1 
ATOM   7665  C CG1 . VAL C 1 105 ? 2.385   51.314  32.181  1.00 29.83  ? 134 VAL C CG1 1 
ATOM   7666  C CG2 . VAL C 1 105 ? 1.550   49.324  33.446  1.00 26.68  ? 134 VAL C CG2 1 
ATOM   7667  N N   . SER C 1 106 ? -0.918  52.983  32.005  1.00 29.47  ? 135 SER C N   1 
ATOM   7668  C CA  A SER C 1 106 ? -1.213  54.255  31.365  0.50 29.75  ? 135 SER C CA  1 
ATOM   7669  C CA  B SER C 1 106 ? -1.183  54.258  31.364  0.50 29.63  ? 135 SER C CA  1 
ATOM   7670  C C   . SER C 1 106 ? -1.558  55.287  32.428  1.00 28.25  ? 135 SER C C   1 
ATOM   7671  O O   . SER C 1 106 ? -1.011  56.391  32.440  1.00 29.91  ? 135 SER C O   1 
ATOM   7672  C CB  A SER C 1 106 ? -2.332  54.126  30.368  0.50 30.65  ? 135 SER C CB  1 
ATOM   7673  C CB  B SER C 1 106 ? -2.224  54.098  30.285  0.50 30.50  ? 135 SER C CB  1 
ATOM   7674  O OG  A SER C 1 106 ? -2.412  55.294  29.570  0.50 31.26  ? 135 SER C OG  1 
ATOM   7675  O OG  B SER C 1 106 ? -1.795  53.116  29.339  0.50 30.02  ? 135 SER C OG  1 
ATOM   7676  N N   . TRP C 1 107 ? -2.482  54.906  33.313  1.00 29.63  ? 136 TRP C N   1 
ATOM   7677  C CA  . TRP C 1 107 ? -2.869  55.739  34.441  1.00 29.16  ? 136 TRP C CA  1 
ATOM   7678  C C   . TRP C 1 107 ? -1.655  56.197  35.252  1.00 26.60  ? 136 TRP C C   1 
ATOM   7679  O O   . TRP C 1 107 ? -1.525  57.374  35.616  1.00 28.05  ? 136 TRP C O   1 
ATOM   7680  C CB  . TRP C 1 107 ? -3.862  55.002  35.336  1.00 30.86  ? 136 TRP C CB  1 
ATOM   7681  C CG  . TRP C 1 107 ? -4.256  55.857  36.500  1.00 35.14  ? 136 TRP C CG  1 
ATOM   7682  C CD1 . TRP C 1 107 ? -5.127  56.904  36.492  1.00 37.77  ? 136 TRP C CD1 1 
ATOM   7683  C CD2 . TRP C 1 107 ? -3.694  55.814  37.822  1.00 36.22  ? 136 TRP C CD2 1 
ATOM   7684  N NE1 . TRP C 1 107 ? -5.189  57.478  37.733  1.00 37.00  ? 136 TRP C NE1 1 
ATOM   7685  C CE2 . TRP C 1 107 ? -4.314  56.840  38.568  1.00 37.95  ? 136 TRP C CE2 1 
ATOM   7686  C CE3 . TRP C 1 107 ? -2.752  54.992  38.451  1.00 36.23  ? 136 TRP C CE3 1 
ATOM   7687  C CZ2 . TRP C 1 107 ? -4.033  57.050  39.920  1.00 37.61  ? 136 TRP C CZ2 1 
ATOM   7688  C CZ3 . TRP C 1 107 ? -2.460  55.214  39.777  1.00 37.76  ? 136 TRP C CZ3 1 
ATOM   7689  C CH2 . TRP C 1 107 ? -3.099  56.222  40.502  1.00 38.26  ? 136 TRP C CH2 1 
ATOM   7690  N N   . LEU C 1 108 ? -0.749  55.262  35.547  1.00 26.80  ? 137 LEU C N   1 
ATOM   7691  C CA  . LEU C 1 108 ? 0.412   55.586  36.377  1.00 24.09  ? 137 LEU C CA  1 
ATOM   7692  C C   . LEU C 1 108 ? 1.345   56.570  35.677  1.00 24.34  ? 137 LEU C C   1 
ATOM   7693  O O   . LEU C 1 108 ? 1.850   57.499  36.320  1.00 24.80  ? 137 LEU C O   1 
ATOM   7694  C CB  . LEU C 1 108 ? 1.123   54.290  36.750  1.00 24.72  ? 137 LEU C CB  1 
ATOM   7695  C CG  . LEU C 1 108 ? 2.222   54.425  37.804  1.00 24.65  ? 137 LEU C CG  1 
ATOM   7696  C CD1 . LEU C 1 108 ? 1.757   55.288  38.961  1.00 22.92  ? 137 LEU C CD1 1 
ATOM   7697  C CD2 . LEU C 1 108 ? 2.650   53.045  38.305  1.00 23.79  ? 137 LEU C CD2 1 
ATOM   7698  N N   . SER C 1 109 ? 1.519   56.419  34.348  1.00 24.46  ? 138 SER C N   1 
ATOM   7699  C CA  . SER C 1 109 ? 2.320   57.355  33.565  1.00 23.61  ? 138 SER C CA  1 
ATOM   7700  C C   . SER C 1 109 ? 1.778   58.774  33.667  1.00 24.10  ? 138 SER C C   1 
ATOM   7701  O O   . SER C 1 109 ? 2.532   59.720  33.833  1.00 25.01  ? 138 SER C O   1 
ATOM   7702  C CB  . SER C 1 109 ? 2.412   56.945  32.096  1.00 25.19  ? 138 SER C CB  1 
ATOM   7703  O OG  . SER C 1 109 ? 3.175   55.755  31.942  1.00 23.37  ? 138 SER C OG  1 
ATOM   7704  N N   . LYS C 1 110 ? 0.467   58.925  33.520  1.00 28.87  ? 139 LYS C N   1 
ATOM   7705  C CA  . LYS C 1 110 ? -0.162  60.228  33.666  1.00 30.86  ? 139 LYS C CA  1 
ATOM   7706  C C   . LYS C 1 110 ? -0.043  60.713  35.107  1.00 28.02  ? 139 LYS C C   1 
ATOM   7707  O O   . LYS C 1 110 ? 0.083   61.905  35.351  1.00 28.11  ? 139 LYS C O   1 
ATOM   7708  C CB  . LYS C 1 110 ? -1.649  60.150  33.318  1.00 35.51  ? 139 LYS C CB  1 
ATOM   7709  C CG  . LYS C 1 110 ? -1.969  59.918  31.852  1.00 38.51  ? 139 LYS C CG  1 
ATOM   7710  C CD  . LYS C 1 110 ? -3.447  59.697  31.623  1.00 41.52  ? 139 LYS C CD  1 
ATOM   7711  C CE  . LYS C 1 110 ? -3.946  58.413  32.247  1.00 45.71  ? 139 LYS C CE  1 
ATOM   7712  N NZ  . LYS C 1 110 ? -5.178  57.908  31.595  1.00 49.02  ? 139 LYS C NZ  1 
ATOM   7713  N N   . GLU C 1 111 ? -0.188  59.793  36.059  1.00 27.99  ? 140 GLU C N   1 
ATOM   7714  C CA  . GLU C 1 111 ? -0.100  60.157  37.463  1.00 30.39  ? 140 GLU C CA  1 
ATOM   7715  C C   . GLU C 1 111 ? 1.261   60.763  37.772  1.00 26.84  ? 140 GLU C C   1 
ATOM   7716  O O   . GLU C 1 111 ? 1.328   61.800  38.420  1.00 27.96  ? 140 GLU C O   1 
ATOM   7717  C CB  . GLU C 1 111 ? -0.365  58.983  38.406  1.00 30.91  ? 140 GLU C CB  1 
ATOM   7718  C CG  . GLU C 1 111 ? -1.766  58.994  38.981  1.00 36.77  ? 140 GLU C CG  1 
ATOM   7719  C CD  . GLU C 1 111 ? -2.184  60.228  39.772  1.00 40.15  ? 140 GLU C CD  1 
ATOM   7720  O OE1 . GLU C 1 111 ? -1.844  60.352  40.987  1.00 37.78  ? 140 GLU C OE1 1 
ATOM   7721  O OE2 . GLU C 1 111 ? -2.853  61.066  39.175  1.00 40.52  ? 140 GLU C OE2 1 
ATOM   7722  N N   . TRP C 1 112 ? 2.342   60.110  37.331  1.00 29.04  ? 141 TRP C N   1 
ATOM   7723  C CA  . TRP C 1 112 ? 3.672   60.659  37.554  1.00 27.00  ? 141 TRP C CA  1 
ATOM   7724  C C   . TRP C 1 112 ? 3.954   61.905  36.724  1.00 30.77  ? 141 TRP C C   1 
ATOM   7725  O O   . TRP C 1 112 ? 4.872   62.637  37.062  1.00 28.88  ? 141 TRP C O   1 
ATOM   7726  C CB  . TRP C 1 112 ? 4.750   59.608  37.314  1.00 27.09  ? 141 TRP C CB  1 
ATOM   7727  C CG  . TRP C 1 112 ? 4.750   58.539  38.360  1.00 24.94  ? 141 TRP C CG  1 
ATOM   7728  C CD1 . TRP C 1 112 ? 4.141   58.562  39.587  1.00 26.28  ? 141 TRP C CD1 1 
ATOM   7729  C CD2 . TRP C 1 112 ? 5.408   57.273  38.262  1.00 24.23  ? 141 TRP C CD2 1 
ATOM   7730  N NE1 . TRP C 1 112 ? 4.326   57.368  40.225  1.00 25.09  ? 141 TRP C NE1 1 
ATOM   7731  C CE2 . TRP C 1 112 ? 5.120   56.573  39.447  1.00 23.66  ? 141 TRP C CE2 1 
ATOM   7732  C CE3 . TRP C 1 112 ? 6.223   56.679  37.295  1.00 24.54  ? 141 TRP C CE3 1 
ATOM   7733  C CZ2 . TRP C 1 112 ? 5.594   55.288  39.671  1.00 22.35  ? 141 TRP C CZ2 1 
ATOM   7734  C CZ3 . TRP C 1 112 ? 6.718   55.420  37.529  1.00 23.64  ? 141 TRP C CZ3 1 
ATOM   7735  C CH2 . TRP C 1 112 ? 6.405   54.737  38.699  1.00 23.20  ? 141 TRP C CH2 1 
ATOM   7736  N N   . ALA C 1 113 ? 3.199   62.141  35.638  1.00 32.42  ? 142 ALA C N   1 
ATOM   7737  C CA  . ALA C 1 113 ? 3.400   63.328  34.819  1.00 33.83  ? 142 ALA C CA  1 
ATOM   7738  C C   . ALA C 1 113 ? 2.858   64.574  35.521  1.00 33.37  ? 142 ALA C C   1 
ATOM   7739  O O   . ALA C 1 113 ? 3.499   65.622  35.485  1.00 30.59  ? 142 ALA C O   1 
ATOM   7740  C CB  . ALA C 1 113 ? 2.783   63.137  33.452  1.00 37.01  ? 142 ALA C CB  1 
ATOM   7741  N N   . LYS C 1 114 ? 1.713   64.438  36.201  1.00 34.65  ? 143 LYS C N   1 
ATOM   7742  C CA  . LYS C 1 114 ? 1.092   65.552  36.907  1.00 35.75  ? 143 LYS C CA  1 
ATOM   7743  C C   . LYS C 1 114 ? 1.885   65.978  38.133  1.00 32.24  ? 143 LYS C C   1 
ATOM   7744  O O   . LYS C 1 114 ? 1.909   67.156  38.478  1.00 26.73  ? 143 LYS C O   1 
ATOM   7745  C CB  . LYS C 1 114 ? -0.300  65.192  37.430  1.00 38.45  ? 143 LYS C CB  1 
ATOM   7746  C CG  . LYS C 1 114 ? -1.368  65.133  36.359  1.00 44.75  ? 143 LYS C CG  1 
ATOM   7747  C CD  . LYS C 1 114 ? -2.764  64.975  36.913  1.00 47.28  ? 143 LYS C CD  1 
ATOM   7748  C CE  . LYS C 1 114 ? -2.983  63.664  37.633  1.00 44.86  ? 143 LYS C CE  1 
ATOM   7749  N NZ  . LYS C 1 114 ? -4.365  63.170  37.426  1.00 43.40  ? 143 LYS C NZ  1 
ATOM   7750  N N   . ARG C 1 115 ? 2.501   65.006  38.808  1.00 28.52  ? 144 ARG C N   1 
ATOM   7751  C CA  . ARG C 1 115 ? 3.176   65.251  40.064  1.00 28.00  ? 144 ARG C CA  1 
ATOM   7752  C C   . ARG C 1 115 ? 4.599   65.749  39.828  1.00 30.47  ? 144 ARG C C   1 
ATOM   7753  O O   . ARG C 1 115 ? 5.263   66.166  40.774  1.00 29.72  ? 144 ARG C O   1 
ATOM   7754  C CB  . ARG C 1 115 ? 3.216   63.952  40.880  1.00 28.11  ? 144 ARG C CB  1 
ATOM   7755  C CG  . ARG C 1 115 ? 1.856   63.419  41.309  1.00 27.65  ? 144 ARG C CG  1 
ATOM   7756  C CD  . ARG C 1 115 ? 2.014   62.050  41.965  1.00 25.37  ? 144 ARG C CD  1 
ATOM   7757  N NE  . ARG C 1 115 ? 0.724   61.547  42.422  1.00 25.38  ? 144 ARG C NE  1 
ATOM   7758  C CZ  . ARG C 1 115 ? 0.332   61.525  43.687  1.00 25.85  ? 144 ARG C CZ  1 
ATOM   7759  N NH1 . ARG C 1 115 ? 1.110   62.006  44.650  1.00 27.05  ? 144 ARG C NH1 1 
ATOM   7760  N NH2 . ARG C 1 115 ? -0.837  60.997  43.982  1.00 23.02  ? 144 ARG C NH2 1 
ATOM   7761  N N   . ALA C 1 116 ? 5.077   65.708  38.572  1.00 31.57  ? 145 ALA C N   1 
ATOM   7762  C CA  . ALA C 1 116 ? 6.467   66.012  38.293  1.00 33.96  ? 145 ALA C CA  1 
ATOM   7763  C C   . ALA C 1 116 ? 6.655   67.523  38.307  1.00 38.33  ? 145 ALA C C   1 
ATOM   7764  O O   . ALA C 1 116 ? 6.379   68.206  37.324  1.00 44.35  ? 145 ALA C O   1 
ATOM   7765  C CB  . ALA C 1 116 ? 6.901   65.422  36.977  1.00 32.11  ? 145 ALA C CB  1 
ATOM   7766  N N   . ALA C 1 117 ? 7.126   68.034  39.441  1.00 39.70  ? 146 ALA C N   1 
ATOM   7767  C CA  . ALA C 1 117 ? 7.528   69.421  39.529  1.00 39.06  ? 146 ALA C CA  1 
ATOM   7768  C C   . ALA C 1 117 ? 8.453   69.659  40.725  1.00 34.38  ? 146 ALA C C   1 
ATOM   7769  O O   . ALA C 1 117 ? 8.318   69.002  41.754  1.00 34.03  ? 146 ALA C O   1 
ATOM   7770  C CB  . ALA C 1 117 ? 6.294   70.236  39.644  1.00 36.10  ? 146 ALA C CB  1 
ATOM   7771  N N   . LEU C 1 118 ? 9.347   70.645  40.573  1.00 31.14  ? 147 LEU C N   1 
ATOM   7772  C CA  . LEU C 1 118 ? 10.326  71.026  41.580  1.00 30.79  ? 147 LEU C CA  1 
ATOM   7773  C C   . LEU C 1 118 ? 10.012  72.403  42.164  1.00 32.02  ? 147 LEU C C   1 
ATOM   7774  O O   . LEU C 1 118 ? 9.684   73.321  41.428  1.00 33.09  ? 147 LEU C O   1 
ATOM   7775  C CB  . LEU C 1 118 ? 11.699  71.079  40.913  1.00 29.37  ? 147 LEU C CB  1 
ATOM   7776  C CG  . LEU C 1 118 ? 12.193  69.754  40.343  1.00 32.08  ? 147 LEU C CG  1 
ATOM   7777  C CD1 . LEU C 1 118 ? 13.628  69.887  39.875  1.00 32.60  ? 147 LEU C CD1 1 
ATOM   7778  C CD2 . LEU C 1 118 ? 12.058  68.646  41.383  1.00 30.58  ? 147 LEU C CD2 1 
ATOM   7779  N N   . PRO C 1 119 ? 10.152  72.605  43.493  1.00 33.25  ? 148 PRO C N   1 
ATOM   7780  C CA  . PRO C 1 119 ? 10.074  73.947  44.065  1.00 31.32  ? 148 PRO C CA  1 
ATOM   7781  C C   . PRO C 1 119 ? 11.254  74.790  43.590  1.00 29.77  ? 148 PRO C C   1 
ATOM   7782  O O   . PRO C 1 119 ? 12.328  74.262  43.337  1.00 27.35  ? 148 PRO C O   1 
ATOM   7783  C CB  . PRO C 1 119 ? 10.085  73.717  45.583  1.00 31.17  ? 148 PRO C CB  1 
ATOM   7784  C CG  . PRO C 1 119 ? 10.645  72.320  45.774  1.00 32.49  ? 148 PRO C CG  1 
ATOM   7785  C CD  . PRO C 1 119 ? 10.370  71.558  44.498  1.00 30.76  ? 148 PRO C CD  1 
ATOM   7786  N N   . SER C 1 120 ? 11.062  76.108  43.494  1.00 30.77  ? 149 SER C N   1 
ATOM   7787  C CA  . SER C 1 120 ? 12.131  77.008  43.100  1.00 30.38  ? 149 SER C CA  1 
ATOM   7788  C C   . SER C 1 120 ? 13.400  76.784  43.930  1.00 28.01  ? 149 SER C C   1 
ATOM   7789  O O   . SER C 1 120 ? 14.517  76.854  43.389  1.00 25.07  ? 149 SER C O   1 
ATOM   7790  C CB  . SER C 1 120 ? 11.680  78.433  43.211  1.00 32.23  ? 149 SER C CB  1 
ATOM   7791  O OG  . SER C 1 120 ? 11.427  78.769  44.565  1.00 38.65  ? 149 SER C OG  1 
ATOM   7792  N N   . HIS C 1 121 ? 13.236  76.540  45.252  1.00 22.91  ? 150 HIS C N   1 
ATOM   7793  C CA  . HIS C 1 121 ? 14.382  76.562  46.140  1.00 21.91  ? 150 HIS C CA  1 
ATOM   7794  C C   . HIS C 1 121 ? 15.361  75.455  45.752  1.00 22.69  ? 150 HIS C C   1 
ATOM   7795  O O   . HIS C 1 121 ? 16.568  75.658  45.809  1.00 23.10  ? 150 HIS C O   1 
ATOM   7796  C CB  . HIS C 1 121 ? 13.973  76.549  47.620  1.00 23.69  ? 150 HIS C CB  1 
ATOM   7797  C CG  . HIS C 1 121 ? 13.618  75.192  48.160  1.00 24.06  ? 150 HIS C CG  1 
ATOM   7798  N ND1 . HIS C 1 121 ? 12.337  74.704  48.078  1.00 25.52  ? 150 HIS C ND1 1 
ATOM   7799  C CD2 . HIS C 1 121 ? 14.313  74.281  48.849  1.00 25.81  ? 150 HIS C CD2 1 
ATOM   7800  C CE1 . HIS C 1 121 ? 12.281  73.514  48.664  1.00 26.22  ? 150 HIS C CE1 1 
ATOM   7801  N NE2 . HIS C 1 121 ? 13.475  73.219  49.122  1.00 24.90  ? 150 HIS C NE2 1 
ATOM   7802  N N   . VAL C 1 122 ? 14.839  74.302  45.325  1.00 25.89  ? 151 VAL C N   1 
ATOM   7803  C CA  . VAL C 1 122 ? 15.665  73.177  44.902  1.00 25.92  ? 151 VAL C CA  1 
ATOM   7804  C C   . VAL C 1 122 ? 16.299  73.442  43.531  1.00 26.74  ? 151 VAL C C   1 
ATOM   7805  O O   . VAL C 1 122 ? 17.433  73.029  43.270  1.00 25.83  ? 151 VAL C O   1 
ATOM   7806  C CB  . VAL C 1 122 ? 14.831  71.876  44.942  1.00 26.71  ? 151 VAL C CB  1 
ATOM   7807  C CG1 . VAL C 1 122 ? 15.567  70.674  44.352  1.00 25.66  ? 151 VAL C CG1 1 
ATOM   7808  C CG2 . VAL C 1 122 ? 14.369  71.566  46.359  1.00 27.14  ? 151 VAL C CG2 1 
ATOM   7809  N N   . VAL C 1 123 ? 15.592  74.156  42.646  1.00 27.66  ? 152 VAL C N   1 
ATOM   7810  C CA  . VAL C 1 123 ? 16.164  74.533  41.361  1.00 26.32  ? 152 VAL C CA  1 
ATOM   7811  C C   . VAL C 1 123 ? 17.327  75.506  41.568  1.00 25.83  ? 152 VAL C C   1 
ATOM   7812  O O   . VAL C 1 123 ? 18.346  75.360  40.904  1.00 22.09  ? 152 VAL C O   1 
ATOM   7813  C CB  . VAL C 1 123 ? 15.094  75.068  40.385  1.00 28.09  ? 152 VAL C CB  1 
ATOM   7814  C CG1 . VAL C 1 123 ? 15.670  75.928  39.259  1.00 25.19  ? 152 VAL C CG1 1 
ATOM   7815  C CG2 . VAL C 1 123 ? 14.291  73.904  39.814  1.00 27.17  ? 152 VAL C CG2 1 
ATOM   7816  N N   . THR C 1 124 ? 17.170  76.512  42.444  1.00 26.80  ? 153 THR C N   1 
ATOM   7817  C CA  . THR C 1 124 ? 18.262  77.423  42.739  1.00 30.54  ? 153 THR C CA  1 
ATOM   7818  C C   . THR C 1 124 ? 19.469  76.655  43.264  1.00 31.44  ? 153 THR C C   1 
ATOM   7819  O O   . THR C 1 124 ? 20.600  76.889  42.844  1.00 33.12  ? 153 THR C O   1 
ATOM   7820  C CB  . THR C 1 124 ? 17.812  78.496  43.731  1.00 31.34  ? 153 THR C CB  1 
ATOM   7821  O OG1 . THR C 1 124 ? 16.708  79.123  43.090  1.00 29.57  ? 153 THR C OG1 1 
ATOM   7822  C CG2 . THR C 1 124 ? 18.882  79.504  44.080  1.00 32.94  ? 153 THR C CG2 1 
ATOM   7823  N N   . MET C 1 125 ? 19.213  75.725  44.191  1.00 31.27  ? 154 MET C N   1 
ATOM   7824  C CA  . MET C 1 125 ? 20.270  74.926  44.781  1.00 31.90  ? 154 MET C CA  1 
ATOM   7825  C C   . MET C 1 125 ? 21.092  74.222  43.702  1.00 29.36  ? 154 MET C C   1 
ATOM   7826  O O   . MET C 1 125 ? 22.319  74.310  43.733  1.00 30.40  ? 154 MET C O   1 
ATOM   7827  C CB  . MET C 1 125 ? 19.699  73.879  45.741  1.00 32.96  ? 154 MET C CB  1 
ATOM   7828  C CG  . MET C 1 125 ? 20.613  73.590  46.904  1.00 32.56  ? 154 MET C CG  1 
ATOM   7829  S SD  . MET C 1 125 ? 20.207  72.010  47.690  1.00 37.60  ? 154 MET C SD  1 
ATOM   7830  C CE  . MET C 1 125 ? 18.438  71.957  47.425  1.00 31.23  ? 154 MET C CE  1 
ATOM   7831  N N   . LEU C 1 126 ? 20.420  73.560  42.753  1.00 25.80  ? 155 LEU C N   1 
ATOM   7832  C CA  . LEU C 1 126 ? 21.085  72.766  41.727  1.00 26.25  ? 155 LEU C CA  1 
ATOM   7833  C C   . LEU C 1 126 ? 21.834  73.662  40.756  1.00 29.20  ? 155 LEU C C   1 
ATOM   7834  O O   . LEU C 1 126 ? 22.934  73.333  40.318  1.00 30.82  ? 155 LEU C O   1 
ATOM   7835  C CB  . LEU C 1 126 ? 20.044  71.928  40.989  1.00 27.80  ? 155 LEU C CB  1 
ATOM   7836  C CG  . LEU C 1 126 ? 19.487  70.771  41.808  1.00 29.00  ? 155 LEU C CG  1 
ATOM   7837  C CD1 . LEU C 1 126 ? 18.159  70.296  41.256  1.00 28.46  ? 155 LEU C CD1 1 
ATOM   7838  C CD2 . LEU C 1 126 ? 20.529  69.661  41.886  1.00 28.31  ? 155 LEU C CD2 1 
ATOM   7839  N N   . ASP C 1 127 ? 21.214  74.801  40.435  1.00 28.56  ? 156 ASP C N   1 
ATOM   7840  C CA  . ASP C 1 127 ? 21.792  75.748  39.498  1.00 31.32  ? 156 ASP C CA  1 
ATOM   7841  C C   . ASP C 1 127 ? 23.000  76.454  40.126  1.00 29.78  ? 156 ASP C C   1 
ATOM   7842  O O   . ASP C 1 127 ? 23.846  77.002  39.423  1.00 30.91  ? 156 ASP C O   1 
ATOM   7843  C CB  . ASP C 1 127 ? 20.715  76.723  39.025  1.00 32.36  ? 156 ASP C CB  1 
ATOM   7844  C CG  . ASP C 1 127 ? 19.650  76.119  38.118  1.00 34.96  ? 156 ASP C CG  1 
ATOM   7845  O OD1 . ASP C 1 127 ? 19.738  74.918  37.786  1.00 35.54  ? 156 ASP C OD1 1 
ATOM   7846  O OD2 . ASP C 1 127 ? 18.719  76.860  37.747  1.00 39.03  ? 156 ASP C OD2 1 
ATOM   7847  N N   . ASN C 1 128 ? 23.078  76.476  41.458  1.00 31.93  ? 157 ASN C N   1 
ATOM   7848  C CA  . ASN C 1 128 ? 24.196  77.110  42.136  1.00 32.56  ? 157 ASN C CA  1 
ATOM   7849  C C   . ASN C 1 128 ? 25.313  76.121  42.437  1.00 33.45  ? 157 ASN C C   1 
ATOM   7850  O O   . ASN C 1 128 ? 26.407  76.551  42.787  1.00 34.27  ? 157 ASN C O   1 
ATOM   7851  C CB  . ASN C 1 128 ? 23.745  77.825  43.406  1.00 34.05  ? 157 ASN C CB  1 
ATOM   7852  C CG  . ASN C 1 128 ? 23.126  79.176  43.108  1.00 35.40  ? 157 ASN C CG  1 
ATOM   7853  O OD1 . ASN C 1 128 ? 23.702  79.962  42.359  1.00 33.26  ? 157 ASN C OD1 1 
ATOM   7854  N ND2 . ASN C 1 128 ? 21.953  79.446  43.664  1.00 33.00  ? 157 ASN C ND2 1 
ATOM   7855  N N   . PHE C 1 129 ? 25.067  74.814  42.281  1.00 30.89  ? 158 PHE C N   1 
ATOM   7856  C CA  . PHE C 1 129 ? 26.100  73.836  42.583  1.00 32.66  ? 158 PHE C CA  1 
ATOM   7857  C C   . PHE C 1 129 ? 27.305  74.053  41.663  1.00 33.23  ? 158 PHE C C   1 
ATOM   7858  O O   . PHE C 1 129 ? 27.154  74.437  40.508  1.00 34.59  ? 158 PHE C O   1 
ATOM   7859  C CB  . PHE C 1 129 ? 25.573  72.402  42.469  1.00 28.85  ? 158 PHE C CB  1 
ATOM   7860  C CG  . PHE C 1 129 ? 24.748  71.887  43.626  1.00 33.59  ? 158 PHE C CG  1 
ATOM   7861  C CD1 . PHE C 1 129 ? 25.062  72.213  44.941  1.00 34.13  ? 158 PHE C CD1 1 
ATOM   7862  C CD2 . PHE C 1 129 ? 23.709  70.988  43.401  1.00 31.73  ? 158 PHE C CD2 1 
ATOM   7863  C CE1 . PHE C 1 129 ? 24.309  71.710  45.991  1.00 32.58  ? 158 PHE C CE1 1 
ATOM   7864  C CE2 . PHE C 1 129 ? 22.973  70.469  44.456  1.00 33.12  ? 158 PHE C CE2 1 
ATOM   7865  C CZ  . PHE C 1 129 ? 23.261  70.851  45.745  1.00 32.87  ? 158 PHE C CZ  1 
ATOM   7866  N N   . PRO C 1 130 ? 28.542  73.796  42.135  1.00 38.30  ? 159 PRO C N   1 
ATOM   7867  C CA  . PRO C 1 130 ? 29.724  73.863  41.277  1.00 36.54  ? 159 PRO C CA  1 
ATOM   7868  C C   . PRO C 1 130 ? 29.982  72.563  40.509  1.00 33.13  ? 159 PRO C C   1 
ATOM   7869  O O   . PRO C 1 130 ? 29.494  71.500  40.868  1.00 30.14  ? 159 PRO C O   1 
ATOM   7870  C CB  . PRO C 1 130 ? 30.805  74.165  42.329  1.00 38.28  ? 159 PRO C CB  1 
ATOM   7871  C CG  . PRO C 1 130 ? 30.378  73.342  43.529  1.00 39.26  ? 159 PRO C CG  1 
ATOM   7872  C CD  . PRO C 1 130 ? 28.864  73.413  43.521  1.00 40.97  ? 159 PRO C CD  1 
ATOM   7873  N N   . THR C 1 131 ? 30.794  72.636  39.453  1.00 34.06  ? 160 THR C N   1 
ATOM   7874  C CA  . THR C 1 131 ? 30.943  71.510  38.544  1.00 38.24  ? 160 THR C CA  1 
ATOM   7875  C C   . THR C 1 131 ? 31.748  70.378  39.181  1.00 34.96  ? 160 THR C C   1 
ATOM   7876  O O   . THR C 1 131 ? 31.742  69.271  38.656  1.00 36.03  ? 160 THR C O   1 
ATOM   7877  C CB  . THR C 1 131 ? 31.592  71.935  37.224  1.00 39.89  ? 160 THR C CB  1 
ATOM   7878  O OG1 . THR C 1 131 ? 32.557  72.916  37.591  1.00 43.14  ? 160 THR C OG1 1 
ATOM   7879  C CG2 . THR C 1 131 ? 30.611  72.492  36.214  1.00 41.65  ? 160 THR C CG2 1 
ATOM   7880  N N   . ASN C 1 132 ? 32.411  70.646  40.312  1.00 35.08  ? 161 ASN C N   1 
ATOM   7881  C CA  . ASN C 1 132 ? 33.237  69.651  40.983  1.00 36.14  ? 161 ASN C CA  1 
ATOM   7882  C C   . ASN C 1 132 ? 32.466  68.984  42.114  1.00 34.24  ? 161 ASN C C   1 
ATOM   7883  O O   . ASN C 1 132 ? 33.046  68.265  42.924  1.00 35.19  ? 161 ASN C O   1 
ATOM   7884  C CB  . ASN C 1 132 ? 34.534  70.236  41.548  1.00 36.43  ? 161 ASN C CB  1 
ATOM   7885  C CG  . ASN C 1 132 ? 34.364  71.018  42.836  1.00 36.26  ? 161 ASN C CG  1 
ATOM   7886  O OD1 . ASN C 1 132 ? 35.129  70.843  43.786  1.00 41.67  ? 161 ASN C OD1 1 
ATOM   7887  N ND2 . ASN C 1 132 ? 33.416  71.936  42.861  1.00 34.85  ? 161 ASN C ND2 1 
ATOM   7888  N N   . LEU C 1 133 ? 31.160  69.239  42.202  1.00 30.55  ? 162 LEU C N   1 
ATOM   7889  C CA  . LEU C 1 133 ? 30.375  68.501  43.169  1.00 26.97  ? 162 LEU C CA  1 
ATOM   7890  C C   . LEU C 1 133 ? 29.763  67.326  42.426  1.00 25.21  ? 162 LEU C C   1 
ATOM   7891  O O   . LEU C 1 133 ? 29.005  67.508  41.479  1.00 22.38  ? 162 LEU C O   1 
ATOM   7892  C CB  . LEU C 1 133 ? 29.333  69.424  43.808  1.00 26.12  ? 162 LEU C CB  1 
ATOM   7893  C CG  . LEU C 1 133 ? 28.404  68.762  44.822  1.00 26.07  ? 162 LEU C CG  1 
ATOM   7894  C CD1 . LEU C 1 133 ? 29.190  68.167  45.974  1.00 25.96  ? 162 LEU C CD1 1 
ATOM   7895  C CD2 . LEU C 1 133 ? 27.385  69.775  45.323  1.00 25.99  ? 162 LEU C CD2 1 
ATOM   7896  N N   . HIS C 1 134 ? 30.122  66.117  42.858  1.00 25.01  ? 163 HIS C N   1 
ATOM   7897  C CA  . HIS C 1 134 ? 29.769  64.897  42.160  1.00 25.03  ? 163 HIS C CA  1 
ATOM   7898  C C   . HIS C 1 134 ? 28.255  64.821  41.954  1.00 24.84  ? 163 HIS C C   1 
ATOM   7899  O O   . HIS C 1 134 ? 27.510  65.274  42.824  1.00 24.46  ? 163 HIS C O   1 
ATOM   7900  C CB  . HIS C 1 134 ? 30.292  63.723  42.976  1.00 25.14  ? 163 HIS C CB  1 
ATOM   7901  C CG  . HIS C 1 134 ? 30.186  62.394  42.332  1.00 24.38  ? 163 HIS C CG  1 
ATOM   7902  N ND1 . HIS C 1 134 ? 29.004  61.701  42.242  1.00 25.22  ? 163 HIS C ND1 1 
ATOM   7903  C CD2 . HIS C 1 134 ? 31.138  61.570  41.871  1.00 26.94  ? 163 HIS C CD2 1 
ATOM   7904  C CE1 . HIS C 1 134 ? 29.224  60.542  41.653  1.00 26.56  ? 163 HIS C CE1 1 
ATOM   7905  N NE2 . HIS C 1 134 ? 30.522  60.424  41.440  1.00 27.43  ? 163 HIS C NE2 1 
ATOM   7906  N N   . PRO C 1 135 ? 27.758  64.254  40.829  1.00 21.49  ? 164 PRO C N   1 
ATOM   7907  C CA  . PRO C 1 135 ? 26.312  64.203  40.585  1.00 21.13  ? 164 PRO C CA  1 
ATOM   7908  C C   . PRO C 1 135 ? 25.490  63.498  41.671  1.00 20.21  ? 164 PRO C C   1 
ATOM   7909  O O   . PRO C 1 135 ? 24.380  63.900  41.949  1.00 18.87  ? 164 PRO C O   1 
ATOM   7910  C CB  . PRO C 1 135 ? 26.144  63.513  39.218  1.00 21.28  ? 164 PRO C CB  1 
ATOM   7911  C CG  . PRO C 1 135 ? 27.518  63.565  38.568  1.00 23.62  ? 164 PRO C CG  1 
ATOM   7912  C CD  . PRO C 1 135 ? 28.539  63.760  39.679  1.00 23.57  ? 164 PRO C CD  1 
ATOM   7913  N N   . MET C 1 136 ? 26.015  62.428  42.271  1.00 20.41  ? 165 MET C N   1 
ATOM   7914  C CA  . MET C 1 136 ? 25.313  61.719  43.329  1.00 21.86  ? 165 MET C CA  1 
ATOM   7915  C C   . MET C 1 136 ? 25.140  62.603  44.555  1.00 20.37  ? 165 MET C C   1 
ATOM   7916  O O   . MET C 1 136 ? 24.174  62.433  45.275  1.00 24.19  ? 165 MET C O   1 
ATOM   7917  C CB  . MET C 1 136 ? 26.039  60.430  43.739  1.00 20.93  ? 165 MET C CB  1 
ATOM   7918  C CG  . MET C 1 136 ? 25.822  59.295  42.782  1.00 20.67  ? 165 MET C CG  1 
ATOM   7919  S SD  . MET C 1 136 ? 24.075  58.911  42.521  1.00 21.26  ? 165 MET C SD  1 
ATOM   7920  C CE  . MET C 1 136 ? 23.641  58.195  44.107  1.00 22.33  ? 165 MET C CE  1 
ATOM   7921  N N   . SER C 1 137 ? 26.090  63.506  44.810  1.00 20.88  ? 166 SER C N   1 
ATOM   7922  C CA  . SER C 1 137 ? 26.023  64.441  45.928  1.00 20.82  ? 166 SER C CA  1 
ATOM   7923  C C   . SER C 1 137 ? 24.957  65.498  45.636  1.00 21.14  ? 166 SER C C   1 
ATOM   7924  O O   . SER C 1 137 ? 24.158  65.831  46.514  1.00 20.42  ? 166 SER C O   1 
ATOM   7925  C CB  . SER C 1 137 ? 27.355  65.097  46.206  1.00 20.86  ? 166 SER C CB  1 
ATOM   7926  O OG  . SER C 1 137 ? 28.377  64.150  46.529  1.00 20.08  ? 166 SER C OG  1 
ATOM   7927  N N   . GLN C 1 138 ? 24.927  65.978  44.390  1.00 20.25  ? 167 GLN C N   1 
ATOM   7928  C CA  . GLN C 1 138 ? 23.889  66.932  43.971  1.00 20.41  ? 167 GLN C CA  1 
ATOM   7929  C C   . GLN C 1 138 ? 22.517  66.278  44.078  1.00 19.23  ? 167 GLN C C   1 
ATOM   7930  O O   . GLN C 1 138 ? 21.521  66.927  44.353  1.00 21.37  ? 167 GLN C O   1 
ATOM   7931  C CB  . GLN C 1 138 ? 24.057  67.428  42.532  1.00 20.66  ? 167 GLN C CB  1 
ATOM   7932  C CG  . GLN C 1 138 ? 25.460  67.963  42.218  1.00 23.00  ? 167 GLN C CG  1 
ATOM   7933  C CD  . GLN C 1 138 ? 25.467  68.868  41.004  1.00 25.24  ? 167 GLN C CD  1 
ATOM   7934  O OE1 . GLN C 1 138 ? 24.418  69.333  40.550  1.00 26.55  ? 167 GLN C OE1 1 
ATOM   7935  N NE2 . GLN C 1 138 ? 26.660  69.182  40.512  1.00 24.31  ? 167 GLN C NE2 1 
ATOM   7936  N N   . LEU C 1 139 ? 22.454  64.983  43.812  1.00 17.23  ? 168 LEU C N   1 
ATOM   7937  C CA  . LEU C 1 139 ? 21.175  64.313  43.823  1.00 18.07  ? 168 LEU C CA  1 
ATOM   7938  C C   . LEU C 1 139 ? 20.661  64.182  45.258  1.00 18.41  ? 168 LEU C C   1 
ATOM   7939  O O   . LEU C 1 139 ? 19.487  64.455  45.522  1.00 18.03  ? 168 LEU C O   1 
ATOM   7940  C CB  . LEU C 1 139 ? 21.332  62.956  43.156  1.00 17.89  ? 168 LEU C CB  1 
ATOM   7941  C CG  . LEU C 1 139 ? 20.117  62.055  43.278  1.00 19.90  ? 168 LEU C CG  1 
ATOM   7942  C CD1 . LEU C 1 139 ? 18.941  62.676  42.530  1.00 21.15  ? 168 LEU C CD1 1 
ATOM   7943  C CD2 . LEU C 1 139 ? 20.449  60.642  42.784  1.00 21.43  ? 168 LEU C CD2 1 
ATOM   7944  N N   . SER C 1 140 ? 21.493  63.613  46.127  1.00 16.92  ? 169 SER C N   1 
ATOM   7945  C CA  . SER C 1 140 ? 21.170  63.438  47.542  1.00 17.98  ? 169 SER C CA  1 
ATOM   7946  C C   . SER C 1 140 ? 20.765  64.757  48.193  1.00 18.35  ? 169 SER C C   1 
ATOM   7947  O O   . SER C 1 140 ? 19.692  64.844  48.766  1.00 21.54  ? 169 SER C O   1 
ATOM   7948  C CB  . SER C 1 140 ? 22.327  62.796  48.287  1.00 19.98  ? 169 SER C CB  1 
ATOM   7949  O OG  . SER C 1 140 ? 22.040  62.617  49.683  1.00 24.35  ? 169 SER C OG  1 
ATOM   7950  N N   . ALA C 1 141 ? 21.611  65.783  48.061  1.00 18.17  ? 170 ALA C N   1 
ATOM   7951  C CA  . ALA C 1 141 ? 21.281  67.110  48.580  1.00 19.51  ? 170 ALA C CA  1 
ATOM   7952  C C   . ALA C 1 141 ? 19.923  67.640  48.081  1.00 20.28  ? 170 ALA C C   1 
ATOM   7953  O O   . ALA C 1 141 ? 19.125  68.134  48.893  1.00 18.94  ? 170 ALA C O   1 
ATOM   7954  C CB  . ALA C 1 141 ? 22.402  68.063  48.267  1.00 20.34  ? 170 ALA C CB  1 
ATOM   7955  N N   . ALA C 1 142 ? 19.639  67.534  46.772  1.00 20.05  ? 171 ALA C N   1 
ATOM   7956  C CA  . ALA C 1 142 ? 18.376  68.026  46.212  1.00 20.04  ? 171 ALA C CA  1 
ATOM   7957  C C   . ALA C 1 142 ? 17.182  67.262  46.776  1.00 19.51  ? 171 ALA C C   1 
ATOM   7958  O O   . ALA C 1 142 ? 16.220  67.854  47.235  1.00 19.28  ? 171 ALA C O   1 
ATOM   7959  C CB  . ALA C 1 142 ? 18.387  67.998  44.706  1.00 20.87  ? 171 ALA C CB  1 
ATOM   7960  N N   . VAL C 1 143 ? 17.278  65.933  46.852  1.00 18.47  ? 172 VAL C N   1 
ATOM   7961  C CA  . VAL C 1 143 ? 16.198  65.151  47.417  1.00 18.46  ? 172 VAL C CA  1 
ATOM   7962  C C   . VAL C 1 143 ? 15.951  65.478  48.898  1.00 18.71  ? 172 VAL C C   1 
ATOM   7963  O O   . VAL C 1 143 ? 14.816  65.495  49.338  1.00 19.50  ? 172 VAL C O   1 
ATOM   7964  C CB  . VAL C 1 143 ? 16.491  63.659  47.201  1.00 18.01  ? 172 VAL C CB  1 
ATOM   7965  C CG1 . VAL C 1 143 ? 15.471  62.794  47.909  1.00 19.93  ? 172 VAL C CG1 1 
ATOM   7966  C CG2 . VAL C 1 143 ? 16.534  63.340  45.712  1.00 20.25  ? 172 VAL C CG2 1 
ATOM   7967  N N   . THR C 1 144 ? 17.012  65.738  49.662  1.00 18.20  ? 173 THR C N   1 
ATOM   7968  C CA  . THR C 1 144 ? 16.899  66.080  51.077  1.00 18.93  ? 173 THR C CA  1 
ATOM   7969  C C   . THR C 1 144 ? 16.184  67.424  51.216  1.00 19.20  ? 173 THR C C   1 
ATOM   7970  O O   . THR C 1 144 ? 15.343  67.596  52.075  1.00 21.43  ? 173 THR C O   1 
ATOM   7971  C CB  . THR C 1 144 ? 18.288  66.218  51.739  1.00 19.08  ? 173 THR C CB  1 
ATOM   7972  O OG1 . THR C 1 144 ? 18.941  64.938  51.758  1.00 18.61  ? 173 THR C OG1 1 
ATOM   7973  C CG2 . THR C 1 144 ? 18.235  66.726  53.163  1.00 19.41  ? 173 THR C CG2 1 
ATOM   7974  N N   . ALA C 1 145 ? 16.528  68.369  50.342  1.00 20.65  ? 174 ALA C N   1 
ATOM   7975  C CA  . ALA C 1 145 ? 15.910  69.690  50.391  1.00 21.97  ? 174 ALA C CA  1 
ATOM   7976  C C   . ALA C 1 145 ? 14.484  69.663  49.828  1.00 21.34  ? 174 ALA C C   1 
ATOM   7977  O O   . ALA C 1 145 ? 13.738  70.640  50.015  1.00 23.01  ? 174 ALA C O   1 
ATOM   7978  C CB  . ALA C 1 145 ? 16.775  70.680  49.666  1.00 22.11  ? 174 ALA C CB  1 
ATOM   7979  N N   . LEU C 1 146 ? 14.101  68.573  49.147  1.00 20.45  ? 175 LEU C N   1 
ATOM   7980  C CA  . LEU C 1 146 ? 12.720  68.396  48.709  1.00 22.40  ? 175 LEU C CA  1 
ATOM   7981  C C   . LEU C 1 146 ? 11.795  68.037  49.882  1.00 21.91  ? 175 LEU C C   1 
ATOM   7982  O O   . LEU C 1 146 ? 10.569  68.057  49.728  1.00 23.79  ? 175 LEU C O   1 
ATOM   7983  C CB  . LEU C 1 146 ? 12.613  67.325  47.604  1.00 20.40  ? 175 LEU C CB  1 
ATOM   7984  C CG  . LEU C 1 146 ? 13.047  67.682  46.179  1.00 24.62  ? 175 LEU C CG  1 
ATOM   7985  C CD1 . LEU C 1 146 ? 12.972  66.457  45.276  1.00 22.75  ? 175 LEU C CD1 1 
ATOM   7986  C CD2 . LEU C 1 146 ? 12.187  68.782  45.601  1.00 24.17  ? 175 LEU C CD2 1 
ATOM   7987  N N   . ASN C 1 147 ? 12.348  67.683  51.053  1.00 20.75  ? 176 ASN C N   1 
ATOM   7988  C CA  . ASN C 1 147 ? 11.538  67.188  52.157  1.00 19.79  ? 176 ASN C CA  1 
ATOM   7989  C C   . ASN C 1 147 ? 10.705  68.330  52.736  1.00 19.72  ? 176 ASN C C   1 
ATOM   7990  O O   . ASN C 1 147 ? 9.814   68.089  53.530  1.00 21.34  ? 176 ASN C O   1 
ATOM   7991  C CB  . ASN C 1 147 ? 12.377  66.454  53.213  1.00 22.05  ? 176 ASN C CB  1 
ATOM   7992  C CG  . ASN C 1 147 ? 12.511  67.202  54.523  1.00 23.29  ? 176 ASN C CG  1 
ATOM   7993  O OD1 . ASN C 1 147 ? 12.980  68.334  54.556  1.00 24.68  ? 176 ASN C OD1 1 
ATOM   7994  N ND2 . ASN C 1 147 ? 12.060  66.595  55.601  1.00 20.52  ? 176 ASN C ND2 1 
ATOM   7995  N N   . SER C 1 148 ? 10.994  69.565  52.303  1.00 19.91  ? 177 SER C N   1 
ATOM   7996  C CA  . SER C 1 148 ? 10.114  70.684  52.586  1.00 22.62  ? 177 SER C CA  1 
ATOM   7997  C C   . SER C 1 148 ? 8.726   70.449  51.981  1.00 25.26  ? 177 SER C C   1 
ATOM   7998  O O   . SER C 1 148 ? 7.770   71.116  52.358  1.00 27.79  ? 177 SER C O   1 
ATOM   7999  C CB  . SER C 1 148 ? 10.722  71.963  52.097  1.00 23.49  ? 177 SER C CB  1 
ATOM   8000  O OG  . SER C 1 148 ? 10.784  72.015  50.679  1.00 23.34  ? 177 SER C OG  1 
ATOM   8001  N N   . GLU C 1 149 ? 8.615   69.509  51.039  1.00 23.35  ? 178 GLU C N   1 
ATOM   8002  C CA  . GLU C 1 149 ? 7.352   69.188  50.398  1.00 26.02  ? 178 GLU C CA  1 
ATOM   8003  C C   . GLU C 1 149 ? 6.711   67.948  50.993  1.00 27.01  ? 178 GLU C C   1 
ATOM   8004  O O   . GLU C 1 149 ? 5.682   67.505  50.476  1.00 30.78  ? 178 GLU C O   1 
ATOM   8005  C CB  . GLU C 1 149 ? 7.553   68.903  48.904  1.00 28.52  ? 178 GLU C CB  1 
ATOM   8006  C CG  . GLU C 1 149 ? 8.374   69.954  48.192  1.00 31.14  ? 178 GLU C CG  1 
ATOM   8007  C CD  . GLU C 1 149 ? 7.740   71.334  48.149  1.00 35.92  ? 178 GLU C CD  1 
ATOM   8008  O OE1 . GLU C 1 149 ? 6.601   71.442  47.630  1.00 37.69  ? 178 GLU C OE1 1 
ATOM   8009  O OE2 . GLU C 1 149 ? 8.389   72.295  48.625  1.00 36.11  ? 178 GLU C OE2 1 
ATOM   8010  N N   . SER C 1 150 ? 7.300   67.367  52.052  1.00 25.94  ? 179 SER C N   1 
ATOM   8011  C CA  . SER C 1 150 ? 6.792   66.094  52.532  1.00 26.67  ? 179 SER C CA  1 
ATOM   8012  C C   . SER C 1 150 ? 5.448   66.275  53.245  1.00 27.92  ? 179 SER C C   1 
ATOM   8013  O O   . SER C 1 150 ? 5.380   66.928  54.296  1.00 25.23  ? 179 SER C O   1 
ATOM   8014  C CB  . SER C 1 150 ? 7.786   65.396  53.420  1.00 28.66  ? 179 SER C CB  1 
ATOM   8015  O OG  . SER C 1 150 ? 7.160   64.337  54.120  1.00 26.84  ? 179 SER C OG  1 
ATOM   8016  N N   . ASN C 1 151 ? 4.406   65.649  52.671  1.00 28.39  ? 180 ASN C N   1 
ATOM   8017  C CA  . ASN C 1 151 ? 3.114   65.503  53.323  1.00 30.69  ? 180 ASN C CA  1 
ATOM   8018  C C   . ASN C 1 151 ? 3.286   64.748  54.644  1.00 28.98  ? 180 ASN C C   1 
ATOM   8019  O O   . ASN C 1 151 ? 2.726   65.123  55.672  1.00 27.51  ? 180 ASN C O   1 
ATOM   8020  C CB  . ASN C 1 151 ? 2.087   64.754  52.464  1.00 34.13  ? 180 ASN C CB  1 
ATOM   8021  C CG  . ASN C 1 151 ? 1.819   65.412  51.132  1.00 39.73  ? 180 ASN C CG  1 
ATOM   8022  O OD1 . ASN C 1 151 ? 1.338   66.541  51.093  1.00 42.86  ? 180 ASN C OD1 1 
ATOM   8023  N ND2 . ASN C 1 151 ? 2.154   64.722  50.049  1.00 44.67  ? 180 ASN C ND2 1 
ATOM   8024  N N   . PHE C 1 152 ? 4.039   63.646  54.606  1.00 25.77  ? 181 PHE C N   1 
ATOM   8025  C CA  . PHE C 1 152 ? 4.163   62.798  55.773  1.00 25.92  ? 181 PHE C CA  1 
ATOM   8026  C C   . PHE C 1 152 ? 4.787   63.592  56.931  1.00 25.24  ? 181 PHE C C   1 
ATOM   8027  O O   . PHE C 1 152 ? 4.316   63.527  58.071  1.00 23.18  ? 181 PHE C O   1 
ATOM   8028  C CB  . PHE C 1 152 ? 4.951   61.509  55.472  1.00 22.79  ? 181 PHE C CB  1 
ATOM   8029  C CG  . PHE C 1 152 ? 5.091   60.665  56.716  1.00 21.69  ? 181 PHE C CG  1 
ATOM   8030  C CD1 . PHE C 1 152 ? 4.037   59.885  57.165  1.00 21.18  ? 181 PHE C CD1 1 
ATOM   8031  C CD2 . PHE C 1 152 ? 6.245   60.727  57.494  1.00 21.62  ? 181 PHE C CD2 1 
ATOM   8032  C CE1 . PHE C 1 152 ? 4.130   59.200  58.369  1.00 20.07  ? 181 PHE C CE1 1 
ATOM   8033  C CE2 . PHE C 1 152 ? 6.343   60.025  58.686  1.00 20.98  ? 181 PHE C CE2 1 
ATOM   8034  C CZ  . PHE C 1 152 ? 5.302   59.231  59.095  1.00 21.70  ? 181 PHE C CZ  1 
ATOM   8035  N N   . ALA C 1 153 ? 5.839   64.358  56.637  1.00 26.02  ? 182 ALA C N   1 
ATOM   8036  C CA  . ALA C 1 153 ? 6.539   65.104  57.672  1.00 27.84  ? 182 ALA C CA  1 
ATOM   8037  C C   . ALA C 1 153 ? 5.581   66.053  58.383  1.00 30.84  ? 182 ALA C C   1 
ATOM   8038  O O   . ALA C 1 153 ? 5.571   66.119  59.611  1.00 27.04  ? 182 ALA C O   1 
ATOM   8039  C CB  . ALA C 1 153 ? 7.698   65.863  57.093  1.00 28.40  ? 182 ALA C CB  1 
ATOM   8040  N N   . ARG C 1 154 ? 4.776   66.791  57.610  1.00 36.68  ? 183 ARG C N   1 
ATOM   8041  C CA  . ARG C 1 154 ? 3.912   67.812  58.201  1.00 36.94  ? 183 ARG C CA  1 
ATOM   8042  C C   . ARG C 1 154 ? 2.729   67.160  58.912  1.00 32.21  ? 183 ARG C C   1 
ATOM   8043  O O   . ARG C 1 154 ? 2.320   67.614  59.980  1.00 32.87  ? 183 ARG C O   1 
ATOM   8044  C CB  . ARG C 1 154 ? 3.388   68.819  57.173  1.00 43.94  ? 183 ARG C CB  1 
ATOM   8045  C CG  . ARG C 1 154 ? 2.641   69.982  57.818  1.00 47.93  ? 183 ARG C CG  1 
ATOM   8046  C CD  . ARG C 1 154 ? 2.245   71.110  56.882  1.00 58.85  ? 183 ARG C CD  1 
ATOM   8047  N NE  . ARG C 1 154 ? 3.320   71.648  56.041  1.00 63.68  ? 183 ARG C NE  1 
ATOM   8048  C CZ  . ARG C 1 154 ? 3.766   72.904  56.078  1.00 63.50  ? 183 ARG C CZ  1 
ATOM   8049  N NH1 . ARG C 1 154 ? 4.590   73.346  55.142  1.00 60.90  ? 183 ARG C NH1 1 
ATOM   8050  N NH2 . ARG C 1 154 ? 3.363   73.726  57.032  1.00 66.76  ? 183 ARG C NH2 1 
ATOM   8051  N N   . ALA C 1 155 ? 2.167   66.115  58.297  1.00 30.58  ? 184 ALA C N   1 
ATOM   8052  C CA  . ALA C 1 155 ? 1.102   65.354  58.923  1.00 29.89  ? 184 ALA C CA  1 
ATOM   8053  C C   . ALA C 1 155 ? 1.571   64.757  60.247  1.00 32.47  ? 184 ALA C C   1 
ATOM   8054  O O   . ALA C 1 155 ? 0.835   64.762  61.237  1.00 28.55  ? 184 ALA C O   1 
ATOM   8055  C CB  . ALA C 1 155 ? 0.592   64.297  57.989  1.00 32.15  ? 184 ALA C CB  1 
ATOM   8056  N N   . TYR C 1 156 ? 2.803   64.227  60.273  1.00 28.12  ? 185 TYR C N   1 
ATOM   8057  C CA  . TYR C 1 156 ? 3.269   63.622  61.503  1.00 25.88  ? 185 TYR C CA  1 
ATOM   8058  C C   . TYR C 1 156 ? 3.358   64.696  62.583  1.00 27.49  ? 185 TYR C C   1 
ATOM   8059  O O   . TYR C 1 156 ? 3.032   64.403  63.722  1.00 26.23  ? 185 TYR C O   1 
ATOM   8060  C CB  . TYR C 1 156 ? 4.593   62.870  61.341  1.00 24.93  ? 185 TYR C CB  1 
ATOM   8061  C CG  . TYR C 1 156 ? 4.979   62.156  62.610  1.00 27.62  ? 185 TYR C CG  1 
ATOM   8062  C CD1 . TYR C 1 156 ? 5.599   62.822  63.667  1.00 25.91  ? 185 TYR C CD1 1 
ATOM   8063  C CD2 . TYR C 1 156 ? 4.632   60.831  62.800  1.00 25.55  ? 185 TYR C CD2 1 
ATOM   8064  C CE1 . TYR C 1 156 ? 5.868   62.178  64.865  1.00 25.56  ? 185 TYR C CE1 1 
ATOM   8065  C CE2 . TYR C 1 156 ? 4.953   60.160  63.962  1.00 26.53  ? 185 TYR C CE2 1 
ATOM   8066  C CZ  . TYR C 1 156 ? 5.565   60.830  65.003  1.00 26.51  ? 185 TYR C CZ  1 
ATOM   8067  O OH  . TYR C 1 156 ? 5.822   60.109  66.149  1.00 25.20  ? 185 TYR C OH  1 
ATOM   8068  N N   . ALA C 1 157 ? 3.788   65.916  62.210  1.00 29.92  ? 186 ALA C N   1 
ATOM   8069  C CA  . ALA C 1 157 ? 3.927   67.018  63.154  1.00 33.16  ? 186 ALA C CA  1 
ATOM   8070  C C   . ALA C 1 157 ? 2.579   67.388  63.777  1.00 37.72  ? 186 ALA C C   1 
ATOM   8071  O O   . ALA C 1 157 ? 2.506   67.697  64.970  1.00 38.78  ? 186 ALA C O   1 
ATOM   8072  C CB  . ALA C 1 157 ? 4.548   68.216  62.479  1.00 32.59  ? 186 ALA C CB  1 
ATOM   8073  N N   . GLN C 1 158 ? 1.512   67.372  62.973  1.00 38.86  ? 187 GLN C N   1 
ATOM   8074  C CA  . GLN C 1 158 ? 0.203   67.779  63.460  1.00 40.30  ? 187 GLN C CA  1 
ATOM   8075  C C   . GLN C 1 158 ? -0.437  66.634  64.227  1.00 38.52  ? 187 GLN C C   1 
ATOM   8076  O O   . GLN C 1 158 ? -1.455  66.831  64.879  1.00 45.57  ? 187 GLN C O   1 
ATOM   8077  C CB  . GLN C 1 158 ? -0.716  68.199  62.317  1.00 43.74  ? 187 GLN C CB  1 
ATOM   8078  C CG  . GLN C 1 158 ? -0.243  69.440  61.583  1.00 52.75  ? 187 GLN C CG  1 
ATOM   8079  C CD  . GLN C 1 158 ? -1.126  69.711  60.391  1.00 57.56  ? 187 GLN C CD  1 
ATOM   8080  O OE1 . GLN C 1 158 ? -0.701  69.574  59.245  1.00 63.55  ? 187 GLN C OE1 1 
ATOM   8081  N NE2 . GLN C 1 158 ? -2.374  70.065  60.661  1.00 53.14  ? 187 GLN C NE2 1 
ATOM   8082  N N   . GLY C 1 159 ? 0.160   65.441  64.144  1.00 35.14  ? 188 GLY C N   1 
ATOM   8083  C CA  . GLY C 1 159 ? -0.331  64.301  64.883  1.00 32.54  ? 188 GLY C CA  1 
ATOM   8084  C C   . GLY C 1 159 ? -1.252  63.476  64.003  1.00 32.74  ? 188 GLY C C   1 
ATOM   8085  O O   . GLY C 1 159 ? -2.231  63.978  63.444  1.00 33.35  ? 188 GLY C O   1 
ATOM   8086  N N   . ILE C 1 160 ? -0.915  62.205  63.869  1.00 30.72  ? 189 ILE C N   1 
ATOM   8087  C CA  . ILE C 1 160 ? -1.731  61.318  63.076  1.00 30.10  ? 189 ILE C CA  1 
ATOM   8088  C C   . ILE C 1 160 ? -1.554  59.915  63.648  1.00 27.16  ? 189 ILE C C   1 
ATOM   8089  O O   . ILE C 1 160 ? -0.486  59.589  64.198  1.00 28.89  ? 189 ILE C O   1 
ATOM   8090  C CB  . ILE C 1 160 ? -1.271  61.431  61.608  1.00 32.45  ? 189 ILE C CB  1 
ATOM   8091  C CG1 . ILE C 1 160 ? -2.259  60.814  60.602  1.00 35.35  ? 189 ILE C CG1 1 
ATOM   8092  C CG2 . ILE C 1 160 ? 0.135   60.852  61.509  1.00 31.18  ? 189 ILE C CG2 1 
ATOM   8093  C CD1 . ILE C 1 160 ? -3.310  61.776  60.060  1.00 38.79  ? 189 ILE C CD1 1 
ATOM   8094  N N   . SER C 1 161 ? -2.598  59.104  63.479  1.00 24.37  ? 190 SER C N   1 
ATOM   8095  C CA  . SER C 1 161 ? -2.603  57.718  63.906  1.00 26.15  ? 190 SER C CA  1 
ATOM   8096  C C   . SER C 1 161 ? -1.607  56.871  63.110  1.00 26.67  ? 190 SER C C   1 
ATOM   8097  O O   . SER C 1 161 ? -1.484  57.034  61.895  1.00 23.57  ? 190 SER C O   1 
ATOM   8098  C CB  . SER C 1 161 ? -3.956  57.139  63.768  1.00 25.69  ? 190 SER C CB  1 
ATOM   8099  O OG  . SER C 1 161 ? -3.932  55.759  64.109  1.00 31.89  ? 190 SER C OG  1 
ATOM   8100  N N   . ARG C 1 162 ? -0.928  55.963  63.835  1.00 28.95  ? 191 ARG C N   1 
ATOM   8101  C CA  . ARG C 1 162 ? -0.095  54.898  63.284  1.00 33.69  ? 191 ARG C CA  1 
ATOM   8102  C C   . ARG C 1 162 ? -0.711  54.258  62.037  1.00 32.51  ? 191 ARG C C   1 
ATOM   8103  O O   . ARG C 1 162 ? -0.012  54.035  61.049  1.00 31.24  ? 191 ARG C O   1 
ATOM   8104  C CB  . ARG C 1 162 ? 0.092   53.776  64.319  1.00 38.35  ? 191 ARG C CB  1 
ATOM   8105  C CG  . ARG C 1 162 ? 1.381   53.843  65.120  1.00 46.25  ? 191 ARG C CG  1 
ATOM   8106  C CD  . ARG C 1 162 ? 1.665   52.528  65.832  1.00 50.36  ? 191 ARG C CD  1 
ATOM   8107  N NE  . ARG C 1 162 ? 3.075   52.139  65.712  1.00 58.54  ? 191 ARG C NE  1 
ATOM   8108  C CZ  . ARG C 1 162 ? 3.534   51.143  64.952  1.00 66.27  ? 191 ARG C CZ  1 
ATOM   8109  N NH1 . ARG C 1 162 ? 2.694   50.350  64.311  1.00 72.27  ? 191 ARG C NH1 1 
ATOM   8110  N NH2 . ARG C 1 162 ? 4.834   50.934  64.826  1.00 70.33  ? 191 ARG C NH2 1 
ATOM   8111  N N   . THR C 1 163 ? -2.005  53.906  62.122  1.00 31.68  ? 192 THR C N   1 
ATOM   8112  C CA  . THR C 1 163 ? -2.740  53.235  61.053  1.00 34.18  ? 192 THR C CA  1 
ATOM   8113  C C   . THR C 1 163 ? -2.697  54.004  59.726  1.00 33.84  ? 192 THR C C   1 
ATOM   8114  O O   . THR C 1 163 ? -2.961  53.418  58.680  1.00 35.22  ? 192 THR C O   1 
ATOM   8115  C CB  . THR C 1 163 ? -4.224  53.019  61.415  1.00 33.40  ? 192 THR C CB  1 
ATOM   8116  O OG1 . THR C 1 163 ? -4.867  54.291  61.500  1.00 30.55  ? 192 THR C OG1 1 
ATOM   8117  C CG2 . THR C 1 163 ? -4.424  52.276  62.718  1.00 36.91  ? 192 THR C CG2 1 
ATOM   8118  N N   . LYS C 1 164 ? -2.364  55.302  59.766  1.00 31.23  ? 193 LYS C N   1 
ATOM   8119  C CA  . LYS C 1 164 ? -2.540  56.187  58.631  1.00 32.14  ? 193 LYS C CA  1 
ATOM   8120  C C   . LYS C 1 164 ? -1.209  56.563  57.978  1.00 27.53  ? 193 LYS C C   1 
ATOM   8121  O O   . LYS C 1 164 ? -1.214  57.167  56.914  1.00 27.33  ? 193 LYS C O   1 
ATOM   8122  C CB  . LYS C 1 164 ? -3.284  57.440  59.105  1.00 36.43  ? 193 LYS C CB  1 
ATOM   8123  C CG  . LYS C 1 164 ? -4.583  57.188  59.867  1.00 41.94  ? 193 LYS C CG  1 
ATOM   8124  C CD  . LYS C 1 164 ? -5.629  56.414  59.076  1.00 44.05  ? 193 LYS C CD  1 
ATOM   8125  C CE  . LYS C 1 164 ? -5.989  57.069  57.758  1.00 44.88  ? 193 LYS C CE  1 
ATOM   8126  N NZ  . LYS C 1 164 ? -6.463  58.467  57.935  1.00 44.49  ? 193 LYS C NZ  1 
ATOM   8127  N N   . TYR C 1 165 ? -0.067  56.193  58.578  1.00 24.29  ? 194 TYR C N   1 
ATOM   8128  C CA  . TYR C 1 165 ? 1.223   56.593  58.031  1.00 22.51  ? 194 TYR C CA  1 
ATOM   8129  C C   . TYR C 1 165 ? 1.346   56.270  56.546  1.00 20.78  ? 194 TYR C C   1 
ATOM   8130  O O   . TYR C 1 165 ? 1.865   57.043  55.761  1.00 22.79  ? 194 TYR C O   1 
ATOM   8131  C CB  . TYR C 1 165 ? 2.387   55.872  58.726  1.00 21.84  ? 194 TYR C CB  1 
ATOM   8132  C CG  . TYR C 1 165 ? 2.635   56.180  60.178  1.00 22.74  ? 194 TYR C CG  1 
ATOM   8133  C CD1 . TYR C 1 165 ? 2.131   57.319  60.790  1.00 21.26  ? 194 TYR C CD1 1 
ATOM   8134  C CD2 . TYR C 1 165 ? 3.475   55.364  60.921  1.00 24.74  ? 194 TYR C CD2 1 
ATOM   8135  C CE1 . TYR C 1 165 ? 2.384   57.592  62.126  1.00 23.02  ? 194 TYR C CE1 1 
ATOM   8136  C CE2 . TYR C 1 165 ? 3.727   55.617  62.267  1.00 25.31  ? 194 TYR C CE2 1 
ATOM   8137  C CZ  . TYR C 1 165 ? 3.187   56.741  62.868  1.00 25.52  ? 194 TYR C CZ  1 
ATOM   8138  O OH  . TYR C 1 165 ? 3.420   57.044  64.189  1.00 27.31  ? 194 TYR C OH  1 
ATOM   8139  N N   . TRP C 1 166 ? 0.875   55.093  56.146  1.00 23.07  ? 195 TRP C N   1 
ATOM   8140  C CA  . TRP C 1 166 ? 1.146   54.581  54.811  1.00 22.00  ? 195 TRP C CA  1 
ATOM   8141  C C   . TRP C 1 166 ? 0.572   55.475  53.711  1.00 21.53  ? 195 TRP C C   1 
ATOM   8142  O O   . TRP C 1 166 ? 1.164   55.576  52.637  1.00 20.21  ? 195 TRP C O   1 
ATOM   8143  C CB  . TRP C 1 166 ? 0.600   53.160  54.691  1.00 21.14  ? 195 TRP C CB  1 
ATOM   8144  C CG  . TRP C 1 166 ? -0.891  53.062  54.521  1.00 21.39  ? 195 TRP C CG  1 
ATOM   8145  C CD1 . TRP C 1 166 ? -1.807  52.769  55.484  1.00 23.14  ? 195 TRP C CD1 1 
ATOM   8146  C CD2 . TRP C 1 166 ? -1.624  53.104  53.280  1.00 20.52  ? 195 TRP C CD2 1 
ATOM   8147  N NE1 . TRP C 1 166 ? -3.066  52.712  54.938  1.00 22.68  ? 195 TRP C NE1 1 
ATOM   8148  C CE2 . TRP C 1 166 ? -2.990  52.907  53.585  1.00 22.08  ? 195 TRP C CE2 1 
ATOM   8149  C CE3 . TRP C 1 166 ? -1.278  53.346  51.950  1.00 20.39  ? 195 TRP C CE3 1 
ATOM   8150  C CZ2 . TRP C 1 166 ? -3.984  52.920  52.607  1.00 21.72  ? 195 TRP C CZ2 1 
ATOM   8151  C CZ3 . TRP C 1 166 ? -2.254  53.388  50.986  1.00 18.88  ? 195 TRP C CZ3 1 
ATOM   8152  C CH2 . TRP C 1 166 ? -3.598  53.166  51.311  1.00 21.05  ? 195 TRP C CH2 1 
ATOM   8153  N N   . GLU C 1 167 ? -0.613  56.072  53.954  1.00 22.23  ? 196 GLU C N   1 
ATOM   8154  C CA  . GLU C 1 167 ? -1.287  56.863  52.933  1.00 22.01  ? 196 GLU C CA  1 
ATOM   8155  C C   . GLU C 1 167 ? -0.422  58.052  52.520  1.00 19.76  ? 196 GLU C C   1 
ATOM   8156  O O   . GLU C 1 167 ? -0.245  58.319  51.324  1.00 19.69  ? 196 GLU C O   1 
ATOM   8157  C CB  . GLU C 1 167 ? -2.628  57.390  53.428  1.00 21.60  ? 196 GLU C CB  1 
ATOM   8158  C CG  . GLU C 1 167 ? -3.666  56.316  53.714  1.00 23.91  ? 196 GLU C CG  1 
ATOM   8159  C CD  . GLU C 1 167 ? -5.031  56.873  54.107  1.00 27.04  ? 196 GLU C CD  1 
ATOM   8160  O OE1 . GLU C 1 167 ? -5.177  58.097  54.254  1.00 30.89  ? 196 GLU C OE1 1 
ATOM   8161  O OE2 . GLU C 1 167 ? -5.953  56.087  54.262  1.00 32.43  ? 196 GLU C OE2 1 
ATOM   8162  N N   . LEU C 1 168 ? 0.051   58.773  53.527  1.00 21.98  ? 197 LEU C N   1 
ATOM   8163  C CA  . LEU C 1 168 ? 0.926   59.923  53.329  1.00 22.83  ? 197 LEU C CA  1 
ATOM   8164  C C   . LEU C 1 168 ? 2.270   59.493  52.743  1.00 22.02  ? 197 LEU C C   1 
ATOM   8165  O O   . LEU C 1 168 ? 2.843   60.212  51.924  1.00 21.18  ? 197 LEU C O   1 
ATOM   8166  C CB  . LEU C 1 168 ? 1.084   60.623  54.685  1.00 24.32  ? 197 LEU C CB  1 
ATOM   8167  C CG  . LEU C 1 168 ? -0.136  61.422  55.138  1.00 28.82  ? 197 LEU C CG  1 
ATOM   8168  C CD1 . LEU C 1 168 ? -0.240  61.450  56.652  1.00 31.19  ? 197 LEU C CD1 1 
ATOM   8169  C CD2 . LEU C 1 168 ? -0.070  62.832  54.610  1.00 27.62  ? 197 LEU C CD2 1 
ATOM   8170  N N   . ILE C 1 169 ? 2.787   58.334  53.188  1.00 20.65  ? 198 ILE C N   1 
ATOM   8171  C CA  . ILE C 1 169 ? 4.026   57.797  52.645  1.00 19.71  ? 198 ILE C CA  1 
ATOM   8172  C C   . ILE C 1 169 ? 3.835   57.497  51.148  1.00 19.00  ? 198 ILE C C   1 
ATOM   8173  O O   . ILE C 1 169 ? 4.714   57.765  50.314  1.00 17.05  ? 198 ILE C O   1 
ATOM   8174  C CB  . ILE C 1 169 ? 4.455   56.555  53.444  1.00 19.59  ? 198 ILE C CB  1 
ATOM   8175  C CG1 . ILE C 1 169 ? 4.800   56.941  54.890  1.00 17.98  ? 198 ILE C CG1 1 
ATOM   8176  C CG2 . ILE C 1 169 ? 5.576   55.809  52.722  1.00 20.40  ? 198 ILE C CG2 1 
ATOM   8177  C CD1 . ILE C 1 169 ? 6.118   57.590  55.070  1.00 17.62  ? 198 ILE C CD1 1 
ATOM   8178  N N   . TYR C 1 170 ? 2.682   56.909  50.816  1.00 17.31  ? 199 TYR C N   1 
ATOM   8179  C CA  . TYR C 1 170 ? 2.328   56.696  49.418  1.00 20.00  ? 199 TYR C CA  1 
ATOM   8180  C C   . TYR C 1 170 ? 2.434   57.999  48.622  1.00 19.08  ? 199 TYR C C   1 
ATOM   8181  O O   . TYR C 1 170 ? 3.029   57.984  47.540  1.00 18.15  ? 199 TYR C O   1 
ATOM   8182  C CB  . TYR C 1 170 ? 0.997   55.940  49.293  1.00 20.39  ? 199 TYR C CB  1 
ATOM   8183  C CG  . TYR C 1 170 ? 0.381   55.928  47.916  1.00 21.76  ? 199 TYR C CG  1 
ATOM   8184  C CD1 . TYR C 1 170 ? -0.423  56.975  47.475  1.00 21.96  ? 199 TYR C CD1 1 
ATOM   8185  C CD2 . TYR C 1 170 ? 0.557   54.849  47.062  1.00 22.38  ? 199 TYR C CD2 1 
ATOM   8186  C CE1 . TYR C 1 170 ? -1.034  56.952  46.232  1.00 22.55  ? 199 TYR C CE1 1 
ATOM   8187  C CE2 . TYR C 1 170 ? -0.033  54.824  45.811  1.00 24.07  ? 199 TYR C CE2 1 
ATOM   8188  C CZ  . TYR C 1 170 ? -0.829  55.872  45.390  1.00 21.38  ? 199 TYR C CZ  1 
ATOM   8189  O OH  . TYR C 1 170 ? -1.403  55.814  44.159  1.00 20.95  ? 199 TYR C OH  1 
ATOM   8190  N N   . GLU C 1 171 ? 1.836   59.103  49.122  1.00 20.64  ? 200 GLU C N   1 
ATOM   8191  C CA  . GLU C 1 171 ? 1.733   60.324  48.336  1.00 20.48  ? 200 GLU C CA  1 
ATOM   8192  C C   . GLU C 1 171 ? 3.118   60.935  48.164  1.00 18.57  ? 200 GLU C C   1 
ATOM   8193  O O   . GLU C 1 171 ? 3.444   61.381  47.061  1.00 17.16  ? 200 GLU C O   1 
ATOM   8194  C CB  . GLU C 1 171 ? 0.789   61.373  48.948  1.00 21.69  ? 200 GLU C CB  1 
ATOM   8195  C CG  . GLU C 1 171 ? -0.660  60.927  49.051  1.00 22.66  ? 200 GLU C CG  1 
ATOM   8196  C CD  . GLU C 1 171 ? -1.396  60.805  47.718  1.00 24.30  ? 200 GLU C CD  1 
ATOM   8197  O OE1 . GLU C 1 171 ? -0.882  61.322  46.708  1.00 22.85  ? 200 GLU C OE1 1 
ATOM   8198  O OE2 . GLU C 1 171 ? -2.458  60.141  47.680  1.00 25.80  ? 200 GLU C OE2 1 
ATOM   8199  N N   . ASP C 1 172 ? 3.934   60.872  49.219  1.00 19.05  ? 201 ASP C N   1 
ATOM   8200  C CA  . ASP C 1 172 ? 5.286   61.415  49.142  1.00 20.21  ? 201 ASP C CA  1 
ATOM   8201  C C   . ASP C 1 172 ? 6.139   60.580  48.185  1.00 19.85  ? 201 ASP C C   1 
ATOM   8202  O O   . ASP C 1 172 ? 6.994   61.137  47.506  1.00 20.30  ? 201 ASP C O   1 
ATOM   8203  C CB  . ASP C 1 172 ? 5.956   61.500  50.520  1.00 20.94  ? 201 ASP C CB  1 
ATOM   8204  C CG  . ASP C 1 172 ? 5.568   62.713  51.361  1.00 24.10  ? 201 ASP C CG  1 
ATOM   8205  O OD1 . ASP C 1 172 ? 4.826   63.604  50.870  1.00 25.95  ? 201 ASP C OD1 1 
ATOM   8206  O OD2 . ASP C 1 172 ? 6.004   62.757  52.502  1.00 23.51  ? 201 ASP C OD2 1 
ATOM   8207  N N   . SER C 1 173 ? 5.926   59.244  48.185  1.00 18.89  ? 202 SER C N   1 
ATOM   8208  C CA  . SER C 1 173 ? 6.712   58.331  47.365  1.00 18.87  ? 202 SER C CA  1 
ATOM   8209  C C   . SER C 1 173 ? 6.368   58.515  45.889  1.00 19.98  ? 202 SER C C   1 
ATOM   8210  O O   . SER C 1 173 ? 7.245   58.463  45.042  1.00 19.93  ? 202 SER C O   1 
ATOM   8211  C CB  . SER C 1 173 ? 6.502   56.886  47.767  1.00 17.52  ? 202 SER C CB  1 
ATOM   8212  O OG  . SER C 1 173 ? 7.065   56.618  49.041  1.00 18.77  ? 202 SER C OG  1 
ATOM   8213  N N   . MET C 1 174 ? 5.075   58.744  45.597  1.00 20.41  ? 203 MET C N   1 
ATOM   8214  C CA  . MET C 1 174 ? 4.613   58.983  44.247  1.00 21.72  ? 203 MET C CA  1 
ATOM   8215  C C   . MET C 1 174 ? 5.154   60.318  43.748  1.00 21.27  ? 203 MET C C   1 
ATOM   8216  O O   . MET C 1 174 ? 5.590   60.421  42.597  1.00 21.59  ? 203 MET C O   1 
ATOM   8217  C CB  . MET C 1 174 ? 3.081   58.962  44.188  1.00 22.12  ? 203 MET C CB  1 
ATOM   8218  C CG  . MET C 1 174 ? 2.499   57.571  44.419  1.00 23.89  ? 203 MET C CG  1 
ATOM   8219  S SD  . MET C 1 174 ? 2.444   56.537  42.915  1.00 24.30  ? 203 MET C SD  1 
ATOM   8220  C CE  . MET C 1 174 ? 0.965   57.205  42.152  1.00 28.55  ? 203 MET C CE  1 
ATOM   8221  N N   . ASP C 1 175 ? 5.144   61.326  44.630  1.00 22.10  ? 204 ASP C N   1 
ATOM   8222  C CA  . ASP C 1 175 ? 5.656   62.641  44.278  1.00 21.30  ? 204 ASP C CA  1 
ATOM   8223  C C   . ASP C 1 175 ? 7.158   62.567  43.992  1.00 20.80  ? 204 ASP C C   1 
ATOM   8224  O O   . ASP C 1 175 ? 7.626   63.130  43.000  1.00 20.50  ? 204 ASP C O   1 
ATOM   8225  C CB  . ASP C 1 175 ? 5.388   63.656  45.397  1.00 25.01  ? 204 ASP C CB  1 
ATOM   8226  C CG  . ASP C 1 175 ? 3.925   64.045  45.533  1.00 27.42  ? 204 ASP C CG  1 
ATOM   8227  O OD1 . ASP C 1 175 ? 3.157   63.757  44.593  1.00 29.73  ? 204 ASP C OD1 1 
ATOM   8228  O OD2 . ASP C 1 175 ? 3.554   64.583  46.605  1.00 29.95  ? 204 ASP C OD2 1 
ATOM   8229  N N   . LEU C 1 176 ? 7.900   61.844  44.845  1.00 17.59  ? 205 LEU C N   1 
ATOM   8230  C CA  . LEU C 1 176 ? 9.352   61.768  44.704  1.00 19.11  ? 205 LEU C CA  1 
ATOM   8231  C C   . LEU C 1 176 ? 9.709   61.030  43.422  1.00 18.02  ? 205 LEU C C   1 
ATOM   8232  O O   . LEU C 1 176 ? 10.549  61.471  42.662  1.00 19.37  ? 205 LEU C O   1 
ATOM   8233  C CB  . LEU C 1 176 ? 9.993   61.112  45.924  1.00 18.54  ? 205 LEU C CB  1 
ATOM   8234  C CG  . LEU C 1 176 ? 11.507  60.864  45.815  1.00 17.91  ? 205 LEU C CG  1 
ATOM   8235  C CD1 . LEU C 1 176 ? 12.228  62.159  45.520  1.00 19.83  ? 205 LEU C CD1 1 
ATOM   8236  C CD2 . LEU C 1 176 ? 12.008  60.235  47.097  1.00 21.77  ? 205 LEU C CD2 1 
ATOM   8237  N N   . ILE C 1 177 ? 9.053   59.902  43.164  1.00 20.74  ? 206 ILE C N   1 
ATOM   8238  C CA  . ILE C 1 177 ? 9.287   59.179  41.930  1.00 20.70  ? 206 ILE C CA  1 
ATOM   8239  C C   . ILE C 1 177 ? 9.026   60.058  40.717  1.00 20.21  ? 206 ILE C C   1 
ATOM   8240  O O   . ILE C 1 177 ? 9.760   59.987  39.747  1.00 21.23  ? 206 ILE C O   1 
ATOM   8241  C CB  . ILE C 1 177 ? 8.404   57.934  41.840  1.00 20.19  ? 206 ILE C CB  1 
ATOM   8242  C CG1 . ILE C 1 177 ? 8.801   56.880  42.865  1.00 20.96  ? 206 ILE C CG1 1 
ATOM   8243  C CG2 . ILE C 1 177 ? 8.427   57.392  40.410  1.00 20.69  ? 206 ILE C CG2 1 
ATOM   8244  C CD1 . ILE C 1 177 ? 7.755   55.786  43.041  1.00 21.17  ? 206 ILE C CD1 1 
ATOM   8245  N N   . ALA C 1 178 ? 7.958   60.861  40.751  1.00 22.18  ? 207 ALA C N   1 
ATOM   8246  C CA  . ALA C 1 178 ? 7.633   61.702  39.608  1.00 23.25  ? 207 ALA C CA  1 
ATOM   8247  C C   . ALA C 1 178 ? 8.709   62.775  39.401  1.00 25.80  ? 207 ALA C C   1 
ATOM   8248  O O   . ALA C 1 178 ? 9.083   63.062  38.264  1.00 24.93  ? 207 ALA C O   1 
ATOM   8249  C CB  . ALA C 1 178 ? 6.265   62.288  39.788  1.00 23.67  ? 207 ALA C CB  1 
ATOM   8250  N N   . LYS C 1 179 ? 9.247   63.308  40.507  1.00 22.10  ? 208 LYS C N   1 
ATOM   8251  C CA  . LYS C 1 179 ? 10.200  64.411  40.490  1.00 21.68  ? 208 LYS C CA  1 
ATOM   8252  C C   . LYS C 1 179 ? 11.614  63.973  40.117  1.00 21.59  ? 208 LYS C C   1 
ATOM   8253  O O   . LYS C 1 179 ? 12.457  64.811  39.786  1.00 22.73  ? 208 LYS C O   1 
ATOM   8254  C CB  . LYS C 1 179 ? 10.269  65.051  41.886  1.00 23.38  ? 208 LYS C CB  1 
ATOM   8255  C CG  . LYS C 1 179 ? 9.044   65.855  42.287  1.00 28.54  ? 208 LYS C CG  1 
ATOM   8256  C CD  . LYS C 1 179 ? 9.002   66.213  43.765  1.00 31.14  ? 208 LYS C CD  1 
ATOM   8257  C CE  . LYS C 1 179 ? 7.599   66.505  44.233  1.00 32.78  ? 208 LYS C CE  1 
ATOM   8258  N NZ  . LYS C 1 179 ? 6.978   67.534  43.373  1.00 33.45  ? 208 LYS C NZ  1 
ATOM   8259  N N   . LEU C 1 180 ? 11.932  62.680  40.254  1.00 18.68  ? 209 LEU C N   1 
ATOM   8260  C CA  . LEU C 1 180 ? 13.333  62.303  40.274  1.00 18.89  ? 209 LEU C CA  1 
ATOM   8261  C C   . LEU C 1 180 ? 13.990  62.594  38.914  1.00 20.60  ? 209 LEU C C   1 
ATOM   8262  O O   . LEU C 1 180 ? 15.097  63.147  38.909  1.00 20.14  ? 209 LEU C O   1 
ATOM   8263  C CB  . LEU C 1 180 ? 13.473  60.833  40.715  1.00 19.02  ? 209 LEU C CB  1 
ATOM   8264  C CG  . LEU C 1 180 ? 13.704  60.678  42.224  1.00 19.64  ? 209 LEU C CG  1 
ATOM   8265  C CD1 . LEU C 1 180 ? 13.594  59.232  42.688  1.00 20.75  ? 209 LEU C CD1 1 
ATOM   8266  C CD2 . LEU C 1 180 ? 15.070  61.229  42.622  1.00 20.47  ? 209 LEU C CD2 1 
ATOM   8267  N N   . PRO C 1 181 ? 13.367  62.234  37.750  1.00 20.11  ? 210 PRO C N   1 
ATOM   8268  C CA  . PRO C 1 181 ? 13.913  62.565  36.427  1.00 19.35  ? 210 PRO C CA  1 
ATOM   8269  C C   . PRO C 1 181 ? 14.176  64.058  36.226  1.00 22.43  ? 210 PRO C C   1 
ATOM   8270  O O   . PRO C 1 181 ? 15.158  64.430  35.575  1.00 24.42  ? 210 PRO C O   1 
ATOM   8271  C CB  . PRO C 1 181 ? 12.834  62.075  35.440  1.00 19.79  ? 210 PRO C CB  1 
ATOM   8272  C CG  . PRO C 1 181 ? 12.187  60.927  36.181  1.00 21.49  ? 210 PRO C CG  1 
ATOM   8273  C CD  . PRO C 1 181 ? 12.162  61.406  37.630  1.00 19.91  ? 210 PRO C CD  1 
ATOM   8274  N N   . CYS C 1 182 ? 13.279  64.907  36.743  1.00 23.09  ? 211 CYS C N   1 
ATOM   8275  C CA  . CYS C 1 182 ? 13.495  66.349  36.696  1.00 24.35  ? 211 CYS C CA  1 
ATOM   8276  C C   . CYS C 1 182 ? 14.793  66.750  37.411  1.00 24.59  ? 211 CYS C C   1 
ATOM   8277  O O   . CYS C 1 182 ? 15.630  67.461  36.841  1.00 20.40  ? 211 CYS C O   1 
ATOM   8278  C CB  . CYS C 1 182 ? 12.331  67.117  37.306  1.00 26.01  ? 211 CYS C CB  1 
ATOM   8279  S SG  . CYS C 1 182 ? 10.774  66.944  36.393  1.00 32.69  ? 211 CYS C SG  1 
ATOM   8280  N N   . VAL C 1 183 ? 14.962  66.280  38.658  1.00 21.64  ? 212 VAL C N   1 
ATOM   8281  C CA  . VAL C 1 183 ? 16.190  66.500  39.406  1.00 21.16  ? 212 VAL C CA  1 
ATOM   8282  C C   . VAL C 1 183 ? 17.390  65.949  38.625  1.00 21.29  ? 212 VAL C C   1 
ATOM   8283  O O   . VAL C 1 183 ? 18.343  66.659  38.336  1.00 23.07  ? 212 VAL C O   1 
ATOM   8284  C CB  . VAL C 1 183 ? 16.125  65.862  40.814  1.00 21.33  ? 212 VAL C CB  1 
ATOM   8285  C CG1 . VAL C 1 183 ? 17.427  66.116  41.576  1.00 19.65  ? 212 VAL C CG1 1 
ATOM   8286  C CG2 . VAL C 1 183 ? 14.913  66.352  41.594  1.00 22.33  ? 212 VAL C CG2 1 
ATOM   8287  N N   . ALA C 1 184 ? 17.320  64.666  38.267  1.00 20.22  ? 213 ALA C N   1 
ATOM   8288  C CA  . ALA C 1 184 ? 18.425  63.966  37.630  1.00 22.07  ? 213 ALA C CA  1 
ATOM   8289  C C   . ALA C 1 184 ? 18.823  64.644  36.320  1.00 23.81  ? 213 ALA C C   1 
ATOM   8290  O O   . ALA C 1 184 ? 20.005  64.717  36.006  1.00 24.36  ? 213 ALA C O   1 
ATOM   8291  C CB  . ALA C 1 184 ? 18.035  62.528  37.397  1.00 22.54  ? 213 ALA C CB  1 
ATOM   8292  N N   . ALA C 1 185 ? 17.837  65.166  35.579  1.00 23.09  ? 214 ALA C N   1 
ATOM   8293  C CA  . ALA C 1 185 ? 18.075  65.734  34.257  1.00 24.02  ? 214 ALA C CA  1 
ATOM   8294  C C   . ALA C 1 185 ? 18.583  67.162  34.395  1.00 25.83  ? 214 ALA C C   1 
ATOM   8295  O O   . ALA C 1 185 ? 19.366  67.638  33.580  1.00 31.30  ? 214 ALA C O   1 
ATOM   8296  C CB  . ALA C 1 185 ? 16.810  65.692  33.431  1.00 28.24  ? 214 ALA C CB  1 
ATOM   8297  N N   . LYS C 1 186 ? 18.165  67.842  35.457  1.00 24.77  ? 215 LYS C N   1 
ATOM   8298  C CA  . LYS C 1 186 ? 18.734  69.146  35.731  1.00 24.40  ? 215 LYS C CA  1 
ATOM   8299  C C   . LYS C 1 186 ? 20.231  69.009  36.069  1.00 25.04  ? 215 LYS C C   1 
ATOM   8300  O O   . LYS C 1 186 ? 21.042  69.874  35.718  1.00 22.36  ? 215 LYS C O   1 
ATOM   8301  C CB  . LYS C 1 186 ? 17.870  69.836  36.790  1.00 25.51  ? 215 LYS C CB  1 
ATOM   8302  C CG  . LYS C 1 186 ? 17.993  71.350  36.821  1.00 28.97  ? 215 LYS C CG  1 
ATOM   8303  C CD  . LYS C 1 186 ? 16.925  72.032  37.651  1.00 31.59  ? 215 LYS C CD  1 
ATOM   8304  C CE  . LYS C 1 186 ? 16.698  73.477  37.267  1.00 34.03  ? 215 LYS C CE  1 
ATOM   8305  N N   . ILE C 1 187 ? 20.621  67.925  36.761  1.00 22.30  ? 216 ILE C N   1 
ATOM   8306  C CA  . ILE C 1 187 ? 22.007  67.731  37.168  1.00 22.95  ? 216 ILE C CA  1 
ATOM   8307  C C   . ILE C 1 187 ? 22.848  67.545  35.907  1.00 23.92  ? 216 ILE C C   1 
ATOM   8308  O O   . ILE C 1 187 ? 23.922  68.139  35.780  1.00 27.70  ? 216 ILE C O   1 
ATOM   8309  C CB  . ILE C 1 187 ? 22.168  66.518  38.118  1.00 22.32  ? 216 ILE C CB  1 
ATOM   8310  C CG1 . ILE C 1 187 ? 21.570  66.747  39.498  1.00 24.21  ? 216 ILE C CG1 1 
ATOM   8311  C CG2 . ILE C 1 187 ? 23.622  66.080  38.226  1.00 20.78  ? 216 ILE C CG2 1 
ATOM   8312  C CD1 . ILE C 1 187 ? 21.337  65.455  40.281  1.00 24.56  ? 216 ILE C CD1 1 
ATOM   8313  N N   . TYR C 1 188 ? 22.353  66.671  35.029  1.00 23.96  ? 217 TYR C N   1 
ATOM   8314  C CA  . TYR C 1 188 ? 23.052  66.252  33.828  1.00 24.74  ? 217 TYR C CA  1 
ATOM   8315  C C   . TYR C 1 188 ? 23.318  67.465  32.949  1.00 25.59  ? 217 TYR C C   1 
ATOM   8316  O O   . TYR C 1 188 ? 24.450  67.698  32.528  1.00 25.35  ? 217 TYR C O   1 
ATOM   8317  C CB  . TYR C 1 188 ? 22.224  65.211  33.074  1.00 24.39  ? 217 TYR C CB  1 
ATOM   8318  C CG  . TYR C 1 188 ? 22.928  64.615  31.888  1.00 24.44  ? 217 TYR C CG  1 
ATOM   8319  C CD1 . TYR C 1 188 ? 23.864  63.617  32.075  1.00 22.93  ? 217 TYR C CD1 1 
ATOM   8320  C CD2 . TYR C 1 188 ? 22.736  65.101  30.598  1.00 24.45  ? 217 TYR C CD2 1 
ATOM   8321  C CE1 . TYR C 1 188 ? 24.529  63.060  30.997  1.00 24.91  ? 217 TYR C CE1 1 
ATOM   8322  C CE2 . TYR C 1 188 ? 23.401  64.549  29.511  1.00 25.93  ? 217 TYR C CE2 1 
ATOM   8323  C CZ  . TYR C 1 188 ? 24.316  63.535  29.714  1.00 24.78  ? 217 TYR C CZ  1 
ATOM   8324  O OH  . TYR C 1 188 ? 25.022  62.964  28.681  1.00 27.09  ? 217 TYR C OH  1 
ATOM   8325  N N   . ARG C 1 189 ? 22.249  68.224  32.694  1.00 27.75  ? 218 ARG C N   1 
ATOM   8326  C CA  . ARG C 1 189 ? 22.329  69.365  31.795  1.00 29.92  ? 218 ARG C CA  1 
ATOM   8327  C C   . ARG C 1 189 ? 23.224  70.452  32.374  1.00 27.81  ? 218 ARG C C   1 
ATOM   8328  O O   . ARG C 1 189 ? 23.955  71.093  31.620  1.00 31.07  ? 218 ARG C O   1 
ATOM   8329  C CB  . ARG C 1 189 ? 20.925  69.873  31.471  1.00 32.96  ? 218 ARG C CB  1 
ATOM   8330  C CG  . ARG C 1 189 ? 20.168  68.940  30.540  1.00 39.62  ? 218 ARG C CG  1 
ATOM   8331  C CD  . ARG C 1 189 ? 19.102  69.671  29.738  1.00 47.06  ? 218 ARG C CD  1 
ATOM   8332  N NE  . ARG C 1 189 ? 18.314  68.805  28.861  1.00 51.30  ? 218 ARG C NE  1 
ATOM   8333  C CZ  . ARG C 1 189 ? 17.787  69.164  27.683  1.00 52.80  ? 218 ARG C CZ  1 
ATOM   8334  N NH1 . ARG C 1 189 ? 17.915  70.399  27.219  1.00 48.36  ? 218 ARG C NH1 1 
ATOM   8335  N NH2 . ARG C 1 189 ? 17.106  68.274  26.979  1.00 54.70  ? 218 ARG C NH2 1 
ATOM   8336  N N   . ASN C 1 190 ? 23.156  70.677  33.691  1.00 25.00  ? 219 ASN C N   1 
ATOM   8337  C CA  . ASN C 1 190 ? 23.974  71.688  34.332  1.00 27.89  ? 219 ASN C CA  1 
ATOM   8338  C C   . ASN C 1 190 ? 25.447  71.308  34.232  1.00 28.77  ? 219 ASN C C   1 
ATOM   8339  O O   . ASN C 1 190 ? 26.286  72.174  34.003  1.00 28.96  ? 219 ASN C O   1 
ATOM   8340  C CB  . ASN C 1 190 ? 23.571  71.920  35.790  1.00 29.20  ? 219 ASN C CB  1 
ATOM   8341  C CG  . ASN C 1 190 ? 22.348  72.799  35.956  1.00 31.99  ? 219 ASN C CG  1 
ATOM   8342  O OD1 . ASN C 1 190 ? 21.785  73.312  34.989  1.00 29.99  ? 219 ASN C OD1 1 
ATOM   8343  N ND2 . ASN C 1 190 ? 21.937  72.981  37.204  1.00 30.82  ? 219 ASN C ND2 1 
ATOM   8344  N N   . LEU C 1 191 ? 25.758  70.013  34.402  1.00 27.60  ? 220 LEU C N   1 
ATOM   8345  C CA  . LEU C 1 191 ? 27.136  69.555  34.393  1.00 27.25  ? 220 LEU C CA  1 
ATOM   8346  C C   . LEU C 1 191 ? 27.669  69.396  32.968  1.00 30.10  ? 220 LEU C C   1 
ATOM   8347  O O   . LEU C 1 191 ? 28.855  69.636  32.756  1.00 34.73  ? 220 LEU C O   1 
ATOM   8348  C CB  . LEU C 1 191 ? 27.246  68.219  35.140  1.00 27.58  ? 220 LEU C CB  1 
ATOM   8349  C CG  . LEU C 1 191 ? 27.208  68.315  36.668  1.00 25.73  ? 220 LEU C CG  1 
ATOM   8350  C CD1 . LEU C 1 191 ? 27.027  66.946  37.290  1.00 26.58  ? 220 LEU C CD1 1 
ATOM   8351  C CD2 . LEU C 1 191 ? 28.466  68.974  37.210  1.00 26.21  ? 220 LEU C CD2 1 
ATOM   8352  N N   . TYR C 1 192 ? 26.843  68.845  32.071  1.00 31.75  ? 221 TYR C N   1 
ATOM   8353  C CA  . TYR C 1 192 ? 27.356  68.401  30.741  1.00 35.95  ? 221 TYR C CA  1 
ATOM   8354  C C   . TYR C 1 192 ? 26.645  68.959  29.514  1.00 32.61  ? 221 TYR C C   1 
ATOM   8355  O O   . TYR C 1 192 ? 27.079  68.610  28.404  1.00 32.63  ? 221 TYR C O   1 
ATOM   8356  C CB  . TYR C 1 192 ? 27.192  66.876  30.775  1.00 35.68  ? 221 TYR C CB  1 
ATOM   8357  C CG  . TYR C 1 192 ? 27.625  66.200  32.069  1.00 36.62  ? 221 TYR C CG  1 
ATOM   8358  C CD1 . TYR C 1 192 ? 28.928  66.315  32.540  1.00 36.65  ? 221 TYR C CD1 1 
ATOM   8359  C CD2 . TYR C 1 192 ? 26.732  65.444  32.817  1.00 35.58  ? 221 TYR C CD2 1 
ATOM   8360  C CE1 . TYR C 1 192 ? 29.325  65.702  33.715  1.00 35.43  ? 221 TYR C CE1 1 
ATOM   8361  C CE2 . TYR C 1 192 ? 27.116  64.827  33.995  1.00 38.36  ? 221 TYR C CE2 1 
ATOM   8362  C CZ  . TYR C 1 192 ? 28.417  64.956  34.444  1.00 37.23  ? 221 TYR C CZ  1 
ATOM   8363  O OH  . TYR C 1 192 ? 28.811  64.356  35.600  1.00 37.76  ? 221 TYR C OH  1 
ATOM   8364  N N   . ARG C 1 193 ? 25.562  69.717  29.703  1.00 34.33  ? 222 ARG C N   1 
ATOM   8365  C CA  . ARG C 1 193 ? 24.784  70.243  28.550  1.00 37.36  ? 222 ARG C CA  1 
ATOM   8366  C C   . ARG C 1 193 ? 24.696  71.771  28.671  1.00 37.44  ? 222 ARG C C   1 
ATOM   8367  O O   . ARG C 1 193 ? 23.718  72.346  28.151  1.00 40.77  ? 222 ARG C O   1 
ATOM   8368  C CB  . ARG C 1 193 ? 23.390  69.611  28.476  1.00 37.69  ? 222 ARG C CB  1 
ATOM   8369  C CG  . ARG C 1 193 ? 23.374  68.107  28.248  1.00 38.54  ? 222 ARG C CG  1 
ATOM   8370  C CD  . ARG C 1 193 ? 22.747  67.755  26.909  1.00 41.33  ? 222 ARG C CD  1 
ATOM   8371  N NE  . ARG C 1 193 ? 22.370  66.340  26.821  1.00 44.65  ? 222 ARG C NE  1 
ATOM   8372  C CZ  . ARG C 1 193 ? 22.994  65.434  26.079  1.00 41.43  ? 222 ARG C CZ  1 
ATOM   8373  N NH1 . ARG C 1 193 ? 24.270  65.169  26.291  1.00 39.92  ? 222 ARG C NH1 1 
ATOM   8374  N NH2 . ARG C 1 193 ? 22.337  64.795  25.129  1.00 40.73  ? 222 ARG C NH2 1 
ATOM   8375  N N   . GLU C 1 194 ? 25.682  72.338  29.367  1.00 40.13  ? 223 GLU C N   1 
ATOM   8376  C CA  . GLU C 1 194 ? 25.800  73.805  29.608  1.00 45.87  ? 223 GLU C CA  1 
ATOM   8377  C C   . GLU C 1 194 ? 24.461  74.409  30.066  1.00 44.61  ? 223 GLU C C   1 
ATOM   8378  O O   . GLU C 1 194 ? 24.024  75.392  29.451  1.00 48.44  ? 223 GLU C O   1 
ATOM   8379  C CB  . GLU C 1 194 ? 26.563  74.475  28.455  1.00 47.70  ? 223 GLU C CB  1 
ATOM   8380  C CG  . GLU C 1 194 ? 28.053  74.144  28.496  1.00 46.66  ? 223 GLU C CG  1 
ATOM   8381  C CD  . GLU C 1 194 ? 28.937  74.747  27.422  1.00 47.80  ? 223 GLU C CD  1 
ATOM   8382  O OE1 . GLU C 1 194 ? 29.575  73.973  26.676  1.00 44.92  ? 223 GLU C OE1 1 
ATOM   8383  O OE2 . GLU C 1 194 ? 28.999  75.990  27.344  1.00 47.14  ? 223 GLU C OE2 1 
ATOM   8384  N N   . GLY C 1 195 ? 23.880  73.855  31.123  1.00 41.80  ? 224 GLY C N   1 
ATOM   8385  C CA  . GLY C 1 195 ? 22.629  74.347  31.734  1.00 45.81  ? 224 GLY C CA  1 
ATOM   8386  C C   . GLY C 1 195 ? 21.511  74.525  30.725  1.00 46.36  ? 224 GLY C C   1 
ATOM   8387  O O   . GLY C 1 195 ? 20.603  75.334  31.004  1.00 49.98  ? 224 GLY C O   1 
ATOM   8388  N N   . SER C 1 196 ? 21.557  73.811  29.595  1.00 48.74  ? 225 SER C N   1 
ATOM   8389  C CA  . SER C 1 196 ? 20.447  73.863  28.619  1.00 50.22  ? 225 SER C CA  1 
ATOM   8390  C C   . SER C 1 196 ? 19.098  73.650  29.321  1.00 57.25  ? 225 SER C C   1 
ATOM   8391  O O   . SER C 1 196 ? 19.021  72.800  30.221  1.00 62.08  ? 225 SER C O   1 
ATOM   8392  C CB  . SER C 1 196 ? 20.631  72.867  27.529  1.00 47.93  ? 225 SER C CB  1 
ATOM   8393  O OG  . SER C 1 196 ? 20.735  71.545  28.025  1.00 44.66  ? 225 SER C OG  1 
ATOM   8394  N N   . GLY C 1 197 ? 18.061  74.367  28.891  1.00 61.81  ? 226 GLY C N   1 
ATOM   8395  C CA  . GLY C 1 197 ? 16.747  74.183  29.488  1.00 67.23  ? 226 GLY C CA  1 
ATOM   8396  C C   . GLY C 1 197 ? 16.255  72.746  29.330  1.00 71.60  ? 226 GLY C C   1 
ATOM   8397  O O   . GLY C 1 197 ? 16.088  72.287  28.199  1.00 71.60  ? 226 GLY C O   1 
ATOM   8398  N N   . ILE C 1 198 ? 16.015  72.071  30.472  1.00 72.84  ? 227 ILE C N   1 
ATOM   8399  C CA  . ILE C 1 198 ? 15.788  70.629  30.518  1.00 70.49  ? 227 ILE C CA  1 
ATOM   8400  C C   . ILE C 1 198 ? 14.508  70.284  29.757  1.00 67.13  ? 227 ILE C C   1 
ATOM   8401  O O   . ILE C 1 198 ? 14.411  69.212  29.156  1.00 59.00  ? 227 ILE C O   1 
ATOM   8402  C CB  . ILE C 1 198 ? 15.790  70.055  31.960  1.00 70.71  ? 227 ILE C CB  1 
ATOM   8403  C CG1 . ILE C 1 198 ? 14.494  70.296  32.748  1.00 70.13  ? 227 ILE C CG1 1 
ATOM   8404  C CG2 . ILE C 1 198 ? 17.013  70.511  32.746  1.00 67.95  ? 227 ILE C CG2 1 
ATOM   8405  C CD1 . ILE C 1 198 ? 14.462  69.618  34.114  1.00 66.46  ? 227 ILE C CD1 1 
ATOM   8406  N N   . GLY C 1 199 ? 13.534  71.201  29.790  1.00 67.24  ? 228 GLY C N   1 
ATOM   8407  C CA  . GLY C 1 199 ? 12.345  71.087  28.966  1.00 59.51  ? 228 GLY C CA  1 
ATOM   8408  C C   . GLY C 1 199 ? 11.161  70.531  29.746  1.00 53.59  ? 228 GLY C C   1 
ATOM   8409  O O   . GLY C 1 199 ? 11.247  70.305  30.953  1.00 52.94  ? 228 GLY C O   1 
ATOM   8410  N N   . ALA C 1 200 ? 10.061  70.323  29.017  1.00 49.05  ? 229 ALA C N   1 
ATOM   8411  C CA  . ALA C 1 200 ? 8.767   70.057  29.616  1.00 49.85  ? 229 ALA C CA  1 
ATOM   8412  C C   . ALA C 1 200 ? 8.510   68.557  29.667  1.00 44.51  ? 229 ALA C C   1 
ATOM   8413  O O   . ALA C 1 200 ? 9.094   67.773  28.927  1.00 53.59  ? 229 ALA C O   1 
ATOM   8414  C CB  . ALA C 1 200 ? 7.677   70.768  28.851  1.00 49.42  ? 229 ALA C CB  1 
ATOM   8415  N N   . ILE C 1 201 ? 7.648   68.183  30.598  1.00 40.24  ? 230 ILE C N   1 
ATOM   8416  C CA  . ILE C 1 201 ? 7.084   66.853  30.638  1.00 40.62  ? 230 ILE C CA  1 
ATOM   8417  C C   . ILE C 1 201 ? 5.972   66.799  29.596  1.00 37.65  ? 230 ILE C C   1 
ATOM   8418  O O   . ILE C 1 201 ? 5.270   67.778  29.397  1.00 35.88  ? 230 ILE C O   1 
ATOM   8419  C CB  . ILE C 1 201 ? 6.560   66.545  32.051  1.00 38.12  ? 230 ILE C CB  1 
ATOM   8420  C CG1 . ILE C 1 201 ? 7.665   66.647  33.108  1.00 40.30  ? 230 ILE C CG1 1 
ATOM   8421  C CG2 . ILE C 1 201 ? 5.877   65.189  32.074  1.00 38.93  ? 230 ILE C CG2 1 
ATOM   8422  C CD1 . ILE C 1 201 ? 8.727   65.576  33.004  1.00 40.70  ? 230 ILE C CD1 1 
ATOM   8423  N N   . ASP C 1 202 ? 5.860   65.666  28.910  1.00 35.97  ? 231 ASP C N   1 
ATOM   8424  C CA  . ASP C 1 202 ? 4.765   65.392  28.000  1.00 38.24  ? 231 ASP C CA  1 
ATOM   8425  C C   . ASP C 1 202 ? 3.845   64.375  28.668  1.00 35.43  ? 231 ASP C C   1 
ATOM   8426  O O   . ASP C 1 202 ? 4.240   63.228  28.835  1.00 33.79  ? 231 ASP C O   1 
ATOM   8427  C CB  . ASP C 1 202 ? 5.321   64.865  26.673  1.00 39.65  ? 231 ASP C CB  1 
ATOM   8428  C CG  . ASP C 1 202 ? 4.287   64.625  25.583  1.00 40.95  ? 231 ASP C CG  1 
ATOM   8429  O OD1 . ASP C 1 202 ? 3.180   64.196  25.920  1.00 33.93  ? 231 ASP C OD1 1 
ATOM   8430  O OD2 . ASP C 1 202 ? 4.637   64.788  24.392  1.00 41.39  ? 231 ASP C OD2 1 
ATOM   8431  N N   . SER C 1 203 ? 2.611   64.778  28.997  1.00 33.74  ? 232 SER C N   1 
ATOM   8432  C CA  . SER C 1 203 ? 1.745   63.968  29.845  1.00 34.65  ? 232 SER C CA  1 
ATOM   8433  C C   . SER C 1 203 ? 1.225   62.701  29.164  1.00 34.36  ? 232 SER C C   1 
ATOM   8434  O O   . SER C 1 203 ? 0.530   61.930  29.813  1.00 39.77  ? 232 SER C O   1 
ATOM   8435  C CB  . SER C 1 203 ? 0.582   64.756  30.383  1.00 40.35  ? 232 SER C CB  1 
ATOM   8436  O OG  . SER C 1 203 ? -0.474  64.865  29.431  1.00 36.94  ? 232 SER C OG  1 
ATOM   8437  N N   . ASN C 1 204 ? 1.499   62.498  27.865  1.00 32.72  ? 233 ASN C N   1 
ATOM   8438  C CA  . ASN C 1 204 ? 1.058   61.278  27.198  1.00 34.72  ? 233 ASN C CA  1 
ATOM   8439  C C   . ASN C 1 204 ? 2.222   60.289  27.105  1.00 31.45  ? 233 ASN C C   1 
ATOM   8440  O O   . ASN C 1 204 ? 2.023   59.097  26.847  1.00 35.82  ? 233 ASN C O   1 
ATOM   8441  C CB  . ASN C 1 204 ? 0.379   61.595  25.855  1.00 33.71  ? 233 ASN C CB  1 
ATOM   8442  C CG  . ASN C 1 204 ? -0.969  62.271  26.038  1.00 31.78  ? 233 ASN C CG  1 
ATOM   8443  O OD1 . ASN C 1 204 ? -1.123  63.455  25.756  1.00 33.81  ? 233 ASN C OD1 1 
ATOM   8444  N ND2 . ASN C 1 204 ? -1.936  61.555  26.585  1.00 35.01  ? 233 ASN C ND2 1 
ATOM   8445  N N   . LEU C 1 205 ? 3.435   60.778  27.366  1.00 32.13  ? 234 LEU C N   1 
ATOM   8446  C CA  . LEU C 1 205 ? 4.633   59.947  27.370  1.00 32.18  ? 234 LEU C CA  1 
ATOM   8447  C C   . LEU C 1 205 ? 4.842   59.259  28.718  1.00 30.53  ? 234 LEU C C   1 
ATOM   8448  O O   . LEU C 1 205 ? 4.449   59.754  29.764  1.00 29.27  ? 234 LEU C O   1 
ATOM   8449  C CB  . LEU C 1 205 ? 5.829   60.831  27.004  1.00 36.33  ? 234 LEU C CB  1 
ATOM   8450  C CG  . LEU C 1 205 ? 5.729   61.501  25.634  1.00 34.47  ? 234 LEU C CG  1 
ATOM   8451  C CD1 . LEU C 1 205 ? 6.997   62.284  25.318  1.00 39.69  ? 234 LEU C CD1 1 
ATOM   8452  C CD2 . LEU C 1 205 ? 5.440   60.462  24.553  1.00 34.77  ? 234 LEU C CD2 1 
ATOM   8453  N N   . ASP C 1 206 ? 5.478   58.085  28.672  1.00 29.40  ? 235 ASP C N   1 
ATOM   8454  C CA  . ASP C 1 206 ? 5.832   57.359  29.880  1.00 28.34  ? 235 ASP C CA  1 
ATOM   8455  C C   . ASP C 1 206 ? 7.062   58.015  30.511  1.00 24.67  ? 235 ASP C C   1 
ATOM   8456  O O   . ASP C 1 206 ? 7.753   58.809  29.882  1.00 26.65  ? 235 ASP C O   1 
ATOM   8457  C CB  . ASP C 1 206 ? 6.025   55.861  29.599  1.00 28.20  ? 235 ASP C CB  1 
ATOM   8458  C CG  . ASP C 1 206 ? 7.114   55.566  28.582  1.00 36.47  ? 235 ASP C CG  1 
ATOM   8459  O OD1 . ASP C 1 206 ? 6.829   55.710  27.358  1.00 39.48  ? 235 ASP C OD1 1 
ATOM   8460  O OD2 . ASP C 1 206 ? 8.243   55.213  29.008  1.00 29.21  ? 235 ASP C OD2 1 
ATOM   8461  N N   . TRP C 1 207 ? 7.268   57.704  31.803  1.00 25.32  ? 236 TRP C N   1 
ATOM   8462  C CA  . TRP C 1 207 ? 8.277   58.274  32.689  1.00 26.11  ? 236 TRP C CA  1 
ATOM   8463  C C   . TRP C 1 207 ? 9.685   58.235  32.080  1.00 23.99  ? 236 TRP C C   1 
ATOM   8464  O O   . TRP C 1 207 ? 10.353  59.258  31.984  1.00 24.53  ? 236 TRP C O   1 
ATOM   8465  C CB  . TRP C 1 207 ? 8.171   57.478  34.005  1.00 25.96  ? 236 TRP C CB  1 
ATOM   8466  C CG  . TRP C 1 207 ? 8.891   57.947  35.230  1.00 26.03  ? 236 TRP C CG  1 
ATOM   8467  C CD1 . TRP C 1 207 ? 8.688   59.087  35.955  1.00 28.02  ? 236 TRP C CD1 1 
ATOM   8468  C CD2 . TRP C 1 207 ? 9.863   57.183  35.960  1.00 25.42  ? 236 TRP C CD2 1 
ATOM   8469  N NE1 . TRP C 1 207 ? 9.500   59.101  37.056  1.00 28.12  ? 236 TRP C NE1 1 
ATOM   8470  C CE2 . TRP C 1 207 ? 10.237  57.944  37.088  1.00 27.07  ? 236 TRP C CE2 1 
ATOM   8471  C CE3 . TRP C 1 207 ? 10.477  55.943  35.751  1.00 26.48  ? 236 TRP C CE3 1 
ATOM   8472  C CZ2 . TRP C 1 207 ? 11.191  57.498  38.007  1.00 27.24  ? 236 TRP C CZ2 1 
ATOM   8473  C CZ3 . TRP C 1 207 ? 11.415  55.502  36.658  1.00 25.27  ? 236 TRP C CZ3 1 
ATOM   8474  C CH2 . TRP C 1 207 ? 11.768  56.269  37.772  1.00 25.85  ? 236 TRP C CH2 1 
ATOM   8475  N N   . SER C 1 208 ? 10.142  57.047  31.656  1.00 24.86  ? 237 SER C N   1 
ATOM   8476  C CA  . SER C 1 208 ? 11.462  56.909  31.061  1.00 26.09  ? 237 SER C CA  1 
ATOM   8477  C C   . SER C 1 208 ? 11.611  57.802  29.823  1.00 26.03  ? 237 SER C C   1 
ATOM   8478  O O   . SER C 1 208 ? 12.689  58.330  29.562  1.00 24.06  ? 237 SER C O   1 
ATOM   8479  C CB  . SER C 1 208 ? 11.765  55.476  30.666  1.00 28.65  ? 237 SER C CB  1 
ATOM   8480  O OG  . SER C 1 208 ? 11.451  54.557  31.680  1.00 24.94  ? 237 SER C OG  1 
ATOM   8481  N N   . HIS C 1 209 ? 10.545  57.965  29.028  1.00 25.43  ? 238 HIS C N   1 
ATOM   8482  C CA  . HIS C 1 209 ? 10.662  58.711  27.774  1.00 27.18  ? 238 HIS C CA  1 
ATOM   8483  C C   . HIS C 1 209 ? 10.842  60.203  28.064  1.00 25.80  ? 238 HIS C C   1 
ATOM   8484  O O   . HIS C 1 209 ? 11.670  60.880  27.461  1.00 26.22  ? 238 HIS C O   1 
ATOM   8485  C CB  . HIS C 1 209 ? 9.483   58.423  26.830  1.00 31.71  ? 238 HIS C CB  1 
ATOM   8486  C CG  . HIS C 1 209 ? 9.677   58.918  25.424  1.00 31.57  ? 238 HIS C CG  1 
ATOM   8487  N ND1 . HIS C 1 209 ? 8.885   58.456  24.393  1.00 37.07  ? 238 HIS C ND1 1 
ATOM   8488  C CD2 . HIS C 1 209 ? 10.557  59.754  24.850  1.00 33.38  ? 238 HIS C CD2 1 
ATOM   8489  C CE1 . HIS C 1 209 ? 9.257   59.025  23.254  1.00 34.78  ? 238 HIS C CE1 1 
ATOM   8490  N NE2 . HIS C 1 209 ? 10.278  59.813  23.503  1.00 33.57  ? 238 HIS C NE2 1 
ATOM   8491  N N   . ASN C 1 210 ? 10.065  60.718  29.012  1.00 26.51  ? 239 ASN C N   1 
ATOM   8492  C CA  . ASN C 1 210 ? 10.211  62.099  29.419  1.00 23.46  ? 239 ASN C CA  1 
ATOM   8493  C C   . ASN C 1 210 ? 11.613  62.298  29.999  1.00 23.10  ? 239 ASN C C   1 
ATOM   8494  O O   . ASN C 1 210 ? 12.187  63.374  29.879  1.00 23.63  ? 239 ASN C O   1 
ATOM   8495  C CB  . ASN C 1 210 ? 9.145   62.492  30.444  1.00 27.24  ? 239 ASN C CB  1 
ATOM   8496  C CG  . ASN C 1 210 ? 7.826   62.946  29.841  1.00 29.43  ? 239 ASN C CG  1 
ATOM   8497  O OD1 . ASN C 1 210 ? 7.809   63.800  28.956  1.00 28.49  ? 239 ASN C OD1 1 
ATOM   8498  N ND2 . ASN C 1 210 ? 6.718   62.421  30.350  1.00 28.13  ? 239 ASN C ND2 1 
ATOM   8499  N N   . PHE C 1 211 ? 12.161  61.246  30.620  1.00 23.26  ? 240 PHE C N   1 
ATOM   8500  C CA  . PHE C 1 211 ? 13.499  61.303  31.190  1.00 23.93  ? 240 PHE C CA  1 
ATOM   8501  C C   . PHE C 1 211 ? 14.537  61.442  30.070  1.00 25.06  ? 240 PHE C C   1 
ATOM   8502  O O   . PHE C 1 211 ? 15.320  62.369  30.059  1.00 23.43  ? 240 PHE C O   1 
ATOM   8503  C CB  . PHE C 1 211 ? 13.719  60.079  32.081  1.00 23.67  ? 240 PHE C CB  1 
ATOM   8504  C CG  . PHE C 1 211 ? 14.942  60.119  32.953  1.00 25.17  ? 240 PHE C CG  1 
ATOM   8505  C CD1 . PHE C 1 211 ? 15.553  61.313  33.287  1.00 24.68  ? 240 PHE C CD1 1 
ATOM   8506  C CD2 . PHE C 1 211 ? 15.472  58.943  33.454  1.00 29.25  ? 240 PHE C CD2 1 
ATOM   8507  C CE1 . PHE C 1 211 ? 16.687  61.331  34.081  1.00 25.76  ? 240 PHE C CE1 1 
ATOM   8508  C CE2 . PHE C 1 211 ? 16.609  58.956  34.243  1.00 29.52  ? 240 PHE C CE2 1 
ATOM   8509  C CZ  . PHE C 1 211 ? 17.210  60.149  34.558  1.00 28.15  ? 240 PHE C CZ  1 
ATOM   8510  N N   . THR C 1 212 ? 14.558  60.515  29.115  1.00 27.77  ? 241 THR C N   1 
ATOM   8511  C CA  . THR C 1 212 ? 15.551  60.563  28.043  1.00 28.98  ? 241 THR C CA  1 
ATOM   8512  C C   . THR C 1 212 ? 15.424  61.845  27.205  1.00 29.39  ? 241 THR C C   1 
ATOM   8513  O O   . THR C 1 212 ? 16.420  62.389  26.727  1.00 31.54  ? 241 THR C O   1 
ATOM   8514  C CB  . THR C 1 212 ? 15.464  59.323  27.148  1.00 28.33  ? 241 THR C CB  1 
ATOM   8515  O OG1 . THR C 1 212 ? 14.136  59.302  26.625  1.00 27.88  ? 241 THR C OG1 1 
ATOM   8516  C CG2 . THR C 1 212 ? 15.780  58.032  27.868  1.00 26.35  ? 241 THR C CG2 1 
ATOM   8517  N N   . ASN C 1 213 ? 14.202  62.348  27.031  1.00 29.17  ? 242 ASN C N   1 
ATOM   8518  C CA  . ASN C 1 213 ? 14.020  63.662  26.432  1.00 29.46  ? 242 ASN C CA  1 
ATOM   8519  C C   . ASN C 1 213 ? 14.724  64.730  27.259  1.00 27.40  ? 242 ASN C C   1 
ATOM   8520  O O   . ASN C 1 213 ? 15.472  65.556  26.732  1.00 25.40  ? 242 ASN C O   1 
ATOM   8521  C CB  . ASN C 1 213 ? 12.533  63.991  26.274  1.00 31.94  ? 242 ASN C CB  1 
ATOM   8522  C CG  . ASN C 1 213 ? 11.908  63.307  25.081  1.00 36.29  ? 242 ASN C CG  1 
ATOM   8523  O OD1 . ASN C 1 213 ? 12.616  62.934  24.144  1.00 37.42  ? 242 ASN C OD1 1 
ATOM   8524  N ND2 . ASN C 1 213 ? 10.589  63.174  25.100  1.00 37.36  ? 242 ASN C ND2 1 
ATOM   8525  N N   . MET C 1 214 ? 14.449  64.747  28.569  1.00 24.22  ? 243 MET C N   1 
ATOM   8526  C CA  . MET C 1 214 ? 14.940  65.845  29.381  1.00 24.17  ? 243 MET C CA  1 
ATOM   8527  C C   . MET C 1 214 ? 16.464  65.763  29.464  1.00 26.47  ? 243 MET C C   1 
ATOM   8528  O O   . MET C 1 214 ? 17.103  66.779  29.672  1.00 27.51  ? 243 MET C O   1 
ATOM   8529  C CB  . MET C 1 214 ? 14.333  65.827  30.792  1.00 25.46  ? 243 MET C CB  1 
ATOM   8530  C CG  . MET C 1 214 ? 13.009  66.591  30.889  1.00 26.08  ? 243 MET C CG  1 
ATOM   8531  S SD  . MET C 1 214 ? 12.283  66.610  32.544  1.00 32.06  ? 243 MET C SD  1 
ATOM   8532  C CE  . MET C 1 214 ? 12.057  64.859  32.816  1.00 25.48  ? 243 MET C CE  1 
ATOM   8533  N N   . LEU C 1 215 ? 17.032  64.560  29.287  1.00 26.35  ? 244 LEU C N   1 
ATOM   8534  C CA  . LEU C 1 215 ? 18.475  64.396  29.218  1.00 27.30  ? 244 LEU C CA  1 
ATOM   8535  C C   . LEU C 1 215 ? 19.027  64.926  27.896  1.00 30.88  ? 244 LEU C C   1 
ATOM   8536  O O   . LEU C 1 215 ? 20.194  65.313  27.833  1.00 35.30  ? 244 LEU C O   1 
ATOM   8537  C CB  . LEU C 1 215 ? 18.818  62.917  29.422  1.00 25.95  ? 244 LEU C CB  1 
ATOM   8538  C CG  . LEU C 1 215 ? 18.625  62.393  30.844  1.00 23.53  ? 244 LEU C CG  1 
ATOM   8539  C CD1 . LEU C 1 215 ? 18.784  60.882  30.885  1.00 22.16  ? 244 LEU C CD1 1 
ATOM   8540  C CD2 . LEU C 1 215 ? 19.584  63.062  31.787  1.00 23.51  ? 244 LEU C CD2 1 
ATOM   8541  N N   . GLY C 1 216 ? 18.188  64.946  26.859  1.00 29.63  ? 245 GLY C N   1 
ATOM   8542  C CA  . GLY C 1 216 ? 18.588  65.412  25.547  1.00 32.69  ? 245 GLY C CA  1 
ATOM   8543  C C   . GLY C 1 216 ? 18.944  64.256  24.624  1.00 31.78  ? 245 GLY C C   1 
ATOM   8544  O O   . GLY C 1 216 ? 19.737  64.423  23.716  1.00 37.63  ? 245 GLY C O   1 
ATOM   8545  N N   . TYR C 1 217 ? 18.331  63.110  24.875  1.00 36.49  ? 246 TYR C N   1 
ATOM   8546  C CA  . TYR C 1 217 ? 18.536  61.939  23.996  1.00 36.28  ? 246 TYR C CA  1 
ATOM   8547  C C   . TYR C 1 217 ? 17.248  61.721  23.157  1.00 39.46  ? 246 TYR C C   1 
ATOM   8548  O O   . TYR C 1 217 ? 16.166  62.059  23.642  1.00 44.13  ? 246 TYR C O   1 
ATOM   8549  C CB  . TYR C 1 217 ? 19.005  60.784  24.885  1.00 31.88  ? 246 TYR C CB  1 
ATOM   8550  C CG  . TYR C 1 217 ? 20.420  60.938  25.424  1.00 32.12  ? 246 TYR C CG  1 
ATOM   8551  C CD1 . TYR C 1 217 ? 20.718  61.880  26.399  1.00 29.19  ? 246 TYR C CD1 1 
ATOM   8552  C CD2 . TYR C 1 217 ? 21.456  60.142  24.956  1.00 32.44  ? 246 TYR C CD2 1 
ATOM   8553  C CE1 . TYR C 1 217 ? 22.002  62.034  26.887  1.00 28.50  ? 246 TYR C CE1 1 
ATOM   8554  C CE2 . TYR C 1 217 ? 22.745  60.282  25.439  1.00 31.99  ? 246 TYR C CE2 1 
ATOM   8555  C CZ  . TYR C 1 217 ? 23.017  61.229  26.409  1.00 29.49  ? 246 TYR C CZ  1 
ATOM   8556  O OH  . TYR C 1 217 ? 24.280  61.386  26.888  1.00 26.43  ? 246 TYR C OH  1 
ATOM   8557  N N   . THR C 1 218 ? 17.372  61.151  21.953  1.00 43.83  ? 247 THR C N   1 
ATOM   8558  C CA  . THR C 1 218 ? 16.180  60.975  21.088  1.00 49.89  ? 247 THR C CA  1 
ATOM   8559  C C   . THR C 1 218 ? 16.067  59.533  20.629  1.00 45.63  ? 247 THR C C   1 
ATOM   8560  O O   . THR C 1 218 ? 14.918  59.050  20.506  1.00 47.36  ? 247 THR C O   1 
ATOM   8561  C CB  . THR C 1 218 ? 16.225  61.965  19.922  1.00 56.36  ? 247 THR C CB  1 
ATOM   8562  O OG1 . THR C 1 218 ? 15.009  62.694  20.054  1.00 49.99  ? 247 THR C OG1 1 
ATOM   8563  C CG2 . THR C 1 218 ? 16.275  61.306  18.555  1.00 59.02  ? 247 THR C CG2 1 
ATOM   8564  N N   . ASP C 1 219 ? 17.196  58.855  20.398  1.00 41.87  ? 248 ASP C N   1 
ATOM   8565  C CA  . ASP C 1 219 ? 17.142  57.469  19.855  1.00 41.12  ? 248 ASP C CA  1 
ATOM   8566  C C   . ASP C 1 219 ? 16.093  56.667  20.631  1.00 39.83  ? 248 ASP C C   1 
ATOM   8567  O O   . ASP C 1 219 ? 16.304  56.424  21.838  1.00 42.06  ? 248 ASP C O   1 
ATOM   8568  C CB  . ASP C 1 219 ? 18.502  56.789  19.879  1.00 41.90  ? 248 ASP C CB  1 
ATOM   8569  C CG  . ASP C 1 219 ? 18.604  55.518  19.047  1.00 43.40  ? 248 ASP C CG  1 
ATOM   8570  O OD1 . ASP C 1 219 ? 17.627  55.196  18.338  1.00 46.99  ? 248 ASP C OD1 1 
ATOM   8571  O OD2 . ASP C 1 219 ? 19.663  54.860  19.111  1.00 44.28  ? 248 ASP C OD2 1 
ATOM   8572  N N   . HIS C 1 220 ? 14.990  56.318  19.985  1.00 39.32  ? 249 HIS C N   1 
ATOM   8573  C CA  . HIS C 1 220 ? 13.988  55.436  20.628  1.00 35.22  ? 249 HIS C CA  1 
ATOM   8574  C C   . HIS C 1 220 ? 14.703  54.262  21.291  1.00 33.33  ? 249 HIS C C   1 
ATOM   8575  O O   . HIS C 1 220 ? 14.203  53.755  22.300  1.00 34.94  ? 249 HIS C O   1 
ATOM   8576  C CB  . HIS C 1 220 ? 12.994  54.916  19.591  1.00 33.93  ? 249 HIS C CB  1 
ATOM   8577  C CG  . HIS C 1 220 ? 12.401  53.583  19.876  1.00 32.76  ? 249 HIS C CG  1 
ATOM   8578  N ND1 . HIS C 1 220 ? 12.784  52.422  19.243  1.00 35.34  ? 249 HIS C ND1 1 
ATOM   8579  C CD2 . HIS C 1 220 ? 11.433  53.239  20.716  1.00 34.70  ? 249 HIS C CD2 1 
ATOM   8580  C CE1 . HIS C 1 220 ? 12.058  51.418  19.703  1.00 33.17  ? 249 HIS C CE1 1 
ATOM   8581  N NE2 . HIS C 1 220 ? 11.222  51.896  20.590  1.00 34.72  ? 249 HIS C NE2 1 
ATOM   8582  N N   . GLN C 1 221 ? 15.842  53.853  20.741  1.00 31.38  ? 250 GLN C N   1 
ATOM   8583  C CA  . GLN C 1 221 ? 16.540  52.693  21.278  1.00 33.40  ? 250 GLN C CA  1 
ATOM   8584  C C   . GLN C 1 221 ? 17.175  52.995  22.638  1.00 30.66  ? 250 GLN C C   1 
ATOM   8585  O O   . GLN C 1 221 ? 17.247  52.133  23.508  1.00 27.82  ? 250 GLN C O   1 
ATOM   8586  C CB  . GLN C 1 221 ? 17.575  52.194  20.273  1.00 38.67  ? 250 GLN C CB  1 
ATOM   8587  C CG  . GLN C 1 221 ? 17.029  51.060  19.437  1.00 45.15  ? 250 GLN C CG  1 
ATOM   8588  C CD  . GLN C 1 221 ? 16.830  49.837  20.297  1.00 53.40  ? 250 GLN C CD  1 
ATOM   8589  O OE1 . GLN C 1 221 ? 17.790  49.294  20.838  1.00 57.82  ? 250 GLN C OE1 1 
ATOM   8590  N NE2 . GLN C 1 221 ? 15.584  49.410  20.448  1.00 56.91  ? 250 GLN C NE2 1 
ATOM   8591  N N   . PHE C 1 222 ? 17.641  54.226  22.816  1.00 28.67  ? 251 PHE C N   1 
ATOM   8592  C CA  . PHE C 1 222 ? 18.123  54.639  24.113  1.00 30.25  ? 251 PHE C CA  1 
ATOM   8593  C C   . PHE C 1 222 ? 16.954  54.711  25.088  1.00 30.09  ? 251 PHE C C   1 
ATOM   8594  O O   . PHE C 1 222 ? 17.106  54.380  26.272  1.00 28.94  ? 251 PHE C O   1 
ATOM   8595  C CB  . PHE C 1 222 ? 18.827  55.989  24.023  1.00 29.25  ? 251 PHE C CB  1 
ATOM   8596  C CG  . PHE C 1 222 ? 19.451  56.383  25.327  1.00 28.10  ? 251 PHE C CG  1 
ATOM   8597  C CD1 . PHE C 1 222 ? 20.491  55.627  25.855  1.00 29.96  ? 251 PHE C CD1 1 
ATOM   8598  C CD2 . PHE C 1 222 ? 18.990  57.477  26.041  1.00 26.93  ? 251 PHE C CD2 1 
ATOM   8599  C CE1 . PHE C 1 222 ? 21.049  55.963  27.077  1.00 31.02  ? 251 PHE C CE1 1 
ATOM   8600  C CE2 . PHE C 1 222 ? 19.548  57.802  27.261  1.00 27.46  ? 251 PHE C CE2 1 
ATOM   8601  C CZ  . PHE C 1 222 ? 20.595  57.061  27.761  1.00 30.24  ? 251 PHE C CZ  1 
ATOM   8602  N N   . THR C 1 223 ? 15.779  55.108  24.571  1.00 25.44  ? 252 THR C N   1 
ATOM   8603  C CA  . THR C 1 223 ? 14.590  55.137  25.411  1.00 25.95  ? 252 THR C CA  1 
ATOM   8604  C C   . THR C 1 223 ? 14.257  53.711  25.843  1.00 26.27  ? 252 THR C C   1 
ATOM   8605  O O   . THR C 1 223 ? 14.027  53.472  27.024  1.00 27.40  ? 252 THR C O   1 
ATOM   8606  C CB  . THR C 1 223 ? 13.442  55.913  24.755  1.00 24.38  ? 252 THR C CB  1 
ATOM   8607  O OG1 . THR C 1 223 ? 13.959  57.228  24.572  1.00 24.98  ? 252 THR C OG1 1 
ATOM   8608  C CG2 . THR C 1 223 ? 12.177  55.953  25.587  1.00 24.63  ? 252 THR C CG2 1 
ATOM   8609  N N   . GLU C 1 224 ? 14.324  52.761  24.911  1.00 23.87  ? 253 GLU C N   1 
ATOM   8610  C CA  . GLU C 1 224 ? 14.083  51.361  25.230  1.00 27.30  ? 253 GLU C CA  1 
ATOM   8611  C C   . GLU C 1 224 ? 15.105  50.877  26.264  1.00 25.88  ? 253 GLU C C   1 
ATOM   8612  O O   . GLU C 1 224 ? 14.728  50.230  27.254  1.00 24.03  ? 253 GLU C O   1 
ATOM   8613  C CB  . GLU C 1 224 ? 14.065  50.552  23.931  1.00 30.58  ? 253 GLU C CB  1 
ATOM   8614  C CG  . GLU C 1 224 ? 12.794  50.785  23.127  1.00 30.92  ? 253 GLU C CG  1 
ATOM   8615  C CD  . GLU C 1 224 ? 11.642  49.938  23.624  1.00 32.15  ? 253 GLU C CD  1 
ATOM   8616  O OE1 . GLU C 1 224 ? 11.676  48.726  23.365  1.00 32.80  ? 253 GLU C OE1 1 
ATOM   8617  O OE2 . GLU C 1 224 ? 10.781  50.472  24.362  1.00 35.59  ? 253 GLU C OE2 1 
ATOM   8618  N N   . LEU C 1 225 ? 16.384  51.248  26.075  1.00 24.83  ? 254 LEU C N   1 
ATOM   8619  C CA  . LEU C 1 225 ? 17.433  50.827  26.980  1.00 27.78  ? 254 LEU C CA  1 
ATOM   8620  C C   . LEU C 1 225 ? 17.106  51.348  28.376  1.00 25.43  ? 254 LEU C C   1 
ATOM   8621  O O   . LEU C 1 225 ? 17.218  50.613  29.350  1.00 27.50  ? 254 LEU C O   1 
ATOM   8622  C CB  . LEU C 1 225 ? 18.790  51.355  26.507  1.00 27.62  ? 254 LEU C CB  1 
ATOM   8623  C CG  . LEU C 1 225 ? 19.930  51.260  27.529  1.00 28.89  ? 254 LEU C CG  1 
ATOM   8624  C CD1 . LEU C 1 225 ? 20.212  49.805  27.891  1.00 28.31  ? 254 LEU C CD1 1 
ATOM   8625  C CD2 . LEU C 1 225 ? 21.182  51.946  27.002  1.00 29.52  ? 254 LEU C CD2 1 
ATOM   8626  N N   . THR C 1 226 ? 16.692  52.614  28.421  1.00 23.33  ? 255 THR C N   1 
ATOM   8627  C CA  . THR C 1 226 ? 16.397  53.307  29.654  1.00 24.35  ? 255 THR C CA  1 
ATOM   8628  C C   . THR C 1 226 ? 15.206  52.652  30.349  1.00 26.27  ? 255 THR C C   1 
ATOM   8629  O O   . THR C 1 226 ? 15.242  52.441  31.557  1.00 24.42  ? 255 THR C O   1 
ATOM   8630  C CB  . THR C 1 226 ? 16.195  54.798  29.376  1.00 24.46  ? 255 THR C CB  1 
ATOM   8631  O OG1 . THR C 1 226 ? 17.478  55.357  29.121  1.00 26.33  ? 255 THR C OG1 1 
ATOM   8632  C CG2 . THR C 1 226 ? 15.530  55.508  30.530  1.00 27.58  ? 255 THR C CG2 1 
ATOM   8633  N N   . ARG C 1 227 ? 14.180  52.280  29.575  1.00 27.74  ? 256 ARG C N   1 
ATOM   8634  C CA  . ARG C 1 227 ? 13.055  51.546  30.116  1.00 26.42  ? 256 ARG C CA  1 
ATOM   8635  C C   . ARG C 1 227 ? 13.551  50.248  30.749  1.00 27.30  ? 256 ARG C C   1 
ATOM   8636  O O   . ARG C 1 227 ? 13.166  49.933  31.866  1.00 24.41  ? 256 ARG C O   1 
ATOM   8637  C CB  . ARG C 1 227 ? 11.984  51.288  29.056  1.00 24.66  ? 256 ARG C CB  1 
ATOM   8638  C CG  . ARG C 1 227 ? 11.301  52.549  28.547  1.00 25.65  ? 256 ARG C CG  1 
ATOM   8639  C CD  . ARG C 1 227 ? 10.429  52.249  27.336  1.00 26.56  ? 256 ARG C CD  1 
ATOM   8640  N NE  . ARG C 1 227 ? 9.638   53.394  26.903  1.00 26.97  ? 256 ARG C NE  1 
ATOM   8641  C CZ  . ARG C 1 227 ? 9.564   53.832  25.651  1.00 27.65  ? 256 ARG C CZ  1 
ATOM   8642  N NH1 . ARG C 1 227 ? 10.145  53.162  24.671  1.00 26.53  ? 256 ARG C NH1 1 
ATOM   8643  N NH2 . ARG C 1 227 ? 8.878   54.925  25.374  1.00 28.17  ? 256 ARG C NH2 1 
ATOM   8644  N N   . LEU C 1 228 ? 14.409  49.507  30.049  1.00 24.32  ? 257 LEU C N   1 
ATOM   8645  C CA  . LEU C 1 228 ? 14.905  48.241  30.570  1.00 27.63  ? 257 LEU C CA  1 
ATOM   8646  C C   . LEU C 1 228 ? 15.778  48.444  31.812  1.00 23.84  ? 257 LEU C C   1 
ATOM   8647  O O   . LEU C 1 228 ? 15.652  47.702  32.795  1.00 27.37  ? 257 LEU C O   1 
ATOM   8648  C CB  . LEU C 1 228 ? 15.700  47.509  29.480  1.00 26.49  ? 257 LEU C CB  1 
ATOM   8649  C CG  . LEU C 1 228 ? 16.497  46.287  29.931  1.00 28.27  ? 257 LEU C CG  1 
ATOM   8650  C CD1 . LEU C 1 228 ? 15.608  45.172  30.434  1.00 30.31  ? 257 LEU C CD1 1 
ATOM   8651  C CD2 . LEU C 1 228 ? 17.336  45.775  28.776  1.00 32.30  ? 257 LEU C CD2 1 
ATOM   8652  N N   . TYR C 1 229 ? 16.700  49.408  31.732  1.00 23.99  ? 258 TYR C N   1 
ATOM   8653  C CA  . TYR C 1 229 ? 17.617  49.727  32.812  1.00 24.71  ? 258 TYR C CA  1 
ATOM   8654  C C   . TYR C 1 229 ? 16.838  50.139  34.062  1.00 24.46  ? 258 TYR C C   1 
ATOM   8655  O O   . TYR C 1 229 ? 17.022  49.550  35.113  1.00 27.42  ? 258 TYR C O   1 
ATOM   8656  C CB  . TYR C 1 229 ? 18.617  50.813  32.397  1.00 26.50  ? 258 TYR C CB  1 
ATOM   8657  C CG  . TYR C 1 229 ? 19.586  51.252  33.479  1.00 29.44  ? 258 TYR C CG  1 
ATOM   8658  C CD1 . TYR C 1 229 ? 19.168  51.998  34.579  1.00 30.72  ? 258 TYR C CD1 1 
ATOM   8659  C CD2 . TYR C 1 229 ? 20.942  50.971  33.393  1.00 31.75  ? 258 TYR C CD2 1 
ATOM   8660  C CE1 . TYR C 1 229 ? 20.057  52.417  35.566  1.00 29.85  ? 258 TYR C CE1 1 
ATOM   8661  C CE2 . TYR C 1 229 ? 21.844  51.405  34.362  1.00 30.22  ? 258 TYR C CE2 1 
ATOM   8662  C CZ  . TYR C 1 229 ? 21.403  52.134  35.455  1.00 29.10  ? 258 TYR C CZ  1 
ATOM   8663  O OH  . TYR C 1 229 ? 22.289  52.534  36.465  1.00 32.81  ? 258 TYR C OH  1 
ATOM   8664  N N   . LEU C 1 230 ? 15.919  51.104  33.953  1.00 22.17  ? 259 LEU C N   1 
ATOM   8665  C CA  . LEU C 1 230 ? 15.198  51.546  35.139  1.00 21.46  ? 259 LEU C CA  1 
ATOM   8666  C C   . LEU C 1 230 ? 14.335  50.407  35.688  1.00 22.20  ? 259 LEU C C   1 
ATOM   8667  O O   . LEU C 1 230 ? 14.123  50.334  36.898  1.00 19.99  ? 259 LEU C O   1 
ATOM   8668  C CB  . LEU C 1 230 ? 14.363  52.802  34.833  1.00 20.45  ? 259 LEU C CB  1 
ATOM   8669  C CG  . LEU C 1 230 ? 15.147  54.073  34.538  1.00 21.88  ? 259 LEU C CG  1 
ATOM   8670  C CD1 . LEU C 1 230 ? 14.207  55.202  34.181  1.00 21.61  ? 259 LEU C CD1 1 
ATOM   8671  C CD2 . LEU C 1 230 ? 16.078  54.493  35.698  1.00 20.63  ? 259 LEU C CD2 1 
ATOM   8672  N N   . THR C 1 231 ? 13.934  49.441  34.849  1.00 21.02  ? 260 THR C N   1 
ATOM   8673  C CA  . THR C 1 231 ? 13.156  48.321  35.353  1.00 22.19  ? 260 THR C CA  1 
ATOM   8674  C C   . THR C 1 231 ? 14.019  47.372  36.189  1.00 23.51  ? 260 THR C C   1 
ATOM   8675  O O   . THR C 1 231 ? 13.599  46.986  37.275  1.00 22.15  ? 260 THR C O   1 
ATOM   8676  C CB  . THR C 1 231 ? 12.436  47.593  34.209  1.00 22.56  ? 260 THR C CB  1 
ATOM   8677  O OG1 . THR C 1 231 ? 11.415  48.488  33.785  1.00 23.01  ? 260 THR C OG1 1 
ATOM   8678  C CG2 . THR C 1 231 ? 11.847  46.255  34.585  1.00 22.51  ? 260 THR C CG2 1 
ATOM   8679  N N   . ILE C 1 232 ? 15.192  46.967  35.677  1.00 24.28  ? 261 ILE C N   1 
ATOM   8680  C CA  . ILE C 1 232 ? 15.975  45.911  36.310  1.00 25.69  ? 261 ILE C CA  1 
ATOM   8681  C C   . ILE C 1 232 ? 16.826  46.421  37.477  1.00 22.95  ? 261 ILE C C   1 
ATOM   8682  O O   . ILE C 1 232 ? 17.305  45.614  38.255  1.00 22.79  ? 261 ILE C O   1 
ATOM   8683  C CB  . ILE C 1 232 ? 16.870  45.183  35.283  1.00 27.30  ? 261 ILE C CB  1 
ATOM   8684  C CG1 . ILE C 1 232 ? 18.011  46.088  34.793  1.00 27.52  ? 261 ILE C CG1 1 
ATOM   8685  C CG2 . ILE C 1 232 ? 16.021  44.614  34.173  1.00 29.30  ? 261 ILE C CG2 1 
ATOM   8686  C CD1 . ILE C 1 232 ? 18.753  45.591  33.558  1.00 28.14  ? 261 ILE C CD1 1 
ATOM   8687  N N   . HIS C 1 233 ? 17.117  47.724  37.567  1.00 20.55  ? 262 HIS C N   1 
ATOM   8688  C CA  . HIS C 1 233 ? 17.890  48.224  38.690  1.00 20.71  ? 262 HIS C CA  1 
ATOM   8689  C C   . HIS C 1 233 ? 16.965  48.572  39.862  1.00 20.17  ? 262 HIS C C   1 
ATOM   8690  O O   . HIS C 1 233 ? 17.432  49.032  40.907  1.00 20.28  ? 262 HIS C O   1 
ATOM   8691  C CB  . HIS C 1 233 ? 18.767  49.423  38.304  1.00 20.58  ? 262 HIS C CB  1 
ATOM   8692  C CG  . HIS C 1 233 ? 19.981  49.056  37.495  1.00 22.37  ? 262 HIS C CG  1 
ATOM   8693  N ND1 . HIS C 1 233 ? 19.929  48.860  36.126  1.00 23.83  ? 262 HIS C ND1 1 
ATOM   8694  C CD2 . HIS C 1 233 ? 21.278  48.871  37.845  1.00 21.50  ? 262 HIS C CD2 1 
ATOM   8695  C CE1 . HIS C 1 233 ? 21.151  48.553  35.688  1.00 23.20  ? 262 HIS C CE1 1 
ATOM   8696  N NE2 . HIS C 1 233 ? 21.976  48.577  36.708  1.00 20.25  ? 262 HIS C NE2 1 
ATOM   8697  N N   . SER C 1 234 ? 15.655  48.343  39.685  1.00 19.02  ? 263 SER C N   1 
ATOM   8698  C CA  . SER C 1 234 ? 14.643  48.883  40.581  1.00 19.58  ? 263 SER C CA  1 
ATOM   8699  C C   . SER C 1 234 ? 14.807  48.438  42.034  1.00 21.06  ? 263 SER C C   1 
ATOM   8700  O O   . SER C 1 234 ? 14.500  49.176  42.969  1.00 17.84  ? 263 SER C O   1 
ATOM   8701  C CB  . SER C 1 234 ? 13.282  48.491  40.081  1.00 18.35  ? 263 SER C CB  1 
ATOM   8702  O OG  . SER C 1 234 ? 13.086  47.077  40.206  1.00 19.46  ? 263 SER C OG  1 
ATOM   8703  N N   . ASP C 1 235 ? 15.116  47.157  42.179  1.00 18.66  ? 264 ASP C N   1 
ATOM   8704  C CA  . ASP C 1 235 ? 15.134  46.558  43.528  1.00 19.22  ? 264 ASP C CA  1 
ATOM   8705  C C   . ASP C 1 235 ? 16.025  45.317  43.530  1.00 20.98  ? 264 ASP C C   1 
ATOM   8706  O O   . ASP C 1 235 ? 16.139  44.688  42.476  1.00 23.52  ? 264 ASP C O   1 
ATOM   8707  C CB  . ASP C 1 235 ? 13.727  46.134  43.899  1.00 21.08  ? 264 ASP C CB  1 
ATOM   8708  C CG  . ASP C 1 235 ? 13.434  46.124  45.387  1.00 21.90  ? 264 ASP C CG  1 
ATOM   8709  O OD1 . ASP C 1 235 ? 13.921  47.024  46.088  1.00 21.87  ? 264 ASP C OD1 1 
ATOM   8710  O OD2 . ASP C 1 235 ? 12.654  45.261  45.815  1.00 26.42  ? 264 ASP C OD2 1 
ATOM   8711  N N   . HIS C 1 236 ? 16.610  44.994  44.680  1.00 22.43  ? 265 HIS C N   1 
ATOM   8712  C CA  . HIS C 1 236 ? 17.462  43.779  44.823  1.00 21.22  ? 265 HIS C CA  1 
ATOM   8713  C C   . HIS C 1 236 ? 17.397  43.302  46.277  1.00 18.02  ? 265 HIS C C   1 
ATOM   8714  O O   . HIS C 1 236 ? 18.443  43.245  46.920  1.00 17.85  ? 265 HIS C O   1 
ATOM   8715  C CB  . HIS C 1 236 ? 18.900  44.048  44.397  1.00 23.00  ? 265 HIS C CB  1 
ATOM   8716  C CG  . HIS C 1 236 ? 19.551  42.912  43.699  1.00 25.37  ? 265 HIS C CG  1 
ATOM   8717  N ND1 . HIS C 1 236 ? 18.903  42.157  42.752  1.00 26.37  ? 265 HIS C ND1 1 
ATOM   8718  C CD2 . HIS C 1 236 ? 20.778  42.406  43.802  1.00 24.12  ? 265 HIS C CD2 1 
ATOM   8719  C CE1 . HIS C 1 236 ? 19.730  41.228  42.311  1.00 28.58  ? 265 HIS C CE1 1 
ATOM   8720  N NE2 . HIS C 1 236 ? 20.872  41.356  42.936  1.00 28.14  ? 265 HIS C NE2 1 
ATOM   8721  N N   . GLU C 1 237 ? 16.198  42.960  46.744  1.00 17.53  ? 266 GLU C N   1 
ATOM   8722  C CA  . GLU C 1 237 ? 15.949  42.530  48.150  1.00 18.81  ? 266 GLU C CA  1 
ATOM   8723  C C   . GLU C 1 237 ? 16.302  43.677  49.113  1.00 18.34  ? 266 GLU C C   1 
ATOM   8724  O O   . GLU C 1 237 ? 16.588  44.783  48.649  1.00 17.04  ? 266 GLU C O   1 
ATOM   8725  C CB  . GLU C 1 237 ? 16.490  41.134  48.480  1.00 20.58  ? 266 GLU C CB  1 
ATOM   8726  C CG  . GLU C 1 237 ? 17.924  41.030  48.974  1.00 21.07  ? 266 GLU C CG  1 
ATOM   8727  C CD  . GLU C 1 237 ? 18.060  39.681  49.653  1.00 25.69  ? 266 GLU C CD  1 
ATOM   8728  O OE1 . GLU C 1 237 ? 17.369  38.733  49.238  1.00 26.95  ? 266 GLU C OE1 1 
ATOM   8729  O OE2 . GLU C 1 237 ? 18.838  39.598  50.613  1.00 27.05  ? 266 GLU C OE2 1 
ATOM   8730  N N   . GLY C 1 238 ? 16.239  43.423  50.413  1.00 19.49  ? 267 GLY C N   1 
ATOM   8731  C CA  . GLY C 1 238 ? 16.407  44.555  51.345  1.00 20.24  ? 267 GLY C CA  1 
ATOM   8732  C C   . GLY C 1 238 ? 17.781  44.739  51.940  1.00 22.39  ? 267 GLY C C   1 
ATOM   8733  O O   . GLY C 1 238 ? 17.998  45.770  52.560  1.00 18.27  ? 267 GLY C O   1 
ATOM   8734  N N   . GLY C 1 239 ? 18.684  43.789  51.715  1.00 21.03  ? 268 GLY C N   1 
ATOM   8735  C CA  . GLY C 1 239 ? 19.983  43.842  52.386  1.00 19.36  ? 268 GLY C CA  1 
ATOM   8736  C C   . GLY C 1 239 ? 21.046  44.566  51.611  1.00 18.83  ? 268 GLY C C   1 
ATOM   8737  O O   . GLY C 1 239 ? 22.132  44.702  52.154  1.00 20.59  ? 268 GLY C O   1 
ATOM   8738  N N   . ASN C 1 240 ? 20.765  44.930  50.367  1.00 16.77  ? 269 ASN C N   1 
ATOM   8739  C CA  . ASN C 1 240 ? 21.750  45.768  49.653  1.00 17.65  ? 269 ASN C CA  1 
ATOM   8740  C C   . ASN C 1 240 ? 21.823  47.065  50.449  1.00 18.80  ? 269 ASN C C   1 
ATOM   8741  O O   . ASN C 1 240 ? 20.836  47.417  51.093  1.00 23.93  ? 269 ASN C O   1 
ATOM   8742  C CB  . ASN C 1 240 ? 21.437  45.988  48.182  1.00 17.62  ? 269 ASN C CB  1 
ATOM   8743  C CG  . ASN C 1 240 ? 20.196  46.806  47.947  1.00 16.92  ? 269 ASN C CG  1 
ATOM   8744  O OD1 . ASN C 1 240 ? 20.253  48.038  47.959  1.00 18.17  ? 269 ASN C OD1 1 
ATOM   8745  N ND2 . ASN C 1 240 ? 19.085  46.135  47.695  1.00 18.10  ? 269 ASN C ND2 1 
ATOM   8746  N N   . VAL C 1 241 ? 22.923  47.777  50.327  1.00 17.44  ? 270 VAL C N   1 
ATOM   8747  C CA  . VAL C 1 241 ? 23.132  48.929  51.209  1.00 16.57  ? 270 VAL C CA  1 
ATOM   8748  C C   . VAL C 1 241 ? 22.064  50.005  50.991  1.00 16.36  ? 270 VAL C C   1 
ATOM   8749  O O   . VAL C 1 241 ? 21.536  50.565  51.944  1.00 17.11  ? 270 VAL C O   1 
ATOM   8750  C CB  . VAL C 1 241 ? 24.564  49.434  51.050  1.00 18.52  ? 270 VAL C CB  1 
ATOM   8751  C CG1 . VAL C 1 241 ? 24.791  50.845  51.591  1.00 18.76  ? 270 VAL C CG1 1 
ATOM   8752  C CG2 . VAL C 1 241 ? 25.519  48.449  51.676  1.00 19.16  ? 270 VAL C CG2 1 
ATOM   8753  N N   . SER C 1 242 ? 21.740  50.306  49.746  1.00 15.70  ? 271 SER C N   1 
ATOM   8754  C CA  . SER C 1 242 ? 20.843  51.426  49.437  1.00 14.85  ? 271 SER C CA  1 
ATOM   8755  C C   . SER C 1 242 ? 19.435  51.092  49.938  1.00 16.24  ? 271 SER C C   1 
ATOM   8756  O O   . SER C 1 242 ? 18.766  51.921  50.543  1.00 19.25  ? 271 SER C O   1 
ATOM   8757  C CB  . SER C 1 242 ? 20.859  51.785  47.961  1.00 14.25  ? 271 SER C CB  1 
ATOM   8758  O OG  . SER C 1 242 ? 20.574  50.647  47.115  1.00 15.34  ? 271 SER C OG  1 
ATOM   8759  N N   . ALA C 1 243 ? 19.002  49.844  49.727  1.00 15.80  ? 272 ALA C N   1 
ATOM   8760  C CA  . ALA C 1 243 ? 17.706  49.398  50.188  1.00 15.28  ? 272 ALA C CA  1 
ATOM   8761  C C   . ALA C 1 243 ? 17.664  49.355  51.712  1.00 15.78  ? 272 ALA C C   1 
ATOM   8762  O O   . ALA C 1 243 ? 16.705  49.812  52.312  1.00 16.14  ? 272 ALA C O   1 
ATOM   8763  C CB  . ALA C 1 243 ? 17.389  48.043  49.644  1.00 16.65  ? 272 ALA C CB  1 
ATOM   8764  N N   . HIS C 1 244 ? 18.669  48.711  52.326  1.00 14.77  ? 273 HIS C N   1 
ATOM   8765  C CA  . HIS C 1 244 ? 18.788  48.648  53.781  1.00 13.65  ? 273 HIS C CA  1 
ATOM   8766  C C   . HIS C 1 244 ? 18.781  50.058  54.394  1.00 14.41  ? 273 HIS C C   1 
ATOM   8767  O O   . HIS C 1 244 ? 18.075  50.314  55.369  1.00 18.00  ? 273 HIS C O   1 
ATOM   8768  C CB  . HIS C 1 244 ? 19.987  47.755  54.154  1.00 15.42  ? 273 HIS C CB  1 
ATOM   8769  C CG  . HIS C 1 244 ? 20.029  47.450  55.622  1.00 16.71  ? 273 HIS C CG  1 
ATOM   8770  N ND1 . HIS C 1 244 ? 21.115  46.875  56.247  1.00 17.47  ? 273 HIS C ND1 1 
ATOM   8771  C CD2 . HIS C 1 244 ? 19.127  47.682  56.586  1.00 18.83  ? 273 HIS C CD2 1 
ATOM   8772  C CE1 . HIS C 1 244 ? 20.851  46.738  57.542  1.00 20.45  ? 273 HIS C CE1 1 
ATOM   8773  N NE2 . HIS C 1 244 ? 19.647  47.228  57.771  1.00 19.36  ? 273 HIS C NE2 1 
ATOM   8774  N N   . THR C 1 245 ? 19.529  50.977  53.812  1.00 13.34  ? 274 THR C N   1 
ATOM   8775  C CA  . THR C 1 245 ? 19.631  52.324  54.344  1.00 14.88  ? 274 THR C CA  1 
ATOM   8776  C C   . THR C 1 245 ? 18.244  52.964  54.351  1.00 14.34  ? 274 THR C C   1 
ATOM   8777  O O   . THR C 1 245 ? 17.844  53.504  55.398  1.00 14.95  ? 274 THR C O   1 
ATOM   8778  C CB  . THR C 1 245 ? 20.703  53.117  53.594  1.00 15.34  ? 274 THR C CB  1 
ATOM   8779  O OG1 . THR C 1 245 ? 21.994  52.571  53.845  1.00 15.28  ? 274 THR C OG1 1 
ATOM   8780  C CG2 . THR C 1 245 ? 20.781  54.577  53.996  1.00 15.05  ? 274 THR C CG2 1 
ATOM   8781  N N   . SER C 1 246 ? 17.535  52.850  53.223  1.00 14.20  ? 275 SER C N   1 
ATOM   8782  C CA  . SER C 1 246 ? 16.198  53.424  53.073  1.00 15.47  ? 275 SER C CA  1 
ATOM   8783  C C   . SER C 1 246 ? 15.299  52.840  54.156  1.00 16.26  ? 275 SER C C   1 
ATOM   8784  O O   . SER C 1 246 ? 14.522  53.525  54.807  1.00 17.26  ? 275 SER C O   1 
ATOM   8785  C CB  . SER C 1 246 ? 15.621  53.206  51.697  1.00 16.47  ? 275 SER C CB  1 
ATOM   8786  O OG  . SER C 1 246 ? 15.247  51.826  51.502  1.00 17.96  ? 275 SER C OG  1 
ATOM   8787  N N   . HIS C 1 247 ? 15.388  51.519  54.338  1.00 14.37  ? 276 HIS C N   1 
ATOM   8788  C CA  . HIS C 1 247 ? 14.576  50.830  55.323  1.00 17.37  ? 276 HIS C CA  1 
ATOM   8789  C C   . HIS C 1 247 ? 14.855  51.314  56.749  1.00 15.80  ? 276 HIS C C   1 
ATOM   8790  O O   . HIS C 1 247 ? 13.949  51.582  57.520  1.00 17.43  ? 276 HIS C O   1 
ATOM   8791  C CB  . HIS C 1 247 ? 14.903  49.339  55.218  1.00 17.29  ? 276 HIS C CB  1 
ATOM   8792  C CG  . HIS C 1 247 ? 13.979  48.376  55.900  1.00 20.78  ? 276 HIS C CG  1 
ATOM   8793  N ND1 . HIS C 1 247 ? 14.313  47.715  57.066  1.00 21.50  ? 276 HIS C ND1 1 
ATOM   8794  C CD2 . HIS C 1 247 ? 12.748  47.966  55.581  1.00 19.72  ? 276 HIS C CD2 1 
ATOM   8795  C CE1 . HIS C 1 247 ? 13.316  46.895  57.369  1.00 21.11  ? 276 HIS C CE1 1 
ATOM   8796  N NE2 . HIS C 1 247 ? 12.361  47.055  56.499  1.00 23.44  ? 276 HIS C NE2 1 
ATOM   8797  N N   . LEU C 1 248 ? 16.149  51.410  57.099  1.00 16.47  ? 277 LEU C N   1 
ATOM   8798  C CA  . LEU C 1 248 ? 16.615  51.700  58.447  1.00 16.78  ? 277 LEU C CA  1 
ATOM   8799  C C   . LEU C 1 248 ? 16.241  53.134  58.831  1.00 15.44  ? 277 LEU C C   1 
ATOM   8800  O O   . LEU C 1 248 ? 15.695  53.386  59.893  1.00 17.46  ? 277 LEU C O   1 
ATOM   8801  C CB  . LEU C 1 248 ? 18.132  51.460  58.410  1.00 18.60  ? 277 LEU C CB  1 
ATOM   8802  C CG  . LEU C 1 248 ? 18.962  52.089  59.519  1.00 20.23  ? 277 LEU C CG  1 
ATOM   8803  C CD1 . LEU C 1 248 ? 18.538  51.575  60.885  1.00 21.72  ? 277 LEU C CD1 1 
ATOM   8804  C CD2 . LEU C 1 248 ? 20.444  51.796  59.262  1.00 20.38  ? 277 LEU C CD2 1 
ATOM   8805  N N   . VAL C 1 249 ? 16.472  54.049  57.902  1.00 16.91  ? 278 VAL C N   1 
ATOM   8806  C CA  . VAL C 1 249 ? 16.166  55.453  58.125  1.00 15.41  ? 278 VAL C CA  1 
ATOM   8807  C C   . VAL C 1 249 ? 14.658  55.628  58.185  1.00 18.47  ? 278 VAL C C   1 
ATOM   8808  O O   . VAL C 1 249 ? 14.132  56.319  59.088  1.00 19.78  ? 278 VAL C O   1 
ATOM   8809  C CB  . VAL C 1 249 ? 16.836  56.301  57.032  1.00 15.15  ? 278 VAL C CB  1 
ATOM   8810  C CG1 . VAL C 1 249 ? 16.309  57.741  57.040  1.00 14.43  ? 278 VAL C CG1 1 
ATOM   8811  C CG2 . VAL C 1 249 ? 18.339  56.256  57.215  1.00 15.22  ? 278 VAL C CG2 1 
ATOM   8812  N N   . GLY C 1 250 ? 13.967  54.991  57.239  1.00 14.65  ? 279 GLY C N   1 
ATOM   8813  C CA  . GLY C 1 250 ? 12.515  55.025  57.209  1.00 15.72  ? 279 GLY C CA  1 
ATOM   8814  C C   . GLY C 1 250 ? 11.890  54.459  58.487  1.00 16.23  ? 279 GLY C C   1 
ATOM   8815  O O   . GLY C 1 250 ? 10.780  54.809  58.856  1.00 15.36  ? 279 GLY C O   1 
ATOM   8816  N N   . SER C 1 251 ? 12.535  53.456  59.098  1.00 17.25  ? 280 SER C N   1 
ATOM   8817  C CA  . SER C 1 251 ? 11.974  52.851  60.301  1.00 18.47  ? 280 SER C CA  1 
ATOM   8818  C C   . SER C 1 251 ? 11.889  53.828  61.476  1.00 17.42  ? 280 SER C C   1 
ATOM   8819  O O   . SER C 1 251 ? 11.199  53.490  62.433  1.00 20.47  ? 280 SER C O   1 
ATOM   8820  C CB  . SER C 1 251 ? 12.700  51.624  60.710  1.00 17.51  ? 280 SER C CB  1 
ATOM   8821  O OG  . SER C 1 251 ? 13.969  51.941  61.220  1.00 16.60  ? 280 SER C OG  1 
ATOM   8822  N N   . ALA C 1 252 ? 12.624  54.966  61.425  1.00 16.05  ? 281 ALA C N   1 
ATOM   8823  C CA  . ALA C 1 252 ? 12.552  56.035  62.416  1.00 18.50  ? 281 ALA C CA  1 
ATOM   8824  C C   . ALA C 1 252 ? 11.435  57.018  62.068  1.00 19.12  ? 281 ALA C C   1 
ATOM   8825  O O   . ALA C 1 252 ? 11.274  57.981  62.824  1.00 20.09  ? 281 ALA C O   1 
ATOM   8826  C CB  . ALA C 1 252 ? 13.868  56.804  62.515  1.00 19.50  ? 281 ALA C CB  1 
ATOM   8827  N N   . LEU C 1 253 ? 10.686  56.742  60.977  1.00 19.43  ? 282 LEU C N   1 
ATOM   8828  C CA  . LEU C 1 253 ? 9.571   57.539  60.449  1.00 21.70  ? 282 LEU C CA  1 
ATOM   8829  C C   . LEU C 1 253 ? 10.079  58.826  59.788  1.00 21.80  ? 282 LEU C C   1 
ATOM   8830  O O   . LEU C 1 253 ? 9.333   59.777  59.541  1.00 20.81  ? 282 LEU C O   1 
ATOM   8831  C CB  . LEU C 1 253 ? 8.521   57.829  61.528  1.00 21.26  ? 282 LEU C CB  1 
ATOM   8832  C CG  . LEU C 1 253 ? 7.829   56.613  62.148  1.00 22.08  ? 282 LEU C CG  1 
ATOM   8833  C CD1 . LEU C 1 253 ? 6.613   57.061  62.954  1.00 21.36  ? 282 LEU C CD1 1 
ATOM   8834  C CD2 . LEU C 1 253 ? 7.429   55.575  61.119  1.00 23.10  ? 282 LEU C CD2 1 
ATOM   8835  N N   . SER C 1 254 ? 11.360  58.845  59.429  1.00 20.53  ? 283 SER C N   1 
ATOM   8836  C CA  . SER C 1 254 ? 11.860  59.839  58.508  1.00 21.94  ? 283 SER C CA  1 
ATOM   8837  C C   . SER C 1 254 ? 11.108  59.716  57.183  1.00 20.46  ? 283 SER C C   1 
ATOM   8838  O O   . SER C 1 254 ? 10.751  58.630  56.726  1.00 18.30  ? 283 SER C O   1 
ATOM   8839  C CB  . SER C 1 254 ? 13.358  59.719  58.313  1.00 20.32  ? 283 SER C CB  1 
ATOM   8840  O OG  . SER C 1 254 ? 14.033  60.030  59.502  1.00 23.06  ? 283 SER C OG  1 
ATOM   8841  N N   . ASP C 1 255 ? 10.798  60.852  56.583  1.00 20.30  ? 284 ASP C N   1 
ATOM   8842  C CA  . ASP C 1 255 ? 9.924   60.837  55.423  1.00 23.00  ? 284 ASP C CA  1 
ATOM   8843  C C   . ASP C 1 255 ? 10.642  60.194  54.236  1.00 21.56  ? 284 ASP C C   1 
ATOM   8844  O O   . ASP C 1 255 ? 11.860  59.999  54.292  1.00 24.54  ? 284 ASP C O   1 
ATOM   8845  C CB  . ASP C 1 255 ? 9.403   62.250  55.128  1.00 21.89  ? 284 ASP C CB  1 
ATOM   8846  C CG  . ASP C 1 255 ? 10.535  63.177  54.733  1.00 25.14  ? 284 ASP C CG  1 
ATOM   8847  O OD1 . ASP C 1 255 ? 11.143  62.912  53.663  1.00 24.38  ? 284 ASP C OD1 1 
ATOM   8848  O OD2 . ASP C 1 255 ? 10.791  64.150  55.480  1.00 25.01  ? 284 ASP C OD2 1 
ATOM   8849  N N   . PRO C 1 256 ? 9.918   59.801  53.168  1.00 20.38  ? 285 PRO C N   1 
ATOM   8850  C CA  . PRO C 1 256 ? 10.528  59.213  51.977  1.00 19.05  ? 285 PRO C CA  1 
ATOM   8851  C C   . PRO C 1 256 ? 11.646  60.035  51.357  1.00 17.47  ? 285 PRO C C   1 
ATOM   8852  O O   . PRO C 1 256 ? 12.608  59.470  50.864  1.00 20.74  ? 285 PRO C O   1 
ATOM   8853  C CB  . PRO C 1 256 ? 9.364   59.122  50.993  1.00 18.67  ? 285 PRO C CB  1 
ATOM   8854  C CG  . PRO C 1 256 ? 8.178   58.921  51.882  1.00 21.06  ? 285 PRO C CG  1 
ATOM   8855  C CD  . PRO C 1 256 ? 8.456   59.872  53.016  1.00 21.32  ? 285 PRO C CD  1 
ATOM   8856  N N   . TYR C 1 257 ? 11.547  61.366  51.379  1.00 17.17  ? 286 TYR C N   1 
ATOM   8857  C CA  . TYR C 1 257 ? 12.629  62.150  50.808  1.00 17.99  ? 286 TYR C CA  1 
ATOM   8858  C C   . TYR C 1 257 ? 13.929  61.944  51.592  1.00 17.26  ? 286 TYR C C   1 
ATOM   8859  O O   . TYR C 1 257 ? 14.998  61.733  51.030  1.00 15.85  ? 286 TYR C O   1 
ATOM   8860  C CB  . TYR C 1 257 ? 12.253  63.634  50.781  1.00 19.56  ? 286 TYR C CB  1 
ATOM   8861  C CG  . TYR C 1 257 ? 11.102  63.964  49.867  1.00 23.19  ? 286 TYR C CG  1 
ATOM   8862  C CD1 . TYR C 1 257 ? 11.323  64.227  48.523  1.00 23.86  ? 286 TYR C CD1 1 
ATOM   8863  C CD2 . TYR C 1 257 ? 9.792   64.017  50.326  1.00 23.44  ? 286 TYR C CD2 1 
ATOM   8864  C CE1 . TYR C 1 257 ? 10.291  64.559  47.671  1.00 23.39  ? 286 TYR C CE1 1 
ATOM   8865  C CE2 . TYR C 1 257 ? 8.743   64.357  49.483  1.00 21.89  ? 286 TYR C CE2 1 
ATOM   8866  C CZ  . TYR C 1 257 ? 8.994   64.631  48.147  1.00 23.22  ? 286 TYR C CZ  1 
ATOM   8867  O OH  . TYR C 1 257 ? 7.995   64.926  47.240  1.00 24.86  ? 286 TYR C OH  1 
ATOM   8868  N N   . LEU C 1 258 ? 13.860  62.031  52.924  1.00 17.86  ? 287 LEU C N   1 
ATOM   8869  C CA  . LEU C 1 258 ? 15.025  61.825  53.773  1.00 17.34  ? 287 LEU C CA  1 
ATOM   8870  C C   . LEU C 1 258 ? 15.530  60.395  53.581  1.00 15.90  ? 287 LEU C C   1 
ATOM   8871  O O   . LEU C 1 258 ? 16.739  60.184  53.541  1.00 18.10  ? 287 LEU C O   1 
ATOM   8872  C CB  . LEU C 1 258 ? 14.609  62.046  55.231  1.00 19.10  ? 287 LEU C CB  1 
ATOM   8873  C CG  . LEU C 1 258 ? 14.214  63.461  55.638  1.00 19.36  ? 287 LEU C CG  1 
ATOM   8874  C CD1 . LEU C 1 258 ? 14.082  63.544  57.139  1.00 19.89  ? 287 LEU C CD1 1 
ATOM   8875  C CD2 . LEU C 1 258 ? 15.195  64.526  55.154  1.00 21.22  ? 287 LEU C CD2 1 
ATOM   8876  N N   . SER C 1 259 ? 14.587  59.439  53.544  1.00 17.93  ? 288 SER C N   1 
ATOM   8877  C CA  . SER C 1 259 ? 14.884  58.011  53.491  1.00 19.45  ? 288 SER C CA  1 
ATOM   8878  C C   . SER C 1 259 ? 15.641  57.629  52.225  1.00 18.88  ? 288 SER C C   1 
ATOM   8879  O O   . SER C 1 259 ? 16.611  56.856  52.257  1.00 15.77  ? 288 SER C O   1 
ATOM   8880  C CB  . SER C 1 259 ? 13.620  57.182  53.549  1.00 20.58  ? 288 SER C CB  1 
ATOM   8881  O OG  . SER C 1 259 ? 13.034  57.275  54.823  1.00 21.62  ? 288 SER C OG  1 
ATOM   8882  N N   . PHE C 1 260 ? 15.130  58.150  51.116  1.00 19.83  ? 289 PHE C N   1 
ATOM   8883  C CA  . PHE C 1 260 ? 15.730  57.963  49.813  1.00 18.42  ? 289 PHE C CA  1 
ATOM   8884  C C   . PHE C 1 260 ? 17.087  58.686  49.696  1.00 18.40  ? 289 PHE C C   1 
ATOM   8885  O O   . PHE C 1 260 ? 18.047  58.175  49.110  1.00 20.19  ? 289 PHE C O   1 
ATOM   8886  C CB  . PHE C 1 260 ? 14.764  58.484  48.752  1.00 18.73  ? 289 PHE C CB  1 
ATOM   8887  C CG  . PHE C 1 260 ? 15.304  58.240  47.374  1.00 17.86  ? 289 PHE C CG  1 
ATOM   8888  C CD1 . PHE C 1 260 ? 15.405  56.934  46.905  1.00 17.80  ? 289 PHE C CD1 1 
ATOM   8889  C CD2 . PHE C 1 260 ? 15.808  59.267  46.598  1.00 17.99  ? 289 PHE C CD2 1 
ATOM   8890  C CE1 . PHE C 1 260 ? 15.903  56.682  45.636  1.00 18.03  ? 289 PHE C CE1 1 
ATOM   8891  C CE2 . PHE C 1 260 ? 16.328  59.005  45.340  1.00 18.11  ? 289 PHE C CE2 1 
ATOM   8892  C CZ  . PHE C 1 260 ? 16.366  57.717  44.859  1.00 17.59  ? 289 PHE C CZ  1 
ATOM   8893  N N   . ALA C 1 261 ? 17.176  59.940  50.156  1.00 16.31  ? 290 ALA C N   1 
ATOM   8894  C CA  . ALA C 1 261 ? 18.436  60.653  50.036  1.00 17.29  ? 290 ALA C CA  1 
ATOM   8895  C C   . ALA C 1 261 ? 19.560  59.935  50.787  1.00 17.30  ? 290 ALA C C   1 
ATOM   8896  O O   . ALA C 1 261 ? 20.728  59.943  50.362  1.00 17.68  ? 290 ALA C O   1 
ATOM   8897  C CB  . ALA C 1 261 ? 18.259  62.082  50.492  1.00 15.98  ? 290 ALA C CB  1 
ATOM   8898  N N   . ALA C 1 262 ? 19.211  59.323  51.922  1.00 15.85  ? 291 ALA C N   1 
ATOM   8899  C CA  . ALA C 1 262 ? 20.175  58.590  52.713  1.00 16.69  ? 291 ALA C CA  1 
ATOM   8900  C C   . ALA C 1 262 ? 20.628  57.353  51.939  1.00 16.26  ? 291 ALA C C   1 
ATOM   8901  O O   . ALA C 1 262 ? 21.813  57.022  51.963  1.00 16.13  ? 291 ALA C O   1 
ATOM   8902  C CB  . ALA C 1 262 ? 19.549  58.241  54.028  1.00 16.62  ? 291 ALA C CB  1 
ATOM   8903  N N   . ALA C 1 263 ? 19.681  56.733  51.235  1.00 16.13  ? 292 ALA C N   1 
ATOM   8904  C CA  . ALA C 1 263 ? 19.943  55.572  50.384  1.00 16.71  ? 292 ALA C CA  1 
ATOM   8905  C C   . ALA C 1 263 ? 20.890  55.935  49.246  1.00 18.49  ? 292 ALA C C   1 
ATOM   8906  O O   . ALA C 1 263 ? 21.758  55.153  48.883  1.00 17.49  ? 292 ALA C O   1 
ATOM   8907  C CB  . ALA C 1 263 ? 18.655  54.990  49.832  1.00 16.04  ? 292 ALA C CB  1 
ATOM   8908  N N   . MET C 1 264 ? 20.766  57.148  48.706  1.00 17.09  ? 293 MET C N   1 
ATOM   8909  C CA  . MET C 1 264 ? 21.654  57.584  47.639  1.00 16.69  ? 293 MET C CA  1 
ATOM   8910  C C   . MET C 1 264 ? 23.067  57.786  48.190  1.00 15.86  ? 293 MET C C   1 
ATOM   8911  O O   . MET C 1 264 ? 24.026  57.520  47.488  1.00 21.07  ? 293 MET C O   1 
ATOM   8912  C CB  . MET C 1 264 ? 21.110  58.877  47.020  1.00 16.94  ? 293 MET C CB  1 
ATOM   8913  C CG  . MET C 1 264 ? 19.813  58.636  46.244  1.00 19.49  ? 293 MET C CG  1 
ATOM   8914  S SD  . MET C 1 264 ? 19.924  57.344  44.963  1.00 20.75  ? 293 MET C SD  1 
ATOM   8915  C CE  . MET C 1 264 ? 19.336  55.925  45.892  1.00 22.06  ? 293 MET C CE  1 
ATOM   8916  N N   . ASN C 1 265 ? 23.215  58.231  49.439  1.00 16.71  ? 294 ASN C N   1 
ATOM   8917  C CA  . ASN C 1 265 ? 24.554  58.369  50.017  1.00 19.43  ? 294 ASN C CA  1 
ATOM   8918  C C   . ASN C 1 265 ? 25.205  56.986  50.144  1.00 18.09  ? 294 ASN C C   1 
ATOM   8919  O O   . ASN C 1 265 ? 26.413  56.869  50.029  1.00 18.26  ? 294 ASN C O   1 
ATOM   8920  C CB  . ASN C 1 265 ? 24.550  59.154  51.331  1.00 21.49  ? 294 ASN C CB  1 
ATOM   8921  C CG  . ASN C 1 265 ? 24.377  60.636  51.104  1.00 24.53  ? 294 ASN C CG  1 
ATOM   8922  O OD1 . ASN C 1 265 ? 24.208  61.089  49.978  1.00 24.94  ? 294 ASN C OD1 1 
ATOM   8923  N ND2 . ASN C 1 265 ? 24.425  61.406  52.169  1.00 27.72  ? 294 ASN C ND2 1 
ATOM   8924  N N   . GLY C 1 266 ? 24.402  55.941  50.331  1.00 18.50  ? 295 GLY C N   1 
ATOM   8925  C CA  . GLY C 1 266 ? 24.956  54.591  50.329  1.00 19.30  ? 295 GLY C CA  1 
ATOM   8926  C C   . GLY C 1 266 ? 25.267  54.073  48.915  1.00 20.42  ? 295 GLY C C   1 
ATOM   8927  O O   . GLY C 1 266 ? 26.317  53.474  48.673  1.00 21.77  ? 295 GLY C O   1 
ATOM   8928  N N   . LEU C 1 267 ? 24.340  54.301  47.996  1.00 18.47  ? 296 LEU C N   1 
ATOM   8929  C CA  . LEU C 1 267 ? 24.516  53.939  46.588  1.00 19.13  ? 296 LEU C CA  1 
ATOM   8930  C C   . LEU C 1 267 ? 25.774  54.593  46.008  1.00 20.47  ? 296 LEU C C   1 
ATOM   8931  O O   . LEU C 1 267 ? 26.459  53.975  45.189  1.00 20.55  ? 296 LEU C O   1 
ATOM   8932  C CB  . LEU C 1 267 ? 23.247  54.298  45.814  1.00 20.35  ? 296 LEU C CB  1 
ATOM   8933  C CG  . LEU C 1 267 ? 23.117  53.737  44.398  1.00 22.04  ? 296 LEU C CG  1 
ATOM   8934  C CD1 . LEU C 1 267 ? 22.912  52.222  44.427  1.00 23.40  ? 296 LEU C CD1 1 
ATOM   8935  C CD2 . LEU C 1 267 ? 21.990  54.399  43.647  1.00 21.71  ? 296 LEU C CD2 1 
ATOM   8936  N N   . ALA C 1 268 ? 26.079  55.835  46.420  1.00 19.90  ? 297 ALA C N   1 
ATOM   8937  C CA  . ALA C 1 268 ? 27.287  56.518  45.984  1.00 19.99  ? 297 ALA C CA  1 
ATOM   8938  C C   . ALA C 1 268 ? 28.583  55.827  46.429  1.00 24.12  ? 297 ALA C C   1 
ATOM   8939  O O   . ALA C 1 268 ? 29.639  56.219  45.941  1.00 24.36  ? 297 ALA C O   1 
ATOM   8940  C CB  . ALA C 1 268 ? 27.270  57.943  46.465  1.00 20.78  ? 297 ALA C CB  1 
ATOM   8941  N N   . GLY C 1 269 ? 28.530  54.852  47.359  1.00 21.70  ? 298 GLY C N   1 
ATOM   8942  C CA  . GLY C 1 269 ? 29.732  54.176  47.832  1.00 21.06  ? 298 GLY C CA  1 
ATOM   8943  C C   . GLY C 1 269 ? 30.416  53.369  46.728  1.00 22.02  ? 298 GLY C C   1 
ATOM   8944  O O   . GLY C 1 269 ? 29.779  52.686  45.947  1.00 23.10  ? 298 GLY C O   1 
ATOM   8945  N N   . PRO C 1 270 ? 31.756  53.399  46.609  1.00 24.31  ? 299 PRO C N   1 
ATOM   8946  C CA  . PRO C 1 270 ? 32.440  52.531  45.644  1.00 23.15  ? 299 PRO C CA  1 
ATOM   8947  C C   . PRO C 1 270 ? 32.072  51.046  45.657  1.00 25.06  ? 299 PRO C C   1 
ATOM   8948  O O   . PRO C 1 270 ? 32.125  50.413  44.609  1.00 26.92  ? 299 PRO C O   1 
ATOM   8949  C CB  . PRO C 1 270 ? 33.907  52.710  46.035  1.00 23.99  ? 299 PRO C CB  1 
ATOM   8950  C CG  . PRO C 1 270 ? 33.963  54.140  46.536  1.00 22.48  ? 299 PRO C CG  1 
ATOM   8951  C CD  . PRO C 1 270 ? 32.672  54.321  47.309  1.00 21.90  ? 299 PRO C CD  1 
ATOM   8952  N N   . LEU C 1 271 ? 31.693  50.486  46.813  1.00 22.62  ? 300 LEU C N   1 
ATOM   8953  C CA  . LEU C 1 271 ? 31.424  49.054  46.893  1.00 21.72  ? 300 LEU C CA  1 
ATOM   8954  C C   . LEU C 1 271 ? 29.962  48.759  46.563  1.00 23.08  ? 300 LEU C C   1 
ATOM   8955  O O   . LEU C 1 271 ? 29.570  47.606  46.558  1.00 26.38  ? 300 LEU C O   1 
ATOM   8956  C CB  . LEU C 1 271 ? 31.802  48.548  48.291  1.00 23.86  ? 300 LEU C CB  1 
ATOM   8957  C CG  . LEU C 1 271 ? 33.301  48.584  48.619  1.00 25.54  ? 300 LEU C CG  1 
ATOM   8958  C CD1 . LEU C 1 271 ? 33.587  47.853  49.922  1.00 23.31  ? 300 LEU C CD1 1 
ATOM   8959  C CD2 . LEU C 1 271 ? 34.127  47.983  47.495  1.00 28.33  ? 300 LEU C CD2 1 
ATOM   8960  N N   . HIS C 1 272 ? 29.235  49.814  46.203  1.00 25.09  ? 301 HIS C N   1 
ATOM   8961  C CA  . HIS C 1 272 ? 27.823  49.656  45.794  1.00 23.20  ? 301 HIS C CA  1 
ATOM   8962  C C   . HIS C 1 272 ? 27.600  50.166  44.375  1.00 25.67  ? 301 HIS C C   1 
ATOM   8963  O O   . HIS C 1 272 ? 28.051  49.490  43.455  1.00 27.35  ? 301 HIS C O   1 
ATOM   8964  C CB  . HIS C 1 272 ? 26.884  50.364  46.774  1.00 22.35  ? 301 HIS C CB  1 
ATOM   8965  C CG  . HIS C 1 272 ? 25.483  49.867  46.712  1.00 21.74  ? 301 HIS C CG  1 
ATOM   8966  N ND1 . HIS C 1 272 ? 24.438  50.444  47.395  1.00 23.19  ? 301 HIS C ND1 1 
ATOM   8967  C CD2 . HIS C 1 272 ? 24.960  48.843  46.041  1.00 22.29  ? 301 HIS C CD2 1 
ATOM   8968  C CE1 . HIS C 1 272 ? 23.334  49.772  47.133  1.00 21.60  ? 301 HIS C CE1 1 
ATOM   8969  N NE2 . HIS C 1 272 ? 23.625  48.800  46.312  1.00 22.92  ? 301 HIS C NE2 1 
ATOM   8970  N N   . GLY C 1 273 ? 27.079  51.385  44.209  1.00 31.52  ? 302 GLY C N   1 
ATOM   8971  C CA  . GLY C 1 273 ? 26.593  51.816  42.903  1.00 32.89  ? 302 GLY C CA  1 
ATOM   8972  C C   . GLY C 1 273 ? 27.660  52.460  42.017  1.00 34.97  ? 302 GLY C C   1 
ATOM   8973  O O   . GLY C 1 273 ? 27.405  52.742  40.854  1.00 37.96  ? 302 GLY C O   1 
ATOM   8974  N N   . LEU C 1 274 ? 28.864  52.682  42.550  1.00 37.19  ? 303 LEU C N   1 
ATOM   8975  C CA  . LEU C 1 274 ? 29.941  53.273  41.773  1.00 37.07  ? 303 LEU C CA  1 
ATOM   8976  C C   . LEU C 1 274 ? 30.718  52.212  40.992  1.00 39.02  ? 303 LEU C C   1 
ATOM   8977  O O   . LEU C 1 274 ? 31.702  52.563  40.356  1.00 44.83  ? 303 LEU C O   1 
ATOM   8978  C CB  . LEU C 1 274 ? 30.853  54.080  42.708  1.00 35.82  ? 303 LEU C CB  1 
ATOM   8979  C CG  . LEU C 1 274 ? 30.840  55.596  42.508  1.00 35.37  ? 303 LEU C CG  1 
ATOM   8980  C CD1 . LEU C 1 274 ? 29.472  56.177  42.828  1.00 37.25  ? 303 LEU C CD1 1 
ATOM   8981  C CD2 . LEU C 1 274 ? 31.930  56.265  43.335  1.00 36.36  ? 303 LEU C CD2 1 
ATOM   8982  N N   . ALA C 1 275 ? 30.241  50.955  40.960  1.00 35.43  ? 304 ALA C N   1 
ATOM   8983  C CA  . ALA C 1 275 ? 30.960  49.856  40.324  1.00 36.46  ? 304 ALA C CA  1 
ATOM   8984  C C   . ALA C 1 275 ? 30.883  49.879  38.792  1.00 38.26  ? 304 ALA C C   1 
ATOM   8985  O O   . ALA C 1 275 ? 31.829  49.461  38.124  1.00 40.72  ? 304 ALA C O   1 
ATOM   8986  C CB  . ALA C 1 275 ? 30.441  48.545  40.858  1.00 36.93  ? 304 ALA C CB  1 
ATOM   8987  N N   . ASN C 1 276 ? 29.743  50.295  38.228  1.00 35.10  ? 305 ASN C N   1 
ATOM   8988  C CA  . ASN C 1 276 ? 29.594  50.433  36.787  1.00 37.29  ? 305 ASN C CA  1 
ATOM   8989  C C   . ASN C 1 276 ? 30.819  51.145  36.201  1.00 32.71  ? 305 ASN C C   1 
ATOM   8990  O O   . ASN C 1 276 ? 31.345  50.705  35.177  1.00 34.45  ? 305 ASN C O   1 
ATOM   8991  C CB  . ASN C 1 276 ? 28.266  51.138  36.471  1.00 37.78  ? 305 ASN C CB  1 
ATOM   8992  C CG  . ASN C 1 276 ? 28.023  51.487  35.012  1.00 39.79  ? 305 ASN C CG  1 
ATOM   8993  O OD1 . ASN C 1 276 ? 28.893  51.357  34.150  1.00 41.70  ? 305 ASN C OD1 1 
ATOM   8994  N ND2 . ASN C 1 276 ? 26.816  51.947  34.722  1.00 38.98  ? 305 ASN C ND2 1 
ATOM   8995  N N   . GLN C 1 277 ? 31.278  52.214  36.871  1.00 31.82  ? 306 GLN C N   1 
ATOM   8996  C CA  . GLN C 1 277 ? 32.340  53.081  36.372  1.00 34.52  ? 306 GLN C CA  1 
ATOM   8997  C C   . GLN C 1 277 ? 33.709  52.401  36.422  1.00 35.57  ? 306 GLN C C   1 
ATOM   8998  O O   . GLN C 1 277 ? 34.561  52.650  35.570  1.00 29.98  ? 306 GLN C O   1 
ATOM   8999  C CB  . GLN C 1 277 ? 32.455  54.367  37.187  1.00 34.30  ? 306 GLN C CB  1 
ATOM   9000  C CG  . GLN C 1 277 ? 31.302  55.336  36.986  1.00 37.81  ? 306 GLN C CG  1 
ATOM   9001  C CD  . GLN C 1 277 ? 30.076  55.020  37.806  1.00 44.50  ? 306 GLN C CD  1 
ATOM   9002  O OE1 . GLN C 1 277 ? 29.652  53.867  37.918  1.00 48.25  ? 306 GLN C OE1 1 
ATOM   9003  N NE2 . GLN C 1 277 ? 29.489  56.057  38.387  1.00 47.06  ? 306 GLN C NE2 1 
ATOM   9004  N N   . GLU C 1 278 ? 33.940  51.590  37.457  1.00 38.06  ? 307 GLU C N   1 
ATOM   9005  C CA  . GLU C 1 278 ? 35.244  50.968  37.617  1.00 39.76  ? 307 GLU C CA  1 
ATOM   9006  C C   . GLU C 1 278 ? 35.413  49.954  36.497  1.00 36.75  ? 307 GLU C C   1 
ATOM   9007  O O   . GLU C 1 278 ? 36.498  49.821  35.941  1.00 37.04  ? 307 GLU C O   1 
ATOM   9008  C CB  . GLU C 1 278 ? 35.387  50.290  38.980  1.00 43.97  ? 307 GLU C CB  1 
ATOM   9009  C CG  . GLU C 1 278 ? 35.266  51.239  40.156  1.00 46.73  ? 307 GLU C CG  1 
ATOM   9010  C CD  . GLU C 1 278 ? 34.946  50.539  41.467  1.00 55.33  ? 307 GLU C CD  1 
ATOM   9011  O OE1 . GLU C 1 278 ? 35.703  49.600  41.829  1.00 54.79  ? 307 GLU C OE1 1 
ATOM   9012  O OE2 . GLU C 1 278 ? 33.932  50.925  42.117  1.00 55.96  ? 307 GLU C OE2 1 
ATOM   9013  N N   . VAL C 1 279 ? 34.325  49.247  36.188  1.00 33.34  ? 308 VAL C N   1 
ATOM   9014  C CA  . VAL C 1 279 ? 34.337  48.271  35.114  1.00 35.41  ? 308 VAL C CA  1 
ATOM   9015  C C   . VAL C 1 279 ? 34.769  48.962  33.831  1.00 33.65  ? 308 VAL C C   1 
ATOM   9016  O O   . VAL C 1 279 ? 35.713  48.510  33.190  1.00 34.85  ? 308 VAL C O   1 
ATOM   9017  C CB  . VAL C 1 279 ? 32.988  47.558  34.944  1.00 32.74  ? 308 VAL C CB  1 
ATOM   9018  C CG1 . VAL C 1 279 ? 32.944  46.703  33.691  1.00 34.93  ? 308 VAL C CG1 1 
ATOM   9019  C CG2 . VAL C 1 279 ? 32.682  46.714  36.162  1.00 37.78  ? 308 VAL C CG2 1 
ATOM   9020  N N   . LEU C 1 280 ? 34.093  50.063  33.499  1.00 31.61  ? 309 LEU C N   1 
ATOM   9021  C CA  . LEU C 1 280 ? 34.329  50.732  32.230  1.00 34.40  ? 309 LEU C CA  1 
ATOM   9022  C C   . LEU C 1 280 ? 35.748  51.308  32.170  1.00 34.03  ? 309 LEU C C   1 
ATOM   9023  O O   . LEU C 1 280 ? 36.386  51.203  31.131  1.00 34.94  ? 309 LEU C O   1 
ATOM   9024  C CB  . LEU C 1 280 ? 33.248  51.796  32.000  1.00 37.17  ? 309 LEU C CB  1 
ATOM   9025  C CG  . LEU C 1 280 ? 33.190  52.405  30.597  1.00 38.21  ? 309 LEU C CG  1 
ATOM   9026  C CD1 . LEU C 1 280 ? 32.989  51.332  29.531  1.00 39.69  ? 309 LEU C CD1 1 
ATOM   9027  C CD2 . LEU C 1 280 ? 32.078  53.445  30.488  1.00 41.31  ? 309 LEU C CD2 1 
ATOM   9028  N N   . VAL C 1 281 ? 36.254  51.898  33.261  1.00 37.10  ? 310 VAL C N   1 
ATOM   9029  C CA  . VAL C 1 281 ? 37.632  52.388  33.268  1.00 37.36  ? 310 VAL C CA  1 
ATOM   9030  C C   . VAL C 1 281 ? 38.571  51.203  33.006  1.00 37.39  ? 310 VAL C C   1 
ATOM   9031  O O   . VAL C 1 281 ? 39.486  51.300  32.193  1.00 36.87  ? 310 VAL C O   1 
ATOM   9032  C CB  . VAL C 1 281 ? 37.992  53.145  34.567  1.00 39.18  ? 310 VAL C CB  1 
ATOM   9033  C CG1 . VAL C 1 281 ? 39.491  53.369  34.710  1.00 41.91  ? 310 VAL C CG1 1 
ATOM   9034  C CG2 . VAL C 1 281 ? 37.268  54.477  34.703  1.00 40.29  ? 310 VAL C CG2 1 
ATOM   9035  N N   . TRP C 1 282 ? 38.303  50.052  33.638  1.00 35.88  ? 311 TRP C N   1 
ATOM   9036  C CA  . TRP C 1 282 ? 39.164  48.880  33.503  1.00 37.10  ? 311 TRP C CA  1 
ATOM   9037  C C   . TRP C 1 282 ? 39.191  48.349  32.069  1.00 34.92  ? 311 TRP C C   1 
ATOM   9038  O O   . TRP C 1 282 ? 40.240  47.944  31.570  1.00 37.29  ? 311 TRP C O   1 
ATOM   9039  C CB  . TRP C 1 282 ? 38.728  47.786  34.485  1.00 35.25  ? 311 TRP C CB  1 
ATOM   9040  C CG  . TRP C 1 282 ? 39.575  46.556  34.434  1.00 37.57  ? 311 TRP C CG  1 
ATOM   9041  C CD1 . TRP C 1 282 ? 40.869  46.428  34.843  1.00 38.61  ? 311 TRP C CD1 1 
ATOM   9042  C CD2 . TRP C 1 282 ? 39.178  45.263  33.947  1.00 39.34  ? 311 TRP C CD2 1 
ATOM   9043  N NE1 . TRP C 1 282 ? 41.305  45.148  34.640  1.00 41.48  ? 311 TRP C NE1 1 
ATOM   9044  C CE2 . TRP C 1 282 ? 40.295  44.412  34.083  1.00 37.07  ? 311 TRP C CE2 1 
ATOM   9045  C CE3 . TRP C 1 282 ? 37.998  44.748  33.402  1.00 40.00  ? 311 TRP C CE3 1 
ATOM   9046  C CZ2 . TRP C 1 282 ? 40.258  43.074  33.704  1.00 38.46  ? 311 TRP C CZ2 1 
ATOM   9047  C CZ3 . TRP C 1 282 ? 37.963  43.427  33.019  1.00 41.17  ? 311 TRP C CZ3 1 
ATOM   9048  C CH2 . TRP C 1 282 ? 39.080  42.604  33.165  1.00 42.00  ? 311 TRP C CH2 1 
ATOM   9049  N N   . LEU C 1 283 ? 38.019  48.261  31.437  1.00 37.84  ? 312 LEU C N   1 
ATOM   9050  C CA  . LEU C 1 283 ? 37.909  47.720  30.094  1.00 35.89  ? 312 LEU C CA  1 
ATOM   9051  C C   . LEU C 1 283 ? 38.652  48.639  29.124  1.00 35.36  ? 312 LEU C C   1 
ATOM   9052  O O   . LEU C 1 283 ? 39.385  48.191  28.243  1.00 37.66  ? 312 LEU C O   1 
ATOM   9053  C CB  . LEU C 1 283 ? 36.418  47.614  29.757  1.00 36.09  ? 312 LEU C CB  1 
ATOM   9054  C CG  . LEU C 1 283 ? 35.617  46.659  30.642  1.00 34.93  ? 312 LEU C CG  1 
ATOM   9055  C CD1 . LEU C 1 283 ? 34.123  46.783  30.396  1.00 33.78  ? 312 LEU C CD1 1 
ATOM   9056  C CD2 . LEU C 1 283 ? 36.071  45.227  30.413  1.00 37.92  ? 312 LEU C CD2 1 
ATOM   9057  N N   . THR C 1 284 ? 38.451  49.945  29.312  1.00 34.76  ? 313 THR C N   1 
ATOM   9058  C CA  . THR C 1 284 ? 39.066  50.966  28.483  1.00 36.46  ? 313 THR C CA  1 
ATOM   9059  C C   . THR C 1 284 ? 40.572  50.751  28.439  1.00 40.13  ? 313 THR C C   1 
ATOM   9060  O O   . THR C 1 284 ? 41.161  50.689  27.360  1.00 42.75  ? 313 THR C O   1 
ATOM   9061  C CB  . THR C 1 284 ? 38.692  52.353  29.016  1.00 36.86  ? 313 THR C CB  1 
ATOM   9062  O OG1 . THR C 1 284 ? 37.278  52.453  28.830  1.00 36.29  ? 313 THR C OG1 1 
ATOM   9063  C CG2 . THR C 1 284 ? 39.411  53.488  28.321  1.00 39.89  ? 313 THR C CG2 1 
ATOM   9064  N N   . GLN C 1 285 ? 41.165  50.617  29.627  1.00 42.94  ? 314 GLN C N   1 
ATOM   9065  C CA  . GLN C 1 285 ? 42.579  50.328  29.758  1.00 44.58  ? 314 GLN C CA  1 
ATOM   9066  C C   . GLN C 1 285 ? 42.886  49.024  29.030  1.00 40.13  ? 314 GLN C C   1 
ATOM   9067  O O   . GLN C 1 285 ? 43.746  48.990  28.163  1.00 42.74  ? 314 GLN C O   1 
ATOM   9068  C CB  . GLN C 1 285 ? 42.972  50.269  31.236  1.00 43.31  ? 314 GLN C CB  1 
ATOM   9069  C CG  . GLN C 1 285 ? 44.452  49.990  31.475  1.00 48.79  ? 314 GLN C CG  1 
ATOM   9070  C CD  . GLN C 1 285 ? 45.345  51.124  31.028  1.00 51.55  ? 314 GLN C CD  1 
ATOM   9071  O OE1 . GLN C 1 285 ? 45.115  52.290  31.341  1.00 60.75  ? 314 GLN C OE1 1 
ATOM   9072  N NE2 . GLN C 1 285 ? 46.383  50.793  30.282  1.00 49.32  ? 314 GLN C NE2 1 
ATOM   9073  N N   . LEU C 1 286 ? 42.157  47.965  29.369  1.00 37.45  ? 315 LEU C N   1 
ATOM   9074  C CA  . LEU C 1 286 ? 42.387  46.649  28.795  1.00 37.06  ? 315 LEU C CA  1 
ATOM   9075  C C   . LEU C 1 286 ? 42.389  46.685  27.257  1.00 42.89  ? 315 LEU C C   1 
ATOM   9076  O O   . LEU C 1 286 ? 43.179  45.978  26.631  1.00 38.89  ? 315 LEU C O   1 
ATOM   9077  C CB  . LEU C 1 286 ? 41.321  45.706  29.362  1.00 32.86  ? 315 LEU C CB  1 
ATOM   9078  C CG  . LEU C 1 286 ? 41.200  44.329  28.712  1.00 34.17  ? 315 LEU C CG  1 
ATOM   9079  C CD1 . LEU C 1 286 ? 42.544  43.656  28.546  1.00 38.05  ? 315 LEU C CD1 1 
ATOM   9080  C CD2 . LEU C 1 286 ? 40.297  43.434  29.537  1.00 31.71  ? 315 LEU C CD2 1 
ATOM   9081  N N   . GLN C 1 287 ? 41.517  47.498  26.639  1.00 42.37  ? 316 GLN C N   1 
ATOM   9082  C CA  . GLN C 1 287 ? 41.497  47.614  25.185  1.00 48.94  ? 316 GLN C CA  1 
ATOM   9083  C C   . GLN C 1 287 ? 42.744  48.324  24.680  1.00 50.86  ? 316 GLN C C   1 
ATOM   9084  O O   . GLN C 1 287 ? 43.114  48.173  23.518  1.00 50.28  ? 316 GLN C O   1 
ATOM   9085  C CB  . GLN C 1 287 ? 40.311  48.426  24.666  1.00 48.60  ? 316 GLN C CB  1 
ATOM   9086  C CG  . GLN C 1 287 ? 39.027  47.627  24.574  1.00 50.51  ? 316 GLN C CG  1 
ATOM   9087  C CD  . GLN C 1 287 ? 38.333  47.848  23.255  1.00 48.87  ? 316 GLN C CD  1 
ATOM   9088  O OE1 . GLN C 1 287 ? 38.143  48.980  22.808  1.00 52.48  ? 316 GLN C OE1 1 
ATOM   9089  N NE2 . GLN C 1 287 ? 37.976  46.749  22.611  1.00 48.09  ? 316 GLN C NE2 1 
ATOM   9090  N N   . LYS C 1 288 ? 43.345  49.126  25.557  1.00 52.36  ? 317 LYS C N   1 
ATOM   9091  C CA  . LYS C 1 288 ? 44.529  49.890  25.223  1.00 56.53  ? 317 LYS C CA  1 
ATOM   9092  C C   . LYS C 1 288 ? 45.753  48.983  25.355  1.00 59.22  ? 317 LYS C C   1 
ATOM   9093  O O   . LYS C 1 288 ? 46.630  49.023  24.499  1.00 66.40  ? 317 LYS C O   1 
ATOM   9094  C CB  . LYS C 1 288 ? 44.561  51.131  26.118  1.00 59.99  ? 317 LYS C CB  1 
ATOM   9095  C CG  . LYS C 1 288 ? 45.370  52.309  25.600  1.00 64.60  ? 317 LYS C CG  1 
ATOM   9096  C CD  . LYS C 1 288 ? 45.240  53.546  26.470  1.00 72.95  ? 317 LYS C CD  1 
ATOM   9097  C CE  . LYS C 1 288 ? 45.479  53.270  27.942  1.00 83.43  ? 317 LYS C CE  1 
ATOM   9098  N NZ  . LYS C 1 288 ? 45.855  54.495  28.692  1.00 85.09  ? 317 LYS C NZ  1 
ATOM   9099  N N   . GLU C 1 289 ? 45.781  48.141  26.401  1.00 60.88  ? 318 GLU C N   1 
ATOM   9100  C CA  . GLU C 1 289 ? 46.943  47.325  26.730  1.00 60.81  ? 318 GLU C CA  1 
ATOM   9101  C C   . GLU C 1 289 ? 47.034  46.094  25.832  1.00 64.12  ? 318 GLU C C   1 
ATOM   9102  O O   . GLU C 1 289 ? 48.138  45.604  25.605  1.00 70.08  ? 318 GLU C O   1 
ATOM   9103  C CB  . GLU C 1 289 ? 46.915  46.846  28.186  1.00 64.26  ? 318 GLU C CB  1 
ATOM   9104  C CG  . GLU C 1 289 ? 47.144  47.947  29.209  1.00 65.05  ? 318 GLU C CG  1 
ATOM   9105  C CD  . GLU C 1 289 ? 47.459  47.480  30.624  1.00 69.30  ? 318 GLU C CD  1 
ATOM   9106  O OE1 . GLU C 1 289 ? 46.579  46.854  31.262  1.00 63.81  ? 318 GLU C OE1 1 
ATOM   9107  O OE2 . GLU C 1 289 ? 48.591  47.746  31.093  1.00 70.68  ? 318 GLU C OE2 1 
ATOM   9108  N N   . VAL C 1 290 ? 45.884  45.568  25.377  1.00 64.05  ? 319 VAL C N   1 
ATOM   9109  C CA  . VAL C 1 290 ? 45.860  44.387  24.520  1.00 67.88  ? 319 VAL C CA  1 
ATOM   9110  C C   . VAL C 1 290 ? 45.255  44.727  23.159  1.00 65.74  ? 319 VAL C C   1 
ATOM   9111  O O   . VAL C 1 290 ? 44.928  43.826  22.388  1.00 62.18  ? 319 VAL C O   1 
ATOM   9112  C CB  . VAL C 1 290 ? 45.102  43.211  25.171  1.00 65.43  ? 319 VAL C CB  1 
ATOM   9113  C CG1 . VAL C 1 290 ? 45.565  42.970  26.600  1.00 63.85  ? 319 VAL C CG1 1 
ATOM   9114  C CG2 . VAL C 1 290 ? 43.592  43.392  25.113  1.00 65.58  ? 319 VAL C CG2 1 
ATOM   9115  N N   . GLY C 1 291 ? 45.096  46.023  22.870  1.00 67.81  ? 320 GLY C N   1 
ATOM   9116  C CA  . GLY C 1 291 ? 44.549  46.453  21.594  1.00 67.02  ? 320 GLY C CA  1 
ATOM   9117  C C   . GLY C 1 291 ? 43.062  46.131  21.459  1.00 67.62  ? 320 GLY C C   1 
ATOM   9118  O O   . GLY C 1 291 ? 42.510  45.342  22.226  1.00 65.79  ? 320 GLY C O   1 
ATOM   9119  N N   . LYS C 1 292 ? 42.445  46.728  20.432  1.00 69.62  ? 321 LYS C N   1 
ATOM   9120  C CA  . LYS C 1 292 ? 41.001  46.731  20.253  1.00 68.64  ? 321 LYS C CA  1 
ATOM   9121  C C   . LYS C 1 292 ? 40.548  45.447  19.553  1.00 65.13  ? 321 LYS C C   1 
ATOM   9122  O O   . LYS C 1 292 ? 39.358  45.266  19.305  1.00 61.12  ? 321 LYS C O   1 
ATOM   9123  C CB  . LYS C 1 292 ? 40.604  47.992  19.473  1.00 66.23  ? 321 LYS C CB  1 
ATOM   9124  C CG  . LYS C 1 292 ? 39.149  48.432  19.602  1.00 62.25  ? 321 LYS C CG  1 
ATOM   9125  C CD  . LYS C 1 292 ? 38.862  49.800  19.000  1.00 60.63  ? 321 LYS C CD  1 
ATOM   9126  C CE  . LYS C 1 292 ? 39.434  50.962  19.788  1.00 62.59  ? 321 LYS C CE  1 
ATOM   9127  N NZ  . LYS C 1 292 ? 38.541  51.370  20.897  1.00 63.67  ? 321 LYS C NZ  1 
ATOM   9128  N N   . ASP C 1 293 ? 41.503  44.567  19.232  1.00 68.24  ? 322 ASP C N   1 
ATOM   9129  C CA  . ASP C 1 293 ? 41.217  43.228  18.735  1.00 72.31  ? 322 ASP C CA  1 
ATOM   9130  C C   . ASP C 1 293 ? 42.175  42.252  19.408  1.00 70.66  ? 322 ASP C C   1 
ATOM   9131  O O   . ASP C 1 293 ? 43.386  42.372  19.229  1.00 69.65  ? 322 ASP C O   1 
ATOM   9132  C CB  . ASP C 1 293 ? 41.348  43.154  17.211  1.00 78.17  ? 322 ASP C CB  1 
ATOM   9133  C CG  . ASP C 1 293 ? 40.045  43.362  16.456  1.00 83.40  ? 322 ASP C CG  1 
ATOM   9134  O OD1 . ASP C 1 293 ? 39.238  42.411  16.427  1.00 80.85  ? 322 ASP C OD1 1 
ATOM   9135  O OD2 . ASP C 1 293 ? 39.850  44.471  15.897  1.00 86.03  ? 322 ASP C OD2 1 
ATOM   9136  N N   . VAL C 1 294 ? 41.633  41.294  20.174  1.00 62.68  ? 323 VAL C N   1 
ATOM   9137  C CA  . VAL C 1 294 ? 42.466  40.444  21.010  1.00 53.98  ? 323 VAL C CA  1 
ATOM   9138  C C   . VAL C 1 294 ? 41.949  39.010  20.951  1.00 50.80  ? 323 VAL C C   1 
ATOM   9139  O O   . VAL C 1 294 ? 40.769  38.785  20.680  1.00 52.31  ? 323 VAL C O   1 
ATOM   9140  C CB  . VAL C 1 294 ? 42.519  40.979  22.454  1.00 57.44  ? 323 VAL C CB  1 
ATOM   9141  C CG1 . VAL C 1 294 ? 41.320  40.537  23.286  1.00 58.65  ? 323 VAL C CG1 1 
ATOM   9142  C CG2 . VAL C 1 294 ? 43.814  40.588  23.145  1.00 58.08  ? 323 VAL C CG2 1 
ATOM   9143  N N   . SER C 1 295 ? 42.858  38.056  21.207  1.00 50.38  ? 324 SER C N   1 
ATOM   9144  C CA  . SER C 1 295 ? 42.582  36.629  21.112  1.00 52.13  ? 324 SER C CA  1 
ATOM   9145  C C   . SER C 1 295 ? 42.131  36.062  22.456  1.00 47.78  ? 324 SER C C   1 
ATOM   9146  O O   . SER C 1 295 ? 42.578  36.503  23.513  1.00 43.42  ? 324 SER C O   1 
ATOM   9147  C CB  . SER C 1 295 ? 43.795  35.884  20.614  1.00 53.53  ? 324 SER C CB  1 
ATOM   9148  O OG  . SER C 1 295 ? 44.258  36.445  19.396  1.00 63.06  ? 324 SER C OG  1 
ATOM   9149  N N   . ASP C 1 296 ? 41.262  35.047  22.396  1.00 50.24  ? 325 ASP C N   1 
ATOM   9150  C CA  . ASP C 1 296 ? 40.829  34.342  23.590  1.00 49.08  ? 325 ASP C CA  1 
ATOM   9151  C C   . ASP C 1 296 ? 42.068  33.948  24.382  1.00 47.72  ? 325 ASP C C   1 
ATOM   9152  O O   . ASP C 1 296 ? 42.103  34.067  25.602  1.00 44.72  ? 325 ASP C O   1 
ATOM   9153  C CB  . ASP C 1 296 ? 39.989  33.106  23.255  1.00 49.72  ? 325 ASP C CB  1 
ATOM   9154  C CG  . ASP C 1 296 ? 38.598  33.416  22.730  1.00 52.73  ? 325 ASP C CG  1 
ATOM   9155  O OD1 . ASP C 1 296 ? 38.302  34.612  22.508  1.00 55.96  ? 325 ASP C OD1 1 
ATOM   9156  O OD2 . ASP C 1 296 ? 37.814  32.459  22.561  1.00 51.46  ? 325 ASP C OD2 1 
ATOM   9157  N N   . GLU C 1 297 ? 43.083  33.507  23.635  1.00 50.36  ? 326 GLU C N   1 
ATOM   9158  C CA  . GLU C 1 297 ? 44.387  33.144  24.157  1.00 53.37  ? 326 GLU C CA  1 
ATOM   9159  C C   . GLU C 1 297 ? 45.015  34.291  24.958  1.00 48.16  ? 326 GLU C C   1 
ATOM   9160  O O   . GLU C 1 297 ? 45.363  34.128  26.127  1.00 46.47  ? 326 GLU C O   1 
ATOM   9161  C CB  . GLU C 1 297 ? 45.246  32.737  22.956  1.00 57.34  ? 326 GLU C CB  1 
ATOM   9162  C CG  . GLU C 1 297 ? 46.520  32.006  23.316  1.00 58.34  ? 326 GLU C CG  1 
ATOM   9163  C CD  . GLU C 1 297 ? 47.295  31.526  22.102  1.00 56.27  ? 326 GLU C CD  1 
ATOM   9164  O OE1 . GLU C 1 297 ? 46.863  30.533  21.475  1.00 49.12  ? 326 GLU C OE1 1 
ATOM   9165  O OE2 . GLU C 1 297 ? 48.314  32.165  21.769  1.00 59.73  ? 326 GLU C OE2 1 
ATOM   9166  N N   . LYS C 1 298 ? 45.180  35.456  24.325  1.00 45.06  ? 327 LYS C N   1 
ATOM   9167  C CA  . LYS C 1 298 ? 45.930  36.544  24.935  1.00 48.21  ? 327 LYS C CA  1 
ATOM   9168  C C   . LYS C 1 298 ? 45.100  37.228  26.020  1.00 49.15  ? 327 LYS C C   1 
ATOM   9169  O O   . LYS C 1 298 ? 45.669  37.833  26.929  1.00 53.08  ? 327 LYS C O   1 
ATOM   9170  C CB  . LYS C 1 298 ? 46.393  37.559  23.883  1.00 44.62  ? 327 LYS C CB  1 
ATOM   9171  C CG  . LYS C 1 298 ? 47.068  38.809  24.437  1.00 45.48  ? 327 LYS C CG  1 
ATOM   9172  C CD  . LYS C 1 298 ? 47.734  39.690  23.385  1.00 49.28  ? 327 LYS C CD  1 
ATOM   9173  C CE  . LYS C 1 298 ? 48.948  39.038  22.748  1.00 47.54  ? 327 LYS C CE  1 
ATOM   9174  N NZ  . LYS C 1 298 ? 49.801  40.026  22.045  1.00 51.33  ? 327 LYS C NZ  1 
ATOM   9175  N N   . LEU C 1 299 ? 43.765  37.173  25.900  1.00 50.34  ? 328 LEU C N   1 
ATOM   9176  C CA  . LEU C 1 299 ? 42.902  37.780  26.900  1.00 46.83  ? 328 LEU C CA  1 
ATOM   9177  C C   . LEU C 1 299 ? 42.963  36.937  28.173  1.00 45.84  ? 328 LEU C C   1 
ATOM   9178  O O   . LEU C 1 299 ? 43.211  37.452  29.263  1.00 41.79  ? 328 LEU C O   1 
ATOM   9179  C CB  . LEU C 1 299 ? 41.471  37.888  26.361  1.00 45.10  ? 328 LEU C CB  1 
ATOM   9180  C CG  . LEU C 1 299 ? 40.499  38.686  27.234  1.00 42.85  ? 328 LEU C CG  1 
ATOM   9181  C CD1 . LEU C 1 299 ? 40.912  40.144  27.322  1.00 42.54  ? 328 LEU C CD1 1 
ATOM   9182  C CD2 . LEU C 1 299 ? 39.074  38.580  26.710  1.00 43.77  ? 328 LEU C CD2 1 
ATOM   9183  N N   . ARG C 1 300 ? 42.763  35.625  28.017  1.00 45.26  ? 329 ARG C N   1 
ATOM   9184  C CA  . ARG C 1 300 ? 42.849  34.719  29.150  1.00 45.78  ? 329 ARG C CA  1 
ATOM   9185  C C   . ARG C 1 300 ? 44.187  34.914  29.861  1.00 47.50  ? 329 ARG C C   1 
ATOM   9186  O O   . ARG C 1 300 ? 44.251  34.871  31.089  1.00 44.27  ? 329 ARG C O   1 
ATOM   9187  C CB  . ARG C 1 300 ? 42.662  33.279  28.683  1.00 44.39  ? 329 ARG C CB  1 
ATOM   9188  C CG  . ARG C 1 300 ? 42.416  32.308  29.823  1.00 45.46  ? 329 ARG C CG  1 
ATOM   9189  C CD  . ARG C 1 300 ? 42.406  30.886  29.321  1.00 50.65  ? 329 ARG C CD  1 
ATOM   9190  N NE  . ARG C 1 300 ? 41.401  30.669  28.292  1.00 50.95  ? 329 ARG C NE  1 
ATOM   9191  C CZ  . ARG C 1 300 ? 41.666  30.465  27.007  1.00 53.16  ? 329 ARG C CZ  1 
ATOM   9192  N NH1 . ARG C 1 300 ? 42.916  30.470  26.581  1.00 57.35  ? 329 ARG C NH1 1 
ATOM   9193  N NH2 . ARG C 1 300 ? 40.682  30.251  26.152  1.00 53.71  ? 329 ARG C NH2 1 
ATOM   9194  N N   . ASP C 1 301 ? 45.246  35.154  29.074  1.00 53.51  ? 330 ASP C N   1 
ATOM   9195  C CA  . ASP C 1 301 ? 46.548  35.533  29.601  1.00 58.43  ? 330 ASP C CA  1 
ATOM   9196  C C   . ASP C 1 301 ? 46.416  36.760  30.506  1.00 60.76  ? 330 ASP C C   1 
ATOM   9197  O O   . ASP C 1 301 ? 46.879  36.738  31.644  1.00 58.26  ? 330 ASP C O   1 
ATOM   9198  C CB  . ASP C 1 301 ? 47.554  35.771  28.467  1.00 62.74  ? 330 ASP C CB  1 
ATOM   9199  C CG  . ASP C 1 301 ? 48.717  36.676  28.844  1.00 65.17  ? 330 ASP C CG  1 
ATOM   9200  O OD1 . ASP C 1 301 ? 49.573  36.223  29.624  1.00 62.17  ? 330 ASP C OD1 1 
ATOM   9201  O OD2 . ASP C 1 301 ? 48.762  37.827  28.340  1.00 67.09  ? 330 ASP C OD2 1 
ATOM   9202  N N   . TYR C 1 302 ? 45.773  37.820  29.998  1.00 59.98  ? 331 TYR C N   1 
ATOM   9203  C CA  . TYR C 1 302 ? 45.673  39.078  30.720  1.00 57.69  ? 331 TYR C CA  1 
ATOM   9204  C C   . TYR C 1 302 ? 44.886  38.919  32.026  1.00 51.99  ? 331 TYR C C   1 
ATOM   9205  O O   . TYR C 1 302 ? 45.107  39.678  32.968  1.00 49.89  ? 331 TYR C O   1 
ATOM   9206  C CB  . TYR C 1 302 ? 45.066  40.168  29.829  1.00 57.10  ? 331 TYR C CB  1 
ATOM   9207  C CG  . TYR C 1 302 ? 45.064  41.530  30.473  1.00 61.23  ? 331 TYR C CG  1 
ATOM   9208  C CD1 . TYR C 1 302 ? 44.039  41.920  31.324  1.00 62.90  ? 331 TYR C CD1 1 
ATOM   9209  C CD2 . TYR C 1 302 ? 46.125  42.405  30.293  1.00 61.03  ? 331 TYR C CD2 1 
ATOM   9210  C CE1 . TYR C 1 302 ? 44.042  43.163  31.939  1.00 62.33  ? 331 TYR C CE1 1 
ATOM   9211  C CE2 . TYR C 1 302 ? 46.154  43.642  30.917  1.00 61.91  ? 331 TYR C CE2 1 
ATOM   9212  C CZ  . TYR C 1 302 ? 45.105  44.025  31.734  1.00 61.60  ? 331 TYR C CZ  1 
ATOM   9213  O OH  . TYR C 1 302 ? 45.125  45.251  32.343  1.00 64.57  ? 331 TYR C OH  1 
ATOM   9214  N N   . ILE C 1 303 ? 43.961  37.950  32.088  1.00 51.49  ? 332 ILE C N   1 
ATOM   9215  C CA  . ILE C 1 303 ? 43.163  37.754  33.289  1.00 52.47  ? 332 ILE C CA  1 
ATOM   9216  C C   . ILE C 1 303 ? 44.063  37.178  34.386  1.00 55.60  ? 332 ILE C C   1 
ATOM   9217  O O   . ILE C 1 303 ? 44.109  37.697  35.504  1.00 55.98  ? 332 ILE C O   1 
ATOM   9218  C CB  . ILE C 1 303 ? 41.925  36.864  33.038  1.00 50.58  ? 332 ILE C CB  1 
ATOM   9219  C CG1 . ILE C 1 303 ? 41.056  37.333  31.864  1.00 50.43  ? 332 ILE C CG1 1 
ATOM   9220  C CG2 . ILE C 1 303 ? 41.108  36.743  34.316  1.00 51.54  ? 332 ILE C CG2 1 
ATOM   9221  C CD1 . ILE C 1 303 ? 40.405  38.685  32.059  1.00 49.76  ? 332 ILE C CD1 1 
ATOM   9222  N N   . TRP C 1 304 ? 44.796  36.111  34.043  1.00 56.11  ? 333 TRP C N   1 
ATOM   9223  C CA  . TRP C 1 304 ? 45.646  35.403  34.990  1.00 56.13  ? 333 TRP C CA  1 
ATOM   9224  C C   . TRP C 1 304 ? 46.696  36.331  35.604  1.00 61.78  ? 333 TRP C C   1 
ATOM   9225  O O   . TRP C 1 304 ? 47.067  36.156  36.761  1.00 62.72  ? 333 TRP C O   1 
ATOM   9226  C CB  . TRP C 1 304 ? 46.278  34.172  34.329  1.00 52.16  ? 333 TRP C CB  1 
ATOM   9227  C CG  . TRP C 1 304 ? 45.405  32.953  34.380  1.00 46.80  ? 333 TRP C CG  1 
ATOM   9228  C CD1 . TRP C 1 304 ? 44.896  32.242  33.330  1.00 44.98  ? 333 TRP C CD1 1 
ATOM   9229  C CD2 . TRP C 1 304 ? 44.945  32.287  35.568  1.00 45.24  ? 333 TRP C CD2 1 
ATOM   9230  N NE1 . TRP C 1 304 ? 44.150  31.182  33.782  1.00 44.21  ? 333 TRP C NE1 1 
ATOM   9231  C CE2 . TRP C 1 304 ? 44.162  31.188  35.153  1.00 45.33  ? 333 TRP C CE2 1 
ATOM   9232  C CE3 . TRP C 1 304 ? 45.124  32.515  36.937  1.00 45.48  ? 333 TRP C CE3 1 
ATOM   9233  C CZ2 . TRP C 1 304 ? 43.558  30.324  36.067  1.00 47.05  ? 333 TRP C CZ2 1 
ATOM   9234  C CZ3 . TRP C 1 304 ? 44.526  31.668  37.837  1.00 44.16  ? 333 TRP C CZ3 1 
ATOM   9235  C CH2 . TRP C 1 304 ? 43.758  30.586  37.406  1.00 48.17  ? 333 TRP C CH2 1 
ATOM   9236  N N   . ASN C 1 305 ? 47.163  37.326  34.842  1.00 64.34  ? 334 ASN C N   1 
ATOM   9237  C CA  . ASN C 1 305 ? 48.048  38.338  35.393  1.00 66.74  ? 334 ASN C CA  1 
ATOM   9238  C C   . ASN C 1 305 ? 47.336  39.084  36.514  1.00 67.26  ? 334 ASN C C   1 
ATOM   9239  O O   . ASN C 1 305 ? 47.826  39.128  37.637  1.00 73.95  ? 334 ASN C O   1 
ATOM   9240  C CB  . ASN C 1 305 ? 48.510  39.338  34.335  1.00 71.85  ? 334 ASN C CB  1 
ATOM   9241  C CG  . ASN C 1 305 ? 49.193  38.679  33.158  1.00 78.30  ? 334 ASN C CG  1 
ATOM   9242  O OD1 . ASN C 1 305 ? 48.748  38.819  32.022  1.00 79.40  ? 334 ASN C OD1 1 
ATOM   9243  N ND2 . ASN C 1 305 ? 50.268  37.954  33.422  1.00 81.36  ? 334 ASN C ND2 1 
ATOM   9244  N N   . THR C 1 306 ? 46.164  39.642  36.195  1.00 70.61  ? 335 THR C N   1 
ATOM   9245  C CA  . THR C 1 306 ? 45.476  40.588  37.062  1.00 67.93  ? 335 THR C CA  1 
ATOM   9246  C C   . THR C 1 306 ? 45.061  39.912  38.372  1.00 62.99  ? 335 THR C C   1 
ATOM   9247  O O   . THR C 1 306 ? 44.761  40.591  39.351  1.00 64.90  ? 335 THR C O   1 
ATOM   9248  C CB  . THR C 1 306 ? 44.303  41.228  36.303  1.00 70.00  ? 335 THR C CB  1 
ATOM   9249  O OG1 . THR C 1 306 ? 44.825  41.747  35.077  1.00 71.11  ? 335 THR C OG1 1 
ATOM   9250  C CG2 . THR C 1 306 ? 43.606  42.327  37.077  1.00 66.59  ? 335 THR C CG2 1 
ATOM   9251  N N   . LEU C 1 307 ? 45.038  38.575  38.380  1.00 55.16  ? 336 LEU C N   1 
ATOM   9252  C CA  . LEU C 1 307 ? 44.781  37.806  39.586  1.00 57.32  ? 336 LEU C CA  1 
ATOM   9253  C C   . LEU C 1 307 ? 46.083  37.593  40.364  1.00 56.52  ? 336 LEU C C   1 
ATOM   9254  O O   . LEU C 1 307 ? 46.110  37.779  41.582  1.00 51.75  ? 336 LEU C O   1 
ATOM   9255  C CB  . LEU C 1 307 ? 44.125  36.479  39.184  1.00 56.22  ? 336 LEU C CB  1 
ATOM   9256  C CG  . LEU C 1 307 ? 42.736  36.600  38.551  1.00 53.75  ? 336 LEU C CG  1 
ATOM   9257  C CD1 . LEU C 1 307 ? 42.091  35.236  38.374  1.00 55.53  ? 336 LEU C CD1 1 
ATOM   9258  C CD2 . LEU C 1 307 ? 41.831  37.510  39.374  1.00 52.87  ? 336 LEU C CD2 1 
ATOM   9259  N N   . ASN C 1 308 ? 47.164  37.234  39.655  1.00 56.90  ? 337 ASN C N   1 
ATOM   9260  C CA  . ASN C 1 308 ? 48.478  37.085  40.266  1.00 61.31  ? 337 ASN C CA  1 
ATOM   9261  C C   . ASN C 1 308 ? 48.977  38.442  40.758  1.00 67.66  ? 337 ASN C C   1 
ATOM   9262  O O   . ASN C 1 308 ? 49.850  38.507  41.619  1.00 65.14  ? 337 ASN C O   1 
ATOM   9263  C CB  . ASN C 1 308 ? 49.520  36.487  39.315  1.00 58.26  ? 337 ASN C CB  1 
ATOM   9264  C CG  . ASN C 1 308 ? 49.111  35.155  38.721  1.00 60.35  ? 337 ASN C CG  1 
ATOM   9265  O OD1 . ASN C 1 308 ? 48.507  34.323  39.395  1.00 63.12  ? 337 ASN C OD1 1 
ATOM   9266  N ND2 . ASN C 1 308 ? 49.414  34.949  37.449  1.00 55.26  ? 337 ASN C ND2 1 
ATOM   9267  N N   . SER C 1 309 ? 48.431  39.517  40.176  1.00 79.14  ? 338 SER C N   1 
ATOM   9268  C CA  . SER C 1 309 ? 48.664  40.875  40.642  1.00 89.02  ? 338 SER C CA  1 
ATOM   9269  C C   . SER C 1 309 ? 48.108  41.056  42.055  1.00 87.80  ? 338 SER C C   1 
ATOM   9270  O O   . SER C 1 309 ? 48.663  41.818  42.846  1.00 88.07  ? 338 SER C O   1 
ATOM   9271  C CB  . SER C 1 309 ? 48.059  41.869  39.673  1.00 96.46  ? 338 SER C CB  1 
ATOM   9272  O OG  . SER C 1 309 ? 48.417  43.203  40.007  1.00 103.20 ? 338 SER C OG  1 
ATOM   9273  N N   . GLY C 1 310 ? 47.013  40.340  42.359  1.00 87.18  ? 339 GLY C N   1 
ATOM   9274  C CA  . GLY C 1 310 ? 46.321  40.441  43.635  1.00 84.66  ? 339 GLY C CA  1 
ATOM   9275  C C   . GLY C 1 310 ? 44.990  41.181  43.507  1.00 80.10  ? 339 GLY C C   1 
ATOM   9276  O O   . GLY C 1 310 ? 44.242  41.278  44.479  1.00 75.85  ? 339 GLY C O   1 
ATOM   9277  N N   . ARG C 1 311 ? 44.717  41.677  42.290  1.00 82.39  ? 340 ARG C N   1 
ATOM   9278  C CA  . ARG C 1 311 ? 43.548  42.485  41.979  1.00 79.84  ? 340 ARG C CA  1 
ATOM   9279  C C   . ARG C 1 311 ? 42.443  41.595  41.396  1.00 78.36  ? 340 ARG C C   1 
ATOM   9280  O O   . ARG C 1 311 ? 42.710  40.491  40.912  1.00 73.74  ? 340 ARG C O   1 
ATOM   9281  C CB  . ARG C 1 311 ? 43.960  43.612  41.021  1.00 78.14  ? 340 ARG C CB  1 
ATOM   9282  C CG  . ARG C 1 311 ? 45.107  44.475  41.535  1.00 73.10  ? 340 ARG C CG  1 
ATOM   9283  C CD  . ARG C 1 311 ? 45.216  45.851  40.896  1.00 70.81  ? 340 ARG C CD  1 
ATOM   9284  N NE  . ARG C 1 311 ? 45.976  45.884  39.651  1.00 68.57  ? 340 ARG C NE  1 
ATOM   9285  C CZ  . ARG C 1 311 ? 47.173  46.450  39.493  1.00 69.59  ? 340 ARG C CZ  1 
ATOM   9286  N NH1 . ARG C 1 311 ? 47.684  46.586  38.281  1.00 65.29  ? 340 ARG C NH1 1 
ATOM   9287  N NH2 . ARG C 1 311 ? 47.845  46.911  40.535  1.00 69.47  ? 340 ARG C NH2 1 
ATOM   9288  N N   . VAL C 1 312 ? 41.203  42.108  41.442  1.00 74.97  ? 341 VAL C N   1 
ATOM   9289  C CA  . VAL C 1 312 ? 40.002  41.354  41.099  1.00 70.02  ? 341 VAL C CA  1 
ATOM   9290  C C   . VAL C 1 312 ? 39.423  41.887  39.787  1.00 60.51  ? 341 VAL C C   1 
ATOM   9291  O O   . VAL C 1 312 ? 39.486  43.085  39.509  1.00 59.38  ? 341 VAL C O   1 
ATOM   9292  C CB  . VAL C 1 312 ? 38.953  41.401  42.234  1.00 69.52  ? 341 VAL C CB  1 
ATOM   9293  C CG1 . VAL C 1 312 ? 39.380  40.564  43.430  1.00 70.97  ? 341 VAL C CG1 1 
ATOM   9294  C CG2 . VAL C 1 312 ? 38.621  42.822  42.677  1.00 69.72  ? 341 VAL C CG2 1 
ATOM   9295  N N   . VAL C 1 313 ? 38.837  40.984  38.993  1.00 48.35  ? 342 VAL C N   1 
ATOM   9296  C CA  . VAL C 1 313 ? 38.189  41.370  37.750  1.00 45.57  ? 342 VAL C CA  1 
ATOM   9297  C C   . VAL C 1 313 ? 36.883  42.081  38.096  1.00 37.88  ? 342 VAL C C   1 
ATOM   9298  O O   . VAL C 1 313 ? 35.962  41.465  38.614  1.00 36.85  ? 342 VAL C O   1 
ATOM   9299  C CB  . VAL C 1 313 ? 37.924  40.162  36.827  1.00 44.64  ? 342 VAL C CB  1 
ATOM   9300  C CG1 . VAL C 1 313 ? 37.241  40.601  35.541  1.00 44.71  ? 342 VAL C CG1 1 
ATOM   9301  C CG2 . VAL C 1 313 ? 39.191  39.383  36.521  1.00 45.35  ? 342 VAL C CG2 1 
ATOM   9302  N N   . PRO C 1 314 ? 36.743  43.394  37.819  1.00 37.00  ? 343 PRO C N   1 
ATOM   9303  C CA  . PRO C 1 314 ? 35.544  44.119  38.224  1.00 34.58  ? 343 PRO C CA  1 
ATOM   9304  C C   . PRO C 1 314 ? 34.305  43.645  37.467  1.00 33.43  ? 343 PRO C C   1 
ATOM   9305  O O   . PRO C 1 314 ? 34.399  43.161  36.325  1.00 28.96  ? 343 PRO C O   1 
ATOM   9306  C CB  . PRO C 1 314 ? 35.918  45.572  37.907  1.00 36.78  ? 343 PRO C CB  1 
ATOM   9307  C CG  . PRO C 1 314 ? 36.794  45.426  36.689  1.00 39.55  ? 343 PRO C CG  1 
ATOM   9308  C CD  . PRO C 1 314 ? 37.676  44.246  37.060  1.00 39.20  ? 343 PRO C CD  1 
ATOM   9309  N N   . GLY C 1 315 ? 33.162  43.773  38.161  1.00 33.66  ? 344 GLY C N   1 
ATOM   9310  C CA  . GLY C 1 315 ? 31.860  43.359  37.664  1.00 33.12  ? 344 GLY C CA  1 
ATOM   9311  C C   . GLY C 1 315 ? 31.629  41.856  37.791  1.00 28.93  ? 344 GLY C C   1 
ATOM   9312  O O   . GLY C 1 315 ? 30.606  41.355  37.344  1.00 29.17  ? 344 GLY C O   1 
ATOM   9313  N N   . TYR C 1 316 ? 32.580  41.146  38.404  1.00 31.13  ? 345 TYR C N   1 
ATOM   9314  C CA  . TYR C 1 316 ? 32.404  39.732  38.698  1.00 30.11  ? 345 TYR C CA  1 
ATOM   9315  C C   . TYR C 1 316 ? 32.319  39.517  40.213  1.00 33.09  ? 345 TYR C C   1 
ATOM   9316  O O   . TYR C 1 316 ? 32.934  40.242  40.985  1.00 34.82  ? 345 TYR C O   1 
ATOM   9317  C CB  . TYR C 1 316 ? 33.520  38.950  38.006  1.00 31.67  ? 345 TYR C CB  1 
ATOM   9318  C CG  . TYR C 1 316 ? 33.312  38.796  36.520  1.00 29.11  ? 345 TYR C CG  1 
ATOM   9319  C CD1 . TYR C 1 316 ? 33.492  39.862  35.652  1.00 30.86  ? 345 TYR C CD1 1 
ATOM   9320  C CD2 . TYR C 1 316 ? 32.869  37.599  35.989  1.00 28.04  ? 345 TYR C CD2 1 
ATOM   9321  C CE1 . TYR C 1 316 ? 33.255  39.732  34.296  1.00 29.62  ? 345 TYR C CE1 1 
ATOM   9322  C CE2 . TYR C 1 316 ? 32.628  37.455  34.634  1.00 28.92  ? 345 TYR C CE2 1 
ATOM   9323  C CZ  . TYR C 1 316 ? 32.828  38.523  33.782  1.00 30.15  ? 345 TYR C CZ  1 
ATOM   9324  O OH  . TYR C 1 316 ? 32.566  38.406  32.435  1.00 30.89  ? 345 TYR C OH  1 
ATOM   9325  N N   . GLY C 1 317 ? 31.535  38.516  40.631  1.00 32.88  ? 346 GLY C N   1 
ATOM   9326  C CA  . GLY C 1 317 ? 31.318  38.235  42.040  1.00 33.24  ? 346 GLY C CA  1 
ATOM   9327  C C   . GLY C 1 317 ? 30.232  39.134  42.631  1.00 32.51  ? 346 GLY C C   1 
ATOM   9328  O O   . GLY C 1 317 ? 29.735  40.011  41.933  1.00 25.08  ? 346 GLY C O   1 
ATOM   9329  N N   . HIS C 1 318 ? 29.853  38.837  43.885  1.00 31.88  ? 347 HIS C N   1 
ATOM   9330  C CA  . HIS C 1 318 ? 28.710  39.511  44.546  1.00 32.23  ? 347 HIS C CA  1 
ATOM   9331  C C   . HIS C 1 318 ? 28.544  38.960  45.966  1.00 33.36  ? 347 HIS C C   1 
ATOM   9332  O O   . HIS C 1 318 ? 28.902  37.801  46.220  1.00 39.20  ? 347 HIS C O   1 
ATOM   9333  C CB  . HIS C 1 318 ? 27.432  39.209  43.769  1.00 32.84  ? 347 HIS C CB  1 
ATOM   9334  C CG  . HIS C 1 318 ? 26.249  40.072  44.049  1.00 32.24  ? 347 HIS C CG  1 
ATOM   9335  N ND1 . HIS C 1 318 ? 25.328  39.780  45.030  1.00 31.24  ? 347 HIS C ND1 1 
ATOM   9336  C CD2 . HIS C 1 318 ? 25.808  41.176  43.445  1.00 30.82  ? 347 HIS C CD2 1 
ATOM   9337  C CE1 . HIS C 1 318 ? 24.381  40.701  45.027  1.00 35.74  ? 347 HIS C CE1 1 
ATOM   9338  N NE2 . HIS C 1 318 ? 24.651  41.556  44.069  1.00 33.07  ? 347 HIS C NE2 1 
ATOM   9339  N N   . ALA C 1 319 ? 27.965  39.753  46.860  1.00 30.52  ? 348 ALA C N   1 
ATOM   9340  C CA  . ALA C 1 319 ? 27.811  39.352  48.247  1.00 32.53  ? 348 ALA C CA  1 
ATOM   9341  C C   . ALA C 1 319 ? 26.869  38.142  48.383  1.00 34.71  ? 348 ALA C C   1 
ATOM   9342  O O   . ALA C 1 319 ? 27.081  37.327  49.277  1.00 34.42  ? 348 ALA C O   1 
ATOM   9343  C CB  . ALA C 1 319 ? 27.380  40.553  49.066  1.00 31.80  ? 348 ALA C CB  1 
ATOM   9344  N N   . VAL C 1 320 ? 25.840  37.991  47.522  1.00 31.78  ? 349 VAL C N   1 
ATOM   9345  C CA  . VAL C 1 320 ? 24.859  36.910  47.694  1.00 34.71  ? 349 VAL C CA  1 
ATOM   9346  C C   . VAL C 1 320 ? 24.606  36.118  46.402  1.00 32.14  ? 349 VAL C C   1 
ATOM   9347  O O   . VAL C 1 320 ? 24.368  34.909  46.463  1.00 28.33  ? 349 VAL C O   1 
ATOM   9348  C CB  . VAL C 1 320 ? 23.533  37.393  48.327  1.00 37.74  ? 349 VAL C CB  1 
ATOM   9349  C CG1 . VAL C 1 320 ? 23.136  38.785  47.883  1.00 42.47  ? 349 VAL C CG1 1 
ATOM   9350  C CG2 . VAL C 1 320 ? 22.367  36.438  48.095  1.00 36.54  ? 349 VAL C CG2 1 
ATOM   9351  N N   . LEU C 1 321 ? 24.616  36.773  45.241  1.00 30.23  ? 350 LEU C N   1 
ATOM   9352  C CA  . LEU C 1 321 ? 24.511  36.052  43.975  1.00 32.95  ? 350 LEU C CA  1 
ATOM   9353  C C   . LEU C 1 321 ? 25.616  35.000  43.908  1.00 32.94  ? 350 LEU C C   1 
ATOM   9354  O O   . LEU C 1 321 ? 26.762  35.333  44.188  1.00 34.35  ? 350 LEU C O   1 
ATOM   9355  C CB  . LEU C 1 321 ? 24.683  37.045  42.820  1.00 31.58  ? 350 LEU C CB  1 
ATOM   9356  C CG  . LEU C 1 321 ? 23.587  37.134  41.757  1.00 32.99  ? 350 LEU C CG  1 
ATOM   9357  C CD1 . LEU C 1 321 ? 22.332  36.353  42.097  1.00 32.43  ? 350 LEU C CD1 1 
ATOM   9358  C CD2 . LEU C 1 321 ? 23.258  38.581  41.470  1.00 33.14  ? 350 LEU C CD2 1 
ATOM   9359  N N   . ARG C 1 322 ? 25.273  33.759  43.516  1.00 36.96  ? 351 ARG C N   1 
ATOM   9360  C CA  . ARG C 1 322 ? 26.259  32.703  43.286  1.00 34.90  ? 351 ARG C CA  1 
ATOM   9361  C C   . ARG C 1 322 ? 26.237  32.228  41.828  1.00 36.53  ? 351 ARG C C   1 
ATOM   9362  O O   . ARG C 1 322 ? 26.904  31.249  41.478  1.00 31.39  ? 351 ARG C O   1 
ATOM   9363  C CB  . ARG C 1 322 ? 26.013  31.515  44.230  1.00 35.03  ? 351 ARG C CB  1 
ATOM   9364  C CG  . ARG C 1 322 ? 26.194  31.830  45.707  1.00 34.26  ? 351 ARG C CG  1 
ATOM   9365  C CD  . ARG C 1 322 ? 27.620  32.260  46.030  1.00 36.67  ? 351 ARG C CD  1 
ATOM   9366  N NE  . ARG C 1 322 ? 27.806  32.790  47.377  1.00 34.38  ? 351 ARG C NE  1 
ATOM   9367  C CZ  . ARG C 1 322 ? 28.117  34.056  47.669  1.00 35.65  ? 351 ARG C CZ  1 
ATOM   9368  N NH1 . ARG C 1 322 ? 28.318  34.398  48.930  1.00 40.04  ? 351 ARG C NH1 1 
ATOM   9369  N NH2 . ARG C 1 322 ? 28.233  34.977  46.721  1.00 30.18  ? 351 ARG C NH2 1 
ATOM   9370  N N   . LYS C 1 323 ? 25.500  32.940  40.961  1.00 37.91  ? 352 LYS C N   1 
ATOM   9371  C CA  . LYS C 1 323 ? 25.432  32.618  39.540  1.00 35.22  ? 352 LYS C CA  1 
ATOM   9372  C C   . LYS C 1 323 ? 25.339  33.914  38.745  1.00 33.80  ? 352 LYS C C   1 
ATOM   9373  O O   . LYS C 1 323 ? 25.161  34.983  39.322  1.00 34.07  ? 352 LYS C O   1 
ATOM   9374  C CB  . LYS C 1 323 ? 24.254  31.679  39.251  1.00 40.41  ? 352 LYS C CB  1 
ATOM   9375  C CG  . LYS C 1 323 ? 23.509  31.919  37.941  1.00 46.25  ? 352 LYS C CG  1 
ATOM   9376  C CD  . LYS C 1 323 ? 23.056  30.662  37.237  1.00 51.38  ? 352 LYS C CD  1 
ATOM   9377  C CE  . LYS C 1 323 ? 22.725  30.907  35.780  1.00 55.08  ? 352 LYS C CE  1 
ATOM   9378  N NZ  . LYS C 1 323 ? 23.145  29.763  34.939  1.00 61.67  ? 352 LYS C NZ  1 
ATOM   9379  N N   . THR C 1 324 ? 25.505  33.796  37.422  1.00 31.54  ? 353 THR C N   1 
ATOM   9380  C CA  . THR C 1 324 ? 25.319  34.904  36.503  1.00 29.63  ? 353 THR C CA  1 
ATOM   9381  C C   . THR C 1 324 ? 24.052  35.668  36.863  1.00 24.61  ? 353 THR C C   1 
ATOM   9382  O O   . THR C 1 324 ? 23.008  35.089  37.101  1.00 23.67  ? 353 THR C O   1 
ATOM   9383  C CB  . THR C 1 324 ? 25.217  34.425  35.056  1.00 29.45  ? 353 THR C CB  1 
ATOM   9384  O OG1 . THR C 1 324 ? 26.440  33.727  34.795  1.00 30.94  ? 353 THR C OG1 1 
ATOM   9385  C CG2 . THR C 1 324 ? 24.996  35.565  34.084  1.00 30.08  ? 353 THR C CG2 1 
ATOM   9386  N N   . ASP C 1 325 ? 24.176  36.988  36.861  1.00 26.28  ? 354 ASP C N   1 
ATOM   9387  C CA  . ASP C 1 325 ? 23.104  37.855  37.299  1.00 28.92  ? 354 ASP C CA  1 
ATOM   9388  C C   . ASP C 1 325 ? 22.139  38.035  36.126  1.00 28.54  ? 354 ASP C C   1 
ATOM   9389  O O   . ASP C 1 325 ? 22.547  38.498  35.061  1.00 26.66  ? 354 ASP C O   1 
ATOM   9390  C CB  . ASP C 1 325 ? 23.762  39.124  37.837  1.00 27.72  ? 354 ASP C CB  1 
ATOM   9391  C CG  . ASP C 1 325 ? 22.877  40.267  38.285  1.00 26.15  ? 354 ASP C CG  1 
ATOM   9392  O OD1 . ASP C 1 325 ? 21.645  40.150  38.190  1.00 26.73  ? 354 ASP C OD1 1 
ATOM   9393  O OD2 . ASP C 1 325 ? 23.467  41.275  38.702  1.00 23.77  ? 354 ASP C OD2 1 
ATOM   9394  N N   . PRO C 1 326 ? 20.828  37.728  36.290  1.00 28.99  ? 355 PRO C N   1 
ATOM   9395  C CA  . PRO C 1 326 ? 19.856  37.918  35.217  1.00 27.90  ? 355 PRO C CA  1 
ATOM   9396  C C   . PRO C 1 326 ? 19.781  39.366  34.732  1.00 25.30  ? 355 PRO C C   1 
ATOM   9397  O O   . PRO C 1 326 ? 19.366  39.608  33.603  1.00 28.26  ? 355 PRO C O   1 
ATOM   9398  C CB  . PRO C 1 326 ? 18.536  37.417  35.826  1.00 28.92  ? 355 PRO C CB  1 
ATOM   9399  C CG  . PRO C 1 326 ? 18.736  37.532  37.334  1.00 30.65  ? 355 PRO C CG  1 
ATOM   9400  C CD  . PRO C 1 326 ? 20.206  37.252  37.539  1.00 31.33  ? 355 PRO C CD  1 
ATOM   9401  N N   . ARG C 1 327 ? 20.265  40.308  35.556  1.00 27.48  ? 356 ARG C N   1 
ATOM   9402  C CA  . ARG C 1 327 ? 20.378  41.700  35.149  1.00 25.70  ? 356 ARG C CA  1 
ATOM   9403  C C   . ARG C 1 327 ? 21.505  41.889  34.136  1.00 25.39  ? 356 ARG C C   1 
ATOM   9404  O O   . ARG C 1 327 ? 21.428  42.776  33.291  1.00 24.71  ? 356 ARG C O   1 
ATOM   9405  C CB  . ARG C 1 327 ? 20.549  42.604  36.372  1.00 26.46  ? 356 ARG C CB  1 
ATOM   9406  C CG  . ARG C 1 327 ? 19.347  42.573  37.306  1.00 28.73  ? 356 ARG C CG  1 
ATOM   9407  C CD  . ARG C 1 327 ? 19.590  43.372  38.567  1.00 27.71  ? 356 ARG C CD  1 
ATOM   9408  N NE  . ARG C 1 327 ? 20.762  42.904  39.287  1.00 28.94  ? 356 ARG C NE  1 
ATOM   9409  C CZ  . ARG C 1 327 ? 21.385  43.591  40.247  1.00 28.52  ? 356 ARG C CZ  1 
ATOM   9410  N NH1 . ARG C 1 327 ? 20.846  44.691  40.744  1.00 25.17  ? 356 ARG C NH1 1 
ATOM   9411  N NH2 . ARG C 1 327 ? 22.538  43.164  40.728  1.00 28.41  ? 356 ARG C NH2 1 
ATOM   9412  N N   . TYR C 1 328 ? 22.582  41.103  34.271  1.00 28.09  ? 357 TYR C N   1 
ATOM   9413  C CA  . TYR C 1 328 ? 23.618  41.026  33.252  1.00 26.99  ? 357 TYR C CA  1 
ATOM   9414  C C   . TYR C 1 328 ? 23.028  40.410  31.985  1.00 27.72  ? 357 TYR C C   1 
ATOM   9415  O O   . TYR C 1 328 ? 23.222  40.932  30.884  1.00 27.48  ? 357 TYR C O   1 
ATOM   9416  C CB  . TYR C 1 328 ? 24.808  40.207  33.765  1.00 26.51  ? 357 TYR C CB  1 
ATOM   9417  C CG  . TYR C 1 328 ? 25.970  40.129  32.813  1.00 26.33  ? 357 TYR C CG  1 
ATOM   9418  C CD1 . TYR C 1 328 ? 26.960  41.101  32.785  1.00 26.10  ? 357 TYR C CD1 1 
ATOM   9419  C CD2 . TYR C 1 328 ? 26.081  39.066  31.939  1.00 27.37  ? 357 TYR C CD2 1 
ATOM   9420  C CE1 . TYR C 1 328 ? 28.025  41.019  31.900  1.00 26.56  ? 357 TYR C CE1 1 
ATOM   9421  C CE2 . TYR C 1 328 ? 27.129  38.979  31.040  1.00 26.74  ? 357 TYR C CE2 1 
ATOM   9422  C CZ  . TYR C 1 328 ? 28.110  39.948  31.026  1.00 26.71  ? 357 TYR C CZ  1 
ATOM   9423  O OH  . TYR C 1 328 ? 29.151  39.849  30.115  1.00 32.85  ? 357 TYR C OH  1 
ATOM   9424  N N   . THR C 1 329 ? 22.323  39.279  32.153  1.00 27.15  ? 358 THR C N   1 
ATOM   9425  C CA  . THR C 1 329 ? 21.832  38.529  31.012  1.00 32.18  ? 358 THR C CA  1 
ATOM   9426  C C   . THR C 1 329 ? 21.017  39.449  30.106  1.00 32.72  ? 358 THR C C   1 
ATOM   9427  O O   . THR C 1 329 ? 21.242  39.495  28.891  1.00 37.28  ? 358 THR C O   1 
ATOM   9428  C CB  . THR C 1 329 ? 21.029  37.291  31.429  1.00 30.67  ? 358 THR C CB  1 
ATOM   9429  O OG1 . THR C 1 329 ? 21.867  36.435  32.200  1.00 30.76  ? 358 THR C OG1 1 
ATOM   9430  C CG2 . THR C 1 329 ? 20.533  36.502  30.240  1.00 36.17  ? 358 THR C CG2 1 
ATOM   9431  N N   . CYS C 1 330 ? 20.092  40.203  30.706  1.00 32.46  ? 359 CYS C N   1 
ATOM   9432  C CA  . CYS C 1 330 ? 19.108  40.923  29.922  1.00 34.28  ? 359 CYS C CA  1 
ATOM   9433  C C   . CYS C 1 330 ? 19.769  42.117  29.234  1.00 31.17  ? 359 CYS C C   1 
ATOM   9434  O O   . CYS C 1 330 ? 19.345  42.534  28.159  1.00 29.95  ? 359 CYS C O   1 
ATOM   9435  C CB  . CYS C 1 330 ? 17.897  41.307  30.766  1.00 38.42  ? 359 CYS C CB  1 
ATOM   9436  S SG  . CYS C 1 330 ? 18.089  42.916  31.560  1.00 49.05  ? 359 CYS C SG  1 
ATOM   9437  N N   . GLN C 1 331 ? 20.859  42.638  29.807  1.00 30.61  ? 360 GLN C N   1 
ATOM   9438  C CA  . GLN C 1 331 ? 21.645  43.637  29.094  1.00 30.22  ? 360 GLN C CA  1 
ATOM   9439  C C   . GLN C 1 331 ? 22.416  42.987  27.943  1.00 30.56  ? 360 GLN C C   1 
ATOM   9440  O O   . GLN C 1 331 ? 22.638  43.617  26.910  1.00 28.09  ? 360 GLN C O   1 
ATOM   9441  C CB  . GLN C 1 331 ? 22.563  44.366  30.064  1.00 31.09  ? 360 GLN C CB  1 
ATOM   9442  C CG  . GLN C 1 331 ? 21.807  45.367  30.912  1.00 34.57  ? 360 GLN C CG  1 
ATOM   9443  C CD  . GLN C 1 331 ? 22.657  45.912  32.030  1.00 36.42  ? 360 GLN C CD  1 
ATOM   9444  O OE1 . GLN C 1 331 ? 23.001  45.197  32.965  1.00 44.39  ? 360 GLN C OE1 1 
ATOM   9445  N NE2 . GLN C 1 331 ? 22.957  47.194  31.960  1.00 38.76  ? 360 GLN C NE2 1 
ATOM   9446  N N   . ARG C 1 332 ? 22.807  41.721  28.121  1.00 32.16  ? 361 ARG C N   1 
ATOM   9447  C CA  . ARG C 1 332 ? 23.542  41.023  27.079  1.00 35.08  ? 361 ARG C CA  1 
ATOM   9448  C C   . ARG C 1 332 ? 22.622  40.875  25.871  1.00 36.30  ? 361 ARG C C   1 
ATOM   9449  O O   . ARG C 1 332 ? 23.026  41.207  24.753  1.00 34.11  ? 361 ARG C O   1 
ATOM   9450  C CB  . ARG C 1 332 ? 24.100  39.679  27.567  1.00 37.06  ? 361 ARG C CB  1 
ATOM   9451  C CG  . ARG C 1 332 ? 24.885  38.910  26.504  1.00 42.16  ? 361 ARG C CG  1 
ATOM   9452  C CD  . ARG C 1 332 ? 25.357  37.523  26.922  1.00 43.60  ? 361 ARG C CD  1 
ATOM   9453  N NE  . ARG C 1 332 ? 25.734  36.722  25.760  1.00 41.88  ? 361 ARG C NE  1 
ATOM   9454  C CZ  . ARG C 1 332 ? 26.724  37.025  24.923  1.00 45.57  ? 361 ARG C CZ  1 
ATOM   9455  N NH1 . ARG C 1 332 ? 27.659  37.885  25.289  1.00 45.93  ? 361 ARG C NH1 1 
ATOM   9456  N NH2 . ARG C 1 332 ? 26.806  36.439  23.738  1.00 42.15  ? 361 ARG C NH2 1 
ATOM   9457  N N   . GLU C 1 333 ? 21.402  40.368  26.121  1.00 37.80  ? 362 GLU C N   1 
ATOM   9458  C CA  . GLU C 1 333 ? 20.416  40.131  25.072  1.00 37.20  ? 362 GLU C CA  1 
ATOM   9459  C C   . GLU C 1 333 ? 20.153  41.403  24.281  1.00 32.19  ? 362 GLU C C   1 
ATOM   9460  O O   . GLU C 1 333 ? 20.126  41.369  23.057  1.00 38.92  ? 362 GLU C O   1 
ATOM   9461  C CB  . GLU C 1 333 ? 19.109  39.613  25.668  1.00 38.68  ? 362 GLU C CB  1 
ATOM   9462  C CG  . GLU C 1 333 ? 19.213  38.180  26.152  1.00 41.93  ? 362 GLU C CG  1 
ATOM   9463  C CD  . GLU C 1 333 ? 18.123  37.725  27.112  1.00 42.44  ? 362 GLU C CD  1 
ATOM   9464  O OE1 . GLU C 1 333 ? 17.369  38.595  27.632  1.00 42.32  ? 362 GLU C OE1 1 
ATOM   9465  O OE2 . GLU C 1 333 ? 18.024  36.504  27.336  1.00 40.24  ? 362 GLU C OE2 1 
ATOM   9466  N N   . PHE C 1 334 ? 20.020  42.530  24.985  1.00 33.63  ? 363 PHE C N   1 
ATOM   9467  C CA  . PHE C 1 334 ? 19.785  43.826  24.377  1.00 28.58  ? 363 PHE C CA  1 
ATOM   9468  C C   . PHE C 1 334 ? 20.944  44.236  23.464  1.00 33.34  ? 363 PHE C C   1 
ATOM   9469  O O   . PHE C 1 334 ? 20.746  44.685  22.326  1.00 36.59  ? 363 PHE C O   1 
ATOM   9470  C CB  . PHE C 1 334 ? 19.551  44.859  25.485  1.00 29.01  ? 363 PHE C CB  1 
ATOM   9471  C CG  . PHE C 1 334 ? 19.193  46.242  24.997  1.00 24.66  ? 363 PHE C CG  1 
ATOM   9472  C CD1 . PHE C 1 334 ? 20.166  47.135  24.578  1.00 24.87  ? 363 PHE C CD1 1 
ATOM   9473  C CD2 . PHE C 1 334 ? 17.868  46.627  24.933  1.00 25.01  ? 363 PHE C CD2 1 
ATOM   9474  C CE1 . PHE C 1 334 ? 19.817  48.397  24.126  1.00 26.98  ? 363 PHE C CE1 1 
ATOM   9475  C CE2 . PHE C 1 334 ? 17.521  47.877  24.457  1.00 25.69  ? 363 PHE C CE2 1 
ATOM   9476  C CZ  . PHE C 1 334 ? 18.494  48.750  24.046  1.00 26.23  ? 363 PHE C CZ  1 
ATOM   9477  N N   . ALA C 1 335 ? 22.178  44.080  23.945  1.00 30.14  ? 364 ALA C N   1 
ATOM   9478  C CA  . ALA C 1 335 ? 23.335  44.394  23.129  1.00 31.07  ? 364 ALA C CA  1 
ATOM   9479  C C   . ALA C 1 335 ? 23.351  43.564  21.843  1.00 33.74  ? 364 ALA C C   1 
ATOM   9480  O O   . ALA C 1 335 ? 23.559  44.113  20.761  1.00 36.43  ? 364 ALA C O   1 
ATOM   9481  C CB  . ALA C 1 335 ? 24.597  44.173  23.909  1.00 30.81  ? 364 ALA C CB  1 
ATOM   9482  N N   . LEU C 1 336 ? 23.172  42.245  21.955  1.00 31.57  ? 365 LEU C N   1 
ATOM   9483  C CA  . LEU C 1 336 ? 23.382  41.389  20.787  1.00 38.45  ? 365 LEU C CA  1 
ATOM   9484  C C   . LEU C 1 336 ? 22.138  41.395  19.899  1.00 43.40  ? 365 LEU C C   1 
ATOM   9485  O O   . LEU C 1 336 ? 22.098  40.722  18.873  1.00 39.81  ? 365 LEU C O   1 
ATOM   9486  C CB  . LEU C 1 336 ? 23.825  39.972  21.183  1.00 40.67  ? 365 LEU C CB  1 
ATOM   9487  C CG  . LEU C 1 336 ? 23.000  39.220  22.228  1.00 43.46  ? 365 LEU C CG  1 
ATOM   9488  C CD1 . LEU C 1 336 ? 21.769  38.566  21.622  1.00 46.79  ? 365 LEU C CD1 1 
ATOM   9489  C CD2 . LEU C 1 336 ? 23.853  38.171  22.930  1.00 41.60  ? 365 LEU C CD2 1 
ATOM   9490  N N   . LYS C 1 337 ? 21.138  42.193  20.291  1.00 44.95  ? 366 LYS C N   1 
ATOM   9491  C CA  . LYS C 1 337 ? 20.025  42.530  19.428  1.00 49.79  ? 366 LYS C CA  1 
ATOM   9492  C C   . LYS C 1 337 ? 20.313  43.833  18.683  1.00 47.37  ? 366 LYS C C   1 
ATOM   9493  O O   . LYS C 1 337 ? 20.028  43.915  17.495  1.00 49.72  ? 366 LYS C O   1 
ATOM   9494  C CB  . LYS C 1 337 ? 18.742  42.621  20.260  1.00 57.10  ? 366 LYS C CB  1 
ATOM   9495  C CG  . LYS C 1 337 ? 17.467  42.755  19.441  1.00 62.18  ? 366 LYS C CG  1 
ATOM   9496  C CD  . LYS C 1 337 ? 16.247  42.144  20.106  1.00 65.92  ? 366 LYS C CD  1 
ATOM   9497  C CE  . LYS C 1 337 ? 15.013  42.213  19.231  1.00 65.80  ? 366 LYS C CE  1 
ATOM   9498  N NZ  . LYS C 1 337 ? 14.644  43.615  18.911  1.00 65.33  ? 366 LYS C NZ  1 
ATOM   9499  N N   . HIS C 1 338 ? 20.908  44.824  19.373  1.00 47.46  ? 367 HIS C N   1 
ATOM   9500  C CA  . HIS C 1 338 ? 20.868  46.217  18.948  1.00 42.42  ? 367 HIS C CA  1 
ATOM   9501  C C   . HIS C 1 338 ? 22.244  46.773  18.591  1.00 39.61  ? 367 HIS C C   1 
ATOM   9502  O O   . HIS C 1 338 ? 22.316  47.777  17.891  1.00 41.71  ? 367 HIS C O   1 
ATOM   9503  C CB  . HIS C 1 338 ? 20.250  47.093  20.045  1.00 45.50  ? 367 HIS C CB  1 
ATOM   9504  C CG  . HIS C 1 338 ? 18.869  46.676  20.378  1.00 46.85  ? 367 HIS C CG  1 
ATOM   9505  N ND1 . HIS C 1 338 ? 17.884  46.620  19.416  1.00 58.11  ? 367 HIS C ND1 1 
ATOM   9506  C CD2 . HIS C 1 338 ? 18.308  46.256  21.507  1.00 51.66  ? 367 HIS C CD2 1 
ATOM   9507  C CE1 . HIS C 1 338 ? 16.757  46.203  19.971  1.00 55.65  ? 367 HIS C CE1 1 
ATOM   9508  N NE2 . HIS C 1 338 ? 16.992  45.981  21.247  1.00 55.11  ? 367 HIS C NE2 1 
ATOM   9509  N N   . LEU C 1 339 ? 23.328  46.163  19.085  1.00 38.97  ? 368 LEU C N   1 
ATOM   9510  C CA  . LEU C 1 339 ? 24.662  46.670  18.797  1.00 41.29  ? 368 LEU C CA  1 
ATOM   9511  C C   . LEU C 1 339 ? 25.715  45.570  18.892  1.00 41.48  ? 368 LEU C C   1 
ATOM   9512  O O   . LEU C 1 339 ? 26.791  45.807  19.436  1.00 41.98  ? 368 LEU C O   1 
ATOM   9513  C CB  . LEU C 1 339 ? 24.985  47.814  19.767  1.00 42.30  ? 368 LEU C CB  1 
ATOM   9514  C CG  . LEU C 1 339 ? 24.732  47.525  21.249  1.00 40.64  ? 368 LEU C CG  1 
ATOM   9515  C CD1 . LEU C 1 339 ? 25.967  47.796  22.085  1.00 34.39  ? 368 LEU C CD1 1 
ATOM   9516  C CD2 . LEU C 1 339 ? 23.545  48.332  21.755  1.00 38.93  ? 368 LEU C CD2 1 
ATOM   9517  N N   . PRO C 1 340 ? 25.491  44.380  18.286  1.00 43.75  ? 369 PRO C N   1 
ATOM   9518  C CA  . PRO C 1 340 ? 26.405  43.252  18.467  1.00 44.59  ? 369 PRO C CA  1 
ATOM   9519  C C   . PRO C 1 340 ? 27.839  43.481  17.976  1.00 45.90  ? 369 PRO C C   1 
ATOM   9520  O O   . PRO C 1 340 ? 28.714  42.694  18.326  1.00 38.94  ? 369 PRO C O   1 
ATOM   9521  C CB  . PRO C 1 340 ? 25.728  42.092  17.720  1.00 44.53  ? 369 PRO C CB  1 
ATOM   9522  C CG  . PRO C 1 340 ? 24.782  42.755  16.733  1.00 46.97  ? 369 PRO C CG  1 
ATOM   9523  C CD  . PRO C 1 340 ? 24.372  44.059  17.386  1.00 49.84  ? 369 PRO C CD  1 
ATOM   9524  N N   . ASN C 1 341 ? 28.093  44.566  17.220  1.00 45.73  ? 370 ASN C N   1 
ATOM   9525  C CA  . ASN C 1 341 ? 29.413  44.805  16.643  1.00 53.43  ? 370 ASN C CA  1 
ATOM   9526  C C   . ASN C 1 341 ? 30.071  46.060  17.211  1.00 50.44  ? 370 ASN C C   1 
ATOM   9527  O O   . ASN C 1 341 ? 30.909  46.670  16.545  1.00 51.92  ? 370 ASN C O   1 
ATOM   9528  C CB  . ASN C 1 341 ? 29.354  44.963  15.122  1.00 59.53  ? 370 ASN C CB  1 
ATOM   9529  C CG  . ASN C 1 341 ? 28.568  43.853  14.458  1.00 64.25  ? 370 ASN C CG  1 
ATOM   9530  O OD1 . ASN C 1 341 ? 28.940  42.686  14.569  1.00 64.82  ? 370 ASN C OD1 1 
ATOM   9531  N ND2 . ASN C 1 341 ? 27.482  44.205  13.784  1.00 68.22  ? 370 ASN C ND2 1 
ATOM   9532  N N   . ASP C 1 342 ? 29.686  46.457  18.428  1.00 48.39  ? 371 ASP C N   1 
ATOM   9533  C CA  . ASP C 1 342 ? 30.403  47.495  19.146  1.00 44.41  ? 371 ASP C CA  1 
ATOM   9534  C C   . ASP C 1 342 ? 31.673  46.857  19.717  1.00 45.71  ? 371 ASP C C   1 
ATOM   9535  O O   . ASP C 1 342 ? 31.589  45.850  20.419  1.00 45.23  ? 371 ASP C O   1 
ATOM   9536  C CB  . ASP C 1 342 ? 29.512  48.129  20.222  1.00 46.05  ? 371 ASP C CB  1 
ATOM   9537  C CG  . ASP C 1 342 ? 30.241  49.014  21.225  1.00 47.19  ? 371 ASP C CG  1 
ATOM   9538  O OD1 . ASP C 1 342 ? 30.715  50.095  20.823  1.00 46.60  ? 371 ASP C OD1 1 
ATOM   9539  O OD2 . ASP C 1 342 ? 30.338  48.610  22.404  1.00 48.22  ? 371 ASP C OD2 1 
ATOM   9540  N N   . PRO C 1 343 ? 32.883  47.391  19.424  1.00 41.93  ? 372 PRO C N   1 
ATOM   9541  C CA  . PRO C 1 343 ? 34.119  46.846  19.986  1.00 41.83  ? 372 PRO C CA  1 
ATOM   9542  C C   . PRO C 1 343 ? 34.007  46.613  21.493  1.00 41.71  ? 372 PRO C C   1 
ATOM   9543  O O   . PRO C 1 343 ? 34.211  45.497  21.958  1.00 39.61  ? 372 PRO C O   1 
ATOM   9544  C CB  . PRO C 1 343 ? 35.163  47.928  19.666  1.00 43.88  ? 372 PRO C CB  1 
ATOM   9545  C CG  . PRO C 1 343 ? 34.636  48.594  18.408  1.00 43.86  ? 372 PRO C CG  1 
ATOM   9546  C CD  . PRO C 1 343 ? 33.129  48.552  18.552  1.00 42.99  ? 372 PRO C CD  1 
ATOM   9547  N N   . MET C 1 344 ? 33.624  47.659  22.242  1.00 39.39  ? 373 MET C N   1 
ATOM   9548  C CA  . MET C 1 344 ? 33.552  47.576  23.692  1.00 38.80  ? 373 MET C CA  1 
ATOM   9549  C C   . MET C 1 344 ? 32.598  46.456  24.098  1.00 35.82  ? 373 MET C C   1 
ATOM   9550  O O   . MET C 1 344 ? 32.935  45.668  24.976  1.00 33.15  ? 373 MET C O   1 
ATOM   9551  C CB  . MET C 1 344 ? 33.121  48.912  24.311  1.00 42.94  ? 373 MET C CB  1 
ATOM   9552  C CG  . MET C 1 344 ? 34.189  49.978  24.205  1.00 48.39  ? 373 MET C CG  1 
ATOM   9553  S SD  . MET C 1 344 ? 35.599  49.710  25.317  1.00 58.49  ? 373 MET C SD  1 
ATOM   9554  C CE  . MET C 1 344 ? 34.876  50.205  26.880  1.00 58.40  ? 373 MET C CE  1 
ATOM   9555  N N   . PHE C 1 345 ? 31.443  46.325  23.422  1.00 35.45  ? 374 PHE C N   1 
ATOM   9556  C CA  . PHE C 1 345 ? 30.543  45.220  23.725  1.00 33.32  ? 374 PHE C CA  1 
ATOM   9557  C C   . PHE C 1 345 ? 31.224  43.876  23.467  1.00 33.68  ? 374 PHE C C   1 
ATOM   9558  O O   . PHE C 1 345 ? 31.047  42.937  24.237  1.00 34.12  ? 374 PHE C O   1 
ATOM   9559  C CB  . PHE C 1 345 ? 29.230  45.287  22.939  1.00 31.84  ? 374 PHE C CB  1 
ATOM   9560  C CG  . PHE C 1 345 ? 28.415  44.022  23.031  1.00 30.93  ? 374 PHE C CG  1 
ATOM   9561  C CD1 . PHE C 1 345 ? 27.889  43.596  24.240  1.00 30.37  ? 374 PHE C CD1 1 
ATOM   9562  C CD2 . PHE C 1 345 ? 28.223  43.217  21.917  1.00 33.09  ? 374 PHE C CD2 1 
ATOM   9563  C CE1 . PHE C 1 345 ? 27.172  42.413  24.325  1.00 30.95  ? 374 PHE C CE1 1 
ATOM   9564  C CE2 . PHE C 1 345 ? 27.508  42.034  22.003  1.00 31.77  ? 374 PHE C CE2 1 
ATOM   9565  C CZ  . PHE C 1 345 ? 26.984  41.631  23.210  1.00 34.04  ? 374 PHE C CZ  1 
ATOM   9566  N N   . LYS C 1 346 ? 31.949  43.749  22.350  1.00 36.71  ? 375 LYS C N   1 
ATOM   9567  C CA  . LYS C 1 346 ? 32.475  42.444  21.969  1.00 41.36  ? 375 LYS C CA  1 
ATOM   9568  C C   . LYS C 1 346 ? 33.552  42.018  22.972  1.00 35.35  ? 375 LYS C C   1 
ATOM   9569  O O   . LYS C 1 346 ? 33.706  40.827  23.233  1.00 33.74  ? 375 LYS C O   1 
ATOM   9570  C CB  . LYS C 1 346 ? 32.965  42.431  20.512  1.00 47.04  ? 375 LYS C CB  1 
ATOM   9571  C CG  . LYS C 1 346 ? 31.856  42.304  19.469  1.00 53.73  ? 375 LYS C CG  1 
ATOM   9572  C CD  . LYS C 1 346 ? 32.322  42.120  18.029  1.00 55.12  ? 375 LYS C CD  1 
ATOM   9573  C CE  . LYS C 1 346 ? 32.974  43.359  17.447  1.00 58.43  ? 375 LYS C CE  1 
ATOM   9574  N NZ  . LYS C 1 346 ? 33.135  43.264  15.973  1.00 57.62  ? 375 LYS C NZ  1 
ATOM   9575  N N   . LEU C 1 347 ? 34.276  42.982  23.560  1.00 33.36  ? 376 LEU C N   1 
ATOM   9576  C CA  . LEU C 1 347 ? 35.224  42.690  24.634  1.00 33.57  ? 376 LEU C CA  1 
ATOM   9577  C C   . LEU C 1 347 ? 34.500  42.139  25.870  1.00 32.65  ? 376 LEU C C   1 
ATOM   9578  O O   . LEU C 1 347 ? 34.872  41.099  26.409  1.00 33.47  ? 376 LEU C O   1 
ATOM   9579  C CB  . LEU C 1 347 ? 35.994  43.966  24.984  1.00 31.78  ? 376 LEU C CB  1 
ATOM   9580  C CG  . LEU C 1 347 ? 36.982  43.832  26.145  1.00 33.99  ? 376 LEU C CG  1 
ATOM   9581  C CD1 . LEU C 1 347 ? 37.932  42.659  25.938  1.00 34.16  ? 376 LEU C CD1 1 
ATOM   9582  C CD2 . LEU C 1 347 ? 37.760  45.116  26.342  1.00 35.02  ? 376 LEU C CD2 1 
ATOM   9583  N N   . VAL C 1 348 ? 33.459  42.850  26.322  1.00 34.10  ? 377 VAL C N   1 
ATOM   9584  C CA  . VAL C 1 348 ? 32.623  42.394  27.424  1.00 32.36  ? 377 VAL C CA  1 
ATOM   9585  C C   . VAL C 1 348 ? 32.111  40.991  27.115  1.00 31.53  ? 377 VAL C C   1 
ATOM   9586  O O   . VAL C 1 348 ? 31.976  40.167  28.014  1.00 32.89  ? 377 VAL C O   1 
ATOM   9587  C CB  . VAL C 1 348 ? 31.450  43.368  27.676  1.00 36.58  ? 377 VAL C CB  1 
ATOM   9588  C CG1 . VAL C 1 348 ? 30.335  42.728  28.494  1.00 38.90  ? 377 VAL C CG1 1 
ATOM   9589  C CG2 . VAL C 1 348 ? 31.911  44.660  28.335  1.00 37.07  ? 377 VAL C CG2 1 
ATOM   9590  N N   . ALA C 1 349 ? 31.815  40.743  25.833  1.00 32.32  ? 378 ALA C N   1 
ATOM   9591  C CA  . ALA C 1 349 ? 31.272  39.475  25.367  1.00 34.65  ? 378 ALA C CA  1 
ATOM   9592  C C   . ALA C 1 349 ? 32.350  38.396  25.395  1.00 35.48  ? 378 ALA C C   1 
ATOM   9593  O O   . ALA C 1 349 ? 32.042  37.231  25.637  1.00 36.75  ? 378 ALA C O   1 
ATOM   9594  C CB  . ALA C 1 349 ? 30.706  39.642  23.983  1.00 36.66  ? 378 ALA C CB  1 
ATOM   9595  N N   . GLN C 1 350 ? 33.607  38.802  25.184  1.00 36.39  ? 379 GLN C N   1 
ATOM   9596  C CA  . GLN C 1 350 ? 34.740  37.888  25.249  1.00 38.57  ? 379 GLN C CA  1 
ATOM   9597  C C   . GLN C 1 350 ? 35.011  37.523  26.709  1.00 37.18  ? 379 GLN C C   1 
ATOM   9598  O O   . GLN C 1 350 ? 35.316  36.377  27.014  1.00 35.79  ? 379 GLN C O   1 
ATOM   9599  C CB  . GLN C 1 350 ? 35.970  38.498  24.567  1.00 38.41  ? 379 GLN C CB  1 
ATOM   9600  C CG  . GLN C 1 350 ? 36.914  37.453  23.973  1.00 41.29  ? 379 GLN C CG  1 
ATOM   9601  C CD  . GLN C 1 350 ? 38.043  38.034  23.151  1.00 41.81  ? 379 GLN C CD  1 
ATOM   9602  O OE1 . GLN C 1 350 ? 38.186  39.245  22.994  1.00 40.07  ? 379 GLN C OE1 1 
ATOM   9603  N NE2 . GLN C 1 350 ? 38.869  37.154  22.604  1.00 42.53  ? 379 GLN C NE2 1 
ATOM   9604  N N   . LEU C 1 351 ? 34.878  38.501  27.607  1.00 33.77  ? 380 LEU C N   1 
ATOM   9605  C CA  . LEU C 1 351 ? 35.090  38.280  29.029  1.00 31.67  ? 380 LEU C CA  1 
ATOM   9606  C C   . LEU C 1 351 ? 34.099  37.245  29.568  1.00 32.83  ? 380 LEU C C   1 
ATOM   9607  O O   . LEU C 1 351 ? 34.461  36.416  30.396  1.00 34.13  ? 380 LEU C O   1 
ATOM   9608  C CB  . LEU C 1 351 ? 34.974  39.623  29.763  1.00 31.11  ? 380 LEU C CB  1 
ATOM   9609  C CG  . LEU C 1 351 ? 36.182  40.558  29.633  1.00 33.14  ? 380 LEU C CG  1 
ATOM   9610  C CD1 . LEU C 1 351 ? 35.942  41.859  30.378  1.00 34.38  ? 380 LEU C CD1 1 
ATOM   9611  C CD2 . LEU C 1 351 ? 37.452  39.912  30.158  1.00 34.01  ? 380 LEU C CD2 1 
ATOM   9612  N N   . TYR C 1 352 ? 32.841  37.311  29.109  1.00 32.50  ? 381 TYR C N   1 
ATOM   9613  C CA  . TYR C 1 352 ? 31.804  36.374  29.517  1.00 31.85  ? 381 TYR C CA  1 
ATOM   9614  C C   . TYR C 1 352 ? 32.210  34.923  29.261  1.00 34.00  ? 381 TYR C C   1 
ATOM   9615  O O   . TYR C 1 352 ? 31.880  34.037  30.050  1.00 32.18  ? 381 TYR C O   1 
ATOM   9616  C CB  . TYR C 1 352 ? 30.501  36.718  28.791  1.00 34.52  ? 381 TYR C CB  1 
ATOM   9617  C CG  . TYR C 1 352 ? 29.260  36.005  29.265  1.00 35.14  ? 381 TYR C CG  1 
ATOM   9618  C CD1 . TYR C 1 352 ? 29.070  35.671  30.601  1.00 36.20  ? 381 TYR C CD1 1 
ATOM   9619  C CD2 . TYR C 1 352 ? 28.229  35.721  28.378  1.00 38.22  ? 381 TYR C CD2 1 
ATOM   9620  C CE1 . TYR C 1 352 ? 27.917  35.030  31.028  1.00 35.06  ? 381 TYR C CE1 1 
ATOM   9621  C CE2 . TYR C 1 352 ? 27.063  35.095  28.792  1.00 38.31  ? 381 TYR C CE2 1 
ATOM   9622  C CZ  . TYR C 1 352 ? 26.905  34.749  30.124  1.00 37.61  ? 381 TYR C CZ  1 
ATOM   9623  O OH  . TYR C 1 352 ? 25.738  34.136  30.551  1.00 41.71  ? 381 TYR C OH  1 
ATOM   9624  N N   . LYS C 1 353 ? 32.940  34.695  28.180  1.00 37.22  ? 382 LYS C N   1 
ATOM   9625  C CA  . LYS C 1 353 ? 33.293  33.305  27.802  1.00 40.65  ? 382 LYS C CA  1 
ATOM   9626  C C   . LYS C 1 353 ? 34.558  32.846  28.525  1.00 37.52  ? 382 LYS C C   1 
ATOM   9627  O O   . LYS C 1 353 ? 34.662  31.647  28.801  1.00 40.02  ? 382 LYS C O   1 
ATOM   9628  C CB  . LYS C 1 353 ? 33.511  33.264  26.292  1.00 44.40  ? 382 LYS C CB  1 
ATOM   9629  C CG  . LYS C 1 353 ? 32.267  33.149  25.447  1.00 45.80  ? 382 LYS C CG  1 
ATOM   9630  C CD  . LYS C 1 353 ? 32.561  32.514  24.096  1.00 46.87  ? 382 LYS C CD  1 
ATOM   9631  C CE  . LYS C 1 353 ? 33.994  32.628  23.699  1.00 49.16  ? 382 LYS C CE  1 
ATOM   9632  N NZ  . LYS C 1 353 ? 34.338  33.949  23.165  1.00 47.27  ? 382 LYS C NZ  1 
ATOM   9633  N N   . ILE C 1 354 ? 35.465  33.766  28.821  1.00 35.28  ? 383 ILE C N   1 
ATOM   9634  C CA  . ILE C 1 354 ? 36.768  33.363  29.417  1.00 36.22  ? 383 ILE C CA  1 
ATOM   9635  C C   . ILE C 1 354 ? 36.758  33.495  30.948  1.00 36.28  ? 383 ILE C C   1 
ATOM   9636  O O   . ILE C 1 354 ? 37.015  32.492  31.628  1.00 39.35  ? 383 ILE C O   1 
ATOM   9637  C CB  . ILE C 1 354 ? 37.856  34.262  28.806  1.00 36.36  ? 383 ILE C CB  1 
ATOM   9638  C CG1 . ILE C 1 354 ? 38.278  33.782  27.437  1.00 37.00  ? 383 ILE C CG1 1 
ATOM   9639  C CG2 . ILE C 1 354 ? 39.064  34.404  29.734  1.00 37.39  ? 383 ILE C CG2 1 
ATOM   9640  C CD1 . ILE C 1 354 ? 39.030  34.831  26.647  1.00 38.56  ? 383 ILE C CD1 1 
ATOM   9641  N N   . VAL C 1 355 ? 36.425  34.671  31.481  1.00 35.61  ? 384 VAL C N   1 
ATOM   9642  C CA  . VAL C 1 355 ? 36.586  34.935  32.943  1.00 35.87  ? 384 VAL C CA  1 
ATOM   9643  C C   . VAL C 1 355 ? 35.857  33.891  33.801  1.00 38.75  ? 384 VAL C C   1 
ATOM   9644  O O   . VAL C 1 355 ? 36.475  33.418  34.766  1.00 37.16  ? 384 VAL C O   1 
ATOM   9645  C CB  . VAL C 1 355 ? 36.222  36.392  33.305  1.00 32.94  ? 384 VAL C CB  1 
ATOM   9646  C CG1 . VAL C 1 355 ? 36.367  36.673  34.793  1.00 31.27  ? 384 VAL C CG1 1 
ATOM   9647  C CG2 . VAL C 1 355 ? 37.033  37.385  32.492  1.00 32.99  ? 384 VAL C CG2 1 
ATOM   9648  N N   . PRO C 1 356 ? 34.584  33.526  33.535  1.00 40.35  ? 385 PRO C N   1 
ATOM   9649  C CA  . PRO C 1 356 ? 33.948  32.484  34.313  1.00 43.06  ? 385 PRO C CA  1 
ATOM   9650  C C   . PRO C 1 356 ? 34.850  31.312  34.686  1.00 48.85  ? 385 PRO C C   1 
ATOM   9651  O O   . PRO C 1 356 ? 35.122  31.118  35.882  1.00 51.72  ? 385 PRO C O   1 
ATOM   9652  C CB  . PRO C 1 356 ? 32.848  32.158  33.297  1.00 41.72  ? 385 PRO C CB  1 
ATOM   9653  C CG  . PRO C 1 356 ? 32.324  33.521  32.975  1.00 41.07  ? 385 PRO C CG  1 
ATOM   9654  C CD  . PRO C 1 356 ? 33.641  34.192  32.645  1.00 39.76  ? 385 PRO C CD  1 
ATOM   9655  N N   . ASN C 1 357 ? 35.324  30.568  33.697  1.00 48.85  ? 386 ASN C N   1 
ATOM   9656  C CA  . ASN C 1 357 ? 36.149  29.353  33.959  1.00 47.19  ? 386 ASN C CA  1 
ATOM   9657  C C   . ASN C 1 357 ? 37.423  29.734  34.716  1.00 45.84  ? 386 ASN C C   1 
ATOM   9658  O O   . ASN C 1 357 ? 37.794  28.986  35.619  1.00 48.60  ? 386 ASN C O   1 
ATOM   9659  C CB  . ASN C 1 357 ? 36.383  28.608  32.650  1.00 48.58  ? 386 ASN C CB  1 
ATOM   9660  C CG  . ASN C 1 357 ? 35.161  27.839  32.216  1.00 53.36  ? 386 ASN C CG  1 
ATOM   9661  O OD1 . ASN C 1 357 ? 35.084  27.391  31.068  1.00 58.74  ? 386 ASN C OD1 1 
ATOM   9662  N ND2 . ASN C 1 357 ? 34.199  27.675  33.110  1.00 52.04  ? 386 ASN C ND2 1 
ATOM   9663  N N   . VAL C 1 358 ? 38.032  30.869  34.388  1.00 38.97  ? 387 VAL C N   1 
ATOM   9664  C CA  . VAL C 1 358 ? 39.222  31.347  35.133  1.00 41.50  ? 387 VAL C CA  1 
ATOM   9665  C C   . VAL C 1 358 ? 38.853  31.635  36.598  1.00 48.43  ? 387 VAL C C   1 
ATOM   9666  O O   . VAL C 1 358 ? 39.448  31.140  37.478  1.00 47.94  ? 387 VAL C O   1 
ATOM   9667  C CB  . VAL C 1 358 ? 39.876  32.586  34.499  1.00 42.13  ? 387 VAL C CB  1 
ATOM   9668  C CG1 . VAL C 1 358 ? 41.009  33.141  35.351  1.00 39.92  ? 387 VAL C CG1 1 
ATOM   9669  C CG2 . VAL C 1 358 ? 40.356  32.313  33.081  1.00 43.44  ? 387 VAL C CG2 1 
ATOM   9670  N N   . LEU C 1 359 ? 37.842  32.405  36.898  1.00 55.98  ? 388 LEU C N   1 
ATOM   9671  C CA  . LEU C 1 359 ? 37.667  32.665  38.358  1.00 58.19  ? 388 LEU C CA  1 
ATOM   9672  C C   . LEU C 1 359 ? 37.564  31.319  39.108  1.00 54.96  ? 388 LEU C C   1 
ATOM   9673  O O   . LEU C 1 359 ? 38.007  31.262  40.263  1.00 62.95  ? 388 LEU C O   1 
ATOM   9674  C CB  . LEU C 1 359 ? 36.477  33.597  38.566  1.00 61.89  ? 388 LEU C CB  1 
ATOM   9675  C CG  . LEU C 1 359 ? 36.722  35.058  38.188  1.00 63.19  ? 388 LEU C CG  1 
ATOM   9676  C CD1 . LEU C 1 359 ? 35.831  35.980  38.991  1.00 65.41  ? 388 LEU C CD1 1 
ATOM   9677  C CD2 . LEU C 1 359 ? 38.179  35.416  38.398  1.00 67.47  ? 388 LEU C CD2 1 
ATOM   9678  N N   . LEU C 1 360 ? 37.018  30.284  38.472  1.00 52.86  ? 389 LEU C N   1 
ATOM   9679  C CA  . LEU C 1 360 ? 36.804  28.955  39.102  1.00 53.38  ? 389 LEU C CA  1 
ATOM   9680  C C   . LEU C 1 360 ? 38.134  28.303  39.508  1.00 55.50  ? 389 LEU C C   1 
ATOM   9681  O O   . LEU C 1 360 ? 38.273  27.942  40.686  1.00 53.49  ? 389 LEU C O   1 
ATOM   9682  C CB  . LEU C 1 360 ? 36.043  28.108  38.089  1.00 55.64  ? 389 LEU C CB  1 
ATOM   9683  C CG  . LEU C 1 360 ? 34.541  28.366  37.969  1.00 58.10  ? 389 LEU C CG  1 
ATOM   9684  C CD1 . LEU C 1 360 ? 33.989  27.644  36.754  1.00 55.68  ? 389 LEU C CD1 1 
ATOM   9685  C CD2 . LEU C 1 360 ? 33.845  27.892  39.227  1.00 56.92  ? 389 LEU C CD2 1 
ATOM   9686  N N   . GLU C 1 361 ? 39.072  28.158  38.574  1.00 53.82  ? 390 GLU C N   1 
ATOM   9687  C CA  . GLU C 1 361 ? 40.373  27.507  38.875  1.00 58.14  ? 390 GLU C CA  1 
ATOM   9688  C C   . GLU C 1 361 ? 41.042  28.189  40.075  1.00 53.25  ? 390 GLU C C   1 
ATOM   9689  O O   . GLU C 1 361 ? 41.481  27.481  40.990  1.00 52.23  ? 390 GLU C O   1 
ATOM   9690  C CB  . GLU C 1 361 ? 41.314  27.582  37.670  1.00 57.70  ? 390 GLU C CB  1 
ATOM   9691  C CG  . GLU C 1 361 ? 40.605  27.827  36.342  1.00 56.97  ? 390 GLU C CG  1 
ATOM   9692  C CD  . GLU C 1 361 ? 39.788  26.681  35.769  1.00 55.84  ? 390 GLU C CD  1 
ATOM   9693  O OE1 . GLU C 1 361 ? 39.088  25.986  36.531  1.00 55.01  ? 390 GLU C OE1 1 
ATOM   9694  O OE2 . GLU C 1 361 ? 39.831  26.501  34.538  1.00 53.58  ? 390 GLU C OE2 1 
ATOM   9695  N N   . GLN C 1 362 ? 41.125  29.508  40.053  1.00 50.24  ? 391 GLN C N   1 
ATOM   9696  C CA  . GLN C 1 362 ? 41.788  30.255  41.113  1.00 52.19  ? 391 GLN C CA  1 
ATOM   9697  C C   . GLN C 1 362 ? 41.173  29.905  42.470  1.00 53.52  ? 391 GLN C C   1 
ATOM   9698  O O   . GLN C 1 362 ? 41.842  30.033  43.489  1.00 55.61  ? 391 GLN C O   1 
ATOM   9699  C CB  . GLN C 1 362 ? 41.694  31.761  40.850  1.00 51.11  ? 391 GLN C CB  1 
ATOM   9700  C CG  . GLN C 1 362 ? 42.683  32.611  41.636  1.00 48.55  ? 391 GLN C CG  1 
ATOM   9701  C CD  . GLN C 1 362 ? 42.110  33.971  41.965  1.00 50.07  ? 391 GLN C CD  1 
ATOM   9702  O OE1 . GLN C 1 362 ? 40.897  34.155  42.046  1.00 50.57  ? 391 GLN C OE1 1 
ATOM   9703  N NE2 . GLN C 1 362 ? 42.982  34.937  42.192  1.00 50.21  ? 391 GLN C NE2 1 
ATOM   9704  N N   . GLY C 1 363 ? 39.890  29.513  42.488  1.00 57.17  ? 392 GLY C N   1 
ATOM   9705  C CA  . GLY C 1 363 ? 39.271  28.933  43.673  1.00 57.26  ? 392 GLY C CA  1 
ATOM   9706  C C   . GLY C 1 363 ? 38.746  29.995  44.636  1.00 58.39  ? 392 GLY C C   1 
ATOM   9707  O O   . GLY C 1 363 ? 37.726  29.793  45.287  1.00 55.56  ? 392 GLY C O   1 
ATOM   9708  N N   . LYS C 1 364 ? 39.383  31.161  44.651  1.00 62.23  ? 393 LYS C N   1 
ATOM   9709  C CA  . LYS C 1 364 ? 39.052  32.218  45.648  1.00 70.11  ? 393 LYS C CA  1 
ATOM   9710  C C   . LYS C 1 364 ? 37.612  32.779  45.546  1.00 72.40  ? 393 LYS C C   1 
ATOM   9711  O O   . LYS C 1 364 ? 37.038  33.086  46.617  1.00 82.60  ? 393 LYS C O   1 
ATOM   9712  C CB  . LYS C 1 364 ? 40.102  33.335  45.545  1.00 69.31  ? 393 LYS C CB  1 
ATOM   9713  C CG  . LYS C 1 364 ? 41.542  32.865  45.605  1.00 72.93  ? 393 LYS C CG  1 
ATOM   9714  C CD  . LYS C 1 364 ? 42.411  33.717  46.521  1.00 75.26  ? 393 LYS C CD  1 
ATOM   9715  C CE  . LYS C 1 364 ? 43.335  34.611  45.759  1.00 75.40  ? 393 LYS C CE  1 
ATOM   9716  N NZ  . LYS C 1 364 ? 43.300  35.990  46.252  1.00 74.67  ? 393 LYS C NZ  1 
ATOM   9717  N N   . ALA C 1 365 ? 37.050  32.966  44.351  1.00 69.15  ? 394 ALA C N   1 
ATOM   9718  C CA  . ALA C 1 365 ? 35.718  33.618  44.264  1.00 65.01  ? 394 ALA C CA  1 
ATOM   9719  C C   . ALA C 1 365 ? 34.582  32.618  44.494  1.00 59.50  ? 394 ALA C C   1 
ATOM   9720  O O   . ALA C 1 365 ? 34.533  31.620  43.771  1.00 62.97  ? 394 ALA C O   1 
ATOM   9721  C CB  . ALA C 1 365 ? 35.589  34.299  42.920  1.00 68.71  ? 394 ALA C CB  1 
ATOM   9722  N N   . LYS C 1 366 ? 33.689  32.880  45.448  1.00 57.34  ? 395 LYS C N   1 
ATOM   9723  C CA  . LYS C 1 366 ? 32.511  31.997  45.674  1.00 55.81  ? 395 LYS C CA  1 
ATOM   9724  C C   . LYS C 1 366 ? 31.589  32.123  44.467  1.00 49.81  ? 395 LYS C C   1 
ATOM   9725  O O   . LYS C 1 366 ? 31.037  31.112  44.024  1.00 50.80  ? 395 LYS C O   1 
ATOM   9726  C CB  . LYS C 1 366 ? 31.814  32.483  46.947  1.00 55.76  ? 395 LYS C CB  1 
ATOM   9727  C CG  . LYS C 1 366 ? 31.154  31.398  47.783  1.00 57.25  ? 395 LYS C CG  1 
ATOM   9728  C CD  . LYS C 1 366 ? 32.057  30.805  48.857  1.00 58.34  ? 395 LYS C CD  1 
ATOM   9729  C CE  . LYS C 1 366 ? 31.435  29.637  49.551  1.00 57.02  ? 395 LYS C CE  1 
ATOM   9730  N NZ  . LYS C 1 366 ? 31.215  28.507  48.646  1.00 55.37  ? 395 LYS C NZ  1 
ATOM   9731  N N   . ASN C 1 367 ? 31.412  33.335  43.992  1.00 47.47  ? 396 ASN C N   1 
ATOM   9732  C CA  . ASN C 1 367 ? 30.665  33.662  42.793  1.00 44.69  ? 396 ASN C CA  1 
ATOM   9733  C C   . ASN C 1 367 ? 31.640  34.014  41.675  1.00 43.32  ? 396 ASN C C   1 
ATOM   9734  O O   . ASN C 1 367 ? 32.202  35.106  41.680  1.00 41.13  ? 396 ASN C O   1 
ATOM   9735  C CB  . ASN C 1 367 ? 29.695  34.822  43.016  1.00 49.20  ? 396 ASN C CB  1 
ATOM   9736  C CG  . ASN C 1 367 ? 29.081  35.297  41.716  1.00 47.94  ? 396 ASN C CG  1 
ATOM   9737  O OD1 . ASN C 1 367 ? 29.269  34.656  40.684  1.00 53.71  ? 396 ASN C OD1 1 
ATOM   9738  N ND2 . ASN C 1 367 ? 28.352  36.402  41.748  1.00 45.27  ? 396 ASN C ND2 1 
ATOM   9739  N N   . PRO C 1 368 ? 31.845  33.117  40.678  1.00 41.84  ? 397 PRO C N   1 
ATOM   9740  C CA  . PRO C 1 368 ? 32.697  33.406  39.518  1.00 41.41  ? 397 PRO C CA  1 
ATOM   9741  C C   . PRO C 1 368 ? 32.054  34.132  38.327  1.00 42.43  ? 397 PRO C C   1 
ATOM   9742  O O   . PRO C 1 368 ? 32.715  34.358  37.306  1.00 40.15  ? 397 PRO C O   1 
ATOM   9743  C CB  . PRO C 1 368 ? 33.108  31.979  39.112  1.00 41.98  ? 397 PRO C CB  1 
ATOM   9744  C CG  . PRO C 1 368 ? 31.861  31.167  39.366  1.00 42.59  ? 397 PRO C CG  1 
ATOM   9745  C CD  . PRO C 1 368 ? 31.296  31.750  40.645  1.00 41.34  ? 397 PRO C CD  1 
ATOM   9746  N N   . TRP C 1 369 ? 30.776  34.526  38.473  1.00 40.07  ? 398 TRP C N   1 
ATOM   9747  C CA  . TRP C 1 369 ? 29.927  34.916  37.351  1.00 36.88  ? 398 TRP C CA  1 
ATOM   9748  C C   . TRP C 1 369 ? 29.684  36.427  37.363  1.00 35.65  ? 398 TRP C C   1 
ATOM   9749  O O   . TRP C 1 369 ? 29.755  37.043  38.422  1.00 34.60  ? 398 TRP C O   1 
ATOM   9750  C CB  . TRP C 1 369 ? 28.593  34.166  37.416  1.00 36.87  ? 398 TRP C CB  1 
ATOM   9751  C CG  . TRP C 1 369 ? 28.706  32.674  37.340  1.00 38.80  ? 398 TRP C CG  1 
ATOM   9752  C CD1 . TRP C 1 369 ? 28.560  31.781  38.364  1.00 38.40  ? 398 TRP C CD1 1 
ATOM   9753  C CD2 . TRP C 1 369 ? 28.900  31.892  36.151  1.00 36.67  ? 398 TRP C CD2 1 
ATOM   9754  N NE1 . TRP C 1 369 ? 28.691  30.501  37.903  1.00 35.37  ? 398 TRP C NE1 1 
ATOM   9755  C CE2 . TRP C 1 369 ? 28.903  30.538  36.548  1.00 41.74  ? 398 TRP C CE2 1 
ATOM   9756  C CE3 . TRP C 1 369 ? 29.103  32.207  34.802  1.00 40.47  ? 398 TRP C CE3 1 
ATOM   9757  C CZ2 . TRP C 1 369 ? 29.095  29.504  35.632  1.00 38.79  ? 398 TRP C CZ2 1 
ATOM   9758  C CZ3 . TRP C 1 369 ? 29.305  31.187  33.902  1.00 40.16  ? 398 TRP C CZ3 1 
ATOM   9759  C CH2 . TRP C 1 369 ? 29.306  29.856  34.318  1.00 41.34  ? 398 TRP C CH2 1 
ATOM   9760  N N   . PRO C 1 370 ? 29.363  37.057  36.207  1.00 29.82  ? 399 PRO C N   1 
ATOM   9761  C CA  . PRO C 1 370 ? 29.240  38.509  36.135  1.00 30.84  ? 399 PRO C CA  1 
ATOM   9762  C C   . PRO C 1 370 ? 27.994  39.001  36.857  1.00 29.13  ? 399 PRO C C   1 
ATOM   9763  O O   . PRO C 1 370 ? 27.036  38.265  37.059  1.00 27.62  ? 399 PRO C O   1 
ATOM   9764  C CB  . PRO C 1 370 ? 29.117  38.799  34.633  1.00 30.17  ? 399 PRO C CB  1 
ATOM   9765  C CG  . PRO C 1 370 ? 28.456  37.560  34.099  1.00 31.13  ? 399 PRO C CG  1 
ATOM   9766  C CD  . PRO C 1 370 ? 29.043  36.426  34.921  1.00 30.71  ? 399 PRO C CD  1 
ATOM   9767  N N   . ASN C 1 371 ? 28.043  40.267  37.254  1.00 30.50  ? 400 ASN C N   1 
ATOM   9768  C CA  . ASN C 1 371 ? 26.898  40.909  37.862  1.00 31.69  ? 400 ASN C CA  1 
ATOM   9769  C C   . ASN C 1 371 ? 26.558  42.093  36.965  1.00 30.11  ? 400 ASN C C   1 
ATOM   9770  O O   . ASN C 1 371 ? 27.274  42.340  35.998  1.00 28.33  ? 400 ASN C O   1 
ATOM   9771  C CB  . ASN C 1 371 ? 27.209  41.285  39.309  1.00 31.72  ? 400 ASN C CB  1 
ATOM   9772  C CG  . ASN C 1 371 ? 28.292  42.333  39.403  1.00 35.11  ? 400 ASN C CG  1 
ATOM   9773  O OD1 . ASN C 1 371 ? 28.111  43.462  38.955  1.00 41.46  ? 400 ASN C OD1 1 
ATOM   9774  N ND2 . ASN C 1 371 ? 29.438  41.974  39.947  1.00 38.08  ? 400 ASN C ND2 1 
ATOM   9775  N N   . VAL C 1 372 ? 25.485  42.820  37.317  1.00 29.95  ? 401 VAL C N   1 
ATOM   9776  C CA  . VAL C 1 372 ? 24.876  43.796  36.434  1.00 27.71  ? 401 VAL C CA  1 
ATOM   9777  C C   . VAL C 1 372 ? 25.913  44.813  35.949  1.00 28.63  ? 401 VAL C C   1 
ATOM   9778  O O   . VAL C 1 372 ? 25.867  45.245  34.787  1.00 26.23  ? 401 VAL C O   1 
ATOM   9779  C CB  . VAL C 1 372 ? 23.687  44.473  37.145  1.00 27.85  ? 401 VAL C CB  1 
ATOM   9780  C CG1 . VAL C 1 372 ? 24.127  45.330  38.312  1.00 26.19  ? 401 VAL C CG1 1 
ATOM   9781  C CG2 . VAL C 1 372 ? 22.816  45.265  36.182  1.00 28.68  ? 401 VAL C CG2 1 
ATOM   9782  N N   . ASP C 1 373 ? 26.866  45.150  36.833  1.00 27.08  ? 402 ASP C N   1 
ATOM   9783  C CA  . ASP C 1 373 ? 27.786  46.265  36.643  1.00 27.64  ? 402 ASP C CA  1 
ATOM   9784  C C   . ASP C 1 373 ? 28.818  45.933  35.565  1.00 25.42  ? 402 ASP C C   1 
ATOM   9785  O O   . ASP C 1 373 ? 29.520  46.809  35.077  1.00 24.52  ? 402 ASP C O   1 
ATOM   9786  C CB  . ASP C 1 373 ? 28.473  46.621  37.967  1.00 34.60  ? 402 ASP C CB  1 
ATOM   9787  C CG  . ASP C 1 373 ? 27.514  47.039  39.069  1.00 42.03  ? 402 ASP C CG  1 
ATOM   9788  O OD1 . ASP C 1 373 ? 26.615  47.902  38.799  1.00 49.35  ? 402 ASP C OD1 1 
ATOM   9789  O OD2 . ASP C 1 373 ? 27.677  46.520  40.197  1.00 47.44  ? 402 ASP C OD2 1 
ATOM   9790  N N   . ALA C 1 374 ? 28.940  44.647  35.232  1.00 23.16  ? 403 ALA C N   1 
ATOM   9791  C CA  . ALA C 1 374 ? 29.815  44.215  34.151  1.00 25.34  ? 403 ALA C CA  1 
ATOM   9792  C C   . ALA C 1 374 ? 29.383  44.729  32.780  1.00 26.90  ? 403 ALA C C   1 
ATOM   9793  O O   . ALA C 1 374 ? 30.219  44.771  31.878  1.00 27.97  ? 403 ALA C O   1 
ATOM   9794  C CB  . ALA C 1 374 ? 29.900  42.709  34.125  1.00 24.17  ? 403 ALA C CB  1 
ATOM   9795  N N   . HIS C 1 375 ? 28.090  45.058  32.609  1.00 25.24  ? 404 HIS C N   1 
ATOM   9796  C CA  . HIS C 1 375 ? 27.526  45.275  31.286  1.00 25.98  ? 404 HIS C CA  1 
ATOM   9797  C C   . HIS C 1 375 ? 27.016  46.703  31.081  1.00 26.82  ? 404 HIS C C   1 
ATOM   9798  O O   . HIS C 1 375 ? 27.006  47.192  29.959  1.00 27.38  ? 404 HIS C O   1 
ATOM   9799  C CB  . HIS C 1 375 ? 26.403  44.267  31.036  1.00 25.92  ? 404 HIS C CB  1 
ATOM   9800  C CG  . HIS C 1 375 ? 26.436  43.795  29.634  1.00 27.99  ? 404 HIS C CG  1 
ATOM   9801  N ND1 . HIS C 1 375 ? 26.457  42.462  29.286  1.00 30.32  ? 404 HIS C ND1 1 
ATOM   9802  C CD2 . HIS C 1 375 ? 26.490  44.489  28.492  1.00 27.02  ? 404 HIS C CD2 1 
ATOM   9803  C CE1 . HIS C 1 375 ? 26.488  42.369  27.962  1.00 27.36  ? 404 HIS C CE1 1 
ATOM   9804  N NE2 . HIS C 1 375 ? 26.528  43.582  27.462  1.00 30.56  ? 404 HIS C NE2 1 
ATOM   9805  N N   . SER C 1 376 ? 26.623  47.394  32.161  1.00 28.53  ? 405 SER C N   1 
ATOM   9806  C CA  . SER C 1 376 ? 25.823  48.604  32.024  1.00 27.18  ? 405 SER C CA  1 
ATOM   9807  C C   . SER C 1 376 ? 26.546  49.743  31.300  1.00 27.95  ? 405 SER C C   1 
ATOM   9808  O O   . SER C 1 376 ? 25.913  50.434  30.502  1.00 32.08  ? 405 SER C O   1 
ATOM   9809  C CB  . SER C 1 376 ? 25.258  49.049  33.359  1.00 29.78  ? 405 SER C CB  1 
ATOM   9810  O OG  . SER C 1 376 ? 26.193  48.949  34.417  1.00 32.63  ? 405 SER C OG  1 
ATOM   9811  N N   . GLY C 1 377 ? 27.839  49.948  31.559  1.00 28.45  ? 406 GLY C N   1 
ATOM   9812  C CA  . GLY C 1 377 ? 28.557  51.117  31.061  1.00 26.65  ? 406 GLY C CA  1 
ATOM   9813  C C   . GLY C 1 377 ? 28.785  51.106  29.549  1.00 27.33  ? 406 GLY C C   1 
ATOM   9814  O O   . GLY C 1 377 ? 28.812  52.162  28.921  1.00 23.94  ? 406 GLY C O   1 
ATOM   9815  N N   . VAL C 1 378 ? 29.039  49.930  28.965  1.00 27.07  ? 407 VAL C N   1 
ATOM   9816  C CA  . VAL C 1 378 ? 29.336  49.867  27.539  1.00 29.74  ? 407 VAL C CA  1 
ATOM   9817  C C   . VAL C 1 378 ? 28.089  50.249  26.737  1.00 30.02  ? 407 VAL C C   1 
ATOM   9818  O O   . VAL C 1 378 ? 28.209  50.811  25.657  1.00 30.72  ? 407 VAL C O   1 
ATOM   9819  C CB  . VAL C 1 378 ? 29.916  48.506  27.094  1.00 29.82  ? 407 VAL C CB  1 
ATOM   9820  C CG1 . VAL C 1 378 ? 31.188  48.185  27.858  1.00 32.26  ? 407 VAL C CG1 1 
ATOM   9821  C CG2 . VAL C 1 378 ? 28.924  47.365  27.196  1.00 32.47  ? 407 VAL C CG2 1 
ATOM   9822  N N   . LEU C 1 379 ? 26.910  49.954  27.297  1.00 33.29  ? 408 LEU C N   1 
ATOM   9823  C CA  . LEU C 1 379 ? 25.623  50.292  26.714  1.00 30.83  ? 408 LEU C CA  1 
ATOM   9824  C C   . LEU C 1 379 ? 25.402  51.796  26.776  1.00 30.38  ? 408 LEU C C   1 
ATOM   9825  O O   . LEU C 1 379 ? 25.079  52.426  25.760  1.00 27.23  ? 408 LEU C O   1 
ATOM   9826  C CB  . LEU C 1 379 ? 24.529  49.534  27.472  1.00 34.41  ? 408 LEU C CB  1 
ATOM   9827  C CG  . LEU C 1 379 ? 24.524  48.016  27.292  1.00 36.04  ? 408 LEU C CG  1 
ATOM   9828  C CD1 . LEU C 1 379 ? 23.378  47.376  28.054  1.00 36.52  ? 408 LEU C CD1 1 
ATOM   9829  C CD2 . LEU C 1 379 ? 24.436  47.651  25.811  1.00 40.00  ? 408 LEU C CD2 1 
ATOM   9830  N N   . LEU C 1 380 ? 25.583  52.366  27.977  1.00 29.81  ? 409 LEU C N   1 
ATOM   9831  C CA  . LEU C 1 380 ? 25.402  53.797  28.132  1.00 29.70  ? 409 LEU C CA  1 
ATOM   9832  C C   . LEU C 1 380 ? 26.397  54.537  27.243  1.00 29.99  ? 409 LEU C C   1 
ATOM   9833  O O   . LEU C 1 380 ? 26.033  55.476  26.549  1.00 26.51  ? 409 LEU C O   1 
ATOM   9834  C CB  . LEU C 1 380 ? 25.585  54.191  29.597  1.00 28.34  ? 409 LEU C CB  1 
ATOM   9835  C CG  . LEU C 1 380 ? 24.585  53.611  30.594  1.00 28.25  ? 409 LEU C CG  1 
ATOM   9836  C CD1 . LEU C 1 380 ? 25.013  53.983  32.008  1.00 27.55  ? 409 LEU C CD1 1 
ATOM   9837  C CD2 . LEU C 1 380 ? 23.146  54.073  30.306  1.00 27.68  ? 409 LEU C CD2 1 
ATOM   9838  N N   . GLN C 1 381 ? 27.667  54.118  27.248  1.00 32.69  ? 410 GLN C N   1 
ATOM   9839  C CA  . GLN C 1 381 ? 28.663  54.794  26.426  1.00 32.14  ? 410 GLN C CA  1 
ATOM   9840  C C   . GLN C 1 381 ? 28.251  54.722  24.953  1.00 31.20  ? 410 GLN C C   1 
ATOM   9841  O O   . GLN C 1 381 ? 28.405  55.701  24.215  1.00 28.40  ? 410 GLN C O   1 
ATOM   9842  C CB  . GLN C 1 381 ? 30.060  54.195  26.639  1.00 33.04  ? 410 GLN C CB  1 
ATOM   9843  C CG  . GLN C 1 381 ? 31.129  54.847  25.777  1.00 35.51  ? 410 GLN C CG  1 
ATOM   9844  C CD  . GLN C 1 381 ? 32.378  55.179  26.551  1.00 40.32  ? 410 GLN C CD  1 
ATOM   9845  O OE1 . GLN C 1 381 ? 33.236  54.332  26.781  1.00 42.30  ? 410 GLN C OE1 1 
ATOM   9846  N NE2 . GLN C 1 381 ? 32.496  56.441  26.936  1.00 45.88  ? 410 GLN C NE2 1 
ATOM   9847  N N   . TYR C 1 382 ? 27.700  53.578  24.531  1.00 32.08  ? 411 TYR C N   1 
ATOM   9848  C CA  . TYR C 1 382 ? 27.376  53.377  23.123  1.00 37.64  ? 411 TYR C CA  1 
ATOM   9849  C C   . TYR C 1 382 ? 26.328  54.370  22.613  1.00 35.51  ? 411 TYR C C   1 
ATOM   9850  O O   . TYR C 1 382 ? 26.410  54.806  21.461  1.00 33.65  ? 411 TYR C O   1 
ATOM   9851  C CB  . TYR C 1 382 ? 26.857  51.971  22.847  1.00 40.89  ? 411 TYR C CB  1 
ATOM   9852  C CG  . TYR C 1 382 ? 26.460  51.805  21.405  1.00 46.91  ? 411 TYR C CG  1 
ATOM   9853  C CD1 . TYR C 1 382 ? 27.397  52.002  20.403  1.00 48.03  ? 411 TYR C CD1 1 
ATOM   9854  C CD2 . TYR C 1 382 ? 25.150  51.545  21.036  1.00 48.03  ? 411 TYR C CD2 1 
ATOM   9855  C CE1 . TYR C 1 382 ? 27.058  51.886  19.066  1.00 49.85  ? 411 TYR C CE1 1 
ATOM   9856  C CE2 . TYR C 1 382 ? 24.792  51.428  19.703  1.00 50.37  ? 411 TYR C CE2 1 
ATOM   9857  C CZ  . TYR C 1 382 ? 25.751  51.599  18.717  1.00 51.49  ? 411 TYR C CZ  1 
ATOM   9858  O OH  . TYR C 1 382 ? 25.452  51.508  17.382  1.00 55.73  ? 411 TYR C OH  1 
ATOM   9859  N N   . TYR C 1 383 ? 25.374  54.748  23.478  1.00 34.60  ? 412 TYR C N   1 
ATOM   9860  C CA  . TYR C 1 383 ? 24.322  55.689  23.109  1.00 32.08  ? 412 TYR C CA  1 
ATOM   9861  C C   . TYR C 1 383 ? 24.747  57.134  23.373  1.00 28.27  ? 412 TYR C C   1 
ATOM   9862  O O   . TYR C 1 383 ? 23.960  58.058  23.168  1.00 30.41  ? 412 TYR C O   1 
ATOM   9863  C CB  . TYR C 1 383 ? 23.010  55.293  23.785  1.00 31.96  ? 412 TYR C CB  1 
ATOM   9864  C CG  . TYR C 1 383 ? 22.391  54.067  23.161  1.00 32.34  ? 412 TYR C CG  1 
ATOM   9865  C CD1 . TYR C 1 383 ? 21.795  54.119  21.911  1.00 32.08  ? 412 TYR C CD1 1 
ATOM   9866  C CD2 . TYR C 1 383 ? 22.449  52.840  23.792  1.00 31.47  ? 412 TYR C CD2 1 
ATOM   9867  C CE1 . TYR C 1 383 ? 21.236  52.996  21.321  1.00 34.32  ? 412 TYR C CE1 1 
ATOM   9868  C CE2 . TYR C 1 383 ? 21.908  51.702  23.214  1.00 35.04  ? 412 TYR C CE2 1 
ATOM   9869  C CZ  . TYR C 1 383 ? 21.306  51.778  21.966  1.00 30.82  ? 412 TYR C CZ  1 
ATOM   9870  O OH  . TYR C 1 383 ? 20.772  50.641  21.444  1.00 37.20  ? 412 TYR C OH  1 
ATOM   9871  N N   . GLY C 1 384 ? 26.001  57.334  23.786  1.00 29.25  ? 413 GLY C N   1 
ATOM   9872  C CA  . GLY C 1 384 ? 26.612  58.654  23.841  1.00 27.92  ? 413 GLY C CA  1 
ATOM   9873  C C   . GLY C 1 384 ? 26.630  59.246  25.245  1.00 31.25  ? 413 GLY C C   1 
ATOM   9874  O O   . GLY C 1 384 ? 27.033  60.397  25.447  1.00 30.73  ? 413 GLY C O   1 
ATOM   9875  N N   . MET C 1 385 ? 26.191  58.428  26.202  1.00 32.23  ? 414 MET C N   1 
ATOM   9876  C CA  . MET C 1 385 ? 26.178  58.758  27.617  1.00 31.83  ? 414 MET C CA  1 
ATOM   9877  C C   . MET C 1 385 ? 27.568  58.423  28.181  1.00 32.89  ? 414 MET C C   1 
ATOM   9878  O O   . MET C 1 385 ? 27.835  57.310  28.636  1.00 26.72  ? 414 MET C O   1 
ATOM   9879  C CB  . MET C 1 385 ? 25.018  57.954  28.226  1.00 32.96  ? 414 MET C CB  1 
ATOM   9880  C CG  . MET C 1 385 ? 24.993  57.708  29.726  1.00 34.88  ? 414 MET C CG  1 
ATOM   9881  S SD  . MET C 1 385 ? 24.086  58.896  30.719  1.00 32.40  ? 414 MET C SD  1 
ATOM   9882  C CE  . MET C 1 385 ? 22.404  58.741  30.122  1.00 35.39  ? 414 MET C CE  1 
ATOM   9883  N N   . THR C 1 386 ? 28.481  59.394  28.046  1.00 33.42  ? 415 THR C N   1 
ATOM   9884  C CA  . THR C 1 386 ? 29.911  59.211  28.248  1.00 36.60  ? 415 THR C CA  1 
ATOM   9885  C C   . THR C 1 386 ? 30.390  59.797  29.587  1.00 35.48  ? 415 THR C C   1 
ATOM   9886  O O   . THR C 1 386 ? 31.563  59.689  29.920  1.00 33.47  ? 415 THR C O   1 
ATOM   9887  C CB  . THR C 1 386 ? 30.697  59.897  27.123  1.00 39.32  ? 415 THR C CB  1 
ATOM   9888  O OG1 . THR C 1 386 ? 30.209  61.238  27.047  1.00 37.44  ? 415 THR C OG1 1 
ATOM   9889  C CG2 . THR C 1 386 ? 30.560  59.220  25.778  1.00 42.76  ? 415 THR C CG2 1 
ATOM   9890  N N   . GLU C 1 387 ? 29.506  60.461  30.342  1.00 31.89  ? 416 GLU C N   1 
ATOM   9891  C CA  . GLU C 1 387 ? 29.877  61.067  31.610  1.00 30.15  ? 416 GLU C CA  1 
ATOM   9892  C C   . GLU C 1 387 ? 29.770  60.001  32.711  1.00 29.69  ? 416 GLU C C   1 
ATOM   9893  O O   . GLU C 1 387 ? 28.722  59.824  33.336  1.00 24.03  ? 416 GLU C O   1 
ATOM   9894  C CB  . GLU C 1 387 ? 29.004  62.299  31.894  1.00 32.64  ? 416 GLU C CB  1 
ATOM   9895  C CG  . GLU C 1 387 ? 29.081  63.367  30.816  1.00 33.89  ? 416 GLU C CG  1 
ATOM   9896  C CD  . GLU C 1 387 ? 28.223  63.154  29.579  1.00 33.52  ? 416 GLU C CD  1 
ATOM   9897  O OE1 . GLU C 1 387 ? 27.543  62.121  29.485  1.00 29.99  ? 416 GLU C OE1 1 
ATOM   9898  O OE2 . GLU C 1 387 ? 28.255  64.028  28.693  1.00 38.38  ? 416 GLU C OE2 1 
ATOM   9899  N N   . MET C 1 388 ? 30.868  59.263  32.925  1.00 26.24  ? 417 MET C N   1 
ATOM   9900  C CA  . MET C 1 388 ? 30.857  58.096  33.786  1.00 26.17  ? 417 MET C CA  1 
ATOM   9901  C C   . MET C 1 388 ? 30.456  58.472  35.213  1.00 23.51  ? 417 MET C C   1 
ATOM   9902  O O   . MET C 1 388 ? 29.835  57.688  35.891  1.00 22.30  ? 417 MET C O   1 
ATOM   9903  C CB  . MET C 1 388 ? 32.237  57.438  33.824  1.00 29.61  ? 417 MET C CB  1 
ATOM   9904  C CG  . MET C 1 388 ? 32.712  56.972  32.463  1.00 35.26  ? 417 MET C CG  1 
ATOM   9905  S SD  . MET C 1 388 ? 34.228  56.000  32.579  1.00 48.38  ? 417 MET C SD  1 
ATOM   9906  C CE  . MET C 1 388 ? 35.068  56.825  33.932  1.00 46.45  ? 417 MET C CE  1 
ATOM   9907  N N   . ASN C 1 389 ? 30.724  59.695  35.678  1.00 22.49  ? 418 ASN C N   1 
ATOM   9908  C CA  . ASN C 1 389 ? 30.364  59.976  37.055  1.00 25.15  ? 418 ASN C CA  1 
ATOM   9909  C C   . ASN C 1 389 ? 28.852  60.032  37.218  1.00 23.48  ? 418 ASN C C   1 
ATOM   9910  O O   . ASN C 1 389 ? 28.376  59.944  38.343  1.00 27.29  ? 418 ASN C O   1 
ATOM   9911  C CB  . ASN C 1 389 ? 30.997  61.258  37.590  1.00 28.15  ? 418 ASN C CB  1 
ATOM   9912  C CG  . ASN C 1 389 ? 32.505  61.153  37.611  1.00 31.44  ? 418 ASN C CG  1 
ATOM   9913  O OD1 . ASN C 1 389 ? 33.062  60.079  37.849  1.00 27.67  ? 418 ASN C OD1 1 
ATOM   9914  N ND2 . ASN C 1 389 ? 33.165  62.242  37.268  1.00 34.43  ? 418 ASN C ND2 1 
ATOM   9915  N N   . TYR C 1 390 ? 28.102  60.139  36.109  1.00 24.99  ? 419 TYR C N   1 
ATOM   9916  C CA  . TYR C 1 390 ? 26.664  60.326  36.191  1.00 23.52  ? 419 TYR C CA  1 
ATOM   9917  C C   . TYR C 1 390 ? 25.964  58.976  36.294  1.00 22.43  ? 419 TYR C C   1 
ATOM   9918  O O   . TYR C 1 390 ? 24.788  58.895  36.622  1.00 22.11  ? 419 TYR C O   1 
ATOM   9919  C CB  . TYR C 1 390 ? 26.181  61.122  34.970  1.00 24.27  ? 419 TYR C CB  1 
ATOM   9920  C CG  . TYR C 1 390 ? 24.725  61.485  35.023  1.00 22.23  ? 419 TYR C CG  1 
ATOM   9921  C CD1 . TYR C 1 390 ? 24.270  62.518  35.819  1.00 24.35  ? 419 TYR C CD1 1 
ATOM   9922  C CD2 . TYR C 1 390 ? 23.790  60.753  34.320  1.00 24.60  ? 419 TYR C CD2 1 
ATOM   9923  C CE1 . TYR C 1 390 ? 22.931  62.847  35.881  1.00 21.48  ? 419 TYR C CE1 1 
ATOM   9924  C CE2 . TYR C 1 390 ? 22.441  61.070  34.360  1.00 23.72  ? 419 TYR C CE2 1 
ATOM   9925  C CZ  . TYR C 1 390 ? 22.004  62.117  35.160  1.00 23.21  ? 419 TYR C CZ  1 
ATOM   9926  O OH  . TYR C 1 390 ? 20.683  62.489  35.205  1.00 22.78  ? 419 TYR C OH  1 
ATOM   9927  N N   . TYR C 1 391 ? 26.664  57.896  35.940  1.00 21.99  ? 420 TYR C N   1 
ATOM   9928  C CA  . TYR C 1 391 ? 25.988  56.635  35.733  1.00 22.16  ? 420 TYR C CA  1 
ATOM   9929  C C   . TYR C 1 391 ? 25.195  56.277  36.977  1.00 22.60  ? 420 TYR C C   1 
ATOM   9930  O O   . TYR C 1 391 ? 24.098  55.755  36.879  1.00 24.41  ? 420 TYR C O   1 
ATOM   9931  C CB  . TYR C 1 391 ? 26.984  55.523  35.398  1.00 22.54  ? 420 TYR C CB  1 
ATOM   9932  C CG  . TYR C 1 391 ? 27.586  55.599  34.010  1.00 23.94  ? 420 TYR C CG  1 
ATOM   9933  C CD1 . TYR C 1 391 ? 27.120  56.507  33.066  1.00 25.34  ? 420 TYR C CD1 1 
ATOM   9934  C CD2 . TYR C 1 391 ? 28.675  54.815  33.667  1.00 24.25  ? 420 TYR C CD2 1 
ATOM   9935  C CE1 . TYR C 1 391 ? 27.685  56.591  31.806  1.00 25.18  ? 420 TYR C CE1 1 
ATOM   9936  C CE2 . TYR C 1 391 ? 29.252  54.887  32.404  1.00 26.79  ? 420 TYR C CE2 1 
ATOM   9937  C CZ  . TYR C 1 391 ? 28.770  55.801  31.483  1.00 25.84  ? 420 TYR C CZ  1 
ATOM   9938  O OH  . TYR C 1 391 ? 29.319  55.889  30.240  1.00 26.01  ? 420 TYR C OH  1 
ATOM   9939  N N   . THR C 1 392 ? 25.757  56.563  38.147  1.00 23.05  ? 421 THR C N   1 
ATOM   9940  C CA  . THR C 1 392 ? 25.110  56.086  39.348  1.00 23.71  ? 421 THR C CA  1 
ATOM   9941  C C   . THR C 1 392 ? 23.791  56.831  39.546  1.00 22.69  ? 421 THR C C   1 
ATOM   9942  O O   . THR C 1 392 ? 22.908  56.336  40.229  1.00 21.08  ? 421 THR C O   1 
ATOM   9943  C CB  . THR C 1 392 ? 26.027  56.148  40.568  1.00 23.23  ? 421 THR C CB  1 
ATOM   9944  O OG1 . THR C 1 392 ? 27.223  55.439  40.223  1.00 25.75  ? 421 THR C OG1 1 
ATOM   9945  C CG2 . THR C 1 392 ? 25.385  55.504  41.774  1.00 22.39  ? 421 THR C CG2 1 
ATOM   9946  N N   . VAL C 1 393 ? 23.657  58.027  38.971  1.00 23.38  ? 422 VAL C N   1 
ATOM   9947  C CA  . VAL C 1 393 ? 22.388  58.716  39.113  1.00 21.91  ? 422 VAL C CA  1 
ATOM   9948  C C   . VAL C 1 393 ? 21.235  57.937  38.476  1.00 19.88  ? 422 VAL C C   1 
ATOM   9949  O O   . VAL C 1 393 ? 20.150  57.951  39.033  1.00 18.43  ? 422 VAL C O   1 
ATOM   9950  C CB  . VAL C 1 393 ? 22.433  60.146  38.565  1.00 22.94  ? 422 VAL C CB  1 
ATOM   9951  C CG1 . VAL C 1 393 ? 21.060  60.772  38.688  1.00 25.73  ? 422 VAL C CG1 1 
ATOM   9952  C CG2 . VAL C 1 393 ? 23.479  60.994  39.259  1.00 24.95  ? 422 VAL C CG2 1 
ATOM   9953  N N   . LEU C 1 394 ? 21.432  57.354  37.278  1.00 20.84  ? 423 LEU C N   1 
ATOM   9954  C CA  . LEU C 1 394 ? 20.447  56.477  36.653  1.00 21.24  ? 423 LEU C CA  1 
ATOM   9955  C C   . LEU C 1 394 ? 20.044  55.335  37.603  1.00 21.64  ? 423 LEU C C   1 
ATOM   9956  O O   . LEU C 1 394 ? 18.864  55.012  37.742  1.00 21.89  ? 423 LEU C O   1 
ATOM   9957  C CB  . LEU C 1 394 ? 21.051  55.934  35.352  1.00 21.96  ? 423 LEU C CB  1 
ATOM   9958  C CG  . LEU C 1 394 ? 21.315  56.970  34.257  1.00 23.98  ? 423 LEU C CG  1 
ATOM   9959  C CD1 . LEU C 1 394 ? 21.781  56.285  32.965  1.00 24.62  ? 423 LEU C CD1 1 
ATOM   9960  C CD2 . LEU C 1 394 ? 20.047  57.777  33.990  1.00 25.60  ? 423 LEU C CD2 1 
ATOM   9961  N N   . PHE C 1 395 ? 21.046  54.713  38.238  1.00 20.26  ? 424 PHE C N   1 
ATOM   9962  C CA  . PHE C 1 395 ? 20.841  53.627  39.197  1.00 19.81  ? 424 PHE C CA  1 
ATOM   9963  C C   . PHE C 1 395 ? 19.941  54.147  40.325  1.00 19.92  ? 424 PHE C C   1 
ATOM   9964  O O   . PHE C 1 395 ? 18.957  53.532  40.690  1.00 19.89  ? 424 PHE C O   1 
ATOM   9965  C CB  . PHE C 1 395 ? 22.207  53.110  39.690  1.00 21.32  ? 424 PHE C CB  1 
ATOM   9966  C CG  . PHE C 1 395 ? 22.273  51.763  40.372  1.00 22.67  ? 424 PHE C CG  1 
ATOM   9967  C CD1 . PHE C 1 395 ? 21.150  51.076  40.773  1.00 25.99  ? 424 PHE C CD1 1 
ATOM   9968  C CD2 . PHE C 1 395 ? 23.508  51.151  40.570  1.00 26.95  ? 424 PHE C CD2 1 
ATOM   9969  C CE1 . PHE C 1 395 ? 21.248  49.821  41.365  1.00 27.46  ? 424 PHE C CE1 1 
ATOM   9970  C CE2 . PHE C 1 395 ? 23.609  49.892  41.144  1.00 25.94  ? 424 PHE C CE2 1 
ATOM   9971  C CZ  . PHE C 1 395 ? 22.469  49.222  41.530  1.00 27.10  ? 424 PHE C CZ  1 
ATOM   9972  N N   . GLY C 1 396 ? 20.223  55.362  40.805  1.00 18.15  ? 425 GLY C N   1 
ATOM   9973  C CA  . GLY C 1 396 ? 19.461  55.942  41.888  1.00 19.72  ? 425 GLY C CA  1 
ATOM   9974  C C   . GLY C 1 396 ? 17.986  56.135  41.528  1.00 20.28  ? 425 GLY C C   1 
ATOM   9975  O O   . GLY C 1 396 ? 17.117  55.801  42.318  1.00 18.47  ? 425 GLY C O   1 
ATOM   9976  N N   . VAL C 1 397 ? 17.719  56.691  40.345  1.00 19.76  ? 426 VAL C N   1 
ATOM   9977  C CA  . VAL C 1 397 ? 16.354  56.921  39.880  1.00 20.66  ? 426 VAL C CA  1 
ATOM   9978  C C   . VAL C 1 397 ? 15.606  55.596  39.811  1.00 19.90  ? 426 VAL C C   1 
ATOM   9979  O O   . VAL C 1 397 ? 14.456  55.527  40.183  1.00 25.11  ? 426 VAL C O   1 
ATOM   9980  C CB  . VAL C 1 397 ? 16.313  57.634  38.515  1.00 22.50  ? 426 VAL C CB  1 
ATOM   9981  C CG1 . VAL C 1 397 ? 14.893  57.654  37.969  1.00 21.32  ? 426 VAL C CG1 1 
ATOM   9982  C CG2 . VAL C 1 397 ? 16.875  59.046  38.571  1.00 22.06  ? 426 VAL C CG2 1 
ATOM   9983  N N   . SER C 1 398 ? 16.283  54.541  39.347  1.00 19.09  ? 427 SER C N   1 
ATOM   9984  C CA  . SER C 1 398 ? 15.684  53.226  39.256  1.00 15.41  ? 427 SER C CA  1 
ATOM   9985  C C   . SER C 1 398 ? 15.281  52.688  40.635  1.00 16.53  ? 427 SER C C   1 
ATOM   9986  O O   . SER C 1 398 ? 14.134  52.268  40.841  1.00 14.66  ? 427 SER C O   1 
ATOM   9987  C CB  . SER C 1 398 ? 16.613  52.287  38.592  1.00 17.57  ? 427 SER C CB  1 
ATOM   9988  O OG  . SER C 1 398 ? 16.084  50.962  38.678  1.00 16.36  ? 427 SER C OG  1 
ATOM   9989  N N   . ARG C 1 399 ? 16.268  52.699  41.534  1.00 16.05  ? 428 ARG C N   1 
ATOM   9990  C CA  . ARG C 1 399 ? 16.209  52.050  42.837  1.00 15.58  ? 428 ARG C CA  1 
ATOM   9991  C C   . ARG C 1 399 ? 15.133  52.728  43.681  1.00 14.06  ? 428 ARG C C   1 
ATOM   9992  O O   . ARG C 1 399 ? 14.621  52.161  44.607  1.00 15.87  ? 428 ARG C O   1 
ATOM   9993  C CB  . ARG C 1 399 ? 17.626  52.020  43.450  1.00 17.22  ? 428 ARG C CB  1 
ATOM   9994  C CG  . ARG C 1 399 ? 17.741  51.375  44.831  1.00 18.33  ? 428 ARG C CG  1 
ATOM   9995  C CD  . ARG C 1 399 ? 17.217  49.937  44.905  1.00 18.19  ? 428 ARG C CD  1 
ATOM   9996  N NE  . ARG C 1 399 ? 17.744  49.136  43.815  1.00 19.48  ? 428 ARG C NE  1 
ATOM   9997  C CZ  . ARG C 1 399 ? 18.725  48.254  43.930  1.00 19.89  ? 428 ARG C CZ  1 
ATOM   9998  N NH1 . ARG C 1 399 ? 19.487  48.246  45.006  1.00 18.07  ? 428 ARG C NH1 1 
ATOM   9999  N NH2 . ARG C 1 399 ? 18.961  47.398  42.953  1.00 20.01  ? 428 ARG C NH2 1 
ATOM   10000 N N   . ALA C 1 400 ? 14.784  53.988  43.394  1.00 16.64  ? 429 ALA C N   1 
ATOM   10001 C CA  . ALA C 1 400 ? 13.674  54.618  44.085  1.00 19.04  ? 429 ALA C CA  1 
ATOM   10002 C C   . ALA C 1 400 ? 12.396  53.792  43.972  1.00 19.80  ? 429 ALA C C   1 
ATOM   10003 O O   . ALA C 1 400 ? 11.627  53.727  44.923  1.00 19.48  ? 429 ALA C O   1 
ATOM   10004 C CB  . ALA C 1 400 ? 13.464  56.020  43.572  1.00 20.38  ? 429 ALA C CB  1 
ATOM   10005 N N   . LEU C 1 401 ? 12.205  53.123  42.826  1.00 19.42  ? 430 LEU C N   1 
ATOM   10006 C CA  . LEU C 1 401 ? 10.982  52.389  42.578  1.00 20.90  ? 430 LEU C CA  1 
ATOM   10007 C C   . LEU C 1 401 ? 10.868  51.282  43.629  1.00 21.85  ? 430 LEU C C   1 
ATOM   10008 O O   . LEU C 1 401 ? 9.814   51.104  44.237  1.00 21.53  ? 430 LEU C O   1 
ATOM   10009 C CB  . LEU C 1 401 ? 10.997  51.856  41.135  1.00 20.95  ? 430 LEU C CB  1 
ATOM   10010 C CG  . LEU C 1 401 ? 11.037  52.927  40.043  1.00 22.20  ? 430 LEU C CG  1 
ATOM   10011 C CD1 . LEU C 1 401 ? 11.082  52.322  38.656  1.00 24.14  ? 430 LEU C CD1 1 
ATOM   10012 C CD2 . LEU C 1 401 ? 9.821   53.839  40.128  1.00 22.56  ? 430 LEU C CD2 1 
ATOM   10013 N N   . GLY C 1 402 ? 11.964  50.564  43.867  1.00 18.54  ? 431 GLY C N   1 
ATOM   10014 C CA  . GLY C 1 402 ? 11.911  49.439  44.774  1.00 18.06  ? 431 GLY C CA  1 
ATOM   10015 C C   . GLY C 1 402 ? 11.812  49.859  46.241  1.00 17.89  ? 431 GLY C C   1 
ATOM   10016 O O   . GLY C 1 402 ? 10.968  49.353  46.995  1.00 18.45  ? 431 GLY C O   1 
ATOM   10017 N N   . VAL C 1 403 ? 12.704  50.768  46.676  1.00 17.48  ? 432 VAL C N   1 
ATOM   10018 C CA  . VAL C 1 403 ? 12.784  51.079  48.098  1.00 18.10  ? 432 VAL C CA  1 
ATOM   10019 C C   . VAL C 1 403 ? 11.529  51.842  48.555  1.00 18.14  ? 432 VAL C C   1 
ATOM   10020 O O   . VAL C 1 403 ? 11.084  51.674  49.701  1.00 18.91  ? 432 VAL C O   1 
ATOM   10021 C CB  . VAL C 1 403 ? 14.118  51.776  48.457  1.00 17.39  ? 432 VAL C CB  1 
ATOM   10022 C CG1 . VAL C 1 403 ? 15.344  51.003  47.943  1.00 17.29  ? 432 VAL C CG1 1 
ATOM   10023 C CG2 . VAL C 1 403 ? 14.170  53.219  47.976  1.00 18.91  ? 432 VAL C CG2 1 
ATOM   10024 N N   . LEU C 1 404 ? 10.935  52.666  47.676  1.00 19.12  ? 433 LEU C N   1 
ATOM   10025 C CA  . LEU C 1 404 ? 9.731   53.404  48.039  1.00 18.26  ? 433 LEU C CA  1 
ATOM   10026 C C   . LEU C 1 404 ? 8.512   52.478  48.036  1.00 19.59  ? 433 LEU C C   1 
ATOM   10027 O O   . LEU C 1 404 ? 7.666   52.565  48.927  1.00 21.73  ? 433 LEU C O   1 
ATOM   10028 C CB  . LEU C 1 404 ? 9.589   54.619  47.116  1.00 18.38  ? 433 LEU C CB  1 
ATOM   10029 C CG  . LEU C 1 404 ? 10.721  55.646  47.224  1.00 19.21  ? 433 LEU C CG  1 
ATOM   10030 C CD1 . LEU C 1 404 ? 10.510  56.828  46.279  1.00 19.43  ? 433 LEU C CD1 1 
ATOM   10031 C CD2 . LEU C 1 404 ? 10.857  56.172  48.658  1.00 19.30  ? 433 LEU C CD2 1 
ATOM   10032 N N   . ALA C 1 405 ? 8.448   51.539  47.090  1.00 19.41  ? 434 ALA C N   1 
ATOM   10033 C CA  . ALA C 1 405 ? 7.444   50.494  47.135  1.00 19.45  ? 434 ALA C CA  1 
ATOM   10034 C C   . ALA C 1 405 ? 7.507   49.770  48.476  1.00 21.08  ? 434 ALA C C   1 
ATOM   10035 O O   . ALA C 1 405 ? 6.491   49.562  49.145  1.00 19.59  ? 434 ALA C O   1 
ATOM   10036 C CB  . ALA C 1 405 ? 7.656   49.538  45.990  1.00 21.39  ? 434 ALA C CB  1 
ATOM   10037 N N   . GLN C 1 406 ? 8.708   49.364  48.920  1.00 19.76  ? 435 GLN C N   1 
ATOM   10038 C CA  . GLN C 1 406 ? 8.765   48.706  50.218  1.00 17.96  ? 435 GLN C CA  1 
ATOM   10039 C C   . GLN C 1 406 ? 8.467   49.674  51.360  1.00 17.86  ? 435 GLN C C   1 
ATOM   10040 O O   . GLN C 1 406 ? 7.869   49.273  52.351  1.00 20.22  ? 435 GLN C O   1 
ATOM   10041 C CB  . GLN C 1 406 ? 10.108  48.015  50.441  1.00 20.87  ? 435 GLN C CB  1 
ATOM   10042 C CG  . GLN C 1 406 ? 10.247  47.392  51.818  1.00 19.14  ? 435 GLN C CG  1 
ATOM   10043 C CD  . GLN C 1 406 ? 9.225   46.331  52.148  1.00 20.55  ? 435 GLN C CD  1 
ATOM   10044 O OE1 . GLN C 1 406 ? 8.854   45.528  51.303  1.00 23.24  ? 435 GLN C OE1 1 
ATOM   10045 N NE2 . GLN C 1 406 ? 8.750   46.323  53.386  1.00 20.59  ? 435 GLN C NE2 1 
ATOM   10046 N N   . LEU C 1 407 ? 8.897   50.954  51.256  1.00 18.04  ? 436 LEU C N   1 
ATOM   10047 C CA  . LEU C 1 407 ? 8.685   51.874  52.369  1.00 18.53  ? 436 LEU C CA  1 
ATOM   10048 C C   . LEU C 1 407 ? 7.190   51.996  52.706  1.00 19.03  ? 436 LEU C C   1 
ATOM   10049 O O   . LEU C 1 407 ? 6.796   52.053  53.887  1.00 19.45  ? 436 LEU C O   1 
ATOM   10050 C CB  . LEU C 1 407 ? 9.300   53.233  52.031  1.00 17.13  ? 436 LEU C CB  1 
ATOM   10051 C CG  . LEU C 1 407 ? 9.195   54.274  53.144  1.00 17.77  ? 436 LEU C CG  1 
ATOM   10052 C CD1 . LEU C 1 407 ? 9.963   53.835  54.395  1.00 18.03  ? 436 LEU C CD1 1 
ATOM   10053 C CD2 . LEU C 1 407 ? 9.659   55.634  52.652  1.00 17.75  ? 436 LEU C CD2 1 
ATOM   10054 N N   . ILE C 1 408 ? 6.365   52.019  51.662  1.00 18.63  ? 437 ILE C N   1 
ATOM   10055 C CA  . ILE C 1 408 ? 4.919   52.102  51.818  1.00 16.79  ? 437 ILE C CA  1 
ATOM   10056 C C   . ILE C 1 408 ? 4.423   50.915  52.635  1.00 16.12  ? 437 ILE C C   1 
ATOM   10057 O O   . ILE C 1 408 ? 3.600   51.060  53.535  1.00 17.65  ? 437 ILE C O   1 
ATOM   10058 C CB  . ILE C 1 408 ? 4.241   52.197  50.447  1.00 17.10  ? 437 ILE C CB  1 
ATOM   10059 C CG1 . ILE C 1 408 ? 4.599   53.518  49.752  1.00 17.05  ? 437 ILE C CG1 1 
ATOM   10060 C CG2 . ILE C 1 408 ? 2.724   52.019  50.575  1.00 16.31  ? 437 ILE C CG2 1 
ATOM   10061 C CD1 . ILE C 1 408 ? 4.445   53.494  48.274  1.00 20.35  ? 437 ILE C CD1 1 
ATOM   10062 N N   . TRP C 1 409 ? 4.934   49.740  52.287  1.00 16.40  ? 438 TRP C N   1 
ATOM   10063 C CA  . TRP C 1 409 ? 4.532   48.508  52.937  1.00 16.56  ? 438 TRP C CA  1 
ATOM   10064 C C   . TRP C 1 409 ? 5.014   48.437  54.386  1.00 15.12  ? 438 TRP C C   1 
ATOM   10065 O O   . TRP C 1 409 ? 4.249   48.058  55.270  1.00 16.47  ? 438 TRP C O   1 
ATOM   10066 C CB  . TRP C 1 409 ? 4.986   47.308  52.116  1.00 18.06  ? 438 TRP C CB  1 
ATOM   10067 C CG  . TRP C 1 409 ? 3.959   46.962  51.071  1.00 19.72  ? 438 TRP C CG  1 
ATOM   10068 C CD1 . TRP C 1 409 ? 4.009   47.189  49.734  1.00 18.85  ? 438 TRP C CD1 1 
ATOM   10069 C CD2 . TRP C 1 409 ? 2.664   46.387  51.316  1.00 19.83  ? 438 TRP C CD2 1 
ATOM   10070 N NE1 . TRP C 1 409 ? 2.836   46.809  49.129  1.00 22.30  ? 438 TRP C NE1 1 
ATOM   10071 C CE2 . TRP C 1 409 ? 2.013   46.265  50.071  1.00 21.56  ? 438 TRP C CE2 1 
ATOM   10072 C CE3 . TRP C 1 409 ? 2.042   45.885  52.453  1.00 20.30  ? 438 TRP C CE3 1 
ATOM   10073 C CZ2 . TRP C 1 409 ? 0.729   45.739  49.944  1.00 19.86  ? 438 TRP C CZ2 1 
ATOM   10074 C CZ3 . TRP C 1 409 ? 0.779   45.352  52.324  1.00 21.20  ? 438 TRP C CZ3 1 
ATOM   10075 C CH2 . TRP C 1 409 ? 0.129   45.310  51.100  1.00 20.29  ? 438 TRP C CH2 1 
ATOM   10076 N N   . SER C 1 410 ? 6.299   48.765  54.622  1.00 15.32  ? 439 SER C N   1 
ATOM   10077 C CA  . SER C 1 410 ? 6.874   48.837  55.963  1.00 16.22  ? 439 SER C CA  1 
ATOM   10078 C C   . SER C 1 410 ? 6.005   49.684  56.891  1.00 16.23  ? 439 SER C C   1 
ATOM   10079 O O   . SER C 1 410 ? 5.745   49.295  58.006  1.00 18.81  ? 439 SER C O   1 
ATOM   10080 C CB  . SER C 1 410 ? 8.287   49.347  55.940  1.00 17.26  ? 439 SER C CB  1 
ATOM   10081 O OG  . SER C 1 410 ? 9.102   48.547  55.090  1.00 18.74  ? 439 SER C OG  1 
ATOM   10082 N N   . ARG C 1 411 ? 5.554   50.865  56.451  1.00 20.49  ? 440 ARG C N   1 
ATOM   10083 C CA  . ARG C 1 411 ? 4.692   51.675  57.289  1.00 20.50  ? 440 ARG C CA  1 
ATOM   10084 C C   . ARG C 1 411 ? 3.261   51.143  57.378  1.00 20.54  ? 440 ARG C C   1 
ATOM   10085 O O   . ARG C 1 411 ? 2.673   51.219  58.457  1.00 23.25  ? 440 ARG C O   1 
ATOM   10086 C CB  . ARG C 1 411 ? 4.675   53.106  56.774  1.00 20.98  ? 440 ARG C CB  1 
ATOM   10087 C CG  . ARG C 1 411 ? 6.046   53.736  56.779  1.00 22.64  ? 440 ARG C CG  1 
ATOM   10088 C CD  . ARG C 1 411 ? 6.732   53.721  58.135  1.00 29.52  ? 440 ARG C CD  1 
ATOM   10089 N NE  . ARG C 1 411 ? 8.010   54.406  57.960  1.00 40.72  ? 440 ARG C NE  1 
ATOM   10090 C CZ  . ARG C 1 411 ? 8.132   55.681  57.575  1.00 40.97  ? 440 ARG C CZ  1 
ATOM   10091 N NH1 . ARG C 1 411 ? 7.124   56.524  57.730  1.00 49.18  ? 440 ARG C NH1 1 
ATOM   10092 N NH2 . ARG C 1 411 ? 9.274   56.138  57.092  1.00 31.97  ? 440 ARG C NH2 1 
ATOM   10093 N N   . ALA C 1 412 ? 2.729   50.593  56.279  1.00 19.49  ? 441 ALA C N   1 
ATOM   10094 C CA  . ALA C 1 412 ? 1.415   49.954  56.265  1.00 19.87  ? 441 ALA C CA  1 
ATOM   10095 C C   . ALA C 1 412 ? 1.374   48.809  57.274  1.00 21.31  ? 441 ALA C C   1 
ATOM   10096 O O   . ALA C 1 412 ? 0.395   48.667  57.995  1.00 20.63  ? 441 ALA C O   1 
ATOM   10097 C CB  . ALA C 1 412 ? 1.062   49.473  54.857  1.00 19.52  ? 441 ALA C CB  1 
ATOM   10098 N N   . LEU C 1 413 ? 2.457   48.029  57.355  1.00 20.89  ? 442 LEU C N   1 
ATOM   10099 C CA  . LEU C 1 413 ? 2.497   46.882  58.236  1.00 22.49  ? 442 LEU C CA  1 
ATOM   10100 C C   . LEU C 1 413 ? 3.027   47.201  59.635  1.00 23.65  ? 442 LEU C C   1 
ATOM   10101 O O   . LEU C 1 413 ? 3.187   46.291  60.433  1.00 26.59  ? 442 LEU C O   1 
ATOM   10102 C CB  . LEU C 1 413 ? 3.370   45.820  57.561  1.00 22.88  ? 442 LEU C CB  1 
ATOM   10103 C CG  . LEU C 1 413 ? 2.862   45.315  56.210  1.00 22.88  ? 442 LEU C CG  1 
ATOM   10104 C CD1 . LEU C 1 413 ? 3.866   44.351  55.593  1.00 23.22  ? 442 LEU C CD1 1 
ATOM   10105 C CD2 . LEU C 1 413 ? 1.516   44.629  56.378  1.00 22.45  ? 442 LEU C CD2 1 
ATOM   10106 N N   . GLY C 1 414 ? 3.265   48.481  59.956  1.00 22.86  ? 443 GLY C N   1 
ATOM   10107 C CA  . GLY C 1 414 ? 3.714   48.893  61.281  1.00 24.07  ? 443 GLY C CA  1 
ATOM   10108 C C   . GLY C 1 414 ? 5.086   48.329  61.679  1.00 22.65  ? 443 GLY C C   1 
ATOM   10109 O O   . GLY C 1 414 ? 5.320   48.125  62.862  1.00 22.17  ? 443 GLY C O   1 
ATOM   10110 N N   . PHE C 1 415 ? 5.994   48.091  60.713  1.00 21.86  ? 444 PHE C N   1 
ATOM   10111 C CA  . PHE C 1 415 ? 7.355   47.684  61.044  1.00 20.62  ? 444 PHE C CA  1 
ATOM   10112 C C   . PHE C 1 415 ? 7.972   48.742  61.948  1.00 21.54  ? 444 PHE C C   1 
ATOM   10113 O O   . PHE C 1 415 ? 7.777   49.931  61.704  1.00 21.94  ? 444 PHE C O   1 
ATOM   10114 C CB  . PHE C 1 415 ? 8.254   47.551  59.800  1.00 22.34  ? 444 PHE C CB  1 
ATOM   10115 C CG  . PHE C 1 415 ? 7.992   46.357  58.926  1.00 21.86  ? 444 PHE C CG  1 
ATOM   10116 C CD1 . PHE C 1 415 ? 6.985   45.461  59.223  1.00 25.11  ? 444 PHE C CD1 1 
ATOM   10117 C CD2 . PHE C 1 415 ? 8.741   46.149  57.776  1.00 21.98  ? 444 PHE C CD2 1 
ATOM   10118 C CE1 . PHE C 1 415 ? 6.742   44.376  58.396  1.00 26.19  ? 444 PHE C CE1 1 
ATOM   10119 C CE2 . PHE C 1 415 ? 8.488   45.064  56.948  1.00 23.87  ? 444 PHE C CE2 1 
ATOM   10120 C CZ  . PHE C 1 415 ? 7.473   44.190  57.253  1.00 21.38  ? 444 PHE C CZ  1 
ATOM   10121 N N   . PRO C 1 416 ? 8.615   48.377  63.077  1.00 22.43  ? 445 PRO C N   1 
ATOM   10122 C CA  . PRO C 1 416 ? 9.111   49.386  64.015  1.00 22.13  ? 445 PRO C CA  1 
ATOM   10123 C C   . PRO C 1 416 ? 10.566  49.765  63.743  1.00 20.88  ? 445 PRO C C   1 
ATOM   10124 O O   . PRO C 1 416 ? 11.196  49.247  62.831  1.00 20.89  ? 445 PRO C O   1 
ATOM   10125 C CB  . PRO C 1 416 ? 8.925   48.699  65.374  1.00 21.14  ? 445 PRO C CB  1 
ATOM   10126 C CG  . PRO C 1 416 ? 9.007   47.182  65.073  1.00 24.15  ? 445 PRO C CG  1 
ATOM   10127 C CD  . PRO C 1 416 ? 8.845   47.006  63.570  1.00 23.73  ? 445 PRO C CD  1 
ATOM   10128 N N   . LEU C 1 417 ? 11.092  50.643  64.598  1.00 22.53  ? 446 LEU C N   1 
ATOM   10129 C CA  . LEU C 1 417 ? 12.495  51.049  64.602  1.00 20.99  ? 446 LEU C CA  1 
ATOM   10130 C C   . LEU C 1 417 ? 13.426  49.852  64.398  1.00 19.73  ? 446 LEU C C   1 
ATOM   10131 O O   . LEU C 1 417 ? 13.423  48.913  65.184  1.00 20.71  ? 446 LEU C O   1 
ATOM   10132 C CB  . LEU C 1 417 ? 12.782  51.737  65.943  1.00 23.25  ? 446 LEU C CB  1 
ATOM   10133 C CG  . LEU C 1 417 ? 14.037  52.610  65.971  1.00 24.50  ? 446 LEU C CG  1 
ATOM   10134 C CD1 . LEU C 1 417 ? 13.828  53.886  65.166  1.00 22.37  ? 446 LEU C CD1 1 
ATOM   10135 C CD2 . LEU C 1 417 ? 14.440  52.956  67.399  1.00 23.62  ? 446 LEU C CD2 1 
ATOM   10136 N N   . GLU C 1 418 ? 14.273  49.938  63.377  1.00 17.52  ? 447 GLU C N   1 
ATOM   10137 C CA  . GLU C 1 418 ? 15.346  48.973  63.199  1.00 20.91  ? 447 GLU C CA  1 
ATOM   10138 C C   . GLU C 1 418 ? 16.449  49.355  64.173  1.00 22.04  ? 447 GLU C C   1 
ATOM   10139 O O   . GLU C 1 418 ? 16.969  50.464  64.148  1.00 22.49  ? 447 GLU C O   1 
ATOM   10140 C CB  . GLU C 1 418 ? 15.857  48.905  61.761  1.00 20.87  ? 447 GLU C CB  1 
ATOM   10141 C CG  . GLU C 1 418 ? 16.912  47.832  61.561  1.00 20.71  ? 447 GLU C CG  1 
ATOM   10142 C CD  . GLU C 1 418 ? 17.476  47.735  60.149  1.00 21.10  ? 447 GLU C CD  1 
ATOM   10143 O OE1 . GLU C 1 418 ? 16.678  47.570  59.244  1.00 22.15  ? 447 GLU C OE1 1 
ATOM   10144 O OE2 . GLU C 1 418 ? 18.732  47.855  59.977  1.00 20.32  ? 447 GLU C OE2 1 
ATOM   10145 N N   . ARG C 1 419 ? 16.757  48.446  65.094  1.00 21.84  ? 448 ARG C N   1 
ATOM   10146 C CA  . ARG C 1 419 ? 17.596  48.789  66.222  1.00 21.69  ? 448 ARG C CA  1 
ATOM   10147 C C   . ARG C 1 419 ? 18.144  47.477  66.757  1.00 22.27  ? 448 ARG C C   1 
ATOM   10148 O O   . ARG C 1 419 ? 17.632  46.911  67.711  1.00 23.45  ? 448 ARG C O   1 
ATOM   10149 C CB  . ARG C 1 419 ? 16.792  49.651  67.200  1.00 22.91  ? 448 ARG C CB  1 
ATOM   10150 C CG  . ARG C 1 419 ? 17.402  49.930  68.574  1.00 24.38  ? 448 ARG C CG  1 
ATOM   10151 C CD  . ARG C 1 419 ? 18.883  49.799  68.802  1.00 20.41  ? 448 ARG C CD  1 
ATOM   10152 N NE  . ARG C 1 419 ? 19.544  50.800  69.644  1.00 21.16  ? 448 ARG C NE  1 
ATOM   10153 C CZ  . ARG C 1 419 ? 20.787  50.684  70.096  1.00 19.07  ? 448 ARG C CZ  1 
ATOM   10154 N NH1 . ARG C 1 419 ? 21.368  51.724  70.663  1.00 19.67  ? 448 ARG C NH1 1 
ATOM   10155 N NH2 . ARG C 1 419 ? 21.468  49.547  69.937  1.00 19.56  ? 448 ARG C NH2 1 
ATOM   10156 N N   . PRO C 1 420 ? 19.186  46.937  66.094  1.00 22.43  ? 449 PRO C N   1 
ATOM   10157 C CA  . PRO C 1 420 ? 19.885  45.763  66.620  1.00 23.05  ? 449 PRO C CA  1 
ATOM   10158 C C   . PRO C 1 420 ? 20.783  46.114  67.814  1.00 22.80  ? 449 PRO C C   1 
ATOM   10159 O O   . PRO C 1 420 ? 21.003  47.273  68.160  1.00 18.70  ? 449 PRO C O   1 
ATOM   10160 C CB  . PRO C 1 420 ? 20.697  45.303  65.400  1.00 21.72  ? 449 PRO C CB  1 
ATOM   10161 C CG  . PRO C 1 420 ? 21.067  46.611  64.726  1.00 23.07  ? 449 PRO C CG  1 
ATOM   10162 C CD  . PRO C 1 420 ? 19.786  47.420  64.842  1.00 21.34  ? 449 PRO C CD  1 
ATOM   10163 N N   . LYS C 1 421 ? 21.311  45.075  68.445  1.00 21.53  ? 450 LYS C N   1 
ATOM   10164 C CA  . LYS C 1 421 ? 22.327  45.215  69.472  1.00 25.75  ? 450 LYS C CA  1 
ATOM   10165 C C   . LYS C 1 421 ? 23.723  45.135  68.861  1.00 23.91  ? 450 LYS C C   1 
ATOM   10166 O O   . LYS C 1 421 ? 23.944  44.344  67.932  1.00 21.78  ? 450 LYS C O   1 
ATOM   10167 C CB  . LYS C 1 421 ? 22.165  44.099  70.511  1.00 26.81  ? 450 LYS C CB  1 
ATOM   10168 C CG  . LYS C 1 421 ? 23.035  44.276  71.739  1.00 28.54  ? 450 LYS C CG  1 
ATOM   10169 C CD  . LYS C 1 421 ? 22.812  45.633  72.378  1.00 30.37  ? 450 LYS C CD  1 
ATOM   10170 C CE  . LYS C 1 421 ? 23.602  45.837  73.647  1.00 32.44  ? 450 LYS C CE  1 
ATOM   10171 N NZ  . LYS C 1 421 ? 22.957  45.160  74.783  1.00 34.27  ? 450 LYS C NZ  1 
ATOM   10172 N N   . SER C 1 422 ? 24.636  45.991  69.347  1.00 22.77  ? 451 SER C N   1 
ATOM   10173 C CA  . SER C 1 422 ? 26.036  45.905  68.970  1.00 23.28  ? 451 SER C CA  1 
ATOM   10174 C C   . SER C 1 422 ? 26.881  45.380  70.131  1.00 23.11  ? 451 SER C C   1 
ATOM   10175 O O   . SER C 1 422 ? 26.446  45.324  71.280  1.00 22.92  ? 451 SER C O   1 
ATOM   10176 C CB  . SER C 1 422 ? 26.583  47.206  68.425  1.00 23.00  ? 451 SER C CB  1 
ATOM   10177 O OG  . SER C 1 422 ? 26.533  48.264  69.382  1.00 20.95  ? 451 SER C OG  1 
ATOM   10178 N N   . MET C 1 423 ? 28.117  44.989  69.814  1.00 25.07  ? 452 MET C N   1 
ATOM   10179 C CA  . MET C 1 423 ? 29.065  44.707  70.874  1.00 27.44  ? 452 MET C CA  1 
ATOM   10180 C C   . MET C 1 423 ? 30.424  45.227  70.456  1.00 25.26  ? 452 MET C C   1 
ATOM   10181 O O   . MET C 1 423 ? 30.694  45.374  69.264  1.00 24.32  ? 452 MET C O   1 
ATOM   10182 C CB  . MET C 1 423 ? 29.169  43.203  71.140  1.00 31.82  ? 452 MET C CB  1 
ATOM   10183 C CG  . MET C 1 423 ? 27.884  42.557  71.646  1.00 36.75  ? 452 MET C CG  1 
ATOM   10184 S SD  . MET C 1 423 ? 27.489  42.866  73.394  1.00 48.67  ? 452 MET C SD  1 
ATOM   10185 C CE  . MET C 1 423 ? 27.782  41.239  74.095  1.00 46.39  ? 452 MET C CE  1 
ATOM   10186 N N   . SER C 1 424 ? 31.282  45.445  71.450  1.00 24.50  ? 453 SER C N   1 
ATOM   10187 C CA  . SER C 1 424 ? 32.680  45.744  71.178  1.00 24.51  ? 453 SER C CA  1 
ATOM   10188 C C   . SER C 1 424 ? 33.453  44.425  71.042  1.00 24.71  ? 453 SER C C   1 
ATOM   10189 O O   . SER C 1 424 ? 32.951  43.371  71.444  1.00 24.86  ? 453 SER C O   1 
ATOM   10190 C CB  . SER C 1 424 ? 33.220  46.559  72.289  1.00 27.21  ? 453 SER C CB  1 
ATOM   10191 O OG  . SER C 1 424 ? 33.240  45.739  73.445  1.00 26.67  ? 453 SER C OG  1 
ATOM   10192 N N   . THR C 1 425 ? 34.689  44.503  70.538  1.00 27.60  ? 454 THR C N   1 
ATOM   10193 C CA  . THR C 1 425 ? 35.572  43.340  70.518  1.00 27.89  ? 454 THR C CA  1 
ATOM   10194 C C   . THR C 1 425 ? 35.838  42.880  71.955  1.00 30.79  ? 454 THR C C   1 
ATOM   10195 O O   . THR C 1 425 ? 35.842  41.678  72.243  1.00 29.35  ? 454 THR C O   1 
ATOM   10196 C CB  . THR C 1 425 ? 36.861  43.610  69.740  1.00 28.57  ? 454 THR C CB  1 
ATOM   10197 O OG1 . THR C 1 425 ? 36.601  43.757  68.328  1.00 28.28  ? 454 THR C OG1 1 
ATOM   10198 C CG2 . THR C 1 425 ? 37.871  42.504  69.969  1.00 26.63  ? 454 THR C CG2 1 
ATOM   10199 N N   . GLU C 1 426 ? 36.082  43.851  72.844  1.00 29.92  ? 455 GLU C N   1 
ATOM   10200 C CA  . GLU C 1 426 ? 36.318  43.609  74.264  1.00 32.24  ? 455 GLU C CA  1 
ATOM   10201 C C   . GLU C 1 426 ? 35.156  42.829  74.877  1.00 31.89  ? 455 GLU C C   1 
ATOM   10202 O O   . GLU C 1 426 ? 35.368  41.809  75.532  1.00 29.95  ? 455 GLU C O   1 
ATOM   10203 C CB  . GLU C 1 426 ? 36.517  44.944  74.987  1.00 36.61  ? 455 GLU C CB  1 
ATOM   10204 C CG  . GLU C 1 426 ? 36.522  44.842  76.517  1.00 44.09  ? 455 GLU C CG  1 
ATOM   10205 C CD  . GLU C 1 426 ? 36.135  46.110  77.272  1.00 50.25  ? 455 GLU C CD  1 
ATOM   10206 O OE1 . GLU C 1 426 ? 36.108  47.210  76.655  1.00 53.25  ? 455 GLU C OE1 1 
ATOM   10207 O OE2 . GLU C 1 426 ? 35.839  45.998  78.487  1.00 57.41  ? 455 GLU C OE2 1 
ATOM   10208 N N   . GLY C 1 427 ? 33.928  43.322  74.656  1.00 31.57  ? 456 GLY C N   1 
ATOM   10209 C CA  . GLY C 1 427 ? 32.731  42.730  75.229  1.00 31.61  ? 456 GLY C CA  1 
ATOM   10210 C C   . GLY C 1 427 ? 32.412  41.359  74.635  1.00 31.99  ? 456 GLY C C   1 
ATOM   10211 O O   . GLY C 1 427 ? 31.877  40.499  75.323  1.00 34.03  ? 456 GLY C O   1 
ATOM   10212 N N   . LEU C 1 428 ? 32.776  41.170  73.361  1.00 31.41  ? 457 LEU C N   1 
ATOM   10213 C CA  . LEU C 1 428 ? 32.464  39.959  72.627  1.00 34.36  ? 457 LEU C CA  1 
ATOM   10214 C C   . LEU C 1 428 ? 33.405  38.838  73.054  1.00 36.21  ? 457 LEU C C   1 
ATOM   10215 O O   . LEU C 1 428 ? 33.009  37.675  73.040  1.00 38.31  ? 457 LEU C O   1 
ATOM   10216 C CB  . LEU C 1 428 ? 32.598  40.274  71.131  1.00 37.95  ? 457 LEU C CB  1 
ATOM   10217 C CG  . LEU C 1 428 ? 31.845  39.346  70.193  1.00 36.21  ? 457 LEU C CG  1 
ATOM   10218 C CD1 . LEU C 1 428 ? 30.380  39.260  70.584  1.00 36.24  ? 457 LEU C CD1 1 
ATOM   10219 C CD2 . LEU C 1 428 ? 32.005  39.810  68.756  1.00 39.53  ? 457 LEU C CD2 1 
ATOM   10220 N N   . MET C 1 429 ? 34.643  39.212  73.410  1.00 36.86  ? 458 MET C N   1 
ATOM   10221 C CA  . MET C 1 429 ? 35.622  38.308  74.000  1.00 36.47  ? 458 MET C CA  1 
ATOM   10222 C C   . MET C 1 429 ? 35.163  37.876  75.388  1.00 37.65  ? 458 MET C C   1 
ATOM   10223 O O   . MET C 1 429 ? 35.299  36.710  75.751  1.00 38.97  ? 458 MET C O   1 
ATOM   10224 C CB  . MET C 1 429 ? 36.985  38.991  74.154  1.00 37.45  ? 458 MET C CB  1 
ATOM   10225 C CG  . MET C 1 429 ? 37.799  39.061  72.877  1.00 39.96  ? 458 MET C CG  1 
ATOM   10226 S SD  . MET C 1 429 ? 39.244  40.139  73.111  1.00 45.97  ? 458 MET C SD  1 
ATOM   10227 C CE  . MET C 1 429 ? 40.492  38.902  73.483  1.00 43.71  ? 458 MET C CE  1 
ATOM   10228 N N   . LYS C 1 430 ? 34.634  38.832  76.163  1.00 40.42  ? 459 LYS C N   1 
ATOM   10229 C CA  . LYS C 1 430 ? 34.071  38.552  77.477  1.00 42.74  ? 459 LYS C CA  1 
ATOM   10230 C C   . LYS C 1 430 ? 32.854  37.641  77.350  1.00 44.11  ? 459 LYS C C   1 
ATOM   10231 O O   . LYS C 1 430 ? 32.732  36.654  78.073  1.00 49.83  ? 459 LYS C O   1 
ATOM   10232 C CB  . LYS C 1 430 ? 33.688  39.846  78.202  1.00 43.78  ? 459 LYS C CB  1 
ATOM   10233 C CG  . LYS C 1 430 ? 34.868  40.751  78.517  1.00 47.17  ? 459 LYS C CG  1 
ATOM   10234 C CD  . LYS C 1 430 ? 34.704  41.609  79.756  1.00 50.63  ? 459 LYS C CD  1 
ATOM   10235 C CE  . LYS C 1 430 ? 35.750  42.704  79.857  1.00 50.36  ? 459 LYS C CE  1 
ATOM   10236 N NZ  . LYS C 1 430 ? 37.128  42.200  79.621  1.00 46.48  ? 459 LYS C NZ  1 
ATOM   10237 N N   . PHE C 1 431 ? 31.965  37.983  76.421  1.00 42.73  ? 460 PHE C N   1 
ATOM   10238 C CA  . PHE C 1 431 ? 30.696  37.292  76.274  1.00 45.51  ? 460 PHE C CA  1 
ATOM   10239 C C   . PHE C 1 431 ? 30.961  35.802  76.063  1.00 52.78  ? 460 PHE C C   1 
ATOM   10240 O O   . PHE C 1 431 ? 30.290  34.962  76.661  1.00 55.00  ? 460 PHE C O   1 
ATOM   10241 C CB  . PHE C 1 431 ? 29.907  37.925  75.120  1.00 48.64  ? 460 PHE C CB  1 
ATOM   10242 C CG  . PHE C 1 431 ? 28.456  37.520  74.993  1.00 51.34  ? 460 PHE C CG  1 
ATOM   10243 C CD1 . PHE C 1 431 ? 27.519  37.878  75.958  1.00 53.34  ? 460 PHE C CD1 1 
ATOM   10244 C CD2 . PHE C 1 431 ? 28.009  36.823  73.876  1.00 51.31  ? 460 PHE C CD2 1 
ATOM   10245 C CE1 . PHE C 1 431 ? 26.183  37.524  75.819  1.00 49.94  ? 460 PHE C CE1 1 
ATOM   10246 C CE2 . PHE C 1 431 ? 26.675  36.465  73.743  1.00 47.19  ? 460 PHE C CE2 1 
ATOM   10247 C CZ  . PHE C 1 431 ? 25.763  36.822  74.709  1.00 46.82  ? 460 PHE C CZ  1 
ATOM   10248 N N   . VAL C 1 432 ? 31.965  35.497  75.227  1.00 57.02  ? 461 VAL C N   1 
ATOM   10249 C CA  . VAL C 1 432 ? 32.228  34.149  74.742  1.00 57.92  ? 461 VAL C CA  1 
ATOM   10250 C C   . VAL C 1 432 ? 32.753  33.250  75.867  1.00 58.43  ? 461 VAL C C   1 
ATOM   10251 O O   . VAL C 1 432 ? 32.506  32.045  75.857  1.00 66.30  ? 461 VAL C O   1 
ATOM   10252 C CB  . VAL C 1 432 ? 33.194  34.191  73.538  1.00 58.19  ? 461 VAL C CB  1 
ATOM   10253 C CG1 . VAL C 1 432 ? 33.837  32.843  73.253  1.00 61.76  ? 461 VAL C CG1 1 
ATOM   10254 C CG2 . VAL C 1 432 ? 32.506  34.715  72.288  1.00 57.70  ? 461 VAL C CG2 1 
ATOM   10255 N N   . ASP C 1 433 ? 33.483  33.826  76.826  1.00 52.82  ? 462 ASP C N   1 
ATOM   10256 C CA  . ASP C 1 433 ? 34.071  33.048  77.905  1.00 56.55  ? 462 ASP C CA  1 
ATOM   10257 C C   . ASP C 1 433 ? 32.992  32.621  78.897  1.00 55.50  ? 462 ASP C C   1 
ATOM   10258 O O   . ASP C 1 433 ? 32.855  31.435  79.190  1.00 51.00  ? 462 ASP C O   1 
ATOM   10259 C CB  . ASP C 1 433 ? 35.166  33.852  78.602  1.00 57.47  ? 462 ASP C CB  1 
ATOM   10260 C CG  . ASP C 1 433 ? 36.217  34.338  77.624  1.00 57.36  ? 462 ASP C CG  1 
ATOM   10261 O OD1 . ASP C 1 433 ? 36.296  33.756  76.521  1.00 63.28  ? 462 ASP C OD1 1 
ATOM   10262 O OD2 . ASP C 1 433 ? 36.907  35.319  77.947  1.00 54.49  ? 462 ASP C OD2 1 
ATOM   10263 N N   . SER C 1 434 ? 32.242  33.609  79.400  1.00 57.78  ? 463 SER C N   1 
ATOM   10264 C CA  . SER C 1 434 ? 31.172  33.394  80.363  1.00 59.84  ? 463 SER C CA  1 
ATOM   10265 C C   . SER C 1 434 ? 30.707  31.935  80.335  1.00 60.18  ? 463 SER C C   1 
ATOM   10266 O O   . SER C 1 434 ? 29.480  31.737  80.260  1.00 59.98  ? 463 SER C O   1 
ATOM   10267 C CB  . SER C 1 434 ? 30.013  34.337  80.105  1.00 61.62  ? 463 SER C CB  1 
ATOM   10268 O OG  . SER C 1 434 ? 30.459  35.682  80.040  1.00 62.29  ? 463 SER C OG  1 
ATOM   10269 N N   . SER D 1 1   ? 53.385  62.514  2.119   1.00 68.26  ? 30  SER D N   1 
ATOM   10270 C CA  . SER D 1 1   ? 53.123  63.910  2.560   1.00 63.38  ? 30  SER D CA  1 
ATOM   10271 C C   . SER D 1 1   ? 51.614  64.132  2.630   1.00 65.49  ? 30  SER D C   1 
ATOM   10272 O O   . SER D 1 1   ? 50.912  63.502  3.437   1.00 51.28  ? 30  SER D O   1 
ATOM   10273 C CB  . SER D 1 1   ? 53.821  64.892  1.634   1.00 62.51  ? 30  SER D CB  1 
ATOM   10274 O OG  . SER D 1 1   ? 53.337  66.222  1.793   1.00 64.30  ? 30  SER D OG  1 
ATOM   10275 N N   . THR D 1 2   ? 51.142  64.988  1.714   1.00 64.07  ? 31  THR D N   1 
ATOM   10276 C CA  . THR D 1 2   ? 49.739  65.325  1.600   1.00 58.74  ? 31  THR D CA  1 
ATOM   10277 C C   . THR D 1 2   ? 49.227  65.088  0.180   1.00 52.95  ? 31  THR D C   1 
ATOM   10278 O O   . THR D 1 2   ? 48.053  65.341  -0.075  1.00 51.00  ? 31  THR D O   1 
ATOM   10279 C CB  . THR D 1 2   ? 49.546  66.770  2.051   1.00 55.86  ? 31  THR D CB  1 
ATOM   10280 O OG1 . THR D 1 2   ? 50.351  67.594  1.205   1.00 59.92  ? 31  THR D OG1 1 
ATOM   10281 C CG2 . THR D 1 2   ? 49.911  66.953  3.505   1.00 56.15  ? 31  THR D CG2 1 
ATOM   10282 N N   . ASN D 1 3   ? 50.068  64.584  -0.738  1.00 40.56  ? 32  ASN D N   1 
ATOM   10283 C CA  . ASN D 1 3   ? 49.545  64.209  -2.043  1.00 32.28  ? 32  ASN D CA  1 
ATOM   10284 C C   . ASN D 1 3   ? 48.783  62.898  -1.898  1.00 27.78  ? 32  ASN D C   1 
ATOM   10285 O O   . ASN D 1 3   ? 49.361  61.828  -1.738  1.00 28.20  ? 32  ASN D O   1 
ATOM   10286 C CB  . ASN D 1 3   ? 50.597  64.111  -3.153  1.00 30.76  ? 32  ASN D CB  1 
ATOM   10287 C CG  . ASN D 1 3   ? 49.957  64.063  -4.531  1.00 30.55  ? 32  ASN D CG  1 
ATOM   10288 O OD1 . ASN D 1 3   ? 48.754  63.847  -4.660  1.00 25.70  ? 32  ASN D OD1 1 
ATOM   10289 N ND2 . ASN D 1 3   ? 50.744  64.279  -5.568  1.00 31.08  ? 32  ASN D ND2 1 
ATOM   10290 N N   . LEU D 1 4   ? 47.458  63.001  -1.942  1.00 25.59  ? 33  LEU D N   1 
ATOM   10291 C CA  . LEU D 1 4   ? 46.578  61.851  -1.802  1.00 23.10  ? 33  LEU D CA  1 
ATOM   10292 C C   . LEU D 1 4   ? 46.839  60.800  -2.885  1.00 23.72  ? 33  LEU D C   1 
ATOM   10293 O O   . LEU D 1 4   ? 46.797  59.606  -2.606  1.00 29.74  ? 33  LEU D O   1 
ATOM   10294 C CB  . LEU D 1 4   ? 45.136  62.373  -1.871  1.00 23.22  ? 33  LEU D CB  1 
ATOM   10295 C CG  . LEU D 1 4   ? 44.027  61.351  -1.686  1.00 22.80  ? 33  LEU D CG  1 
ATOM   10296 C CD1 . LEU D 1 4   ? 44.249  60.491  -0.465  1.00 24.14  ? 33  LEU D CD1 1 
ATOM   10297 C CD2 . LEU D 1 4   ? 42.695  62.083  -1.577  1.00 21.21  ? 33  LEU D CD2 1 
ATOM   10298 N N   . LYS D 1 5   ? 47.097  61.227  -4.117  1.00 25.41  ? 34  LYS D N   1 
ATOM   10299 C CA  . LYS D 1 5   ? 47.364  60.303  -5.209  1.00 24.08  ? 34  LYS D CA  1 
ATOM   10300 C C   . LYS D 1 5   ? 48.601  59.445  -4.922  1.00 24.33  ? 34  LYS D C   1 
ATOM   10301 O O   . LYS D 1 5   ? 48.642  58.262  -5.271  1.00 21.75  ? 34  LYS D O   1 
ATOM   10302 C CB  . LYS D 1 5   ? 47.518  61.100  -6.506  1.00 26.33  ? 34  LYS D CB  1 
ATOM   10303 C CG  . LYS D 1 5   ? 47.493  60.285  -7.793  1.00 26.64  ? 34  LYS D CG  1 
ATOM   10304 C CD  . LYS D 1 5   ? 47.812  61.172  -8.949  1.00 27.98  ? 34  LYS D CD  1 
ATOM   10305 C CE  . LYS D 1 5   ? 47.693  60.516  -10.305 1.00 30.18  ? 34  LYS D CE  1 
ATOM   10306 N NZ  . LYS D 1 5   ? 47.717  61.542  -11.377 1.00 32.55  ? 34  LYS D NZ  1 
ATOM   10307 N N   . ASP D 1 6   ? 49.614  60.018  -4.270  1.00 26.00  ? 35  ASP D N   1 
ATOM   10308 C CA  . ASP D 1 6   ? 50.767  59.242  -3.819  1.00 28.74  ? 35  ASP D CA  1 
ATOM   10309 C C   . ASP D 1 6   ? 50.349  58.186  -2.802  1.00 26.82  ? 35  ASP D C   1 
ATOM   10310 O O   . ASP D 1 6   ? 50.736  57.024  -2.906  1.00 30.26  ? 35  ASP D O   1 
ATOM   10311 C CB  . ASP D 1 6   ? 51.860  60.148  -3.252  1.00 29.10  ? 35  ASP D CB  1 
ATOM   10312 C CG  . ASP D 1 6   ? 52.630  60.890  -4.318  1.00 32.86  ? 35  ASP D CG  1 
ATOM   10313 O OD1 . ASP D 1 6   ? 52.531  60.482  -5.493  1.00 30.78  ? 35  ASP D OD1 1 
ATOM   10314 O OD2 . ASP D 1 6   ? 53.317  61.879  -3.957  1.00 32.89  ? 35  ASP D OD2 1 
ATOM   10315 N N   . ILE D 1 7   ? 49.548  58.587  -1.807  1.00 26.41  ? 36  ILE D N   1 
ATOM   10316 C CA  . ILE D 1 7   ? 49.044  57.657  -0.811  1.00 25.81  ? 36  ILE D CA  1 
ATOM   10317 C C   . ILE D 1 7   ? 48.265  56.516  -1.472  1.00 26.29  ? 36  ILE D C   1 
ATOM   10318 O O   . ILE D 1 7   ? 48.413  55.355  -1.088  1.00 23.14  ? 36  ILE D O   1 
ATOM   10319 C CB  . ILE D 1 7   ? 48.183  58.440  0.201   1.00 29.12  ? 36  ILE D CB  1 
ATOM   10320 C CG1 . ILE D 1 7   ? 49.046  59.307  1.120   1.00 29.27  ? 36  ILE D CG1 1 
ATOM   10321 C CG2 . ILE D 1 7   ? 47.271  57.517  0.985   1.00 29.58  ? 36  ILE D CG2 1 
ATOM   10322 C CD1 . ILE D 1 7   ? 48.441  60.650  1.372   1.00 30.56  ? 36  ILE D CD1 1 
ATOM   10323 N N   . LEU D 1 8   ? 47.416  56.854  -2.457  1.00 29.11  ? 37  LEU D N   1 
ATOM   10324 C CA  . LEU D 1 8   ? 46.548  55.874  -3.111  1.00 28.26  ? 37  LEU D CA  1 
ATOM   10325 C C   . LEU D 1 8   ? 47.415  54.880  -3.886  1.00 27.43  ? 37  LEU D C   1 
ATOM   10326 O O   . LEU D 1 8   ? 47.152  53.672  -3.904  1.00 30.08  ? 37  LEU D O   1 
ATOM   10327 C CB  . LEU D 1 8   ? 45.605  56.678  -4.017  1.00 30.75  ? 37  LEU D CB  1 
ATOM   10328 C CG  . LEU D 1 8   ? 44.142  56.258  -4.165  1.00 32.27  ? 37  LEU D CG  1 
ATOM   10329 C CD1 . LEU D 1 8   ? 43.569  55.550  -2.956  1.00 30.34  ? 37  LEU D CD1 1 
ATOM   10330 C CD2 . LEU D 1 8   ? 43.308  57.493  -4.493  1.00 32.61  ? 37  LEU D CD2 1 
ATOM   10331 N N   . ALA D 1 9   ? 48.481  55.394  -4.512  1.00 28.96  ? 38  ALA D N   1 
ATOM   10332 C CA  . ALA D 1 9   ? 49.404  54.553  -5.263  1.00 29.35  ? 38  ALA D CA  1 
ATOM   10333 C C   . ALA D 1 9   ? 50.126  53.539  -4.371  1.00 28.66  ? 38  ALA D C   1 
ATOM   10334 O O   . ALA D 1 9   ? 50.482  52.480  -4.871  1.00 25.53  ? 38  ALA D O   1 
ATOM   10335 C CB  . ALA D 1 9   ? 50.383  55.392  -6.043  1.00 32.28  ? 38  ALA D CB  1 
ATOM   10336 N N   . ASP D 1 10  ? 50.312  53.810  -3.063  1.00 28.11  ? 39  ASP D N   1 
ATOM   10337 C CA  . ASP D 1 10  ? 50.873  52.798  -2.173  1.00 29.68  ? 39  ASP D CA  1 
ATOM   10338 C C   . ASP D 1 10  ? 49.811  51.772  -1.787  1.00 28.71  ? 39  ASP D C   1 
ATOM   10339 O O   . ASP D 1 10  ? 50.088  50.574  -1.808  1.00 27.55  ? 39  ASP D O   1 
ATOM   10340 C CB  . ASP D 1 10  ? 51.563  53.395  -0.938  1.00 38.48  ? 39  ASP D CB  1 
ATOM   10341 C CG  . ASP D 1 10  ? 53.087  53.411  -1.000  1.00 46.16  ? 39  ASP D CG  1 
ATOM   10342 O OD1 . ASP D 1 10  ? 53.655  53.057  -2.072  1.00 50.88  ? 39  ASP D OD1 1 
ATOM   10343 O OD2 . ASP D 1 10  ? 53.708  53.771  0.032   1.00 52.92  ? 39  ASP D OD2 1 
ATOM   10344 N N   . LEU D 1 11  ? 48.574  52.228  -1.510  1.00 25.56  ? 40  LEU D N   1 
ATOM   10345 C CA  . LEU D 1 11  ? 47.527  51.354  -1.006  1.00 27.94  ? 40  LEU D CA  1 
ATOM   10346 C C   . LEU D 1 11  ? 47.035  50.357  -2.056  1.00 26.17  ? 40  LEU D C   1 
ATOM   10347 O O   . LEU D 1 11  ? 46.762  49.196  -1.745  1.00 27.97  ? 40  LEU D O   1 
ATOM   10348 C CB  . LEU D 1 11  ? 46.366  52.239  -0.545  1.00 29.14  ? 40  LEU D CB  1 
ATOM   10349 C CG  . LEU D 1 11  ? 46.607  53.088  0.699   1.00 30.67  ? 40  LEU D CG  1 
ATOM   10350 C CD1 . LEU D 1 11  ? 45.420  54.001  0.951   1.00 28.91  ? 40  LEU D CD1 1 
ATOM   10351 C CD2 . LEU D 1 11  ? 46.871  52.211  1.910   1.00 32.70  ? 40  LEU D CD2 1 
ATOM   10352 N N   . ILE D 1 12  ? 46.860  50.811  -3.299  1.00 27.65  ? 41  ILE D N   1 
ATOM   10353 C CA  . ILE D 1 12  ? 46.055  50.079  -4.261  1.00 26.35  ? 41  ILE D CA  1 
ATOM   10354 C C   . ILE D 1 12  ? 46.599  48.670  -4.449  1.00 27.45  ? 41  ILE D C   1 
ATOM   10355 O O   . ILE D 1 12  ? 45.832  47.723  -4.334  1.00 27.42  ? 41  ILE D O   1 
ATOM   10356 C CB  . ILE D 1 12  ? 45.920  50.870  -5.576  1.00 27.49  ? 41  ILE D CB  1 
ATOM   10357 C CG1 . ILE D 1 12  ? 44.873  51.978  -5.412  1.00 25.00  ? 41  ILE D CG1 1 
ATOM   10358 C CG2 . ILE D 1 12  ? 45.590  49.960  -6.756  1.00 29.00  ? 41  ILE D CG2 1 
ATOM   10359 C CD1 . ILE D 1 12  ? 44.970  53.073  -6.425  1.00 24.44  ? 41  ILE D CD1 1 
ATOM   10360 N N   . PRO D 1 13  ? 47.905  48.489  -4.771  1.00 30.10  ? 42  PRO D N   1 
ATOM   10361 C CA  . PRO D 1 13  ? 48.463  47.160  -5.015  1.00 30.06  ? 42  PRO D CA  1 
ATOM   10362 C C   . PRO D 1 13  ? 48.296  46.151  -3.888  1.00 30.55  ? 42  PRO D C   1 
ATOM   10363 O O   . PRO D 1 13  ? 48.168  44.968  -4.184  1.00 29.61  ? 42  PRO D O   1 
ATOM   10364 C CB  . PRO D 1 13  ? 49.971  47.393  -5.186  1.00 31.45  ? 42  PRO D CB  1 
ATOM   10365 C CG  . PRO D 1 13  ? 50.106  48.842  -5.559  1.00 33.28  ? 42  PRO D CG  1 
ATOM   10366 C CD  . PRO D 1 13  ? 48.908  49.551  -4.958  1.00 28.93  ? 42  PRO D CD  1 
ATOM   10367 N N   . LYS D 1 14  ? 48.318  46.607  -2.620  1.00 31.34  ? 43  LYS D N   1 
ATOM   10368 C CA  . LYS D 1 14  ? 48.092  45.710  -1.495  1.00 35.06  ? 43  LYS D CA  1 
ATOM   10369 C C   . LYS D 1 14  ? 46.656  45.191  -1.542  1.00 33.24  ? 43  LYS D C   1 
ATOM   10370 O O   . LYS D 1 14  ? 46.426  43.993  -1.418  1.00 33.47  ? 43  LYS D O   1 
ATOM   10371 C CB  . LYS D 1 14  ? 48.314  46.385  -0.136  1.00 39.11  ? 43  LYS D CB  1 
ATOM   10372 C CG  . LYS D 1 14  ? 49.662  47.068  0.077   1.00 42.04  ? 43  LYS D CG  1 
ATOM   10373 C CD  . LYS D 1 14  ? 50.020  47.240  1.547   1.00 43.68  ? 43  LYS D CD  1 
ATOM   10374 C CE  . LYS D 1 14  ? 50.683  48.566  1.862   1.00 44.85  ? 43  LYS D CE  1 
ATOM   10375 N NZ  . LYS D 1 14  ? 51.884  48.816  1.031   1.00 45.29  ? 43  LYS D NZ  1 
ATOM   10376 N N   . GLU D 1 15  ? 45.683  46.093  -1.734  1.00 30.66  ? 44  GLU D N   1 
ATOM   10377 C CA  . GLU D 1 15  ? 44.296  45.662  -1.846  1.00 28.83  ? 44  GLU D CA  1 
ATOM   10378 C C   . GLU D 1 15  ? 44.087  44.714  -3.026  1.00 28.40  ? 44  GLU D C   1 
ATOM   10379 O O   . GLU D 1 15  ? 43.346  43.742  -2.879  1.00 30.52  ? 44  GLU D O   1 
ATOM   10380 C CB  . GLU D 1 15  ? 43.321  46.826  -2.036  1.00 31.34  ? 44  GLU D CB  1 
ATOM   10381 C CG  . GLU D 1 15  ? 42.744  47.385  -0.766  1.00 33.24  ? 44  GLU D CG  1 
ATOM   10382 C CD  . GLU D 1 15  ? 42.183  46.411  0.254   1.00 36.34  ? 44  GLU D CD  1 
ATOM   10383 O OE1 . GLU D 1 15  ? 40.946  46.263  0.324   1.00 39.70  ? 44  GLU D OE1 1 
ATOM   10384 O OE2 . GLU D 1 15  ? 42.977  45.860  1.026   1.00 41.99  ? 44  GLU D OE2 1 
ATOM   10385 N N   . GLN D 1 16  ? 44.714  45.015  -4.175  1.00 26.19  ? 45  GLN D N   1 
ATOM   10386 C CA  . GLN D 1 16  ? 44.628  44.165  -5.352  1.00 28.78  ? 45  GLN D CA  1 
ATOM   10387 C C   . GLN D 1 16  ? 45.080  42.759  -4.967  1.00 26.00  ? 45  GLN D C   1 
ATOM   10388 O O   . GLN D 1 16  ? 44.435  41.788  -5.313  1.00 25.09  ? 45  GLN D O   1 
ATOM   10389 C CB  . GLN D 1 16  ? 45.459  44.695  -6.524  1.00 27.08  ? 45  GLN D CB  1 
ATOM   10390 C CG  . GLN D 1 16  ? 44.999  46.041  -7.087  1.00 28.08  ? 45  GLN D CG  1 
ATOM   10391 C CD  . GLN D 1 16  ? 45.803  46.468  -8.295  1.00 30.00  ? 45  GLN D CD  1 
ATOM   10392 O OE1 . GLN D 1 16  ? 46.998  46.216  -8.406  1.00 32.20  ? 45  GLN D OE1 1 
ATOM   10393 N NE2 . GLN D 1 16  ? 45.151  47.081  -9.262  1.00 34.30  ? 45  GLN D NE2 1 
ATOM   10394 N N   . ALA D 1 17  ? 46.186  42.686  -4.223  1.00 31.65  ? 46  ALA D N   1 
ATOM   10395 C CA  . ALA D 1 17  ? 46.776  41.427  -3.787  1.00 30.33  ? 46  ALA D CA  1 
ATOM   10396 C C   . ALA D 1 17  ? 45.916  40.787  -2.703  1.00 30.63  ? 46  ALA D C   1 
ATOM   10397 O O   . ALA D 1 17  ? 45.792  39.570  -2.662  1.00 30.01  ? 46  ALA D O   1 
ATOM   10398 C CB  . ALA D 1 17  ? 48.192  41.667  -3.300  1.00 30.62  ? 46  ALA D CB  1 
ATOM   10399 N N   . ARG D 1 18  ? 45.333  41.598  -1.814  1.00 31.21  ? 47  ARG D N   1 
ATOM   10400 C CA  . ARG D 1 18  ? 44.450  41.065  -0.790  1.00 35.58  ? 47  ARG D CA  1 
ATOM   10401 C C   . ARG D 1 18  ? 43.234  40.394  -1.430  1.00 34.01  ? 47  ARG D C   1 
ATOM   10402 O O   . ARG D 1 18  ? 42.829  39.324  -1.000  1.00 32.58  ? 47  ARG D O   1 
ATOM   10403 C CB  . ARG D 1 18  ? 44.024  42.165  0.189   1.00 40.65  ? 47  ARG D CB  1 
ATOM   10404 C CG  . ARG D 1 18  ? 43.048  41.709  1.263   1.00 45.20  ? 47  ARG D CG  1 
ATOM   10405 C CD  . ARG D 1 18  ? 42.867  42.783  2.327   1.00 50.35  ? 47  ARG D CD  1 
ATOM   10406 N NE  . ARG D 1 18  ? 42.153  42.287  3.491   1.00 52.77  ? 47  ARG D NE  1 
ATOM   10407 C CZ  . ARG D 1 18  ? 41.588  43.066  4.406   1.00 55.94  ? 47  ARG D CZ  1 
ATOM   10408 N NH1 . ARG D 1 18  ? 40.862  42.534  5.374   1.00 54.43  ? 47  ARG D NH1 1 
ATOM   10409 N NH2 . ARG D 1 18  ? 41.717  44.379  4.321   1.00 55.76  ? 47  ARG D NH2 1 
ATOM   10410 N N   . ILE D 1 19  ? 42.642  41.042  -2.443  1.00 33.65  ? 48  ILE D N   1 
ATOM   10411 C CA  . ILE D 1 19  ? 41.372  40.593  -2.991  1.00 29.02  ? 48  ILE D CA  1 
ATOM   10412 C C   . ILE D 1 19  ? 41.592  39.390  -3.912  1.00 30.31  ? 48  ILE D C   1 
ATOM   10413 O O   . ILE D 1 19  ? 40.787  38.477  -3.892  1.00 32.77  ? 48  ILE D O   1 
ATOM   10414 C CB  . ILE D 1 19  ? 40.641  41.788  -3.651  1.00 30.00  ? 48  ILE D CB  1 
ATOM   10415 C CG1 . ILE D 1 19  ? 39.978  42.631  -2.557  1.00 26.23  ? 48  ILE D CG1 1 
ATOM   10416 C CG2 . ILE D 1 19  ? 39.630  41.341  -4.691  1.00 25.50  ? 48  ILE D CG2 1 
ATOM   10417 C CD1 . ILE D 1 19  ? 39.627  44.032  -2.967  1.00 26.76  ? 48  ILE D CD1 1 
ATOM   10418 N N   . LYS D 1 20  ? 42.696  39.377  -4.661  1.00 30.73  ? 49  LYS D N   1 
ATOM   10419 C CA  . LYS D 1 20  ? 43.041  38.259  -5.525  1.00 34.96  ? 49  LYS D CA  1 
ATOM   10420 C C   . LYS D 1 20  ? 43.074  36.970  -4.699  1.00 33.28  ? 49  LYS D C   1 
ATOM   10421 O O   . LYS D 1 20  ? 42.374  35.996  -5.003  1.00 32.24  ? 49  LYS D O   1 
ATOM   10422 C CB  . LYS D 1 20  ? 44.376  38.569  -6.210  1.00 37.66  ? 49  LYS D CB  1 
ATOM   10423 C CG  . LYS D 1 20  ? 44.874  37.531  -7.203  1.00 39.06  ? 49  LYS D CG  1 
ATOM   10424 C CD  . LYS D 1 20  ? 45.701  38.149  -8.309  1.00 41.26  ? 49  LYS D CD  1 
ATOM   10425 C CE  . LYS D 1 20  ? 45.926  37.209  -9.473  1.00 46.16  ? 49  LYS D CE  1 
ATOM   10426 N NZ  . LYS D 1 20  ? 46.831  36.095  -9.112  1.00 44.55  ? 49  LYS D NZ  1 
ATOM   10427 N N   . THR D 1 21  ? 43.868  37.008  -3.623  1.00 34.58  ? 50  THR D N   1 
ATOM   10428 C CA  . THR D 1 21  ? 44.013  35.891  -2.700  1.00 37.08  ? 50  THR D CA  1 
ATOM   10429 C C   . THR D 1 21  ? 42.664  35.485  -2.113  1.00 35.04  ? 50  THR D C   1 
ATOM   10430 O O   . THR D 1 21  ? 42.344  34.301  -2.045  1.00 36.10  ? 50  THR D O   1 
ATOM   10431 C CB  . THR D 1 21  ? 44.975  36.255  -1.565  1.00 40.66  ? 50  THR D CB  1 
ATOM   10432 O OG1 . THR D 1 21  ? 46.164  36.744  -2.180  1.00 49.76  ? 50  THR D OG1 1 
ATOM   10433 C CG2 . THR D 1 21  ? 45.290  35.090  -0.657  1.00 42.66  ? 50  THR D CG2 1 
ATOM   10434 N N   . PHE D 1 22  ? 41.869  36.474  -1.696  1.00 33.04  ? 51  PHE D N   1 
ATOM   10435 C CA  . PHE D 1 22  ? 40.585  36.201  -1.077  1.00 33.47  ? 51  PHE D CA  1 
ATOM   10436 C C   . PHE D 1 22  ? 39.654  35.484  -2.058  1.00 31.32  ? 51  PHE D C   1 
ATOM   10437 O O   . PHE D 1 22  ? 38.966  34.534  -1.679  1.00 32.77  ? 51  PHE D O   1 
ATOM   10438 C CB  . PHE D 1 22  ? 39.971  37.499  -0.545  1.00 33.21  ? 51  PHE D CB  1 
ATOM   10439 C CG  . PHE D 1 22  ? 38.584  37.328  0.023   1.00 36.22  ? 51  PHE D CG  1 
ATOM   10440 C CD1 . PHE D 1 22  ? 38.342  36.378  1.006   1.00 35.71  ? 51  PHE D CD1 1 
ATOM   10441 C CD2 . PHE D 1 22  ? 37.531  38.129  -0.402  1.00 33.39  ? 51  PHE D CD2 1 
ATOM   10442 C CE1 . PHE D 1 22  ? 37.073  36.222  1.538   1.00 37.05  ? 51  PHE D CE1 1 
ATOM   10443 C CE2 . PHE D 1 22  ? 36.270  37.989  0.152   1.00 35.21  ? 51  PHE D CE2 1 
ATOM   10444 C CZ  . PHE D 1 22  ? 36.041  37.030  1.114   1.00 37.27  ? 51  PHE D CZ  1 
ATOM   10445 N N   . ARG D 1 23  ? 39.636  35.929  -3.324  1.00 30.74  ? 52  ARG D N   1 
ATOM   10446 C CA  . ARG D 1 23  ? 38.802  35.322  -4.353  1.00 32.03  ? 52  ARG D CA  1 
ATOM   10447 C C   . ARG D 1 23  ? 39.254  33.886  -4.631  1.00 34.16  ? 52  ARG D C   1 
ATOM   10448 O O   . ARG D 1 23  ? 38.439  32.988  -4.833  1.00 29.03  ? 52  ARG D O   1 
ATOM   10449 C CB  . ARG D 1 23  ? 38.853  36.174  -5.626  1.00 34.16  ? 52  ARG D CB  1 
ATOM   10450 C CG  . ARG D 1 23  ? 38.226  37.552  -5.439  1.00 38.07  ? 52  ARG D CG  1 
ATOM   10451 C CD  . ARG D 1 23  ? 38.017  38.356  -6.712  1.00 36.46  ? 52  ARG D CD  1 
ATOM   10452 N NE  . ARG D 1 23  ? 36.920  37.867  -7.553  1.00 38.93  ? 52  ARG D NE  1 
ATOM   10453 C CZ  . ARG D 1 23  ? 36.656  38.315  -8.782  1.00 38.93  ? 52  ARG D CZ  1 
ATOM   10454 N NH1 . ARG D 1 23  ? 37.315  39.351  -9.265  1.00 38.82  ? 52  ARG D NH1 1 
ATOM   10455 N NH2 . ARG D 1 23  ? 35.718  37.748  -9.522  1.00 38.56  ? 52  ARG D NH2 1 
ATOM   10456 N N   . GLN D 1 24  ? 40.567  33.669  -4.601  1.00 36.31  ? 53  GLN D N   1 
ATOM   10457 C CA  . GLN D 1 24  ? 41.115  32.393  -5.018  1.00 45.13  ? 53  GLN D CA  1 
ATOM   10458 C C   . GLN D 1 24  ? 40.893  31.332  -3.939  1.00 48.26  ? 53  GLN D C   1 
ATOM   10459 O O   . GLN D 1 24  ? 40.939  30.138  -4.237  1.00 56.62  ? 53  GLN D O   1 
ATOM   10460 C CB  . GLN D 1 24  ? 42.576  32.570  -5.414  1.00 50.46  ? 53  GLN D CB  1 
ATOM   10461 C CG  . GLN D 1 24  ? 43.047  31.471  -6.348  1.00 62.74  ? 53  GLN D CG  1 
ATOM   10462 C CD  . GLN D 1 24  ? 42.438  31.482  -7.733  1.00 66.81  ? 53  GLN D CD  1 
ATOM   10463 O OE1 . GLN D 1 24  ? 41.972  30.456  -8.233  1.00 63.94  ? 53  GLN D OE1 1 
ATOM   10464 N NE2 . GLN D 1 24  ? 42.479  32.635  -8.384  1.00 70.87  ? 53  GLN D NE2 1 
ATOM   10465 N N   . GLN D 1 25  ? 40.625  31.759  -2.698  1.00 49.96  ? 54  GLN D N   1 
ATOM   10466 C CA  . GLN D 1 25  ? 40.023  30.878  -1.711  1.00 52.04  ? 54  GLN D CA  1 
ATOM   10467 C C   . GLN D 1 25  ? 38.518  30.848  -1.947  1.00 50.33  ? 54  GLN D C   1 
ATOM   10468 O O   . GLN D 1 25  ? 37.965  29.827  -2.343  1.00 53.58  ? 54  GLN D O   1 
ATOM   10469 C CB  . GLN D 1 25  ? 40.200  31.340  -0.261  1.00 60.34  ? 54  GLN D CB  1 
ATOM   10470 C CG  . GLN D 1 25  ? 41.515  32.028  0.054   1.00 67.12  ? 54  GLN D CG  1 
ATOM   10471 C CD  . GLN D 1 25  ? 41.502  32.590  1.457   1.00 76.06  ? 54  GLN D CD  1 
ATOM   10472 O OE1 . GLN D 1 25  ? 40.509  32.487  2.179   1.00 73.73  ? 54  GLN D OE1 1 
ATOM   10473 N NE2 . GLN D 1 25  ? 42.609  33.205  1.848   1.00 78.56  ? 54  GLN D NE2 1 
ATOM   10474 N N   . HIS D 1 26  ? 37.880  32.006  -1.736  1.00 41.72  ? 55  HIS D N   1 
ATOM   10475 C CA  . HIS D 1 26  ? 36.490  32.038  -1.310  1.00 40.23  ? 55  HIS D CA  1 
ATOM   10476 C C   . HIS D 1 26  ? 35.569  32.538  -2.419  1.00 36.61  ? 55  HIS D C   1 
ATOM   10477 O O   . HIS D 1 26  ? 34.393  32.771  -2.159  1.00 31.61  ? 55  HIS D O   1 
ATOM   10478 C CB  . HIS D 1 26  ? 36.358  32.853  -0.017  1.00 46.07  ? 55  HIS D CB  1 
ATOM   10479 C CG  . HIS D 1 26  ? 36.661  32.100  1.243   1.00 50.13  ? 55  HIS D CG  1 
ATOM   10480 N ND1 . HIS D 1 26  ? 36.129  30.855  1.522   1.00 53.36  ? 55  HIS D ND1 1 
ATOM   10481 C CD2 . HIS D 1 26  ? 37.409  32.432  2.304   1.00 47.39  ? 55  HIS D CD2 1 
ATOM   10482 C CE1 . HIS D 1 26  ? 36.572  30.448  2.701   1.00 50.95  ? 55  HIS D CE1 1 
ATOM   10483 N NE2 . HIS D 1 26  ? 37.339  31.399  3.200   1.00 51.42  ? 55  HIS D NE2 1 
ATOM   10484 N N   . GLY D 1 27  ? 36.089  32.649  -3.651  1.00 32.93  ? 56  GLY D N   1 
ATOM   10485 C CA  . GLY D 1 27  ? 35.293  33.050  -4.798  1.00 35.69  ? 56  GLY D CA  1 
ATOM   10486 C C   . GLY D 1 27  ? 34.008  32.236  -4.956  1.00 34.68  ? 56  GLY D C   1 
ATOM   10487 O O   . GLY D 1 27  ? 32.940  32.793  -5.176  1.00 34.63  ? 56  GLY D O   1 
ATOM   10488 N N   . LYS D 1 28  ? 34.096  30.916  -4.792  1.00 35.79  ? 57  LYS D N   1 
ATOM   10489 C CA  . LYS D 1 28  ? 32.962  30.040  -5.034  1.00 35.63  ? 57  LYS D CA  1 
ATOM   10490 C C   . LYS D 1 28  ? 32.064  29.951  -3.806  1.00 33.98  ? 57  LYS D C   1 
ATOM   10491 O O   . LYS D 1 28  ? 31.098  29.193  -3.819  1.00 33.35  ? 57  LYS D O   1 
ATOM   10492 C CB  . LYS D 1 28  ? 33.456  28.635  -5.395  1.00 38.29  ? 57  LYS D CB  1 
ATOM   10493 C CG  . LYS D 1 28  ? 34.418  28.596  -6.569  1.00 40.67  ? 57  LYS D CG  1 
ATOM   10494 C CD  . LYS D 1 28  ? 35.077  27.264  -6.775  1.00 44.53  ? 57  LYS D CD  1 
ATOM   10495 C CE  . LYS D 1 28  ? 35.502  27.038  -8.212  1.00 52.02  ? 57  LYS D CE  1 
ATOM   10496 N NZ  . LYS D 1 28  ? 34.338  26.751  -9.091  1.00 58.65  ? 57  LYS D NZ  1 
ATOM   10497 N N   . THR D 1 29  ? 32.397  30.691  -2.742  1.00 33.41  ? 58  THR D N   1 
ATOM   10498 C CA  . THR D 1 29  ? 31.652  30.605  -1.497  1.00 35.64  ? 58  THR D CA  1 
ATOM   10499 C C   . THR D 1 29  ? 30.334  31.346  -1.659  1.00 34.63  ? 58  THR D C   1 
ATOM   10500 O O   . THR D 1 29  ? 30.337  32.516  -2.017  1.00 34.46  ? 58  THR D O   1 
ATOM   10501 C CB  . THR D 1 29  ? 32.366  31.253  -0.300  1.00 36.34  ? 58  THR D CB  1 
ATOM   10502 O OG1 . THR D 1 29  ? 33.654  30.673  -0.131  1.00 36.84  ? 58  THR D OG1 1 
ATOM   10503 C CG2 . THR D 1 29  ? 31.577  31.109  0.983   1.00 38.51  ? 58  THR D CG2 1 
ATOM   10504 N N   . VAL D 1 30  ? 29.236  30.660  -1.342  1.00 37.17  ? 59  VAL D N   1 
ATOM   10505 C CA  . VAL D 1 30  ? 27.911  31.249  -1.344  1.00 39.85  ? 59  VAL D CA  1 
ATOM   10506 C C   . VAL D 1 30  ? 27.743  32.167  -0.136  1.00 39.31  ? 59  VAL D C   1 
ATOM   10507 O O   . VAL D 1 30  ? 27.950  31.742  0.993   1.00 43.72  ? 59  VAL D O   1 
ATOM   10508 C CB  . VAL D 1 30  ? 26.846  30.137  -1.336  1.00 38.18  ? 59  VAL D CB  1 
ATOM   10509 C CG1 . VAL D 1 30  ? 25.454  30.685  -1.070  1.00 37.52  ? 59  VAL D CG1 1 
ATOM   10510 C CG2 . VAL D 1 30  ? 26.876  29.334  -2.624  1.00 36.64  ? 59  VAL D CG2 1 
ATOM   10511 N N   . VAL D 1 31  ? 27.311  33.412  -0.373  1.00 37.14  ? 60  VAL D N   1 
ATOM   10512 C CA  . VAL D 1 31  ? 27.120  34.372  0.700   1.00 35.66  ? 60  VAL D CA  1 
ATOM   10513 C C   . VAL D 1 31  ? 25.646  34.745  0.877   1.00 35.46  ? 60  VAL D C   1 
ATOM   10514 O O   . VAL D 1 31  ? 25.305  35.352  1.888   1.00 32.00  ? 60  VAL D O   1 
ATOM   10515 C CB  . VAL D 1 31  ? 27.985  35.617  0.446   1.00 43.29  ? 60  VAL D CB  1 
ATOM   10516 C CG1 . VAL D 1 31  ? 29.460  35.250  0.402   1.00 44.37  ? 60  VAL D CG1 1 
ATOM   10517 C CG2 . VAL D 1 31  ? 27.578  36.334  -0.826  1.00 46.71  ? 60  VAL D CG2 1 
ATOM   10518 N N   . GLY D 1 32  ? 24.781  34.379  -0.088  1.00 34.50  ? 61  GLY D N   1 
ATOM   10519 C CA  . GLY D 1 32  ? 23.366  34.713  -0.026  1.00 34.14  ? 61  GLY D CA  1 
ATOM   10520 C C   . GLY D 1 32  ? 22.534  33.912  -1.023  1.00 36.29  ? 61  GLY D C   1 
ATOM   10521 O O   . GLY D 1 32  ? 23.075  33.238  -1.897  1.00 37.66  ? 61  GLY D O   1 
ATOM   10522 N N   . GLN D 1 33  ? 21.207  33.964  -0.861  1.00 37.86  ? 62  GLN D N   1 
ATOM   10523 C CA  . GLN D 1 33  ? 20.296  33.341  -1.810  1.00 40.95  ? 62  GLN D CA  1 
ATOM   10524 C C   . GLN D 1 33  ? 19.613  34.452  -2.614  1.00 40.04  ? 62  GLN D C   1 
ATOM   10525 O O   . GLN D 1 33  ? 19.676  35.620  -2.238  1.00 35.75  ? 62  GLN D O   1 
ATOM   10526 C CB  . GLN D 1 33  ? 19.285  32.457  -1.071  1.00 47.43  ? 62  GLN D CB  1 
ATOM   10527 C CG  . GLN D 1 33  ? 19.879  31.599  0.047   1.00 51.66  ? 62  GLN D CG  1 
ATOM   10528 C CD  . GLN D 1 33  ? 20.197  30.178  -0.347  1.00 55.41  ? 62  GLN D CD  1 
ATOM   10529 O OE1 . GLN D 1 33  ? 21.356  29.783  -0.430  1.00 58.68  ? 62  GLN D OE1 1 
ATOM   10530 N NE2 . GLN D 1 33  ? 19.165  29.381  -0.574  1.00 60.64  ? 62  GLN D NE2 1 
ATOM   10531 N N   . ILE D 1 34  ? 18.962  34.093  -3.730  1.00 37.10  ? 63  ILE D N   1 
ATOM   10532 C CA  . ILE D 1 34  ? 18.089  35.021  -4.430  1.00 32.03  ? 63  ILE D CA  1 
ATOM   10533 C C   . ILE D 1 34  ? 16.713  34.373  -4.508  1.00 29.53  ? 63  ILE D C   1 
ATOM   10534 O O   . ILE D 1 34  ? 16.594  33.205  -4.870  1.00 28.36  ? 63  ILE D O   1 
ATOM   10535 C CB  . ILE D 1 34  ? 18.656  35.371  -5.820  1.00 32.88  ? 63  ILE D CB  1 
ATOM   10536 C CG1 . ILE D 1 34  ? 19.993  36.100  -5.694  1.00 32.19  ? 63  ILE D CG1 1 
ATOM   10537 C CG2 . ILE D 1 34  ? 17.660  36.181  -6.631  1.00 33.97  ? 63  ILE D CG2 1 
ATOM   10538 C CD1 . ILE D 1 34  ? 20.756  36.211  -6.976  1.00 34.74  ? 63  ILE D CD1 1 
ATOM   10539 N N   . THR D 1 35  ? 15.675  35.135  -4.168  1.00 26.46  ? 64  THR D N   1 
ATOM   10540 C CA  . THR D 1 35  ? 14.323  34.605  -4.183  1.00 29.37  ? 64  THR D CA  1 
ATOM   10541 C C   . THR D 1 35  ? 13.466  35.412  -5.144  1.00 28.23  ? 64  THR D C   1 
ATOM   10542 O O   . THR D 1 35  ? 13.836  36.526  -5.518  1.00 30.27  ? 64  THR D O   1 
ATOM   10543 C CB  . THR D 1 35  ? 13.667  34.586  -2.795  1.00 28.56  ? 64  THR D CB  1 
ATOM   10544 O OG1 . THR D 1 35  ? 13.500  35.928  -2.347  1.00 31.63  ? 64  THR D OG1 1 
ATOM   10545 C CG2 . THR D 1 35  ? 14.436  33.760  -1.783  1.00 28.68  ? 64  THR D CG2 1 
ATOM   10546 N N   . VAL D 1 36  ? 12.335  34.808  -5.519  1.00 31.16  ? 65  VAL D N   1 
ATOM   10547 C CA  . VAL D 1 36  ? 11.356  35.419  -6.407  1.00 26.72  ? 65  VAL D CA  1 
ATOM   10548 C C   . VAL D 1 36  ? 10.932  36.761  -5.814  1.00 29.56  ? 65  VAL D C   1 
ATOM   10549 O O   . VAL D 1 36  ? 10.849  37.752  -6.530  1.00 26.04  ? 65  VAL D O   1 
ATOM   10550 C CB  . VAL D 1 36  ? 10.147  34.495  -6.627  1.00 28.87  ? 65  VAL D CB  1 
ATOM   10551 C CG1 . VAL D 1 36  ? 9.029   35.207  -7.366  1.00 26.55  ? 65  VAL D CG1 1 
ATOM   10552 C CG2 . VAL D 1 36  ? 10.528  33.200  -7.339  1.00 27.79  ? 65  VAL D CG2 1 
ATOM   10553 N N   . ASP D 1 37  ? 10.665  36.783  -4.499  1.00 28.46  ? 66  ASP D N   1 
ATOM   10554 C CA  . ASP D 1 37  ? 10.199  37.995  -3.845  1.00 29.97  ? 66  ASP D CA  1 
ATOM   10555 C C   . ASP D 1 37  ? 11.249  39.098  -3.952  1.00 31.80  ? 66  ASP D C   1 
ATOM   10556 O O   . ASP D 1 37  ? 10.869  40.260  -4.097  1.00 30.08  ? 66  ASP D O   1 
ATOM   10557 C CB  . ASP D 1 37  ? 9.790   37.735  -2.390  1.00 31.24  ? 66  ASP D CB  1 
ATOM   10558 C CG  . ASP D 1 37  ? 8.347   37.290  -2.197  1.00 33.86  ? 66  ASP D CG  1 
ATOM   10559 O OD1 . ASP D 1 37  ? 7.506   37.517  -3.103  1.00 32.98  ? 66  ASP D OD1 1 
ATOM   10560 O OD2 . ASP D 1 37  ? 8.062   36.709  -1.140  1.00 36.58  ? 66  ASP D OD2 1 
ATOM   10561 N N   . MET D 1 38  ? 12.542  38.730  -3.879  1.00 29.69  ? 67  MET D N   1 
ATOM   10562 C CA  . MET D 1 38  ? 13.641  39.672  -4.007  1.00 31.09  ? 67  MET D CA  1 
ATOM   10563 C C   . MET D 1 38  ? 13.712  40.265  -5.413  1.00 28.54  ? 67  MET D C   1 
ATOM   10564 O O   . MET D 1 38  ? 14.055  41.449  -5.564  1.00 29.72  ? 67  MET D O   1 
ATOM   10565 C CB  . MET D 1 38  ? 14.998  39.008  -3.747  1.00 32.71  ? 67  MET D CB  1 
ATOM   10566 C CG  . MET D 1 38  ? 15.365  38.874  -2.305  1.00 34.99  ? 67  MET D CG  1 
ATOM   10567 S SD  . MET D 1 38  ? 16.962  38.030  -2.178  1.00 34.99  ? 67  MET D SD  1 
ATOM   10568 C CE  . MET D 1 38  ? 16.416  36.529  -1.373  1.00 35.57  ? 67  MET D CE  1 
ATOM   10569 N N   . MET D 1 39  ? 13.456  39.428  -6.434  1.00 27.19  ? 68  MET D N   1 
ATOM   10570 C CA  . MET D 1 39  ? 13.500  39.876  -7.821  1.00 24.72  ? 68  MET D CA  1 
ATOM   10571 C C   . MET D 1 39  ? 12.349  40.860  -8.048  1.00 25.76  ? 68  MET D C   1 
ATOM   10572 O O   . MET D 1 39  ? 12.522  41.863  -8.744  1.00 26.29  ? 68  MET D O   1 
ATOM   10573 C CB  . MET D 1 39  ? 13.416  38.700  -8.797  1.00 25.12  ? 68  MET D CB  1 
ATOM   10574 C CG  . MET D 1 39  ? 14.663  37.870  -8.790  1.00 28.20  ? 68  MET D CG  1 
ATOM   10575 S SD  . MET D 1 39  ? 14.575  36.499  -9.973  1.00 32.32  ? 68  MET D SD  1 
ATOM   10576 C CE  . MET D 1 39  ? 14.650  37.425  -11.508 1.00 33.15  ? 68  MET D CE  1 
ATOM   10577 N N   . TYR D 1 40  ? 11.197  40.607  -7.413  1.00 24.58  ? 69  TYR D N   1 
ATOM   10578 C CA  . TYR D 1 40  ? 10.076  41.539  -7.472  1.00 26.09  ? 69  TYR D CA  1 
ATOM   10579 C C   . TYR D 1 40  ? 10.288  42.745  -6.556  1.00 27.55  ? 69  TYR D C   1 
ATOM   10580 O O   . TYR D 1 40  ? 9.812   43.838  -6.872  1.00 25.14  ? 69  TYR D O   1 
ATOM   10581 C CB  . TYR D 1 40  ? 8.758   40.827  -7.184  1.00 26.23  ? 69  TYR D CB  1 
ATOM   10582 C CG  . TYR D 1 40  ? 8.229   40.037  -8.355  1.00 25.17  ? 69  TYR D CG  1 
ATOM   10583 C CD1 . TYR D 1 40  ? 7.615   40.662  -9.430  1.00 23.93  ? 69  TYR D CD1 1 
ATOM   10584 C CD2 . TYR D 1 40  ? 8.382   38.663  -8.414  1.00 24.19  ? 69  TYR D CD2 1 
ATOM   10585 C CE1 . TYR D 1 40  ? 7.114   39.942  -10.503 1.00 25.70  ? 69  TYR D CE1 1 
ATOM   10586 C CE2 . TYR D 1 40  ? 7.887   37.930  -9.479  1.00 26.65  ? 69  TYR D CE2 1 
ATOM   10587 C CZ  . TYR D 1 40  ? 7.267   38.570  -10.533 1.00 24.75  ? 69  TYR D CZ  1 
ATOM   10588 O OH  . TYR D 1 40  ? 6.797   37.854  -11.592 1.00 25.55  ? 69  TYR D OH  1 
ATOM   10589 N N   . GLY D 1 41  ? 10.972  42.548  -5.419  1.00 28.31  ? 70  GLY D N   1 
ATOM   10590 C CA  . GLY D 1 41  ? 11.098  43.595  -4.407  1.00 26.98  ? 70  GLY D CA  1 
ATOM   10591 C C   . GLY D 1 41  ? 12.388  44.416  -4.507  1.00 25.06  ? 70  GLY D C   1 
ATOM   10592 O O   . GLY D 1 41  ? 12.953  44.797  -3.485  1.00 22.92  ? 70  GLY D O   1 
ATOM   10593 N N   . GLY D 1 42  ? 12.862  44.703  -5.730  1.00 26.28  ? 71  GLY D N   1 
ATOM   10594 C CA  . GLY D 1 42  ? 13.984  45.628  -5.910  1.00 23.31  ? 71  GLY D CA  1 
ATOM   10595 C C   . GLY D 1 42  ? 15.271  45.160  -5.220  1.00 24.56  ? 71  GLY D C   1 
ATOM   10596 O O   . GLY D 1 42  ? 16.020  45.943  -4.612  1.00 21.63  ? 71  GLY D O   1 
ATOM   10597 N N   . MET D 1 43  ? 15.522  43.847  -5.293  1.00 22.68  ? 72  MET D N   1 
ATOM   10598 C CA  . MET D 1 43  ? 16.778  43.295  -4.801  1.00 24.75  ? 72  MET D CA  1 
ATOM   10599 C C   . MET D 1 43  ? 16.887  43.422  -3.272  1.00 24.60  ? 72  MET D C   1 
ATOM   10600 O O   . MET D 1 43  ? 17.989  43.381  -2.735  1.00 26.90  ? 72  MET D O   1 
ATOM   10601 C CB  . MET D 1 43  ? 17.970  44.020  -5.439  1.00 23.93  ? 72  MET D CB  1 
ATOM   10602 C CG  . MET D 1 43  ? 18.088  43.824  -6.950  1.00 24.11  ? 72  MET D CG  1 
ATOM   10603 S SD  . MET D 1 43  ? 19.582  44.626  -7.612  1.00 29.05  ? 72  MET D SD  1 
ATOM   10604 C CE  . MET D 1 43  ? 19.513  44.315  -9.378  1.00 29.58  ? 72  MET D CE  1 
ATOM   10605 N N   . ARG D 1 44  ? 15.759  43.576  -2.572  1.00 26.25  ? 73  ARG D N   1 
ATOM   10606 C CA  . ARG D 1 44  ? 15.759  43.793  -1.130  1.00 29.50  ? 73  ARG D CA  1 
ATOM   10607 C C   . ARG D 1 44  ? 16.411  42.600  -0.413  1.00 29.92  ? 73  ARG D C   1 
ATOM   10608 O O   . ARG D 1 44  ? 15.952  41.471  -0.537  1.00 29.13  ? 73  ARG D O   1 
ATOM   10609 C CB  . ARG D 1 44  ? 14.316  44.027  -0.669  1.00 32.80  ? 73  ARG D CB  1 
ATOM   10610 C CG  . ARG D 1 44  ? 14.138  44.743  0.664   1.00 36.83  ? 73  ARG D CG  1 
ATOM   10611 C CD  . ARG D 1 44  ? 12.672  45.138  0.763   1.00 40.81  ? 73  ARG D CD  1 
ATOM   10612 N NE  . ARG D 1 44  ? 12.186  45.635  2.047   1.00 46.73  ? 73  ARG D NE  1 
ATOM   10613 C CZ  . ARG D 1 44  ? 11.843  46.897  2.300   1.00 46.13  ? 73  ARG D CZ  1 
ATOM   10614 N NH1 . ARG D 1 44  ? 12.113  47.850  1.427   1.00 47.06  ? 73  ARG D NH1 1 
ATOM   10615 N NH2 . ARG D 1 44  ? 11.271  47.216  3.449   1.00 55.98  ? 73  ARG D NH2 1 
ATOM   10616 N N   . GLY D 1 45  ? 17.507  42.870  0.309   1.00 30.82  ? 74  GLY D N   1 
ATOM   10617 C CA  . GLY D 1 45  ? 18.206  41.868  1.102   1.00 30.03  ? 74  GLY D CA  1 
ATOM   10618 C C   . GLY D 1 45  ? 19.197  41.065  0.270   1.00 30.35  ? 74  GLY D C   1 
ATOM   10619 O O   . GLY D 1 45  ? 19.876  40.188  0.788   1.00 35.22  ? 74  GLY D O   1 
ATOM   10620 N N   . MET D 1 46  ? 19.324  41.396  -1.014  1.00 27.03  ? 75  MET D N   1 
ATOM   10621 C CA  . MET D 1 46  ? 20.232  40.675  -1.872  1.00 26.88  ? 75  MET D CA  1 
ATOM   10622 C C   . MET D 1 46  ? 21.626  41.289  -1.785  1.00 23.52  ? 75  MET D C   1 
ATOM   10623 O O   . MET D 1 46  ? 21.828  42.480  -1.982  1.00 21.77  ? 75  MET D O   1 
ATOM   10624 C CB  . MET D 1 46  ? 19.723  40.729  -3.309  1.00 28.83  ? 75  MET D CB  1 
ATOM   10625 C CG  . MET D 1 46  ? 20.609  40.049  -4.303  1.00 30.85  ? 75  MET D CG  1 
ATOM   10626 S SD  . MET D 1 46  ? 19.980  40.277  -5.988  1.00 36.64  ? 75  MET D SD  1 
ATOM   10627 C CE  . MET D 1 46  ? 18.336  39.597  -5.792  1.00 33.98  ? 75  MET D CE  1 
ATOM   10628 N N   . LYS D 1 47  ? 22.618  40.434  -1.602  1.00 23.87  ? 76  LYS D N   1 
ATOM   10629 C CA  . LYS D 1 47  ? 23.993  40.857  -1.469  1.00 28.39  ? 76  LYS D CA  1 
ATOM   10630 C C   . LYS D 1 47  ? 24.591  40.973  -2.866  1.00 29.72  ? 76  LYS D C   1 
ATOM   10631 O O   . LYS D 1 47  ? 25.051  39.990  -3.437  1.00 33.66  ? 76  LYS D O   1 
ATOM   10632 C CB  . LYS D 1 47  ? 24.774  39.839  -0.636  1.00 33.00  ? 76  LYS D CB  1 
ATOM   10633 C CG  . LYS D 1 47  ? 24.418  39.816  0.844   1.00 37.08  ? 76  LYS D CG  1 
ATOM   10634 C CD  . LYS D 1 47  ? 25.353  38.954  1.681   1.00 44.09  ? 76  LYS D CD  1 
ATOM   10635 C CE  . LYS D 1 47  ? 26.633  39.666  2.061   1.00 49.62  ? 76  LYS D CE  1 
ATOM   10636 N NZ  . LYS D 1 47  ? 27.459  39.982  0.872   1.00 51.46  ? 76  LYS D NZ  1 
ATOM   10637 N N   . GLY D 1 48  ? 24.552  42.181  -3.419  1.00 28.36  ? 77  GLY D N   1 
ATOM   10638 C CA  . GLY D 1 48  ? 24.640  42.342  -4.859  1.00 29.08  ? 77  GLY D CA  1 
ATOM   10639 C C   . GLY D 1 48  ? 25.978  42.901  -5.328  1.00 27.96  ? 77  GLY D C   1 
ATOM   10640 O O   . GLY D 1 48  ? 26.323  42.712  -6.489  1.00 28.83  ? 77  GLY D O   1 
ATOM   10641 N N   . LEU D 1 49  ? 26.700  43.625  -4.462  1.00 23.51  ? 78  LEU D N   1 
ATOM   10642 C CA  . LEU D 1 49  ? 27.894  44.296  -4.945  1.00 24.90  ? 78  LEU D CA  1 
ATOM   10643 C C   . LEU D 1 49  ? 28.896  44.537  -3.820  1.00 23.56  ? 78  LEU D C   1 
ATOM   10644 O O   . LEU D 1 49  ? 28.537  44.635  -2.647  1.00 23.79  ? 78  LEU D O   1 
ATOM   10645 C CB  . LEU D 1 49  ? 27.462  45.613  -5.592  1.00 29.13  ? 78  LEU D CB  1 
ATOM   10646 C CG  . LEU D 1 49  ? 27.024  46.701  -4.619  1.00 28.78  ? 78  LEU D CG  1 
ATOM   10647 C CD1 . LEU D 1 49  ? 27.784  47.979  -4.886  1.00 32.62  ? 78  LEU D CD1 1 
ATOM   10648 C CD2 . LEU D 1 49  ? 25.516  46.932  -4.689  1.00 29.73  ? 78  LEU D CD2 1 
ATOM   10649 N N   . VAL D 1 50  ? 30.161  44.685  -4.227  1.00 23.24  ? 79  VAL D N   1 
ATOM   10650 C CA  . VAL D 1 50  ? 31.235  45.108  -3.350  1.00 24.88  ? 79  VAL D CA  1 
ATOM   10651 C C   . VAL D 1 50  ? 31.315  46.631  -3.414  1.00 22.37  ? 79  VAL D C   1 
ATOM   10652 O O   . VAL D 1 50  ? 31.380  47.208  -4.485  1.00 22.16  ? 79  VAL D O   1 
ATOM   10653 C CB  . VAL D 1 50  ? 32.582  44.467  -3.735  1.00 23.43  ? 79  VAL D CB  1 
ATOM   10654 C CG1 . VAL D 1 50  ? 33.686  44.830  -2.756  1.00 25.33  ? 79  VAL D CG1 1 
ATOM   10655 C CG2 . VAL D 1 50  ? 32.480  42.957  -3.874  1.00 25.11  ? 79  VAL D CG2 1 
ATOM   10656 N N   . TYR D 1 51  ? 31.330  47.250  -2.241  1.00 22.61  ? 80  TYR D N   1 
ATOM   10657 C CA  . TYR D 1 51  ? 31.498  48.686  -2.104  1.00 23.31  ? 80  TYR D CA  1 
ATOM   10658 C C   . TYR D 1 51  ? 32.374  48.901  -0.871  1.00 20.64  ? 80  TYR D C   1 
ATOM   10659 O O   . TYR D 1 51  ? 31.998  48.501  0.209   1.00 21.73  ? 80  TYR D O   1 
ATOM   10660 C CB  . TYR D 1 51  ? 30.094  49.296  -2.025  1.00 20.92  ? 80  TYR D CB  1 
ATOM   10661 C CG  . TYR D 1 51  ? 29.972  50.780  -2.284  1.00 20.69  ? 80  TYR D CG  1 
ATOM   10662 C CD1 . TYR D 1 51  ? 29.902  51.280  -3.568  1.00 18.75  ? 80  TYR D CD1 1 
ATOM   10663 C CD2 . TYR D 1 51  ? 29.911  51.672  -1.233  1.00 20.14  ? 80  TYR D CD2 1 
ATOM   10664 C CE1 . TYR D 1 51  ? 29.740  52.640  -3.801  1.00 19.34  ? 80  TYR D CE1 1 
ATOM   10665 C CE2 . TYR D 1 51  ? 29.792  53.039  -1.446  1.00 19.25  ? 80  TYR D CE2 1 
ATOM   10666 C CZ  . TYR D 1 51  ? 29.704  53.520  -2.736  1.00 20.48  ? 80  TYR D CZ  1 
ATOM   10667 O OH  . TYR D 1 51  ? 29.554  54.890  -2.942  1.00 21.58  ? 80  TYR D OH  1 
ATOM   10668 N N   . GLU D 1 52  ? 33.527  49.563  -1.022  1.00 23.55  ? 81  GLU D N   1 
ATOM   10669 C CA  . GLU D 1 52  ? 34.580  49.529  -0.021  1.00 25.12  ? 81  GLU D CA  1 
ATOM   10670 C C   . GLU D 1 52  ? 34.457  50.703  0.963   1.00 25.62  ? 81  GLU D C   1 
ATOM   10671 O O   . GLU D 1 52  ? 34.796  50.567  2.127   1.00 26.50  ? 81  GLU D O   1 
ATOM   10672 C CB  . GLU D 1 52  ? 35.942  49.561  -0.717  1.00 25.39  ? 81  GLU D CB  1 
ATOM   10673 C CG  . GLU D 1 52  ? 36.194  48.429  -1.711  1.00 26.44  ? 81  GLU D CG  1 
ATOM   10674 C CD  . GLU D 1 52  ? 36.428  47.064  -1.098  1.00 24.54  ? 81  GLU D CD  1 
ATOM   10675 O OE1 . GLU D 1 52  ? 36.145  46.902  0.119   1.00 26.81  ? 81  GLU D OE1 1 
ATOM   10676 O OE2 . GLU D 1 52  ? 36.939  46.184  -1.812  1.00 25.87  ? 81  GLU D OE2 1 
ATOM   10677 N N   . THR D 1 53  ? 33.946  51.857  0.518   1.00 25.19  ? 82  THR D N   1 
ATOM   10678 C CA  . THR D 1 53  ? 34.087  53.081  1.295   1.00 23.42  ? 82  THR D CA  1 
ATOM   10679 C C   . THR D 1 53  ? 33.230  53.081  2.567   1.00 25.10  ? 82  THR D C   1 
ATOM   10680 O O   . THR D 1 53  ? 33.657  53.628  3.575   1.00 24.41  ? 82  THR D O   1 
ATOM   10681 C CB  . THR D 1 53  ? 33.778  54.308  0.440   1.00 22.89  ? 82  THR D CB  1 
ATOM   10682 O OG1 . THR D 1 53  ? 32.454  54.116  -0.084  1.00 21.40  ? 82  THR D OG1 1 
ATOM   10683 C CG2 . THR D 1 53  ? 34.787  54.501  -0.675  1.00 22.82  ? 82  THR D CG2 1 
ATOM   10684 N N   . SER D 1 54  ? 32.020  52.520  2.522   1.00 27.62  ? 83  SER D N   1 
ATOM   10685 C CA  . SER D 1 54  ? 31.136  52.557  3.676   1.00 25.24  ? 83  SER D CA  1 
ATOM   10686 C C   . SER D 1 54  ? 30.250  51.319  3.684   1.00 23.76  ? 83  SER D C   1 
ATOM   10687 O O   . SER D 1 54  ? 30.008  50.723  2.644   1.00 21.75  ? 83  SER D O   1 
ATOM   10688 C CB  . SER D 1 54  ? 30.340  53.844  3.733   1.00 27.20  ? 83  SER D CB  1 
ATOM   10689 O OG  . SER D 1 54  ? 29.309  53.867  2.761   1.00 27.11  ? 83  SER D OG  1 
ATOM   10690 N N   . VAL D 1 55  ? 29.782  50.928  4.876   1.00 20.93  ? 84  VAL D N   1 
ATOM   10691 C CA  . VAL D 1 55  ? 28.923  49.770  5.026   1.00 21.70  ? 84  VAL D CA  1 
ATOM   10692 C C   . VAL D 1 55  ? 27.829  50.120  6.012   1.00 21.70  ? 84  VAL D C   1 
ATOM   10693 O O   . VAL D 1 55  ? 28.120  50.603  7.100   1.00 21.60  ? 84  VAL D O   1 
ATOM   10694 C CB  . VAL D 1 55  ? 29.713  48.536  5.498   1.00 24.22  ? 84  VAL D CB  1 
ATOM   10695 C CG1 . VAL D 1 55  ? 28.816  47.319  5.687   1.00 24.04  ? 84  VAL D CG1 1 
ATOM   10696 C CG2 . VAL D 1 55  ? 30.881  48.194  4.580   1.00 25.16  ? 84  VAL D CG2 1 
ATOM   10697 N N   . LEU D 1 56  ? 26.578  49.802  5.641   1.00 22.18  ? 85  LEU D N   1 
ATOM   10698 C CA  . LEU D 1 56  ? 25.432  50.112  6.455   1.00 24.68  ? 85  LEU D CA  1 
ATOM   10699 C C   . LEU D 1 56  ? 25.054  48.877  7.245   1.00 24.45  ? 85  LEU D C   1 
ATOM   10700 O O   . LEU D 1 56  ? 24.851  47.822  6.658   1.00 24.99  ? 85  LEU D O   1 
ATOM   10701 C CB  . LEU D 1 56  ? 24.273  50.534  5.548   1.00 26.98  ? 85  LEU D CB  1 
ATOM   10702 C CG  . LEU D 1 56  ? 22.973  50.836  6.279   1.00 29.75  ? 85  LEU D CG  1 
ATOM   10703 C CD1 . LEU D 1 56  ? 23.207  51.813  7.424   1.00 30.07  ? 85  LEU D CD1 1 
ATOM   10704 C CD2 . LEU D 1 56  ? 21.937  51.386  5.312   1.00 31.41  ? 85  LEU D CD2 1 
ATOM   10705 N N   . ASP D 1 57  ? 24.980  49.045  8.563   1.00 32.23  ? 86  ASP D N   1 
ATOM   10706 C CA  . ASP D 1 57  ? 24.545  47.997  9.470   1.00 35.17  ? 86  ASP D CA  1 
ATOM   10707 C C   . ASP D 1 57  ? 23.052  48.205  9.700   1.00 32.39  ? 86  ASP D C   1 
ATOM   10708 O O   . ASP D 1 57  ? 22.639  49.325  9.997   1.00 30.73  ? 86  ASP D O   1 
ATOM   10709 C CB  . ASP D 1 57  ? 25.370  48.057  10.758  1.00 38.73  ? 86  ASP D CB  1 
ATOM   10710 C CG  . ASP D 1 57  ? 25.176  46.858  11.666  1.00 44.84  ? 86  ASP D CG  1 
ATOM   10711 O OD1 . ASP D 1 57  ? 24.011  46.521  11.938  1.00 49.18  ? 86  ASP D OD1 1 
ATOM   10712 O OD2 . ASP D 1 57  ? 26.192  46.281  12.094  1.00 48.71  ? 86  ASP D OD2 1 
ATOM   10713 N N   . PRO D 1 58  ? 22.187  47.188  9.487   1.00 33.30  ? 87  PRO D N   1 
ATOM   10714 C CA  . PRO D 1 58  ? 20.742  47.349  9.663   1.00 34.50  ? 87  PRO D CA  1 
ATOM   10715 C C   . PRO D 1 58  ? 20.347  47.815  11.062  1.00 33.37  ? 87  PRO D C   1 
ATOM   10716 O O   . PRO D 1 58  ? 19.344  48.500  11.222  1.00 28.09  ? 87  PRO D O   1 
ATOM   10717 C CB  . PRO D 1 58  ? 20.164  45.943  9.432   1.00 35.70  ? 87  PRO D CB  1 
ATOM   10718 C CG  . PRO D 1 58  ? 21.201  45.251  8.578   1.00 37.77  ? 87  PRO D CG  1 
ATOM   10719 C CD  . PRO D 1 58  ? 22.538  45.850  8.976   1.00 38.71  ? 87  PRO D CD  1 
ATOM   10720 N N   . ASP D 1 59  ? 21.163  47.439  12.052  1.00 35.58  ? 88  ASP D N   1 
ATOM   10721 C CA  . ASP D 1 59  ? 20.917  47.766  13.448  1.00 39.07  ? 88  ASP D CA  1 
ATOM   10722 C C   . ASP D 1 59  ? 21.625  49.061  13.842  1.00 40.93  ? 88  ASP D C   1 
ATOM   10723 O O   . ASP D 1 59  ? 21.000  49.944  14.426  1.00 43.13  ? 88  ASP D O   1 
ATOM   10724 C CB  . ASP D 1 59  ? 21.371  46.605  14.334  1.00 43.43  ? 88  ASP D CB  1 
ATOM   10725 C CG  . ASP D 1 59  ? 20.541  45.352  14.122  1.00 43.53  ? 88  ASP D CG  1 
ATOM   10726 O OD1 . ASP D 1 59  ? 19.303  45.464  14.189  1.00 48.08  ? 88  ASP D OD1 1 
ATOM   10727 O OD2 . ASP D 1 59  ? 21.139  44.289  13.876  1.00 51.59  ? 88  ASP D OD2 1 
ATOM   10728 N N   . GLU D 1 60  ? 22.914  49.165  13.490  1.00 37.13  ? 89  GLU D N   1 
ATOM   10729 C CA  . GLU D 1 60  ? 23.818  50.173  14.026  1.00 34.56  ? 89  GLU D CA  1 
ATOM   10730 C C   . GLU D 1 60  ? 23.800  51.455  13.198  1.00 29.98  ? 89  GLU D C   1 
ATOM   10731 O O   . GLU D 1 60  ? 24.091  52.540  13.698  1.00 29.18  ? 89  GLU D O   1 
ATOM   10732 C CB  . GLU D 1 60  ? 25.255  49.657  14.012  1.00 40.47  ? 89  GLU D CB  1 
ATOM   10733 C CG  . GLU D 1 60  ? 25.431  48.305  14.661  1.00 47.44  ? 89  GLU D CG  1 
ATOM   10734 C CD  . GLU D 1 60  ? 25.866  48.361  16.110  1.00 48.84  ? 89  GLU D CD  1 
ATOM   10735 O OE1 . GLU D 1 60  ? 26.807  47.618  16.470  1.00 47.23  ? 89  GLU D OE1 1 
ATOM   10736 O OE2 . GLU D 1 60  ? 25.266  49.151  16.868  1.00 59.35  ? 89  GLU D OE2 1 
ATOM   10737 N N   . GLY D 1 61  ? 23.541  51.322  11.904  1.00 27.15  ? 90  GLY D N   1 
ATOM   10738 C CA  . GLY D 1 61  ? 23.649  52.445  10.988  1.00 26.92  ? 90  GLY D CA  1 
ATOM   10739 C C   . GLY D 1 61  ? 24.944  52.387  10.195  1.00 25.54  ? 90  GLY D C   1 
ATOM   10740 O O   . GLY D 1 61  ? 25.578  51.339  10.090  1.00 26.48  ? 90  GLY D O   1 
ATOM   10741 N N   . ILE D 1 62  ? 25.336  53.533  9.651   1.00 24.08  ? 91  ILE D N   1 
ATOM   10742 C CA  . ILE D 1 62  ? 26.445  53.576  8.721   1.00 25.74  ? 91  ILE D CA  1 
ATOM   10743 C C   . ILE D 1 62  ? 27.765  53.578  9.492   1.00 24.85  ? 91  ILE D C   1 
ATOM   10744 O O   . ILE D 1 62  ? 27.864  54.170  10.570  1.00 24.16  ? 91  ILE D O   1 
ATOM   10745 C CB  . ILE D 1 62  ? 26.297  54.778  7.766   1.00 24.38  ? 91  ILE D CB  1 
ATOM   10746 C CG1 . ILE D 1 62  ? 27.307  54.742  6.613   1.00 25.28  ? 91  ILE D CG1 1 
ATOM   10747 C CG2 . ILE D 1 62  ? 26.350  56.110  8.487   1.00 23.89  ? 91  ILE D CG2 1 
ATOM   10748 C CD1 . ILE D 1 62  ? 27.015  53.691  5.575   1.00 27.66  ? 91  ILE D CD1 1 
ATOM   10749 N N   . ARG D 1 63  ? 28.741  52.846  8.942   1.00 23.20  ? 92  ARG D N   1 
ATOM   10750 C CA  . ARG D 1 63  ? 30.150  52.972  9.297   1.00 26.44  ? 92  ARG D CA  1 
ATOM   10751 C C   . ARG D 1 63  ? 30.921  53.388  8.049   1.00 23.59  ? 92  ARG D C   1 
ATOM   10752 O O   . ARG D 1 63  ? 30.815  52.747  7.006   1.00 22.08  ? 92  ARG D O   1 
ATOM   10753 C CB  . ARG D 1 63  ? 30.733  51.662  9.857   1.00 27.73  ? 92  ARG D CB  1 
ATOM   10754 C CG  . ARG D 1 63  ? 30.413  51.436  11.330  1.00 31.99  ? 92  ARG D CG  1 
ATOM   10755 C CD  . ARG D 1 63  ? 30.985  50.133  11.852  1.00 38.32  ? 92  ARG D CD  1 
ATOM   10756 N NE  . ARG D 1 63  ? 30.481  49.769  13.175  1.00 43.38  ? 92  ARG D NE  1 
ATOM   10757 C CZ  . ARG D 1 63  ? 30.760  50.392  14.320  1.00 43.42  ? 92  ARG D CZ  1 
ATOM   10758 N NH1 . ARG D 1 63  ? 31.648  51.371  14.375  1.00 44.67  ? 92  ARG D NH1 1 
ATOM   10759 N NH2 . ARG D 1 63  ? 30.161  50.002  15.430  1.00 47.79  ? 92  ARG D NH2 1 
ATOM   10760 N N   . PHE D 1 64  ? 31.680  54.476  8.182   1.00 23.23  ? 93  PHE D N   1 
ATOM   10761 C CA  . PHE D 1 64  ? 32.607  54.929  7.165   1.00 22.62  ? 93  PHE D CA  1 
ATOM   10762 C C   . PHE D 1 64  ? 33.963  54.273  7.398   1.00 24.60  ? 93  PHE D C   1 
ATOM   10763 O O   . PHE D 1 64  ? 34.650  54.601  8.370   1.00 25.89  ? 93  PHE D O   1 
ATOM   10764 C CB  . PHE D 1 64  ? 32.733  56.450  7.218   1.00 21.45  ? 93  PHE D CB  1 
ATOM   10765 C CG  . PHE D 1 64  ? 31.433  57.179  7.035   1.00 24.86  ? 93  PHE D CG  1 
ATOM   10766 C CD1 . PHE D 1 64  ? 30.762  57.148  5.827   1.00 25.86  ? 93  PHE D CD1 1 
ATOM   10767 C CD2 . PHE D 1 64  ? 30.883  57.909  8.077   1.00 30.21  ? 93  PHE D CD2 1 
ATOM   10768 C CE1 . PHE D 1 64  ? 29.569  57.839  5.675   1.00 28.59  ? 93  PHE D CE1 1 
ATOM   10769 C CE2 . PHE D 1 64  ? 29.685  58.585  7.923   1.00 29.50  ? 93  PHE D CE2 1 
ATOM   10770 C CZ  . PHE D 1 64  ? 29.032  58.556  6.723   1.00 29.51  ? 93  PHE D CZ  1 
ATOM   10771 N N   . ARG D 1 65  ? 34.323  53.327  6.522   1.00 20.81  ? 94  ARG D N   1 
ATOM   10772 C CA  . ARG D 1 65  ? 35.565  52.593  6.665   1.00 22.38  ? 94  ARG D CA  1 
ATOM   10773 C C   . ARG D 1 65  ? 35.716  52.078  8.103   1.00 24.20  ? 94  ARG D C   1 
ATOM   10774 O O   . ARG D 1 65  ? 36.809  52.118  8.647   1.00 25.19  ? 94  ARG D O   1 
ATOM   10775 C CB  . ARG D 1 65  ? 36.735  53.499  6.289   1.00 20.00  ? 94  ARG D CB  1 
ATOM   10776 C CG  . ARG D 1 65  ? 36.874  53.747  4.800   1.00 20.92  ? 94  ARG D CG  1 
ATOM   10777 C CD  . ARG D 1 65  ? 37.354  52.533  4.043   1.00 22.07  ? 94  ARG D CD  1 
ATOM   10778 N NE  . ARG D 1 65  ? 37.663  52.880  2.663   1.00 22.81  ? 94  ARG D NE  1 
ATOM   10779 C CZ  . ARG D 1 65  ? 38.316  52.093  1.814   1.00 25.94  ? 94  ARG D CZ  1 
ATOM   10780 N NH1 . ARG D 1 65  ? 38.515  50.829  2.126   1.00 26.82  ? 94  ARG D NH1 1 
ATOM   10781 N NH2 . ARG D 1 65  ? 38.731  52.557  0.645   1.00 24.65  ? 94  ARG D NH2 1 
ATOM   10782 N N   . GLY D 1 66  ? 34.607  51.667  8.722   1.00 25.23  ? 95  GLY D N   1 
ATOM   10783 C CA  . GLY D 1 66  ? 34.620  51.096  10.060  1.00 25.00  ? 95  GLY D CA  1 
ATOM   10784 C C   . GLY D 1 66  ? 34.240  52.079  11.164  1.00 23.17  ? 95  GLY D C   1 
ATOM   10785 O O   . GLY D 1 66  ? 34.028  51.654  12.293  1.00 23.18  ? 95  GLY D O   1 
ATOM   10786 N N   . PHE D 1 67  ? 34.224  53.395  10.871  1.00 25.98  ? 96  PHE D N   1 
ATOM   10787 C CA  . PHE D 1 67  ? 33.958  54.405  11.881  1.00 24.37  ? 96  PHE D CA  1 
ATOM   10788 C C   . PHE D 1 67  ? 32.497  54.862  11.865  1.00 23.57  ? 96  PHE D C   1 
ATOM   10789 O O   . PHE D 1 67  ? 32.012  55.312  10.831  1.00 23.12  ? 96  PHE D O   1 
ATOM   10790 C CB  . PHE D 1 67  ? 34.862  55.622  11.668  1.00 24.98  ? 96  PHE D CB  1 
ATOM   10791 C CG  . PHE D 1 67  ? 36.345  55.330  11.722  1.00 26.47  ? 96  PHE D CG  1 
ATOM   10792 C CD1 . PHE D 1 67  ? 37.025  54.851  10.613  1.00 25.32  ? 96  PHE D CD1 1 
ATOM   10793 C CD2 . PHE D 1 67  ? 37.048  55.487  12.903  1.00 26.97  ? 96  PHE D CD2 1 
ATOM   10794 C CE1 . PHE D 1 67  ? 38.386  54.595  10.669  1.00 27.49  ? 96  PHE D CE1 1 
ATOM   10795 C CE2 . PHE D 1 67  ? 38.410  55.210  12.963  1.00 26.66  ? 96  PHE D CE2 1 
ATOM   10796 C CZ  . PHE D 1 67  ? 39.075  54.762  11.851  1.00 27.44  ? 96  PHE D CZ  1 
ATOM   10797 N N   . SER D 1 68  ? 31.859  54.850  13.053  1.00 23.46  ? 97  SER D N   1 
ATOM   10798 C CA  . SER D 1 68  ? 30.517  55.370  13.276  1.00 24.92  ? 97  SER D CA  1 
ATOM   10799 C C   . SER D 1 68  ? 30.493  56.880  13.135  1.00 25.82  ? 97  SER D C   1 
ATOM   10800 O O   . SER D 1 68  ? 31.539  57.524  13.144  1.00 27.58  ? 97  SER D O   1 
ATOM   10801 C CB  . SER D 1 68  ? 30.007  54.983  14.644  1.00 26.69  ? 97  SER D CB  1 
ATOM   10802 O OG  . SER D 1 68  ? 30.579  55.803  15.646  1.00 26.77  ? 97  SER D OG  1 
ATOM   10803 N N   . ILE D 1 69  ? 29.287  57.450  13.045  1.00 25.60  ? 98  ILE D N   1 
ATOM   10804 C CA  . ILE D 1 69  ? 29.195  58.894  12.907  1.00 24.51  ? 98  ILE D CA  1 
ATOM   10805 C C   . ILE D 1 69  ? 29.764  59.575  14.150  1.00 28.15  ? 98  ILE D C   1 
ATOM   10806 O O   . ILE D 1 69  ? 30.577  60.485  14.011  1.00 27.46  ? 98  ILE D O   1 
ATOM   10807 C CB  . ILE D 1 69  ? 27.773  59.351  12.550  1.00 25.66  ? 98  ILE D CB  1 
ATOM   10808 C CG1 . ILE D 1 69  ? 27.542  59.207  11.040  1.00 26.55  ? 98  ILE D CG1 1 
ATOM   10809 C CG2 . ILE D 1 69  ? 27.539  60.776  13.012  1.00 24.85  ? 98  ILE D CG2 1 
ATOM   10810 C CD1 . ILE D 1 69  ? 26.087  59.249  10.634  1.00 27.57  ? 98  ILE D CD1 1 
ATOM   10811 N N   . PRO D 1 70  ? 29.352  59.196  15.388  1.00 30.14  ? 99  PRO D N   1 
ATOM   10812 C CA  . PRO D 1 70  ? 29.946  59.767  16.604  1.00 31.22  ? 99  PRO D CA  1 
ATOM   10813 C C   . PRO D 1 70  ? 31.474  59.682  16.626  1.00 29.93  ? 99  PRO D C   1 
ATOM   10814 O O   . PRO D 1 70  ? 32.138  60.661  16.954  1.00 32.96  ? 99  PRO D O   1 
ATOM   10815 C CB  . PRO D 1 70  ? 29.301  58.937  17.713  1.00 30.12  ? 99  PRO D CB  1 
ATOM   10816 C CG  . PRO D 1 70  ? 27.959  58.590  17.138  1.00 27.24  ? 99  PRO D CG  1 
ATOM   10817 C CD  . PRO D 1 70  ? 28.274  58.244  15.698  1.00 26.74  ? 99  PRO D CD  1 
ATOM   10818 N N   . GLU D 1 71  ? 32.031  58.541  16.215  1.00 28.32  ? 100 GLU D N   1 
ATOM   10819 C CA  . GLU D 1 71  ? 33.477  58.378  16.142  1.00 29.24  ? 100 GLU D CA  1 
ATOM   10820 C C   . GLU D 1 71  ? 34.100  59.375  15.159  1.00 30.34  ? 100 GLU D C   1 
ATOM   10821 O O   . GLU D 1 71  ? 35.142  59.962  15.469  1.00 31.15  ? 100 GLU D O   1 
ATOM   10822 C CB  . GLU D 1 71  ? 33.830  56.927  15.814  1.00 32.44  ? 100 GLU D CB  1 
ATOM   10823 C CG  . GLU D 1 71  ? 33.499  55.960  16.944  1.00 33.16  ? 100 GLU D CG  1 
ATOM   10824 C CD  . GLU D 1 71  ? 33.567  54.495  16.555  1.00 36.15  ? 100 GLU D CD  1 
ATOM   10825 O OE1 . GLU D 1 71  ? 33.851  54.207  15.380  1.00 38.41  ? 100 GLU D OE1 1 
ATOM   10826 O OE2 . GLU D 1 71  ? 33.333  53.638  17.427  1.00 40.27  ? 100 GLU D OE2 1 
ATOM   10827 N N   . CYS D 1 72  ? 33.452  59.593  14.001  1.00 30.02  ? 101 CYS D N   1 
ATOM   10828 C CA  . CYS D 1 72  ? 33.901  60.586  13.032  1.00 28.38  ? 101 CYS D CA  1 
ATOM   10829 C C   . CYS D 1 72  ? 33.734  62.015  13.552  1.00 29.49  ? 101 CYS D C   1 
ATOM   10830 O O   . CYS D 1 72  ? 34.518  62.885  13.201  1.00 28.49  ? 101 CYS D O   1 
ATOM   10831 C CB  . CYS D 1 72  ? 33.139  60.482  11.716  1.00 31.19  ? 101 CYS D CB  1 
ATOM   10832 S SG  . CYS D 1 72  ? 33.595  59.026  10.748  1.00 29.45  ? 101 CYS D SG  1 
ATOM   10833 N N   . GLN D 1 73  ? 32.718  62.264  14.381  1.00 33.94  ? 102 GLN D N   1 
ATOM   10834 C CA  . GLN D 1 73  ? 32.513  63.596  14.933  1.00 38.00  ? 102 GLN D CA  1 
ATOM   10835 C C   . GLN D 1 73  ? 33.687  63.988  15.828  1.00 38.64  ? 102 GLN D C   1 
ATOM   10836 O O   . GLN D 1 73  ? 34.000  65.170  15.965  1.00 35.31  ? 102 GLN D O   1 
ATOM   10837 C CB  . GLN D 1 73  ? 31.232  63.678  15.761  1.00 41.85  ? 102 GLN D CB  1 
ATOM   10838 C CG  . GLN D 1 73  ? 29.972  63.881  14.943  1.00 48.17  ? 102 GLN D CG  1 
ATOM   10839 C CD  . GLN D 1 73  ? 28.766  63.957  15.848  1.00 53.26  ? 102 GLN D CD  1 
ATOM   10840 O OE1 . GLN D 1 73  ? 28.249  62.939  16.305  1.00 55.33  ? 102 GLN D OE1 1 
ATOM   10841 N NE2 . GLN D 1 73  ? 28.309  65.173  16.110  1.00 54.21  ? 102 GLN D NE2 1 
ATOM   10842 N N   . LYS D 1 74  ? 34.312  62.982  16.442  1.00 39.05  ? 103 LYS D N   1 
ATOM   10843 C CA  . LYS D 1 74  ? 35.424  63.188  17.352  1.00 43.08  ? 103 LYS D CA  1 
ATOM   10844 C C   . LYS D 1 74  ? 36.736  63.225  16.575  1.00 39.55  ? 103 LYS D C   1 
ATOM   10845 O O   . LYS D 1 74  ? 37.475  64.200  16.682  1.00 44.23  ? 103 LYS D O   1 
ATOM   10846 C CB  . LYS D 1 74  ? 35.431  62.080  18.408  1.00 45.48  ? 103 LYS D CB  1 
ATOM   10847 C CG  . LYS D 1 74  ? 34.216  62.063  19.327  1.00 48.31  ? 103 LYS D CG  1 
ATOM   10848 C CD  . LYS D 1 74  ? 34.552  61.881  20.802  1.00 46.96  ? 103 LYS D CD  1 
ATOM   10849 C CE  . LYS D 1 74  ? 35.523  62.927  21.305  1.00 45.69  ? 103 LYS D CE  1 
ATOM   10850 N NZ  . LYS D 1 74  ? 34.905  64.274  21.340  1.00 44.34  ? 103 LYS D NZ  1 
ATOM   10851 N N   . LEU D 1 75  ? 36.983  62.189  15.759  1.00 32.72  ? 104 LEU D N   1 
ATOM   10852 C CA  . LEU D 1 75  ? 38.321  61.909  15.256  1.00 32.31  ? 104 LEU D CA  1 
ATOM   10853 C C   . LEU D 1 75  ? 38.656  62.779  14.048  1.00 28.87  ? 104 LEU D C   1 
ATOM   10854 O O   . LEU D 1 75  ? 39.803  63.174  13.889  1.00 27.61  ? 104 LEU D O   1 
ATOM   10855 C CB  . LEU D 1 75  ? 38.463  60.424  14.900  1.00 35.15  ? 104 LEU D CB  1 
ATOM   10856 C CG  . LEU D 1 75  ? 38.720  59.436  16.047  1.00 36.98  ? 104 LEU D CG  1 
ATOM   10857 C CD1 . LEU D 1 75  ? 39.134  58.080  15.493  1.00 36.64  ? 104 LEU D CD1 1 
ATOM   10858 C CD2 . LEU D 1 75  ? 39.786  59.926  17.024  1.00 41.63  ? 104 LEU D CD2 1 
ATOM   10859 N N   . LEU D 1 76  ? 37.683  63.068  13.182  1.00 29.94  ? 105 LEU D N   1 
ATOM   10860 C CA  . LEU D 1 76  ? 37.970  63.833  11.972  1.00 27.83  ? 105 LEU D CA  1 
ATOM   10861 C C   . LEU D 1 76  ? 38.356  65.268  12.312  1.00 32.69  ? 105 LEU D C   1 
ATOM   10862 O O   . LEU D 1 76  ? 37.779  65.864  13.231  1.00 30.91  ? 105 LEU D O   1 
ATOM   10863 C CB  . LEU D 1 76  ? 36.743  63.846  11.055  1.00 28.43  ? 105 LEU D CB  1 
ATOM   10864 C CG  . LEU D 1 76  ? 36.388  62.503  10.423  1.00 27.70  ? 105 LEU D CG  1 
ATOM   10865 C CD1 . LEU D 1 76  ? 35.150  62.620  9.559   1.00 28.32  ? 105 LEU D CD1 1 
ATOM   10866 C CD2 . LEU D 1 76  ? 37.557  61.960  9.620   1.00 29.08  ? 105 LEU D CD2 1 
ATOM   10867 N N   . PRO D 1 77  ? 39.328  65.854  11.563  1.00 27.22  ? 106 PRO D N   1 
ATOM   10868 C CA  . PRO D 1 77  ? 39.660  67.273  11.680  1.00 30.08  ? 106 PRO D CA  1 
ATOM   10869 C C   . PRO D 1 77  ? 38.491  68.232  11.484  1.00 27.68  ? 106 PRO D C   1 
ATOM   10870 O O   . PRO D 1 77  ? 37.629  68.069  10.632  1.00 24.60  ? 106 PRO D O   1 
ATOM   10871 C CB  . PRO D 1 77  ? 40.711  67.512  10.589  1.00 28.33  ? 106 PRO D CB  1 
ATOM   10872 C CG  . PRO D 1 77  ? 41.388  66.169  10.463  1.00 27.79  ? 106 PRO D CG  1 
ATOM   10873 C CD  . PRO D 1 77  ? 40.272  65.159  10.667  1.00 27.26  ? 106 PRO D CD  1 
ATOM   10874 N N   . LYS D 1 78  ? 38.498  69.250  12.331  1.00 29.11  ? 107 LYS D N   1 
ATOM   10875 C CA  . LYS D 1 78  ? 37.485  70.274  12.360  1.00 27.08  ? 107 LYS D CA  1 
ATOM   10876 C C   . LYS D 1 78  ? 38.127  71.501  11.746  1.00 26.93  ? 107 LYS D C   1 
ATOM   10877 O O   . LYS D 1 78  ? 39.350  71.548  11.658  1.00 24.70  ? 107 LYS D O   1 
ATOM   10878 C CB  . LYS D 1 78  ? 37.067  70.472  13.812  1.00 27.13  ? 107 LYS D CB  1 
ATOM   10879 C CG  . LYS D 1 78  ? 36.614  69.187  14.481  1.00 29.39  ? 107 LYS D CG  1 
ATOM   10880 C CD  . LYS D 1 78  ? 36.545  69.245  15.991  1.00 32.51  ? 107 LYS D CD  1 
ATOM   10881 C CE  . LYS D 1 78  ? 35.806  68.068  16.596  1.00 34.22  ? 107 LYS D CE  1 
ATOM   10882 N NZ  . LYS D 1 78  ? 36.269  66.774  16.032  1.00 36.35  ? 107 LYS D NZ  1 
ATOM   10883 N N   . ALA D 1 79  ? 37.286  72.428  11.279  1.00 26.66  ? 108 ALA D N   1 
ATOM   10884 C CA  . ALA D 1 79  ? 37.702  73.800  11.096  1.00 30.67  ? 108 ALA D CA  1 
ATOM   10885 C C   . ALA D 1 79  ? 38.377  74.304  12.371  1.00 35.83  ? 108 ALA D C   1 
ATOM   10886 O O   . ALA D 1 79  ? 38.090  73.848  13.476  1.00 38.53  ? 108 ALA D O   1 
ATOM   10887 C CB  . ALA D 1 79  ? 36.516  74.653  10.743  1.00 31.87  ? 108 ALA D CB  1 
ATOM   10888 N N   . LYS D 1 80  ? 39.271  75.272  12.181  1.00 41.04  ? 109 LYS D N   1 
ATOM   10889 C CA  . LYS D 1 80  ? 40.039  75.881  13.251  1.00 42.56  ? 109 LYS D CA  1 
ATOM   10890 C C   . LYS D 1 80  ? 39.102  76.583  14.240  1.00 38.48  ? 109 LYS D C   1 
ATOM   10891 O O   . LYS D 1 80  ? 39.207  76.377  15.450  1.00 39.92  ? 109 LYS D O   1 
ATOM   10892 C CB  . LYS D 1 80  ? 41.077  76.818  12.623  1.00 47.35  ? 109 LYS D CB  1 
ATOM   10893 C CG  . LYS D 1 80  ? 42.081  76.159  11.672  1.00 53.95  ? 109 LYS D CG  1 
ATOM   10894 C CD  . LYS D 1 80  ? 41.632  75.910  10.224  1.00 57.98  ? 109 LYS D CD  1 
ATOM   10895 C CE  . LYS D 1 80  ? 41.058  77.118  9.508   1.00 62.02  ? 109 LYS D CE  1 
ATOM   10896 N NZ  . LYS D 1 80  ? 39.577  77.197  9.591   1.00 64.14  ? 109 LYS D NZ  1 
ATOM   10897 N N   . GLY D 1 81  ? 38.138  77.372  13.756  1.00 37.09  ? 110 GLY D N   1 
ATOM   10898 C CA  . GLY D 1 81  ? 37.227  78.051  14.676  1.00 38.17  ? 110 GLY D CA  1 
ATOM   10899 C C   . GLY D 1 81  ? 35.979  77.253  15.087  1.00 35.10  ? 110 GLY D C   1 
ATOM   10900 O O   . GLY D 1 81  ? 34.983  77.846  15.481  1.00 33.77  ? 110 GLY D O   1 
ATOM   10901 N N   . GLY D 1 82  ? 35.987  75.914  15.000  1.00 33.38  ? 111 GLY D N   1 
ATOM   10902 C CA  . GLY D 1 82  ? 34.717  75.210  14.926  1.00 32.45  ? 111 GLY D CA  1 
ATOM   10903 C C   . GLY D 1 82  ? 34.724  73.819  15.554  1.00 30.93  ? 111 GLY D C   1 
ATOM   10904 O O   . GLY D 1 82  ? 35.758  73.339  16.014  1.00 35.42  ? 111 GLY D O   1 
ATOM   10905 N N   . GLU D 1 83  ? 33.553  73.168  15.509  1.00 31.18  ? 112 GLU D N   1 
ATOM   10906 C CA  . GLU D 1 83  ? 33.296  71.956  16.266  1.00 32.39  ? 112 GLU D CA  1 
ATOM   10907 C C   . GLU D 1 83  ? 32.827  70.806  15.361  1.00 31.72  ? 112 GLU D C   1 
ATOM   10908 O O   . GLU D 1 83  ? 32.737  69.674  15.826  1.00 32.86  ? 112 GLU D O   1 
ATOM   10909 C CB  . GLU D 1 83  ? 32.278  72.251  17.371  1.00 38.54  ? 112 GLU D CB  1 
ATOM   10910 C CG  . GLU D 1 83  ? 32.408  73.627  18.020  1.00 43.37  ? 112 GLU D CG  1 
ATOM   10911 C CD  . GLU D 1 83  ? 33.603  73.881  18.932  1.00 51.56  ? 112 GLU D CD  1 
ATOM   10912 O OE1 . GLU D 1 83  ? 34.302  72.903  19.301  1.00 49.10  ? 112 GLU D OE1 1 
ATOM   10913 O OE2 . GLU D 1 83  ? 33.841  75.079  19.277  1.00 53.81  ? 112 GLU D OE2 1 
ATOM   10914 N N   . GLU D 1 84  ? 32.553  71.054  14.076  1.00 25.19  ? 113 GLU D N   1 
ATOM   10915 C CA  . GLU D 1 84  ? 31.979  70.018  13.223  1.00 26.09  ? 113 GLU D CA  1 
ATOM   10916 C C   . GLU D 1 84  ? 33.063  69.416  12.324  1.00 26.46  ? 113 GLU D C   1 
ATOM   10917 O O   . GLU D 1 84  ? 33.963  70.120  11.872  1.00 23.23  ? 113 GLU D O   1 
ATOM   10918 C CB  . GLU D 1 84  ? 30.793  70.564  12.418  1.00 25.40  ? 113 GLU D CB  1 
ATOM   10919 C CG  . GLU D 1 84  ? 29.625  71.003  13.287  1.00 27.16  ? 113 GLU D CG  1 
ATOM   10920 C CD  . GLU D 1 84  ? 29.085  69.910  14.188  1.00 26.33  ? 113 GLU D CD  1 
ATOM   10921 O OE1 . GLU D 1 84  ? 29.400  68.743  13.924  1.00 31.23  ? 113 GLU D OE1 1 
ATOM   10922 O OE2 . GLU D 1 84  ? 28.379  70.205  15.171  1.00 29.11  ? 113 GLU D OE2 1 
ATOM   10923 N N   . PRO D 1 85  ? 32.978  68.101  12.015  1.00 23.83  ? 114 PRO D N   1 
ATOM   10924 C CA  . PRO D 1 85  ? 33.899  67.458  11.082  1.00 23.38  ? 114 PRO D CA  1 
ATOM   10925 C C   . PRO D 1 85  ? 33.844  68.095  9.697   1.00 22.56  ? 114 PRO D C   1 
ATOM   10926 O O   . PRO D 1 85  ? 32.767  68.405  9.188   1.00 22.89  ? 114 PRO D O   1 
ATOM   10927 C CB  . PRO D 1 85  ? 33.420  65.993  11.079  1.00 24.53  ? 114 PRO D CB  1 
ATOM   10928 C CG  . PRO D 1 85  ? 31.976  66.074  11.464  1.00 25.91  ? 114 PRO D CG  1 
ATOM   10929 C CD  . PRO D 1 85  ? 31.943  67.171  12.511  1.00 24.68  ? 114 PRO D CD  1 
ATOM   10930 N N   . LEU D 1 86  ? 35.026  68.278  9.100   1.00 23.84  ? 115 LEU D N   1 
ATOM   10931 C CA  . LEU D 1 86  ? 35.146  68.782  7.740   1.00 24.14  ? 115 LEU D CA  1 
ATOM   10932 C C   . LEU D 1 86  ? 34.924  67.663  6.743   1.00 23.45  ? 115 LEU D C   1 
ATOM   10933 O O   . LEU D 1 86  ? 35.505  66.587  6.885   1.00 22.13  ? 115 LEU D O   1 
ATOM   10934 C CB  . LEU D 1 86  ? 36.540  69.377  7.528   1.00 25.11  ? 115 LEU D CB  1 
ATOM   10935 C CG  . LEU D 1 86  ? 36.846  70.647  8.324   1.00 25.87  ? 115 LEU D CG  1 
ATOM   10936 C CD1 . LEU D 1 86  ? 38.205  71.221  7.919   1.00 27.02  ? 115 LEU D CD1 1 
ATOM   10937 C CD2 . LEU D 1 86  ? 35.774  71.695  8.130   1.00 28.72  ? 115 LEU D CD2 1 
ATOM   10938 N N   . PRO D 1 87  ? 34.121  67.889  5.684   1.00 20.68  ? 116 PRO D N   1 
ATOM   10939 C CA  . PRO D 1 87  ? 33.924  66.856  4.657   1.00 20.34  ? 116 PRO D CA  1 
ATOM   10940 C C   . PRO D 1 87  ? 35.224  66.462  3.959   1.00 19.15  ? 116 PRO D C   1 
ATOM   10941 O O   . PRO D 1 87  ? 35.417  65.299  3.629   1.00 19.12  ? 116 PRO D O   1 
ATOM   10942 C CB  . PRO D 1 87  ? 32.851  67.425  3.738   1.00 20.70  ? 116 PRO D CB  1 
ATOM   10943 C CG  . PRO D 1 87  ? 32.868  68.918  4.029   1.00 19.55  ? 116 PRO D CG  1 
ATOM   10944 C CD  . PRO D 1 87  ? 33.200  69.019  5.499   1.00 20.90  ? 116 PRO D CD  1 
ATOM   10945 N N   . GLU D 1 88  ? 36.156  67.394  3.800   1.00 18.81  ? 117 GLU D N   1 
ATOM   10946 C CA  . GLU D 1 88  ? 37.460  67.023  3.280   1.00 20.60  ? 117 GLU D CA  1 
ATOM   10947 C C   . GLU D 1 88  ? 37.989  65.789  4.001   1.00 21.26  ? 117 GLU D C   1 
ATOM   10948 O O   . GLU D 1 88  ? 38.511  64.878  3.358   1.00 22.01  ? 117 GLU D O   1 
ATOM   10949 C CB  . GLU D 1 88  ? 38.477  68.149  3.467   1.00 22.89  ? 117 GLU D CB  1 
ATOM   10950 C CG  . GLU D 1 88  ? 38.278  69.327  2.547   1.00 23.05  ? 117 GLU D CG  1 
ATOM   10951 C CD  . GLU D 1 88  ? 37.454  70.488  3.062   1.00 23.34  ? 117 GLU D CD  1 
ATOM   10952 O OE1 . GLU D 1 88  ? 36.386  70.234  3.683   1.00 23.98  ? 117 GLU D OE1 1 
ATOM   10953 O OE2 . GLU D 1 88  ? 37.840  71.652  2.770   1.00 22.52  ? 117 GLU D OE2 1 
ATOM   10954 N N   . GLY D 1 89  ? 37.931  65.766  5.343   1.00 18.85  ? 118 GLY D N   1 
ATOM   10955 C CA  . GLY D 1 89  ? 38.530  64.672  6.076   1.00 20.23  ? 118 GLY D CA  1 
ATOM   10956 C C   . GLY D 1 89  ? 37.761  63.375  5.914   1.00 20.75  ? 118 GLY D C   1 
ATOM   10957 O O   . GLY D 1 89  ? 38.365  62.313  5.951   1.00 22.49  ? 118 GLY D O   1 
ATOM   10958 N N   . LEU D 1 90  ? 36.439  63.455  5.790   1.00 20.85  ? 119 LEU D N   1 
ATOM   10959 C CA  . LEU D 1 90  ? 35.669  62.240  5.566   1.00 22.92  ? 119 LEU D CA  1 
ATOM   10960 C C   . LEU D 1 90  ? 36.075  61.603  4.234   1.00 20.20  ? 119 LEU D C   1 
ATOM   10961 O O   . LEU D 1 90  ? 36.297  60.385  4.150   1.00 21.53  ? 119 LEU D O   1 
ATOM   10962 C CB  . LEU D 1 90  ? 34.169  62.547  5.563   1.00 25.74  ? 119 LEU D CB  1 
ATOM   10963 C CG  . LEU D 1 90  ? 33.327  61.293  5.320   1.00 30.47  ? 119 LEU D CG  1 
ATOM   10964 C CD1 . LEU D 1 90  ? 32.368  60.996  6.463   1.00 33.22  ? 119 LEU D CD1 1 
ATOM   10965 C CD2 . LEU D 1 90  ? 32.622  61.406  3.984   1.00 39.18  ? 119 LEU D CD2 1 
ATOM   10966 N N   . PHE D 1 91  ? 36.149  62.427  3.194   1.00 21.90  ? 120 PHE D N   1 
ATOM   10967 C CA  . PHE D 1 91  ? 36.628  61.974  1.891   1.00 19.36  ? 120 PHE D CA  1 
ATOM   10968 C C   . PHE D 1 91  ? 37.971  61.269  2.057   1.00 20.42  ? 120 PHE D C   1 
ATOM   10969 O O   . PHE D 1 91  ? 38.162  60.153  1.572   1.00 22.29  ? 120 PHE D O   1 
ATOM   10970 C CB  . PHE D 1 91  ? 36.815  63.156  0.935   1.00 18.32  ? 120 PHE D CB  1 
ATOM   10971 C CG  . PHE D 1 91  ? 37.210  62.770  -0.468  1.00 17.09  ? 120 PHE D CG  1 
ATOM   10972 C CD1 . PHE D 1 91  ? 36.313  62.122  -1.300  1.00 17.12  ? 120 PHE D CD1 1 
ATOM   10973 C CD2 . PHE D 1 91  ? 38.488  63.020  -0.962  1.00 17.99  ? 120 PHE D CD2 1 
ATOM   10974 C CE1 . PHE D 1 91  ? 36.658  61.744  -2.594  1.00 16.97  ? 120 PHE D CE1 1 
ATOM   10975 C CE2 . PHE D 1 91  ? 38.818  62.669  -2.265  1.00 20.21  ? 120 PHE D CE2 1 
ATOM   10976 C CZ  . PHE D 1 91  ? 37.922  61.990  -3.067  1.00 18.34  ? 120 PHE D CZ  1 
ATOM   10977 N N   . TRP D 1 92  ? 38.920  61.928  2.727   1.00 21.54  ? 121 TRP D N   1 
ATOM   10978 C CA  . TRP D 1 92  ? 40.209  61.298  2.962   1.00 19.87  ? 121 TRP D CA  1 
ATOM   10979 C C   . TRP D 1 92  ? 40.032  59.896  3.534   1.00 22.23  ? 121 TRP D C   1 
ATOM   10980 O O   . TRP D 1 92  ? 40.665  58.950  3.058   1.00 24.86  ? 121 TRP D O   1 
ATOM   10981 C CB  . TRP D 1 92  ? 41.100  62.171  3.847   1.00 22.30  ? 121 TRP D CB  1 
ATOM   10982 C CG  . TRP D 1 92  ? 42.502  61.652  3.896   1.00 20.56  ? 121 TRP D CG  1 
ATOM   10983 C CD1 . TRP D 1 92  ? 42.947  60.546  4.556   1.00 20.80  ? 121 TRP D CD1 1 
ATOM   10984 C CD2 . TRP D 1 92  ? 43.640  62.220  3.243   1.00 22.79  ? 121 TRP D CD2 1 
ATOM   10985 N NE1 . TRP D 1 92  ? 44.299  60.410  4.405   1.00 19.74  ? 121 TRP D NE1 1 
ATOM   10986 C CE2 . TRP D 1 92  ? 44.750  61.413  3.587   1.00 20.94  ? 121 TRP D CE2 1 
ATOM   10987 C CE3 . TRP D 1 92  ? 43.835  63.338  2.432   1.00 21.42  ? 121 TRP D CE3 1 
ATOM   10988 C CZ2 . TRP D 1 92  ? 46.027  61.678  3.105   1.00 22.80  ? 121 TRP D CZ2 1 
ATOM   10989 C CZ3 . TRP D 1 92  ? 45.102  63.605  1.970   1.00 26.38  ? 121 TRP D CZ3 1 
ATOM   10990 C CH2 . TRP D 1 92  ? 46.186  62.797  2.318   1.00 24.10  ? 121 TRP D CH2 1 
ATOM   10991 N N   . LEU D 1 93  ? 39.182  59.785  4.566   1.00 21.25  ? 122 LEU D N   1 
ATOM   10992 C CA  . LEU D 1 93  ? 38.917  58.522  5.229   1.00 21.57  ? 122 LEU D CA  1 
ATOM   10993 C C   . LEU D 1 93  ? 38.423  57.485  4.235   1.00 22.88  ? 122 LEU D C   1 
ATOM   10994 O O   . LEU D 1 93  ? 38.997  56.401  4.181   1.00 21.81  ? 122 LEU D O   1 
ATOM   10995 C CB  . LEU D 1 93  ? 37.928  58.752  6.375   1.00 22.23  ? 122 LEU D CB  1 
ATOM   10996 C CG  . LEU D 1 93  ? 37.398  57.507  7.072   1.00 21.92  ? 122 LEU D CG  1 
ATOM   10997 C CD1 . LEU D 1 93  ? 38.565  56.665  7.571   1.00 21.10  ? 122 LEU D CD1 1 
ATOM   10998 C CD2 . LEU D 1 93  ? 36.469  57.864  8.232   1.00 21.53  ? 122 LEU D CD2 1 
ATOM   10999 N N   . LEU D 1 94  ? 37.319  57.788  3.526   1.00 24.64  ? 123 LEU D N   1 
ATOM   11000 C CA  . LEU D 1 94  ? 36.713  56.897  2.539   1.00 22.18  ? 123 LEU D CA  1 
ATOM   11001 C C   . LEU D 1 94  ? 37.763  56.416  1.545   1.00 21.64  ? 123 LEU D C   1 
ATOM   11002 O O   . LEU D 1 94  ? 37.849  55.225  1.255   1.00 25.74  ? 123 LEU D O   1 
ATOM   11003 C CB  . LEU D 1 94  ? 35.597  57.638  1.786   1.00 23.58  ? 123 LEU D CB  1 
ATOM   11004 C CG  . LEU D 1 94  ? 34.399  58.058  2.632   1.00 24.86  ? 123 LEU D CG  1 
ATOM   11005 C CD1 . LEU D 1 94  ? 33.200  58.374  1.756   1.00 23.00  ? 123 LEU D CD1 1 
ATOM   11006 C CD2 . LEU D 1 94  ? 34.058  56.968  3.629   1.00 23.30  ? 123 LEU D CD2 1 
ATOM   11007 N N   . VAL D 1 95  ? 38.519  57.360  1.010   1.00 21.49  ? 124 VAL D N   1 
ATOM   11008 C CA  . VAL D 1 95  ? 39.496  57.059  -0.018  1.00 25.67  ? 124 VAL D CA  1 
ATOM   11009 C C   . VAL D 1 95  ? 40.609  56.178  0.518   1.00 23.86  ? 124 VAL D C   1 
ATOM   11010 O O   . VAL D 1 95  ? 41.042  55.324  -0.223  1.00 25.83  ? 124 VAL D O   1 
ATOM   11011 C CB  . VAL D 1 95  ? 40.030  58.345  -0.674  1.00 26.57  ? 124 VAL D CB  1 
ATOM   11012 C CG1 . VAL D 1 95  ? 41.457  58.259  -1.182  1.00 26.53  ? 124 VAL D CG1 1 
ATOM   11013 C CG2 . VAL D 1 95  ? 39.094  58.729  -1.796  1.00 28.92  ? 124 VAL D CG2 1 
ATOM   11014 N N   . THR D 1 96  ? 41.062  56.375  1.770   1.00 24.88  ? 125 THR D N   1 
ATOM   11015 C CA  . THR D 1 96  ? 42.322  55.766  2.206   1.00 23.16  ? 125 THR D CA  1 
ATOM   11016 C C   . THR D 1 96  ? 42.111  54.639  3.202   1.00 28.35  ? 125 THR D C   1 
ATOM   11017 O O   . THR D 1 96  ? 43.019  53.832  3.409   1.00 31.38  ? 125 THR D O   1 
ATOM   11018 C CB  . THR D 1 96  ? 43.268  56.727  2.944   1.00 23.30  ? 125 THR D CB  1 
ATOM   11019 O OG1 . THR D 1 96  ? 42.663  57.184  4.159   1.00 21.13  ? 125 THR D OG1 1 
ATOM   11020 C CG2 . THR D 1 96  ? 43.706  57.900  2.102   1.00 23.80  ? 125 THR D CG2 1 
ATOM   11021 N N   . GLY D 1 97  ? 40.987  54.660  3.929   1.00 28.10  ? 126 GLY D N   1 
ATOM   11022 C CA  . GLY D 1 97  ? 40.864  53.793  5.089   1.00 26.87  ? 126 GLY D CA  1 
ATOM   11023 C C   . GLY D 1 97  ? 41.415  54.404  6.376   1.00 27.66  ? 126 GLY D C   1 
ATOM   11024 O O   . GLY D 1 97  ? 41.244  53.803  7.431   1.00 24.66  ? 126 GLY D O   1 
ATOM   11025 N N   . HIS D 1 98  ? 42.013  55.606  6.318   1.00 27.88  ? 127 HIS D N   1 
ATOM   11026 C CA  . HIS D 1 98  ? 42.706  56.181  7.462   1.00 29.43  ? 127 HIS D CA  1 
ATOM   11027 C C   . HIS D 1 98  ? 42.110  57.519  7.878   1.00 27.15  ? 127 HIS D C   1 
ATOM   11028 O O   . HIS D 1 98  ? 41.695  58.310  7.042   1.00 33.12  ? 127 HIS D O   1 
ATOM   11029 C CB  . HIS D 1 98  ? 44.160  56.520  7.124   1.00 32.58  ? 127 HIS D CB  1 
ATOM   11030 C CG  . HIS D 1 98  ? 44.962  55.329  6.740   1.00 35.61  ? 127 HIS D CG  1 
ATOM   11031 N ND1 . HIS D 1 98  ? 44.918  54.143  7.429   1.00 40.52  ? 127 HIS D ND1 1 
ATOM   11032 C CD2 . HIS D 1 98  ? 45.770  55.137  5.704   1.00 39.34  ? 127 HIS D CD2 1 
ATOM   11033 C CE1 . HIS D 1 98  ? 45.710  53.269  6.819   1.00 45.09  ? 127 HIS D CE1 1 
ATOM   11034 N NE2 . HIS D 1 98  ? 46.230  53.853  5.765   1.00 39.34  ? 127 HIS D NE2 1 
ATOM   11035 N N   . ILE D 1 99  ? 42.124  57.801  9.178   1.00 25.12  ? 128 ILE D N   1 
ATOM   11036 C CA  . ILE D 1 99  ? 41.747  59.131  9.632   1.00 24.67  ? 128 ILE D CA  1 
ATOM   11037 C C   . ILE D 1 99  ? 42.883  60.079  9.255   1.00 24.40  ? 128 ILE D C   1 
ATOM   11038 O O   . ILE D 1 99  ? 44.028  59.817  9.626   1.00 22.97  ? 128 ILE D O   1 
ATOM   11039 C CB  . ILE D 1 99  ? 41.482  59.145  11.144  1.00 24.30  ? 128 ILE D CB  1 
ATOM   11040 C CG1 . ILE D 1 99  ? 40.370  58.177  11.569  1.00 24.51  ? 128 ILE D CG1 1 
ATOM   11041 C CG2 . ILE D 1 99  ? 41.273  60.570  11.632  1.00 22.60  ? 128 ILE D CG2 1 
ATOM   11042 C CD1 . ILE D 1 99  ? 38.983  58.506  11.076  1.00 24.88  ? 128 ILE D CD1 1 
ATOM   11043 N N   . PRO D 1 100 ? 42.596  61.203  8.553   1.00 23.11  ? 129 PRO D N   1 
ATOM   11044 C CA  . PRO D 1 100 ? 43.616  62.166  8.127   1.00 25.80  ? 129 PRO D CA  1 
ATOM   11045 C C   . PRO D 1 100 ? 44.155  63.036  9.254   1.00 29.45  ? 129 PRO D C   1 
ATOM   11046 O O   . PRO D 1 100 ? 43.494  63.202  10.276  1.00 24.58  ? 129 PRO D O   1 
ATOM   11047 C CB  . PRO D 1 100 ? 42.825  63.123  7.238   1.00 27.25  ? 129 PRO D CB  1 
ATOM   11048 C CG  . PRO D 1 100 ? 41.484  63.120  7.934   1.00 24.77  ? 129 PRO D CG  1 
ATOM   11049 C CD  . PRO D 1 100 ? 41.259  61.638  8.148   1.00 23.00  ? 129 PRO D CD  1 
ATOM   11050 N N   . THR D 1 101 ? 45.354  63.581  9.040   1.00 30.58  ? 130 THR D N   1 
ATOM   11051 C CA  . THR D 1 101 ? 45.907  64.594  9.923   1.00 29.36  ? 130 THR D CA  1 
ATOM   11052 C C   . THR D 1 101 ? 45.281  65.934  9.549   1.00 33.02  ? 130 THR D C   1 
ATOM   11053 O O   . THR D 1 101 ? 44.697  66.074  8.475   1.00 29.64  ? 130 THR D O   1 
ATOM   11054 C CB  . THR D 1 101 ? 47.433  64.660  9.793   1.00 30.23  ? 130 THR D CB  1 
ATOM   11055 O OG1 . THR D 1 101 ? 47.754  65.155  8.495   1.00 28.43  ? 130 THR D OG1 1 
ATOM   11056 C CG2 . THR D 1 101 ? 48.098  63.316  9.980   1.00 30.50  ? 130 THR D CG2 1 
ATOM   11057 N N   . GLU D 1 102 ? 45.440  66.925  10.436  1.00 30.74  ? 131 GLU D N   1 
ATOM   11058 C CA  . GLU D 1 102 ? 45.025  68.281  10.129  1.00 29.07  ? 131 GLU D CA  1 
ATOM   11059 C C   . GLU D 1 102 ? 45.746  68.787  8.881   1.00 27.35  ? 131 GLU D C   1 
ATOM   11060 O O   . GLU D 1 102 ? 45.201  69.612  8.163   1.00 24.06  ? 131 GLU D O   1 
ATOM   11061 C CB  . GLU D 1 102 ? 45.348  69.212  11.292  1.00 36.55  ? 131 GLU D CB  1 
ATOM   11062 C CG  . GLU D 1 102 ? 44.611  68.855  12.562  1.00 40.91  ? 131 GLU D CG  1 
ATOM   11063 C CD  . GLU D 1 102 ? 43.408  69.730  12.845  1.00 48.82  ? 131 GLU D CD  1 
ATOM   11064 O OE1 . GLU D 1 102 ? 43.539  70.984  12.743  1.00 54.99  ? 131 GLU D OE1 1 
ATOM   11065 O OE2 . GLU D 1 102 ? 42.356  69.162  13.192  1.00 53.68  ? 131 GLU D OE2 1 
ATOM   11066 N N   . GLU D 1 103 ? 47.001  68.357  8.681   1.00 24.82  ? 132 GLU D N   1 
ATOM   11067 C CA  . GLU D 1 103 ? 47.803  68.805  7.547   1.00 26.70  ? 132 GLU D CA  1 
ATOM   11068 C C   . GLU D 1 103 ? 47.260  68.207  6.244   1.00 24.82  ? 132 GLU D C   1 
ATOM   11069 O O   . GLU D 1 103 ? 47.304  68.829  5.177   1.00 26.78  ? 132 GLU D O   1 
ATOM   11070 C CB  . GLU D 1 103 ? 49.282  68.426  7.733   1.00 26.51  ? 132 GLU D CB  1 
ATOM   11071 C CG  . GLU D 1 103 ? 49.988  69.194  8.840   1.00 31.11  ? 132 GLU D CG  1 
ATOM   11072 C CD  . GLU D 1 103 ? 49.542  68.797  10.243  1.00 34.90  ? 132 GLU D CD  1 
ATOM   11073 O OE1 . GLU D 1 103 ? 49.536  67.574  10.539  1.00 33.37  ? 132 GLU D OE1 1 
ATOM   11074 O OE2 . GLU D 1 103 ? 49.184  69.698  11.029  1.00 35.85  ? 132 GLU D OE2 1 
ATOM   11075 N N   . GLN D 1 104 ? 46.817  66.946  6.291   1.00 25.48  ? 133 GLN D N   1 
ATOM   11076 C CA  . GLN D 1 104 ? 46.311  66.324  5.075   1.00 24.30  ? 133 GLN D CA  1 
ATOM   11077 C C   . GLN D 1 104 ? 45.008  67.013  4.648   1.00 26.12  ? 133 GLN D C   1 
ATOM   11078 O O   . GLN D 1 104 ? 44.796  67.308  3.470   1.00 26.21  ? 133 GLN D O   1 
ATOM   11079 C CB  . GLN D 1 104 ? 46.177  64.831  5.334   1.00 23.73  ? 133 GLN D CB  1 
ATOM   11080 C CG  . GLN D 1 104 ? 47.517  64.116  5.318   1.00 24.46  ? 133 GLN D CG  1 
ATOM   11081 C CD  . GLN D 1 104 ? 47.450  62.711  5.848   1.00 25.28  ? 133 GLN D CD  1 
ATOM   11082 O OE1 . GLN D 1 104 ? 46.588  62.372  6.649   1.00 27.36  ? 133 GLN D OE1 1 
ATOM   11083 N NE2 . GLN D 1 104 ? 48.438  61.905  5.499   1.00 27.28  ? 133 GLN D NE2 1 
ATOM   11084 N N   . VAL D 1 105 ? 44.157  67.316  5.621   1.00 25.48  ? 134 VAL D N   1 
ATOM   11085 C CA  . VAL D 1 105 ? 42.890  67.976  5.341   1.00 25.20  ? 134 VAL D CA  1 
ATOM   11086 C C   . VAL D 1 105 ? 43.160  69.362  4.772   1.00 24.56  ? 134 VAL D C   1 
ATOM   11087 O O   . VAL D 1 105 ? 42.498  69.761  3.817   1.00 24.29  ? 134 VAL D O   1 
ATOM   11088 C CB  . VAL D 1 105 ? 41.988  67.985  6.589   1.00 24.81  ? 134 VAL D CB  1 
ATOM   11089 C CG1 . VAL D 1 105 ? 40.903  69.052  6.539   1.00 26.36  ? 134 VAL D CG1 1 
ATOM   11090 C CG2 . VAL D 1 105 ? 41.384  66.604  6.799   1.00 26.10  ? 134 VAL D CG2 1 
ATOM   11091 N N   . SER D 1 106 ? 44.129  70.091  5.345   1.00 23.92  ? 135 SER D N   1 
ATOM   11092 C CA  A SER D 1 106 ? 44.478  71.424  4.883   0.50 24.75  ? 135 SER D CA  1 
ATOM   11093 C CA  B SER D 1 106 ? 44.467  71.427  4.879   0.50 24.06  ? 135 SER D CA  1 
ATOM   11094 C C   . SER D 1 106 ? 44.948  71.364  3.429   1.00 24.96  ? 135 SER D C   1 
ATOM   11095 O O   . SER D 1 106 ? 44.614  72.216  2.608   1.00 24.96  ? 135 SER D O   1 
ATOM   11096 C CB  A SER D 1 106 ? 45.518  72.050  5.785   0.50 25.79  ? 135 SER D CB  1 
ATOM   11097 C CB  B SER D 1 106 ? 45.501  72.093  5.759   0.50 24.19  ? 135 SER D CB  1 
ATOM   11098 O OG  A SER D 1 106 ? 46.232  73.079  5.119   0.50 28.13  ? 135 SER D OG  1 
ATOM   11099 O OG  B SER D 1 106 ? 45.017  72.273  7.081   0.50 24.59  ? 135 SER D OG  1 
ATOM   11100 N N   . TRP D 1 107 ? 45.730  70.342  3.110   1.00 25.60  ? 136 TRP D N   1 
ATOM   11101 C CA  . TRP D 1 107 ? 46.189  70.175  1.747   1.00 29.18  ? 136 TRP D CA  1 
ATOM   11102 C C   . TRP D 1 107 ? 45.009  70.002  0.786   1.00 24.32  ? 136 TRP D C   1 
ATOM   11103 O O   . TRP D 1 107 ? 44.988  70.635  -0.246  1.00 24.45  ? 136 TRP D O   1 
ATOM   11104 C CB  . TRP D 1 107 ? 47.177  69.012  1.653   1.00 28.99  ? 136 TRP D CB  1 
ATOM   11105 C CG  . TRP D 1 107 ? 47.510  68.686  0.233   1.00 28.53  ? 136 TRP D CG  1 
ATOM   11106 C CD1 . TRP D 1 107 ? 48.407  69.309  -0.586  1.00 26.06  ? 136 TRP D CD1 1 
ATOM   11107 C CD2 . TRP D 1 107 ? 46.841  67.711  -0.574  1.00 27.11  ? 136 TRP D CD2 1 
ATOM   11108 N NE1 . TRP D 1 107 ? 48.390  68.746  -1.831  1.00 27.86  ? 136 TRP D NE1 1 
ATOM   11109 C CE2 . TRP D 1 107 ? 47.441  67.758  -1.855  1.00 27.49  ? 136 TRP D CE2 1 
ATOM   11110 C CE3 . TRP D 1 107 ? 45.814  66.792  -0.328  1.00 26.93  ? 136 TRP D CE3 1 
ATOM   11111 C CZ2 . TRP D 1 107 ? 47.032  66.929  -2.897  1.00 28.43  ? 136 TRP D CZ2 1 
ATOM   11112 C CZ3 . TRP D 1 107 ? 45.416  65.970  -1.357  1.00 25.05  ? 136 TRP D CZ3 1 
ATOM   11113 C CH2 . TRP D 1 107 ? 46.027  66.024  -2.610  1.00 27.45  ? 136 TRP D CH2 1 
ATOM   11114 N N   . LEU D 1 108 ? 44.097  69.085  1.111   1.00 24.66  ? 137 LEU D N   1 
ATOM   11115 C CA  . LEU D 1 108 ? 42.902  68.775  0.353   1.00 27.50  ? 137 LEU D CA  1 
ATOM   11116 C C   . LEU D 1 108 ? 42.038  70.034  0.167   1.00 26.33  ? 137 LEU D C   1 
ATOM   11117 O O   . LEU D 1 108 ? 41.573  70.290  -0.940  1.00 25.32  ? 137 LEU D O   1 
ATOM   11118 C CB  . LEU D 1 108 ? 42.205  67.611  1.086   1.00 28.81  ? 137 LEU D CB  1 
ATOM   11119 C CG  . LEU D 1 108 ? 41.228  66.714  0.320   1.00 30.08  ? 137 LEU D CG  1 
ATOM   11120 C CD1 . LEU D 1 108 ? 41.755  66.291  -1.050  1.00 28.25  ? 137 LEU D CD1 1 
ATOM   11121 C CD2 . LEU D 1 108 ? 40.901  65.460  1.134   1.00 26.66  ? 137 LEU D CD2 1 
ATOM   11122 N N   . SER D 1 109 ? 41.862  70.853  1.217   1.00 23.32  ? 138 SER D N   1 
ATOM   11123 C CA  . SER D 1 109 ? 41.071  72.074  1.097   1.00 23.10  ? 138 SER D CA  1 
ATOM   11124 C C   . SER D 1 109 ? 41.641  72.982  0.006   1.00 24.83  ? 138 SER D C   1 
ATOM   11125 O O   . SER D 1 109 ? 40.900  73.591  -0.756  1.00 24.86  ? 138 SER D O   1 
ATOM   11126 C CB  . SER D 1 109 ? 41.005  72.820  2.405   1.00 21.42  ? 138 SER D CB  1 
ATOM   11127 O OG  . SER D 1 109 ? 40.437  72.028  3.434   1.00 24.15  ? 138 SER D OG  1 
ATOM   11128 N N   . LYS D 1 110 ? 42.974  73.145  0.010   1.00 23.33  ? 139 LYS D N   1 
ATOM   11129 C CA  . LYS D 1 110 ? 43.635  73.932  -1.009  1.00 27.89  ? 139 LYS D CA  1 
ATOM   11130 C C   . LYS D 1 110 ? 43.533  73.256  -2.373  1.00 23.46  ? 139 LYS D C   1 
ATOM   11131 O O   . LYS D 1 110 ? 43.460  73.940  -3.372  1.00 24.70  ? 139 LYS D O   1 
ATOM   11132 C CB  . LYS D 1 110 ? 45.115  74.132  -0.669  1.00 34.49  ? 139 LYS D CB  1 
ATOM   11133 C CG  . LYS D 1 110 ? 45.409  75.036  0.526   1.00 42.31  ? 139 LYS D CG  1 
ATOM   11134 C CD  . LYS D 1 110 ? 46.898  75.378  0.654   1.00 46.39  ? 139 LYS D CD  1 
ATOM   11135 C CE  . LYS D 1 110 ? 47.790  74.156  0.760   1.00 50.40  ? 139 LYS D CE  1 
ATOM   11136 N NZ  . LYS D 1 110 ? 47.501  73.359  1.983   1.00 52.98  ? 139 LYS D NZ  1 
ATOM   11137 N N   . GLU D 1 111 ? 43.626  71.917  -2.433  1.00 26.00  ? 140 GLU D N   1 
ATOM   11138 C CA  . GLU D 1 111 ? 43.629  71.236  -3.715  1.00 28.80  ? 140 GLU D CA  1 
ATOM   11139 C C   . GLU D 1 111 ? 42.321  71.515  -4.453  1.00 28.50  ? 140 GLU D C   1 
ATOM   11140 O O   . GLU D 1 111 ? 42.308  71.731  -5.673  1.00 28.05  ? 140 GLU D O   1 
ATOM   11141 C CB  . GLU D 1 111 ? 43.776  69.722  -3.554  1.00 31.51  ? 140 GLU D CB  1 
ATOM   11142 C CG  . GLU D 1 111 ? 45.096  69.160  -4.027  1.00 35.37  ? 140 GLU D CG  1 
ATOM   11143 C CD  . GLU D 1 111 ? 45.660  69.727  -5.314  1.00 35.95  ? 140 GLU D CD  1 
ATOM   11144 O OE1 . GLU D 1 111 ? 45.447  69.130  -6.364  1.00 36.83  ? 140 GLU D OE1 1 
ATOM   11145 O OE2 . GLU D 1 111 ? 46.357  70.742  -5.244  1.00 37.45  ? 140 GLU D OE2 1 
ATOM   11146 N N   . TRP D 1 112 ? 41.222  71.523  -3.695  1.00 25.64  ? 141 TRP D N   1 
ATOM   11147 C CA  . TRP D 1 112 ? 39.903  71.732  -4.266  1.00 21.64  ? 141 TRP D CA  1 
ATOM   11148 C C   . TRP D 1 112 ? 39.673  73.206  -4.560  1.00 25.76  ? 141 TRP D C   1 
ATOM   11149 O O   . TRP D 1 112 ? 38.931  73.538  -5.486  1.00 28.39  ? 141 TRP D O   1 
ATOM   11150 C CB  . TRP D 1 112 ? 38.821  71.183  -3.341  1.00 21.06  ? 141 TRP D CB  1 
ATOM   11151 C CG  . TRP D 1 112 ? 38.791  69.689  -3.267  1.00 20.55  ? 141 TRP D CG  1 
ATOM   11152 C CD1 . TRP D 1 112 ? 39.382  68.799  -4.103  1.00 20.62  ? 141 TRP D CD1 1 
ATOM   11153 C CD2 . TRP D 1 112 ? 38.100  68.912  -2.280  1.00 21.10  ? 141 TRP D CD2 1 
ATOM   11154 N NE1 . TRP D 1 112 ? 39.096  67.518  -3.707  1.00 20.91  ? 141 TRP D NE1 1 
ATOM   11155 C CE2 . TRP D 1 112 ? 38.334  67.553  -2.578  1.00 19.60  ? 141 TRP D CE2 1 
ATOM   11156 C CE3 . TRP D 1 112 ? 37.313  69.218  -1.176  1.00 19.93  ? 141 TRP D CE3 1 
ATOM   11157 C CZ2 . TRP D 1 112 ? 37.828  66.513  -1.805  1.00 21.26  ? 141 TRP D CZ2 1 
ATOM   11158 C CZ3 . TRP D 1 112 ? 36.800  68.191  -0.424  1.00 19.23  ? 141 TRP D CZ3 1 
ATOM   11159 C CH2 . TRP D 1 112 ? 37.072  66.856  -0.713  1.00 19.82  ? 141 TRP D CH2 1 
ATOM   11160 N N   . ALA D 1 113 ? 40.337  74.088  -3.803  1.00 25.39  ? 142 ALA D N   1 
ATOM   11161 C CA  . ALA D 1 113 ? 40.267  75.511  -4.104  1.00 23.80  ? 142 ALA D CA  1 
ATOM   11162 C C   . ALA D 1 113 ? 40.981  75.809  -5.427  1.00 25.62  ? 142 ALA D C   1 
ATOM   11163 O O   . ALA D 1 113 ? 40.520  76.635  -6.202  1.00 27.50  ? 142 ALA D O   1 
ATOM   11164 C CB  . ALA D 1 113 ? 40.827  76.318  -2.947  1.00 23.72  ? 142 ALA D CB  1 
ATOM   11165 N N   . LYS D 1 114 ? 42.067  75.098  -5.725  1.00 24.74  ? 143 LYS D N   1 
ATOM   11166 C CA  . LYS D 1 114 ? 42.795  75.269  -6.971  1.00 27.89  ? 143 LYS D CA  1 
ATOM   11167 C C   . LYS D 1 114 ? 42.023  74.749  -8.189  1.00 26.11  ? 143 LYS D C   1 
ATOM   11168 O O   . LYS D 1 114 ? 42.248  75.234  -9.300  1.00 25.81  ? 143 LYS D O   1 
ATOM   11169 C CB  . LYS D 1 114 ? 44.158  74.578  -6.860  1.00 28.30  ? 143 LYS D CB  1 
ATOM   11170 C CG  . LYS D 1 114 ? 45.038  75.162  -5.758  1.00 31.44  ? 143 LYS D CG  1 
ATOM   11171 C CD  . LYS D 1 114 ? 46.507  74.833  -5.873  1.00 33.27  ? 143 LYS D CD  1 
ATOM   11172 C CE  . LYS D 1 114 ? 46.736  73.368  -6.154  1.00 38.40  ? 143 LYS D CE  1 
ATOM   11173 N NZ  . LYS D 1 114 ? 48.033  72.917  -5.589  1.00 43.99  ? 143 LYS D NZ  1 
ATOM   11174 N N   . ARG D 1 115 ? 41.112  73.789  -7.987  1.00 22.54  ? 144 ARG D N   1 
ATOM   11175 C CA  . ARG D 1 115 ? 40.470  73.074  -9.087  1.00 26.00  ? 144 ARG D CA  1 
ATOM   11176 C C   . ARG D 1 115 ? 39.038  73.555  -9.377  1.00 26.78  ? 144 ARG D C   1 
ATOM   11177 O O   . ARG D 1 115 ? 38.388  73.011  -10.282 1.00 29.91  ? 144 ARG D O   1 
ATOM   11178 C CB  . ARG D 1 115 ? 40.443  71.583  -8.731  1.00 25.73  ? 144 ARG D CB  1 
ATOM   11179 C CG  . ARG D 1 115 ? 41.783  70.878  -8.853  1.00 28.24  ? 144 ARG D CG  1 
ATOM   11180 C CD  . ARG D 1 115 ? 41.745  69.519  -8.186  1.00 32.79  ? 144 ARG D CD  1 
ATOM   11181 N NE  . ARG D 1 115 ? 43.038  68.849  -8.263  1.00 32.84  ? 144 ARG D NE  1 
ATOM   11182 C CZ  . ARG D 1 115 ? 43.344  67.855  -9.100  1.00 32.54  ? 144 ARG D CZ  1 
ATOM   11183 N NH1 . ARG D 1 115 ? 42.466  67.406  -9.970  1.00 35.45  ? 144 ARG D NH1 1 
ATOM   11184 N NH2 . ARG D 1 115 ? 44.555  67.326  -9.084  1.00 34.77  ? 144 ARG D NH2 1 
ATOM   11185 N N   . ALA D 1 116 ? 38.557  74.616  -8.699  1.00 30.36  ? 145 ALA D N   1 
ATOM   11186 C CA  . ALA D 1 116 ? 37.124  74.905  -8.584  1.00 34.68  ? 145 ALA D CA  1 
ATOM   11187 C C   . ALA D 1 116 ? 36.533  75.805  -9.679  1.00 44.93  ? 145 ALA D C   1 
ATOM   11188 O O   . ALA D 1 116 ? 35.503  76.432  -9.435  1.00 55.80  ? 145 ALA D O   1 
ATOM   11189 C CB  . ALA D 1 116 ? 36.850  75.548  -7.246  1.00 38.40  ? 145 ALA D CB  1 
ATOM   11190 N N   . ALA D 1 117 ? 37.096  75.833  -10.894 1.00 40.69  ? 146 ALA D N   1 
ATOM   11191 C CA  . ALA D 1 117 ? 36.635  76.747  -11.938 1.00 37.41  ? 146 ALA D CA  1 
ATOM   11192 C C   . ALA D 1 117 ? 35.757  76.024  -12.962 1.00 32.64  ? 146 ALA D C   1 
ATOM   11193 O O   . ALA D 1 117 ? 36.012  74.866  -13.258 1.00 29.42  ? 146 ALA D O   1 
ATOM   11194 C CB  . ALA D 1 117 ? 37.827  77.370  -12.619 1.00 36.70  ? 146 ALA D CB  1 
ATOM   11195 N N   . LEU D 1 118 ? 34.772  76.745  -13.537 1.00 31.33  ? 147 LEU D N   1 
ATOM   11196 C CA  . LEU D 1 118 ? 33.867  76.202  -14.546 1.00 27.83  ? 147 LEU D CA  1 
ATOM   11197 C C   . LEU D 1 118 ? 34.252  76.683  -15.952 1.00 28.03  ? 147 LEU D C   1 
ATOM   11198 O O   . LEU D 1 118 ? 34.619  77.835  -16.137 1.00 31.32  ? 147 LEU D O   1 
ATOM   11199 C CB  . LEU D 1 118 ? 32.444  76.663  -14.241 1.00 25.19  ? 147 LEU D CB  1 
ATOM   11200 C CG  . LEU D 1 118 ? 31.830  76.169  -12.932 1.00 24.11  ? 147 LEU D CG  1 
ATOM   11201 C CD1 . LEU D 1 118 ? 30.392  76.628  -12.815 1.00 24.04  ? 147 LEU D CD1 1 
ATOM   11202 C CD2 . LEU D 1 118 ? 31.897  74.650  -12.861 1.00 24.74  ? 147 LEU D CD2 1 
ATOM   11203 N N   . PRO D 1 119 ? 34.157  75.857  -17.007 1.00 28.54  ? 148 PRO D N   1 
ATOM   11204 C CA  . PRO D 1 119 ? 34.245  76.366  -18.383 1.00 28.29  ? 148 PRO D CA  1 
ATOM   11205 C C   . PRO D 1 119 ? 33.028  77.223  -18.718 1.00 29.33  ? 148 PRO D C   1 
ATOM   11206 O O   . PRO D 1 119 ? 31.971  77.092  -18.086 1.00 26.89  ? 148 PRO D O   1 
ATOM   11207 C CB  . PRO D 1 119 ? 34.319  75.128  -19.281 1.00 28.33  ? 148 PRO D CB  1 
ATOM   11208 C CG  . PRO D 1 119 ? 33.730  74.020  -18.414 1.00 29.90  ? 148 PRO D CG  1 
ATOM   11209 C CD  . PRO D 1 119 ? 33.970  74.406  -16.966 1.00 28.11  ? 148 PRO D CD  1 
ATOM   11210 N N   . SER D 1 120 ? 33.192  78.110  -19.707 1.00 29.74  ? 149 SER D N   1 
ATOM   11211 C CA  . SER D 1 120 ? 32.190  79.142  -19.961 1.00 29.33  ? 149 SER D CA  1 
ATOM   11212 C C   . SER D 1 120 ? 30.893  78.591  -20.576 1.00 26.48  ? 149 SER D C   1 
ATOM   11213 O O   . SER D 1 120 ? 29.848  79.197  -20.394 1.00 25.34  ? 149 SER D O   1 
ATOM   11214 C CB  . SER D 1 120 ? 32.784  80.293  -20.763 1.00 31.70  ? 149 SER D CB  1 
ATOM   11215 O OG  . SER D 1 120 ? 34.076  79.960  -21.246 1.00 33.23  ? 149 SER D OG  1 
ATOM   11216 N N   . HIS D 1 121 ? 30.917  77.423  -21.239 1.00 25.30  ? 150 HIS D N   1 
ATOM   11217 C CA  . HIS D 1 121 ? 29.687  76.860  -21.785 1.00 27.07  ? 150 HIS D CA  1 
ATOM   11218 C C   . HIS D 1 121 ? 28.773  76.365  -20.672 1.00 25.84  ? 150 HIS D C   1 
ATOM   11219 O O   . HIS D 1 121 ? 27.563  76.254  -20.884 1.00 24.56  ? 150 HIS D O   1 
ATOM   11220 C CB  . HIS D 1 121 ? 29.901  75.707  -22.769 1.00 26.90  ? 150 HIS D CB  1 
ATOM   11221 C CG  . HIS D 1 121 ? 30.420  74.408  -22.228 1.00 28.34  ? 150 HIS D CG  1 
ATOM   11222 N ND1 . HIS D 1 121 ? 31.763  74.222  -22.002 1.00 27.98  ? 150 HIS D ND1 1 
ATOM   11223 C CD2 . HIS D 1 121 ? 29.828  73.227  -21.942 1.00 28.01  ? 150 HIS D CD2 1 
ATOM   11224 C CE1 . HIS D 1 121 ? 31.977  72.987  -21.546 1.00 29.02  ? 150 HIS D CE1 1 
ATOM   11225 N NE2 . HIS D 1 121 ? 30.817  72.357  -21.522 1.00 30.44  ? 150 HIS D NE2 1 
ATOM   11226 N N   . VAL D 1 122 ? 29.365  76.009  -19.535 1.00 25.02  ? 151 VAL D N   1 
ATOM   11227 C CA  . VAL D 1 122 ? 28.575  75.536  -18.418 1.00 26.58  ? 151 VAL D CA  1 
ATOM   11228 C C   . VAL D 1 122 ? 27.925  76.752  -17.773 1.00 26.30  ? 151 VAL D C   1 
ATOM   11229 O O   . VAL D 1 122 ? 26.738  76.719  -17.456 1.00 25.86  ? 151 VAL D O   1 
ATOM   11230 C CB  . VAL D 1 122 ? 29.416  74.674  -17.454 1.00 26.13  ? 151 VAL D CB  1 
ATOM   11231 C CG1 . VAL D 1 122 ? 28.652  74.280  -16.207 1.00 23.80  ? 151 VAL D CG1 1 
ATOM   11232 C CG2 . VAL D 1 122 ? 29.934  73.429  -18.163 1.00 25.55  ? 151 VAL D CG2 1 
ATOM   11233 N N   . VAL D 1 123 ? 28.702  77.841  -17.670 1.00 26.92  ? 152 VAL D N   1 
ATOM   11234 C CA  . VAL D 1 123 ? 28.217  79.115  -17.167 1.00 29.22  ? 152 VAL D CA  1 
ATOM   11235 C C   . VAL D 1 123 ? 27.060  79.616  -18.032 1.00 28.73  ? 152 VAL D C   1 
ATOM   11236 O O   . VAL D 1 123 ? 26.008  79.970  -17.487 1.00 26.58  ? 152 VAL D O   1 
ATOM   11237 C CB  . VAL D 1 123 ? 29.359  80.150  -17.070 1.00 30.05  ? 152 VAL D CB  1 
ATOM   11238 C CG1 . VAL D 1 123 ? 28.850  81.520  -16.641 1.00 32.20  ? 152 VAL D CG1 1 
ATOM   11239 C CG2 . VAL D 1 123 ? 30.465  79.693  -16.130 1.00 28.07  ? 152 VAL D CG2 1 
ATOM   11240 N N   . THR D 1 124 ? 27.266  79.642  -19.367 1.00 27.01  ? 153 THR D N   1 
ATOM   11241 C CA  . THR D 1 124 ? 26.244  80.038  -20.329 1.00 27.58  ? 153 THR D CA  1 
ATOM   11242 C C   . THR D 1 124 ? 24.972  79.215  -20.123 1.00 22.68  ? 153 THR D C   1 
ATOM   11243 O O   . THR D 1 124 ? 23.892  79.751  -20.001 1.00 25.80  ? 153 THR D O   1 
ATOM   11244 C CB  . THR D 1 124 ? 26.716  79.868  -21.784 1.00 27.86  ? 153 THR D CB  1 
ATOM   11245 O OG1 . THR D 1 124 ? 27.832  80.719  -22.040 1.00 29.74  ? 153 THR D OG1 1 
ATOM   11246 C CG2 . THR D 1 124 ? 25.635  80.155  -22.799 1.00 30.10  ? 153 THR D CG2 1 
ATOM   11247 N N   . MET D 1 125 ? 25.109  77.893  -20.068 1.00 22.98  ? 154 MET D N   1 
ATOM   11248 C CA  . MET D 1 125 ? 23.956  77.014  -19.927 1.00 23.54  ? 154 MET D CA  1 
ATOM   11249 C C   . MET D 1 125 ? 23.230  77.249  -18.593 1.00 24.79  ? 154 MET D C   1 
ATOM   11250 O O   . MET D 1 125 ? 21.992  77.332  -18.558 1.00 27.10  ? 154 MET D O   1 
ATOM   11251 C CB  . MET D 1 125 ? 24.462  75.568  -20.025 1.00 26.31  ? 154 MET D CB  1 
ATOM   11252 C CG  . MET D 1 125 ? 23.392  74.499  -20.049 1.00 28.30  ? 154 MET D CG  1 
ATOM   11253 S SD  . MET D 1 125 ? 23.976  72.832  -19.596 1.00 35.63  ? 154 MET D SD  1 
ATOM   11254 C CE  . MET D 1 125 ? 25.687  73.181  -19.199 1.00 30.54  ? 154 MET D CE  1 
ATOM   11255 N N   . LEU D 1 126 ? 23.977  77.371  -17.482 1.00 26.87  ? 155 LEU D N   1 
ATOM   11256 C CA  . LEU D 1 126 ? 23.358  77.664  -16.192 1.00 28.55  ? 155 LEU D CA  1 
ATOM   11257 C C   . LEU D 1 126 ? 22.661  79.027  -16.237 1.00 32.49  ? 155 LEU D C   1 
ATOM   11258 O O   . LEU D 1 126 ? 21.580  79.199  -15.685 1.00 32.14  ? 155 LEU D O   1 
ATOM   11259 C CB  . LEU D 1 126 ? 24.397  77.628  -15.066 1.00 29.05  ? 155 LEU D CB  1 
ATOM   11260 C CG  . LEU D 1 126 ? 24.889  76.232  -14.680 1.00 29.76  ? 155 LEU D CG  1 
ATOM   11261 C CD1 . LEU D 1 126 ? 26.059  76.287  -13.721 1.00 30.33  ? 155 LEU D CD1 1 
ATOM   11262 C CD2 . LEU D 1 126 ? 23.761  75.436  -14.058 1.00 30.68  ? 155 LEU D CD2 1 
ATOM   11263 N N   . ASP D 1 127 ? 23.286  80.012  -16.876 1.00 32.28  ? 156 ASP D N   1 
ATOM   11264 C CA  . ASP D 1 127 ? 22.740  81.359  -16.815 1.00 35.14  ? 156 ASP D CA  1 
ATOM   11265 C C   . ASP D 1 127 ? 21.428  81.419  -17.592 1.00 34.00  ? 156 ASP D C   1 
ATOM   11266 O O   . ASP D 1 127 ? 20.556  82.215  -17.256 1.00 34.30  ? 156 ASP D O   1 
ATOM   11267 C CB  . ASP D 1 127 ? 23.767  82.409  -17.250 1.00 33.75  ? 156 ASP D CB  1 
ATOM   11268 C CG  . ASP D 1 127 ? 24.860  82.608  -16.209 1.00 37.61  ? 156 ASP D CG  1 
ATOM   11269 O OD1 . ASP D 1 127 ? 24.542  82.476  -15.013 1.00 34.99  ? 156 ASP D OD1 1 
ATOM   11270 O OD2 . ASP D 1 127 ? 26.011  82.911  -16.591 1.00 38.01  ? 156 ASP D OD2 1 
ATOM   11271 N N   . ASN D 1 128 ? 21.266  80.554  -18.599 1.00 34.99  ? 157 ASN D N   1 
ATOM   11272 C CA  . ASN D 1 128 ? 20.102  80.637  -19.469 1.00 35.23  ? 157 ASN D CA  1 
ATOM   11273 C C   . ASN D 1 128 ? 19.012  79.657  -19.062 1.00 31.08  ? 157 ASN D C   1 
ATOM   11274 O O   . ASN D 1 128 ? 17.933  79.701  -19.649 1.00 36.07  ? 157 ASN D O   1 
ATOM   11275 C CB  . ASN D 1 128 ? 20.460  80.405  -20.934 1.00 35.42  ? 157 ASN D CB  1 
ATOM   11276 C CG  . ASN D 1 128 ? 21.255  81.548  -21.516 1.00 40.30  ? 157 ASN D CG  1 
ATOM   11277 O OD1 . ASN D 1 128 ? 20.845  82.697  -21.390 1.00 43.86  ? 157 ASN D OD1 1 
ATOM   11278 N ND2 . ASN D 1 128 ? 22.390  81.249  -22.132 1.00 41.97  ? 157 ASN D ND2 1 
ATOM   11279 N N   . PHE D 1 129 ? 19.273  78.766  -18.092 1.00 29.04  ? 158 PHE D N   1 
ATOM   11280 C CA  . PHE D 1 129 ? 18.216  77.871  -17.652 1.00 29.31  ? 158 PHE D CA  1 
ATOM   11281 C C   . PHE D 1 129 ? 17.024  78.696  -17.163 1.00 33.09  ? 158 PHE D C   1 
ATOM   11282 O O   . PHE D 1 129 ? 17.195  79.697  -16.456 1.00 31.01  ? 158 PHE D O   1 
ATOM   11283 C CB  . PHE D 1 129 ? 18.631  76.931  -16.513 1.00 32.17  ? 158 PHE D CB  1 
ATOM   11284 C CG  . PHE D 1 129 ? 19.482  75.750  -16.902 1.00 30.85  ? 158 PHE D CG  1 
ATOM   11285 C CD1 . PHE D 1 129 ? 19.305  75.112  -18.118 1.00 32.11  ? 158 PHE D CD1 1 
ATOM   11286 C CD2 . PHE D 1 129 ? 20.452  75.260  -16.032 1.00 31.03  ? 158 PHE D CD2 1 
ATOM   11287 C CE1 . PHE D 1 129 ? 20.091  74.020  -18.467 1.00 34.26  ? 158 PHE D CE1 1 
ATOM   11288 C CE2 . PHE D 1 129 ? 21.244  74.181  -16.395 1.00 30.26  ? 158 PHE D CE2 1 
ATOM   11289 C CZ  . PHE D 1 129 ? 21.051  73.554  -17.601 1.00 30.11  ? 158 PHE D CZ  1 
ATOM   11290 N N   . PRO D 1 130 ? 15.782  78.244  -17.443 1.00 29.74  ? 159 PRO D N   1 
ATOM   11291 C CA  . PRO D 1 130 ? 14.595  78.925  -16.925 1.00 27.74  ? 159 PRO D CA  1 
ATOM   11292 C C   . PRO D 1 130 ? 14.341  78.606  -15.458 1.00 29.66  ? 159 PRO D C   1 
ATOM   11293 O O   . PRO D 1 130 ? 14.696  77.540  -14.973 1.00 28.27  ? 159 PRO D O   1 
ATOM   11294 C CB  . PRO D 1 130 ? 13.496  78.356  -17.809 1.00 25.40  ? 159 PRO D CB  1 
ATOM   11295 C CG  . PRO D 1 130 ? 13.944  76.926  -18.092 1.00 24.70  ? 159 PRO D CG  1 
ATOM   11296 C CD  . PRO D 1 130 ? 15.455  77.014  -18.186 1.00 26.96  ? 159 PRO D CD  1 
ATOM   11297 N N   . THR D 1 131 ? 13.617  79.502  -14.789 1.00 28.46  ? 160 THR D N   1 
ATOM   11298 C CA  . THR D 1 131 ? 13.384  79.435  -13.358 1.00 29.85  ? 160 THR D CA  1 
ATOM   11299 C C   . THR D 1 131 ? 12.499  78.247  -12.989 1.00 28.45  ? 160 THR D C   1 
ATOM   11300 O O   . THR D 1 131 ? 12.433  77.887  -11.819 1.00 29.29  ? 160 THR D O   1 
ATOM   11301 C CB  . THR D 1 131 ? 12.755  80.747  -12.873 1.00 33.35  ? 160 THR D CB  1 
ATOM   11302 O OG1 . THR D 1 131 ? 11.496  80.883  -13.538 1.00 34.42  ? 160 THR D OG1 1 
ATOM   11303 C CG2 . THR D 1 131 ? 13.655  81.933  -13.140 1.00 31.57  ? 160 THR D CG2 1 
ATOM   11304 N N   . ASN D 1 132 ? 11.861  77.606  -13.982 1.00 29.26  ? 161 ASN D N   1 
ATOM   11305 C CA  . ASN D 1 132 ? 10.979  76.482  -13.705 1.00 28.26  ? 161 ASN D CA  1 
ATOM   11306 C C   . ASN D 1 132 ? 11.708  75.158  -13.936 1.00 26.33  ? 161 ASN D C   1 
ATOM   11307 O O   . ASN D 1 132 ? 11.116  74.097  -13.792 1.00 25.10  ? 161 ASN D O   1 
ATOM   11308 C CB  . ASN D 1 132 ? 9.667   76.579  -14.490 1.00 31.92  ? 161 ASN D CB  1 
ATOM   11309 C CG  . ASN D 1 132 ? 9.811   76.146  -15.932 1.00 33.23  ? 161 ASN D CG  1 
ATOM   11310 O OD1 . ASN D 1 132 ? 9.207   75.161  -16.352 1.00 36.22  ? 161 ASN D OD1 1 
ATOM   11311 N ND2 . ASN D 1 132 ? 10.634  76.852  -16.687 1.00 34.58  ? 161 ASN D ND2 1 
ATOM   11312 N N   . LEU D 1 133 ? 13.000  75.211  -14.256 1.00 26.80  ? 162 LEU D N   1 
ATOM   11313 C CA  . LEU D 1 133 ? 13.780  73.984  -14.323 1.00 24.82  ? 162 LEU D CA  1 
ATOM   11314 C C   . LEU D 1 133 ? 14.321  73.689  -12.931 1.00 23.91  ? 162 LEU D C   1 
ATOM   11315 O O   . LEU D 1 133 ? 15.081  74.499  -12.385 1.00 26.00  ? 162 LEU D O   1 
ATOM   11316 C CB  . LEU D 1 133 ? 14.884  74.131  -15.377 1.00 23.31  ? 162 LEU D CB  1 
ATOM   11317 C CG  . LEU D 1 133 ? 15.747  72.894  -15.612 1.00 24.41  ? 162 LEU D CG  1 
ATOM   11318 C CD1 . LEU D 1 133 ? 14.910  71.669  -15.896 1.00 22.98  ? 162 LEU D CD1 1 
ATOM   11319 C CD2 . LEU D 1 133 ? 16.704  73.112  -16.778 1.00 24.68  ? 162 LEU D CD2 1 
ATOM   11320 N N   . HIS D 1 134 ? 13.973  72.492  -12.422 1.00 24.16  ? 163 HIS D N   1 
ATOM   11321 C CA  . HIS D 1 134 ? 14.221  72.120  -11.037 1.00 21.09  ? 163 HIS D CA  1 
ATOM   11322 C C   . HIS D 1 134 ? 15.727  72.152  -10.740 1.00 20.24  ? 163 HIS D C   1 
ATOM   11323 O O   . HIS D 1 134 ? 16.534  71.716  -11.557 1.00 17.96  ? 163 HIS D O   1 
ATOM   11324 C CB  . HIS D 1 134 ? 13.636  70.732  -10.723 1.00 24.03  ? 163 HIS D CB  1 
ATOM   11325 C CG  . HIS D 1 134 ? 13.720  70.351  -9.260  1.00 21.50  ? 163 HIS D CG  1 
ATOM   11326 N ND1 . HIS D 1 134 ? 14.847  69.888  -8.611  1.00 24.22  ? 163 HIS D ND1 1 
ATOM   11327 C CD2 . HIS D 1 134 ? 12.790  70.464  -8.310  1.00 25.43  ? 163 HIS D CD2 1 
ATOM   11328 C CE1 . HIS D 1 134 ? 14.573  69.691  -7.336  1.00 22.56  ? 163 HIS D CE1 1 
ATOM   11329 N NE2 . HIS D 1 134 ? 13.322  70.054  -7.134  1.00 23.92  ? 163 HIS D NE2 1 
ATOM   11330 N N   . PRO D 1 135 ? 16.166  72.670  -9.577  1.00 19.22  ? 164 PRO D N   1 
ATOM   11331 C CA  . PRO D 1 135 ? 17.591  72.700  -9.234  1.00 17.22  ? 164 PRO D CA  1 
ATOM   11332 C C   . PRO D 1 135 ? 18.365  71.409  -9.515  1.00 17.53  ? 164 PRO D C   1 
ATOM   11333 O O   . PRO D 1 135 ? 19.515  71.464  -9.931  1.00 20.84  ? 164 PRO D O   1 
ATOM   11334 C CB  . PRO D 1 135 ? 17.514  72.935  -7.719  1.00 19.21  ? 164 PRO D CB  1 
ATOM   11335 C CG  . PRO D 1 135 ? 16.362  73.908  -7.617  1.00 19.59  ? 164 PRO D CG  1 
ATOM   11336 C CD  . PRO D 1 135 ? 15.335  73.266  -8.503  1.00 20.93  ? 164 PRO D CD  1 
ATOM   11337 N N   . MET D 1 136 ? 17.752  70.262  -9.230  1.00 19.17  ? 165 MET D N   1 
ATOM   11338 C CA  . MET D 1 136 ? 18.450  68.991  -9.361  1.00 18.30  ? 165 MET D CA  1 
ATOM   11339 C C   . MET D 1 136 ? 18.683  68.691  -10.849 1.00 19.59  ? 165 MET D C   1 
ATOM   11340 O O   . MET D 1 136 ? 19.675  68.057  -11.214 1.00 17.17  ? 165 MET D O   1 
ATOM   11341 C CB  . MET D 1 136 ? 17.656  67.865  -8.706  1.00 17.63  ? 165 MET D CB  1 
ATOM   11342 C CG  . MET D 1 136 ? 17.871  67.782  -7.193  1.00 18.14  ? 165 MET D CG  1 
ATOM   11343 S SD  . MET D 1 136 ? 19.611  67.518  -6.736  1.00 19.23  ? 165 MET D SD  1 
ATOM   11344 C CE  . MET D 1 136 ? 19.751  65.738  -7.005  1.00 15.93  ? 165 MET D CE  1 
ATOM   11345 N N   . SER D 1 137 ? 17.770  69.175  -11.689 1.00 19.97  ? 166 SER D N   1 
ATOM   11346 C CA  . SER D 1 137 ? 17.898  69.045  -13.137 1.00 20.19  ? 166 SER D CA  1 
ATOM   11347 C C   . SER D 1 137 ? 19.010  69.929  -13.673 1.00 19.81  ? 166 SER D C   1 
ATOM   11348 O O   . SER D 1 137 ? 19.793  69.502  -14.510 1.00 19.58  ? 166 SER D O   1 
ATOM   11349 C CB  . SER D 1 137 ? 16.602  69.361  -13.805 1.00 21.90  ? 166 SER D CB  1 
ATOM   11350 O OG  . SER D 1 137 ? 15.647  68.367  -13.485 1.00 22.39  ? 166 SER D OG  1 
ATOM   11351 N N   . GLN D 1 138 ? 19.045  71.187  -13.236 1.00 18.76  ? 167 GLN D N   1 
ATOM   11352 C CA  . GLN D 1 138 ? 20.140  72.065  -13.619 1.00 19.31  ? 167 GLN D CA  1 
ATOM   11353 C C   . GLN D 1 138 ? 21.497  71.485  -13.232 1.00 18.92  ? 167 GLN D C   1 
ATOM   11354 O O   . GLN D 1 138 ? 22.443  71.601  -13.998 1.00 19.20  ? 167 GLN D O   1 
ATOM   11355 C CB  . GLN D 1 138 ? 19.953  73.433  -12.980 1.00 19.20  ? 167 GLN D CB  1 
ATOM   11356 C CG  . GLN D 1 138 ? 18.640  74.061  -13.408 1.00 19.37  ? 167 GLN D CG  1 
ATOM   11357 C CD  . GLN D 1 138 ? 18.613  75.528  -13.104 1.00 20.03  ? 167 GLN D CD  1 
ATOM   11358 O OE1 . GLN D 1 138 ? 19.652  76.136  -12.873 1.00 22.05  ? 167 GLN D OE1 1 
ATOM   11359 N NE2 . GLN D 1 138 ? 17.430  76.102  -13.149 1.00 23.53  ? 167 GLN D NE2 1 
ATOM   11360 N N   . LEU D 1 139 ? 21.550  70.838  -12.065 1.00 19.09  ? 168 LEU D N   1 
ATOM   11361 C CA  . LEU D 1 139 ? 22.788  70.307  -11.540 1.00 18.16  ? 168 LEU D CA  1 
ATOM   11362 C C   . LEU D 1 139 ? 23.242  69.166  -12.439 1.00 16.70  ? 168 LEU D C   1 
ATOM   11363 O O   . LEU D 1 139 ? 24.400  69.100  -12.843 1.00 16.23  ? 168 LEU D O   1 
ATOM   11364 C CB  . LEU D 1 139 ? 22.561  69.792  -10.119 1.00 18.25  ? 168 LEU D CB  1 
ATOM   11365 C CG  . LEU D 1 139 ? 23.756  69.046  -9.530  1.00 20.41  ? 168 LEU D CG  1 
ATOM   11366 C CD1 . LEU D 1 139 ? 24.956  69.980  -9.389  1.00 18.69  ? 168 LEU D CD1 1 
ATOM   11367 C CD2 . LEU D 1 139 ? 23.413  68.373  -8.199  1.00 20.31  ? 168 LEU D CD2 1 
ATOM   11368 N N   . SER D 1 140 ? 22.296  68.257  -12.682 1.00 17.61  ? 169 SER D N   1 
ATOM   11369 C CA  . SER D 1 140 ? 22.588  67.053  -13.420 1.00 18.77  ? 169 SER D CA  1 
ATOM   11370 C C   . SER D 1 140 ? 23.024  67.445  -14.826 1.00 16.67  ? 169 SER D C   1 
ATOM   11371 O O   . SER D 1 140 ? 24.064  67.000  -15.279 1.00 20.01  ? 169 SER D O   1 
ATOM   11372 C CB  . SER D 1 140 ? 21.415  66.131  -13.446 1.00 19.44  ? 169 SER D CB  1 
ATOM   11373 O OG  . SER D 1 140 ? 21.641  65.102  -14.403 1.00 25.30  ? 169 SER D OG  1 
ATOM   11374 N N   . ALA D 1 141 ? 22.302  68.395  -15.448 1.00 17.14  ? 170 ALA D N   1 
ATOM   11375 C CA  . ALA D 1 141 ? 22.572  68.769  -16.828 1.00 16.58  ? 170 ALA D CA  1 
ATOM   11376 C C   . ALA D 1 141 ? 23.936  69.434  -16.881 1.00 17.19  ? 170 ALA D C   1 
ATOM   11377 O O   . ALA D 1 141 ? 24.663  69.214  -17.836 1.00 17.79  ? 170 ALA D O   1 
ATOM   11378 C CB  . ALA D 1 141 ? 21.490  69.661  -17.409 1.00 16.78  ? 170 ALA D CB  1 
ATOM   11379 N N   . ALA D 1 142 ? 24.264  70.211  -15.837 1.00 19.36  ? 171 ALA D N   1 
ATOM   11380 C CA  . ALA D 1 142 ? 25.514  70.967  -15.818 1.00 21.25  ? 171 ALA D CA  1 
ATOM   11381 C C   . ALA D 1 142 ? 26.690  70.015  -15.669 1.00 22.13  ? 171 ALA D C   1 
ATOM   11382 O O   . ALA D 1 142 ? 27.720  70.176  -16.325 1.00 23.48  ? 171 ALA D O   1 
ATOM   11383 C CB  . ALA D 1 142 ? 25.504  72.041  -14.745 1.00 21.99  ? 171 ALA D CB  1 
ATOM   11384 N N   . VAL D 1 143 ? 26.526  68.997  -14.817 1.00 21.42  ? 172 VAL D N   1 
ATOM   11385 C CA  . VAL D 1 143 ? 27.606  68.052  -14.598 1.00 21.49  ? 172 VAL D CA  1 
ATOM   11386 C C   . VAL D 1 143 ? 27.830  67.222  -15.873 1.00 19.00  ? 172 VAL D C   1 
ATOM   11387 O O   . VAL D 1 143 ? 28.976  66.935  -16.211 1.00 18.90  ? 172 VAL D O   1 
ATOM   11388 C CB  . VAL D 1 143 ? 27.355  67.201  -13.341 1.00 21.78  ? 172 VAL D CB  1 
ATOM   11389 C CG1 . VAL D 1 143 ? 28.367  66.069  -13.188 1.00 21.14  ? 172 VAL D CG1 1 
ATOM   11390 C CG2 . VAL D 1 143 ? 27.363  68.084  -12.095 1.00 22.93  ? 172 VAL D CG2 1 
ATOM   11391 N N   . THR D 1 144 ? 26.748  66.830  -16.547 1.00 18.50  ? 173 THR D N   1 
ATOM   11392 C CA  . THR D 1 144 ? 26.833  66.129  -17.819 1.00 20.42  ? 173 THR D CA  1 
ATOM   11393 C C   . THR D 1 144 ? 27.688  66.965  -18.770 1.00 21.69  ? 173 THR D C   1 
ATOM   11394 O O   . THR D 1 144 ? 28.663  66.447  -19.313 1.00 21.59  ? 173 THR D O   1 
ATOM   11395 C CB  . THR D 1 144 ? 25.453  65.799  -18.394 1.00 21.90  ? 173 THR D CB  1 
ATOM   11396 O OG1 . THR D 1 144 ? 24.851  64.858  -17.517 1.00 24.73  ? 173 THR D OG1 1 
ATOM   11397 C CG2 . THR D 1 144 ? 25.502  65.228  -19.789 1.00 20.62  ? 173 THR D CG2 1 
ATOM   11398 N N   . ALA D 1 145 ? 27.383  68.273  -18.837 1.00 20.49  ? 174 ALA D N   1 
ATOM   11399 C CA  . ALA D 1 145 ? 28.038  69.190  -19.758 1.00 20.19  ? 174 ALA D CA  1 
ATOM   11400 C C   . ALA D 1 145 ? 29.530  69.326  -19.445 1.00 19.81  ? 174 ALA D C   1 
ATOM   11401 O O   . ALA D 1 145 ? 30.325  69.671  -20.327 1.00 20.78  ? 174 ALA D O   1 
ATOM   11402 C CB  . ALA D 1 145 ? 27.384  70.541  -19.632 1.00 19.79  ? 174 ALA D CB  1 
ATOM   11403 N N   . LEU D 1 146 ? 29.889  69.160  -18.155 1.00 18.18  ? 175 LEU D N   1 
ATOM   11404 C CA  . LEU D 1 146 ? 31.271  69.276  -17.690 1.00 19.04  ? 175 LEU D CA  1 
ATOM   11405 C C   . LEU D 1 146 ? 32.152  68.140  -18.205 1.00 21.78  ? 175 LEU D C   1 
ATOM   11406 O O   . LEU D 1 146 ? 33.374  68.240  -18.122 1.00 23.98  ? 175 LEU D O   1 
ATOM   11407 C CB  . LEU D 1 146 ? 31.287  69.326  -16.155 1.00 21.00  ? 175 LEU D CB  1 
ATOM   11408 C CG  . LEU D 1 146 ? 31.008  70.694  -15.554 1.00 21.37  ? 175 LEU D CG  1 
ATOM   11409 C CD1 . LEU D 1 146 ? 30.954  70.662  -14.035 1.00 20.69  ? 175 LEU D CD1 1 
ATOM   11410 C CD2 . LEU D 1 146 ? 32.101  71.659  -15.981 1.00 22.07  ? 175 LEU D CD2 1 
ATOM   11411 N N   . ASN D 1 147 ? 31.555  67.056  -18.722 1.00 23.58  ? 176 ASN D N   1 
ATOM   11412 C CA  . ASN D 1 147 ? 32.351  65.912  -19.156 1.00 23.48  ? 176 ASN D CA  1 
ATOM   11413 C C   . ASN D 1 147 ? 33.181  66.247  -20.406 1.00 25.21  ? 176 ASN D C   1 
ATOM   11414 O O   . ASN D 1 147 ? 34.094  65.511  -20.761 1.00 26.31  ? 176 ASN D O   1 
ATOM   11415 C CB  . ASN D 1 147 ? 31.485  64.657  -19.336 1.00 23.64  ? 176 ASN D CB  1 
ATOM   11416 C CG  . ASN D 1 147 ? 31.292  64.287  -20.786 1.00 22.49  ? 176 ASN D CG  1 
ATOM   11417 O OD1 . ASN D 1 147 ? 30.937  65.129  -21.588 1.00 23.23  ? 176 ASN D OD1 1 
ATOM   11418 N ND2 . ASN D 1 147 ? 31.548  63.037  -21.138 1.00 23.35  ? 176 ASN D ND2 1 
ATOM   11419 N N   . SER D 1 148 ? 32.953  67.400  -21.041 1.00 26.57  ? 177 SER D N   1 
ATOM   11420 C CA  . SER D 1 148 ? 33.919  67.910  -22.005 1.00 26.83  ? 177 SER D CA  1 
ATOM   11421 C C   . SER D 1 148 ? 35.311  68.101  -21.368 1.00 28.45  ? 177 SER D C   1 
ATOM   11422 O O   . SER D 1 148 ? 36.324  68.068  -22.063 1.00 30.28  ? 177 SER D O   1 
ATOM   11423 C CB  . SER D 1 148 ? 33.395  69.183  -22.641 1.00 26.33  ? 177 SER D CB  1 
ATOM   11424 O OG  . SER D 1 148 ? 33.238  70.198  -21.668 1.00 29.37  ? 177 SER D OG  1 
ATOM   11425 N N   . GLU D 1 149 ? 35.367  68.256  -20.038 1.00 30.83  ? 178 GLU D N   1 
ATOM   11426 C CA  . GLU D 1 149 ? 36.605  68.514  -19.317 1.00 32.32  ? 178 GLU D CA  1 
ATOM   11427 C C   . GLU D 1 149 ? 37.244  67.212  -18.830 1.00 29.53  ? 178 GLU D C   1 
ATOM   11428 O O   . GLU D 1 149 ? 38.307  67.233  -18.213 1.00 31.68  ? 178 GLU D O   1 
ATOM   11429 C CB  . GLU D 1 149 ? 36.334  69.408  -18.104 1.00 35.75  ? 178 GLU D CB  1 
ATOM   11430 C CG  . GLU D 1 149 ? 35.481  70.628  -18.411 1.00 43.58  ? 178 GLU D CG  1 
ATOM   11431 C CD  . GLU D 1 149 ? 36.140  71.658  -19.313 1.00 47.25  ? 178 GLU D CD  1 
ATOM   11432 O OE1 . GLU D 1 149 ? 37.105  72.284  -18.853 1.00 51.57  ? 178 GLU D OE1 1 
ATOM   11433 O OE2 . GLU D 1 149 ? 35.681  71.844  -20.464 1.00 50.72  ? 178 GLU D OE2 1 
ATOM   11434 N N   . SER D 1 150 ? 36.618  66.074  -19.121 1.00 25.50  ? 179 SER D N   1 
ATOM   11435 C CA  . SER D 1 150 ? 37.045  64.801  -18.571 1.00 23.32  ? 179 SER D CA  1 
ATOM   11436 C C   . SER D 1 150 ? 38.365  64.322  -19.184 1.00 23.52  ? 179 SER D C   1 
ATOM   11437 O O   . SER D 1 150 ? 38.486  64.199  -20.407 1.00 25.55  ? 179 SER D O   1 
ATOM   11438 C CB  . SER D 1 150 ? 35.967  63.787  -18.740 1.00 21.74  ? 179 SER D CB  1 
ATOM   11439 O OG  . SER D 1 150 ? 36.461  62.496  -18.429 1.00 21.87  ? 179 SER D OG  1 
ATOM   11440 N N   . ASN D 1 151 ? 39.313  64.005  -18.289 1.00 25.43  ? 180 ASN D N   1 
ATOM   11441 C CA  . ASN D 1 151 ? 40.624  63.470  -18.614 1.00 26.36  ? 180 ASN D CA  1 
ATOM   11442 C C   . ASN D 1 151 ? 40.476  61.981  -18.872 1.00 24.47  ? 180 ASN D C   1 
ATOM   11443 O O   . ASN D 1 151 ? 41.161  61.433  -19.721 1.00 22.94  ? 180 ASN D O   1 
ATOM   11444 C CB  . ASN D 1 151 ? 41.644  63.701  -17.486 1.00 31.64  ? 180 ASN D CB  1 
ATOM   11445 C CG  . ASN D 1 151 ? 41.926  65.165  -17.197 1.00 34.96  ? 180 ASN D CG  1 
ATOM   11446 O OD1 . ASN D 1 151 ? 42.471  65.874  -18.041 1.00 36.06  ? 180 ASN D OD1 1 
ATOM   11447 N ND2 . ASN D 1 151 ? 41.571  65.627  -16.006 1.00 37.37  ? 180 ASN D ND2 1 
ATOM   11448 N N   . PHE D 1 152 ? 39.569  61.326  -18.149 1.00 23.51  ? 181 PHE D N   1 
ATOM   11449 C CA  . PHE D 1 152 ? 39.353  59.908  -18.370 1.00 23.86  ? 181 PHE D CA  1 
ATOM   11450 C C   . PHE D 1 152 ? 38.814  59.665  -19.776 1.00 25.40  ? 181 PHE D C   1 
ATOM   11451 O O   . PHE D 1 152 ? 39.337  58.799  -20.479 1.00 25.45  ? 181 PHE D O   1 
ATOM   11452 C CB  . PHE D 1 152 ? 38.406  59.310  -17.334 1.00 24.81  ? 181 PHE D CB  1 
ATOM   11453 C CG  . PHE D 1 152 ? 38.236  57.819  -17.436 1.00 25.01  ? 181 PHE D CG  1 
ATOM   11454 C CD1 . PHE D 1 152 ? 39.195  56.971  -16.915 1.00 26.71  ? 181 PHE D CD1 1 
ATOM   11455 C CD2 . PHE D 1 152 ? 37.133  57.267  -18.058 1.00 23.89  ? 181 PHE D CD2 1 
ATOM   11456 C CE1 . PHE D 1 152 ? 39.055  55.599  -17.022 1.00 28.00  ? 181 PHE D CE1 1 
ATOM   11457 C CE2 . PHE D 1 152 ? 36.991  55.891  -18.144 1.00 26.55  ? 181 PHE D CE2 1 
ATOM   11458 C CZ  . PHE D 1 152 ? 37.938  55.064  -17.605 1.00 26.51  ? 181 PHE D CZ  1 
ATOM   11459 N N   . ALA D 1 153 ? 37.779  60.419  -20.194 1.00 24.81  ? 182 ALA D N   1 
ATOM   11460 C CA  . ALA D 1 153 ? 37.183  60.140  -21.496 1.00 29.73  ? 182 ALA D CA  1 
ATOM   11461 C C   . ALA D 1 153 ? 38.216  60.332  -22.606 1.00 30.82  ? 182 ALA D C   1 
ATOM   11462 O O   . ALA D 1 153 ? 38.363  59.506  -23.497 1.00 28.87  ? 182 ALA D O   1 
ATOM   11463 C CB  . ALA D 1 153 ? 35.983  61.013  -21.730 1.00 29.96  ? 182 ALA D CB  1 
ATOM   11464 N N   . ARG D 1 154 ? 38.970  61.423  -22.533 1.00 31.28  ? 183 ARG D N   1 
ATOM   11465 C CA  . ARG D 1 154 ? 39.949  61.709  -23.564 1.00 34.94  ? 183 ARG D CA  1 
ATOM   11466 C C   . ARG D 1 154 ? 41.038  60.628  -23.575 1.00 35.13  ? 183 ARG D C   1 
ATOM   11467 O O   . ARG D 1 154 ? 41.423  60.132  -24.634 1.00 34.27  ? 183 ARG D O   1 
ATOM   11468 C CB  . ARG D 1 154 ? 40.455  63.131  -23.326 1.00 38.13  ? 183 ARG D CB  1 
ATOM   11469 C CG  . ARG D 1 154 ? 41.693  63.509  -24.125 1.00 40.01  ? 183 ARG D CG  1 
ATOM   11470 C CD  . ARG D 1 154 ? 41.580  64.907  -24.692 1.00 43.13  ? 183 ARG D CD  1 
ATOM   11471 N NE  . ARG D 1 154 ? 40.820  65.812  -23.838 1.00 49.84  ? 183 ARG D NE  1 
ATOM   11472 C CZ  . ARG D 1 154 ? 40.507  67.061  -24.156 1.00 51.96  ? 183 ARG D CZ  1 
ATOM   11473 N NH1 . ARG D 1 154 ? 39.609  67.711  -23.437 1.00 56.24  ? 183 ARG D NH1 1 
ATOM   11474 N NH2 . ARG D 1 154 ? 41.049  67.631  -25.221 1.00 52.40  ? 183 ARG D NH2 1 
ATOM   11475 N N   . ALA D 1 155 ? 41.513  60.236  -22.383 1.00 35.78  ? 184 ALA D N   1 
ATOM   11476 C CA  . ALA D 1 155 ? 42.592  59.269  -22.252 1.00 34.43  ? 184 ALA D CA  1 
ATOM   11477 C C   . ALA D 1 155 ? 42.152  57.880  -22.709 1.00 34.90  ? 184 ALA D C   1 
ATOM   11478 O O   . ALA D 1 155 ? 42.979  57.087  -23.167 1.00 37.82  ? 184 ALA D O   1 
ATOM   11479 C CB  . ALA D 1 155 ? 43.071  59.231  -20.830 1.00 34.43  ? 184 ALA D CB  1 
ATOM   11480 N N   . TYR D 1 156 ? 40.858  57.582  -22.559 1.00 35.15  ? 185 TYR D N   1 
ATOM   11481 C CA  . TYR D 1 156 ? 40.307  56.319  -23.028 1.00 33.52  ? 185 TYR D CA  1 
ATOM   11482 C C   . TYR D 1 156 ? 40.361  56.257  -24.550 1.00 33.68  ? 185 TYR D C   1 
ATOM   11483 O O   . TYR D 1 156 ? 40.657  55.208  -25.115 1.00 33.36  ? 185 TYR D O   1 
ATOM   11484 C CB  . TYR D 1 156 ? 38.843  56.129  -22.614 1.00 32.44  ? 185 TYR D CB  1 
ATOM   11485 C CG  . TYR D 1 156 ? 38.346  54.730  -22.880 1.00 32.58  ? 185 TYR D CG  1 
ATOM   11486 C CD1 . TYR D 1 156 ? 38.472  53.732  -21.927 1.00 32.66  ? 185 TYR D CD1 1 
ATOM   11487 C CD2 . TYR D 1 156 ? 37.873  54.368  -24.131 1.00 31.01  ? 185 TYR D CD2 1 
ATOM   11488 C CE1 . TYR D 1 156 ? 38.075  52.429  -22.186 1.00 31.68  ? 185 TYR D CE1 1 
ATOM   11489 C CE2 . TYR D 1 156 ? 37.488  53.065  -24.407 1.00 30.18  ? 185 TYR D CE2 1 
ATOM   11490 C CZ  . TYR D 1 156 ? 37.578  52.094  -23.431 1.00 32.41  ? 185 TYR D CZ  1 
ATOM   11491 O OH  . TYR D 1 156 ? 37.170  50.806  -23.714 1.00 37.25  ? 185 TYR D OH  1 
ATOM   11492 N N   . ALA D 1 157 ? 40.053  57.383  -25.203 1.00 34.84  ? 186 ALA D N   1 
ATOM   11493 C CA  . ALA D 1 157 ? 40.025  57.452  -26.657 1.00 35.01  ? 186 ALA D CA  1 
ATOM   11494 C C   . ALA D 1 157 ? 41.418  57.259  -27.258 1.00 34.82  ? 186 ALA D C   1 
ATOM   11495 O O   . ALA D 1 157 ? 41.534  56.889  -28.427 1.00 33.48  ? 186 ALA D O   1 
ATOM   11496 C CB  . ALA D 1 157 ? 39.447  58.769  -27.098 1.00 36.25  ? 186 ALA D CB  1 
ATOM   11497 N N   . GLN D 1 158 ? 42.463  57.545  -26.473 1.00 35.91  ? 187 GLN D N   1 
ATOM   11498 C CA  . GLN D 1 158 ? 43.832  57.410  -26.943 1.00 34.37  ? 187 GLN D CA  1 
ATOM   11499 C C   . GLN D 1 158 ? 44.439  56.085  -26.493 1.00 31.45  ? 187 GLN D C   1 
ATOM   11500 O O   . GLN D 1 158 ? 45.636  55.880  -26.647 1.00 36.53  ? 187 GLN D O   1 
ATOM   11501 C CB  . GLN D 1 158 ? 44.653  58.613  -26.480 1.00 35.80  ? 187 GLN D CB  1 
ATOM   11502 C CG  . GLN D 1 158 ? 44.141  59.928  -27.050 1.00 36.19  ? 187 GLN D CG  1 
ATOM   11503 C CD  . GLN D 1 158 ? 44.615  61.093  -26.223 1.00 39.01  ? 187 GLN D CD  1 
ATOM   11504 O OE1 . GLN D 1 158 ? 44.573  61.053  -24.996 1.00 41.33  ? 187 GLN D OE1 1 
ATOM   11505 N NE2 . GLN D 1 158 ? 45.091  62.138  -26.879 1.00 44.67  ? 187 GLN D NE2 1 
ATOM   11506 N N   . GLY D 1 159 ? 43.616  55.181  -25.956 1.00 29.39  ? 188 GLY D N   1 
ATOM   11507 C CA  . GLY D 1 159 ? 44.006  53.801  -25.718 1.00 29.04  ? 188 GLY D CA  1 
ATOM   11508 C C   . GLY D 1 159 ? 44.830  53.590  -24.448 1.00 31.12  ? 188 GLY D C   1 
ATOM   11509 O O   . GLY D 1 159 ? 45.561  52.603  -24.359 1.00 33.15  ? 188 GLY D O   1 
ATOM   11510 N N   . ILE D 1 160 ? 44.680  54.490  -23.465 1.00 32.16  ? 189 ILE D N   1 
ATOM   11511 C CA  . ILE D 1 160 ? 45.382  54.423  -22.177 1.00 29.80  ? 189 ILE D CA  1 
ATOM   11512 C C   . ILE D 1 160 ? 45.234  53.048  -21.509 1.00 25.35  ? 189 ILE D C   1 
ATOM   11513 O O   . ILE D 1 160 ? 44.191  52.412  -21.579 1.00 27.47  ? 189 ILE D O   1 
ATOM   11514 C CB  . ILE D 1 160 ? 44.892  55.550  -21.247 1.00 37.32  ? 189 ILE D CB  1 
ATOM   11515 C CG1 . ILE D 1 160 ? 45.872  55.822  -20.104 1.00 42.40  ? 189 ILE D CG1 1 
ATOM   11516 C CG2 . ILE D 1 160 ? 43.477  55.288  -20.750 1.00 38.92  ? 189 ILE D CG2 1 
ATOM   11517 C CD1 . ILE D 1 160 ? 47.016  56.720  -20.502 1.00 41.91  ? 189 ILE D CD1 1 
ATOM   11518 N N   . SER D 1 161 ? 46.299  52.591  -20.835 1.00 24.48  ? 190 SER D N   1 
ATOM   11519 C CA  . SER D 1 161 ? 46.314  51.286  -20.177 1.00 21.77  ? 190 SER D CA  1 
ATOM   11520 C C   . SER D 1 161 ? 45.321  51.259  -19.013 1.00 22.04  ? 190 SER D C   1 
ATOM   11521 O O   . SER D 1 161 ? 45.162  52.243  -18.311 1.00 23.35  ? 190 SER D O   1 
ATOM   11522 C CB  . SER D 1 161 ? 47.717  50.972  -19.698 1.00 24.35  ? 190 SER D CB  1 
ATOM   11523 O OG  . SER D 1 161 ? 47.720  50.109  -18.565 1.00 20.88  ? 190 SER D OG  1 
ATOM   11524 N N   . ARG D 1 162 ? 44.677  50.114  -18.793 1.00 23.52  ? 191 ARG D N   1 
ATOM   11525 C CA  . ARG D 1 162 ? 43.740  49.906  -17.697 1.00 29.68  ? 191 ARG D CA  1 
ATOM   11526 C C   . ARG D 1 162 ? 44.395  50.189  -16.345 1.00 26.38  ? 191 ARG D C   1 
ATOM   11527 O O   . ARG D 1 162 ? 43.724  50.606  -15.402 1.00 25.33  ? 191 ARG D O   1 
ATOM   11528 C CB  . ARG D 1 162 ? 43.236  48.454  -17.699 1.00 34.01  ? 191 ARG D CB  1 
ATOM   11529 C CG  . ARG D 1 162 ? 42.057  48.193  -18.627 1.00 38.27  ? 191 ARG D CG  1 
ATOM   11530 C CD  . ARG D 1 162 ? 41.379  46.841  -18.430 1.00 40.32  ? 191 ARG D CD  1 
ATOM   11531 N NE  . ARG D 1 162 ? 40.677  46.695  -17.154 1.00 46.11  ? 191 ARG D NE  1 
ATOM   11532 C CZ  . ARG D 1 162 ? 40.708  45.613  -16.361 1.00 49.74  ? 191 ARG D CZ  1 
ATOM   11533 N NH1 . ARG D 1 162 ? 41.584  44.644  -16.572 1.00 50.50  ? 191 ARG D NH1 1 
ATOM   11534 N NH2 . ARG D 1 162 ? 39.867  45.507  -15.342 1.00 49.34  ? 191 ARG D NH2 1 
ATOM   11535 N N   . THR D 1 163 ? 45.713  49.947  -16.247 1.00 25.14  ? 192 THR D N   1 
ATOM   11536 C CA  . THR D 1 163 ? 46.446  50.198  -15.020 1.00 27.11  ? 192 THR D CA  1 
ATOM   11537 C C   . THR D 1 163 ? 46.375  51.676  -14.647 1.00 27.17  ? 192 THR D C   1 
ATOM   11538 O O   . THR D 1 163 ? 46.649  52.022  -13.505 1.00 29.55  ? 192 THR D O   1 
ATOM   11539 C CB  . THR D 1 163 ? 47.904  49.741  -15.140 1.00 27.76  ? 192 THR D CB  1 
ATOM   11540 O OG1 . THR D 1 163 ? 48.538  50.586  -16.099 1.00 27.73  ? 192 THR D OG1 1 
ATOM   11541 C CG2 . THR D 1 163 ? 48.007  48.282  -15.544 1.00 27.17  ? 192 THR D CG2 1 
ATOM   11542 N N   . LYS D 1 164 ? 46.004  52.530  -15.606 1.00 30.78  ? 193 LYS D N   1 
ATOM   11543 C CA  . LYS D 1 164 ? 46.013  53.968  -15.407 1.00 31.24  ? 193 LYS D CA  1 
ATOM   11544 C C   . LYS D 1 164 ? 44.623  54.521  -15.097 1.00 27.36  ? 193 LYS D C   1 
ATOM   11545 O O   . LYS D 1 164 ? 44.513  55.712  -14.817 1.00 26.57  ? 193 LYS D O   1 
ATOM   11546 C CB  . LYS D 1 164 ? 46.499  54.696  -16.662 1.00 34.52  ? 193 LYS D CB  1 
ATOM   11547 C CG  . LYS D 1 164 ? 47.753  54.123  -17.300 1.00 44.31  ? 193 LYS D CG  1 
ATOM   11548 C CD  . LYS D 1 164 ? 49.016  54.810  -16.865 1.00 46.66  ? 193 LYS D CD  1 
ATOM   11549 C CE  . LYS D 1 164 ? 49.325  54.679  -15.390 1.00 49.25  ? 193 LYS D CE  1 
ATOM   11550 N NZ  . LYS D 1 164 ? 49.980  55.910  -14.889 1.00 51.55  ? 193 LYS D NZ  1 
ATOM   11551 N N   . TYR D 1 165 ? 43.588  53.689  -15.228 1.00 25.10  ? 194 TYR D N   1 
ATOM   11552 C CA  . TYR D 1 165 ? 42.215  54.146  -15.090 1.00 22.41  ? 194 TYR D CA  1 
ATOM   11553 C C   . TYR D 1 165 ? 42.035  54.899  -13.777 1.00 22.71  ? 194 TYR D C   1 
ATOM   11554 O O   . TYR D 1 165 ? 41.472  55.989  -13.775 1.00 23.75  ? 194 TYR D O   1 
ATOM   11555 C CB  . TYR D 1 165 ? 41.227  52.986  -15.214 1.00 22.54  ? 194 TYR D CB  1 
ATOM   11556 C CG  . TYR D 1 165 ? 40.981  52.502  -16.628 1.00 21.26  ? 194 TYR D CG  1 
ATOM   11557 C CD1 . TYR D 1 165 ? 41.554  53.140  -17.711 1.00 22.50  ? 194 TYR D CD1 1 
ATOM   11558 C CD2 . TYR D 1 165 ? 40.236  51.364  -16.889 1.00 20.63  ? 194 TYR D CD2 1 
ATOM   11559 C CE1 . TYR D 1 165 ? 41.364  52.712  -19.014 1.00 21.76  ? 194 TYR D CE1 1 
ATOM   11560 C CE2 . TYR D 1 165 ? 40.033  50.914  -18.192 1.00 22.40  ? 194 TYR D CE2 1 
ATOM   11561 C CZ  . TYR D 1 165 ? 40.583  51.599  -19.263 1.00 22.45  ? 194 TYR D CZ  1 
ATOM   11562 O OH  . TYR D 1 165 ? 40.410  51.262  -20.607 1.00 21.86  ? 194 TYR D OH  1 
ATOM   11563 N N   . TRP D 1 166 ? 42.523  54.353  -12.669 1.00 22.58  ? 195 TRP D N   1 
ATOM   11564 C CA  . TRP D 1 166 ? 42.235  54.945  -11.377 1.00 19.41  ? 195 TRP D CA  1 
ATOM   11565 C C   . TRP D 1 166 ? 42.779  56.363  -11.281 1.00 22.17  ? 195 TRP D C   1 
ATOM   11566 O O   . TRP D 1 166 ? 42.129  57.206  -10.680 1.00 22.55  ? 195 TRP D O   1 
ATOM   11567 C CB  . TRP D 1 166 ? 42.698  54.042  -10.243 1.00 23.38  ? 195 TRP D CB  1 
ATOM   11568 C CG  . TRP D 1 166 ? 44.169  53.973  -9.979  1.00 22.14  ? 195 TRP D CG  1 
ATOM   11569 C CD1 . TRP D 1 166 ? 45.007  52.937  -10.270 1.00 26.62  ? 195 TRP D CD1 1 
ATOM   11570 C CD2 . TRP D 1 166 ? 44.954  54.935  -9.252  1.00 22.09  ? 195 TRP D CD2 1 
ATOM   11571 N NE1 . TRP D 1 166 ? 46.273  53.208  -9.821  1.00 27.66  ? 195 TRP D NE1 1 
ATOM   11572 C CE2 . TRP D 1 166 ? 46.271  54.429  -9.186  1.00 24.24  ? 195 TRP D CE2 1 
ATOM   11573 C CE3 . TRP D 1 166 ? 44.680  56.186  -8.689  1.00 22.02  ? 195 TRP D CE3 1 
ATOM   11574 C CZ2 . TRP D 1 166 ? 47.294  55.117  -8.541  1.00 25.52  ? 195 TRP D CZ2 1 
ATOM   11575 C CZ3 . TRP D 1 166 ? 45.694  56.872  -8.065  1.00 23.91  ? 195 TRP D CZ3 1 
ATOM   11576 C CH2 . TRP D 1 166 ? 46.996  56.357  -8.019  1.00 24.79  ? 195 TRP D CH2 1 
ATOM   11577 N N   . GLU D 1 167 ? 43.959  56.596  -11.881 1.00 21.76  ? 196 GLU D N   1 
ATOM   11578 C CA  . GLU D 1 167 ? 44.627  57.889  -11.842 1.00 25.77  ? 196 GLU D CA  1 
ATOM   11579 C C   . GLU D 1 167 ? 43.789  58.945  -12.550 1.00 26.56  ? 196 GLU D C   1 
ATOM   11580 O O   . GLU D 1 167 ? 43.692  60.080  -12.091 1.00 25.67  ? 196 GLU D O   1 
ATOM   11581 C CB  . GLU D 1 167 ? 45.995  57.802  -12.521 1.00 27.33  ? 196 GLU D CB  1 
ATOM   11582 C CG  . GLU D 1 167 ? 46.894  56.778  -11.871 1.00 28.78  ? 196 GLU D CG  1 
ATOM   11583 C CD  . GLU D 1 167 ? 48.342  56.867  -12.298 1.00 34.27  ? 196 GLU D CD  1 
ATOM   11584 O OE1 . GLU D 1 167 ? 48.881  57.996  -12.332 1.00 38.51  ? 196 GLU D OE1 1 
ATOM   11585 O OE2 . GLU D 1 167 ? 48.936  55.808  -12.535 1.00 38.98  ? 196 GLU D OE2 1 
ATOM   11586 N N   . LEU D 1 168 ? 43.205  58.577  -13.694 1.00 26.94  ? 197 LEU D N   1 
ATOM   11587 C CA  . LEU D 1 168 ? 42.420  59.542  -14.453 1.00 27.75  ? 197 LEU D CA  1 
ATOM   11588 C C   . LEU D 1 168 ? 41.075  59.768  -13.753 1.00 22.91  ? 197 LEU D C   1 
ATOM   11589 O O   . LEU D 1 168 ? 40.593  60.896  -13.682 1.00 21.77  ? 197 LEU D O   1 
ATOM   11590 C CB  . LEU D 1 168 ? 42.260  59.040  -15.893 1.00 28.67  ? 197 LEU D CB  1 
ATOM   11591 C CG  . LEU D 1 168 ? 43.536  59.020  -16.731 1.00 30.99  ? 197 LEU D CG  1 
ATOM   11592 C CD1 . LEU D 1 168 ? 43.429  57.998  -17.857 1.00 33.71  ? 197 LEU D CD1 1 
ATOM   11593 C CD2 . LEU D 1 168 ? 43.850  60.384  -17.307 1.00 30.07  ? 197 LEU D CD2 1 
ATOM   11594 N N   . ILE D 1 169 ? 40.517  58.716  -13.163 1.00 21.40  ? 198 ILE D N   1 
ATOM   11595 C CA  . ILE D 1 169 ? 39.301  58.835  -12.372 1.00 21.48  ? 198 ILE D CA  1 
ATOM   11596 C C   . ILE D 1 169 ? 39.544  59.742  -11.162 1.00 22.26  ? 198 ILE D C   1 
ATOM   11597 O O   . ILE D 1 169 ? 38.690  60.567  -10.825 1.00 21.30  ? 198 ILE D O   1 
ATOM   11598 C CB  . ILE D 1 169 ? 38.806  57.439  -11.947 1.00 23.15  ? 198 ILE D CB  1 
ATOM   11599 C CG1 . ILE D 1 169 ? 38.389  56.610  -13.159 1.00 25.51  ? 198 ILE D CG1 1 
ATOM   11600 C CG2 . ILE D 1 169 ? 37.699  57.526  -10.907 1.00 21.65  ? 198 ILE D CG2 1 
ATOM   11601 C CD1 . ILE D 1 169 ? 37.090  57.044  -13.790 1.00 23.75  ? 198 ILE D CD1 1 
ATOM   11602 N N   . TYR D 1 170 ? 40.728  59.610  -10.544 1.00 21.19  ? 199 TYR D N   1 
ATOM   11603 C CA  . TYR D 1 170 ? 41.095  60.414  -9.381  1.00 21.28  ? 199 TYR D CA  1 
ATOM   11604 C C   . TYR D 1 170 ? 41.127  61.887  -9.783  1.00 19.99  ? 199 TYR D C   1 
ATOM   11605 O O   . TYR D 1 170 ? 40.504  62.711  -9.135  1.00 20.11  ? 199 TYR D O   1 
ATOM   11606 C CB  . TYR D 1 170 ? 42.441  59.960  -8.782  1.00 21.86  ? 199 TYR D CB  1 
ATOM   11607 C CG  . TYR D 1 170 ? 43.073  60.941  -7.812  1.00 20.54  ? 199 TYR D CG  1 
ATOM   11608 C CD1 . TYR D 1 170 ? 42.768  60.960  -6.451  1.00 21.57  ? 199 TYR D CD1 1 
ATOM   11609 C CD2 . TYR D 1 170 ? 43.968  61.881  -8.277  1.00 21.12  ? 199 TYR D CD2 1 
ATOM   11610 C CE1 . TYR D 1 170 ? 43.328  61.896  -5.593  1.00 20.67  ? 199 TYR D CE1 1 
ATOM   11611 C CE2 . TYR D 1 170 ? 44.539  62.819  -7.442  1.00 20.55  ? 199 TYR D CE2 1 
ATOM   11612 C CZ  . TYR D 1 170 ? 44.235  62.813  -6.094  1.00 20.99  ? 199 TYR D CZ  1 
ATOM   11613 O OH  . TYR D 1 170 ? 44.838  63.778  -5.374  1.00 22.48  ? 199 TYR D OH  1 
ATOM   11614 N N   . GLU D 1 171 ? 41.795  62.205  -10.892 1.00 19.82  ? 200 GLU D N   1 
ATOM   11615 C CA  . GLU D 1 171 ? 41.914  63.597  -11.298 1.00 21.12  ? 200 GLU D CA  1 
ATOM   11616 C C   . GLU D 1 171 ? 40.539  64.159  -11.652 1.00 21.37  ? 200 GLU D C   1 
ATOM   11617 O O   . GLU D 1 171 ? 40.231  65.290  -11.269 1.00 21.44  ? 200 GLU D O   1 
ATOM   11618 C CB  . GLU D 1 171 ? 42.863  63.781  -12.484 1.00 23.77  ? 200 GLU D CB  1 
ATOM   11619 C CG  . GLU D 1 171 ? 44.274  63.339  -12.181 1.00 25.10  ? 200 GLU D CG  1 
ATOM   11620 C CD  . GLU D 1 171 ? 45.015  64.173  -11.150 1.00 26.36  ? 200 GLU D CD  1 
ATOM   11621 O OE1 . GLU D 1 171 ? 44.559  65.287  -10.849 1.00 26.54  ? 200 GLU D OE1 1 
ATOM   11622 O OE2 . GLU D 1 171 ? 46.083  63.724  -10.692 1.00 25.74  ? 200 GLU D OE2 1 
ATOM   11623 N N   . ASP D 1 172 ? 39.730  63.414  -12.419 1.00 21.68  ? 201 ASP D N   1 
ATOM   11624 C CA  . ASP D 1 172 ? 38.411  63.919  -12.803 1.00 22.52  ? 201 ASP D CA  1 
ATOM   11625 C C   . ASP D 1 172 ? 37.547  64.133  -11.562 1.00 23.72  ? 201 ASP D C   1 
ATOM   11626 O O   . ASP D 1 172 ? 36.768  65.093  -11.516 1.00 21.27  ? 201 ASP D O   1 
ATOM   11627 C CB  . ASP D 1 172 ? 37.702  62.997  -13.800 1.00 24.10  ? 201 ASP D CB  1 
ATOM   11628 C CG  . ASP D 1 172 ? 38.108  63.166  -15.262 1.00 25.63  ? 201 ASP D CG  1 
ATOM   11629 O OD1 . ASP D 1 172 ? 38.753  64.176  -15.591 1.00 26.77  ? 201 ASP D OD1 1 
ATOM   11630 O OD2 . ASP D 1 172 ? 37.791  62.267  -16.069 1.00 21.40  ? 201 ASP D OD2 1 
ATOM   11631 N N   . SER D 1 173 ? 37.663  63.218  -10.586 1.00 20.64  ? 202 SER D N   1 
ATOM   11632 C CA  . SER D 1 173 ? 36.838  63.227  -9.379  1.00 21.39  ? 202 SER D CA  1 
ATOM   11633 C C   . SER D 1 173 ? 37.166  64.401  -8.463  1.00 21.57  ? 202 SER D C   1 
ATOM   11634 O O   . SER D 1 173 ? 36.257  65.096  -7.964  1.00 19.20  ? 202 SER D O   1 
ATOM   11635 C CB  . SER D 1 173 ? 36.973  61.945  -8.625  1.00 23.15  ? 202 SER D CB  1 
ATOM   11636 O OG  . SER D 1 173 ? 36.454  60.883  -9.385  1.00 24.79  ? 202 SER D OG  1 
ATOM   11637 N N   . MET D 1 174 ? 38.479  64.607  -8.253  1.00 21.62  ? 203 MET D N   1 
ATOM   11638 C CA  . MET D 1 174 ? 38.982  65.784  -7.577  1.00 20.13  ? 203 MET D CA  1 
ATOM   11639 C C   . MET D 1 174 ? 38.513  67.068  -8.259  1.00 18.52  ? 203 MET D C   1 
ATOM   11640 O O   . MET D 1 174 ? 38.055  67.971  -7.560  1.00 19.85  ? 203 MET D O   1 
ATOM   11641 C CB  . MET D 1 174 ? 40.515  65.769  -7.533  1.00 19.80  ? 203 MET D CB  1 
ATOM   11642 C CG  . MET D 1 174 ? 41.065  64.649  -6.636  1.00 19.62  ? 203 MET D CG  1 
ATOM   11643 S SD  . MET D 1 174 ? 40.928  64.980  -4.863  1.00 21.78  ? 203 MET D SD  1 
ATOM   11644 C CE  . MET D 1 174 ? 41.849  66.518  -4.821  1.00 20.99  ? 203 MET D CE  1 
ATOM   11645 N N   . ASP D 1 175 ? 38.586  67.156  -9.601  1.00 18.56  ? 204 ASP D N   1 
ATOM   11646 C CA  . ASP D 1 175 ? 38.097  68.338  -10.305 1.00 19.84  ? 204 ASP D CA  1 
ATOM   11647 C C   . ASP D 1 175 ? 36.595  68.531  -10.069 1.00 19.61  ? 204 ASP D C   1 
ATOM   11648 O O   . ASP D 1 175 ? 36.128  69.654  -9.888  1.00 20.26  ? 204 ASP D O   1 
ATOM   11649 C CB  . ASP D 1 175 ? 38.349  68.274  -11.820 1.00 21.54  ? 204 ASP D CB  1 
ATOM   11650 C CG  . ASP D 1 175 ? 39.805  68.486  -12.214 1.00 25.32  ? 204 ASP D CG  1 
ATOM   11651 O OD1 . ASP D 1 175 ? 40.579  68.952  -11.360 1.00 27.16  ? 204 ASP D OD1 1 
ATOM   11652 O OD2 . ASP D 1 175 ? 40.171  68.130  -13.368 1.00 30.69  ? 204 ASP D OD2 1 
ATOM   11653 N N   . LEU D 1 176 ? 35.830  67.445  -10.119 1.00 16.83  ? 205 LEU D N   1 
ATOM   11654 C CA  . LEU D 1 176 ? 34.374  67.562  -10.027 1.00 16.27  ? 205 LEU D CA  1 
ATOM   11655 C C   . LEU D 1 176 ? 33.971  68.013  -8.613  1.00 17.51  ? 205 LEU D C   1 
ATOM   11656 O O   . LEU D 1 176 ? 33.271  69.016  -8.445  1.00 18.22  ? 205 LEU D O   1 
ATOM   11657 C CB  . LEU D 1 176 ? 33.762  66.209  -10.380 1.00 15.56  ? 205 LEU D CB  1 
ATOM   11658 C CG  . LEU D 1 176 ? 32.246  66.062  -10.239 1.00 15.80  ? 205 LEU D CG  1 
ATOM   11659 C CD1 . LEU D 1 176 ? 31.480  67.209  -10.841 1.00 18.33  ? 205 LEU D CD1 1 
ATOM   11660 C CD2 . LEU D 1 176 ? 31.787  64.772  -10.866 1.00 16.45  ? 205 LEU D CD2 1 
ATOM   11661 N N   . ILE D 1 177 ? 34.496  67.344  -7.586  1.00 19.48  ? 206 ILE D N   1 
ATOM   11662 C CA  . ILE D 1 177 ? 34.216  67.708  -6.204  1.00 19.78  ? 206 ILE D CA  1 
ATOM   11663 C C   . ILE D 1 177 ? 34.491  69.197  -6.038  1.00 20.62  ? 206 ILE D C   1 
ATOM   11664 O O   . ILE D 1 177 ? 33.666  69.915  -5.504  1.00 22.03  ? 206 ILE D O   1 
ATOM   11665 C CB  . ILE D 1 177 ? 34.999  66.821  -5.212  1.00 23.00  ? 206 ILE D CB  1 
ATOM   11666 C CG1 . ILE D 1 177 ? 34.389  65.421  -5.175  1.00 23.24  ? 206 ILE D CG1 1 
ATOM   11667 C CG2 . ILE D 1 177 ? 35.038  67.435  -3.811  1.00 25.00  ? 206 ILE D CG2 1 
ATOM   11668 C CD1 . ILE D 1 177 ? 35.291  64.388  -4.531  1.00 25.17  ? 206 ILE D CD1 1 
ATOM   11669 N N   . ALA D 1 178 ? 35.647  69.642  -6.533  1.00 21.66  ? 207 ALA D N   1 
ATOM   11670 C CA  . ALA D 1 178 ? 36.037  71.050  -6.467  1.00 22.46  ? 207 ALA D CA  1 
ATOM   11671 C C   . ALA D 1 178 ? 34.998  71.960  -7.109  1.00 25.08  ? 207 ALA D C   1 
ATOM   11672 O O   . ALA D 1 178 ? 34.737  73.033  -6.587  1.00 22.45  ? 207 ALA D O   1 
ATOM   11673 C CB  . ALA D 1 178 ? 37.364  71.246  -7.136  1.00 22.32  ? 207 ALA D CB  1 
ATOM   11674 N N   . LYS D 1 179 ? 34.437  71.556  -8.256  1.00 24.74  ? 208 LYS D N   1 
ATOM   11675 C CA  . LYS D 1 179 ? 33.615  72.456  -9.053  1.00 25.27  ? 208 LYS D CA  1 
ATOM   11676 C C   . LYS D 1 179 ? 32.172  72.476  -8.570  1.00 24.18  ? 208 LYS D C   1 
ATOM   11677 O O   . LYS D 1 179 ? 31.423  73.380  -8.927  1.00 29.30  ? 208 LYS D O   1 
ATOM   11678 C CB  . LYS D 1 179 ? 33.593  72.028  -10.520 1.00 24.87  ? 208 LYS D CB  1 
ATOM   11679 C CG  . LYS D 1 179 ? 34.904  72.206  -11.262 1.00 24.67  ? 208 LYS D CG  1 
ATOM   11680 C CD  . LYS D 1 179 ? 34.893  71.549  -12.608 1.00 27.92  ? 208 LYS D CD  1 
ATOM   11681 C CE  . LYS D 1 179 ? 36.281  71.132  -13.045 1.00 30.13  ? 208 LYS D CE  1 
ATOM   11682 N NZ  . LYS D 1 179 ? 37.211  72.289  -13.098 1.00 35.73  ? 208 LYS D NZ  1 
ATOM   11683 N N   . LEU D 1 180 ? 31.784  71.469  -7.803  1.00 24.42  ? 209 LEU D N   1 
ATOM   11684 C CA  . LEU D 1 180 ? 30.383  71.229  -7.506  1.00 22.76  ? 209 LEU D CA  1 
ATOM   11685 C C   . LEU D 1 180 ? 29.780  72.381  -6.716  1.00 23.56  ? 209 LEU D C   1 
ATOM   11686 O O   . LEU D 1 180 ? 28.646  72.745  -7.022  1.00 22.43  ? 209 LEU D O   1 
ATOM   11687 C CB  . LEU D 1 180 ? 30.243  69.886  -6.796  1.00 24.85  ? 209 LEU D CB  1 
ATOM   11688 C CG  . LEU D 1 180 ? 30.054  68.706  -7.749  1.00 21.59  ? 209 LEU D CG  1 
ATOM   11689 C CD1 . LEU D 1 180 ? 30.336  67.391  -7.065  1.00 22.65  ? 209 LEU D CD1 1 
ATOM   11690 C CD2 . LEU D 1 180 ? 28.647  68.698  -8.324  1.00 20.99  ? 209 LEU D CD2 1 
ATOM   11691 N N   . PRO D 1 181 ? 30.465  72.932  -5.671  1.00 23.56  ? 210 PRO D N   1 
ATOM   11692 C CA  . PRO D 1 181 ? 30.063  74.221  -5.085  1.00 22.03  ? 210 PRO D CA  1 
ATOM   11693 C C   . PRO D 1 181 ? 29.860  75.301  -6.148  1.00 22.63  ? 210 PRO D C   1 
ATOM   11694 O O   . PRO D 1 181 ? 28.916  76.076  -6.076  1.00 22.27  ? 210 PRO D O   1 
ATOM   11695 C CB  . PRO D 1 181 ? 31.227  74.531  -4.126  1.00 24.15  ? 210 PRO D CB  1 
ATOM   11696 C CG  . PRO D 1 181 ? 31.720  73.147  -3.692  1.00 23.42  ? 210 PRO D CG  1 
ATOM   11697 C CD  . PRO D 1 181 ? 31.592  72.320  -4.944  1.00 23.37  ? 210 PRO D CD  1 
ATOM   11698 N N   . CYS D 1 182 ? 30.752  75.387  -7.143  1.00 25.39  ? 211 CYS D N   1 
ATOM   11699 C CA  . CYS D 1 182 ? 30.616  76.447  -8.135  1.00 25.40  ? 211 CYS D CA  1 
ATOM   11700 C C   . CYS D 1 182 ? 29.308  76.263  -8.915  1.00 23.05  ? 211 CYS D C   1 
ATOM   11701 O O   . CYS D 1 182 ? 28.511  77.187  -9.022  1.00 23.59  ? 211 CYS D O   1 
ATOM   11702 C CB  . CYS D 1 182 ? 31.827  76.515  -9.043  1.00 29.57  ? 211 CYS D CB  1 
ATOM   11703 S SG  . CYS D 1 182 ? 33.300  77.191  -8.236  1.00 34.00  ? 211 CYS D SG  1 
ATOM   11704 N N   . VAL D 1 183 ? 29.011  75.028  -9.346  1.00 21.11  ? 212 VAL D N   1 
ATOM   11705 C CA  . VAL D 1 183 ? 27.747  74.760  -10.022 1.00 22.17  ? 212 VAL D CA  1 
ATOM   11706 C C   . VAL D 1 183 ? 26.550  75.000  -9.105  1.00 20.96  ? 212 VAL D C   1 
ATOM   11707 O O   . VAL D 1 183 ? 25.600  75.652  -9.515  1.00 22.97  ? 212 VAL D O   1 
ATOM   11708 C CB  . VAL D 1 183 ? 27.684  73.316  -10.546 1.00 20.89  ? 212 VAL D CB  1 
ATOM   11709 C CG1 . VAL D 1 183 ? 26.270  72.972  -10.983 1.00 21.45  ? 212 VAL D CG1 1 
ATOM   11710 C CG2 . VAL D 1 183 ? 28.704  73.103  -11.649 1.00 24.26  ? 212 VAL D CG2 1 
ATOM   11711 N N   . ALA D 1 184 ? 26.580  74.425  -7.899  1.00 20.15  ? 213 ALA D N   1 
ATOM   11712 C CA  . ALA D 1 184 ? 25.438  74.459  -7.003  1.00 20.38  ? 213 ALA D CA  1 
ATOM   11713 C C   . ALA D 1 184 ? 25.113  75.888  -6.554  1.00 20.55  ? 213 ALA D C   1 
ATOM   11714 O O   . ALA D 1 184 ? 23.943  76.271  -6.392  1.00 21.61  ? 213 ALA D O   1 
ATOM   11715 C CB  . ALA D 1 184 ? 25.695  73.561  -5.826  1.00 18.91  ? 213 ALA D CB  1 
ATOM   11716 N N   . ALA D 1 185 ? 26.155  76.680  -6.335  1.00 21.87  ? 214 ALA D N   1 
ATOM   11717 C CA  . ALA D 1 185 ? 25.937  78.049  -5.875  1.00 22.36  ? 214 ALA D CA  1 
ATOM   11718 C C   . ALA D 1 185 ? 25.463  78.950  -7.008  1.00 20.69  ? 214 ALA D C   1 
ATOM   11719 O O   . ALA D 1 185 ? 24.656  79.848  -6.767  1.00 24.35  ? 214 ALA D O   1 
ATOM   11720 C CB  . ALA D 1 185 ? 27.180  78.587  -5.225  1.00 19.72  ? 214 ALA D CB  1 
ATOM   11721 N N   . LYS D 1 186 ? 25.937  78.727  -8.241  1.00 22.27  ? 215 LYS D N   1 
ATOM   11722 C CA  . LYS D 1 186 ? 25.397  79.458  -9.384  1.00 23.96  ? 215 LYS D CA  1 
ATOM   11723 C C   . LYS D 1 186 ? 23.902  79.167  -9.508  1.00 24.43  ? 215 LYS D C   1 
ATOM   11724 O O   . LYS D 1 186 ? 23.122  80.074  -9.810  1.00 22.92  ? 215 LYS D O   1 
ATOM   11725 C CB  . LYS D 1 186 ? 26.134  79.134  -10.693 1.00 24.86  ? 215 LYS D CB  1 
ATOM   11726 C CG  . LYS D 1 186 ? 25.748  79.976  -11.899 1.00 29.55  ? 215 LYS D CG  1 
ATOM   11727 C CD  . LYS D 1 186 ? 26.895  80.251  -12.892 1.00 27.68  ? 215 LYS D CD  1 
ATOM   11728 C CE  . LYS D 1 186 ? 27.107  81.734  -13.165 1.00 28.21  ? 215 LYS D CE  1 
ATOM   11729 N N   . ILE D 1 187 ? 23.494  77.908  -9.246  1.00 23.28  ? 216 ILE D N   1 
ATOM   11730 C CA  . ILE D 1 187 ? 22.094  77.550  -9.378  1.00 23.42  ? 216 ILE D CA  1 
ATOM   11731 C C   . ILE D 1 187 ? 21.272  78.366  -8.392  1.00 24.70  ? 216 ILE D C   1 
ATOM   11732 O O   . ILE D 1 187 ? 20.231  78.915  -8.757  1.00 25.83  ? 216 ILE D O   1 
ATOM   11733 C CB  . ILE D 1 187 ? 21.891  76.027  -9.224  1.00 24.84  ? 216 ILE D CB  1 
ATOM   11734 C CG1 . ILE D 1 187 ? 22.358  75.325  -10.499 1.00 23.16  ? 216 ILE D CG1 1 
ATOM   11735 C CG2 . ILE D 1 187 ? 20.441  75.695  -8.919  1.00 23.69  ? 216 ILE D CG2 1 
ATOM   11736 C CD1 . ILE D 1 187 ? 22.577  73.847  -10.356 1.00 23.24  ? 216 ILE D CD1 1 
ATOM   11737 N N   . TYR D 1 188 ? 21.757  78.400  -7.152  1.00 24.88  ? 217 TYR D N   1 
ATOM   11738 C CA  . TYR D 1 188 ? 21.092  79.057  -6.049  1.00 23.34  ? 217 TYR D CA  1 
ATOM   11739 C C   . TYR D 1 188 ? 20.926  80.534  -6.385  1.00 22.31  ? 217 TYR D C   1 
ATOM   11740 O O   . TYR D 1 188 ? 19.818  81.046  -6.318  1.00 24.78  ? 217 TYR D O   1 
ATOM   11741 C CB  . TYR D 1 188 ? 21.852  78.797  -4.744  1.00 22.20  ? 217 TYR D CB  1 
ATOM   11742 C CG  . TYR D 1 188 ? 21.133  79.282  -3.511  1.00 24.16  ? 217 TYR D CG  1 
ATOM   11743 C CD1 . TYR D 1 188 ? 20.141  78.528  -2.901  1.00 23.26  ? 217 TYR D CD1 1 
ATOM   11744 C CD2 . TYR D 1 188 ? 21.377  80.549  -3.010  1.00 24.69  ? 217 TYR D CD2 1 
ATOM   11745 C CE1 . TYR D 1 188 ? 19.474  78.987  -1.777  1.00 26.10  ? 217 TYR D CE1 1 
ATOM   11746 C CE2 . TYR D 1 188 ? 20.692  81.039  -1.905  1.00 26.94  ? 217 TYR D CE2 1 
ATOM   11747 C CZ  . TYR D 1 188 ? 19.741  80.254  -1.282  1.00 26.60  ? 217 TYR D CZ  1 
ATOM   11748 O OH  . TYR D 1 188 ? 19.040  80.697  -0.185  1.00 28.04  ? 217 TYR D OH  1 
ATOM   11749 N N   . ARG D 1 189 ? 21.991  81.201  -6.819  1.00 23.76  ? 218 ARG D N   1 
ATOM   11750 C CA  . ARG D 1 189 ? 21.939  82.659  -6.939  1.00 26.55  ? 218 ARG D CA  1 
ATOM   11751 C C   . ARG D 1 189 ? 21.100  83.105  -8.148  1.00 28.86  ? 218 ARG D C   1 
ATOM   11752 O O   . ARG D 1 189 ? 20.435  84.152  -8.103  1.00 28.67  ? 218 ARG D O   1 
ATOM   11753 C CB  . ARG D 1 189 ? 23.370  83.206  -6.986  1.00 29.12  ? 218 ARG D CB  1 
ATOM   11754 C CG  . ARG D 1 189 ? 24.130  83.088  -5.672  1.00 34.07  ? 218 ARG D CG  1 
ATOM   11755 C CD  . ARG D 1 189 ? 25.442  83.847  -5.687  1.00 36.12  ? 218 ARG D CD  1 
ATOM   11756 N NE  . ARG D 1 189 ? 25.674  84.406  -4.370  1.00 40.37  ? 218 ARG D NE  1 
ATOM   11757 C CZ  . ARG D 1 189 ? 25.745  85.701  -4.079  1.00 46.86  ? 218 ARG D CZ  1 
ATOM   11758 N NH1 . ARG D 1 189 ? 25.350  86.101  -2.882  1.00 48.64  ? 218 ARG D NH1 1 
ATOM   11759 N NH2 . ARG D 1 189 ? 26.091  86.598  -4.993  1.00 45.03  ? 218 ARG D NH2 1 
ATOM   11760 N N   . ASN D 1 190 ? 21.167  82.357  -9.256  1.00 24.73  ? 219 ASN D N   1 
ATOM   11761 C CA  . ASN D 1 190 ? 20.354  82.622  -10.426 1.00 29.01  ? 219 ASN D CA  1 
ATOM   11762 C C   . ASN D 1 190 ? 18.872  82.423  -10.091 1.00 29.17  ? 219 ASN D C   1 
ATOM   11763 O O   . ASN D 1 190 ? 18.014  83.153  -10.579 1.00 32.98  ? 219 ASN D O   1 
ATOM   11764 C CB  . ASN D 1 190 ? 20.725  81.723  -11.612 1.00 28.20  ? 219 ASN D CB  1 
ATOM   11765 C CG  . ASN D 1 190 ? 22.115  81.960  -12.172 1.00 26.63  ? 219 ASN D CG  1 
ATOM   11766 O OD1 . ASN D 1 190 ? 22.764  82.954  -11.886 1.00 30.36  ? 219 ASN D OD1 1 
ATOM   11767 N ND2 . ASN D 1 190 ? 22.572  81.077  -13.033 1.00 27.38  ? 219 ASN D ND2 1 
ATOM   11768 N N   . LEU D 1 191 ? 18.570  81.419  -9.266  1.00 25.57  ? 220 LEU D N   1 
ATOM   11769 C CA  . LEU D 1 191 ? 17.192  81.090  -8.964  1.00 27.00  ? 220 LEU D CA  1 
ATOM   11770 C C   . LEU D 1 191 ? 16.630  82.022  -7.892  1.00 28.51  ? 220 LEU D C   1 
ATOM   11771 O O   . LEU D 1 191 ? 15.466  82.430  -7.957  1.00 26.73  ? 220 LEU D O   1 
ATOM   11772 C CB  . LEU D 1 191 ? 17.088  79.633  -8.498  1.00 26.94  ? 220 LEU D CB  1 
ATOM   11773 C CG  . LEU D 1 191 ? 16.973  78.573  -9.590  1.00 26.91  ? 220 LEU D CG  1 
ATOM   11774 C CD1 . LEU D 1 191 ? 16.539  77.235  -9.013  1.00 24.58  ? 220 LEU D CD1 1 
ATOM   11775 C CD2 . LEU D 1 191 ? 16.006  79.002  -10.683 1.00 27.47  ? 220 LEU D CD2 1 
ATOM   11776 N N   . TYR D 1 192 ? 17.405  82.250  -6.837  1.00 29.24  ? 221 TYR D N   1 
ATOM   11777 C CA  . TYR D 1 192 ? 16.782  82.915  -5.666  1.00 32.37  ? 221 TYR D CA  1 
ATOM   11778 C C   . TYR D 1 192 ? 17.452  84.182  -5.228  1.00 32.93  ? 221 TYR D C   1 
ATOM   11779 O O   . TYR D 1 192 ? 17.083  84.707  -4.175  1.00 35.83  ? 221 TYR D O   1 
ATOM   11780 C CB  . TYR D 1 192 ? 16.905  81.844  -4.580  1.00 30.41  ? 221 TYR D CB  1 
ATOM   11781 C CG  . TYR D 1 192 ? 16.357  80.468  -4.935  1.00 29.39  ? 221 TYR D CG  1 
ATOM   11782 C CD1 . TYR D 1 192 ? 15.042  80.310  -5.348  1.00 27.12  ? 221 TYR D CD1 1 
ATOM   11783 C CD2 . TYR D 1 192 ? 17.146  79.329  -4.838  1.00 28.41  ? 221 TYR D CD2 1 
ATOM   11784 C CE1 . TYR D 1 192 ? 14.529  79.067  -5.667  1.00 28.08  ? 221 TYR D CE1 1 
ATOM   11785 C CE2 . TYR D 1 192 ? 16.643  78.077  -5.150  1.00 27.93  ? 221 TYR D CE2 1 
ATOM   11786 C CZ  . TYR D 1 192 ? 15.331  77.947  -5.568  1.00 28.69  ? 221 TYR D CZ  1 
ATOM   11787 O OH  . TYR D 1 192 ? 14.807  76.732  -5.886  1.00 28.98  ? 221 TYR D OH  1 
ATOM   11788 N N   . ARG D 1 193 ? 18.403  84.660  -6.008  1.00 37.11  ? 222 ARG D N   1 
ATOM   11789 C CA  . ARG D 1 193 ? 19.151  85.874  -5.603  1.00 44.07  ? 222 ARG D CA  1 
ATOM   11790 C C   . ARG D 1 193 ? 19.257  86.796  -6.816  1.00 47.04  ? 222 ARG D C   1 
ATOM   11791 O O   . ARG D 1 193 ? 20.160  87.635  -6.841  1.00 51.23  ? 222 ARG D O   1 
ATOM   11792 C CB  . ARG D 1 193 ? 20.528  85.543  -5.020  1.00 44.83  ? 222 ARG D CB  1 
ATOM   11793 C CG  . ARG D 1 193 ? 20.530  84.573  -3.849  1.00 45.06  ? 222 ARG D CG  1 
ATOM   11794 C CD  . ARG D 1 193 ? 20.977  85.222  -2.555  1.00 50.51  ? 222 ARG D CD  1 
ATOM   11795 N NE  . ARG D 1 193 ? 19.859  85.330  -1.612  1.00 51.36  ? 222 ARG D NE  1 
ATOM   11796 C CZ  . ARG D 1 193 ? 19.402  84.342  -0.861  1.00 49.52  ? 222 ARG D CZ  1 
ATOM   11797 N NH1 . ARG D 1 193 ? 18.317  83.683  -1.223  1.00 43.64  ? 222 ARG D NH1 1 
ATOM   11798 N NH2 . ARG D 1 193 ? 20.031  84.021  0.253   1.00 52.39  ? 222 ARG D NH2 1 
ATOM   11799 N N   . GLU D 1 194 ? 18.354  86.621  -7.767  1.00 53.28  ? 223 GLU D N   1 
ATOM   11800 C CA  . GLU D 1 194 ? 18.323  87.492  -8.978  1.00 60.04  ? 223 GLU D CA  1 
ATOM   11801 C C   . GLU D 1 194 ? 19.743  87.658  -9.573  1.00 60.25  ? 223 GLU D C   1 
ATOM   11802 O O   . GLU D 1 194 ? 20.318  88.832  -9.495  1.00 57.17  ? 223 GLU D O   1 
ATOM   11803 C CB  . GLU D 1 194 ? 17.457  88.710  -8.636  1.00 61.16  ? 223 GLU D CB  1 
ATOM   11804 C CG  . GLU D 1 194 ? 15.974  88.459  -8.908  1.00 62.19  ? 223 GLU D CG  1 
ATOM   11805 C CD  . GLU D 1 194 ? 15.222  87.371  -8.149  1.00 65.06  ? 223 GLU D CD  1 
ATOM   11806 O OE1 . GLU D 1 194 ? 14.277  87.748  -7.423  1.00 64.70  ? 223 GLU D OE1 1 
ATOM   11807 O OE2 . GLU D 1 194 ? 15.530  86.166  -8.283  1.00 66.48  ? 223 GLU D OE2 1 
ATOM   11808 N N   . GLY D 1 195 ? 20.279  86.540  -10.101 1.00 57.88  ? 224 GLY D N   1 
ATOM   11809 C CA  . GLY D 1 195 ? 21.564  86.532  -10.823 1.00 61.42  ? 224 GLY D CA  1 
ATOM   11810 C C   . GLY D 1 195 ? 22.779  86.382  -9.947  1.00 63.62  ? 224 GLY D C   1 
ATOM   11811 O O   . GLY D 1 195 ? 23.093  85.253  -9.553  1.00 58.08  ? 224 GLY D O   1 
ATOM   11812 N N   . SER D 1 196 ? 23.550  87.445  -9.826  1.00 66.78  ? 225 SER D N   1 
ATOM   11813 C CA  . SER D 1 196 ? 24.707  87.498  -8.897  1.00 69.87  ? 225 SER D CA  1 
ATOM   11814 C C   . SER D 1 196 ? 25.549  86.215  -8.900  1.00 72.72  ? 225 SER D C   1 
ATOM   11815 O O   . SER D 1 196 ? 25.840  85.754  -7.807  1.00 73.98  ? 225 SER D O   1 
ATOM   11816 C CB  . SER D 1 196 ? 24.162  87.782  -7.522  1.00 65.09  ? 225 SER D CB  1 
ATOM   11817 O OG  . SER D 1 196 ? 23.397  86.694  -7.028  1.00 63.70  ? 225 SER D OG  1 
ATOM   11818 N N   . GLY D 1 197 ? 25.959  85.671  -10.051 1.00 78.32  ? 226 GLY D N   1 
ATOM   11819 C CA  . GLY D 1 197 ? 26.679  84.368  -10.093 1.00 78.86  ? 226 GLY D CA  1 
ATOM   11820 C C   . GLY D 1 197 ? 28.179  84.499  -9.871  1.00 83.51  ? 226 GLY D C   1 
ATOM   11821 O O   . GLY D 1 197 ? 28.856  85.049  -10.753 1.00 75.37  ? 226 GLY D O   1 
ATOM   11822 N N   . ILE D 1 198 ? 28.693  83.946  -8.767  1.00 87.56  ? 227 ILE D N   1 
ATOM   11823 C CA  . ILE D 1 198 ? 30.127  84.199  -8.412  1.00 86.91  ? 227 ILE D CA  1 
ATOM   11824 C C   . ILE D 1 198 ? 30.995  82.933  -8.377  1.00 80.30  ? 227 ILE D C   1 
ATOM   11825 O O   . ILE D 1 198 ? 30.461  81.823  -8.546  1.00 73.85  ? 227 ILE D O   1 
ATOM   11826 C CB  . ILE D 1 198 ? 30.230  84.938  -7.063  1.00 82.94  ? 227 ILE D CB  1 
ATOM   11827 C CG1 . ILE D 1 198 ? 28.897  85.508  -6.614  1.00 85.86  ? 227 ILE D CG1 1 
ATOM   11828 C CG2 . ILE D 1 198 ? 31.296  86.029  -7.133  1.00 81.44  ? 227 ILE D CG2 1 
ATOM   11829 C CD1 . ILE D 1 198 ? 28.740  86.990  -6.904  1.00 83.22  ? 227 ILE D CD1 1 
ATOM   11830 N N   . GLY D 1 199 ? 32.303  83.133  -8.271  1.00 70.59  ? 228 GLY D N   1 
ATOM   11831 C CA  . GLY D 1 199 ? 33.259  82.036  -8.104  1.00 67.55  ? 228 GLY D CA  1 
ATOM   11832 C C   . GLY D 1 199 ? 34.125  82.474  -6.944  1.00 59.75  ? 228 GLY D C   1 
ATOM   11833 O O   . GLY D 1 199 ? 35.343  82.286  -7.059  1.00 58.75  ? 228 GLY D O   1 
ATOM   11834 N N   . ALA D 1 200 ? 33.526  83.070  -5.894  1.00 47.10  ? 229 ALA D N   1 
ATOM   11835 C CA  . ALA D 1 200 ? 34.249  83.527  -4.668  1.00 41.94  ? 229 ALA D CA  1 
ATOM   11836 C C   . ALA D 1 200 ? 34.965  82.376  -3.961  1.00 36.68  ? 229 ALA D C   1 
ATOM   11837 O O   . ALA D 1 200 ? 34.338  81.647  -3.195  1.00 30.46  ? 229 ALA D O   1 
ATOM   11838 C CB  . ALA D 1 200 ? 33.283  84.177  -3.748  1.00 44.09  ? 229 ALA D CB  1 
ATOM   11839 N N   . ILE D 1 201 ? 36.278  82.282  -4.169  1.00 37.25  ? 230 ILE D N   1 
ATOM   11840 C CA  . ILE D 1 201 ? 37.038  81.126  -3.628  1.00 38.16  ? 230 ILE D CA  1 
ATOM   11841 C C   . ILE D 1 201 ? 38.268  81.643  -2.878  1.00 35.13  ? 230 ILE D C   1 
ATOM   11842 O O   . ILE D 1 201 ? 38.975  82.474  -3.455  1.00 35.37  ? 230 ILE D O   1 
ATOM   11843 C CB  . ILE D 1 201 ? 37.430  80.172  -4.771  1.00 43.27  ? 230 ILE D CB  1 
ATOM   11844 C CG1 . ILE D 1 201 ? 36.215  79.510  -5.408  1.00 44.39  ? 230 ILE D CG1 1 
ATOM   11845 C CG2 . ILE D 1 201 ? 38.449  79.138  -4.294  1.00 43.74  ? 230 ILE D CG2 1 
ATOM   11846 C CD1 . ILE D 1 201 ? 35.627  78.385  -4.583  1.00 44.17  ? 230 ILE D CD1 1 
ATOM   11847 N N   . ASP D 1 202 ? 38.463  81.198  -1.634  1.00 32.50  ? 231 ASP D N   1 
ATOM   11848 C CA  . ASP D 1 202 ? 39.673  81.569  -0.847  1.00 30.78  ? 231 ASP D CA  1 
ATOM   11849 C C   . ASP D 1 202 ? 40.562  80.334  -0.707  1.00 28.83  ? 231 ASP D C   1 
ATOM   11850 O O   . ASP D 1 202 ? 40.084  79.339  -0.163  1.00 27.32  ? 231 ASP D O   1 
ATOM   11851 C CB  . ASP D 1 202 ? 39.329  82.189  0.499   1.00 30.49  ? 231 ASP D CB  1 
ATOM   11852 C CG  . ASP D 1 202 ? 40.498  82.795  1.260   1.00 31.15  ? 231 ASP D CG  1 
ATOM   11853 O OD1 . ASP D 1 202 ? 41.523  82.110  1.411   1.00 28.28  ? 231 ASP D OD1 1 
ATOM   11854 O OD2 . ASP D 1 202 ? 40.366  83.953  1.689   1.00 41.47  ? 231 ASP D OD2 1 
ATOM   11855 N N   . SER D 1 203 ? 41.822  80.439  -1.128  1.00 26.28  ? 232 SER D N   1 
ATOM   11856 C CA  . SER D 1 203 ? 42.698  79.265  -1.123  1.00 27.30  ? 232 SER D CA  1 
ATOM   11857 C C   . SER D 1 203 ? 42.960  78.721  0.280   1.00 26.56  ? 232 SER D C   1 
ATOM   11858 O O   . SER D 1 203 ? 43.487  77.618  0.390   1.00 29.25  ? 232 SER D O   1 
ATOM   11859 C CB  . SER D 1 203 ? 43.996  79.512  -1.835  1.00 26.71  ? 232 SER D CB  1 
ATOM   11860 O OG  . SER D 1 203 ? 44.436  80.828  -1.619  1.00 29.70  ? 232 SER D OG  1 
ATOM   11861 N N   . ASN D 1 204 ? 42.596  79.479  1.326   1.00 25.48  ? 233 ASN D N   1 
ATOM   11862 C CA  . ASN D 1 204 ? 42.874  79.119  2.707   1.00 28.35  ? 233 ASN D CA  1 
ATOM   11863 C C   . ASN D 1 204 ? 41.592  78.810  3.474   1.00 25.56  ? 233 ASN D C   1 
ATOM   11864 O O   . ASN D 1 204 ? 41.638  78.635  4.690   1.00 25.25  ? 233 ASN D O   1 
ATOM   11865 C CB  . ASN D 1 204 ? 43.578  80.254  3.454   1.00 30.92  ? 233 ASN D CB  1 
ATOM   11866 C CG  . ASN D 1 204 ? 44.862  80.655  2.766   1.00 36.57  ? 233 ASN D CG  1 
ATOM   11867 O OD1 . ASN D 1 204 ? 45.057  81.827  2.459   1.00 45.87  ? 233 ASN D OD1 1 
ATOM   11868 N ND2 . ASN D 1 204 ? 45.704  79.682  2.457   1.00 36.68  ? 233 ASN D ND2 1 
ATOM   11869 N N   . LEU D 1 205 ? 40.456  78.754  2.768   1.00 26.64  ? 234 LEU D N   1 
ATOM   11870 C CA  . LEU D 1 205 ? 39.204  78.340  3.384   1.00 24.57  ? 234 LEU D CA  1 
ATOM   11871 C C   . LEU D 1 205 ? 38.942  76.874  3.054   1.00 25.47  ? 234 LEU D C   1 
ATOM   11872 O O   . LEU D 1 205 ? 39.413  76.356  2.046   1.00 26.16  ? 234 LEU D O   1 
ATOM   11873 C CB  . LEU D 1 205 ? 38.057  79.215  2.886   1.00 23.53  ? 234 LEU D CB  1 
ATOM   11874 C CG  . LEU D 1 205 ? 37.906  80.570  3.570   1.00 24.49  ? 234 LEU D CG  1 
ATOM   11875 C CD1 . LEU D 1 205 ? 36.639  81.282  3.107   1.00 25.16  ? 234 LEU D CD1 1 
ATOM   11876 C CD2 . LEU D 1 205 ? 37.895  80.387  5.079   1.00 25.13  ? 234 LEU D CD2 1 
ATOM   11877 N N   . ASP D 1 206 ? 38.195  76.204  3.930   1.00 26.83  ? 235 ASP D N   1 
ATOM   11878 C CA  . ASP D 1 206 ? 37.728  74.864  3.607   1.00 25.84  ? 235 ASP D CA  1 
ATOM   11879 C C   . ASP D 1 206 ? 36.592  74.951  2.577   1.00 26.38  ? 235 ASP D C   1 
ATOM   11880 O O   . ASP D 1 206 ? 36.009  76.006  2.294   1.00 24.49  ? 235 ASP D O   1 
ATOM   11881 C CB  . ASP D 1 206 ? 37.346  74.086  4.873   1.00 27.82  ? 235 ASP D CB  1 
ATOM   11882 C CG  . ASP D 1 206 ? 36.239  74.747  5.677   1.00 29.38  ? 235 ASP D CG  1 
ATOM   11883 O OD1 . ASP D 1 206 ? 36.508  75.827  6.238   1.00 29.99  ? 235 ASP D OD1 1 
ATOM   11884 O OD2 . ASP D 1 206 ? 35.139  74.176  5.758   1.00 27.48  ? 235 ASP D OD2 1 
ATOM   11885 N N   . TRP D 1 207 ? 36.307  73.781  2.008   1.00 25.72  ? 236 TRP D N   1 
ATOM   11886 C CA  . TRP D 1 207 ? 35.368  73.560  0.913   1.00 22.54  ? 236 TRP D CA  1 
ATOM   11887 C C   . TRP D 1 207 ? 33.979  74.090  1.270   1.00 22.00  ? 236 TRP D C   1 
ATOM   11888 O O   . TRP D 1 207 ? 33.364  74.810  0.478   1.00 22.25  ? 236 TRP D O   1 
ATOM   11889 C CB  . TRP D 1 207 ? 35.397  72.047  0.600   1.00 22.35  ? 236 TRP D CB  1 
ATOM   11890 C CG  . TRP D 1 207 ? 34.691  71.558  -0.641  1.00 21.90  ? 236 TRP D CG  1 
ATOM   11891 C CD1 . TRP D 1 207 ? 34.914  71.890  -1.951  1.00 23.59  ? 236 TRP D CD1 1 
ATOM   11892 C CD2 . TRP D 1 207 ? 33.660  70.545  -0.668  1.00 22.59  ? 236 TRP D CD2 1 
ATOM   11893 N NE1 . TRP D 1 207 ? 34.091  71.161  -2.788  1.00 23.43  ? 236 TRP D NE1 1 
ATOM   11894 C CE2 . TRP D 1 207 ? 33.318  70.324  -2.022  1.00 21.51  ? 236 TRP D CE2 1 
ATOM   11895 C CE3 . TRP D 1 207 ? 32.998  69.807  0.326   1.00 20.83  ? 236 TRP D CE3 1 
ATOM   11896 C CZ2 . TRP D 1 207 ? 32.322  69.414  -2.391  1.00 19.02  ? 236 TRP D CZ2 1 
ATOM   11897 C CZ3 . TRP D 1 207 ? 32.018  68.911  -0.043  1.00 19.19  ? 236 TRP D CZ3 1 
ATOM   11898 C CH2 . TRP D 1 207 ? 31.724  68.688  -1.388  1.00 19.84  ? 236 TRP D CH2 1 
ATOM   11899 N N   . SER D 1 208 ? 33.517  73.725  2.474   1.00 21.15  ? 237 SER D N   1 
ATOM   11900 C CA  . SER D 1 208 ? 32.223  74.098  3.022   1.00 22.36  ? 237 SER D CA  1 
ATOM   11901 C C   . SER D 1 208 ? 32.128  75.610  3.145   1.00 21.89  ? 237 SER D C   1 
ATOM   11902 O O   . SER D 1 208 ? 31.048  76.165  3.000   1.00 22.78  ? 237 SER D O   1 
ATOM   11903 C CB  . SER D 1 208 ? 31.987  73.495  4.389   1.00 22.62  ? 237 SER D CB  1 
ATOM   11904 O OG  . SER D 1 208 ? 31.908  72.074  4.341   1.00 23.37  ? 237 SER D OG  1 
ATOM   11905 N N   . HIS D 1 209 ? 33.248  76.247  3.476   1.00 23.38  ? 238 HIS D N   1 
ATOM   11906 C CA  . HIS D 1 209 ? 33.208  77.683  3.759   1.00 25.05  ? 238 HIS D CA  1 
ATOM   11907 C C   . HIS D 1 209 ? 33.115  78.457  2.446   1.00 23.79  ? 238 HIS D C   1 
ATOM   11908 O O   . HIS D 1 209 ? 32.281  79.353  2.326   1.00 28.55  ? 238 HIS D O   1 
ATOM   11909 C CB  . HIS D 1 209 ? 34.332  78.087  4.720   1.00 25.32  ? 238 HIS D CB  1 
ATOM   11910 C CG  . HIS D 1 209 ? 34.137  79.427  5.388   1.00 26.82  ? 238 HIS D CG  1 
ATOM   11911 N ND1 . HIS D 1 209 ? 34.773  79.748  6.579   1.00 31.04  ? 238 HIS D ND1 1 
ATOM   11912 C CD2 . HIS D 1 209 ? 33.417  80.508  5.065   1.00 29.03  ? 238 HIS D CD2 1 
ATOM   11913 C CE1 . HIS D 1 209 ? 34.430  80.982  6.953   1.00 28.04  ? 238 HIS D CE1 1 
ATOM   11914 N NE2 . HIS D 1 209 ? 33.611  81.469  6.052   1.00 26.95  ? 238 HIS D NE2 1 
ATOM   11915 N N   . ASN D 1 210 ? 33.912  78.050  1.445   1.00 25.54  ? 239 ASN D N   1 
ATOM   11916 C CA  . ASN D 1 210 ? 33.901  78.638  0.112   1.00 24.37  ? 239 ASN D CA  1 
ATOM   11917 C C   . ASN D 1 210 ? 32.483  78.520  -0.467  1.00 24.08  ? 239 ASN D C   1 
ATOM   11918 O O   . ASN D 1 210 ? 31.990  79.416  -1.163  1.00 24.49  ? 239 ASN D O   1 
ATOM   11919 C CB  . ASN D 1 210 ? 34.948  77.979  -0.818  1.00 23.67  ? 239 ASN D CB  1 
ATOM   11920 C CG  . ASN D 1 210 ? 36.370  78.491  -0.663  1.00 26.31  ? 239 ASN D CG  1 
ATOM   11921 O OD1 . ASN D 1 210 ? 36.604  79.696  -0.650  1.00 27.47  ? 239 ASN D OD1 1 
ATOM   11922 N ND2 . ASN D 1 210 ? 37.331  77.593  -0.497  1.00 29.06  ? 239 ASN D ND2 1 
ATOM   11923 N N   . PHE D 1 211 ? 31.833  77.381  -0.199  1.00 25.24  ? 240 PHE D N   1 
ATOM   11924 C CA  . PHE D 1 211 ? 30.464  77.129  -0.646  1.00 23.96  ? 240 PHE D CA  1 
ATOM   11925 C C   . PHE D 1 211 ? 29.465  78.092  0.000   1.00 21.48  ? 240 PHE D C   1 
ATOM   11926 O O   . PHE D 1 211 ? 28.710  78.749  -0.712  1.00 21.70  ? 240 PHE D O   1 
ATOM   11927 C CB  . PHE D 1 211 ? 30.129  75.656  -0.397  1.00 22.32  ? 240 PHE D CB  1 
ATOM   11928 C CG  . PHE D 1 211 ? 28.813  75.189  -0.969  1.00 23.05  ? 240 PHE D CG  1 
ATOM   11929 C CD1 . PHE D 1 211 ? 28.227  75.794  -2.072  1.00 24.08  ? 240 PHE D CD1 1 
ATOM   11930 C CD2 . PHE D 1 211 ? 28.159  74.114  -0.399  1.00 23.95  ? 240 PHE D CD2 1 
ATOM   11931 C CE1 . PHE D 1 211 ? 27.005  75.363  -2.562  1.00 22.98  ? 240 PHE D CE1 1 
ATOM   11932 C CE2 . PHE D 1 211 ? 26.947  73.663  -0.901  1.00 23.77  ? 240 PHE D CE2 1 
ATOM   11933 C CZ  . PHE D 1 211 ? 26.362  74.292  -1.976  1.00 25.43  ? 240 PHE D CZ  1 
ATOM   11934 N N   . THR D 1 212 ? 29.461  78.208  1.335   1.00 21.39  ? 241 THR D N   1 
ATOM   11935 C CA  . THR D 1 212 ? 28.495  79.071  1.990   1.00 22.37  ? 241 THR D CA  1 
ATOM   11936 C C   . THR D 1 212 ? 28.743  80.535  1.645   1.00 23.47  ? 241 THR D C   1 
ATOM   11937 O O   . THR D 1 212 ? 27.791  81.307  1.522   1.00 24.17  ? 241 THR D O   1 
ATOM   11938 C CB  . THR D 1 212 ? 28.430  78.856  3.505   1.00 24.22  ? 241 THR D CB  1 
ATOM   11939 O OG1 . THR D 1 212 ? 29.692  79.128  4.127   1.00 25.62  ? 241 THR D OG1 1 
ATOM   11940 C CG2 . THR D 1 212 ? 27.952  77.455  3.796   1.00 22.26  ? 241 THR D CG2 1 
ATOM   11941 N N   . ASN D 1 213 ? 29.996  80.922  1.447   1.00 23.75  ? 242 ASN D N   1 
ATOM   11942 C CA  . ASN D 1 213 ? 30.243  82.284  0.995   1.00 25.12  ? 242 ASN D CA  1 
ATOM   11943 C C   . ASN D 1 213 ? 29.646  82.492  -0.408  1.00 25.80  ? 242 ASN D C   1 
ATOM   11944 O O   . ASN D 1 213 ? 29.142  83.574  -0.733  1.00 25.32  ? 242 ASN D O   1 
ATOM   11945 C CB  . ASN D 1 213 ? 31.728  82.638  0.959   1.00 25.93  ? 242 ASN D CB  1 
ATOM   11946 C CG  . ASN D 1 213 ? 32.379  82.851  2.312   1.00 25.21  ? 242 ASN D CG  1 
ATOM   11947 O OD1 . ASN D 1 213 ? 31.724  83.038  3.346   1.00 26.68  ? 242 ASN D OD1 1 
ATOM   11948 N ND2 . ASN D 1 213 ? 33.706  82.817  2.308   1.00 26.10  ? 242 ASN D ND2 1 
ATOM   11949 N N   . MET D 1 214 ? 29.729  81.449  -1.247  1.00 25.86  ? 243 MET D N   1 
ATOM   11950 C CA  . MET D 1 214 ? 29.284  81.512  -2.629  1.00 26.02  ? 243 MET D CA  1 
ATOM   11951 C C   . MET D 1 214 ? 27.752  81.538  -2.652  1.00 25.76  ? 243 MET D C   1 
ATOM   11952 O O   . MET D 1 214 ? 27.174  82.109  -3.564  1.00 24.75  ? 243 MET D O   1 
ATOM   11953 C CB  . MET D 1 214 ? 29.861  80.347  -3.454  1.00 24.56  ? 243 MET D CB  1 
ATOM   11954 C CG  . MET D 1 214 ? 31.294  80.618  -3.954  1.00 25.57  ? 243 MET D CG  1 
ATOM   11955 S SD  . MET D 1 214 ? 31.889  79.553  -5.285  1.00 28.78  ? 243 MET D SD  1 
ATOM   11956 C CE  . MET D 1 214 ? 31.745  77.892  -4.630  1.00 27.95  ? 243 MET D CE  1 
ATOM   11957 N N   . LEU D 1 215 ? 27.109  80.995  -1.598  1.00 24.97  ? 244 LEU D N   1 
ATOM   11958 C CA  . LEU D 1 215 ? 25.655  80.992  -1.488  1.00 25.96  ? 244 LEU D CA  1 
ATOM   11959 C C   . LEU D 1 215 ? 25.175  82.323  -0.905  1.00 27.81  ? 244 LEU D C   1 
ATOM   11960 O O   . LEU D 1 215 ? 23.969  82.585  -0.890  1.00 24.00  ? 244 LEU D O   1 
ATOM   11961 C CB  . LEU D 1 215 ? 25.233  79.836  -0.586  1.00 26.56  ? 244 LEU D CB  1 
ATOM   11962 C CG  . LEU D 1 215 ? 25.339  78.419  -1.162  1.00 25.43  ? 244 LEU D CG  1 
ATOM   11963 C CD1 . LEU D 1 215 ? 25.136  77.384  -0.055  1.00 24.71  ? 244 LEU D CD1 1 
ATOM   11964 C CD2 . LEU D 1 215 ? 24.313  78.201  -2.271  1.00 24.59  ? 244 LEU D CD2 1 
ATOM   11965 N N   . GLY D 1 216 ? 26.137  83.104  -0.372  1.00 26.81  ? 245 GLY D N   1 
ATOM   11966 C CA  . GLY D 1 216 ? 25.881  84.435  0.157   1.00 26.09  ? 245 GLY D CA  1 
ATOM   11967 C C   . GLY D 1 216 ? 25.363  84.412  1.589   1.00 27.07  ? 245 GLY D C   1 
ATOM   11968 O O   . GLY D 1 216 ? 24.650  85.330  1.997   1.00 33.91  ? 245 GLY D O   1 
ATOM   11969 N N   . TYR D 1 217 ? 25.719  83.373  2.346   1.00 25.52  ? 246 TYR D N   1 
ATOM   11970 C CA  . TYR D 1 217 ? 25.456  83.312  3.783   1.00 25.54  ? 246 TYR D CA  1 
ATOM   11971 C C   . TYR D 1 217 ? 26.692  83.781  4.560   1.00 29.62  ? 246 TYR D C   1 
ATOM   11972 O O   . TYR D 1 217 ? 27.804  83.779  4.026   1.00 31.55  ? 246 TYR D O   1 
ATOM   11973 C CB  . TYR D 1 217 ? 25.032  81.895  4.184   1.00 24.83  ? 246 TYR D CB  1 
ATOM   11974 C CG  . TYR D 1 217 ? 23.646  81.527  3.696   1.00 23.26  ? 246 TYR D CG  1 
ATOM   11975 C CD1 . TYR D 1 217 ? 23.346  81.447  2.334   1.00 22.98  ? 246 TYR D CD1 1 
ATOM   11976 C CD2 . TYR D 1 217 ? 22.613  81.328  4.590   1.00 22.21  ? 246 TYR D CD2 1 
ATOM   11977 C CE1 . TYR D 1 217 ? 22.067  81.180  1.879   1.00 21.49  ? 246 TYR D CE1 1 
ATOM   11978 C CE2 . TYR D 1 217 ? 21.336  81.045  4.150   1.00 22.82  ? 246 TYR D CE2 1 
ATOM   11979 C CZ  . TYR D 1 217 ? 21.055  80.972  2.800   1.00 21.91  ? 246 TYR D CZ  1 
ATOM   11980 O OH  . TYR D 1 217 ? 19.765  80.709  2.415   1.00 28.05  ? 246 TYR D OH  1 
ATOM   11981 N N   . THR D 1 218 ? 26.508  84.210  5.824   1.00 31.72  ? 247 THR D N   1 
ATOM   11982 C CA  . THR D 1 218 ? 27.651  84.677  6.594   1.00 33.18  ? 247 THR D CA  1 
ATOM   11983 C C   . THR D 1 218 ? 27.679  84.071  7.993   1.00 38.30  ? 247 THR D C   1 
ATOM   11984 O O   . THR D 1 218 ? 28.730  84.056  8.641   1.00 40.62  ? 247 THR D O   1 
ATOM   11985 C CB  . THR D 1 218 ? 27.692  86.210  6.654   1.00 35.99  ? 247 THR D CB  1 
ATOM   11986 O OG1 . THR D 1 218 ? 26.415  86.652  7.112   1.00 39.06  ? 247 THR D OG1 1 
ATOM   11987 C CG2 . THR D 1 218 ? 28.027  86.831  5.317   1.00 39.76  ? 247 THR D CG2 1 
ATOM   11988 N N   . ASP D 1 219 ? 26.539  83.524  8.418   1.00 33.62  ? 248 ASP D N   1 
ATOM   11989 C CA  . ASP D 1 219 ? 26.371  83.019  9.756   1.00 33.84  ? 248 ASP D CA  1 
ATOM   11990 C C   . ASP D 1 219 ? 27.298  81.826  9.960   1.00 33.53  ? 248 ASP D C   1 
ATOM   11991 O O   . ASP D 1 219 ? 27.094  80.793  9.326   1.00 30.51  ? 248 ASP D O   1 
ATOM   11992 C CB  . ASP D 1 219 ? 24.910  82.635  9.966   1.00 34.29  ? 248 ASP D CB  1 
ATOM   11993 C CG  . ASP D 1 219 ? 24.638  82.191  11.388  1.00 35.39  ? 248 ASP D CG  1 
ATOM   11994 O OD1 . ASP D 1 219 ? 25.435  81.386  11.900  1.00 38.37  ? 248 ASP D OD1 1 
ATOM   11995 O OD2 . ASP D 1 219 ? 23.637  82.652  11.953  1.00 32.62  ? 248 ASP D OD2 1 
ATOM   11996 N N   . HIS D 1 220 ? 28.260  81.962  10.888  1.00 28.57  ? 249 HIS D N   1 
ATOM   11997 C CA  . HIS D 1 220 ? 29.208  80.902  11.200  1.00 30.50  ? 249 HIS D CA  1 
ATOM   11998 C C   . HIS D 1 220 ? 28.507  79.560  11.423  1.00 28.81  ? 249 HIS D C   1 
ATOM   11999 O O   . HIS D 1 220 ? 29.016  78.539  10.956  1.00 28.36  ? 249 HIS D O   1 
ATOM   12000 C CB  . HIS D 1 220 ? 30.081  81.260  12.410  1.00 30.25  ? 249 HIS D CB  1 
ATOM   12001 C CG  . HIS D 1 220 ? 31.014  80.178  12.847  1.00 30.76  ? 249 HIS D CG  1 
ATOM   12002 N ND1 . HIS D 1 220 ? 30.769  79.412  13.969  1.00 30.74  ? 249 HIS D ND1 1 
ATOM   12003 C CD2 . HIS D 1 220 ? 32.166  79.725  12.337  1.00 29.49  ? 249 HIS D CD2 1 
ATOM   12004 C CE1 . HIS D 1 220 ? 31.769  78.560  14.131  1.00 33.54  ? 249 HIS D CE1 1 
ATOM   12005 N NE2 . HIS D 1 220 ? 32.618  78.724  13.143  1.00 32.75  ? 249 HIS D NE2 1 
ATOM   12006 N N   . GLN D 1 221 ? 27.409  79.536  12.194  1.00 27.10  ? 250 GLN D N   1 
ATOM   12007 C CA  . GLN D 1 221 ? 26.733  78.271  12.501  1.00 31.44  ? 250 GLN D CA  1 
ATOM   12008 C C   . GLN D 1 221 ? 26.116  77.622  11.258  1.00 26.85  ? 250 GLN D C   1 
ATOM   12009 O O   . GLN D 1 221 ? 25.878  76.408  11.269  1.00 28.43  ? 250 GLN D O   1 
ATOM   12010 C CB  . GLN D 1 221 ? 25.627  78.412  13.552  1.00 34.88  ? 250 GLN D CB  1 
ATOM   12011 C CG  . GLN D 1 221 ? 26.133  78.622  14.974  1.00 40.37  ? 250 GLN D CG  1 
ATOM   12012 C CD  . GLN D 1 221 ? 27.226  77.669  15.410  1.00 44.15  ? 250 GLN D CD  1 
ATOM   12013 O OE1 . GLN D 1 221 ? 27.366  76.556  14.898  1.00 47.28  ? 250 GLN D OE1 1 
ATOM   12014 N NE2 . GLN D 1 221 ? 28.020  78.099  16.384  1.00 45.79  ? 250 GLN D NE2 1 
ATOM   12015 N N   . PHE D 1 222 ? 25.825  78.409  10.215  1.00 22.75  ? 251 PHE D N   1 
ATOM   12016 C CA  . PHE D 1 222 ? 25.364  77.848  8.945   1.00 24.99  ? 251 PHE D CA  1 
ATOM   12017 C C   . PHE D 1 222 ? 26.542  77.170  8.246   1.00 22.85  ? 251 PHE D C   1 
ATOM   12018 O O   . PHE D 1 222 ? 26.420  76.042  7.773   1.00 23.95  ? 251 PHE D O   1 
ATOM   12019 C CB  . PHE D 1 222 ? 24.663  78.892  8.061   1.00 25.16  ? 251 PHE D CB  1 
ATOM   12020 C CG  . PHE D 1 222 ? 24.143  78.323  6.755   1.00 24.94  ? 251 PHE D CG  1 
ATOM   12021 C CD1 . PHE D 1 222 ? 23.140  77.362  6.746   1.00 26.06  ? 251 PHE D CD1 1 
ATOM   12022 C CD2 . PHE D 1 222 ? 24.705  78.667  5.548   1.00 24.71  ? 251 PHE D CD2 1 
ATOM   12023 C CE1 . PHE D 1 222 ? 22.669  76.823  5.562   1.00 24.49  ? 251 PHE D CE1 1 
ATOM   12024 C CE2 . PHE D 1 222 ? 24.234  78.126  4.360   1.00 28.34  ? 251 PHE D CE2 1 
ATOM   12025 C CZ  . PHE D 1 222 ? 23.229  77.191  4.370   1.00 24.78  ? 251 PHE D CZ  1 
ATOM   12026 N N   . THR D 1 223 ? 27.720  77.810  8.272   1.00 22.33  ? 252 THR D N   1 
ATOM   12027 C CA  . THR D 1 223 ? 28.928  77.141  7.813   1.00 22.56  ? 252 THR D CA  1 
ATOM   12028 C C   . THR D 1 223 ? 29.140  75.830  8.571   1.00 22.37  ? 252 THR D C   1 
ATOM   12029 O O   . THR D 1 223 ? 29.502  74.836  7.955   1.00 24.78  ? 252 THR D O   1 
ATOM   12030 C CB  . THR D 1 223 ? 30.177  78.031  7.867   1.00 25.36  ? 252 THR D CB  1 
ATOM   12031 O OG1 . THR D 1 223 ? 29.927  79.233  7.142   1.00 22.71  ? 252 THR D OG1 1 
ATOM   12032 C CG2 . THR D 1 223 ? 31.393  77.328  7.299   1.00 25.83  ? 252 THR D CG2 1 
ATOM   12033 N N   . GLU D 1 224 ? 28.971  75.840  9.896   1.00 21.34  ? 253 GLU D N   1 
ATOM   12034 C CA  . GLU D 1 224 ? 29.201  74.650  10.701  1.00 23.46  ? 253 GLU D CA  1 
ATOM   12035 C C   . GLU D 1 224 ? 28.161  73.577  10.367  1.00 21.10  ? 253 GLU D C   1 
ATOM   12036 O O   . GLU D 1 224 ? 28.470  72.381  10.379  1.00 19.19  ? 253 GLU D O   1 
ATOM   12037 C CB  . GLU D 1 224 ? 29.174  75.018  12.195  1.00 23.98  ? 253 GLU D CB  1 
ATOM   12038 C CG  . GLU D 1 224 ? 30.453  75.689  12.681  1.00 24.34  ? 253 GLU D CG  1 
ATOM   12039 C CD  . GLU D 1 224 ? 31.556  74.666  12.903  1.00 25.69  ? 253 GLU D CD  1 
ATOM   12040 O OE1 . GLU D 1 224 ? 31.516  74.002  13.937  1.00 30.01  ? 253 GLU D OE1 1 
ATOM   12041 O OE2 . GLU D 1 224 ? 32.417  74.503  12.016  1.00 27.03  ? 253 GLU D OE2 1 
ATOM   12042 N N   . LEU D 1 225 ? 26.915  73.999  10.114  1.00 21.78  ? 254 LEU D N   1 
ATOM   12043 C CA  . LEU D 1 225 ? 25.868  73.064  9.743   1.00 22.50  ? 254 LEU D CA  1 
ATOM   12044 C C   . LEU D 1 225 ? 26.197  72.441  8.380   1.00 20.00  ? 254 LEU D C   1 
ATOM   12045 O O   . LEU D 1 225 ? 25.982  71.255  8.167   1.00 18.52  ? 254 LEU D O   1 
ATOM   12046 C CB  . LEU D 1 225 ? 24.525  73.808  9.717   1.00 24.14  ? 254 LEU D CB  1 
ATOM   12047 C CG  . LEU D 1 225 ? 23.377  73.090  9.000   1.00 24.63  ? 254 LEU D CG  1 
ATOM   12048 C CD1 . LEU D 1 225 ? 22.982  71.822  9.716   1.00 24.54  ? 254 LEU D CD1 1 
ATOM   12049 C CD2 . LEU D 1 225 ? 22.168  74.000  8.856   1.00 26.14  ? 254 LEU D CD2 1 
ATOM   12050 N N   . THR D 1 226 ? 26.704  73.246  7.463   1.00 18.28  ? 255 THR D N   1 
ATOM   12051 C CA  . THR D 1 226 ? 27.060  72.800  6.125   1.00 20.02  ? 255 THR D CA  1 
ATOM   12052 C C   . THR D 1 226 ? 28.167  71.746  6.201   1.00 22.04  ? 255 THR D C   1 
ATOM   12053 O O   . THR D 1 226 ? 28.073  70.698  5.563   1.00 17.65  ? 255 THR D O   1 
ATOM   12054 C CB  . THR D 1 226 ? 27.432  74.007  5.268   1.00 21.72  ? 255 THR D CB  1 
ATOM   12055 O OG1 . THR D 1 226 ? 26.231  74.771  5.111   1.00 21.97  ? 255 THR D OG1 1 
ATOM   12056 C CG2 . THR D 1 226 ? 27.992  73.611  3.928   1.00 21.04  ? 255 THR D CG2 1 
ATOM   12057 N N   . ARG D 1 227 ? 29.193  72.019  7.029   1.00 21.87  ? 256 ARG D N   1 
ATOM   12058 C CA  . ARG D 1 227 ? 30.284  71.074  7.246   1.00 20.61  ? 256 ARG D CA  1 
ATOM   12059 C C   . ARG D 1 227 ? 29.682  69.744  7.703   1.00 21.65  ? 256 ARG D C   1 
ATOM   12060 O O   . ARG D 1 227 ? 29.993  68.702  7.135   1.00 19.81  ? 256 ARG D O   1 
ATOM   12061 C CB  . ARG D 1 227 ? 31.303  71.622  8.253   1.00 21.33  ? 256 ARG D CB  1 
ATOM   12062 C CG  . ARG D 1 227 ? 32.200  72.737  7.744   1.00 22.90  ? 256 ARG D CG  1 
ATOM   12063 C CD  . ARG D 1 227 ? 32.690  73.634  8.885   1.00 23.04  ? 256 ARG D CD  1 
ATOM   12064 N NE  . ARG D 1 227 ? 33.702  74.556  8.381   1.00 25.93  ? 256 ARG D NE  1 
ATOM   12065 C CZ  . ARG D 1 227 ? 34.061  75.703  8.962   1.00 26.05  ? 256 ARG D CZ  1 
ATOM   12066 N NH1 . ARG D 1 227 ? 33.519  76.098  10.097  1.00 26.62  ? 256 ARG D NH1 1 
ATOM   12067 N NH2 . ARG D 1 227 ? 34.968  76.463  8.385   1.00 24.68  ? 256 ARG D NH2 1 
ATOM   12068 N N   . LEU D 1 228 ? 28.817  69.787  8.728   1.00 22.67  ? 257 LEU D N   1 
ATOM   12069 C CA  . LEU D 1 228 ? 28.206  68.576  9.267   1.00 22.84  ? 257 LEU D CA  1 
ATOM   12070 C C   . LEU D 1 228 ? 27.367  67.907  8.175   1.00 22.47  ? 257 LEU D C   1 
ATOM   12071 O O   . LEU D 1 228 ? 27.499  66.718  7.939   1.00 23.97  ? 257 LEU D O   1 
ATOM   12072 C CB  . LEU D 1 228 ? 27.340  68.896  10.492  1.00 25.15  ? 257 LEU D CB  1 
ATOM   12073 C CG  . LEU D 1 228 ? 26.608  67.683  11.084  1.00 25.46  ? 257 LEU D CG  1 
ATOM   12074 C CD1 . LEU D 1 228 ? 27.611  66.718  11.699  1.00 26.82  ? 257 LEU D CD1 1 
ATOM   12075 C CD2 . LEU D 1 228 ? 25.573  68.056  12.128  1.00 27.05  ? 257 LEU D CD2 1 
ATOM   12076 N N   . TYR D 1 229 ? 26.471  68.678  7.550   1.00 21.09  ? 258 TYR D N   1 
ATOM   12077 C CA  . TYR D 1 229 ? 25.582  68.199  6.486   1.00 20.47  ? 258 TYR D CA  1 
ATOM   12078 C C   . TYR D 1 229 ? 26.358  67.456  5.402   1.00 19.21  ? 258 TYR D C   1 
ATOM   12079 O O   . TYR D 1 229 ? 26.012  66.322  5.053   1.00 19.15  ? 258 TYR D O   1 
ATOM   12080 C CB  . TYR D 1 229 ? 24.805  69.388  5.896   1.00 20.62  ? 258 TYR D CB  1 
ATOM   12081 C CG  . TYR D 1 229 ? 23.662  69.046  4.970   1.00 22.06  ? 258 TYR D CG  1 
ATOM   12082 C CD1 . TYR D 1 229 ? 23.882  68.558  3.684   1.00 24.13  ? 258 TYR D CD1 1 
ATOM   12083 C CD2 . TYR D 1 229 ? 22.349  69.289  5.342   1.00 24.48  ? 258 TYR D CD2 1 
ATOM   12084 C CE1 . TYR D 1 229 ? 22.830  68.254  2.826   1.00 23.68  ? 258 TYR D CE1 1 
ATOM   12085 C CE2 . TYR D 1 229 ? 21.291  69.017  4.491   1.00 25.57  ? 258 TYR D CE2 1 
ATOM   12086 C CZ  . TYR D 1 229 ? 21.529  68.520  3.219   1.00 25.42  ? 258 TYR D CZ  1 
ATOM   12087 O OH  . TYR D 1 229 ? 20.462  68.228  2.414   1.00 27.32  ? 258 TYR D OH  1 
ATOM   12088 N N   . LEU D 1 230 ? 27.450  68.069  4.929   1.00 18.89  ? 259 LEU D N   1 
ATOM   12089 C CA  . LEU D 1 230 ? 28.151  67.551  3.766   1.00 20.03  ? 259 LEU D CA  1 
ATOM   12090 C C   . LEU D 1 230 ? 28.944  66.331  4.195   1.00 20.76  ? 259 LEU D C   1 
ATOM   12091 O O   . LEU D 1 230 ? 29.179  65.445  3.365   1.00 20.51  ? 259 LEU D O   1 
ATOM   12092 C CB  . LEU D 1 230 ? 29.063  68.613  3.157   1.00 20.79  ? 259 LEU D CB  1 
ATOM   12093 C CG  . LEU D 1 230 ? 28.328  69.831  2.593   1.00 21.47  ? 259 LEU D CG  1 
ATOM   12094 C CD1 . LEU D 1 230 ? 29.278  70.801  1.964   1.00 19.57  ? 259 LEU D CD1 1 
ATOM   12095 C CD2 . LEU D 1 230 ? 27.255  69.440  1.587   1.00 22.54  ? 259 LEU D CD2 1 
ATOM   12096 N N   . THR D 1 231 ? 29.299  66.284  5.497   1.00 19.69  ? 260 THR D N   1 
ATOM   12097 C CA  . THR D 1 231 ? 29.962  65.099  6.020   1.00 19.27  ? 260 THR D CA  1 
ATOM   12098 C C   . THR D 1 231 ? 28.982  63.932  6.106   1.00 21.46  ? 260 THR D C   1 
ATOM   12099 O O   . THR D 1 231 ? 29.345  62.827  5.691   1.00 21.68  ? 260 THR D O   1 
ATOM   12100 C CB  . THR D 1 231 ? 30.626  65.355  7.375   1.00 20.08  ? 260 THR D CB  1 
ATOM   12101 O OG1 . THR D 1 231 ? 31.725  66.248  7.221   1.00 20.11  ? 260 THR D OG1 1 
ATOM   12102 C CG2 . THR D 1 231 ? 31.158  64.101  8.019   1.00 18.99  ? 260 THR D CG2 1 
ATOM   12103 N N   . ILE D 1 232 ? 27.804  64.128  6.724   1.00 21.03  ? 261 ILE D N   1 
ATOM   12104 C CA  . ILE D 1 232 ? 27.040  62.947  7.095   1.00 21.11  ? 261 ILE D CA  1 
ATOM   12105 C C   . ILE D 1 232 ? 26.193  62.423  5.939   1.00 20.92  ? 261 ILE D C   1 
ATOM   12106 O O   . ILE D 1 232 ? 25.669  61.328  6.056   1.00 21.44  ? 261 ILE D O   1 
ATOM   12107 C CB  . ILE D 1 232 ? 26.207  63.137  8.380   1.00 21.44  ? 261 ILE D CB  1 
ATOM   12108 C CG1 . ILE D 1 232 ? 25.063  64.127  8.186   1.00 21.29  ? 261 ILE D CG1 1 
ATOM   12109 C CG2 . ILE D 1 232 ? 27.130  63.523  9.533   1.00 21.18  ? 261 ILE D CG2 1 
ATOM   12110 C CD1 . ILE D 1 232 ? 24.239  64.318  9.399   1.00 20.20  ? 261 ILE D CD1 1 
ATOM   12111 N N   . HIS D 1 233 ? 26.073  63.159  4.828   1.00 21.64  ? 262 HIS D N   1 
ATOM   12112 C CA  . HIS D 1 233 ? 25.327  62.668  3.682   1.00 24.03  ? 262 HIS D CA  1 
ATOM   12113 C C   . HIS D 1 233 ? 26.271  62.085  2.628   1.00 22.14  ? 262 HIS D C   1 
ATOM   12114 O O   . HIS D 1 233 ? 25.833  61.855  1.514   1.00 21.00  ? 262 HIS D O   1 
ATOM   12115 C CB  . HIS D 1 233 ? 24.537  63.799  3.006   1.00 24.89  ? 262 HIS D CB  1 
ATOM   12116 C CG  . HIS D 1 233 ? 23.342  64.296  3.732   1.00 24.92  ? 262 HIS D CG  1 
ATOM   12117 N ND1 . HIS D 1 233 ? 23.433  65.216  4.748   1.00 26.51  ? 262 HIS D ND1 1 
ATOM   12118 C CD2 . HIS D 1 233 ? 22.024  64.106  3.513   1.00 24.16  ? 262 HIS D CD2 1 
ATOM   12119 C CE1 . HIS D 1 233 ? 22.199  65.532  5.155   1.00 25.98  ? 262 HIS D CE1 1 
ATOM   12120 N NE2 . HIS D 1 233 ? 21.330  64.863  4.430   1.00 21.73  ? 262 HIS D NE2 1 
ATOM   12121 N N   . SER D 1 234 ? 27.544  61.836  2.986   1.00 20.12  ? 263 SER D N   1 
ATOM   12122 C CA  . SER D 1 234 ? 28.577  61.677  1.988   1.00 18.61  ? 263 SER D CA  1 
ATOM   12123 C C   . SER D 1 234 ? 28.442  60.320  1.308   1.00 17.58  ? 263 SER D C   1 
ATOM   12124 O O   . SER D 1 234 ? 28.683  60.209  0.103   1.00 17.02  ? 263 SER D O   1 
ATOM   12125 C CB  . SER D 1 234 ? 29.944  61.821  2.593   1.00 18.90  ? 263 SER D CB  1 
ATOM   12126 O OG  . SER D 1 234 ? 30.103  60.908  3.648   1.00 19.76  ? 263 SER D OG  1 
ATOM   12127 N N   . ASP D 1 235 ? 28.065  59.335  2.128   1.00 18.19  ? 264 ASP D N   1 
ATOM   12128 C CA  . ASP D 1 235 ? 28.015  57.933  1.647   1.00 20.73  ? 264 ASP D CA  1 
ATOM   12129 C C   . ASP D 1 235 ? 27.036  57.127  2.493   1.00 20.83  ? 264 ASP D C   1 
ATOM   12130 O O   . ASP D 1 235 ? 26.882  57.455  3.664   1.00 20.97  ? 264 ASP D O   1 
ATOM   12131 C CB  . ASP D 1 235 ? 29.392  57.309  1.719   1.00 21.33  ? 264 ASP D CB  1 
ATOM   12132 C CG  . ASP D 1 235 ? 29.759  56.359  0.587   1.00 24.03  ? 264 ASP D CG  1 
ATOM   12133 O OD1 . ASP D 1 235 ? 29.256  56.547  -0.534  1.00 20.62  ? 264 ASP D OD1 1 
ATOM   12134 O OD2 . ASP D 1 235 ? 30.557  55.444  0.840   1.00 29.43  ? 264 ASP D OD2 1 
ATOM   12135 N N   . HIS D 1 236 ? 26.443  56.088  1.904   1.00 21.10  ? 265 HIS D N   1 
ATOM   12136 C CA  . HIS D 1 236 ? 25.453  55.232  2.603   1.00 20.14  ? 265 HIS D CA  1 
ATOM   12137 C C   . HIS D 1 236 ? 25.521  53.859  1.939   1.00 20.49  ? 265 HIS D C   1 
ATOM   12138 O O   . HIS D 1 236 ? 24.512  53.328  1.483   1.00 18.73  ? 265 HIS D O   1 
ATOM   12139 C CB  . HIS D 1 236 ? 24.063  55.852  2.601   1.00 19.89  ? 265 HIS D CB  1 
ATOM   12140 C CG  . HIS D 1 236 ? 23.353  55.552  3.867   1.00 19.96  ? 265 HIS D CG  1 
ATOM   12141 N ND1 . HIS D 1 236 ? 23.996  55.694  5.071   1.00 21.23  ? 265 HIS D ND1 1 
ATOM   12142 C CD2 . HIS D 1 236 ? 22.132  55.109  4.151   1.00 18.99  ? 265 HIS D CD2 1 
ATOM   12143 C CE1 . HIS D 1 236 ? 23.168  55.358  6.036   1.00 20.16  ? 265 HIS D CE1 1 
ATOM   12144 N NE2 . HIS D 1 236 ? 22.030  55.001  5.507   1.00 20.72  ? 265 HIS D NE2 1 
ATOM   12145 N N   . GLU D 1 237 ? 26.735  53.335  1.908   1.00 19.63  ? 266 GLU D N   1 
ATOM   12146 C CA  . GLU D 1 237 ? 26.995  52.029  1.251   1.00 20.43  ? 266 GLU D CA  1 
ATOM   12147 C C   . GLU D 1 237 ? 26.683  52.149  -0.256  1.00 18.53  ? 266 GLU D C   1 
ATOM   12148 O O   . GLU D 1 237 ? 26.483  53.265  -0.749  1.00 18.17  ? 266 GLU D O   1 
ATOM   12149 C CB  . GLU D 1 237 ? 26.442  50.857  2.075   1.00 21.98  ? 266 GLU D CB  1 
ATOM   12150 C CG  . GLU D 1 237 ? 25.074  50.312  1.687   1.00 25.26  ? 266 GLU D CG  1 
ATOM   12151 C CD  . GLU D 1 237 ? 24.897  48.934  2.299   1.00 25.08  ? 266 GLU D CD  1 
ATOM   12152 O OE1 . GLU D 1 237 ? 25.721  48.560  3.156   1.00 23.89  ? 266 GLU D OE1 1 
ATOM   12153 O OE2 . GLU D 1 237 ? 23.943  48.241  1.916   1.00 23.12  ? 266 GLU D OE2 1 
ATOM   12154 N N   . GLY D 1 238 ? 26.724  51.035  -0.965  1.00 17.52  ? 267 GLY D N   1 
ATOM   12155 C CA  . GLY D 1 238 ? 26.615  51.126  -2.435  1.00 16.91  ? 267 GLY D CA  1 
ATOM   12156 C C   . GLY D 1 238 ? 25.277  50.703  -2.987  1.00 18.19  ? 267 GLY D C   1 
ATOM   12157 O O   . GLY D 1 238 ? 25.114  50.778  -4.201  1.00 18.80  ? 267 GLY D O   1 
ATOM   12158 N N   . GLY D 1 239 ? 24.374  50.271  -2.118  1.00 20.27  ? 268 GLY D N   1 
ATOM   12159 C CA  . GLY D 1 239 ? 23.055  49.798  -2.555  1.00 19.71  ? 268 GLY D CA  1 
ATOM   12160 C C   . GLY D 1 239 ? 22.013  50.900  -2.625  1.00 20.81  ? 268 GLY D C   1 
ATOM   12161 O O   . GLY D 1 239 ? 20.918  50.642  -3.111  1.00 20.63  ? 268 GLY D O   1 
ATOM   12162 N N   . ASN D 1 240 ? 22.353  52.093  -2.155  1.00 18.69  ? 269 ASN D N   1 
ATOM   12163 C CA  . ASN D 1 240 ? 21.374  53.160  -2.304  1.00 17.35  ? 269 ASN D CA  1 
ATOM   12164 C C   . ASN D 1 240 ? 21.288  53.559  -3.775  1.00 17.36  ? 269 ASN D C   1 
ATOM   12165 O O   . ASN D 1 240 ? 22.218  53.282  -4.550  1.00 15.13  ? 269 ASN D O   1 
ATOM   12166 C CB  . ASN D 1 240 ? 21.678  54.344  -1.384  1.00 17.81  ? 269 ASN D CB  1 
ATOM   12167 C CG  . ASN D 1 240 ? 22.928  55.119  -1.706  1.00 19.45  ? 269 ASN D CG  1 
ATOM   12168 O OD1 . ASN D 1 240 ? 22.942  55.917  -2.636  1.00 18.48  ? 269 ASN D OD1 1 
ATOM   12169 N ND2 . ASN D 1 240 ? 23.974  54.921  -0.925  1.00 20.54  ? 269 ASN D ND2 1 
ATOM   12170 N N   . VAL D 1 241 ? 20.175  54.208  -4.190  1.00 16.55  ? 270 VAL D N   1 
ATOM   12171 C CA  . VAL D 1 241 ? 20.003  54.442  -5.624  1.00 16.48  ? 270 VAL D CA  1 
ATOM   12172 C C   . VAL D 1 241 ? 21.140  55.280  -6.216  1.00 14.75  ? 270 VAL D C   1 
ATOM   12173 O O   . VAL D 1 241 ? 21.591  55.004  -7.321  1.00 15.35  ? 270 VAL D O   1 
ATOM   12174 C CB  . VAL D 1 241 ? 18.621  55.022  -5.999  1.00 17.03  ? 270 VAL D CB  1 
ATOM   12175 C CG1 . VAL D 1 241 ? 18.575  55.499  -7.434  1.00 17.85  ? 270 VAL D CG1 1 
ATOM   12176 C CG2 . VAL D 1 241 ? 17.524  54.002  -5.775  1.00 17.47  ? 270 VAL D CG2 1 
ATOM   12177 N N   . SER D 1 242 ? 21.547  56.365  -5.563  1.00 15.35  ? 271 SER D N   1 
ATOM   12178 C CA  . SER D 1 242 ? 22.495  57.258  -6.195  1.00 17.32  ? 271 SER D CA  1 
ATOM   12179 C C   . SER D 1 242 ? 23.862  56.570  -6.294  1.00 16.94  ? 271 SER D C   1 
ATOM   12180 O O   . SER D 1 242 ? 24.515  56.625  -7.335  1.00 16.58  ? 271 SER D O   1 
ATOM   12181 C CB  . SER D 1 242 ? 22.539  58.628  -5.499  1.00 17.26  ? 271 SER D CB  1 
ATOM   12182 O OG  . SER D 1 242 ? 22.741  58.539  -4.096  1.00 14.88  ? 271 SER D OG  1 
ATOM   12183 N N   . ALA D 1 243 ? 24.256  55.871  -5.236  1.00 17.30  ? 272 ALA D N   1 
ATOM   12184 C CA  . ALA D 1 243 ? 25.565  55.245  -5.183  1.00 17.66  ? 272 ALA D CA  1 
ATOM   12185 C C   . ALA D 1 243 ? 25.603  54.106  -6.207  1.00 18.69  ? 272 ALA D C   1 
ATOM   12186 O O   . ALA D 1 243 ? 26.511  53.970  -7.039  1.00 18.43  ? 272 ALA D O   1 
ATOM   12187 C CB  . ALA D 1 243 ? 25.842  54.775  -3.775  1.00 19.19  ? 272 ALA D CB  1 
ATOM   12188 N N   . HIS D 1 244 ? 24.548  53.293  -6.158  1.00 17.77  ? 273 HIS D N   1 
ATOM   12189 C CA  . HIS D 1 244 ? 24.428  52.187  -7.091  1.00 18.24  ? 273 HIS D CA  1 
ATOM   12190 C C   . HIS D 1 244 ? 24.388  52.668  -8.540  1.00 18.28  ? 273 HIS D C   1 
ATOM   12191 O O   . HIS D 1 244 ? 24.982  52.069  -9.435  1.00 18.50  ? 273 HIS D O   1 
ATOM   12192 C CB  . HIS D 1 244 ? 23.183  51.380  -6.767  1.00 16.31  ? 273 HIS D CB  1 
ATOM   12193 C CG  . HIS D 1 244 ? 23.107  50.077  -7.510  1.00 17.44  ? 273 HIS D CG  1 
ATOM   12194 N ND1 . HIS D 1 244 ? 21.904  49.431  -7.577  1.00 18.33  ? 273 HIS D ND1 1 
ATOM   12195 C CD2 . HIS D 1 244 ? 23.975  49.342  -8.213  1.00 18.55  ? 273 HIS D CD2 1 
ATOM   12196 C CE1 . HIS D 1 244 ? 22.054  48.302  -8.272  1.00 18.86  ? 273 HIS D CE1 1 
ATOM   12197 N NE2 . HIS D 1 244 ? 23.310  48.231  -8.659  1.00 18.11  ? 273 HIS D NE2 1 
ATOM   12198 N N   . THR D 1 245 ? 23.730  53.794  -8.797  1.00 16.46  ? 274 THR D N   1 
ATOM   12199 C CA  . THR D 1 245 ? 23.683  54.286  -10.156 1.00 17.62  ? 274 THR D CA  1 
ATOM   12200 C C   . THR D 1 245 ? 25.084  54.708  -10.596 1.00 17.00  ? 274 THR D C   1 
ATOM   12201 O O   . THR D 1 245 ? 25.461  54.443  -11.727 1.00 15.02  ? 274 THR D O   1 
ATOM   12202 C CB  . THR D 1 245 ? 22.701  55.439  -10.366 1.00 16.59  ? 274 THR D CB  1 
ATOM   12203 O OG1 . THR D 1 245 ? 21.387  54.966  -10.058 1.00 16.03  ? 274 THR D OG1 1 
ATOM   12204 C CG2 . THR D 1 245 ? 22.764  55.932  -11.798 1.00 15.84  ? 274 THR D CG2 1 
ATOM   12205 N N   . SER D 1 246 ? 25.783  55.490  -9.767  1.00 20.12  ? 275 SER D N   1 
ATOM   12206 C CA  . SER D 1 246 ? 27.151  55.880  -10.095 1.00 21.62  ? 275 SER D CA  1 
ATOM   12207 C C   . SER D 1 246 ? 27.989  54.647  -10.400 1.00 19.29  ? 275 SER D C   1 
ATOM   12208 O O   . SER D 1 246 ? 28.801  54.690  -11.331 1.00 17.77  ? 275 SER D O   1 
ATOM   12209 C CB  . SER D 1 246 ? 27.802  56.682  -9.005  1.00 23.35  ? 275 SER D CB  1 
ATOM   12210 O OG  . SER D 1 246 ? 28.113  55.873  -7.887  1.00 24.52  ? 275 SER D OG  1 
ATOM   12211 N N   . HIS D 1 247 ? 27.783  53.611  -9.569  1.00 19.29  ? 276 HIS D N   1 
ATOM   12212 C CA  . HIS D 1 247 ? 28.533  52.355  -9.614  1.00 17.56  ? 276 HIS D CA  1 
ATOM   12213 C C   . HIS D 1 247 ? 28.290  51.653  -10.947 1.00 18.27  ? 276 HIS D C   1 
ATOM   12214 O O   . HIS D 1 247 ? 29.208  51.191  -11.638 1.00 17.76  ? 276 HIS D O   1 
ATOM   12215 C CB  . HIS D 1 247 ? 28.113  51.485  -8.426  1.00 18.25  ? 276 HIS D CB  1 
ATOM   12216 C CG  . HIS D 1 247 ? 29.001  50.301  -8.249  1.00 18.96  ? 276 HIS D CG  1 
ATOM   12217 N ND1 . HIS D 1 247 ? 28.655  48.968  -8.338  1.00 23.25  ? 276 HIS D ND1 1 
ATOM   12218 C CD2 . HIS D 1 247 ? 30.301  50.336  -7.967  1.00 18.89  ? 276 HIS D CD2 1 
ATOM   12219 C CE1 . HIS D 1 247 ? 29.727  48.244  -8.084  1.00 17.97  ? 276 HIS D CE1 1 
ATOM   12220 N NE2 . HIS D 1 247 ? 30.729  49.062  -7.868  1.00 19.47  ? 276 HIS D NE2 1 
ATOM   12221 N N   . LEU D 1 248 ? 26.998  51.569  -11.308 1.00 17.37  ? 277 LEU D N   1 
ATOM   12222 C CA  . LEU D 1 248 ? 26.546  50.862  -12.482 1.00 16.94  ? 277 LEU D CA  1 
ATOM   12223 C C   . LEU D 1 248 ? 27.034  51.605  -13.735 1.00 19.11  ? 277 LEU D C   1 
ATOM   12224 O O   . LEU D 1 248 ? 27.609  51.016  -14.634 1.00 20.52  ? 277 LEU D O   1 
ATOM   12225 C CB  . LEU D 1 248 ? 25.023  50.775  -12.355 1.00 16.59  ? 277 LEU D CB  1 
ATOM   12226 C CG  . LEU D 1 248 ? 24.229  50.394  -13.596 1.00 17.09  ? 277 LEU D CG  1 
ATOM   12227 C CD1 . LEU D 1 248 ? 24.612  49.018  -14.099 1.00 18.32  ? 277 LEU D CD1 1 
ATOM   12228 C CD2 . LEU D 1 248 ? 22.735  50.437  -13.317 1.00 17.53  ? 277 LEU D CD2 1 
ATOM   12229 N N   . VAL D 1 249 ? 26.869  52.946  -13.772 1.00 19.40  ? 278 VAL D N   1 
ATOM   12230 C CA  . VAL D 1 249 ? 27.252  53.718  -14.934 1.00 16.56  ? 278 VAL D CA  1 
ATOM   12231 C C   . VAL D 1 249 ? 28.776  53.730  -15.090 1.00 16.51  ? 278 VAL D C   1 
ATOM   12232 O O   . VAL D 1 249 ? 29.267  53.618  -16.215 1.00 18.05  ? 278 VAL D O   1 
ATOM   12233 C CB  . VAL D 1 249 ? 26.633  55.133  -14.894 1.00 16.05  ? 278 VAL D CB  1 
ATOM   12234 C CG1 . VAL D 1 249 ? 27.173  56.032  -15.990 1.00 18.14  ? 278 VAL D CG1 1 
ATOM   12235 C CG2 . VAL D 1 249 ? 25.129  55.008  -14.971 1.00 15.23  ? 278 VAL D CG2 1 
ATOM   12236 N N   . GLY D 1 250 ? 29.503  53.850  -13.978 1.00 15.09  ? 279 GLY D N   1 
ATOM   12237 C CA  . GLY D 1 250 ? 30.947  53.888  -14.025 1.00 15.12  ? 279 GLY D CA  1 
ATOM   12238 C C   . GLY D 1 250 ? 31.510  52.521  -14.416 1.00 15.59  ? 279 GLY D C   1 
ATOM   12239 O O   . GLY D 1 250 ? 32.610  52.442  -14.952 1.00 17.19  ? 279 GLY D O   1 
ATOM   12240 N N   . SER D 1 251 ? 30.742  51.456  -14.169 1.00 16.87  ? 280 SER D N   1 
ATOM   12241 C CA  . SER D 1 251 ? 31.221  50.122  -14.518 1.00 15.98  ? 280 SER D CA  1 
ATOM   12242 C C   . SER D 1 251 ? 31.348  49.954  -16.035 1.00 17.91  ? 280 SER D C   1 
ATOM   12243 O O   . SER D 1 251 ? 32.018  49.037  -16.510 1.00 16.32  ? 280 SER D O   1 
ATOM   12244 C CB  . SER D 1 251 ? 30.320  49.077  -13.962 1.00 17.71  ? 280 SER D CB  1 
ATOM   12245 O OG  . SER D 1 251 ? 29.095  48.957  -14.702 1.00 19.14  ? 280 SER D OG  1 
ATOM   12246 N N   . ALA D 1 252 ? 30.654  50.810  -16.792 1.00 17.68  ? 281 ALA D N   1 
ATOM   12247 C CA  . ALA D 1 252 ? 30.744  50.859  -18.245 1.00 18.11  ? 281 ALA D CA  1 
ATOM   12248 C C   . ALA D 1 252 ? 31.879  51.759  -18.724 1.00 18.29  ? 281 ALA D C   1 
ATOM   12249 O O   . ALA D 1 252 ? 32.069  51.904  -19.936 1.00 18.61  ? 281 ALA D O   1 
ATOM   12250 C CB  . ALA D 1 252 ? 29.427  51.302  -18.823 1.00 19.81  ? 281 ALA D CB  1 
ATOM   12251 N N   . LEU D 1 253 ? 32.646  52.288  -17.773 1.00 18.78  ? 282 LEU D N   1 
ATOM   12252 C CA  . LEU D 1 253 ? 33.806  53.137  -17.990 1.00 19.35  ? 282 LEU D CA  1 
ATOM   12253 C C   . LEU D 1 253 ? 33.326  54.515  -18.406 1.00 21.40  ? 282 LEU D C   1 
ATOM   12254 O O   . LEU D 1 253 ? 34.089  55.258  -19.037 1.00 20.25  ? 282 LEU D O   1 
ATOM   12255 C CB  . LEU D 1 253 ? 34.808  52.548  -18.983 1.00 19.58  ? 282 LEU D CB  1 
ATOM   12256 C CG  . LEU D 1 253 ? 35.466  51.239  -18.536 1.00 20.36  ? 282 LEU D CG  1 
ATOM   12257 C CD1 . LEU D 1 253 ? 36.671  50.885  -19.400 1.00 18.55  ? 282 LEU D CD1 1 
ATOM   12258 C CD2 . LEU D 1 253 ? 35.853  51.295  -17.071 1.00 20.18  ? 282 LEU D CD2 1 
ATOM   12259 N N   . SER D 1 254 ? 32.058  54.828  -18.071 1.00 20.99  ? 283 SER D N   1 
ATOM   12260 C CA  . SER D 1 254 ? 31.637  56.225  -18.119 1.00 21.32  ? 283 SER D CA  1 
ATOM   12261 C C   . SER D 1 254 ? 32.490  57.009  -17.125 1.00 22.90  ? 283 SER D C   1 
ATOM   12262 O O   . SER D 1 254 ? 32.877  56.515  -16.072 1.00 25.83  ? 283 SER D O   1 
ATOM   12263 C CB  . SER D 1 254 ? 30.155  56.412  -17.872 1.00 22.50  ? 283 SER D CB  1 
ATOM   12264 O OG  . SER D 1 254 ? 29.388  55.815  -18.912 1.00 23.24  ? 283 SER D OG  1 
ATOM   12265 N N   . ASP D 1 255 ? 32.815  58.248  -17.501 1.00 22.91  ? 284 ASP D N   1 
ATOM   12266 C CA  . ASP D 1 255 ? 33.728  59.058  -16.718 1.00 22.57  ? 284 ASP D CA  1 
ATOM   12267 C C   . ASP D 1 255 ? 32.999  59.516  -15.453 1.00 18.77  ? 284 ASP D C   1 
ATOM   12268 O O   . ASP D 1 255 ? 31.797  59.291  -15.335 1.00 19.78  ? 284 ASP D O   1 
ATOM   12269 C CB  . ASP D 1 255 ? 34.291  60.208  -17.558 1.00 22.61  ? 284 ASP D CB  1 
ATOM   12270 C CG  . ASP D 1 255 ? 33.249  61.172  -18.084 1.00 25.13  ? 284 ASP D CG  1 
ATOM   12271 O OD1 . ASP D 1 255 ? 32.601  61.828  -17.237 1.00 25.23  ? 284 ASP D OD1 1 
ATOM   12272 O OD2 . ASP D 1 255 ? 33.127  61.285  -19.344 1.00 22.06  ? 284 ASP D OD2 1 
ATOM   12273 N N   . PRO D 1 256 ? 33.692  60.117  -14.468 1.00 20.90  ? 285 PRO D N   1 
ATOM   12274 C CA  . PRO D 1 256 ? 33.042  60.564  -13.232 1.00 19.66  ? 285 PRO D CA  1 
ATOM   12275 C C   . PRO D 1 256 ? 31.916  61.592  -13.411 1.00 20.07  ? 285 PRO D C   1 
ATOM   12276 O O   . PRO D 1 256 ? 31.001  61.661  -12.588 1.00 20.23  ? 285 PRO D O   1 
ATOM   12277 C CB  . PRO D 1 256 ? 34.211  61.189  -12.464 1.00 21.48  ? 285 PRO D CB  1 
ATOM   12278 C CG  . PRO D 1 256 ? 35.394  60.359  -12.907 1.00 21.55  ? 285 PRO D CG  1 
ATOM   12279 C CD  . PRO D 1 256 ? 35.159  60.244  -14.392 1.00 19.68  ? 285 PRO D CD  1 
ATOM   12280 N N   . TYR D 1 257 ? 32.023  62.463  -14.424 1.00 19.20  ? 286 TYR D N   1 
ATOM   12281 C CA  . TYR D 1 257 ? 30.976  63.454  -14.643 1.00 20.60  ? 286 TYR D CA  1 
ATOM   12282 C C   . TYR D 1 257 ? 29.663  62.738  -15.006 1.00 19.94  ? 286 TYR D C   1 
ATOM   12283 O O   . TYR D 1 257 ? 28.652  62.940  -14.350 1.00 18.87  ? 286 TYR D O   1 
ATOM   12284 C CB  . TYR D 1 257 ? 31.388  64.518  -15.671 1.00 23.39  ? 286 TYR D CB  1 
ATOM   12285 C CG  . TYR D 1 257 ? 32.613  65.311  -15.273 1.00 22.70  ? 286 TYR D CG  1 
ATOM   12286 C CD1 . TYR D 1 257 ? 33.892  64.869  -15.578 1.00 26.42  ? 286 TYR D CD1 1 
ATOM   12287 C CD2 . TYR D 1 257 ? 32.493  66.517  -14.620 1.00 24.07  ? 286 TYR D CD2 1 
ATOM   12288 C CE1 . TYR D 1 257 ? 35.018  65.600  -15.217 1.00 26.92  ? 286 TYR D CE1 1 
ATOM   12289 C CE2 . TYR D 1 257 ? 33.601  67.265  -14.248 1.00 25.02  ? 286 TYR D CE2 1 
ATOM   12290 C CZ  . TYR D 1 257 ? 34.870  66.802  -14.540 1.00 27.08  ? 286 TYR D CZ  1 
ATOM   12291 O OH  . TYR D 1 257 ? 35.962  67.543  -14.160 1.00 26.41  ? 286 TYR D OH  1 
ATOM   12292 N N   . LEU D 1 258 ? 29.710  61.824  -15.988 1.00 19.74  ? 287 LEU D N   1 
ATOM   12293 C CA  . LEU D 1 258 ? 28.543  61.096  -16.459 1.00 19.50  ? 287 LEU D CA  1 
ATOM   12294 C C   . LEU D 1 258 ? 27.986  60.220  -15.336 1.00 21.60  ? 287 LEU D C   1 
ATOM   12295 O O   . LEU D 1 258 ? 26.769  60.137  -15.169 1.00 17.18  ? 287 LEU D O   1 
ATOM   12296 C CB  . LEU D 1 258 ? 28.914  60.281  -17.712 1.00 20.46  ? 287 LEU D CB  1 
ATOM   12297 C CG  . LEU D 1 258 ? 29.303  61.082  -18.956 1.00 21.74  ? 287 LEU D CG  1 
ATOM   12298 C CD1 . LEU D 1 258 ? 29.247  60.208  -20.211 1.00 22.45  ? 287 LEU D CD1 1 
ATOM   12299 C CD2 . LEU D 1 258 ? 28.413  62.313  -19.149 1.00 21.62  ? 287 LEU D CD2 1 
ATOM   12300 N N   . SER D 1 259 ? 28.884  59.596  -14.549 1.00 19.77  ? 288 SER D N   1 
ATOM   12301 C CA  . SER D 1 259 ? 28.484  58.685  -13.482 1.00 19.84  ? 288 SER D CA  1 
ATOM   12302 C C   . SER D 1 259 ? 27.793  59.429  -12.355 1.00 20.15  ? 288 SER D C   1 
ATOM   12303 O O   . SER D 1 259 ? 26.755  58.987  -11.865 1.00 21.44  ? 288 SER D O   1 
ATOM   12304 C CB  . SER D 1 259 ? 29.687  57.929  -12.989 1.00 21.06  ? 288 SER D CB  1 
ATOM   12305 O OG  . SER D 1 259 ? 30.340  57.355  -14.099 1.00 24.34  ? 288 SER D OG  1 
ATOM   12306 N N   . PHE D 1 260 ? 28.318  60.610  -12.032 1.00 18.19  ? 289 PHE D N   1 
ATOM   12307 C CA  . PHE D 1 260 ? 27.749  61.409  -10.959 1.00 20.47  ? 289 PHE D CA  1 
ATOM   12308 C C   . PHE D 1 260 ? 26.413  62.006  -11.411 1.00 19.35  ? 289 PHE D C   1 
ATOM   12309 O O   . PHE D 1 260 ? 25.455  62.015  -10.657 1.00 18.89  ? 289 PHE D O   1 
ATOM   12310 C CB  . PHE D 1 260 ? 28.722  62.510  -10.527 1.00 21.14  ? 289 PHE D CB  1 
ATOM   12311 C CG  . PHE D 1 260 ? 28.185  63.356  -9.402  1.00 21.75  ? 289 PHE D CG  1 
ATOM   12312 C CD1 . PHE D 1 260 ? 28.084  62.848  -8.124  1.00 24.43  ? 289 PHE D CD1 1 
ATOM   12313 C CD2 . PHE D 1 260 ? 27.673  64.611  -9.658  1.00 23.54  ? 289 PHE D CD2 1 
ATOM   12314 C CE1 . PHE D 1 260 ? 27.536  63.604  -7.095  1.00 25.44  ? 289 PHE D CE1 1 
ATOM   12315 C CE2 . PHE D 1 260 ? 27.109  65.360  -8.637  1.00 23.58  ? 289 PHE D CE2 1 
ATOM   12316 C CZ  . PHE D 1 260 ? 27.048  64.862  -7.366  1.00 22.73  ? 289 PHE D CZ  1 
ATOM   12317 N N   . ALA D 1 261 ? 26.336  62.457  -12.673 1.00 17.93  ? 290 ALA D N   1 
ATOM   12318 C CA  . ALA D 1 261 ? 25.117  63.059  -13.204 1.00 19.21  ? 290 ALA D CA  1 
ATOM   12319 C C   . ALA D 1 261 ? 23.960  62.063  -13.187 1.00 18.77  ? 290 ALA D C   1 
ATOM   12320 O O   . ALA D 1 261 ? 22.829  62.397  -12.798 1.00 16.89  ? 290 ALA D O   1 
ATOM   12321 C CB  . ALA D 1 261 ? 25.386  63.599  -14.598 1.00 20.18  ? 290 ALA D CB  1 
ATOM   12322 N N   . ALA D 1 262 ? 24.246  60.835  -13.633 1.00 16.07  ? 291 ALA D N   1 
ATOM   12323 C CA  . ALA D 1 262 ? 23.312  59.746  -13.497 1.00 16.31  ? 291 ALA D CA  1 
ATOM   12324 C C   . ALA D 1 262 ? 22.876  59.564  -12.038 1.00 15.34  ? 291 ALA D C   1 
ATOM   12325 O O   . ALA D 1 262 ? 21.682  59.417  -11.771 1.00 14.65  ? 291 ALA D O   1 
ATOM   12326 C CB  . ALA D 1 262 ? 23.952  58.490  -14.029 1.00 16.79  ? 291 ALA D CB  1 
ATOM   12327 N N   . ALA D 1 263 ? 23.841  59.551  -11.116 1.00 15.78  ? 292 ALA D N   1 
ATOM   12328 C CA  . ALA D 1 263 ? 23.610  59.408  -9.680  1.00 15.95  ? 292 ALA D CA  1 
ATOM   12329 C C   . ALA D 1 263 ? 22.625  60.482  -9.184  1.00 16.23  ? 292 ALA D C   1 
ATOM   12330 O O   . ALA D 1 263 ? 21.726  60.234  -8.387  1.00 16.31  ? 292 ALA D O   1 
ATOM   12331 C CB  . ALA D 1 263 ? 24.944  59.486  -8.985  1.00 18.89  ? 292 ALA D CB  1 
ATOM   12332 N N   . MET D 1 264 ? 22.823  61.701  -9.673  1.00 17.00  ? 293 MET D N   1 
ATOM   12333 C CA  . MET D 1 264 ? 21.970  62.821  -9.298  1.00 17.57  ? 293 MET D CA  1 
ATOM   12334 C C   . MET D 1 264 ? 20.533  62.614  -9.783  1.00 17.83  ? 293 MET D C   1 
ATOM   12335 O O   . MET D 1 264 ? 19.624  62.924  -9.037  1.00 18.43  ? 293 MET D O   1 
ATOM   12336 C CB  . MET D 1 264 ? 22.517  64.141  -9.853  1.00 17.99  ? 293 MET D CB  1 
ATOM   12337 C CG  . MET D 1 264 ? 23.778  64.636  -9.139  1.00 18.39  ? 293 MET D CG  1 
ATOM   12338 S SD  . MET D 1 264 ? 23.695  64.597  -7.356  1.00 19.46  ? 293 MET D SD  1 
ATOM   12339 C CE  . MET D 1 264 ? 24.166  62.906  -6.989  1.00 16.95  ? 293 MET D CE  1 
ATOM   12340 N N   . ASN D 1 265 ? 20.316  62.163  -11.028 1.00 17.25  ? 294 ASN D N   1 
ATOM   12341 C CA  . ASN D 1 265 ? 18.981  61.821  -11.509 1.00 16.13  ? 294 ASN D CA  1 
ATOM   12342 C C   . ASN D 1 265 ? 18.316  60.835  -10.545 1.00 16.87  ? 294 ASN D C   1 
ATOM   12343 O O   . ASN D 1 265 ? 17.118  60.918  -10.313 1.00 17.07  ? 294 ASN D O   1 
ATOM   12344 C CB  . ASN D 1 265 ? 19.013  61.347  -12.963 1.00 19.10  ? 294 ASN D CB  1 
ATOM   12345 C CG  . ASN D 1 265 ? 19.290  62.473  -13.935 1.00 20.83  ? 294 ASN D CG  1 
ATOM   12346 O OD1 . ASN D 1 265 ? 19.488  63.614  -13.530 1.00 23.74  ? 294 ASN D OD1 1 
ATOM   12347 N ND2 . ASN D 1 265 ? 19.280  62.171  -15.220 1.00 23.73  ? 294 ASN D ND2 1 
ATOM   12348 N N   . GLY D 1 266 ? 19.071  59.857  -10.023 1.00 18.42  ? 295 GLY D N   1 
ATOM   12349 C CA  . GLY D 1 266 ? 18.518  58.946  -9.026  1.00 19.63  ? 295 GLY D CA  1 
ATOM   12350 C C   . GLY D 1 266 ? 18.183  59.644  -7.697  1.00 18.70  ? 295 GLY D C   1 
ATOM   12351 O O   . GLY D 1 266 ? 17.151  59.390  -7.097  1.00 18.39  ? 295 GLY D O   1 
ATOM   12352 N N   . LEU D 1 267 ? 19.113  60.470  -7.224  1.00 17.01  ? 296 LEU D N   1 
ATOM   12353 C CA  . LEU D 1 267 ? 18.954  61.185  -5.964  1.00 16.11  ? 296 LEU D CA  1 
ATOM   12354 C C   . LEU D 1 267 ? 17.724  62.091  -6.055  1.00 15.10  ? 296 LEU D C   1 
ATOM   12355 O O   . LEU D 1 267 ? 17.079  62.307  -5.053  1.00 16.02  ? 296 LEU D O   1 
ATOM   12356 C CB  . LEU D 1 267 ? 20.192  62.038  -5.718  1.00 16.80  ? 296 LEU D CB  1 
ATOM   12357 C CG  . LEU D 1 267 ? 20.344  62.626  -4.311  1.00 17.82  ? 296 LEU D CG  1 
ATOM   12358 C CD1 . LEU D 1 267 ? 20.457  61.557  -3.245  1.00 18.91  ? 296 LEU D CD1 1 
ATOM   12359 C CD2 . LEU D 1 267 ? 21.561  63.533  -4.266  1.00 17.15  ? 296 LEU D CD2 1 
ATOM   12360 N N   . ALA D 1 268 ? 17.419  62.590  -7.251  1.00 16.25  ? 297 ALA D N   1 
ATOM   12361 C CA  . ALA D 1 268 ? 16.296  63.524  -7.468  1.00 14.58  ? 297 ALA D CA  1 
ATOM   12362 C C   . ALA D 1 268 ? 14.946  62.827  -7.390  1.00 15.86  ? 297 ALA D C   1 
ATOM   12363 O O   . ALA D 1 268 ? 13.901  63.463  -7.472  1.00 18.43  ? 297 ALA D O   1 
ATOM   12364 C CB  . ALA D 1 268 ? 16.440  64.212  -8.797  1.00 15.27  ? 297 ALA D CB  1 
ATOM   12365 N N   . GLY D 1 269 ? 14.936  61.511  -7.246  1.00 15.82  ? 298 GLY D N   1 
ATOM   12366 C CA  . GLY D 1 269 ? 13.686  60.811  -7.071  1.00 17.01  ? 298 GLY D CA  1 
ATOM   12367 C C   . GLY D 1 269 ? 13.057  61.018  -5.690  1.00 15.70  ? 298 GLY D C   1 
ATOM   12368 O O   . GLY D 1 269 ? 13.745  60.979  -4.647  1.00 16.34  ? 298 GLY D O   1 
ATOM   12369 N N   . PRO D 1 270 ? 11.713  61.146  -5.643  1.00 17.96  ? 299 PRO D N   1 
ATOM   12370 C CA  . PRO D 1 270 ? 11.007  61.317  -4.363  1.00 20.52  ? 299 PRO D CA  1 
ATOM   12371 C C   . PRO D 1 270 ? 11.285  60.239  -3.309  1.00 20.65  ? 299 PRO D C   1 
ATOM   12372 O O   . PRO D 1 270 ? 11.230  60.462  -2.109  1.00 23.13  ? 299 PRO D O   1 
ATOM   12373 C CB  . PRO D 1 270 ? 9.531   61.314  -4.817  1.00 19.77  ? 299 PRO D CB  1 
ATOM   12374 C CG  . PRO D 1 270 ? 9.573   61.834  -6.229  1.00 19.96  ? 299 PRO D CG  1 
ATOM   12375 C CD  . PRO D 1 270 ? 10.804  61.173  -6.798  1.00 20.52  ? 299 PRO D CD  1 
ATOM   12376 N N   . LEU D 1 271 ? 11.517  58.999  -3.735  1.00 19.55  ? 300 LEU D N   1 
ATOM   12377 C CA  . LEU D 1 271 ? 11.764  57.967  -2.748  1.00 18.20  ? 300 LEU D CA  1 
ATOM   12378 C C   . LEU D 1 271 ? 13.231  57.907  -2.309  1.00 19.44  ? 300 LEU D C   1 
ATOM   12379 O O   . LEU D 1 271 ? 13.564  57.108  -1.453  1.00 21.56  ? 300 LEU D O   1 
ATOM   12380 C CB  . LEU D 1 271 ? 11.379  56.598  -3.313  1.00 18.60  ? 300 LEU D CB  1 
ATOM   12381 C CG  . LEU D 1 271 ? 9.919   56.393  -3.683  1.00 19.51  ? 300 LEU D CG  1 
ATOM   12382 C CD1 . LEU D 1 271 ? 9.681   54.896  -3.944  1.00 19.55  ? 300 LEU D CD1 1 
ATOM   12383 C CD2 . LEU D 1 271 ? 9.005   56.947  -2.576  1.00 18.26  ? 300 LEU D CD2 1 
ATOM   12384 N N   . HIS D 1 272 ? 14.081  58.761  -2.874  1.00 19.66  ? 301 HIS D N   1 
ATOM   12385 C CA  . HIS D 1 272 ? 15.475  58.877  -2.478  1.00 19.81  ? 301 HIS D CA  1 
ATOM   12386 C C   . HIS D 1 272 ? 15.704  60.291  -1.952  1.00 22.21  ? 301 HIS D C   1 
ATOM   12387 O O   . HIS D 1 272 ? 14.987  60.699  -1.044  1.00 21.91  ? 301 HIS D O   1 
ATOM   12388 C CB  . HIS D 1 272 ? 16.359  58.466  -3.655  1.00 19.78  ? 301 HIS D CB  1 
ATOM   12389 C CG  . HIS D 1 272 ? 17.786  58.236  -3.253  1.00 18.46  ? 301 HIS D CG  1 
ATOM   12390 N ND1 . HIS D 1 272 ? 18.812  58.140  -4.168  1.00 21.09  ? 301 HIS D ND1 1 
ATOM   12391 C CD2 . HIS D 1 272 ? 18.326  58.080  -2.065  1.00 17.08  ? 301 HIS D CD2 1 
ATOM   12392 C CE1 . HIS D 1 272 ? 19.935  57.897  -3.511  1.00 15.75  ? 301 HIS D CE1 1 
ATOM   12393 N NE2 . HIS D 1 272 ? 19.674  57.849  -2.229  1.00 19.19  ? 301 HIS D NE2 1 
ATOM   12394 N N   . GLY D 1 273 ? 16.633  61.030  -2.566  1.00 22.20  ? 302 GLY D N   1 
ATOM   12395 C CA  . GLY D 1 273 ? 17.149  62.273  -2.026  1.00 21.53  ? 302 GLY D CA  1 
ATOM   12396 C C   . GLY D 1 273 ? 16.130  63.407  -2.004  1.00 23.09  ? 302 GLY D C   1 
ATOM   12397 O O   . GLY D 1 273 ? 16.189  64.276  -1.134  1.00 23.73  ? 302 GLY D O   1 
ATOM   12398 N N   . LEU D 1 274 ? 15.168  63.378  -2.923  1.00 21.15  ? 303 LEU D N   1 
ATOM   12399 C CA  . LEU D 1 274 ? 14.216  64.473  -3.017  1.00 22.30  ? 303 LEU D CA  1 
ATOM   12400 C C   . LEU D 1 274 ? 13.332  64.491  -1.773  1.00 21.97  ? 303 LEU D C   1 
ATOM   12401 O O   . LEU D 1 274 ? 12.628  65.460  -1.526  1.00 25.15  ? 303 LEU D O   1 
ATOM   12402 C CB  . LEU D 1 274 ? 13.367  64.353  -4.280  1.00 22.02  ? 303 LEU D CB  1 
ATOM   12403 C CG  . LEU D 1 274 ? 12.677  65.644  -4.711  1.00 23.26  ? 303 LEU D CG  1 
ATOM   12404 C CD1 . LEU D 1 274 ? 13.676  66.559  -5.386  1.00 22.14  ? 303 LEU D CD1 1 
ATOM   12405 C CD2 . LEU D 1 274 ? 11.497  65.347  -5.623  1.00 23.10  ? 303 LEU D CD2 1 
ATOM   12406 N N   . ALA D 1 275 ? 13.371  63.417  -0.983  1.00 24.04  ? 304 ALA D N   1 
ATOM   12407 C CA  . ALA D 1 275 ? 12.535  63.356  0.200   1.00 22.72  ? 304 ALA D CA  1 
ATOM   12408 C C   . ALA D 1 275 ? 12.842  64.533  1.115   1.00 22.96  ? 304 ALA D C   1 
ATOM   12409 O O   . ALA D 1 275 ? 11.962  64.955  1.855   1.00 25.34  ? 304 ALA D O   1 
ATOM   12410 C CB  . ALA D 1 275 ? 12.713  62.031  0.923   1.00 22.54  ? 304 ALA D CB  1 
ATOM   12411 N N   . ASN D 1 276 ? 14.085  65.056  1.083   1.00 23.14  ? 305 ASN D N   1 
ATOM   12412 C CA  . ASN D 1 276 ? 14.440  66.156  1.976   1.00 24.33  ? 305 ASN D CA  1 
ATOM   12413 C C   . ASN D 1 276 ? 13.613  67.396  1.626   1.00 22.93  ? 305 ASN D C   1 
ATOM   12414 O O   . ASN D 1 276 ? 13.158  68.077  2.549   1.00 24.10  ? 305 ASN D O   1 
ATOM   12415 C CB  . ASN D 1 276 ? 15.960  66.370  2.116   1.00 21.10  ? 305 ASN D CB  1 
ATOM   12416 C CG  . ASN D 1 276 ? 16.717  66.765  0.862   1.00 22.89  ? 305 ASN D CG  1 
ATOM   12417 O OD1 . ASN D 1 276 ? 17.953  66.714  0.838   1.00 26.62  ? 305 ASN D OD1 1 
ATOM   12418 N ND2 . ASN D 1 276 ? 16.022  67.173  -0.175  1.00 22.86  ? 305 ASN D ND2 1 
ATOM   12419 N N   . GLN D 1 277 ? 13.383  67.631  0.324   1.00 23.64  ? 306 GLN D N   1 
ATOM   12420 C CA  . GLN D 1 277 ? 12.469  68.667  -0.165  1.00 24.00  ? 306 GLN D CA  1 
ATOM   12421 C C   . GLN D 1 277 ? 11.025  68.356  0.230   1.00 25.28  ? 306 GLN D C   1 
ATOM   12422 O O   . GLN D 1 277 ? 10.268  69.236  0.660   1.00 26.52  ? 306 GLN D O   1 
ATOM   12423 C CB  . GLN D 1 277 ? 12.582  68.755  -1.695  1.00 23.78  ? 306 GLN D CB  1 
ATOM   12424 C CG  . GLN D 1 277 ? 11.537  69.618  -2.397  1.00 23.39  ? 306 GLN D CG  1 
ATOM   12425 C CD  . GLN D 1 277 ? 11.606  69.428  -3.904  1.00 22.91  ? 306 GLN D CD  1 
ATOM   12426 O OE1 . GLN D 1 277 ? 12.617  69.699  -4.557  1.00 21.40  ? 306 GLN D OE1 1 
ATOM   12427 N NE2 . GLN D 1 277 ? 10.534  68.910  -4.475  1.00 21.51  ? 306 GLN D NE2 1 
ATOM   12428 N N   . GLU D 1 278 ? 10.621  67.102  0.027   1.00 24.95  ? 307 GLU D N   1 
ATOM   12429 C CA  . GLU D 1 278 ? 9.234   66.713  0.201   1.00 24.99  ? 307 GLU D CA  1 
ATOM   12430 C C   . GLU D 1 278 ? 8.819   66.777  1.671   1.00 24.78  ? 307 GLU D C   1 
ATOM   12431 O O   . GLU D 1 278 ? 7.655   67.065  1.948   1.00 25.91  ? 307 GLU D O   1 
ATOM   12432 C CB  . GLU D 1 278 ? 9.018   65.313  -0.355  1.00 27.65  ? 307 GLU D CB  1 
ATOM   12433 C CG  . GLU D 1 278 ? 9.148   65.315  -1.861  1.00 32.73  ? 307 GLU D CG  1 
ATOM   12434 C CD  . GLU D 1 278 ? 9.137   63.954  -2.518  1.00 40.50  ? 307 GLU D CD  1 
ATOM   12435 O OE1 . GLU D 1 278 ? 9.263   62.932  -1.798  1.00 47.91  ? 307 GLU D OE1 1 
ATOM   12436 O OE2 . GLU D 1 278 ? 9.001   63.933  -3.754  1.00 50.21  ? 307 GLU D OE2 1 
ATOM   12437 N N   . VAL D 1 279 ? 9.751   66.514  2.600   1.00 23.87  ? 308 VAL D N   1 
ATOM   12438 C CA  . VAL D 1 279 ? 9.487   66.673  4.023   1.00 22.73  ? 308 VAL D CA  1 
ATOM   12439 C C   . VAL D 1 279 ? 8.976   68.077  4.303   1.00 26.08  ? 308 VAL D C   1 
ATOM   12440 O O   . VAL D 1 279 ? 7.975   68.239  4.997   1.00 27.48  ? 308 VAL D O   1 
ATOM   12441 C CB  . VAL D 1 279 ? 10.723  66.370  4.883   1.00 23.82  ? 308 VAL D CB  1 
ATOM   12442 C CG1 . VAL D 1 279 ? 10.641  66.924  6.304   1.00 22.36  ? 308 VAL D CG1 1 
ATOM   12443 C CG2 . VAL D 1 279 ? 10.961  64.875  4.927   1.00 22.06  ? 308 VAL D CG2 1 
ATOM   12444 N N   . LEU D 1 280 ? 9.696   69.096  3.836   1.00 27.69  ? 309 LEU D N   1 
ATOM   12445 C CA  . LEU D 1 280 ? 9.315   70.446  4.227   1.00 31.78  ? 309 LEU D CA  1 
ATOM   12446 C C   . LEU D 1 280 ? 8.048   70.926  3.487   1.00 31.89  ? 309 LEU D C   1 
ATOM   12447 O O   . LEU D 1 280 ? 7.327   71.775  4.002   1.00 33.91  ? 309 LEU D O   1 
ATOM   12448 C CB  . LEU D 1 280 ? 10.537  71.366  4.107   1.00 34.05  ? 309 LEU D CB  1 
ATOM   12449 C CG  . LEU D 1 280 ? 11.337  71.495  5.409   1.00 35.52  ? 309 LEU D CG  1 
ATOM   12450 C CD1 . LEU D 1 280 ? 12.072  70.208  5.725   1.00 39.10  ? 309 LEU D CD1 1 
ATOM   12451 C CD2 . LEU D 1 280 ? 12.309  72.666  5.401   1.00 37.56  ? 309 LEU D CD2 1 
ATOM   12452 N N   . VAL D 1 281 ? 7.716   70.364  2.322   1.00 31.37  ? 310 VAL D N   1 
ATOM   12453 C CA  . VAL D 1 281 ? 6.418   70.623  1.702   1.00 31.56  ? 310 VAL D CA  1 
ATOM   12454 C C   . VAL D 1 281 ? 5.313   70.048  2.597   1.00 30.82  ? 310 VAL D C   1 
ATOM   12455 O O   . VAL D 1 281 ? 4.329   70.725  2.908   1.00 28.01  ? 310 VAL D O   1 
ATOM   12456 C CB  . VAL D 1 281 ? 6.324   70.055  0.269   1.00 30.59  ? 310 VAL D CB  1 
ATOM   12457 C CG1 . VAL D 1 281 ? 5.012   70.445  -0.416  1.00 32.97  ? 310 VAL D CG1 1 
ATOM   12458 C CG2 . VAL D 1 281 ? 7.503   70.481  -0.581  1.00 32.14  ? 310 VAL D CG2 1 
ATOM   12459 N N   . TRP D 1 282 ? 5.492   68.783  3.001   1.00 30.03  ? 311 TRP D N   1 
ATOM   12460 C CA  . TRP D 1 282 ? 4.531   68.038  3.799   1.00 29.03  ? 311 TRP D CA  1 
ATOM   12461 C C   . TRP D 1 282 ? 4.245   68.763  5.119   1.00 28.06  ? 311 TRP D C   1 
ATOM   12462 O O   . TRP D 1 282 ? 3.090   68.853  5.554   1.00 26.38  ? 311 TRP D O   1 
ATOM   12463 C CB  . TRP D 1 282 ? 5.096   66.636  4.025   1.00 30.30  ? 311 TRP D CB  1 
ATOM   12464 C CG  . TRP D 1 282 ? 4.148   65.628  4.589   1.00 31.15  ? 311 TRP D CG  1 
ATOM   12465 C CD1 . TRP D 1 282 ? 3.088   65.043  3.957   1.00 29.30  ? 311 TRP D CD1 1 
ATOM   12466 C CD2 . TRP D 1 282 ? 4.191   65.060  5.916   1.00 31.76  ? 311 TRP D CD2 1 
ATOM   12467 N NE1 . TRP D 1 282 ? 2.470   64.156  4.802   1.00 28.22  ? 311 TRP D NE1 1 
ATOM   12468 C CE2 . TRP D 1 282 ? 3.125   64.139  6.002   1.00 27.72  ? 311 TRP D CE2 1 
ATOM   12469 C CE3 . TRP D 1 282 ? 5.020   65.238  7.031   1.00 32.38  ? 311 TRP D CE3 1 
ATOM   12470 C CZ2 . TRP D 1 282 ? 2.856   63.416  7.167   1.00 30.76  ? 311 TRP D CZ2 1 
ATOM   12471 C CZ3 . TRP D 1 282 ? 4.769   64.508  8.175   1.00 32.47  ? 311 TRP D CZ3 1 
ATOM   12472 C CH2 . TRP D 1 282 ? 3.706   63.608  8.235   1.00 37.34  ? 311 TRP D CH2 1 
ATOM   12473 N N   . LEU D 1 283 ? 5.323   69.253  5.741   1.00 27.63  ? 312 LEU D N   1 
ATOM   12474 C CA  . LEU D 1 283 ? 5.292   69.926  7.034   1.00 26.53  ? 312 LEU D CA  1 
ATOM   12475 C C   . LEU D 1 283 ? 4.641   71.296  6.896   1.00 25.61  ? 312 LEU D C   1 
ATOM   12476 O O   . LEU D 1 283 ? 3.940   71.715  7.798   1.00 28.55  ? 312 LEU D O   1 
ATOM   12477 C CB  . LEU D 1 283 ? 6.732   70.104  7.539   1.00 26.76  ? 312 LEU D CB  1 
ATOM   12478 C CG  . LEU D 1 283 ? 7.495   68.844  7.973   1.00 28.46  ? 312 LEU D CG  1 
ATOM   12479 C CD1 . LEU D 1 283 ? 8.947   69.211  8.271   1.00 29.30  ? 312 LEU D CD1 1 
ATOM   12480 C CD2 . LEU D 1 283 ? 6.875   68.118  9.179   1.00 32.04  ? 312 LEU D CD2 1 
ATOM   12481 N N   . THR D 1 284 ? 5.005   72.044  5.848   1.00 27.45  ? 313 THR D N   1 
ATOM   12482 C CA  . THR D 1 284 ? 4.337   73.297  5.515   1.00 28.61  ? 313 THR D CA  1 
ATOM   12483 C C   . THR D 1 284 ? 2.824   73.072  5.416   1.00 30.96  ? 313 THR D C   1 
ATOM   12484 O O   . THR D 1 284 ? 2.046   73.788  6.058   1.00 30.44  ? 313 THR D O   1 
ATOM   12485 C CB  . THR D 1 284 ? 4.809   73.851  4.165   1.00 30.33  ? 313 THR D CB  1 
ATOM   12486 O OG1 . THR D 1 284 ? 6.199   74.158  4.260   1.00 29.89  ? 313 THR D OG1 1 
ATOM   12487 C CG2 . THR D 1 284 ? 4.017   75.066  3.730   1.00 31.15  ? 313 THR D CG2 1 
ATOM   12488 N N   . GLN D 1 285 ? 2.440   72.061  4.613   1.00 31.58  ? 314 GLN D N   1 
ATOM   12489 C CA  . GLN D 1 285 ? 1.047   71.705  4.365   1.00 34.30  ? 314 GLN D CA  1 
ATOM   12490 C C   . GLN D 1 285 ? 0.349   71.340  5.672   1.00 32.88  ? 314 GLN D C   1 
ATOM   12491 O O   . GLN D 1 285 ? -0.768  71.780  5.896   1.00 31.69  ? 314 GLN D O   1 
ATOM   12492 C CB  . GLN D 1 285 ? 0.926   70.540  3.378   1.00 41.85  ? 314 GLN D CB  1 
ATOM   12493 C CG  . GLN D 1 285 ? 0.951   70.966  1.913   1.00 51.15  ? 314 GLN D CG  1 
ATOM   12494 C CD  . GLN D 1 285 ? -0.360  71.546  1.423   1.00 56.10  ? 314 GLN D CD  1 
ATOM   12495 O OE1 . GLN D 1 285 ? -0.974  72.392  2.075   1.00 57.69  ? 314 GLN D OE1 1 
ATOM   12496 N NE2 . GLN D 1 285 ? -0.809  71.087  0.261   1.00 55.62  ? 314 GLN D NE2 1 
ATOM   12497 N N   . LEU D 1 286 ? 1.020   70.546  6.514   1.00 31.88  ? 315 LEU D N   1 
ATOM   12498 C CA  . LEU D 1 286 ? 0.542   70.225  7.850   1.00 32.16  ? 315 LEU D CA  1 
ATOM   12499 C C   . LEU D 1 286 ? 0.234   71.502  8.637   1.00 35.24  ? 315 LEU D C   1 
ATOM   12500 O O   . LEU D 1 286 ? -0.853  71.612  9.210   1.00 37.69  ? 315 LEU D O   1 
ATOM   12501 C CB  . LEU D 1 286 ? 1.590   69.343  8.541   1.00 36.73  ? 315 LEU D CB  1 
ATOM   12502 C CG  . LEU D 1 286 ? 1.449   69.157  10.050  1.00 39.80  ? 315 LEU D CG  1 
ATOM   12503 C CD1 . LEU D 1 286 ? 0.089   68.601  10.407  1.00 44.35  ? 315 LEU D CD1 1 
ATOM   12504 C CD2 . LEU D 1 286 ? 2.533   68.225  10.568  1.00 43.41  ? 315 LEU D CD2 1 
ATOM   12505 N N   . GLN D 1 287 ? 1.150   72.466  8.623   1.00 32.84  ? 316 GLN D N   1 
ATOM   12506 C CA  . GLN D 1 287 ? 0.947   73.688  9.447   1.00 34.38  ? 316 GLN D CA  1 
ATOM   12507 C C   . GLN D 1 287 ? -0.291  74.459  8.965   1.00 36.94  ? 316 GLN D C   1 
ATOM   12508 O O   . GLN D 1 287 ? -0.973  75.062  9.804   1.00 33.31  ? 316 GLN D O   1 
ATOM   12509 C CB  . GLN D 1 287 ? 2.186   74.574  9.426   1.00 37.73  ? 316 GLN D CB  1 
ATOM   12510 C CG  . GLN D 1 287 ? 3.367   74.005  10.194  1.00 40.47  ? 316 GLN D CG  1 
ATOM   12511 C CD  . GLN D 1 287 ? 4.483   75.011  10.347  1.00 46.43  ? 316 GLN D CD  1 
ATOM   12512 O OE1 . GLN D 1 287 ? 4.316   76.204  10.077  1.00 49.57  ? 316 GLN D OE1 1 
ATOM   12513 N NE2 . GLN D 1 287 ? 5.631   74.532  10.797  1.00 48.63  ? 316 GLN D NE2 1 
ATOM   12514 N N   . LYS D 1 288 ? -0.576  74.407  7.669   1.00 37.49  ? 317 LYS D N   1 
ATOM   12515 C CA  . LYS D 1 288 ? -1.738  75.147  7.100   1.00 43.33  ? 317 LYS D CA  1 
ATOM   12516 C C   . LYS D 1 288 ? -3.055  74.378  7.332   1.00 39.28  ? 317 LYS D C   1 
ATOM   12517 O O   . LYS D 1 288 ? -4.068  75.046  7.584   1.00 39.79  ? 317 LYS D O   1 
ATOM   12518 C CB  . LYS D 1 288 ? -1.544  75.424  5.604   1.00 44.18  ? 317 LYS D CB  1 
ATOM   12519 C CG  . LYS D 1 288 ? -0.148  75.782  5.143   1.00 46.35  ? 317 LYS D CG  1 
ATOM   12520 C CD  . LYS D 1 288 ? 0.094   77.279  5.010   1.00 49.31  ? 317 LYS D CD  1 
ATOM   12521 C CE  . LYS D 1 288 ? 1.537   77.632  5.190   1.00 53.00  ? 317 LYS D CE  1 
ATOM   12522 N NZ  . LYS D 1 288 ? 2.210   76.724  6.124   1.00 57.32  ? 317 LYS D NZ  1 
ATOM   12523 N N   . GLU D 1 289 ? -3.023  73.051  7.283   1.00 37.66  ? 318 GLU D N   1 
ATOM   12524 C CA  . GLU D 1 289 ? -4.265  72.258  7.421   1.00 41.26  ? 318 GLU D CA  1 
ATOM   12525 C C   . GLU D 1 289 ? -4.660  72.057  8.893   1.00 41.08  ? 318 GLU D C   1 
ATOM   12526 O O   . GLU D 1 289 ? -5.860  71.931  9.174   1.00 34.41  ? 318 GLU D O   1 
ATOM   12527 C CB  . GLU D 1 289 ? -4.029  70.875  6.825   1.00 45.78  ? 318 GLU D CB  1 
ATOM   12528 C CG  . GLU D 1 289 ? -4.612  70.705  5.427   1.00 52.10  ? 318 GLU D CG  1 
ATOM   12529 C CD  . GLU D 1 289 ? -3.552  70.719  4.343   1.00 56.64  ? 318 GLU D CD  1 
ATOM   12530 O OE1 . GLU D 1 289 ? -3.136  69.638  3.888   1.00 58.00  ? 318 GLU D OE1 1 
ATOM   12531 O OE2 . GLU D 1 289 ? -3.139  71.827  3.962   1.00 66.50  ? 318 GLU D OE2 1 
ATOM   12532 N N   . VAL D 1 290 ? -3.694  72.075  9.807   1.00 50.11  ? 319 VAL D N   1 
ATOM   12533 C CA  . VAL D 1 290 ? -4.025  71.695  11.208  1.00 53.12  ? 319 VAL D CA  1 
ATOM   12534 C C   . VAL D 1 290 ? -3.432  72.660  12.244  1.00 58.46  ? 319 VAL D C   1 
ATOM   12535 O O   . VAL D 1 290 ? -3.813  72.524  13.430  1.00 69.55  ? 319 VAL D O   1 
ATOM   12536 C CB  . VAL D 1 290 ? -3.494  70.251  11.265  1.00 58.99  ? 319 VAL D CB  1 
ATOM   12537 C CG1 . VAL D 1 290 ? -2.921  69.819  12.602  1.00 58.91  ? 319 VAL D CG1 1 
ATOM   12538 C CG2 . VAL D 1 290 ? -4.507  69.230  10.765  1.00 59.22  ? 319 VAL D CG2 1 
ATOM   12539 N N   . GLY D 1 291 ? -2.652  73.668  11.837  1.00 57.84  ? 320 GLY D N   1 
ATOM   12540 C CA  . GLY D 1 291 ? -2.155  74.669  12.800  1.00 62.54  ? 320 GLY D CA  1 
ATOM   12541 C C   . GLY D 1 291 ? -0.684  74.490  13.124  1.00 64.37  ? 320 GLY D C   1 
ATOM   12542 O O   . GLY D 1 291 ? -0.156  73.407  12.804  1.00 66.43  ? 320 GLY D O   1 
ATOM   12543 N N   . LYS D 1 292 ? -0.043  75.484  13.765  1.00 67.33  ? 321 LYS D N   1 
ATOM   12544 C CA  . LYS D 1 292 ? 1.427   75.424  14.009  1.00 59.08  ? 321 LYS D CA  1 
ATOM   12545 C C   . LYS D 1 292 ? 1.682   74.439  15.156  1.00 64.98  ? 321 LYS D C   1 
ATOM   12546 O O   . LYS D 1 292 ? 2.412   73.449  14.925  1.00 61.33  ? 321 LYS D O   1 
ATOM   12547 C CB  . LYS D 1 292 ? 1.999   76.809  14.309  1.00 57.05  ? 321 LYS D CB  1 
ATOM   12548 C CG  . LYS D 1 292 ? 2.770   77.496  13.194  1.00 54.61  ? 321 LYS D CG  1 
ATOM   12549 C CD  . LYS D 1 292 ? 4.275   77.328  13.351  1.00 52.84  ? 321 LYS D CD  1 
ATOM   12550 C CE  . LYS D 1 292 ? 5.019   78.620  13.382  1.00 52.73  ? 321 LYS D CE  1 
ATOM   12551 N NZ  . LYS D 1 292 ? 6.439   78.392  13.109  1.00 51.92  ? 321 LYS D NZ  1 
ATOM   12552 N N   . ASP D 1 293 ? 1.113   74.704  16.334  1.00 60.63  ? 322 ASP D N   1 
ATOM   12553 C CA  . ASP D 1 293 ? 1.207   73.722  17.442  1.00 59.20  ? 322 ASP D CA  1 
ATOM   12554 C C   . ASP D 1 293 ? -0.163  73.049  17.517  1.00 57.34  ? 322 ASP D C   1 
ATOM   12555 O O   . ASP D 1 293 ? -1.176  73.775  17.487  1.00 62.24  ? 322 ASP D O   1 
ATOM   12556 C CB  . ASP D 1 293 ? 1.606   74.365  18.764  1.00 61.51  ? 322 ASP D CB  1 
ATOM   12557 C CG  . ASP D 1 293 ? 3.095   74.485  19.021  1.00 60.03  ? 322 ASP D CG  1 
ATOM   12558 O OD1 . ASP D 1 293 ? 3.786   73.445  18.948  1.00 60.91  ? 322 ASP D OD1 1 
ATOM   12559 O OD2 . ASP D 1 293 ? 3.544   75.617  19.298  1.00 65.29  ? 322 ASP D OD2 1 
ATOM   12560 N N   . VAL D 1 294 ? -0.193  71.721  17.559  1.00 49.20  ? 323 VAL D N   1 
ATOM   12561 C CA  . VAL D 1 294 ? -1.487  70.992  17.674  1.00 49.74  ? 323 VAL D CA  1 
ATOM   12562 C C   . VAL D 1 294 ? -1.320  69.750  18.559  1.00 46.48  ? 323 VAL D C   1 
ATOM   12563 O O   . VAL D 1 294 ? -0.183  69.458  18.958  1.00 47.17  ? 323 VAL D O   1 
ATOM   12564 C CB  . VAL D 1 294 ? -2.061  70.586  16.308  1.00 49.92  ? 323 VAL D CB  1 
ATOM   12565 C CG1 . VAL D 1 294 ? -3.504  71.040  16.154  1.00 53.29  ? 323 VAL D CG1 1 
ATOM   12566 C CG2 . VAL D 1 294 ? -1.199  71.082  15.158  1.00 51.20  ? 323 VAL D CG2 1 
ATOM   12567 N N   . SER D 1 295 ? -2.425  69.072  18.838  1.00 40.66  ? 324 SER D N   1 
ATOM   12568 C CA  . SER D 1 295 ? -2.416  67.858  19.626  1.00 43.85  ? 324 SER D CA  1 
ATOM   12569 C C   . SER D 1 295 ? -1.781  66.713  18.844  1.00 42.16  ? 324 SER D C   1 
ATOM   12570 O O   . SER D 1 295 ? -1.562  66.808  17.635  1.00 39.60  ? 324 SER D O   1 
ATOM   12571 C CB  . SER D 1 295 ? -3.813  67.507  20.058  1.00 44.07  ? 324 SER D CB  1 
ATOM   12572 O OG  . SER D 1 295 ? -4.643  67.240  18.928  1.00 50.64  ? 324 SER D OG  1 
ATOM   12573 N N   . ASP D 1 296 ? -1.502  65.626  19.573  1.00 42.67  ? 325 ASP D N   1 
ATOM   12574 C CA  . ASP D 1 296 ? -0.999  64.399  18.984  1.00 41.99  ? 325 ASP D CA  1 
ATOM   12575 C C   . ASP D 1 296 ? -2.083  63.760  18.121  1.00 43.59  ? 325 ASP D C   1 
ATOM   12576 O O   . ASP D 1 296 ? -1.761  63.143  17.108  1.00 44.64  ? 325 ASP D O   1 
ATOM   12577 C CB  . ASP D 1 296 ? -0.515  63.430  20.064  1.00 41.73  ? 325 ASP D CB  1 
ATOM   12578 C CG  . ASP D 1 296 ? 0.753   63.873  20.774  1.00 41.23  ? 325 ASP D CG  1 
ATOM   12579 O OD1 . ASP D 1 296 ? 1.327   64.907  20.375  1.00 42.63  ? 325 ASP D OD1 1 
ATOM   12580 O OD2 . ASP D 1 296 ? 1.153   63.173  21.727  1.00 41.57  ? 325 ASP D OD2 1 
ATOM   12581 N N   . GLU D 1 297 ? -3.340  63.877  18.537  1.00 43.23  ? 326 GLU D N   1 
ATOM   12582 C CA  . GLU D 1 297 ? -4.481  63.278  17.786  1.00 43.54  ? 326 GLU D CA  1 
ATOM   12583 C C   . GLU D 1 297 ? -4.519  63.924  16.404  1.00 38.83  ? 326 GLU D C   1 
ATOM   12584 O O   . GLU D 1 297 ? -4.570  63.201  15.411  1.00 35.15  ? 326 GLU D O   1 
ATOM   12585 C CB  . GLU D 1 297 ? -5.724  63.472  18.642  1.00 47.15  ? 326 GLU D CB  1 
ATOM   12586 C CG  . GLU D 1 297 ? -5.611  62.755  19.982  1.00 53.70  ? 326 GLU D CG  1 
ATOM   12587 C CD  . GLU D 1 297 ? -5.241  63.664  21.137  1.00 55.82  ? 326 GLU D CD  1 
ATOM   12588 O OE1 . GLU D 1 297 ? -4.045  63.989  21.282  1.00 46.86  ? 326 GLU D OE1 1 
ATOM   12589 O OE2 . GLU D 1 297 ? -6.165  64.033  21.891  1.00 57.32  ? 326 GLU D OE2 1 
ATOM   12590 N N   . LYS D 1 298 ? -4.439  65.244  16.353  1.00 38.15  ? 327 LYS D N   1 
ATOM   12591 C CA  . LYS D 1 298 ? -4.521  65.974  15.068  1.00 44.08  ? 327 LYS D CA  1 
ATOM   12592 C C   . LYS D 1 298 ? -3.344  65.676  14.128  1.00 43.99  ? 327 LYS D C   1 
ATOM   12593 O O   . LYS D 1 298 ? -3.551  65.711  12.899  1.00 52.73  ? 327 LYS D O   1 
ATOM   12594 C CB  . LYS D 1 298 ? -4.546  67.476  15.319  1.00 45.77  ? 327 LYS D CB  1 
ATOM   12595 C CG  . LYS D 1 298 ? -5.475  68.193  14.364  1.00 49.32  ? 327 LYS D CG  1 
ATOM   12596 C CD  . LYS D 1 298 ? -6.907  67.762  14.626  1.00 50.51  ? 327 LYS D CD  1 
ATOM   12597 C CE  . LYS D 1 298 ? -7.397  68.398  15.883  1.00 53.67  ? 327 LYS D CE  1 
ATOM   12598 N NZ  . LYS D 1 298 ? -7.082  69.827  15.895  1.00 55.15  ? 327 LYS D NZ  1 
ATOM   12599 N N   . LEU D 1 299 ? -2.157  65.428  14.650  1.00 46.12  ? 328 LEU D N   1 
ATOM   12600 C CA  . LEU D 1 299 ? -1.062  65.076  13.714  1.00 41.42  ? 328 LEU D CA  1 
ATOM   12601 C C   . LEU D 1 299 ? -1.332  63.674  13.174  1.00 35.46  ? 328 LEU D C   1 
ATOM   12602 O O   . LEU D 1 299 ? -1.103  63.430  11.995  1.00 31.97  ? 328 LEU D O   1 
ATOM   12603 C CB  . LEU D 1 299 ? 0.260   65.161  14.466  1.00 40.50  ? 328 LEU D CB  1 
ATOM   12604 C CG  . LEU D 1 299 ? 1.007   66.491  14.330  1.00 43.03  ? 328 LEU D CG  1 
ATOM   12605 C CD1 . LEU D 1 299 ? 0.091   67.691  14.211  1.00 40.74  ? 328 LEU D CD1 1 
ATOM   12606 C CD2 . LEU D 1 299 ? 1.951   66.687  15.479  1.00 45.59  ? 328 LEU D CD2 1 
ATOM   12607 N N   . ARG D 1 300 ? -1.819  62.814  14.046  1.00 32.67  ? 329 ARG D N   1 
ATOM   12608 C CA  . ARG D 1 300 ? -2.080  61.418  13.662  1.00 36.60  ? 329 ARG D CA  1 
ATOM   12609 C C   . ARG D 1 300 ? -3.115  61.449  12.528  1.00 32.04  ? 329 ARG D C   1 
ATOM   12610 O O   . ARG D 1 300 ? -2.976  60.660  11.580  1.00 30.71  ? 329 ARG D O   1 
ATOM   12611 C CB  . ARG D 1 300 ? -2.414  60.865  15.050  1.00 41.22  ? 329 ARG D CB  1 
ATOM   12612 C CG  . ARG D 1 300 ? -1.490  59.788  15.603  1.00 45.06  ? 329 ARG D CG  1 
ATOM   12613 C CD  . ARG D 1 300 ? -1.928  59.180  16.927  1.00 47.48  ? 329 ARG D CD  1 
ATOM   12614 N NE  . ARG D 1 300 ? -1.827  60.134  18.036  1.00 53.38  ? 329 ARG D NE  1 
ATOM   12615 C CZ  . ARG D 1 300 ? -1.477  59.828  19.277  1.00 53.86  ? 329 ARG D CZ  1 
ATOM   12616 N NH1 . ARG D 1 300 ? -2.089  60.398  20.296  1.00 52.12  ? 329 ARG D NH1 1 
ATOM   12617 N NH2 . ARG D 1 300 ? -0.505  58.962  19.496  1.00 55.97  ? 329 ARG D NH2 1 
ATOM   12618 N N   . ASP D 1 301 ? -4.140  62.271  12.668  1.00 32.61  ? 330 ASP D N   1 
ATOM   12619 C CA  . ASP D 1 301 ? -5.121  62.509  11.627  1.00 29.79  ? 330 ASP D CA  1 
ATOM   12620 C C   . ASP D 1 301 ? -4.410  62.817  10.316  1.00 29.99  ? 330 ASP D C   1 
ATOM   12621 O O   . ASP D 1 301 ? -4.662  62.158  9.314   1.00 28.99  ? 330 ASP D O   1 
ATOM   12622 C CB  . ASP D 1 301 ? -6.054  63.659  12.034  1.00 33.72  ? 330 ASP D CB  1 
ATOM   12623 C CG  . ASP D 1 301 ? -6.976  63.321  13.204  1.00 37.29  ? 330 ASP D CG  1 
ATOM   12624 O OD1 . ASP D 1 301 ? -7.079  62.124  13.528  1.00 37.84  ? 330 ASP D OD1 1 
ATOM   12625 O OD2 . ASP D 1 301 ? -7.598  64.261  13.782  1.00 31.59  ? 330 ASP D OD2 1 
ATOM   12626 N N   . TYR D 1 302 ? -3.543  63.836  10.314  1.00 27.48  ? 331 TYR D N   1 
ATOM   12627 C CA  . TYR D 1 302 ? -2.942  64.264  9.064   1.00 30.02  ? 331 TYR D CA  1 
ATOM   12628 C C   . TYR D 1 302 ? -2.072  63.131  8.514   1.00 31.33  ? 331 TYR D C   1 
ATOM   12629 O O   . TYR D 1 302 ? -2.042  62.902  7.316   1.00 33.52  ? 331 TYR D O   1 
ATOM   12630 C CB  . TYR D 1 302 ? -2.227  65.602  9.269   1.00 33.74  ? 331 TYR D CB  1 
ATOM   12631 C CG  . TYR D 1 302 ? -1.436  66.116  8.094   1.00 33.06  ? 331 TYR D CG  1 
ATOM   12632 C CD1 . TYR D 1 302 ? -0.127  65.705  7.881   1.00 32.86  ? 331 TYR D CD1 1 
ATOM   12633 C CD2 . TYR D 1 302 ? -1.987  67.017  7.191   1.00 35.92  ? 331 TYR D CD2 1 
ATOM   12634 C CE1 . TYR D 1 302 ? 0.613   66.190  6.815   1.00 33.10  ? 331 TYR D CE1 1 
ATOM   12635 C CE2 . TYR D 1 302 ? -1.263  67.493  6.109   1.00 31.90  ? 331 TYR D CE2 1 
ATOM   12636 C CZ  . TYR D 1 302 ? 0.048   67.087  5.926   1.00 33.54  ? 331 TYR D CZ  1 
ATOM   12637 O OH  . TYR D 1 302 ? 0.816   67.537  4.862   1.00 32.84  ? 331 TYR D OH  1 
ATOM   12638 N N   . ILE D 1 303 ? -1.391  62.389  9.388   1.00 33.08  ? 332 ILE D N   1 
ATOM   12639 C CA  . ILE D 1 303 ? -0.506  61.325  8.937   1.00 31.95  ? 332 ILE D CA  1 
ATOM   12640 C C   . ILE D 1 303 ? -1.310  60.234  8.233   1.00 31.30  ? 332 ILE D C   1 
ATOM   12641 O O   . ILE D 1 303 ? -0.914  59.762  7.166   1.00 29.76  ? 332 ILE D O   1 
ATOM   12642 C CB  . ILE D 1 303 ? 0.281   60.758  10.132  1.00 28.48  ? 332 ILE D CB  1 
ATOM   12643 C CG1 . ILE D 1 303 ? 1.295   61.785  10.636  1.00 26.06  ? 332 ILE D CG1 1 
ATOM   12644 C CG2 . ILE D 1 303 ? 0.920   59.436  9.758   1.00 28.14  ? 332 ILE D CG2 1 
ATOM   12645 C CD1 . ILE D 1 303 ? 1.674   61.617  12.110  1.00 25.82  ? 332 ILE D CD1 1 
ATOM   12646 N N   . TRP D 1 304 ? -2.395  59.806  8.878   1.00 31.15  ? 333 TRP D N   1 
ATOM   12647 C CA  . TRP D 1 304 ? -3.253  58.761  8.348   1.00 33.82  ? 333 TRP D CA  1 
ATOM   12648 C C   . TRP D 1 304 ? -3.856  59.195  7.019   1.00 32.78  ? 333 TRP D C   1 
ATOM   12649 O O   . TRP D 1 304 ? -4.071  58.364  6.138   1.00 36.33  ? 333 TRP D O   1 
ATOM   12650 C CB  . TRP D 1 304 ? -4.350  58.401  9.358   1.00 32.51  ? 333 TRP D CB  1 
ATOM   12651 C CG  . TRP D 1 304 ? -4.011  57.252  10.253  1.00 32.17  ? 333 TRP D CG  1 
ATOM   12652 C CD1 . TRP D 1 304 ? -4.007  57.256  11.614  1.00 32.72  ? 333 TRP D CD1 1 
ATOM   12653 C CD2 . TRP D 1 304 ? -3.670  55.913  9.858   1.00 31.04  ? 333 TRP D CD2 1 
ATOM   12654 N NE1 . TRP D 1 304 ? -3.695  56.015  12.095  1.00 33.53  ? 333 TRP D NE1 1 
ATOM   12655 C CE2 . TRP D 1 304 ? -3.488  55.170  11.042  1.00 28.25  ? 333 TRP D CE2 1 
ATOM   12656 C CE3 . TRP D 1 304 ? -3.513  55.261  8.629   1.00 31.19  ? 333 TRP D CE3 1 
ATOM   12657 C CZ2 . TRP D 1 304 ? -3.139  53.823  11.032  1.00 30.33  ? 333 TRP D CZ2 1 
ATOM   12658 C CZ3 . TRP D 1 304 ? -3.178  53.924  8.618   1.00 31.46  ? 333 TRP D CZ3 1 
ATOM   12659 C CH2 . TRP D 1 304 ? -2.993  53.215  9.807   1.00 30.02  ? 333 TRP D CH2 1 
ATOM   12660 N N   . ASN D 1 305 ? -4.151  60.494  6.908   1.00 31.86  ? 334 ASN D N   1 
ATOM   12661 C CA  . ASN D 1 305 ? -4.627  61.073  5.668   1.00 35.00  ? 334 ASN D CA  1 
ATOM   12662 C C   . ASN D 1 305 ? -3.651  60.700  4.552   1.00 33.92  ? 334 ASN D C   1 
ATOM   12663 O O   . ASN D 1 305 ? -4.047  60.169  3.513   1.00 32.73  ? 334 ASN D O   1 
ATOM   12664 C CB  . ASN D 1 305 ? -4.949  62.564  5.847   1.00 39.64  ? 334 ASN D CB  1 
ATOM   12665 C CG  . ASN D 1 305 ? -3.825  63.569  5.650   1.00 49.38  ? 334 ASN D CG  1 
ATOM   12666 O OD1 . ASN D 1 305 ? -2.696  63.249  5.269   1.00 50.72  ? 334 ASN D OD1 1 
ATOM   12667 N ND2 . ASN D 1 305 ? -4.152  64.837  5.861   1.00 56.25  ? 334 ASN D ND2 1 
ATOM   12668 N N   . THR D 1 306 ? -2.363  60.971  4.768   1.00 30.26  ? 335 THR D N   1 
ATOM   12669 C CA  . THR D 1 306 ? -1.370  60.721  3.738   1.00 25.77  ? 335 THR D CA  1 
ATOM   12670 C C   . THR D 1 306 ? -1.321  59.238  3.392   1.00 24.39  ? 335 THR D C   1 
ATOM   12671 O O   . THR D 1 306 ? -1.280  58.858  2.216   1.00 22.51  ? 335 THR D O   1 
ATOM   12672 C CB  . THR D 1 306 ? 0.001   61.237  4.191   1.00 28.66  ? 335 THR D CB  1 
ATOM   12673 O OG1 . THR D 1 306 ? -0.206  62.624  4.459   1.00 26.63  ? 335 THR D OG1 1 
ATOM   12674 C CG2 . THR D 1 306 ? 1.077   61.026  3.148   1.00 27.49  ? 335 THR D CG2 1 
ATOM   12675 N N   . LEU D 1 307 ? -1.277  58.403  4.426   1.00 23.52  ? 336 LEU D N   1 
ATOM   12676 C CA  . LEU D 1 307 ? -1.106  56.981  4.200   1.00 23.62  ? 336 LEU D CA  1 
ATOM   12677 C C   . LEU D 1 307 ? -2.317  56.429  3.446   1.00 25.59  ? 336 LEU D C   1 
ATOM   12678 O O   . LEU D 1 307 ? -2.159  55.605  2.548   1.00 24.91  ? 336 LEU D O   1 
ATOM   12679 C CB  . LEU D 1 307 ? -0.897  56.289  5.549   1.00 24.86  ? 336 LEU D CB  1 
ATOM   12680 C CG  . LEU D 1 307 ? 0.409   56.654  6.261   1.00 24.56  ? 336 LEU D CG  1 
ATOM   12681 C CD1 . LEU D 1 307 ? 0.465   56.010  7.641   1.00 24.10  ? 336 LEU D CD1 1 
ATOM   12682 C CD2 . LEU D 1 307 ? 1.621   56.267  5.427   1.00 25.00  ? 336 LEU D CD2 1 
ATOM   12683 N N   . ASN D 1 308 ? -3.521  56.902  3.792   1.00 24.45  ? 337 ASN D N   1 
ATOM   12684 C CA  . ASN D 1 308 ? -4.741  56.412  3.165   1.00 29.50  ? 337 ASN D CA  1 
ATOM   12685 C C   . ASN D 1 308 ? -4.889  56.907  1.720   1.00 29.62  ? 337 ASN D C   1 
ATOM   12686 O O   . ASN D 1 308 ? -5.650  56.317  0.960   1.00 34.49  ? 337 ASN D O   1 
ATOM   12687 C CB  . ASN D 1 308 ? -5.977  56.816  3.968   1.00 30.10  ? 337 ASN D CB  1 
ATOM   12688 C CG  . ASN D 1 308 ? -6.072  56.086  5.287   1.00 33.02  ? 337 ASN D CG  1 
ATOM   12689 O OD1 . ASN D 1 308 ? -5.492  55.009  5.445   1.00 30.94  ? 337 ASN D OD1 1 
ATOM   12690 N ND2 . ASN D 1 308 ? -6.817  56.656  6.224   1.00 33.50  ? 337 ASN D ND2 1 
ATOM   12691 N N   . SER D 1 309 ? -4.172  57.977  1.340   1.00 27.05  ? 338 SER D N   1 
ATOM   12692 C CA  . SER D 1 309 ? -4.185  58.505  -0.021  1.00 26.91  ? 338 SER D CA  1 
ATOM   12693 C C   . SER D 1 309 ? -3.205  57.797  -0.962  1.00 25.95  ? 338 SER D C   1 
ATOM   12694 O O   . SER D 1 309 ? -3.058  58.177  -2.142  1.00 26.34  ? 338 SER D O   1 
ATOM   12695 C CB  . SER D 1 309 ? -3.917  59.977  -0.005  1.00 25.65  ? 338 SER D CB  1 
ATOM   12696 O OG  . SER D 1 309 ? -4.893  60.613  0.805   1.00 26.68  ? 338 SER D OG  1 
ATOM   12697 N N   . GLY D 1 310 ? -2.519  56.776  -0.465  1.00 25.23  ? 339 GLY D N   1 
ATOM   12698 C CA  . GLY D 1 310 ? -1.653  55.983  -1.322  1.00 25.95  ? 339 GLY D CA  1 
ATOM   12699 C C   . GLY D 1 310 ? -0.307  56.671  -1.515  1.00 28.07  ? 339 GLY D C   1 
ATOM   12700 O O   . GLY D 1 310 ? 0.366   56.480  -2.531  1.00 27.54  ? 339 GLY D O   1 
ATOM   12701 N N   . ARG D 1 311 ? 0.031   57.498  -0.523  1.00 26.61  ? 340 ARG D N   1 
ATOM   12702 C CA  . ARG D 1 311 ? 1.259   58.269  -0.488  1.00 27.56  ? 340 ARG D CA  1 
ATOM   12703 C C   . ARG D 1 311 ? 2.122   57.785  0.684   1.00 28.49  ? 340 ARG D C   1 
ATOM   12704 O O   . ARG D 1 311 ? 1.600   57.124  1.592   1.00 31.09  ? 340 ARG D O   1 
ATOM   12705 C CB  . ARG D 1 311 ? 0.882   59.747  -0.341  1.00 27.65  ? 340 ARG D CB  1 
ATOM   12706 C CG  . ARG D 1 311 ? 0.185   60.360  -1.549  1.00 33.76  ? 340 ARG D CG  1 
ATOM   12707 C CD  . ARG D 1 311 ? -0.567  61.641  -1.193  1.00 35.33  ? 340 ARG D CD  1 
ATOM   12708 N NE  . ARG D 1 311 ? 0.114   62.411  -0.157  1.00 44.14  ? 340 ARG D NE  1 
ATOM   12709 C CZ  . ARG D 1 311 ? -0.370  63.507  0.422   1.00 50.45  ? 340 ARG D CZ  1 
ATOM   12710 N NH1 . ARG D 1 311 ? 0.184   63.972  1.533   1.00 47.20  ? 340 ARG D NH1 1 
ATOM   12711 N NH2 . ARG D 1 311 ? -1.454  64.083  -0.073  1.00 50.07  ? 340 ARG D NH2 1 
ATOM   12712 N N   . VAL D 1 312 ? 3.430   58.124  0.674   1.00 26.59  ? 341 VAL D N   1 
ATOM   12713 C CA  . VAL D 1 312 ? 4.302   57.853  1.809   1.00 27.64  ? 341 VAL D CA  1 
ATOM   12714 C C   . VAL D 1 312 ? 4.486   59.106  2.678   1.00 27.52  ? 341 VAL D C   1 
ATOM   12715 O O   . VAL D 1 312 ? 4.322   60.252  2.242   1.00 27.40  ? 341 VAL D O   1 
ATOM   12716 C CB  . VAL D 1 312 ? 5.666   57.253  1.379   1.00 30.15  ? 341 VAL D CB  1 
ATOM   12717 C CG1 . VAL D 1 312 ? 5.507   55.896  0.711   1.00 30.89  ? 341 VAL D CG1 1 
ATOM   12718 C CG2 . VAL D 1 312 ? 6.485   58.195  0.499   1.00 29.80  ? 341 VAL D CG2 1 
ATOM   12719 N N   . VAL D 1 313 ? 4.814   58.869  3.958   1.00 30.09  ? 342 VAL D N   1 
ATOM   12720 C CA  . VAL D 1 313 ? 5.336   59.906  4.831   1.00 27.95  ? 342 VAL D CA  1 
ATOM   12721 C C   . VAL D 1 313 ? 6.788   60.141  4.427   1.00 26.24  ? 342 VAL D C   1 
ATOM   12722 O O   . VAL D 1 313 ? 7.615   59.259  4.629   1.00 26.18  ? 342 VAL D O   1 
ATOM   12723 C CB  . VAL D 1 313 ? 5.237   59.488  6.317   1.00 27.74  ? 342 VAL D CB  1 
ATOM   12724 C CG1 . VAL D 1 313 ? 5.766   60.555  7.247   1.00 25.94  ? 342 VAL D CG1 1 
ATOM   12725 C CG2 . VAL D 1 313 ? 3.842   59.102  6.738   1.00 28.09  ? 342 VAL D CG2 1 
ATOM   12726 N N   . PRO D 1 314 ? 7.180   61.298  3.831   1.00 26.22  ? 343 PRO D N   1 
ATOM   12727 C CA  . PRO D 1 314 ? 8.590   61.520  3.500   1.00 27.60  ? 343 PRO D CA  1 
ATOM   12728 C C   . PRO D 1 314 ? 9.473   61.575  4.750   1.00 23.68  ? 343 PRO D C   1 
ATOM   12729 O O   . PRO D 1 314 ? 9.047   62.058  5.793   1.00 20.84  ? 343 PRO D O   1 
ATOM   12730 C CB  . PRO D 1 314 ? 8.595   62.872  2.774   1.00 28.56  ? 343 PRO D CB  1 
ATOM   12731 C CG  . PRO D 1 314 ? 7.353   63.554  3.280   1.00 27.50  ? 343 PRO D CG  1 
ATOM   12732 C CD  . PRO D 1 314 ? 6.342   62.446  3.454   1.00 26.46  ? 343 PRO D CD  1 
ATOM   12733 N N   . GLY D 1 315 ? 10.711  61.077  4.609   1.00 24.59  ? 344 GLY D N   1 
ATOM   12734 C CA  . GLY D 1 315 ? 11.718  61.147  5.653   1.00 26.76  ? 344 GLY D CA  1 
ATOM   12735 C C   . GLY D 1 315 ? 11.673  59.925  6.570   1.00 25.08  ? 344 GLY D C   1 
ATOM   12736 O O   . GLY D 1 315 ? 12.507  59.776  7.457   1.00 24.73  ? 344 GLY D O   1 
ATOM   12737 N N   . TYR D 1 316 ? 10.690  59.046  6.334   1.00 24.81  ? 345 TYR D N   1 
ATOM   12738 C CA  . TYR D 1 316 ? 10.499  57.875  7.171   1.00 25.55  ? 345 TYR D CA  1 
ATOM   12739 C C   . TYR D 1 316 ? 10.686  56.617  6.338   1.00 25.38  ? 345 TYR D C   1 
ATOM   12740 O O   . TYR D 1 316 ? 10.516  56.631  5.126   1.00 25.56  ? 345 TYR D O   1 
ATOM   12741 C CB  . TYR D 1 316 ? 9.151   57.959  7.887   1.00 27.13  ? 345 TYR D CB  1 
ATOM   12742 C CG  . TYR D 1 316 ? 9.218   58.835  9.109   1.00 27.11  ? 345 TYR D CG  1 
ATOM   12743 C CD1 . TYR D 1 316 ? 9.248   60.215  9.004   1.00 29.61  ? 345 TYR D CD1 1 
ATOM   12744 C CD2 . TYR D 1 316 ? 9.297   58.282  10.374  1.00 29.07  ? 345 TYR D CD2 1 
ATOM   12745 C CE1 . TYR D 1 316 ? 9.319   61.021  10.129  1.00 27.60  ? 345 TYR D CE1 1 
ATOM   12746 C CE2 . TYR D 1 316 ? 9.361   59.073  11.508  1.00 27.19  ? 345 TYR D CE2 1 
ATOM   12747 C CZ  . TYR D 1 316 ? 9.363   60.449  11.385  1.00 27.04  ? 345 TYR D CZ  1 
ATOM   12748 O OH  . TYR D 1 316 ? 9.455   61.220  12.521  1.00 30.16  ? 345 TYR D OH  1 
ATOM   12749 N N   . GLY D 1 317 ? 11.159  55.559  6.993   1.00 23.45  ? 346 GLY D N   1 
ATOM   12750 C CA  . GLY D 1 317 ? 11.398  54.302  6.313   1.00 24.72  ? 346 GLY D CA  1 
ATOM   12751 C C   . GLY D 1 317 ? 12.807  54.206  5.750   1.00 23.93  ? 346 GLY D C   1 
ATOM   12752 O O   . GLY D 1 317 ? 13.505  55.205  5.565   1.00 24.39  ? 346 GLY D O   1 
ATOM   12753 N N   . HIS D 1 318 ? 13.227  52.967  5.507   1.00 21.99  ? 347 HIS D N   1 
ATOM   12754 C CA  . HIS D 1 318 ? 14.505  52.704  4.883   1.00 21.44  ? 347 HIS D CA  1 
ATOM   12755 C C   . HIS D 1 318 ? 14.531  51.246  4.455   1.00 23.44  ? 347 HIS D C   1 
ATOM   12756 O O   . HIS D 1 318 ? 13.920  50.426  5.114   1.00 23.00  ? 347 HIS D O   1 
ATOM   12757 C CB  . HIS D 1 318 ? 15.639  52.992  5.866   1.00 24.43  ? 347 HIS D CB  1 
ATOM   12758 C CG  . HIS D 1 318 ? 16.899  53.300  5.165   1.00 24.22  ? 347 HIS D CG  1 
ATOM   12759 N ND1 . HIS D 1 318 ? 17.734  52.308  4.704   1.00 21.91  ? 347 HIS D ND1 1 
ATOM   12760 C CD2 . HIS D 1 318 ? 17.449  54.466  4.805   1.00 22.34  ? 347 HIS D CD2 1 
ATOM   12761 C CE1 . HIS D 1 318 ? 18.780  52.870  4.112   1.00 23.67  ? 347 HIS D CE1 1 
ATOM   12762 N NE2 . HIS D 1 318 ? 18.620  54.181  4.148   1.00 21.89  ? 347 HIS D NE2 1 
ATOM   12763 N N   . ALA D 1 319 ? 15.278  50.919  3.393   1.00 24.78  ? 348 ALA D N   1 
ATOM   12764 C CA  . ALA D 1 319 ? 15.294  49.560  2.878   1.00 27.32  ? 348 ALA D CA  1 
ATOM   12765 C C   . ALA D 1 319 ? 16.210  48.640  3.679   1.00 29.02  ? 348 ALA D C   1 
ATOM   12766 O O   . ALA D 1 319 ? 16.132  47.414  3.527   1.00 25.05  ? 348 ALA D O   1 
ATOM   12767 C CB  . ALA D 1 319 ? 15.692  49.551  1.421   1.00 28.98  ? 348 ALA D CB  1 
ATOM   12768 N N   . VAL D 1 320 ? 17.133  49.188  4.475   1.00 29.69  ? 349 VAL D N   1 
ATOM   12769 C CA  . VAL D 1 320 ? 18.016  48.307  5.238   1.00 31.19  ? 349 VAL D CA  1 
ATOM   12770 C C   . VAL D 1 320 ? 18.111  48.728  6.709   1.00 30.60  ? 349 VAL D C   1 
ATOM   12771 O O   . VAL D 1 320 ? 18.228  47.870  7.593   1.00 27.12  ? 349 VAL D O   1 
ATOM   12772 C CB  . VAL D 1 320 ? 19.385  48.142  4.544   1.00 32.45  ? 349 VAL D CB  1 
ATOM   12773 C CG1 . VAL D 1 320 ? 19.645  49.185  3.468   1.00 39.38  ? 349 VAL D CG1 1 
ATOM   12774 C CG2 . VAL D 1 320 ? 20.550  48.066  5.510   1.00 31.39  ? 349 VAL D CG2 1 
ATOM   12775 N N   . LEU D 1 321 ? 18.083  50.034  6.995   1.00 28.13  ? 350 LEU D N   1 
ATOM   12776 C CA  . LEU D 1 321 ? 18.120  50.475  8.384   1.00 30.13  ? 350 LEU D CA  1 
ATOM   12777 C C   . LEU D 1 321 ? 16.880  49.935  9.103   1.00 28.43  ? 350 LEU D C   1 
ATOM   12778 O O   . LEU D 1 321 ? 15.764  50.025  8.589   1.00 26.73  ? 350 LEU D O   1 
ATOM   12779 C CB  . LEU D 1 321 ? 18.214  52.011  8.381   1.00 30.95  ? 350 LEU D CB  1 
ATOM   12780 C CG  . LEU D 1 321 ? 19.024  52.711  9.475   1.00 35.66  ? 350 LEU D CG  1 
ATOM   12781 C CD1 . LEU D 1 321 ? 20.135  51.862  10.055  1.00 34.49  ? 350 LEU D CD1 1 
ATOM   12782 C CD2 . LEU D 1 321 ? 19.613  54.002  8.930   1.00 39.54  ? 350 LEU D CD2 1 
ATOM   12783 N N   . ARG D 1 322 ? 17.080  49.308  10.271  1.00 28.01  ? 351 ARG D N   1 
ATOM   12784 C CA  . ARG D 1 322 ? 15.959  48.805  11.047  1.00 30.78  ? 351 ARG D CA  1 
ATOM   12785 C C   . ARG D 1 322 ? 15.772  49.600  12.339  1.00 33.61  ? 351 ARG D C   1 
ATOM   12786 O O   . ARG D 1 322 ? 14.910  49.258  13.147  1.00 35.49  ? 351 ARG D O   1 
ATOM   12787 C CB  . ARG D 1 322 ? 16.102  47.292  11.252  1.00 32.32  ? 351 ARG D CB  1 
ATOM   12788 C CG  . ARG D 1 322 ? 15.843  46.503  9.974   1.00 37.96  ? 351 ARG D CG  1 
ATOM   12789 C CD  . ARG D 1 322 ? 14.532  46.856  9.271   1.00 45.38  ? 351 ARG D CD  1 
ATOM   12790 N NE  . ARG D 1 322 ? 14.397  46.245  7.943   1.00 51.72  ? 351 ARG D NE  1 
ATOM   12791 C CZ  . ARG D 1 322 ? 14.320  46.907  6.783   1.00 52.64  ? 351 ARG D CZ  1 
ATOM   12792 N NH1 . ARG D 1 322 ? 14.179  46.234  5.651   1.00 50.84  ? 351 ARG D NH1 1 
ATOM   12793 N NH2 . ARG D 1 322 ? 14.379  48.230  6.748   1.00 47.28  ? 351 ARG D NH2 1 
ATOM   12794 N N   . LYS D 1 323 ? 16.522  50.700  12.487  1.00 32.40  ? 352 LYS D N   1 
ATOM   12795 C CA  . LYS D 1 323 ? 16.369  51.618  13.604  1.00 35.04  ? 352 LYS D CA  1 
ATOM   12796 C C   . LYS D 1 323 ? 16.357  53.051  13.079  1.00 28.68  ? 352 LYS D C   1 
ATOM   12797 O O   . LYS D 1 323 ? 16.566  53.298  11.893  1.00 23.46  ? 352 LYS D O   1 
ATOM   12798 C CB  . LYS D 1 323 ? 17.523  51.461  14.606  1.00 39.55  ? 352 LYS D CB  1 
ATOM   12799 C CG  . LYS D 1 323 ? 17.283  50.455  15.727  1.00 49.37  ? 352 LYS D CG  1 
ATOM   12800 C CD  . LYS D 1 323 ? 18.510  50.154  16.576  1.00 53.21  ? 352 LYS D CD  1 
ATOM   12801 C CE  . LYS D 1 323 ? 19.246  51.369  17.108  1.00 55.83  ? 352 LYS D CE  1 
ATOM   12802 N NZ  . LYS D 1 323 ? 20.172  51.014  18.219  1.00 53.51  ? 352 LYS D NZ  1 
ATOM   12803 N N   . THR D 1 324 ? 16.113  53.988  13.988  1.00 26.44  ? 353 THR D N   1 
ATOM   12804 C CA  . THR D 1 324 ? 16.324  55.396  13.711  1.00 25.62  ? 353 THR D CA  1 
ATOM   12805 C C   . THR D 1 324 ? 17.725  55.563  13.136  1.00 26.81  ? 353 THR D C   1 
ATOM   12806 O O   . THR D 1 324 ? 18.668  54.966  13.643  1.00 20.41  ? 353 THR D O   1 
ATOM   12807 C CB  . THR D 1 324 ? 16.193  56.244  14.981  1.00 25.35  ? 353 THR D CB  1 
ATOM   12808 O OG1 . THR D 1 324 ? 14.864  56.137  15.505  1.00 24.87  ? 353 THR D OG1 1 
ATOM   12809 C CG2 . THR D 1 324 ? 16.500  57.711  14.745  1.00 26.88  ? 353 THR D CG2 1 
ATOM   12810 N N   . ASP D 1 325 ? 17.819  56.403  12.091  1.00 25.43  ? 354 ASP D N   1 
ATOM   12811 C CA  . ASP D 1 325 ? 19.049  56.665  11.368  1.00 25.14  ? 354 ASP D CA  1 
ATOM   12812 C C   . ASP D 1 325 ? 19.963  57.501  12.253  1.00 23.83  ? 354 ASP D C   1 
ATOM   12813 O O   . ASP D 1 325 ? 19.543  58.544  12.757  1.00 23.50  ? 354 ASP D O   1 
ATOM   12814 C CB  . ASP D 1 325 ? 18.688  57.387  10.064  1.00 23.80  ? 354 ASP D CB  1 
ATOM   12815 C CG  . ASP D 1 325 ? 19.773  57.610  9.030   1.00 23.23  ? 354 ASP D CG  1 
ATOM   12816 O OD1 . ASP D 1 325 ? 20.986  57.622  9.383   1.00 27.03  ? 354 ASP D OD1 1 
ATOM   12817 O OD2 . ASP D 1 325 ? 19.381  57.792  7.867   1.00 28.29  ? 354 ASP D OD2 1 
ATOM   12818 N N   . PRO D 1 326 ? 21.232  57.105  12.477  1.00 21.37  ? 355 PRO D N   1 
ATOM   12819 C CA  . PRO D 1 326 ? 22.154  57.957  13.227  1.00 21.81  ? 355 PRO D CA  1 
ATOM   12820 C C   . PRO D 1 326 ? 22.367  59.351  12.638  1.00 20.58  ? 355 PRO D C   1 
ATOM   12821 O O   . PRO D 1 326 ? 22.784  60.269  13.332  1.00 20.94  ? 355 PRO D O   1 
ATOM   12822 C CB  . PRO D 1 326 ? 23.457  57.143  13.267  1.00 23.33  ? 355 PRO D CB  1 
ATOM   12823 C CG  . PRO D 1 326 ? 23.315  56.121  12.147  1.00 23.38  ? 355 PRO D CG  1 
ATOM   12824 C CD  . PRO D 1 326 ? 21.835  55.814  12.094  1.00 22.15  ? 355 PRO D CD  1 
ATOM   12825 N N   . ARG D 1 327 ? 22.172  59.490  11.335  1.00 19.01  ? 356 ARG D N   1 
ATOM   12826 C CA  . ARG D 1 327 ? 22.285  60.803  10.708  1.00 19.74  ? 356 ARG D CA  1 
ATOM   12827 C C   . ARG D 1 327 ? 21.103  61.663  11.166  1.00 21.73  ? 356 ARG D C   1 
ATOM   12828 O O   . ARG D 1 327 ? 21.178  62.890  11.272  1.00 21.50  ? 356 ARG D O   1 
ATOM   12829 C CB  . ARG D 1 327 ? 22.285  60.658  9.178   1.00 19.14  ? 356 ARG D CB  1 
ATOM   12830 C CG  . ARG D 1 327 ? 23.453  59.845  8.636   1.00 21.62  ? 356 ARG D CG  1 
ATOM   12831 C CD  . ARG D 1 327 ? 23.365  59.577  7.157   1.00 20.44  ? 356 ARG D CD  1 
ATOM   12832 N NE  . ARG D 1 327 ? 22.215  58.759  6.810   1.00 19.59  ? 356 ARG D NE  1 
ATOM   12833 C CZ  . ARG D 1 327 ? 21.793  58.540  5.582   1.00 21.26  ? 356 ARG D CZ  1 
ATOM   12834 N NH1 . ARG D 1 327 ? 22.470  58.997  4.535   1.00 21.26  ? 356 ARG D NH1 1 
ATOM   12835 N NH2 . ARG D 1 327 ? 20.643  57.924  5.403   1.00 18.92  ? 356 ARG D NH2 1 
ATOM   12836 N N   . TYR D 1 328 ? 19.962  61.032  11.426  1.00 21.63  ? 357 TYR D N   1 
ATOM   12837 C CA  . TYR D 1 328 ? 18.857  61.808  11.991  1.00 23.12  ? 357 TYR D CA  1 
ATOM   12838 C C   . TYR D 1 328 ? 19.237  62.294  13.393  1.00 24.38  ? 357 TYR D C   1 
ATOM   12839 O O   . TYR D 1 328 ? 19.106  63.483  13.690  1.00 21.25  ? 357 TYR D O   1 
ATOM   12840 C CB  . TYR D 1 328 ? 17.572  60.968  11.973  1.00 22.97  ? 357 TYR D CB  1 
ATOM   12841 C CG  . TYR D 1 328 ? 16.359  61.583  12.623  1.00 23.15  ? 357 TYR D CG  1 
ATOM   12842 C CD1 . TYR D 1 328 ? 16.113  61.437  13.983  1.00 25.94  ? 357 TYR D CD1 1 
ATOM   12843 C CD2 . TYR D 1 328 ? 15.435  62.295  11.871  1.00 26.71  ? 357 TYR D CD2 1 
ATOM   12844 C CE1 . TYR D 1 328 ? 14.989  61.994  14.581  1.00 26.48  ? 357 TYR D CE1 1 
ATOM   12845 C CE2 . TYR D 1 328 ? 14.292  62.833  12.449  1.00 26.75  ? 357 TYR D CE2 1 
ATOM   12846 C CZ  . TYR D 1 328 ? 14.071  62.678  13.812  1.00 27.28  ? 357 TYR D CZ  1 
ATOM   12847 O OH  . TYR D 1 328 ? 12.958  63.246  14.400  1.00 29.73  ? 357 TYR D OH  1 
ATOM   12848 N N   . THR D 1 329 ? 19.706  61.376  14.244  1.00 22.34  ? 358 THR D N   1 
ATOM   12849 C CA  . THR D 1 329 ? 20.065  61.702  15.622  1.00 22.81  ? 358 THR D CA  1 
ATOM   12850 C C   . THR D 1 329 ? 21.128  62.801  15.668  1.00 23.44  ? 358 THR D C   1 
ATOM   12851 O O   . THR D 1 329 ? 21.082  63.699  16.512  1.00 25.56  ? 358 THR D O   1 
ATOM   12852 C CB  . THR D 1 329 ? 20.601  60.459  16.331  1.00 26.82  ? 358 THR D CB  1 
ATOM   12853 O OG1 . THR D 1 329 ? 19.561  59.485  16.269  1.00 25.32  ? 358 THR D OG1 1 
ATOM   12854 C CG2 . THR D 1 329 ? 21.050  60.734  17.753  1.00 24.88  ? 358 THR D CG2 1 
ATOM   12855 N N   . CYS D 1 330 ? 22.093  62.713  14.748  1.00 23.94  ? 359 CYS D N   1 
ATOM   12856 C CA  . CYS D 1 330 ? 23.191  63.662  14.681  1.00 26.98  ? 359 CYS D CA  1 
ATOM   12857 C C   . CYS D 1 330 ? 22.678  65.071  14.368  1.00 28.16  ? 359 CYS D C   1 
ATOM   12858 O O   . CYS D 1 330 ? 23.239  66.061  14.865  1.00 26.31  ? 359 CYS D O   1 
ATOM   12859 C CB  . CYS D 1 330 ? 24.207  63.177  13.659  1.00 30.34  ? 359 CYS D CB  1 
ATOM   12860 S SG  . CYS D 1 330 ? 25.349  64.463  13.114  1.00 37.44  ? 359 CYS D SG  1 
ATOM   12861 N N   . GLN D 1 331 ? 21.630  65.159  13.528  1.00 25.98  ? 360 GLN D N   1 
ATOM   12862 C CA  . GLN D 1 331 ? 21.046  66.442  13.144  1.00 25.31  ? 360 GLN D CA  1 
ATOM   12863 C C   . GLN D 1 331 ? 20.197  66.998  14.290  1.00 26.67  ? 360 GLN D C   1 
ATOM   12864 O O   . GLN D 1 331 ? 20.160  68.214  14.522  1.00 23.60  ? 360 GLN D O   1 
ATOM   12865 C CB  . GLN D 1 331 ? 20.248  66.302  11.841  1.00 28.25  ? 360 GLN D CB  1 
ATOM   12866 C CG  . GLN D 1 331 ? 21.129  66.138  10.595  1.00 26.80  ? 360 GLN D CG  1 
ATOM   12867 C CD  . GLN D 1 331 ? 20.332  65.853  9.339   1.00 28.73  ? 360 GLN D CD  1 
ATOM   12868 O OE1 . GLN D 1 331 ? 19.654  64.835  9.218   1.00 26.07  ? 360 GLN D OE1 1 
ATOM   12869 N NE2 . GLN D 1 331 ? 20.366  66.776  8.399   1.00 29.48  ? 360 GLN D NE2 1 
ATOM   12870 N N   . ARG D 1 332 ? 19.490  66.103  14.995  1.00 28.09  ? 361 ARG D N   1 
ATOM   12871 C CA  . ARG D 1 332 ? 18.780  66.446  16.227  1.00 28.95  ? 361 ARG D CA  1 
ATOM   12872 C C   . ARG D 1 332 ? 19.745  67.039  17.260  1.00 30.26  ? 361 ARG D C   1 
ATOM   12873 O O   . ARG D 1 332 ? 19.429  68.048  17.883  1.00 27.07  ? 361 ARG D O   1 
ATOM   12874 C CB  . ARG D 1 332 ? 18.085  65.195  16.774  1.00 33.76  ? 361 ARG D CB  1 
ATOM   12875 C CG  . ARG D 1 332 ? 17.792  65.211  18.268  1.00 37.94  ? 361 ARG D CG  1 
ATOM   12876 C CD  . ARG D 1 332 ? 16.339  65.332  18.643  1.00 43.45  ? 361 ARG D CD  1 
ATOM   12877 N NE  . ARG D 1 332 ? 16.295  65.491  20.089  1.00 50.10  ? 361 ARG D NE  1 
ATOM   12878 C CZ  . ARG D 1 332 ? 15.415  66.230  20.757  1.00 53.00  ? 361 ARG D CZ  1 
ATOM   12879 N NH1 . ARG D 1 332 ? 14.265  66.578  20.208  1.00 48.86  ? 361 ARG D NH1 1 
ATOM   12880 N NH2 . ARG D 1 332 ? 15.670  66.563  22.010  1.00 57.69  ? 361 ARG D NH2 1 
ATOM   12881 N N   . GLU D 1 333 ? 20.906  66.393  17.453  1.00 26.96  ? 362 GLU D N   1 
ATOM   12882 C CA  . GLU D 1 333 ? 21.946  66.903  18.336  1.00 28.29  ? 362 GLU D CA  1 
ATOM   12883 C C   . GLU D 1 333 ? 22.287  68.346  17.982  1.00 27.82  ? 362 GLU D C   1 
ATOM   12884 O O   . GLU D 1 333 ? 22.424  69.184  18.861  1.00 26.54  ? 362 GLU D O   1 
ATOM   12885 C CB  . GLU D 1 333 ? 23.215  66.052  18.238  1.00 34.84  ? 362 GLU D CB  1 
ATOM   12886 C CG  . GLU D 1 333 ? 23.219  64.857  19.164  1.00 41.47  ? 362 GLU D CG  1 
ATOM   12887 C CD  . GLU D 1 333 ? 24.372  63.876  19.021  1.00 45.01  ? 362 GLU D CD  1 
ATOM   12888 O OE1 . GLU D 1 333 ? 24.991  63.801  17.934  1.00 46.29  ? 362 GLU D OE1 1 
ATOM   12889 O OE2 . GLU D 1 333 ? 24.656  63.194  20.017  1.00 52.15  ? 362 GLU D OE2 1 
ATOM   12890 N N   . PHE D 1 334 ? 22.472  68.615  16.686  1.00 25.47  ? 363 PHE D N   1 
ATOM   12891 C CA  . PHE D 1 334 ? 22.905  69.929  16.247  1.00 25.47  ? 363 PHE D CA  1 
ATOM   12892 C C   . PHE D 1 334 ? 21.798  70.964  16.465  1.00 27.36  ? 363 PHE D C   1 
ATOM   12893 O O   . PHE D 1 334 ? 22.109  72.111  16.768  1.00 33.42  ? 363 PHE D O   1 
ATOM   12894 C CB  . PHE D 1 334 ? 23.408  69.872  14.799  1.00 25.38  ? 363 PHE D CB  1 
ATOM   12895 C CG  . PHE D 1 334 ? 23.853  71.201  14.239  1.00 23.63  ? 363 PHE D CG  1 
ATOM   12896 C CD1 . PHE D 1 334 ? 22.926  72.148  13.814  1.00 24.95  ? 363 PHE D CD1 1 
ATOM   12897 C CD2 . PHE D 1 334 ? 25.200  71.530  14.178  1.00 26.22  ? 363 PHE D CD2 1 
ATOM   12898 C CE1 . PHE D 1 334 ? 23.332  73.386  13.341  1.00 24.36  ? 363 PHE D CE1 1 
ATOM   12899 C CE2 . PHE D 1 334 ? 25.608  72.767  13.679  1.00 23.72  ? 363 PHE D CE2 1 
ATOM   12900 C CZ  . PHE D 1 334 ? 24.677  73.690  13.260  1.00 25.23  ? 363 PHE D CZ  1 
ATOM   12901 N N   . ALA D 1 335 ? 20.526  70.596  16.255  1.00 26.09  ? 364 ALA D N   1 
ATOM   12902 C CA  . ALA D 1 335 ? 19.417  71.490  16.559  1.00 29.92  ? 364 ALA D CA  1 
ATOM   12903 C C   . ALA D 1 335 ? 19.391  71.809  18.055  1.00 34.39  ? 364 ALA D C   1 
ATOM   12904 O O   . ALA D 1 335 ? 19.324  72.977  18.448  1.00 37.78  ? 364 ALA D O   1 
ATOM   12905 C CB  . ALA D 1 335 ? 18.114  70.883  16.118  1.00 31.24  ? 364 ALA D CB  1 
ATOM   12906 N N   . LEU D 1 336 ? 19.453  70.784  18.914  1.00 32.99  ? 365 LEU D N   1 
ATOM   12907 C CA  . LEU D 1 336 ? 19.215  71.046  20.329  1.00 36.85  ? 365 LEU D CA  1 
ATOM   12908 C C   . LEU D 1 336 ? 20.335  71.899  20.929  1.00 36.62  ? 365 LEU D C   1 
ATOM   12909 O O   . LEU D 1 336 ? 20.120  72.543  21.949  1.00 40.28  ? 365 LEU D O   1 
ATOM   12910 C CB  . LEU D 1 336 ? 19.054  69.731  21.089  1.00 39.54  ? 365 LEU D CB  1 
ATOM   12911 C CG  . LEU D 1 336 ? 20.294  68.851  21.139  1.00 48.51  ? 365 LEU D CG  1 
ATOM   12912 C CD1 . LEU D 1 336 ? 21.191  69.196  22.328  1.00 50.52  ? 365 LEU D CD1 1 
ATOM   12913 C CD2 . LEU D 1 336 ? 19.879  67.388  21.148  1.00 53.54  ? 365 LEU D CD2 1 
ATOM   12914 N N   . LYS D 1 337 ? 21.529  71.896  20.322  1.00 37.42  ? 366 LYS D N   1 
ATOM   12915 C CA  . LYS D 1 337 ? 22.607  72.781  20.743  1.00 36.09  ? 366 LYS D CA  1 
ATOM   12916 C C   . LYS D 1 337 ? 22.384  74.213  20.244  1.00 38.65  ? 366 LYS D C   1 
ATOM   12917 O O   . LYS D 1 337 ? 22.659  75.157  20.988  1.00 37.04  ? 366 LYS D O   1 
ATOM   12918 C CB  . LYS D 1 337 ? 23.959  72.239  20.259  1.00 41.28  ? 366 LYS D CB  1 
ATOM   12919 C CG  . LYS D 1 337 ? 25.191  72.981  20.774  1.00 41.85  ? 366 LYS D CG  1 
ATOM   12920 C CD  . LYS D 1 337 ? 26.494  72.205  20.635  1.00 45.01  ? 366 LYS D CD  1 
ATOM   12921 C CE  . LYS D 1 337 ? 27.722  73.091  20.633  1.00 48.82  ? 366 LYS D CE  1 
ATOM   12922 N NZ  . LYS D 1 337 ? 27.725  74.045  21.774  1.00 50.78  ? 366 LYS D NZ  1 
ATOM   12923 N N   . HIS D 1 338 ? 21.928  74.393  18.987  1.00 34.29  ? 367 HIS D N   1 
ATOM   12924 C CA  . HIS D 1 338 ? 21.958  75.712  18.359  1.00 34.16  ? 367 HIS D CA  1 
ATOM   12925 C C   . HIS D 1 338 ? 20.583  76.292  18.043  1.00 34.89  ? 367 HIS D C   1 
ATOM   12926 O O   . HIS D 1 338 ? 20.495  77.489  17.780  1.00 38.86  ? 367 HIS D O   1 
ATOM   12927 C CB  . HIS D 1 338 ? 22.787  75.733  17.067  1.00 34.24  ? 367 HIS D CB  1 
ATOM   12928 C CG  . HIS D 1 338 ? 24.153  75.190  17.257  1.00 34.74  ? 367 HIS D CG  1 
ATOM   12929 N ND1 . HIS D 1 338 ? 25.160  75.870  17.902  1.00 35.78  ? 367 HIS D ND1 1 
ATOM   12930 C CD2 . HIS D 1 338 ? 24.660  74.006  16.898  1.00 32.78  ? 367 HIS D CD2 1 
ATOM   12931 C CE1 . HIS D 1 338 ? 26.250  75.109  17.928  1.00 39.78  ? 367 HIS D CE1 1 
ATOM   12932 N NE2 . HIS D 1 338 ? 25.966  73.971  17.320  1.00 39.18  ? 367 HIS D NE2 1 
ATOM   12933 N N   . LEU D 1 339 ? 19.522  75.479  18.016  1.00 32.02  ? 368 LEU D N   1 
ATOM   12934 C CA  . LEU D 1 339 ? 18.203  76.043  17.796  1.00 33.22  ? 368 LEU D CA  1 
ATOM   12935 C C   . LEU D 1 339 ? 17.154  75.219  18.531  1.00 32.80  ? 368 LEU D C   1 
ATOM   12936 O O   . LEU D 1 339 ? 16.153  74.837  17.943  1.00 35.73  ? 368 LEU D O   1 
ATOM   12937 C CB  . LEU D 1 339 ? 17.952  76.107  16.286  1.00 32.47  ? 368 LEU D CB  1 
ATOM   12938 C CG  . LEU D 1 339 ? 18.055  74.776  15.542  1.00 33.45  ? 368 LEU D CG  1 
ATOM   12939 C CD1 . LEU D 1 339 ? 16.788  74.506  14.736  1.00 36.35  ? 368 LEU D CD1 1 
ATOM   12940 C CD2 . LEU D 1 339 ? 19.290  74.742  14.649  1.00 35.68  ? 368 LEU D CD2 1 
ATOM   12941 N N   . PRO D 1 340 ? 17.298  74.989  19.853  1.00 34.90  ? 369 PRO D N   1 
ATOM   12942 C CA  . PRO D 1 340 ? 16.426  74.051  20.561  1.00 37.63  ? 369 PRO D CA  1 
ATOM   12943 C C   . PRO D 1 340 ? 14.948  74.452  20.636  1.00 40.54  ? 369 PRO D C   1 
ATOM   12944 O O   . PRO D 1 340 ? 14.103  73.630  20.977  1.00 42.79  ? 369 PRO D O   1 
ATOM   12945 C CB  . PRO D 1 340 ? 17.004  74.012  21.983  1.00 36.98  ? 369 PRO D CB  1 
ATOM   12946 C CG  . PRO D 1 340 ? 17.761  75.312  22.133  1.00 36.50  ? 369 PRO D CG  1 
ATOM   12947 C CD  . PRO D 1 340 ? 18.261  75.656  20.743  1.00 38.10  ? 369 PRO D CD  1 
ATOM   12948 N N   . ASN D 1 341 ? 14.642  75.710  20.304  1.00 42.96  ? 370 ASN D N   1 
ATOM   12949 C CA  . ASN D 1 341 ? 13.326  76.265  20.550  1.00 44.49  ? 370 ASN D CA  1 
ATOM   12950 C C   . ASN D 1 341 ? 12.591  76.618  19.261  1.00 43.34  ? 370 ASN D C   1 
ATOM   12951 O O   . ASN D 1 341 ? 11.431  77.017  19.348  1.00 40.12  ? 370 ASN D O   1 
ATOM   12952 C CB  . ASN D 1 341 ? 13.419  77.520  21.415  1.00 52.05  ? 370 ASN D CB  1 
ATOM   12953 C CG  . ASN D 1 341 ? 14.030  77.269  22.777  1.00 52.47  ? 370 ASN D CG  1 
ATOM   12954 O OD1 . ASN D 1 341 ? 13.606  76.360  23.489  1.00 47.40  ? 370 ASN D OD1 1 
ATOM   12955 N ND2 . ASN D 1 341 ? 15.007  78.081  23.150  1.00 55.67  ? 370 ASN D ND2 1 
ATOM   12956 N N   . ASP D 1 342 ? 13.262  76.507  18.095  1.00 39.69  ? 371 ASP D N   1 
ATOM   12957 C CA  . ASP D 1 342 ? 12.624  76.702  16.802  1.00 37.18  ? 371 ASP D CA  1 
ATOM   12958 C C   . ASP D 1 342 ? 11.362  75.849  16.752  1.00 35.90  ? 371 ASP D C   1 
ATOM   12959 O O   . ASP D 1 342 ? 11.437  74.667  17.075  1.00 35.45  ? 371 ASP D O   1 
ATOM   12960 C CB  . ASP D 1 342 ? 13.520  76.276  15.627  1.00 38.42  ? 371 ASP D CB  1 
ATOM   12961 C CG  . ASP D 1 342 ? 12.957  76.594  14.244  1.00 39.01  ? 371 ASP D CG  1 
ATOM   12962 O OD1 . ASP D 1 342 ? 13.181  77.729  13.764  1.00 38.29  ? 371 ASP D OD1 1 
ATOM   12963 O OD2 . ASP D 1 342 ? 12.273  75.713  13.654  1.00 41.47  ? 371 ASP D OD2 1 
ATOM   12964 N N   . PRO D 1 343 ? 10.193  76.412  16.350  1.00 37.93  ? 372 PRO D N   1 
ATOM   12965 C CA  . PRO D 1 343 ? 8.933   75.659  16.275  1.00 34.60  ? 372 PRO D CA  1 
ATOM   12966 C C   . PRO D 1 343 ? 8.886   74.518  15.258  1.00 36.83  ? 372 PRO D C   1 
ATOM   12967 O O   . PRO D 1 343 ? 8.226   73.515  15.511  1.00 33.30  ? 372 PRO D O   1 
ATOM   12968 C CB  . PRO D 1 343 ? 7.884   76.710  15.858  1.00 36.44  ? 372 PRO D CB  1 
ATOM   12969 C CG  . PRO D 1 343 ? 8.517   78.049  16.222  1.00 35.93  ? 372 PRO D CG  1 
ATOM   12970 C CD  . PRO D 1 343 ? 10.001  77.839  16.024  1.00 37.80  ? 372 PRO D CD  1 
ATOM   12971 N N   . MET D 1 344 ? 9.572   74.670  14.108  1.00 38.50  ? 373 MET D N   1 
ATOM   12972 C CA  . MET D 1 344 ? 9.579   73.615  13.101  1.00 38.22  ? 373 MET D CA  1 
ATOM   12973 C C   . MET D 1 344 ? 10.364  72.407  13.604  1.00 36.11  ? 373 MET D C   1 
ATOM   12974 O O   . MET D 1 344 ? 9.958   71.272  13.347  1.00 35.03  ? 373 MET D O   1 
ATOM   12975 C CB  . MET D 1 344 ? 10.146  74.076  11.751  1.00 40.41  ? 373 MET D CB  1 
ATOM   12976 C CG  . MET D 1 344 ? 9.155   73.904  10.602  1.00 45.92  ? 373 MET D CG  1 
ATOM   12977 S SD  . MET D 1 344 ? 9.245   75.193  9.341   1.00 48.28  ? 373 MET D SD  1 
ATOM   12978 C CE  . MET D 1 344 ? 7.680   74.974  8.495   1.00 48.95  ? 373 MET D CE  1 
ATOM   12979 N N   . PHE D 1 345 ? 11.488  72.657  14.296  1.00 33.40  ? 374 PHE D N   1 
ATOM   12980 C CA  . PHE D 1 345 ? 12.256  71.597  14.925  1.00 32.45  ? 374 PHE D CA  1 
ATOM   12981 C C   . PHE D 1 345 ? 11.377  70.859  15.936  1.00 28.71  ? 374 PHE D C   1 
ATOM   12982 O O   . PHE D 1 345 ? 11.391  69.629  15.999  1.00 28.21  ? 374 PHE D O   1 
ATOM   12983 C CB  . PHE D 1 345 ? 13.540  72.144  15.558  1.00 34.77  ? 374 PHE D CB  1 
ATOM   12984 C CG  . PHE D 1 345 ? 14.177  71.186  16.530  1.00 37.17  ? 374 PHE D CG  1 
ATOM   12985 C CD1 . PHE D 1 345 ? 14.480  69.885  16.147  1.00 37.84  ? 374 PHE D CD1 1 
ATOM   12986 C CD2 . PHE D 1 345 ? 14.435  71.567  17.841  1.00 35.97  ? 374 PHE D CD2 1 
ATOM   12987 C CE1 . PHE D 1 345 ? 15.040  68.993  17.051  1.00 42.06  ? 374 PHE D CE1 1 
ATOM   12988 C CE2 . PHE D 1 345 ? 15.018  70.681  18.731  1.00 37.26  ? 374 PHE D CE2 1 
ATOM   12989 C CZ  . PHE D 1 345 ? 15.317  69.395  18.337  1.00 40.19  ? 374 PHE D CZ  1 
ATOM   12990 N N   . LYS D 1 346 ? 10.591  71.626  16.706  1.00 29.87  ? 375 LYS D N   1 
ATOM   12991 C CA  . LYS D 1 346 ? 9.642   71.081  17.663  1.00 32.11  ? 375 LYS D CA  1 
ATOM   12992 C C   . LYS D 1 346 ? 8.639   70.166  16.953  1.00 31.16  ? 375 LYS D C   1 
ATOM   12993 O O   . LYS D 1 346 ? 8.325   69.090  17.467  1.00 28.17  ? 375 LYS D O   1 
ATOM   12994 C CB  . LYS D 1 346 ? 8.878   72.196  18.394  1.00 34.59  ? 375 LYS D CB  1 
ATOM   12995 C CG  . LYS D 1 346 ? 8.773   72.032  19.907  1.00 43.17  ? 375 LYS D CG  1 
ATOM   12996 C CD  . LYS D 1 346 ? 10.108  72.063  20.647  1.00 40.95  ? 375 LYS D CD  1 
ATOM   12997 C CE  . LYS D 1 346 ? 10.937  73.293  20.338  1.00 44.63  ? 375 LYS D CE  1 
ATOM   12998 N NZ  . LYS D 1 346 ? 11.784  73.110  19.130  1.00 45.28  ? 375 LYS D NZ  1 
ATOM   12999 N N   . LEU D 1 347 ? 8.177   70.572  15.756  1.00 28.77  ? 376 LEU D N   1 
ATOM   13000 C CA  . LEU D 1 347 ? 7.179   69.796  15.022  1.00 29.48  ? 376 LEU D CA  1 
ATOM   13001 C C   . LEU D 1 347 ? 7.802   68.494  14.505  1.00 29.79  ? 376 LEU D C   1 
ATOM   13002 O O   . LEU D 1 347 ? 7.187   67.428  14.580  1.00 28.02  ? 376 LEU D O   1 
ATOM   13003 C CB  . LEU D 1 347 ? 6.606   70.642  13.885  1.00 33.49  ? 376 LEU D CB  1 
ATOM   13004 C CG  . LEU D 1 347 ? 5.546   69.960  13.022  1.00 37.43  ? 376 LEU D CG  1 
ATOM   13005 C CD1 . LEU D 1 347 ? 4.332   69.577  13.847  1.00 38.14  ? 376 LEU D CD1 1 
ATOM   13006 C CD2 . LEU D 1 347 ? 5.124   70.854  11.862  1.00 36.47  ? 376 LEU D CD2 1 
ATOM   13007 N N   . VAL D 1 348 ? 9.049   68.578  14.021  1.00 25.70  ? 377 VAL D N   1 
ATOM   13008 C CA  . VAL D 1 348 ? 9.770   67.391  13.582  1.00 28.07  ? 377 VAL D CA  1 
ATOM   13009 C C   . VAL D 1 348 ? 9.893   66.473  14.788  1.00 28.44  ? 377 VAL D C   1 
ATOM   13010 O O   . VAL D 1 348 ? 9.743   65.264  14.675  1.00 27.78  ? 377 VAL D O   1 
ATOM   13011 C CB  . VAL D 1 348 ? 11.156  67.759  13.006  1.00 28.80  ? 377 VAL D CB  1 
ATOM   13012 C CG1 . VAL D 1 348 ? 12.123  66.586  12.972  1.00 27.89  ? 377 VAL D CG1 1 
ATOM   13013 C CG2 . VAL D 1 348 ? 11.020  68.401  11.624  1.00 29.52  ? 377 VAL D CG2 1 
ATOM   13014 N N   . ALA D 1 349 ? 10.178  67.076  15.948  1.00 30.34  ? 378 ALA D N   1 
ATOM   13015 C CA  . ALA D 1 349 ? 10.402  66.314  17.160  1.00 33.28  ? 378 ALA D CA  1 
ATOM   13016 C C   . ALA D 1 349 ? 9.095   65.678  17.649  1.00 34.15  ? 378 ALA D C   1 
ATOM   13017 O O   . ALA D 1 349 ? 9.127   64.620  18.294  1.00 29.96  ? 378 ALA D O   1 
ATOM   13018 C CB  . ALA D 1 349 ? 11.033  67.207  18.206  1.00 34.60  ? 378 ALA D CB  1 
ATOM   13019 N N   . GLN D 1 350 ? 7.943   66.317  17.392  1.00 29.40  ? 379 GLN D N   1 
ATOM   13020 C CA  . GLN D 1 350 ? 6.692   65.724  17.851  1.00 32.50  ? 379 GLN D CA  1 
ATOM   13021 C C   . GLN D 1 350 ? 6.313   64.599  16.889  1.00 30.87  ? 379 GLN D C   1 
ATOM   13022 O O   . GLN D 1 350 ? 5.764   63.581  17.311  1.00 33.09  ? 379 GLN D O   1 
ATOM   13023 C CB  . GLN D 1 350 ? 5.598   66.782  18.057  1.00 36.23  ? 379 GLN D CB  1 
ATOM   13024 C CG  . GLN D 1 350 ? 5.772   67.611  19.330  1.00 39.50  ? 379 GLN D CG  1 
ATOM   13025 C CD  . GLN D 1 350 ? 4.808   67.324  20.456  1.00 41.21  ? 379 GLN D CD  1 
ATOM   13026 O OE1 . GLN D 1 350 ? 4.099   68.210  20.936  1.00 45.41  ? 379 GLN D OE1 1 
ATOM   13027 N NE2 . GLN D 1 350 ? 4.781   66.081  20.903  1.00 44.55  ? 379 GLN D NE2 1 
ATOM   13028 N N   . LEU D 1 351 ? 6.621   64.766  15.595  1.00 27.63  ? 380 LEU D N   1 
ATOM   13029 C CA  . LEU D 1 351 ? 6.377   63.700  14.639  1.00 26.40  ? 380 LEU D CA  1 
ATOM   13030 C C   . LEU D 1 351 ? 7.157   62.446  15.017  1.00 26.51  ? 380 LEU D C   1 
ATOM   13031 O O   . LEU D 1 351 ? 6.655   61.334  14.844  1.00 23.82  ? 380 LEU D O   1 
ATOM   13032 C CB  . LEU D 1 351 ? 6.715   64.165  13.216  1.00 29.05  ? 380 LEU D CB  1 
ATOM   13033 C CG  . LEU D 1 351 ? 5.553   64.661  12.342  1.00 31.90  ? 380 LEU D CG  1 
ATOM   13034 C CD1 . LEU D 1 351 ? 4.236   63.997  12.696  1.00 33.54  ? 380 LEU D CD1 1 
ATOM   13035 C CD2 . LEU D 1 351 ? 5.403   66.156  12.392  1.00 33.74  ? 380 LEU D CD2 1 
ATOM   13036 N N   . TYR D 1 352 ? 8.353   62.608  15.596  1.00 26.16  ? 381 TYR D N   1 
ATOM   13037 C CA  . TYR D 1 352 ? 9.135   61.426  15.938  1.00 24.92  ? 381 TYR D CA  1 
ATOM   13038 C C   . TYR D 1 352 ? 8.331   60.526  16.876  1.00 26.18  ? 381 TYR D C   1 
ATOM   13039 O O   . TYR D 1 352 ? 8.343   59.299  16.731  1.00 26.77  ? 381 TYR D O   1 
ATOM   13040 C CB  . TYR D 1 352 ? 10.480  61.841  16.523  1.00 26.14  ? 381 TYR D CB  1 
ATOM   13041 C CG  . TYR D 1 352 ? 11.406  60.685  16.766  1.00 27.80  ? 381 TYR D CG  1 
ATOM   13042 C CD1 . TYR D 1 352 ? 12.117  60.134  15.725  1.00 26.86  ? 381 TYR D CD1 1 
ATOM   13043 C CD2 . TYR D 1 352 ? 11.556  60.136  18.032  1.00 29.90  ? 381 TYR D CD2 1 
ATOM   13044 C CE1 . TYR D 1 352 ? 12.987  59.080  15.938  1.00 30.35  ? 381 TYR D CE1 1 
ATOM   13045 C CE2 . TYR D 1 352 ? 12.407  59.070  18.257  1.00 28.86  ? 381 TYR D CE2 1 
ATOM   13046 C CZ  . TYR D 1 352 ? 13.138  58.550  17.208  1.00 30.38  ? 381 TYR D CZ  1 
ATOM   13047 O OH  . TYR D 1 352 ? 13.993  57.494  17.419  1.00 32.17  ? 381 TYR D OH  1 
ATOM   13048 N N   . LYS D 1 353 ? 7.566   61.138  17.790  1.00 28.88  ? 382 LYS D N   1 
ATOM   13049 C CA  . LYS D 1 353 ? 6.850   60.386  18.812  1.00 28.98  ? 382 LYS D CA  1 
ATOM   13050 C C   . LYS D 1 353 ? 5.599   59.723  18.242  1.00 30.24  ? 382 LYS D C   1 
ATOM   13051 O O   . LYS D 1 353 ? 5.039   58.828  18.878  1.00 29.89  ? 382 LYS D O   1 
ATOM   13052 C CB  . LYS D 1 353 ? 6.406   61.284  19.977  1.00 30.82  ? 382 LYS D CB  1 
ATOM   13053 C CG  . LYS D 1 353 ? 7.460   62.235  20.537  1.00 30.93  ? 382 LYS D CG  1 
ATOM   13054 C CD  . LYS D 1 353 ? 6.848   63.281  21.478  1.00 32.48  ? 382 LYS D CD  1 
ATOM   13055 C CE  . LYS D 1 353 ? 7.759   64.454  21.745  1.00 36.33  ? 382 LYS D CE  1 
ATOM   13056 N NZ  . LYS D 1 353 ? 8.987   64.032  22.475  1.00 39.84  ? 382 LYS D NZ  1 
ATOM   13057 N N   . ILE D 1 354 ? 5.146   60.188  17.069  1.00 29.19  ? 383 ILE D N   1 
ATOM   13058 C CA  . ILE D 1 354 ? 3.844   59.815  16.545  1.00 25.48  ? 383 ILE D CA  1 
ATOM   13059 C C   . ILE D 1 354 ? 3.975   58.876  15.347  1.00 26.79  ? 383 ILE D C   1 
ATOM   13060 O O   . ILE D 1 354 ? 3.367   57.806  15.369  1.00 29.16  ? 383 ILE D O   1 
ATOM   13061 C CB  . ILE D 1 354 ? 3.021   61.092  16.265  1.00 27.36  ? 383 ILE D CB  1 
ATOM   13062 C CG1 . ILE D 1 354 ? 2.760   61.890  17.548  1.00 25.62  ? 383 ILE D CG1 1 
ATOM   13063 C CG2 . ILE D 1 354 ? 1.709   60.771  15.565  1.00 25.53  ? 383 ILE D CG2 1 
ATOM   13064 C CD1 . ILE D 1 354 ? 1.994   61.126  18.596  1.00 27.31  ? 383 ILE D CD1 1 
ATOM   13065 N N   . VAL D 1 355 ? 4.765   59.256  14.336  1.00 27.13  ? 384 VAL D N   1 
ATOM   13066 C CA  . VAL D 1 355 ? 4.790   58.517  13.024  1.00 26.07  ? 384 VAL D CA  1 
ATOM   13067 C C   . VAL D 1 355 ? 5.178   57.041  13.136  1.00 25.78  ? 384 VAL D C   1 
ATOM   13068 O O   . VAL D 1 355 ? 4.478   56.238  12.528  1.00 24.29  ? 384 VAL D O   1 
ATOM   13069 C CB  . VAL D 1 355 ? 5.435   59.221  11.808  1.00 29.85  ? 384 VAL D CB  1 
ATOM   13070 C CG1 . VAL D 1 355 ? 6.109   60.551  12.076  1.00 32.00  ? 384 VAL D CG1 1 
ATOM   13071 C CG2 . VAL D 1 355 ? 6.127   58.306  10.819  1.00 28.69  ? 384 VAL D CG2 1 
ATOM   13072 N N   . PRO D 1 356 ? 6.224   56.665  13.879  1.00 30.61  ? 385 PRO D N   1 
ATOM   13073 C CA  . PRO D 1 356 ? 6.551   55.258  13.953  1.00 32.28  ? 385 PRO D CA  1 
ATOM   13074 C C   . PRO D 1 356 ? 5.404   54.338  14.387  1.00 37.06  ? 385 PRO D C   1 
ATOM   13075 O O   . PRO D 1 356 ? 5.232   53.309  13.744  1.00 47.69  ? 385 PRO D O   1 
ATOM   13076 C CB  . PRO D 1 356 ? 7.759   55.284  14.894  1.00 29.88  ? 385 PRO D CB  1 
ATOM   13077 C CG  . PRO D 1 356 ? 8.390   56.623  14.626  1.00 29.57  ? 385 PRO D CG  1 
ATOM   13078 C CD  . PRO D 1 356 ? 7.186   57.529  14.530  1.00 30.06  ? 385 PRO D CD  1 
ATOM   13079 N N   . ASN D 1 357 ? 4.604   54.738  15.365  1.00 42.64  ? 386 ASN D N   1 
ATOM   13080 C CA  . ASN D 1 357 ? 3.428   53.926  15.805  1.00 38.60  ? 386 ASN D CA  1 
ATOM   13081 C C   . ASN D 1 357 ? 2.356   53.821  14.703  1.00 35.12  ? 386 ASN D C   1 
ATOM   13082 O O   . ASN D 1 357 ? 1.746   52.757  14.580  1.00 35.33  ? 386 ASN D O   1 
ATOM   13083 C CB  . ASN D 1 357 ? 2.834   54.541  17.062  1.00 40.21  ? 386 ASN D CB  1 
ATOM   13084 C CG  . ASN D 1 357 ? 2.455   53.545  18.122  1.00 41.25  ? 386 ASN D CG  1 
ATOM   13085 O OD1 . ASN D 1 357 ? 1.429   52.868  18.001  1.00 41.23  ? 386 ASN D OD1 1 
ATOM   13086 N ND2 . ASN D 1 357 ? 3.245   53.486  19.181  1.00 40.34  ? 386 ASN D ND2 1 
ATOM   13087 N N   . VAL D 1 358 ? 2.116   54.894  13.953  1.00 33.74  ? 387 VAL D N   1 
ATOM   13088 C CA  . VAL D 1 358 ? 1.084   54.905  12.879  1.00 31.17  ? 387 VAL D CA  1 
ATOM   13089 C C   . VAL D 1 358 ? 1.591   54.002  11.756  1.00 29.88  ? 387 VAL D C   1 
ATOM   13090 O O   . VAL D 1 358 ? 0.807   53.195  11.242  1.00 32.14  ? 387 VAL D O   1 
ATOM   13091 C CB  . VAL D 1 358 ? 0.797   56.326  12.370  1.00 30.18  ? 387 VAL D CB  1 
ATOM   13092 C CG1 . VAL D 1 358 ? -0.117  56.327  11.156  1.00 31.42  ? 387 VAL D CG1 1 
ATOM   13093 C CG2 . VAL D 1 358 ? 0.216   57.202  13.472  1.00 30.00  ? 387 VAL D CG2 1 
ATOM   13094 N N   . LEU D 1 359 ? 2.880   54.091  11.468  1.00 27.61  ? 388 LEU D N   1 
ATOM   13095 C CA  . LEU D 1 359 ? 3.417   53.323  10.350  1.00 29.90  ? 388 LEU D CA  1 
ATOM   13096 C C   . LEU D 1 359 ? 3.334   51.824  10.661  1.00 30.45  ? 388 LEU D C   1 
ATOM   13097 O O   . LEU D 1 359 ? 3.008   51.013  9.784   1.00 33.60  ? 388 LEU D O   1 
ATOM   13098 C CB  . LEU D 1 359 ? 4.864   53.739  10.078  1.00 30.82  ? 388 LEU D CB  1 
ATOM   13099 C CG  . LEU D 1 359 ? 5.128   54.251  8.664   1.00 36.66  ? 388 LEU D CG  1 
ATOM   13100 C CD1 . LEU D 1 359 ? 5.626   55.676  8.715   1.00 37.01  ? 388 LEU D CD1 1 
ATOM   13101 C CD2 . LEU D 1 359 ? 6.129   53.364  7.922   1.00 38.41  ? 388 LEU D CD2 1 
ATOM   13102 N N   . LEU D 1 360 ? 3.677   51.464  11.903  1.00 29.51  ? 389 LEU D N   1 
ATOM   13103 C CA  . LEU D 1 360 ? 3.613   50.078  12.364  1.00 29.27  ? 389 LEU D CA  1 
ATOM   13104 C C   . LEU D 1 360 ? 2.176   49.550  12.271  1.00 33.61  ? 389 LEU D C   1 
ATOM   13105 O O   . LEU D 1 360 ? 1.945   48.370  12.005  1.00 29.22  ? 389 LEU D O   1 
ATOM   13106 C CB  . LEU D 1 360 ? 4.095   50.028  13.813  1.00 32.49  ? 389 LEU D CB  1 
ATOM   13107 C CG  . LEU D 1 360 ? 5.594   50.234  14.037  1.00 34.57  ? 389 LEU D CG  1 
ATOM   13108 C CD1 . LEU D 1 360 ? 5.892   50.322  15.528  1.00 37.19  ? 389 LEU D CD1 1 
ATOM   13109 C CD2 . LEU D 1 360 ? 6.405   49.118  13.384  1.00 36.10  ? 389 LEU D CD2 1 
ATOM   13110 N N   . GLU D 1 361 ? 1.221   50.433  12.531  1.00 30.80  ? 390 GLU D N   1 
ATOM   13111 C CA  . GLU D 1 361 ? -0.198  50.021  12.526  1.00 37.80  ? 390 GLU D CA  1 
ATOM   13112 C C   . GLU D 1 361 ? -0.627  49.783  11.074  1.00 37.92  ? 390 GLU D C   1 
ATOM   13113 O O   . GLU D 1 361 ? -1.317  48.795  10.809  1.00 33.76  ? 390 GLU D O   1 
ATOM   13114 C CB  . GLU D 1 361 ? -0.952  51.139  13.241  1.00 38.88  ? 390 GLU D CB  1 
ATOM   13115 C CG  . GLU D 1 361 ? -1.058  50.917  14.745  1.00 43.34  ? 390 GLU D CG  1 
ATOM   13116 C CD  . GLU D 1 361 ? -1.842  52.007  15.448  1.00 42.02  ? 390 GLU D CD  1 
ATOM   13117 O OE1 . GLU D 1 361 ? -1.971  53.111  14.888  1.00 46.43  ? 390 GLU D OE1 1 
ATOM   13118 O OE2 . GLU D 1 361 ? -2.327  51.741  16.562  1.00 51.39  ? 390 GLU D OE2 1 
ATOM   13119 N N   . GLN D 1 362 ? -0.266  50.715  10.196  1.00 37.19  ? 391 GLN D N   1 
ATOM   13120 C CA  . GLN D 1 362 ? -0.545  50.500  8.762   1.00 41.36  ? 391 GLN D CA  1 
ATOM   13121 C C   . GLN D 1 362 ? 0.277   49.278  8.384   1.00 45.65  ? 391 GLN D C   1 
ATOM   13122 O O   . GLN D 1 362 ? -0.177  48.510  7.513   1.00 42.27  ? 391 GLN D O   1 
ATOM   13123 C CB  . GLN D 1 362 ? -0.133  51.750  7.990   1.00 41.91  ? 391 GLN D CB  1 
ATOM   13124 C CG  . GLN D 1 362 ? -0.614  51.788  6.544   1.00 40.90  ? 391 GLN D CG  1 
ATOM   13125 C CD  . GLN D 1 362 ? 0.355   52.475  5.607   1.00 38.75  ? 391 GLN D CD  1 
ATOM   13126 O OE1 . GLN D 1 362 ? 1.565   52.525  5.848   1.00 38.48  ? 391 GLN D OE1 1 
ATOM   13127 N NE2 . GLN D 1 362 ? -0.176  53.004  4.517   1.00 39.03  ? 391 GLN D NE2 1 
ATOM   13128 N N   . GLY D 1 363 ? 1.378   49.077  9.104   1.00 47.96  ? 392 GLY D N   1 
ATOM   13129 C CA  . GLY D 1 363 ? 2.320   47.989  8.806   1.00 50.53  ? 392 GLY D CA  1 
ATOM   13130 C C   . GLY D 1 363 ? 3.175   48.492  7.687   1.00 55.84  ? 392 GLY D C   1 
ATOM   13131 O O   . GLY D 1 363 ? 3.960   49.500  8.101   1.00 57.67  ? 392 GLY D O   1 
ATOM   13132 N N   . LYS D 1 364 ? 2.936   47.901  6.489   1.00 53.55  ? 393 LYS D N   1 
ATOM   13133 C CA  . LYS D 1 364 ? 3.572   48.235  5.192   1.00 54.42  ? 393 LYS D CA  1 
ATOM   13134 C C   . LYS D 1 364 ? 5.083   48.247  5.298   1.00 56.57  ? 393 LYS D C   1 
ATOM   13135 O O   . LYS D 1 364 ? 5.746   47.291  4.840   1.00 57.36  ? 393 LYS D O   1 
ATOM   13136 C CB  . LYS D 1 364 ? 3.036   49.588  4.711   1.00 54.56  ? 393 LYS D CB  1 
ATOM   13137 C CG  . LYS D 1 364 ? 1.580   49.532  4.279   1.00 51.41  ? 393 LYS D CG  1 
ATOM   13138 C CD  . LYS D 1 364 ? 1.346   50.042  2.863   1.00 52.07  ? 393 LYS D CD  1 
ATOM   13139 C CE  . LYS D 1 364 ? -0.102  50.023  2.494   1.00 52.24  ? 393 LYS D CE  1 
ATOM   13140 N NZ  . LYS D 1 364 ? -0.501  51.254  1.807   1.00 52.10  ? 393 LYS D NZ  1 
ATOM   13141 N N   . ALA D 1 365 ? 5.577   49.303  5.891   1.00 59.45  ? 394 ALA D N   1 
ATOM   13142 C CA  . ALA D 1 365 ? 7.039   49.521  5.995   1.00 62.32  ? 394 ALA D CA  1 
ATOM   13143 C C   . ALA D 1 365 ? 7.673   48.665  7.094   1.00 61.22  ? 394 ALA D C   1 
ATOM   13144 O O   . ALA D 1 365 ? 7.158   48.681  8.224   1.00 56.75  ? 394 ALA D O   1 
ATOM   13145 C CB  . ALA D 1 365 ? 7.278   50.973  6.231   1.00 64.92  ? 394 ALA D CB  1 
ATOM   13146 N N   . LYS D 1 366 ? 8.790   47.993  6.786   1.00 64.12  ? 395 LYS D N   1 
ATOM   13147 C CA  . LYS D 1 366 ? 9.492   47.197  7.828   1.00 63.82  ? 395 LYS D CA  1 
ATOM   13148 C C   . LYS D 1 366 ? 10.162  48.133  8.854   1.00 55.77  ? 395 LYS D C   1 
ATOM   13149 O O   . LYS D 1 366 ? 10.458  47.661  9.971   1.00 52.06  ? 395 LYS D O   1 
ATOM   13150 C CB  . LYS D 1 366 ? 10.565  46.267  7.246   1.00 65.56  ? 395 LYS D CB  1 
ATOM   13151 N N   . ASN D 1 367 ? 10.388  49.400  8.496   1.00 47.74  ? 396 ASN D N   1 
ATOM   13152 C CA  . ASN D 1 367 ? 11.095  50.360  9.388   1.00 39.71  ? 396 ASN D CA  1 
ATOM   13153 C C   . ASN D 1 367 ? 10.260  51.644  9.494   1.00 34.81  ? 396 ASN D C   1 
ATOM   13154 O O   . ASN D 1 367 ? 10.123  52.295  8.460   1.00 31.11  ? 396 ASN D O   1 
ATOM   13155 C CB  . ASN D 1 367 ? 12.506  50.556  8.860   1.00 39.77  ? 396 ASN D CB  1 
ATOM   13156 C CG  . ASN D 1 367 ? 13.273  51.622  9.598   1.00 42.75  ? 396 ASN D CG  1 
ATOM   13157 O OD1 . ASN D 1 367 ? 13.369  51.566  10.821  1.00 37.88  ? 396 ASN D OD1 1 
ATOM   13158 N ND2 . ASN D 1 367 ? 13.844  52.576  8.881   1.00 44.48  ? 396 ASN D ND2 1 
ATOM   13159 N N   . PRO D 1 368 ? 9.652   51.979  10.666  1.00 29.52  ? 397 PRO D N   1 
ATOM   13160 C CA  . PRO D 1 368 ? 8.794   53.140  10.846  1.00 27.09  ? 397 PRO D CA  1 
ATOM   13161 C C   . PRO D 1 368 ? 9.647   54.279  11.355  1.00 26.51  ? 397 PRO D C   1 
ATOM   13162 O O   . PRO D 1 368 ? 9.097   55.351  11.668  1.00 25.23  ? 397 PRO D O   1 
ATOM   13163 C CB  . PRO D 1 368 ? 7.841   52.611  11.910  1.00 28.35  ? 397 PRO D CB  1 
ATOM   13164 C CG  . PRO D 1 368 ? 8.748   51.794  12.798  1.00 29.82  ? 397 PRO D CG  1 
ATOM   13165 C CD  . PRO D 1 368 ? 9.631   51.063  11.799  1.00 29.03  ? 397 PRO D CD  1 
ATOM   13166 N N   . TRP D 1 369 ? 10.963  54.068  11.418  1.00 23.68  ? 398 TRP D N   1 
ATOM   13167 C CA  . TRP D 1 369 ? 11.879  55.083  11.992  1.00 23.43  ? 398 TRP D CA  1 
ATOM   13168 C C   . TRP D 1 369 ? 12.343  56.066  10.922  1.00 23.83  ? 398 TRP D C   1 
ATOM   13169 O O   . TRP D 1 369 ? 12.373  55.706  9.724   1.00 23.63  ? 398 TRP D O   1 
ATOM   13170 C CB  . TRP D 1 369 ? 13.056  54.360  12.658  1.00 25.67  ? 398 TRP D CB  1 
ATOM   13171 C CG  . TRP D 1 369 ? 12.577  53.296  13.606  1.00 24.29  ? 398 TRP D CG  1 
ATOM   13172 C CD1 . TRP D 1 369 ? 12.720  51.946  13.488  1.00 25.54  ? 398 TRP D CD1 1 
ATOM   13173 C CD2 . TRP D 1 369 ? 11.811  53.518  14.808  1.00 24.84  ? 398 TRP D CD2 1 
ATOM   13174 N NE1 . TRP D 1 369 ? 12.117  51.312  14.541  1.00 24.90  ? 398 TRP D NE1 1 
ATOM   13175 C CE2 . TRP D 1 369 ? 11.548  52.248  15.365  1.00 25.23  ? 398 TRP D CE2 1 
ATOM   13176 C CE3 . TRP D 1 369 ? 11.334  54.656  15.466  1.00 27.60  ? 398 TRP D CE3 1 
ATOM   13177 C CZ2 . TRP D 1 369 ? 10.827  52.094  16.545  1.00 25.08  ? 398 TRP D CZ2 1 
ATOM   13178 C CZ3 . TRP D 1 369 ? 10.622  54.500  16.634  1.00 27.27  ? 398 TRP D CZ3 1 
ATOM   13179 C CH2 . TRP D 1 369 ? 10.363  53.235  17.156  1.00 27.54  ? 398 TRP D CH2 1 
ATOM   13180 N N   . PRO D 1 370 ? 12.695  57.310  11.310  1.00 25.06  ? 399 PRO D N   1 
ATOM   13181 C CA  . PRO D 1 370 ? 13.124  58.320  10.352  1.00 25.56  ? 399 PRO D CA  1 
ATOM   13182 C C   . PRO D 1 370 ? 14.494  58.043  9.740   1.00 23.74  ? 399 PRO D C   1 
ATOM   13183 O O   . PRO D 1 370 ? 15.312  57.325  10.312  1.00 25.10  ? 399 PRO D O   1 
ATOM   13184 C CB  . PRO D 1 370 ? 13.086  59.599  11.179  1.00 25.22  ? 399 PRO D CB  1 
ATOM   13185 C CG  . PRO D 1 370 ? 13.363  59.145  12.584  1.00 25.06  ? 399 PRO D CG  1 
ATOM   13186 C CD  . PRO D 1 370 ? 12.661  57.808  12.697  1.00 26.03  ? 399 PRO D CD  1 
ATOM   13187 N N   . ASN D 1 371 ? 14.682  58.584  8.534   1.00 21.83  ? 400 ASN D N   1 
ATOM   13188 C CA  . ASN D 1 371 ? 15.973  58.638  7.858   1.00 22.25  ? 400 ASN D CA  1 
ATOM   13189 C C   . ASN D 1 371 ? 16.455  60.081  7.895   1.00 22.05  ? 400 ASN D C   1 
ATOM   13190 O O   . ASN D 1 371 ? 15.748  60.954  8.391   1.00 21.34  ? 400 ASN D O   1 
ATOM   13191 C CB  . ASN D 1 371 ? 15.911  58.085  6.430   1.00 24.18  ? 400 ASN D CB  1 
ATOM   13192 C CG  . ASN D 1 371 ? 14.911  58.813  5.546   1.00 26.10  ? 400 ASN D CG  1 
ATOM   13193 O OD1 . ASN D 1 371 ? 15.096  59.990  5.233   1.00 23.61  ? 400 ASN D OD1 1 
ATOM   13194 N ND2 . ASN D 1 371 ? 13.839  58.125  5.169   1.00 23.68  ? 400 ASN D ND2 1 
ATOM   13195 N N   . VAL D 1 372 ? 17.648  60.299  7.342   1.00 21.91  ? 401 VAL D N   1 
ATOM   13196 C CA  . VAL D 1 372 ? 18.345  61.572  7.366   1.00 23.58  ? 401 VAL D CA  1 
ATOM   13197 C C   . VAL D 1 372 ? 17.467  62.684  6.791   1.00 26.21  ? 401 VAL D C   1 
ATOM   13198 O O   . VAL D 1 372 ? 17.596  63.852  7.184   1.00 24.22  ? 401 VAL D O   1 
ATOM   13199 C CB  . VAL D 1 372 ? 19.668  61.441  6.590   1.00 26.34  ? 401 VAL D CB  1 
ATOM   13200 C CG1 . VAL D 1 372 ? 19.423  61.236  5.106   1.00 26.46  ? 401 VAL D CG1 1 
ATOM   13201 C CG2 . VAL D 1 372 ? 20.593  62.633  6.829   1.00 26.75  ? 401 VAL D CG2 1 
ATOM   13202 N N   . ASP D 1 373 ? 16.600  62.327  5.830   1.00 24.81  ? 402 ASP D N   1 
ATOM   13203 C CA  . ASP D 1 373 ? 15.840  63.322  5.084   1.00 24.92  ? 402 ASP D CA  1 
ATOM   13204 C C   . ASP D 1 373 ? 14.718  63.920  5.935   1.00 23.19  ? 402 ASP D C   1 
ATOM   13205 O O   . ASP D 1 373 ? 14.218  64.988  5.597   1.00 23.21  ? 402 ASP D O   1 
ATOM   13206 C CB  . ASP D 1 373 ? 15.346  62.732  3.756   1.00 25.93  ? 402 ASP D CB  1 
ATOM   13207 C CG  . ASP D 1 373 ? 16.501  62.465  2.808   1.00 26.53  ? 402 ASP D CG  1 
ATOM   13208 O OD1 . ASP D 1 373 ? 17.426  63.288  2.795   1.00 26.10  ? 402 ASP D OD1 1 
ATOM   13209 O OD2 . ASP D 1 373 ? 16.464  61.462  2.089   1.00 29.21  ? 402 ASP D OD2 1 
ATOM   13210 N N   . ALA D 1 374 ? 14.311  63.248  7.022   1.00 24.82  ? 403 ALA D N   1 
ATOM   13211 C CA  . ALA D 1 374 ? 13.306  63.761  7.956   1.00 23.62  ? 403 ALA D CA  1 
ATOM   13212 C C   . ALA D 1 374 ? 13.739  65.051  8.660   1.00 22.23  ? 403 ALA D C   1 
ATOM   13213 O O   . ALA D 1 374 ? 12.888  65.821  9.073   1.00 19.49  ? 403 ALA D O   1 
ATOM   13214 C CB  . ALA D 1 374 ? 12.969  62.698  8.974   1.00 22.64  ? 403 ALA D CB  1 
ATOM   13215 N N   . HIS D 1 375 ? 15.044  65.309  8.805   1.00 25.17  ? 404 HIS D N   1 
ATOM   13216 C CA  . HIS D 1 375 ? 15.487  66.344  9.737   1.00 25.66  ? 404 HIS D CA  1 
ATOM   13217 C C   . HIS D 1 375 ? 16.312  67.425  9.049   1.00 27.55  ? 404 HIS D C   1 
ATOM   13218 O O   . HIS D 1 375 ? 16.506  68.491  9.631   1.00 26.08  ? 404 HIS D O   1 
ATOM   13219 C CB  . HIS D 1 375 ? 16.256  65.725  10.904  1.00 28.29  ? 404 HIS D CB  1 
ATOM   13220 C CG  . HIS D 1 375 ? 16.180  66.500  12.180  1.00 26.16  ? 404 HIS D CG  1 
ATOM   13221 N ND1 . HIS D 1 375 ? 15.826  65.906  13.372  1.00 27.11  ? 404 HIS D ND1 1 
ATOM   13222 C CD2 . HIS D 1 375 ? 16.365  67.800  12.462  1.00 26.90  ? 404 HIS D CD2 1 
ATOM   13223 C CE1 . HIS D 1 375 ? 15.803  66.808  14.334  1.00 25.98  ? 404 HIS D CE1 1 
ATOM   13224 N NE2 . HIS D 1 375 ? 16.168  67.957  13.821  1.00 28.08  ? 404 HIS D NE2 1 
ATOM   13225 N N   . SER D 1 376 ? 16.762  67.182  7.804   1.00 25.14  ? 405 SER D N   1 
ATOM   13226 C CA  . SER D 1 376 ? 17.797  68.022  7.233   1.00 25.62  ? 405 SER D CA  1 
ATOM   13227 C C   . SER D 1 376 ? 17.240  69.403  6.921   1.00 27.94  ? 405 SER D C   1 
ATOM   13228 O O   . SER D 1 376 ? 17.891  70.413  7.169   1.00 31.41  ? 405 SER D O   1 
ATOM   13229 C CB  . SER D 1 376 ? 18.433  67.353  6.002   1.00 25.08  ? 405 SER D CB  1 
ATOM   13230 O OG  . SER D 1 376 ? 17.480  67.124  4.976   1.00 25.35  ? 405 SER D OG  1 
ATOM   13231 N N   . GLY D 1 377 ? 16.012  69.438  6.404   1.00 31.07  ? 406 GLY D N   1 
ATOM   13232 C CA  . GLY D 1 377 ? 15.454  70.659  5.867   1.00 30.06  ? 406 GLY D CA  1 
ATOM   13233 C C   . GLY D 1 377 ? 15.121  71.680  6.950   1.00 27.21  ? 406 GLY D C   1 
ATOM   13234 O O   . GLY D 1 377 ? 15.340  72.869  6.732   1.00 25.95  ? 406 GLY D O   1 
ATOM   13235 N N   . VAL D 1 378 ? 14.588  71.229  8.097   1.00 28.87  ? 407 VAL D N   1 
ATOM   13236 C CA  . VAL D 1 378 ? 14.235  72.155  9.172   1.00 30.92  ? 407 VAL D CA  1 
ATOM   13237 C C   . VAL D 1 378 ? 15.482  72.843  9.723   1.00 29.89  ? 407 VAL D C   1 
ATOM   13238 O O   . VAL D 1 378 ? 15.352  73.930  10.282  1.00 28.84  ? 407 VAL D O   1 
ATOM   13239 C CB  . VAL D 1 378 ? 13.437  71.528  10.335  1.00 33.90  ? 407 VAL D CB  1 
ATOM   13240 C CG1 . VAL D 1 378 ? 11.953  71.407  10.015  1.00 37.82  ? 407 VAL D CG1 1 
ATOM   13241 C CG2 . VAL D 1 378 ? 14.009  70.197  10.793  1.00 36.88  ? 407 VAL D CG2 1 
ATOM   13242 N N   . LEU D 1 379 ? 16.665  72.212  9.623   1.00 25.24  ? 408 LEU D N   1 
ATOM   13243 C CA  . LEU D 1 379 ? 17.884  72.923  9.983   1.00 27.83  ? 408 LEU D CA  1 
ATOM   13244 C C   . LEU D 1 379 ? 18.136  74.040  8.967   1.00 24.17  ? 408 LEU D C   1 
ATOM   13245 O O   . LEU D 1 379 ? 18.425  75.183  9.324   1.00 23.96  ? 408 LEU D O   1 
ATOM   13246 C CB  . LEU D 1 379 ? 19.069  71.956  10.082  1.00 28.65  ? 408 LEU D CB  1 
ATOM   13247 C CG  . LEU D 1 379 ? 18.913  70.844  11.119  1.00 33.65  ? 408 LEU D CG  1 
ATOM   13248 C CD1 . LEU D 1 379 ? 20.142  69.947  11.167  1.00 31.98  ? 408 LEU D CD1 1 
ATOM   13249 C CD2 . LEU D 1 379 ? 18.636  71.444  12.493  1.00 35.08  ? 408 LEU D CD2 1 
ATOM   13250 N N   . LEU D 1 380 ? 18.096  73.717  7.681   1.00 23.23  ? 409 LEU D N   1 
ATOM   13251 C CA  . LEU D 1 380 ? 18.380  74.744  6.696   1.00 23.18  ? 409 LEU D CA  1 
ATOM   13252 C C   . LEU D 1 380 ? 17.439  75.944  6.848   1.00 24.27  ? 409 LEU D C   1 
ATOM   13253 O O   . LEU D 1 380 ? 17.910  77.082  6.836   1.00 24.50  ? 409 LEU D O   1 
ATOM   13254 C CB  . LEU D 1 380 ? 18.259  74.139  5.302   1.00 21.76  ? 409 LEU D CB  1 
ATOM   13255 C CG  . LEU D 1 380 ? 19.251  73.034  4.923   1.00 20.47  ? 409 LEU D CG  1 
ATOM   13256 C CD1 . LEU D 1 380 ? 18.937  72.551  3.516   1.00 20.07  ? 409 LEU D CD1 1 
ATOM   13257 C CD2 . LEU D 1 380 ? 20.688  73.516  4.984   1.00 22.43  ? 409 LEU D CD2 1 
ATOM   13258 N N   . GLN D 1 381 ? 16.125  75.683  6.935   1.00 25.35  ? 410 GLN D N   1 
ATOM   13259 C CA  . GLN D 1 381 ? 15.097  76.720  7.048   1.00 30.87  ? 410 GLN D CA  1 
ATOM   13260 C C   . GLN D 1 381 ? 15.440  77.761  8.125   1.00 28.30  ? 410 GLN D C   1 
ATOM   13261 O O   . GLN D 1 381 ? 15.202  78.965  7.954   1.00 27.51  ? 410 GLN D O   1 
ATOM   13262 C CB  . GLN D 1 381 ? 13.755  76.064  7.402   1.00 36.76  ? 410 GLN D CB  1 
ATOM   13263 C CG  . GLN D 1 381 ? 12.529  76.926  7.114   1.00 42.14  ? 410 GLN D CG  1 
ATOM   13264 C CD  . GLN D 1 381 ? 11.764  76.511  5.872   1.00 43.57  ? 410 GLN D CD  1 
ATOM   13265 O OE1 . GLN D 1 381 ? 10.530  76.533  5.845   1.00 35.79  ? 410 GLN D OE1 1 
ATOM   13266 N NE2 . GLN D 1 381 ? 12.490  76.125  4.828   1.00 43.16  ? 410 GLN D NE2 1 
ATOM   13267 N N   . TYR D 1 382 ? 15.992  77.279  9.238   1.00 29.73  ? 411 TYR D N   1 
ATOM   13268 C CA  . TYR D 1 382 ? 16.306  78.087  10.411  1.00 27.51  ? 411 TYR D CA  1 
ATOM   13269 C C   . TYR D 1 382 ? 17.316  79.189  10.096  1.00 27.31  ? 411 TYR D C   1 
ATOM   13270 O O   . TYR D 1 382 ? 17.232  80.283  10.641  1.00 25.63  ? 411 TYR D O   1 
ATOM   13271 C CB  . TYR D 1 382 ? 16.904  77.221  11.517  1.00 27.33  ? 411 TYR D CB  1 
ATOM   13272 C CG  . TYR D 1 382 ? 17.278  78.024  12.738  1.00 26.04  ? 411 TYR D CG  1 
ATOM   13273 C CD1 . TYR D 1 382 ? 16.292  78.524  13.572  1.00 26.60  ? 411 TYR D CD1 1 
ATOM   13274 C CD2 . TYR D 1 382 ? 18.603  78.363  13.007  1.00 24.98  ? 411 TYR D CD2 1 
ATOM   13275 C CE1 . TYR D 1 382 ? 16.611  79.278  14.686  1.00 28.86  ? 411 TYR D CE1 1 
ATOM   13276 C CE2 . TYR D 1 382 ? 18.938  79.095  14.129  1.00 26.30  ? 411 TYR D CE2 1 
ATOM   13277 C CZ  . TYR D 1 382 ? 17.933  79.545  14.974  1.00 27.87  ? 411 TYR D CZ  1 
ATOM   13278 O OH  . TYR D 1 382 ? 18.190  80.302  16.081  1.00 33.87  ? 411 TYR D OH  1 
ATOM   13279 N N   . TYR D 1 383 ? 18.277  78.907  9.216   1.00 26.57  ? 412 TYR D N   1 
ATOM   13280 C CA  . TYR D 1 383 ? 19.348  79.853  8.945   1.00 27.26  ? 412 TYR D CA  1 
ATOM   13281 C C   . TYR D 1 383 ? 18.988  80.697  7.726   1.00 27.52  ? 412 TYR D C   1 
ATOM   13282 O O   . TYR D 1 383 ? 19.815  81.462  7.246   1.00 28.76  ? 412 TYR D O   1 
ATOM   13283 C CB  . TYR D 1 383 ? 20.679  79.116  8.788   1.00 27.18  ? 412 TYR D CB  1 
ATOM   13284 C CG  . TYR D 1 383 ? 21.213  78.532  10.064  1.00 26.15  ? 412 TYR D CG  1 
ATOM   13285 C CD1 . TYR D 1 383 ? 21.740  79.347  11.047  1.00 27.64  ? 412 TYR D CD1 1 
ATOM   13286 C CD2 . TYR D 1 383 ? 21.115  77.171  10.324  1.00 23.64  ? 412 TYR D CD2 1 
ATOM   13287 C CE1 . TYR D 1 383 ? 22.195  78.828  12.249  1.00 28.00  ? 412 TYR D CE1 1 
ATOM   13288 C CE2 . TYR D 1 383 ? 21.579  76.633  11.511  1.00 26.32  ? 412 TYR D CE2 1 
ATOM   13289 C CZ  . TYR D 1 383 ? 22.114  77.468  12.479  1.00 28.68  ? 412 TYR D CZ  1 
ATOM   13290 O OH  . TYR D 1 383 ? 22.547  76.981  13.671  1.00 29.38  ? 412 TYR D OH  1 
ATOM   13291 N N   . GLY D 1 384 ? 17.766  80.513  7.200   1.00 27.91  ? 413 GLY D N   1 
ATOM   13292 C CA  . GLY D 1 384 ? 17.235  81.398  6.182   1.00 28.01  ? 413 GLY D CA  1 
ATOM   13293 C C   . GLY D 1 384 ? 17.154  80.755  4.797   1.00 27.97  ? 413 GLY D C   1 
ATOM   13294 O O   . GLY D 1 384 ? 16.555  81.356  3.904   1.00 25.91  ? 413 GLY D O   1 
ATOM   13295 N N   . MET D 1 385 ? 17.709  79.533  4.632   1.00 25.26  ? 414 MET D N   1 
ATOM   13296 C CA  . MET D 1 385 ? 17.606  78.788  3.379   1.00 23.71  ? 414 MET D CA  1 
ATOM   13297 C C   . MET D 1 385 ? 16.249  78.084  3.316   1.00 23.27  ? 414 MET D C   1 
ATOM   13298 O O   . MET D 1 385 ? 16.121  76.900  3.635   1.00 22.69  ? 414 MET D O   1 
ATOM   13299 C CB  . MET D 1 385 ? 18.704  77.738  3.218   1.00 25.43  ? 414 MET D CB  1 
ATOM   13300 C CG  . MET D 1 385 ? 18.538  76.973  1.906   1.00 26.75  ? 414 MET D CG  1 
ATOM   13301 S SD  . MET D 1 385 ? 19.976  76.054  1.411   1.00 26.35  ? 414 MET D SD  1 
ATOM   13302 C CE  . MET D 1 385 ? 21.122  77.390  1.074   1.00 22.95  ? 414 MET D CE  1 
ATOM   13303 N N   . THR D 1 386 ? 15.238  78.855  2.913   1.00 21.33  ? 415 THR D N   1 
ATOM   13304 C CA  . THR D 1 386 ? 13.840  78.484  2.892   1.00 23.56  ? 415 THR D CA  1 
ATOM   13305 C C   . THR D 1 386 ? 13.439  77.842  1.565   1.00 25.08  ? 415 THR D C   1 
ATOM   13306 O O   . THR D 1 386 ? 12.306  77.412  1.399   1.00 25.37  ? 415 THR D O   1 
ATOM   13307 C CB  . THR D 1 386 ? 13.009  79.752  3.108   1.00 28.06  ? 415 THR D CB  1 
ATOM   13308 O OG1 . THR D 1 386 ? 13.406  80.671  2.089   1.00 33.86  ? 415 THR D OG1 1 
ATOM   13309 C CG2 . THR D 1 386 ? 13.232  80.347  4.482   1.00 30.64  ? 415 THR D CG2 1 
ATOM   13310 N N   . GLU D 1 387 ? 14.375  77.806  0.614   1.00 25.91  ? 416 GLU D N   1 
ATOM   13311 C CA  . GLU D 1 387 ? 14.093  77.348  -0.730  1.00 24.79  ? 416 GLU D CA  1 
ATOM   13312 C C   . GLU D 1 387 ? 14.172  75.822  -0.784  1.00 23.45  ? 416 GLU D C   1 
ATOM   13313 O O   . GLU D 1 387 ? 15.211  75.276  -1.140  1.00 21.47  ? 416 GLU D O   1 
ATOM   13314 C CB  . GLU D 1 387 ? 15.069  77.996  -1.709  1.00 26.96  ? 416 GLU D CB  1 
ATOM   13315 C CG  . GLU D 1 387 ? 15.001  79.515  -1.712  1.00 29.40  ? 416 GLU D CG  1 
ATOM   13316 C CD  . GLU D 1 387 ? 15.908  80.226  -0.718  1.00 29.45  ? 416 GLU D CD  1 
ATOM   13317 O OE1 . GLU D 1 387 ? 16.513  79.544  0.127   1.00 25.38  ? 416 GLU D OE1 1 
ATOM   13318 O OE2 . GLU D 1 387 ? 16.025  81.472  -0.815  1.00 28.35  ? 416 GLU D OE2 1 
ATOM   13319 N N   . MET D 1 388 ? 13.045  75.160  -0.495  1.00 23.33  ? 417 MET D N   1 
ATOM   13320 C CA  . MET D 1 388 ? 13.029  73.719  -0.274  1.00 25.10  ? 417 MET D CA  1 
ATOM   13321 C C   . MET D 1 388 ? 13.353  72.952  -1.549  1.00 24.13  ? 417 MET D C   1 
ATOM   13322 O O   . MET D 1 388 ? 13.880  71.837  -1.464  1.00 23.03  ? 417 MET D O   1 
ATOM   13323 C CB  . MET D 1 388 ? 11.665  73.238  0.230   1.00 30.00  ? 417 MET D CB  1 
ATOM   13324 C CG  . MET D 1 388 ? 11.483  73.496  1.701   1.00 37.88  ? 417 MET D CG  1 
ATOM   13325 S SD  . MET D 1 388 ? 9.752   73.568  2.225   1.00 55.76  ? 417 MET D SD  1 
ATOM   13326 C CE  . MET D 1 388 ? 9.040   74.819  1.161   1.00 51.74  ? 417 MET D CE  1 
ATOM   13327 N N   . ASN D 1 389 ? 13.079  73.549  -2.719  1.00 22.78  ? 418 ASN D N   1 
ATOM   13328 C CA  . ASN D 1 389 ? 13.372  72.879  -3.969  1.00 24.57  ? 418 ASN D CA  1 
ATOM   13329 C C   . ASN D 1 389 ? 14.872  72.841  -4.248  1.00 23.82  ? 418 ASN D C   1 
ATOM   13330 O O   . ASN D 1 389 ? 15.254  72.183  -5.191  1.00 23.86  ? 418 ASN D O   1 
ATOM   13331 C CB  . ASN D 1 389 ? 12.581  73.437  -5.154  1.00 26.45  ? 418 ASN D CB  1 
ATOM   13332 C CG  . ASN D 1 389 ? 11.167  72.888  -5.226  1.00 30.32  ? 418 ASN D CG  1 
ATOM   13333 O OD1 . ASN D 1 389 ? 10.581  72.458  -4.224  1.00 30.59  ? 418 ASN D OD1 1 
ATOM   13334 N ND2 . ASN D 1 389 ? 10.612  72.899  -6.422  1.00 30.22  ? 418 ASN D ND2 1 
ATOM   13335 N N   . TYR D 1 390 ? 15.703  73.497  -3.428  1.00 23.61  ? 419 TYR D N   1 
ATOM   13336 C CA  . TYR D 1 390 ? 17.145  73.486  -3.580  1.00 22.76  ? 419 TYR D CA  1 
ATOM   13337 C C   . TYR D 1 390 ? 17.813  72.398  -2.735  1.00 21.87  ? 419 TYR D C   1 
ATOM   13338 O O   . TYR D 1 390 ? 18.979  72.089  -2.903  1.00 22.28  ? 419 TYR D O   1 
ATOM   13339 C CB  . TYR D 1 390 ? 17.697  74.837  -3.125  1.00 21.85  ? 419 TYR D CB  1 
ATOM   13340 C CG  . TYR D 1 390 ? 19.177  74.993  -3.360  1.00 20.99  ? 419 TYR D CG  1 
ATOM   13341 C CD1 . TYR D 1 390 ? 19.675  75.150  -4.650  1.00 20.08  ? 419 TYR D CD1 1 
ATOM   13342 C CD2 . TYR D 1 390 ? 20.070  74.953  -2.322  1.00 19.59  ? 419 TYR D CD2 1 
ATOM   13343 C CE1 . TYR D 1 390 ? 21.037  75.274  -4.874  1.00 19.20  ? 419 TYR D CE1 1 
ATOM   13344 C CE2 . TYR D 1 390 ? 21.437  75.039  -2.527  1.00 21.42  ? 419 TYR D CE2 1 
ATOM   13345 C CZ  . TYR D 1 390 ? 21.921  75.205  -3.818  1.00 21.15  ? 419 TYR D CZ  1 
ATOM   13346 O OH  . TYR D 1 390 ? 23.290  75.309  -4.035  1.00 20.56  ? 419 TYR D OH  1 
ATOM   13347 N N   . TYR D 1 391 ? 17.071  71.848  -1.782  1.00 23.82  ? 420 TYR D N   1 
ATOM   13348 C CA  . TYR D 1 391 ? 17.636  71.067  -0.695  1.00 22.75  ? 420 TYR D CA  1 
ATOM   13349 C C   . TYR D 1 391 ? 18.369  69.833  -1.219  1.00 20.09  ? 420 TYR D C   1 
ATOM   13350 O O   . TYR D 1 391 ? 19.414  69.494  -0.687  1.00 19.30  ? 420 TYR D O   1 
ATOM   13351 C CB  . TYR D 1 391 ? 16.518  70.675  0.267   1.00 21.83  ? 420 TYR D CB  1 
ATOM   13352 C CG  . TYR D 1 391 ? 15.990  71.805  1.124   1.00 22.14  ? 420 TYR D CG  1 
ATOM   13353 C CD1 . TYR D 1 391 ? 16.438  73.108  0.971   1.00 25.04  ? 420 TYR D CD1 1 
ATOM   13354 C CD2 . TYR D 1 391 ? 15.097  71.543  2.142   1.00 24.62  ? 420 TYR D CD2 1 
ATOM   13355 C CE1 . TYR D 1 391 ? 15.985  74.136  1.787   1.00 26.54  ? 420 TYR D CE1 1 
ATOM   13356 C CE2 . TYR D 1 391 ? 14.634  72.551  2.973   1.00 25.35  ? 420 TYR D CE2 1 
ATOM   13357 C CZ  . TYR D 1 391 ? 15.081  73.853  2.799   1.00 28.96  ? 420 TYR D CZ  1 
ATOM   13358 O OH  . TYR D 1 391 ? 14.618  74.863  3.626   1.00 26.41  ? 420 TYR D OH  1 
ATOM   13359 N N   . THR D 1 392 ? 17.818  69.180  -2.257  1.00 21.67  ? 421 THR D N   1 
ATOM   13360 C CA  . THR D 1 392 ? 18.424  67.955  -2.767  1.00 19.38  ? 421 THR D CA  1 
ATOM   13361 C C   . THR D 1 392 ? 19.753  68.253  -3.457  1.00 19.61  ? 421 THR D C   1 
ATOM   13362 O O   . THR D 1 392 ? 20.593  67.363  -3.587  1.00 21.84  ? 421 THR D O   1 
ATOM   13363 C CB  . THR D 1 392 ? 17.451  67.163  -3.638  1.00 18.82  ? 421 THR D CB  1 
ATOM   13364 O OG1 . THR D 1 392 ? 16.243  67.106  -2.878  1.00 18.60  ? 421 THR D OG1 1 
ATOM   13365 C CG2 . THR D 1 392 ? 17.938  65.761  -3.959  1.00 19.67  ? 421 THR D CG2 1 
ATOM   13366 N N   . VAL D 1 393 ? 19.956  69.495  -3.887  1.00 17.83  ? 422 VAL D N   1 
ATOM   13367 C CA  . VAL D 1 393 ? 21.264  69.914  -4.395  1.00 20.02  ? 422 VAL D CA  1 
ATOM   13368 C C   . VAL D 1 393 ? 22.341  69.806  -3.320  1.00 19.39  ? 422 VAL D C   1 
ATOM   13369 O O   . VAL D 1 393 ? 23.449  69.365  -3.626  1.00 19.53  ? 422 VAL D O   1 
ATOM   13370 C CB  . VAL D 1 393 ? 21.211  71.341  -4.968  1.00 20.08  ? 422 VAL D CB  1 
ATOM   13371 C CG1 . VAL D 1 393 ? 22.577  71.852  -5.417  1.00 20.02  ? 422 VAL D CG1 1 
ATOM   13372 C CG2 . VAL D 1 393 ? 20.240  71.422  -6.115  1.00 21.98  ? 422 VAL D CG2 1 
ATOM   13373 N N   . LEU D 1 394 ? 22.057  70.189  -2.053  1.00 18.25  ? 423 LEU D N   1 
ATOM   13374 C CA  . LEU D 1 394 ? 23.071  70.037  -1.008  1.00 18.90  ? 423 LEU D CA  1 
ATOM   13375 C C   . LEU D 1 394 ? 23.386  68.555  -0.823  1.00 18.11  ? 423 LEU D C   1 
ATOM   13376 O O   . LEU D 1 394 ? 24.538  68.204  -0.684  1.00 18.19  ? 423 LEU D O   1 
ATOM   13377 C CB  . LEU D 1 394 ? 22.624  70.649  0.319   1.00 20.18  ? 423 LEU D CB  1 
ATOM   13378 C CG  . LEU D 1 394 ? 22.351  72.154  0.281   1.00 21.91  ? 423 LEU D CG  1 
ATOM   13379 C CD1 . LEU D 1 394 ? 21.797  72.611  1.611   1.00 24.81  ? 423 LEU D CD1 1 
ATOM   13380 C CD2 . LEU D 1 394 ? 23.591  72.953  -0.028  1.00 22.42  ? 423 LEU D CD2 1 
ATOM   13381 N N   . PHE D 1 395 ? 22.356  67.701  -0.844  1.00 17.50  ? 424 PHE D N   1 
ATOM   13382 C CA  . PHE D 1 395 ? 22.588  66.276  -0.704  1.00 17.06  ? 424 PHE D CA  1 
ATOM   13383 C C   . PHE D 1 395 ? 23.519  65.834  -1.842  1.00 18.76  ? 424 PHE D C   1 
ATOM   13384 O O   . PHE D 1 395 ? 24.509  65.144  -1.605  1.00 20.43  ? 424 PHE D O   1 
ATOM   13385 C CB  . PHE D 1 395 ? 21.232  65.583  -0.608  1.00 16.72  ? 424 PHE D CB  1 
ATOM   13386 C CG  . PHE D 1 395 ? 21.217  64.160  -0.120  1.00 16.67  ? 424 PHE D CG  1 
ATOM   13387 C CD1 . PHE D 1 395 ? 22.377  63.426  0.015   1.00 17.05  ? 424 PHE D CD1 1 
ATOM   13388 C CD2 . PHE D 1 395 ? 20.022  63.566  0.235   1.00 18.35  ? 424 PHE D CD2 1 
ATOM   13389 C CE1 . PHE D 1 395 ? 22.323  62.097  0.408   1.00 17.71  ? 424 PHE D CE1 1 
ATOM   13390 C CE2 . PHE D 1 395 ? 19.974  62.255  0.693   1.00 18.64  ? 424 PHE D CE2 1 
ATOM   13391 C CZ  . PHE D 1 395 ? 21.132  61.522  0.785   1.00 16.43  ? 424 PHE D CZ  1 
ATOM   13392 N N   . GLY D 1 396 ? 23.255  66.308  -3.063  1.00 18.96  ? 425 GLY D N   1 
ATOM   13393 C CA  . GLY D 1 396 ? 24.011  65.932  -4.245  1.00 20.25  ? 425 GLY D CA  1 
ATOM   13394 C C   . GLY D 1 396 ? 25.486  66.271  -4.063  1.00 20.64  ? 425 GLY D C   1 
ATOM   13395 O O   . GLY D 1 396 ? 26.397  65.451  -4.252  1.00 20.96  ? 425 GLY D O   1 
ATOM   13396 N N   . VAL D 1 397 ? 25.727  67.478  -3.574  1.00 19.12  ? 426 VAL D N   1 
ATOM   13397 C CA  . VAL D 1 397 ? 27.100  67.921  -3.393  1.00 19.90  ? 426 VAL D CA  1 
ATOM   13398 C C   . VAL D 1 397 ? 27.857  67.027  -2.408  1.00 19.27  ? 426 VAL D C   1 
ATOM   13399 O O   . VAL D 1 397 ? 29.028  66.723  -2.629  1.00 19.27  ? 426 VAL D O   1 
ATOM   13400 C CB  . VAL D 1 397 ? 27.119  69.413  -3.010  1.00 20.71  ? 426 VAL D CB  1 
ATOM   13401 C CG1 . VAL D 1 397 ? 28.491  69.839  -2.560  1.00 20.96  ? 426 VAL D CG1 1 
ATOM   13402 C CG2 . VAL D 1 397 ? 26.659  70.290  -4.166  1.00 22.38  ? 426 VAL D CG2 1 
ATOM   13403 N N   . SER D 1 398 ? 27.216  66.640  -1.293  1.00 20.19  ? 427 SER D N   1 
ATOM   13404 C CA  . SER D 1 398 ? 27.744  65.712  -0.302  1.00 21.32  ? 427 SER D CA  1 
ATOM   13405 C C   . SER D 1 398 ? 28.061  64.330  -0.885  1.00 18.42  ? 427 SER D C   1 
ATOM   13406 O O   . SER D 1 398 ? 29.135  63.750  -0.628  1.00 17.25  ? 427 SER D O   1 
ATOM   13407 C CB  . SER D 1 398 ? 26.727  65.564  0.783   1.00 19.46  ? 427 SER D CB  1 
ATOM   13408 O OG  . SER D 1 398 ? 27.130  64.638  1.759   1.00 20.45  ? 427 SER D OG  1 
ATOM   13409 N N   . ARG D 1 399 ? 27.075  63.774  -1.595  1.00 18.77  ? 428 ARG D N   1 
ATOM   13410 C CA  . ARG D 1 399 ? 27.142  62.372  -1.996  1.00 17.64  ? 428 ARG D CA  1 
ATOM   13411 C C   . ARG D 1 399 ? 28.224  62.159  -3.059  1.00 19.54  ? 428 ARG D C   1 
ATOM   13412 O O   . ARG D 1 399 ? 28.686  61.039  -3.267  1.00 20.70  ? 428 ARG D O   1 
ATOM   13413 C CB  . ARG D 1 399 ? 25.743  61.965  -2.461  1.00 17.47  ? 428 ARG D CB  1 
ATOM   13414 C CG  . ARG D 1 399 ? 25.567  60.509  -2.869  1.00 16.24  ? 428 ARG D CG  1 
ATOM   13415 C CD  . ARG D 1 399 ? 26.082  59.524  -1.835  1.00 16.03  ? 428 ARG D CD  1 
ATOM   13416 N NE  . ARG D 1 399 ? 25.510  59.639  -0.490  1.00 18.26  ? 428 ARG D NE  1 
ATOM   13417 C CZ  . ARG D 1 399 ? 24.338  59.121  -0.127  1.00 18.67  ? 428 ARG D CZ  1 
ATOM   13418 N NH1 . ARG D 1 399 ? 23.663  58.366  -0.968  1.00 19.52  ? 428 ARG D NH1 1 
ATOM   13419 N NH2 . ARG D 1 399 ? 23.892  59.266  1.111   1.00 19.67  ? 428 ARG D NH2 1 
ATOM   13420 N N   . ALA D 1 400 ? 28.651  63.222  -3.728  1.00 17.44  ? 429 ALA D N   1 
ATOM   13421 C CA  . ALA D 1 400 ? 29.830  63.170  -4.579  1.00 20.87  ? 429 ALA D CA  1 
ATOM   13422 C C   . ALA D 1 400 ? 31.022  62.542  -3.845  1.00 20.27  ? 429 ALA D C   1 
ATOM   13423 O O   . ALA D 1 400 ? 31.795  61.818  -4.468  1.00 18.60  ? 429 ALA D O   1 
ATOM   13424 C CB  . ALA D 1 400 ? 30.178  64.550  -5.056  1.00 20.77  ? 429 ALA D CB  1 
ATOM   13425 N N   . LEU D 1 401 ? 31.210  62.898  -2.560  1.00 21.02  ? 430 LEU D N   1 
ATOM   13426 C CA  . LEU D 1 401 ? 32.375  62.476  -1.788  1.00 21.30  ? 430 LEU D CA  1 
ATOM   13427 C C   . LEU D 1 401 ? 32.378  60.954  -1.684  1.00 20.39  ? 430 LEU D C   1 
ATOM   13428 O O   . LEU D 1 401 ? 33.406  60.327  -1.900  1.00 25.04  ? 430 LEU D O   1 
ATOM   13429 C CB  . LEU D 1 401 ? 32.367  63.119  -0.395  1.00 22.66  ? 430 LEU D CB  1 
ATOM   13430 C CG  . LEU D 1 401 ? 32.358  64.650  -0.406  1.00 24.15  ? 430 LEU D CG  1 
ATOM   13431 C CD1 . LEU D 1 401 ? 32.160  65.197  0.990   1.00 26.03  ? 430 LEU D CD1 1 
ATOM   13432 C CD2 . LEU D 1 401 ? 33.630  65.201  -1.033  1.00 23.51  ? 430 LEU D CD2 1 
ATOM   13433 N N   . GLY D 1 402 ? 31.239  60.363  -1.350  1.00 19.44  ? 431 GLY D N   1 
ATOM   13434 C CA  . GLY D 1 402 ? 31.186  58.918  -1.222  1.00 20.24  ? 431 GLY D CA  1 
ATOM   13435 C C   . GLY D 1 402 ? 31.381  58.217  -2.561  1.00 23.33  ? 431 GLY D C   1 
ATOM   13436 O O   . GLY D 1 402 ? 32.196  57.280  -2.661  1.00 20.38  ? 431 GLY D O   1 
ATOM   13437 N N   . VAL D 1 403 ? 30.631  58.659  -3.578  1.00 19.76  ? 432 VAL D N   1 
ATOM   13438 C CA  . VAL D 1 403 ? 30.500  57.835  -4.770  1.00 20.25  ? 432 VAL D CA  1 
ATOM   13439 C C   . VAL D 1 403 ? 31.778  57.922  -5.598  1.00 20.81  ? 432 VAL D C   1 
ATOM   13440 O O   . VAL D 1 403 ? 32.130  56.967  -6.290  1.00 20.39  ? 432 VAL D O   1 
ATOM   13441 C CB  . VAL D 1 403 ? 29.227  58.139  -5.593  1.00 20.80  ? 432 VAL D CB  1 
ATOM   13442 C CG1 . VAL D 1 403 ? 27.985  58.027  -4.723  1.00 20.38  ? 432 VAL D CG1 1 
ATOM   13443 C CG2 . VAL D 1 403 ? 29.286  59.494  -6.290  1.00 21.09  ? 432 VAL D CG2 1 
ATOM   13444 N N   . LEU D 1 404 ? 32.463  59.069  -5.542  1.00 19.76  ? 433 LEU D N   1 
ATOM   13445 C CA  . LEU D 1 404 ? 33.684  59.230  -6.300  1.00 19.24  ? 433 LEU D CA  1 
ATOM   13446 C C   . LEU D 1 404 ? 34.840  58.566  -5.563  1.00 19.99  ? 433 LEU D C   1 
ATOM   13447 O O   . LEU D 1 404 ? 35.732  58.062  -6.202  1.00 19.00  ? 433 LEU D O   1 
ATOM   13448 C CB  . LEU D 1 404 ? 33.949  60.717  -6.527  1.00 21.16  ? 433 LEU D CB  1 
ATOM   13449 C CG  . LEU D 1 404 ? 32.863  61.426  -7.335  1.00 21.13  ? 433 LEU D CG  1 
ATOM   13450 C CD1 . LEU D 1 404 ? 33.197  62.903  -7.470  1.00 21.32  ? 433 LEU D CD1 1 
ATOM   13451 C CD2 . LEU D 1 404 ? 32.661  60.773  -8.706  1.00 22.85  ? 433 LEU D CD2 1 
ATOM   13452 N N   . ALA D 1 405 ? 34.812  58.552  -4.220  1.00 20.10  ? 434 ALA D N   1 
ATOM   13453 C CA  . ALA D 1 405 ? 35.821  57.839  -3.449  1.00 18.54  ? 434 ALA D CA  1 
ATOM   13454 C C   . ALA D 1 405 ? 35.798  56.358  -3.836  1.00 19.98  ? 434 ALA D C   1 
ATOM   13455 O O   . ALA D 1 405 ? 36.855  55.791  -4.114  1.00 19.53  ? 434 ALA D O   1 
ATOM   13456 C CB  . ALA D 1 405 ? 35.579  58.044  -1.978  1.00 18.14  ? 434 ALA D CB  1 
ATOM   13457 N N   . GLN D 1 406 ? 34.596  55.785  -4.008  1.00 17.89  ? 435 GLN D N   1 
ATOM   13458 C CA  . GLN D 1 406 ? 34.474  54.392  -4.418  1.00 18.65  ? 435 GLN D CA  1 
ATOM   13459 C C   . GLN D 1 406 ? 34.803  54.199  -5.906  1.00 20.33  ? 435 GLN D C   1 
ATOM   13460 O O   . GLN D 1 406 ? 35.286  53.141  -6.308  1.00 21.82  ? 435 GLN D O   1 
ATOM   13461 C CB  . GLN D 1 406 ? 33.059  53.867  -4.156  1.00 19.88  ? 435 GLN D CB  1 
ATOM   13462 C CG  . GLN D 1 406 ? 32.823  52.458  -4.692  1.00 20.51  ? 435 GLN D CG  1 
ATOM   13463 C CD  . GLN D 1 406 ? 33.812  51.465  -4.131  1.00 21.61  ? 435 GLN D CD  1 
ATOM   13464 O OE1 . GLN D 1 406 ? 34.038  51.423  -2.923  1.00 21.85  ? 435 GLN D OE1 1 
ATOM   13465 N NE2 . GLN D 1 406 ? 34.351  50.607  -4.993  1.00 20.83  ? 435 GLN D NE2 1 
ATOM   13466 N N   . LEU D 1 407 ? 34.396  55.142  -6.746  1.00 19.47  ? 436 LEU D N   1 
ATOM   13467 C CA  . LEU D 1 407 ? 34.632  55.025  -8.177  1.00 19.40  ? 436 LEU D CA  1 
ATOM   13468 C C   . LEU D 1 407 ? 36.130  54.900  -8.452  1.00 19.22  ? 436 LEU D C   1 
ATOM   13469 O O   . LEU D 1 407 ? 36.531  54.158  -9.338  1.00 21.13  ? 436 LEU D O   1 
ATOM   13470 C CB  . LEU D 1 407 ? 34.079  56.259  -8.906  1.00 18.17  ? 436 LEU D CB  1 
ATOM   13471 C CG  . LEU D 1 407 ? 34.027  56.129  -10.427 1.00 19.34  ? 436 LEU D CG  1 
ATOM   13472 C CD1 . LEU D 1 407 ? 33.184  54.936  -10.831 1.00 18.68  ? 436 LEU D CD1 1 
ATOM   13473 C CD2 . LEU D 1 407 ? 33.478  57.385  -11.083 1.00 20.02  ? 436 LEU D CD2 1 
ATOM   13474 N N   . ILE D 1 408 ? 36.947  55.676  -7.739  1.00 19.57  ? 437 ILE D N   1 
ATOM   13475 C CA  . ILE D 1 408 ? 38.398  55.511  -7.802  1.00 18.94  ? 437 ILE D CA  1 
ATOM   13476 C C   . ILE D 1 408 ? 38.747  54.041  -7.557  1.00 19.98  ? 437 ILE D C   1 
ATOM   13477 O O   . ILE D 1 408 ? 39.488  53.446  -8.336  1.00 21.60  ? 437 ILE D O   1 
ATOM   13478 C CB  . ILE D 1 408 ? 39.118  56.426  -6.794  1.00 21.17  ? 437 ILE D CB  1 
ATOM   13479 C CG1 . ILE D 1 408 ? 38.815  57.903  -7.051  1.00 21.76  ? 437 ILE D CG1 1 
ATOM   13480 C CG2 . ILE D 1 408 ? 40.621  56.164  -6.767  1.00 20.92  ? 437 ILE D CG2 1 
ATOM   13481 C CD1 . ILE D 1 408 ? 39.073  58.777  -5.846  1.00 22.45  ? 437 ILE D CD1 1 
ATOM   13482 N N   . TRP D 1 409 ? 38.226  53.494  -6.457  1.00 19.66  ? 438 TRP D N   1 
ATOM   13483 C CA  . TRP D 1 409 ? 38.566  52.150  -6.038  1.00 20.20  ? 438 TRP D CA  1 
ATOM   13484 C C   . TRP D 1 409 ? 37.990  51.111  -7.001  1.00 20.09  ? 438 TRP D C   1 
ATOM   13485 O O   . TRP D 1 409 ? 38.619  50.101  -7.271  1.00 18.36  ? 438 TRP D O   1 
ATOM   13486 C CB  . TRP D 1 409 ? 38.132  51.913  -4.588  1.00 19.91  ? 438 TRP D CB  1 
ATOM   13487 C CG  . TRP D 1 409 ? 39.144  52.433  -3.619  1.00 19.51  ? 438 TRP D CG  1 
ATOM   13488 C CD1 . TRP D 1 409 ? 39.135  53.645  -2.978  1.00 20.35  ? 438 TRP D CD1 1 
ATOM   13489 C CD2 . TRP D 1 409 ? 40.395  51.808  -3.254  1.00 19.43  ? 438 TRP D CD2 1 
ATOM   13490 N NE1 . TRP D 1 409 ? 40.263  53.782  -2.199  1.00 18.56  ? 438 TRP D NE1 1 
ATOM   13491 C CE2 . TRP D 1 409 ? 41.043  52.664  -2.338  1.00 20.94  ? 438 TRP D CE2 1 
ATOM   13492 C CE3 . TRP D 1 409 ? 41.002  50.586  -3.562  1.00 20.09  ? 438 TRP D CE3 1 
ATOM   13493 C CZ2 . TRP D 1 409 ? 42.280  52.355  -1.771  1.00 21.89  ? 438 TRP D CZ2 1 
ATOM   13494 C CZ3 . TRP D 1 409 ? 42.243  50.291  -3.027  1.00 20.75  ? 438 TRP D CZ3 1 
ATOM   13495 C CH2 . TRP D 1 409 ? 42.857  51.155  -2.124  1.00 20.93  ? 438 TRP D CH2 1 
ATOM   13496 N N   . SER D 1 410 ? 36.757  51.292  -7.479  1.00 18.84  ? 439 SER D N   1 
ATOM   13497 C CA  . SER D 1 410 ? 36.216  50.332  -8.445  1.00 17.61  ? 439 SER D CA  1 
ATOM   13498 C C   . SER D 1 410 ? 37.153  50.182  -9.642  1.00 17.84  ? 439 SER D C   1 
ATOM   13499 O O   . SER D 1 410 ? 37.340  49.099  -10.172 1.00 20.93  ? 439 SER D O   1 
ATOM   13500 C CB  . SER D 1 410 ? 34.838  50.714  -8.914  1.00 17.27  ? 439 SER D CB  1 
ATOM   13501 O OG  . SER D 1 410 ? 34.035  51.006  -7.804  1.00 19.93  ? 439 SER D OG  1 
ATOM   13502 N N   . ARG D 1 411 ? 37.785  51.265  -10.086 1.00 17.95  ? 440 ARG D N   1 
ATOM   13503 C CA  . ARG D 1 411 ? 38.642  51.158  -11.253 1.00 20.16  ? 440 ARG D CA  1 
ATOM   13504 C C   . ARG D 1 411 ? 40.041  50.673  -10.852 1.00 19.50  ? 440 ARG D C   1 
ATOM   13505 O O   . ARG D 1 411 ? 40.686  49.944  -11.594 1.00 19.51  ? 440 ARG D O   1 
ATOM   13506 C CB  . ARG D 1 411 ? 38.671  52.486  -12.001 1.00 23.12  ? 440 ARG D CB  1 
ATOM   13507 C CG  . ARG D 1 411 ? 37.309  52.890  -12.558 1.00 27.47  ? 440 ARG D CG  1 
ATOM   13508 C CD  . ARG D 1 411 ? 36.444  51.802  -13.228 1.00 30.41  ? 440 ARG D CD  1 
ATOM   13509 N NE  . ARG D 1 411 ? 35.209  52.472  -13.629 1.00 40.94  ? 440 ARG D NE  1 
ATOM   13510 C CZ  . ARG D 1 411 ? 35.188  53.586  -14.373 1.00 41.13  ? 440 ARG D CZ  1 
ATOM   13511 N NH1 . ARG D 1 411 ? 36.270  53.946  -15.041 1.00 47.71  ? 440 ARG D NH1 1 
ATOM   13512 N NH2 . ARG D 1 411 ? 34.102  54.333  -14.488 1.00 26.60  ? 440 ARG D NH2 1 
ATOM   13513 N N   . ALA D 1 412 ? 40.503  51.079  -9.665  1.00 22.34  ? 441 ALA D N   1 
ATOM   13514 C CA  . ALA D 1 412 ? 41.807  50.638  -9.171  1.00 21.48  ? 441 ALA D CA  1 
ATOM   13515 C C   . ALA D 1 412 ? 41.796  49.121  -9.100  1.00 21.92  ? 441 ALA D C   1 
ATOM   13516 O O   . ALA D 1 412 ? 42.790  48.486  -9.469  1.00 27.01  ? 441 ALA D O   1 
ATOM   13517 C CB  . ALA D 1 412 ? 42.067  51.273  -7.832  1.00 24.25  ? 441 ALA D CB  1 
ATOM   13518 N N   . LEU D 1 413 ? 40.641  48.565  -8.725  1.00 22.02  ? 442 LEU D N   1 
ATOM   13519 C CA  . LEU D 1 413 ? 40.522  47.128  -8.504  1.00 23.08  ? 442 LEU D CA  1 
ATOM   13520 C C   . LEU D 1 413 ? 40.038  46.354  -9.724  1.00 22.00  ? 442 LEU D C   1 
ATOM   13521 O O   . LEU D 1 413 ? 39.920  45.151  -9.592  1.00 21.84  ? 442 LEU D O   1 
ATOM   13522 C CB  . LEU D 1 413 ? 39.580  46.870  -7.330  1.00 23.62  ? 442 LEU D CB  1 
ATOM   13523 C CG  . LEU D 1 413 ? 39.985  47.565  -6.036  1.00 21.99  ? 442 LEU D CG  1 
ATOM   13524 C CD1 . LEU D 1 413 ? 39.053  47.202  -4.896  1.00 22.79  ? 442 LEU D CD1 1 
ATOM   13525 C CD2 . LEU D 1 413 ? 41.463  47.267  -5.703  1.00 21.04  ? 442 LEU D CD2 1 
ATOM   13526 N N   . GLY D 1 414 ? 39.731  47.023  -10.845 1.00 23.52  ? 443 GLY D N   1 
ATOM   13527 C CA  . GLY D 1 414 ? 39.338  46.387  -12.096 1.00 21.94  ? 443 GLY D CA  1 
ATOM   13528 C C   . GLY D 1 414 ? 37.944  45.757  -12.047 1.00 24.16  ? 443 GLY D C   1 
ATOM   13529 O O   . GLY D 1 414 ? 37.644  44.831  -12.807 1.00 22.83  ? 443 GLY D O   1 
ATOM   13530 N N   . PHE D 1 415 ? 37.080  46.270  -11.158 1.00 21.46  ? 444 PHE D N   1 
ATOM   13531 C CA  . PHE D 1 415 ? 35.687  45.867  -11.141 1.00 21.80  ? 444 PHE D CA  1 
ATOM   13532 C C   . PHE D 1 415 ? 35.115  45.937  -12.556 1.00 19.14  ? 444 PHE D C   1 
ATOM   13533 O O   . PHE D 1 415 ? 35.223  46.932  -13.278 1.00 17.07  ? 444 PHE D O   1 
ATOM   13534 C CB  . PHE D 1 415 ? 34.847  46.762  -10.233 1.00 21.99  ? 444 PHE D CB  1 
ATOM   13535 C CG  . PHE D 1 415 ? 34.974  46.535  -8.746  1.00 23.33  ? 444 PHE D CG  1 
ATOM   13536 C CD1 . PHE D 1 415 ? 35.944  45.699  -8.203  1.00 19.94  ? 444 PHE D CD1 1 
ATOM   13537 C CD2 . PHE D 1 415 ? 34.132  47.229  -7.883  1.00 24.38  ? 444 PHE D CD2 1 
ATOM   13538 C CE1 . PHE D 1 415 ? 36.035  45.530  -6.825  1.00 23.85  ? 444 PHE D CE1 1 
ATOM   13539 C CE2 . PHE D 1 415 ? 34.229  47.067  -6.508  1.00 26.23  ? 444 PHE D CE2 1 
ATOM   13540 C CZ  . PHE D 1 415 ? 35.188  46.214  -5.977  1.00 24.86  ? 444 PHE D CZ  1 
ATOM   13541 N N   . PRO D 1 416 ? 34.495  44.858  -13.041 1.00 18.81  ? 445 PRO D N   1 
ATOM   13542 C CA  . PRO D 1 416 ? 33.999  44.811  -14.424 1.00 18.09  ? 445 PRO D CA  1 
ATOM   13543 C C   . PRO D 1 416 ? 32.613  45.434  -14.584 1.00 19.56  ? 445 PRO D C   1 
ATOM   13544 O O   . PRO D 1 416 ? 32.011  45.893  -13.607 1.00 20.42  ? 445 PRO D O   1 
ATOM   13545 C CB  . PRO D 1 416 ? 33.858  43.304  -14.636 1.00 17.49  ? 445 PRO D CB  1 
ATOM   13546 C CG  . PRO D 1 416 ? 33.383  42.844  -13.268 1.00 18.37  ? 445 PRO D CG  1 
ATOM   13547 C CD  . PRO D 1 416 ? 34.272  43.590  -12.314 1.00 19.98  ? 445 PRO D CD  1 
ATOM   13548 N N   . LEU D 1 417 ? 32.103  45.354  -15.809 1.00 18.80  ? 446 LEU D N   1 
ATOM   13549 C CA  . LEU D 1 417 ? 30.751  45.791  -16.125 1.00 17.97  ? 446 LEU D CA  1 
ATOM   13550 C C   . LEU D 1 417 ? 29.758  45.107  -15.200 1.00 19.10  ? 446 LEU D C   1 
ATOM   13551 O O   . LEU D 1 417 ? 29.736  43.879  -15.091 1.00 18.36  ? 446 LEU D O   1 
ATOM   13552 C CB  . LEU D 1 417 ? 30.476  45.442  -17.587 1.00 17.86  ? 446 LEU D CB  1 
ATOM   13553 C CG  . LEU D 1 417 ? 29.104  45.871  -18.099 1.00 19.35  ? 446 LEU D CG  1 
ATOM   13554 C CD1 . LEU D 1 417 ? 29.160  47.365  -18.405 1.00 19.55  ? 446 LEU D CD1 1 
ATOM   13555 C CD2 . LEU D 1 417 ? 28.711  45.084  -19.331 1.00 20.87  ? 446 LEU D CD2 1 
ATOM   13556 N N   . GLU D 1 418 ? 28.866  45.897  -14.599 1.00 18.57  ? 447 GLU D N   1 
ATOM   13557 C CA  . GLU D 1 418 ? 27.744  45.372  -13.853 1.00 18.44  ? 447 GLU D CA  1 
ATOM   13558 C C   . GLU D 1 418 ? 26.634  44.987  -14.822 1.00 17.10  ? 447 GLU D C   1 
ATOM   13559 O O   . GLU D 1 418 ? 26.064  45.806  -15.517 1.00 16.68  ? 447 GLU D O   1 
ATOM   13560 C CB  . GLU D 1 418 ? 27.249  46.358  -12.788 1.00 17.83  ? 447 GLU D CB  1 
ATOM   13561 C CG  . GLU D 1 418 ? 26.111  45.812  -11.951 1.00 18.92  ? 447 GLU D CG  1 
ATOM   13562 C CD  . GLU D 1 418 ? 25.584  46.730  -10.858 1.00 20.32  ? 447 GLU D CD  1 
ATOM   13563 O OE1 . GLU D 1 418 ? 26.393  47.148  -10.026 1.00 23.46  ? 447 GLU D OE1 1 
ATOM   13564 O OE2 . GLU D 1 418 ? 24.343  47.006  -10.844 1.00 17.83  ? 447 GLU D OE2 1 
ATOM   13565 N N   . ARG D 1 419 ? 26.309  43.697  -14.879 1.00 18.81  ? 448 ARG D N   1 
ATOM   13566 C CA  . ARG D 1 419 ? 25.388  43.172  -15.874 1.00 20.10  ? 448 ARG D CA  1 
ATOM   13567 C C   . ARG D 1 419 ? 24.723  41.927  -15.288 1.00 21.42  ? 448 ARG D C   1 
ATOM   13568 O O   . ARG D 1 419 ? 25.130  40.803  -15.570 1.00 23.71  ? 448 ARG D O   1 
ATOM   13569 C CB  . ARG D 1 419 ? 26.180  42.939  -17.176 1.00 21.52  ? 448 ARG D CB  1 
ATOM   13570 C CG  . ARG D 1 419 ? 25.510  42.129  -18.277 1.00 24.38  ? 448 ARG D CG  1 
ATOM   13571 C CD  . ARG D 1 419 ? 24.019  42.278  -18.452 1.00 23.12  ? 448 ARG D CD  1 
ATOM   13572 N NE  . ARG D 1 419 ? 23.467  42.161  -19.793 1.00 22.18  ? 448 ARG D NE  1 
ATOM   13573 C CZ  . ARG D 1 419 ? 22.250  41.666  -20.032 1.00 23.99  ? 448 ARG D CZ  1 
ATOM   13574 N NH1 . ARG D 1 419 ? 21.663  41.859  -21.203 1.00 24.35  ? 448 ARG D NH1 1 
ATOM   13575 N NH2 . ARG D 1 419 ? 21.592  41.065  -19.053 1.00 22.75  ? 448 ARG D NH2 1 
ATOM   13576 N N   . PRO D 1 420 ? 23.694  42.101  -14.430 1.00 20.24  ? 449 PRO D N   1 
ATOM   13577 C CA  . PRO D 1 420 ? 22.909  40.985  -13.926 1.00 22.65  ? 449 PRO D CA  1 
ATOM   13578 C C   . PRO D 1 420 ? 22.021  40.412  -15.030 1.00 21.92  ? 449 PRO D C   1 
ATOM   13579 O O   . PRO D 1 420 ? 22.011  40.896  -16.160 1.00 19.59  ? 449 PRO D O   1 
ATOM   13580 C CB  . PRO D 1 420 ? 22.132  41.572  -12.739 1.00 20.41  ? 449 PRO D CB  1 
ATOM   13581 C CG  . PRO D 1 420 ? 22.010  43.053  -13.043 1.00 20.46  ? 449 PRO D CG  1 
ATOM   13582 C CD  . PRO D 1 420 ? 23.181  43.393  -13.939 1.00 20.38  ? 449 PRO D CD  1 
ATOM   13583 N N   . LYS D 1 421 ? 21.404  39.270  -14.715 1.00 23.69  ? 450 LYS D N   1 
ATOM   13584 C CA  . LYS D 1 421 ? 20.393  38.660  -15.543 1.00 24.16  ? 450 LYS D CA  1 
ATOM   13585 C C   . LYS D 1 421 ? 19.022  39.138  -15.083 1.00 21.99  ? 450 LYS D C   1 
ATOM   13586 O O   . LYS D 1 421 ? 18.766  39.203  -13.882 1.00 22.65  ? 450 LYS D O   1 
ATOM   13587 C CB  . LYS D 1 421 ? 20.462  37.134  -15.411 1.00 25.62  ? 450 LYS D CB  1 
ATOM   13588 C CG  . LYS D 1 421 ? 19.706  36.361  -16.475 1.00 29.91  ? 450 LYS D CG  1 
ATOM   13589 C CD  . LYS D 1 421 ? 20.232  36.674  -17.871 1.00 33.65  ? 450 LYS D CD  1 
ATOM   13590 C CE  . LYS D 1 421 ? 19.474  35.993  -18.984 1.00 36.53  ? 450 LYS D CE  1 
ATOM   13591 N NZ  . LYS D 1 421 ? 19.757  34.542  -19.027 1.00 44.24  ? 450 LYS D NZ  1 
ATOM   13592 N N   . SER D 1 422 ? 18.139  39.393  -16.043 1.00 21.61  ? 451 SER D N   1 
ATOM   13593 C CA  . SER D 1 422 ? 16.739  39.639  -15.772 1.00 20.55  ? 451 SER D CA  1 
ATOM   13594 C C   . SER D 1 422 ? 15.868  38.481  -16.251 1.00 23.60  ? 451 SER D C   1 
ATOM   13595 O O   . SER D 1 422 ? 16.240  37.701  -17.139 1.00 23.55  ? 451 SER D O   1 
ATOM   13596 C CB  . SER D 1 422 ? 16.251  40.928  -16.379 1.00 19.55  ? 451 SER D CB  1 
ATOM   13597 O OG  . SER D 1 422 ? 16.347  40.927  -17.790 1.00 18.85  ? 451 SER D OG  1 
ATOM   13598 N N   . MET D 1 423 ? 14.674  38.424  -15.679 1.00 21.04  ? 452 MET D N   1 
ATOM   13599 C CA  . MET D 1 423 ? 13.640  37.528  -16.158 1.00 27.54  ? 452 MET D CA  1 
ATOM   13600 C C   . MET D 1 423 ? 12.317  38.273  -16.222 1.00 25.28  ? 452 MET D C   1 
ATOM   13601 O O   . MET D 1 423 ? 12.140  39.274  -15.520 1.00 25.12  ? 452 MET D O   1 
ATOM   13602 C CB  . MET D 1 423 ? 13.465  36.336  -15.219 1.00 31.04  ? 452 MET D CB  1 
ATOM   13603 C CG  . MET D 1 423 ? 14.742  35.609  -14.958 1.00 34.94  ? 452 MET D CG  1 
ATOM   13604 S SD  . MET D 1 423 ? 15.337  34.591  -16.328 1.00 38.35  ? 452 MET D SD  1 
ATOM   13605 C CE  . MET D 1 423 ? 14.069  33.319  -16.414 1.00 38.62  ? 452 MET D CE  1 
ATOM   13606 N N   . SER D 1 424 ? 11.431  37.791  -17.112 1.00 24.40  ? 453 SER D N   1 
ATOM   13607 C CA  . SER D 1 424 ? 10.039  38.224  -17.200 1.00 24.42  ? 453 SER D CA  1 
ATOM   13608 C C   . SER D 1 424 ? 9.223   37.392  -16.231 1.00 24.86  ? 453 SER D C   1 
ATOM   13609 O O   . SER D 1 424 ? 9.691   36.348  -15.796 1.00 26.37  ? 453 SER D O   1 
ATOM   13610 C CB  . SER D 1 424 ? 9.461   38.056  -18.589 1.00 24.01  ? 453 SER D CB  1 
ATOM   13611 O OG  . SER D 1 424 ? 9.176   36.685  -18.865 1.00 27.04  ? 453 SER D OG  1 
ATOM   13612 N N   . THR D 1 425 ? 8.013   37.849  -15.924 1.00 23.99  ? 454 THR D N   1 
ATOM   13613 C CA  . THR D 1 425 ? 7.154   37.085  -15.033 1.00 24.59  ? 454 THR D CA  1 
ATOM   13614 C C   . THR D 1 425 ? 6.868   35.716  -15.634 1.00 28.46  ? 454 THR D C   1 
ATOM   13615 O O   . THR D 1 425 ? 6.941   34.701  -14.926 1.00 28.09  ? 454 THR D O   1 
ATOM   13616 C CB  . THR D 1 425 ? 5.817   37.766  -14.758 1.00 24.21  ? 454 THR D CB  1 
ATOM   13617 O OG1 . THR D 1 425 ? 6.077   38.942  -14.008 1.00 22.59  ? 454 THR D OG1 1 
ATOM   13618 C CG2 . THR D 1 425 ? 4.883   36.865  -13.993 1.00 25.24  ? 454 THR D CG2 1 
ATOM   13619 N N   . GLU D 1 426 ? 6.514   35.724  -16.931 1.00 28.74  ? 455 GLU D N   1 
ATOM   13620 C CA  . GLU D 1 426 ? 6.348   34.505  -17.711 1.00 30.98  ? 455 GLU D CA  1 
ATOM   13621 C C   . GLU D 1 426 ? 7.559   33.596  -17.534 1.00 30.50  ? 455 GLU D C   1 
ATOM   13622 O O   . GLU D 1 426 ? 7.435   32.422  -17.170 1.00 31.16  ? 455 GLU D O   1 
ATOM   13623 C CB  . GLU D 1 426 ? 6.187   34.890  -19.186 1.00 37.10  ? 455 GLU D CB  1 
ATOM   13624 C CG  . GLU D 1 426 ? 6.509   33.751  -20.146 1.00 42.30  ? 455 GLU D CG  1 
ATOM   13625 C CD  . GLU D 1 426 ? 7.386   34.085  -21.345 1.00 48.82  ? 455 GLU D CD  1 
ATOM   13626 O OE1 . GLU D 1 426 ? 7.482   35.285  -21.726 1.00 53.92  ? 455 GLU D OE1 1 
ATOM   13627 O OE2 . GLU D 1 426 ? 7.986   33.130  -21.900 1.00 48.50  ? 455 GLU D OE2 1 
ATOM   13628 N N   . GLY D 1 427 ? 8.739   34.141  -17.853 1.00 28.26  ? 456 GLY D N   1 
ATOM   13629 C CA  . GLY D 1 427 ? 9.975   33.389  -17.769 1.00 30.16  ? 456 GLY D CA  1 
ATOM   13630 C C   . GLY D 1 427 ? 10.250  32.853  -16.369 1.00 29.98  ? 456 GLY D C   1 
ATOM   13631 O O   . GLY D 1 427 ? 10.769  31.753  -16.221 1.00 28.54  ? 456 GLY D O   1 
ATOM   13632 N N   . LEU D 1 428 ? 9.920   33.644  -15.345 1.00 28.30  ? 457 LEU D N   1 
ATOM   13633 C CA  . LEU D 1 428 ? 10.141  33.248  -13.960 1.00 31.17  ? 457 LEU D CA  1 
ATOM   13634 C C   . LEU D 1 428 ? 9.102   32.204  -13.543 1.00 31.51  ? 457 LEU D C   1 
ATOM   13635 O O   . LEU D 1 428 ? 9.417   31.297  -12.773 1.00 34.45  ? 457 LEU D O   1 
ATOM   13636 C CB  . LEU D 1 428 ? 10.107  34.515  -13.087 1.00 32.05  ? 457 LEU D CB  1 
ATOM   13637 C CG  . LEU D 1 428 ? 10.741  34.437  -11.700 1.00 31.80  ? 457 LEU D CG  1 
ATOM   13638 C CD1 . LEU D 1 428 ? 12.131  33.809  -11.730 1.00 31.21  ? 457 LEU D CD1 1 
ATOM   13639 C CD2 . LEU D 1 428 ? 10.827  35.828  -11.105 1.00 31.73  ? 457 LEU D CD2 1 
ATOM   13640 N N   . MET D 1 429 ? 7.873   32.299  -14.065 1.00 36.07  ? 458 MET D N   1 
ATOM   13641 C CA  . MET D 1 429 ? 6.885   31.251  -13.851 1.00 35.77  ? 458 MET D CA  1 
ATOM   13642 C C   . MET D 1 429 ? 7.391   29.933  -14.444 1.00 35.45  ? 458 MET D C   1 
ATOM   13643 O O   . MET D 1 429 ? 7.217   28.882  -13.847 1.00 36.13  ? 458 MET D O   1 
ATOM   13644 C CB  . MET D 1 429 ? 5.534   31.616  -14.467 1.00 39.64  ? 458 MET D CB  1 
ATOM   13645 C CG  . MET D 1 429 ? 4.747   32.591  -13.612 1.00 41.12  ? 458 MET D CG  1 
ATOM   13646 S SD  . MET D 1 429 ? 3.247   33.199  -14.408 1.00 45.02  ? 458 MET D SD  1 
ATOM   13647 C CE  . MET D 1 429 ? 2.018   32.268  -13.491 1.00 44.64  ? 458 MET D CE  1 
ATOM   13648 N N   . LYS D 1 430 ? 8.065   29.982  -15.593 1.00 37.96  ? 459 LYS D N   1 
ATOM   13649 C CA  . LYS D 1 430 ? 8.554   28.760  -16.214 1.00 42.28  ? 459 LYS D CA  1 
ATOM   13650 C C   . LYS D 1 430 ? 9.729   28.209  -15.410 1.00 41.42  ? 459 LYS D C   1 
ATOM   13651 O O   . LYS D 1 430 ? 9.776   27.019  -15.119 1.00 41.48  ? 459 LYS D O   1 
ATOM   13652 C CB  . LYS D 1 430 ? 8.997   28.982  -17.665 1.00 47.85  ? 459 LYS D CB  1 
ATOM   13653 C CG  . LYS D 1 430 ? 7.886   29.153  -18.694 1.00 52.90  ? 459 LYS D CG  1 
ATOM   13654 C CD  . LYS D 1 430 ? 8.384   29.026  -20.125 1.00 59.85  ? 459 LYS D CD  1 
ATOM   13655 C CE  . LYS D 1 430 ? 7.738   30.006  -21.083 1.00 63.33  ? 459 LYS D CE  1 
ATOM   13656 N NZ  . LYS D 1 430 ? 6.263   29.867  -21.116 1.00 65.16  ? 459 LYS D NZ  1 
ATOM   13657 N N   . PHE D 1 431 ? 10.675  29.092  -15.072 1.00 42.80  ? 460 PHE D N   1 
ATOM   13658 C CA  . PHE D 1 431 ? 11.937  28.712  -14.458 1.00 40.74  ? 460 PHE D CA  1 
ATOM   13659 C C   . PHE D 1 431 ? 11.720  28.093  -13.079 1.00 41.79  ? 460 PHE D C   1 
ATOM   13660 O O   . PHE D 1 431 ? 12.534  27.291  -12.625 1.00 42.76  ? 460 PHE D O   1 
ATOM   13661 C CB  . PHE D 1 431 ? 12.864  29.922  -14.334 1.00 41.54  ? 460 PHE D CB  1 
ATOM   13662 C CG  . PHE D 1 431 ? 14.236  29.549  -13.837 1.00 41.30  ? 460 PHE D CG  1 
ATOM   13663 C CD1 . PHE D 1 431 ? 15.212  29.121  -14.721 1.00 43.17  ? 460 PHE D CD1 1 
ATOM   13664 C CD2 . PHE D 1 431 ? 14.513  29.521  -12.480 1.00 38.08  ? 460 PHE D CD2 1 
ATOM   13665 C CE1 . PHE D 1 431 ? 16.466  28.745  -14.260 1.00 42.73  ? 460 PHE D CE1 1 
ATOM   13666 C CE2 . PHE D 1 431 ? 15.758  29.124  -12.019 1.00 42.04  ? 460 PHE D CE2 1 
ATOM   13667 C CZ  . PHE D 1 431 ? 16.733  28.736  -12.912 1.00 42.78  ? 460 PHE D CZ  1 
ATOM   13668 N N   . VAL D 1 432 ? 10.639  28.497  -12.407 1.00 43.63  ? 461 VAL D N   1 
ATOM   13669 C CA  . VAL D 1 432 ? 10.209  27.846  -11.178 1.00 45.06  ? 461 VAL D CA  1 
ATOM   13670 C C   . VAL D 1 432 ? 9.590   26.482  -11.500 1.00 45.34  ? 461 VAL D C   1 
ATOM   13671 O O   . VAL D 1 432 ? 9.484   25.643  -10.621 1.00 43.79  ? 461 VAL D O   1 
ATOM   13672 C CB  . VAL D 1 432 ? 9.249   28.747  -10.372 1.00 43.68  ? 461 VAL D CB  1 
ATOM   13673 C CG1 . VAL D 1 432 ? 8.590   28.020  -9.210  1.00 44.56  ? 461 VAL D CG1 1 
ATOM   13674 C CG2 . VAL D 1 432 ? 9.954   29.996  -9.866  1.00 44.75  ? 461 VAL D CG2 1 
ATOM   13675 N N   . ASP D 1 433 ? 9.183   26.250  -12.754 1.00 55.70  ? 462 ASP D N   1 
ATOM   13676 C CA  . ASP D 1 433 ? 8.604   24.974  -13.161 1.00 56.82  ? 462 ASP D CA  1 
ATOM   13677 C C   . ASP D 1 433 ? 9.561   24.236  -14.098 1.00 62.10  ? 462 ASP D C   1 
ATOM   13678 O O   . ASP D 1 433 ? 9.176   23.854  -15.203 1.00 64.05  ? 462 ASP D O   1 
ATOM   13679 C CB  . ASP D 1 433 ? 7.258   25.183  -13.860 1.00 57.30  ? 462 ASP D CB  1 
ATOM   13680 C CG  . ASP D 1 433 ? 6.230   25.976  -13.076 1.00 57.50  ? 462 ASP D CG  1 
ATOM   13681 O OD1 . ASP D 1 433 ? 6.488   26.266  -11.903 1.00 61.97  ? 462 ASP D OD1 1 
ATOM   13682 O OD2 . ASP D 1 433 ? 5.181   26.315  -13.665 1.00 63.90  ? 462 ASP D OD2 1 
ATOM   13683 N N   . SER D 1 434 ? 10.815  24.047  -13.663 1.00 64.67  ? 463 SER D N   1 
ATOM   13684 C CA  . SER D 1 434 ? 11.801  23.310  -14.440 1.00 61.40  ? 463 SER D CA  1 
ATOM   13685 C C   . SER D 1 434 ? 13.143  23.304  -13.706 1.00 58.94  ? 463 SER D C   1 
ATOM   13686 O O   . SER D 1 434 ? 13.902  22.360  -13.971 1.00 53.90  ? 463 SER D O   1 
ATOM   13687 C CB  . SER D 1 434 ? 11.975  23.865  -15.832 1.00 64.70  ? 463 SER D CB  1 
ATOM   13688 O OG  . SER D 1 434 ? 12.393  25.222  -15.785 1.00 69.59  ? 463 SER D OG  1 
HETATM 13689 C C1  . CIT E 2 .   ? 5.860   16.063  11.589  1.00 25.80  ? 501 CIT A C1  1 
HETATM 13690 O O1  . CIT E 2 .   ? 6.918   16.564  11.209  1.00 24.91  ? 501 CIT A O1  1 
HETATM 13691 O O2  . CIT E 2 .   ? 5.261   16.412  12.653  1.00 31.01  ? 501 CIT A O2  1 
HETATM 13692 C C2  . CIT E 2 .   ? 5.272   14.926  10.781  1.00 26.08  ? 501 CIT A C2  1 
HETATM 13693 C C3  . CIT E 2 .   ? 5.814   14.685  9.349   1.00 24.78  ? 501 CIT A C3  1 
HETATM 13694 O O7  . CIT E 2 .   ? 5.786   15.880  8.578   1.00 25.86  ? 501 CIT A O7  1 
HETATM 13695 C C4  . CIT E 2 .   ? 4.909   13.635  8.697   1.00 26.07  ? 501 CIT A C4  1 
HETATM 13696 C C5  . CIT E 2 .   ? 3.426   13.928  8.824   1.00 30.18  ? 501 CIT A C5  1 
HETATM 13697 O O3  . CIT E 2 .   ? 2.731   13.138  9.488   1.00 30.27  ? 501 CIT A O3  1 
HETATM 13698 O O4  . CIT E 2 .   ? 2.992   14.963  8.281   1.00 34.38  ? 501 CIT A O4  1 
HETATM 13699 C C6  . CIT E 2 .   ? 7.252   14.093  9.402   1.00 24.37  ? 501 CIT A C6  1 
HETATM 13700 O O5  . CIT E 2 .   ? 7.898   14.032  8.350   1.00 26.48  ? 501 CIT A O5  1 
HETATM 13701 O O6  . CIT E 2 .   ? 7.665   13.713  10.494  1.00 22.02  ? 501 CIT A O6  1 
HETATM 13702 C C1  . CIT F 2 .   ? 10.163  5.691   35.785  1.00 22.76  ? 501 CIT B C1  1 
HETATM 13703 O O1  . CIT F 2 .   ? 9.181   5.814   36.575  1.00 20.61  ? 501 CIT B O1  1 
HETATM 13704 O O2  . CIT F 2 .   ? 10.730  6.643   35.235  1.00 17.72  ? 501 CIT B O2  1 
HETATM 13705 C C2  . CIT F 2 .   ? 10.748  4.321   35.524  1.00 24.10  ? 501 CIT B C2  1 
HETATM 13706 C C3  . CIT F 2 .   ? 10.213  3.137   36.356  1.00 31.08  ? 501 CIT B C3  1 
HETATM 13707 O O7  . CIT F 2 .   ? 10.297  3.458   37.735  1.00 31.04  ? 501 CIT B O7  1 
HETATM 13708 C C4  . CIT F 2 .   ? 11.133  1.930   36.142  1.00 36.40  ? 501 CIT B C4  1 
HETATM 13709 C C5  . CIT F 2 .   ? 12.047  1.597   37.316  1.00 46.06  ? 501 CIT B C5  1 
HETATM 13710 O O3  . CIT F 2 .   ? 11.800  0.530   37.920  1.00 58.18  ? 501 CIT B O3  1 
HETATM 13711 O O4  . CIT F 2 .   ? 13.007  2.380   37.621  1.00 37.69  ? 501 CIT B O4  1 
HETATM 13712 C C6  . CIT F 2 .   ? 8.761   2.746   35.925  1.00 25.39  ? 501 CIT B C6  1 
HETATM 13713 O O5  . CIT F 2 .   ? 8.115   2.015   36.665  1.00 25.40  ? 501 CIT B O5  1 
HETATM 13714 O O6  . CIT F 2 .   ? 8.334   3.176   34.854  1.00 24.96  ? 501 CIT B O6  1 
HETATM 13715 C C1  . CIT G 2 .   ? 23.492  43.945  46.392  1.00 26.09  ? 501 CIT C C1  1 
HETATM 13716 O O1  . CIT G 2 .   ? 22.521  43.312  45.939  1.00 29.07  ? 501 CIT C O1  1 
HETATM 13717 O O2  . CIT G 2 .   ? 24.054  43.652  47.474  1.00 26.06  ? 501 CIT C O2  1 
HETATM 13718 C C2  . CIT G 2 .   ? 23.986  45.171  45.642  1.00 28.09  ? 501 CIT C C2  1 
HETATM 13719 C C3  . CIT G 2 .   ? 23.496  45.398  44.199  1.00 30.82  ? 501 CIT C C3  1 
HETATM 13720 O O7  . CIT G 2 .   ? 23.652  44.204  43.444  1.00 31.95  ? 501 CIT C O7  1 
HETATM 13721 C C4  . CIT G 2 .   ? 24.332  46.504  43.534  1.00 32.20  ? 501 CIT C C4  1 
HETATM 13722 C C5  . CIT G 2 .   ? 25.825  46.261  43.454  1.00 35.89  ? 501 CIT C C5  1 
HETATM 13723 O O3  . CIT G 2 .   ? 26.239  45.413  42.621  1.00 40.49  ? 501 CIT C O3  1 
HETATM 13724 O O4  . CIT G 2 .   ? 26.562  46.920  44.216  1.00 35.99  ? 501 CIT C O4  1 
HETATM 13725 C C6  . CIT G 2 .   ? 22.009  45.876  44.207  1.00 27.69  ? 501 CIT C C6  1 
HETATM 13726 O O5  . CIT G 2 .   ? 21.441  45.900  43.149  1.00 27.90  ? 501 CIT C O5  1 
HETATM 13727 O O6  . CIT G 2 .   ? 21.515  46.295  45.271  1.00 27.11  ? 501 CIT C O6  1 
HETATM 13728 C C1  . CIT H 2 .   ? 19.592  54.335  1.252   1.00 24.18  ? 501 CIT D C1  1 
HETATM 13729 O O1  . CIT H 2 .   ? 20.672  54.181  1.914   1.00 23.50  ? 501 CIT D O1  1 
HETATM 13730 O O2  . CIT H 2 .   ? 18.965  53.404  0.715   1.00 20.74  ? 501 CIT D O2  1 
HETATM 13731 C C2  . CIT H 2 .   ? 19.032  55.728  0.986   1.00 23.82  ? 501 CIT D C2  1 
HETATM 13732 C C3  . CIT H 2 .   ? 19.578  56.937  1.770   1.00 26.50  ? 501 CIT D C3  1 
HETATM 13733 O O7  . CIT H 2 .   ? 19.480  56.685  3.172   1.00 25.20  ? 501 CIT D O7  1 
HETATM 13734 C C4  . CIT H 2 .   ? 18.673  58.136  1.450   1.00 27.85  ? 501 CIT D C4  1 
HETATM 13735 C C5  . CIT H 2 .   ? 17.512  58.336  2.417   1.00 33.66  ? 501 CIT D C5  1 
HETATM 13736 O O3  . CIT H 2 .   ? 17.412  59.438  3.012   1.00 42.45  ? 501 CIT D O3  1 
HETATM 13737 O O4  . CIT H 2 .   ? 16.732  57.391  2.595   1.00 31.74  ? 501 CIT D O4  1 
HETATM 13738 C C6  . CIT H 2 .   ? 21.032  57.306  1.335   1.00 23.39  ? 501 CIT D C6  1 
HETATM 13739 O O5  . CIT H 2 .   ? 21.670  58.013  2.110   1.00 24.77  ? 501 CIT D O5  1 
HETATM 13740 O O6  . CIT H 2 .   ? 21.466  56.920  0.231   1.00 23.22  ? 501 CIT D O6  1 
HETATM 13741 O O   . HOH I 3 .   ? 6.690   -4.791  1.378   1.00 39.13  ? 601 HOH A O   1 
HETATM 13742 O O   . HOH I 3 .   ? 3.574   7.175   -18.566 1.00 32.63  ? 602 HOH A O   1 
HETATM 13743 O O   . HOH I 3 .   ? 20.374  2.748   14.946  1.00 37.77  ? 603 HOH A O   1 
HETATM 13744 O O   . HOH I 3 .   ? 26.866  5.923   16.858  1.00 42.04  ? 604 HOH A O   1 
HETATM 13745 O O   . HOH I 3 .   ? 8.789   10.645  23.510  1.00 48.96  ? 605 HOH A O   1 
HETATM 13746 O O   . HOH I 3 .   ? 31.712  18.780  0.508   1.00 35.68  ? 606 HOH A O   1 
HETATM 13747 O O   . HOH I 3 .   ? 7.455   6.158   6.707   1.00 40.86  ? 607 HOH A O   1 
HETATM 13748 O O   . HOH I 3 .   ? 25.373  -8.336  14.217  1.00 35.93  ? 608 HOH A O   1 
HETATM 13749 O O   . HOH I 3 .   ? 29.885  -8.284  22.313  1.00 39.09  ? 609 HOH A O   1 
HETATM 13750 O O   . HOH I 3 .   ? 27.293  14.125  -8.411  1.00 32.42  ? 610 HOH A O   1 
HETATM 13751 O O   . HOH I 3 .   ? 3.005   15.886  5.993   1.00 37.75  ? 611 HOH A O   1 
HETATM 13752 O O   . HOH I 3 .   ? 22.708  10.436  8.832   1.00 55.83  ? 612 HOH A O   1 
HETATM 13753 O O   . HOH I 3 .   ? 30.661  -3.610  11.821  1.00 33.38  ? 613 HOH A O   1 
HETATM 13754 O O   . HOH I 3 .   ? 5.070   11.338  2.080   1.00 23.49  ? 614 HOH A O   1 
HETATM 13755 O O   . HOH I 3 .   ? 27.889  -3.239  12.052  1.00 60.11  ? 615 HOH A O   1 
HETATM 13756 O O   . HOH I 3 .   ? 11.929  22.003  -2.127  1.00 28.46  ? 616 HOH A O   1 
HETATM 13757 O O   . HOH I 3 .   ? 3.131   11.891  6.938   1.00 39.30  ? 617 HOH A O   1 
HETATM 13758 O O   . HOH I 3 .   ? -15.410 24.713  -13.039 1.00 38.64  ? 618 HOH A O   1 
HETATM 13759 O O   . HOH I 3 .   ? 15.488  4.637   3.032   1.00 39.60  ? 619 HOH A O   1 
HETATM 13760 O O   . HOH I 3 .   ? 16.940  9.039   17.214  1.00 23.01  ? 620 HOH A O   1 
HETATM 13761 O O   . HOH I 3 .   ? 29.981  17.178  -2.773  1.00 34.84  ? 621 HOH A O   1 
HETATM 13762 O O   . HOH I 3 .   ? 27.699  17.842  21.526  1.00 56.78  ? 622 HOH A O   1 
HETATM 13763 O O   . HOH I 3 .   ? 3.582   28.795  0.843   1.00 39.59  ? 623 HOH A O   1 
HETATM 13764 O O   . HOH I 3 .   ? 11.449  -10.647 -3.392  1.00 44.87  ? 624 HOH A O   1 
HETATM 13765 O O   . HOH I 3 .   ? 33.216  0.392   10.764  1.00 29.94  ? 625 HOH A O   1 
HETATM 13766 O O   . HOH I 3 .   ? 32.591  1.649   2.853   1.00 54.89  ? 626 HOH A O   1 
HETATM 13767 O O   . HOH I 3 .   ? 1.418   -1.567  11.801  1.00 26.77  ? 627 HOH A O   1 
HETATM 13768 O O   . HOH I 3 .   ? -2.340  3.280   -5.150  1.00 42.96  ? 628 HOH A O   1 
HETATM 13769 O O   . HOH I 3 .   ? 18.465  -3.217  23.223  1.00 25.95  ? 629 HOH A O   1 
HETATM 13770 O O   . HOH I 3 .   ? 20.894  10.794  -9.128  1.00 30.46  ? 630 HOH A O   1 
HETATM 13771 O O   . HOH I 3 .   ? -2.261  15.631  25.253  1.00 24.54  ? 631 HOH A O   1 
HETATM 13772 O O   . HOH I 3 .   ? -17.857 27.375  2.430   1.00 50.61  ? 632 HOH A O   1 
HETATM 13773 O O   . HOH I 3 .   ? 19.337  -1.600  -12.897 1.00 42.28  ? 633 HOH A O   1 
HETATM 13774 O O   . HOH I 3 .   ? 5.522   -11.295 4.278   1.00 27.78  ? 634 HOH A O   1 
HETATM 13775 O O   . HOH I 3 .   ? 15.203  28.303  5.121   1.00 47.00  ? 635 HOH A O   1 
HETATM 13776 O O   . HOH I 3 .   ? 28.799  1.734   26.185  1.00 41.27  ? 636 HOH A O   1 
HETATM 13777 O O   . HOH I 3 .   ? 4.378   14.211  -6.776  1.00 48.50  ? 637 HOH A O   1 
HETATM 13778 O O   . HOH I 3 .   ? 21.038  20.539  1.623   1.00 42.10  ? 638 HOH A O   1 
HETATM 13779 O O   . HOH I 3 .   ? 35.955  0.939   15.157  1.00 40.21  ? 639 HOH A O   1 
HETATM 13780 O O   . HOH I 3 .   ? 28.763  4.714   -4.245  1.00 37.63  ? 640 HOH A O   1 
HETATM 13781 O O   . HOH I 3 .   ? -9.100  11.902  44.508  1.00 37.96  ? 641 HOH A O   1 
HETATM 13782 O O   . HOH I 3 .   ? 29.913  26.453  23.831  1.00 36.62  ? 642 HOH A O   1 
HETATM 13783 O O   . HOH I 3 .   ? 8.772   12.610  5.563   1.00 46.36  ? 643 HOH A O   1 
HETATM 13784 O O   . HOH I 3 .   ? -2.605  -7.419  10.482  1.00 56.69  ? 644 HOH A O   1 
HETATM 13785 O O   . HOH I 3 .   ? 30.781  9.608   23.749  1.00 30.18  ? 645 HOH A O   1 
HETATM 13786 O O   . HOH I 3 .   ? -0.341  -5.113  -7.197  1.00 40.28  ? 646 HOH A O   1 
HETATM 13787 O O   . HOH I 3 .   ? -12.897 17.492  3.667   1.00 50.70  ? 647 HOH A O   1 
HETATM 13788 O O   . HOH I 3 .   ? -17.922 18.030  2.876   1.00 41.51  ? 648 HOH A O   1 
HETATM 13789 O O   . HOH I 3 .   ? 17.592  5.209   5.750   1.00 35.57  ? 649 HOH A O   1 
HETATM 13790 O O   . HOH I 3 .   ? -21.081 21.200  2.118   1.00 37.46  ? 650 HOH A O   1 
HETATM 13791 O O   . HOH I 3 .   ? 2.581   24.547  -1.693  1.00 44.75  ? 651 HOH A O   1 
HETATM 13792 O O   . HOH I 3 .   ? -5.830  -11.878 11.191  1.00 40.92  ? 652 HOH A O   1 
HETATM 13793 O O   . HOH I 3 .   ? 8.306   -6.761  -11.006 1.00 47.97  ? 653 HOH A O   1 
HETATM 13794 O O   . HOH I 3 .   ? 29.071  19.331  -3.060  1.00 34.62  ? 654 HOH A O   1 
HETATM 13795 O O   . HOH I 3 .   ? 20.550  -4.998  -7.267  1.00 30.32  ? 655 HOH A O   1 
HETATM 13796 O O   . HOH I 3 .   ? 20.892  5.748   -3.198  1.00 22.70  ? 656 HOH A O   1 
HETATM 13797 O O   . HOH I 3 .   ? 3.001   22.870  4.925   1.00 27.40  ? 657 HOH A O   1 
HETATM 13798 O O   . HOH I 3 .   ? 23.977  -4.969  13.826  1.00 19.49  ? 658 HOH A O   1 
HETATM 13799 O O   . HOH I 3 .   ? 9.687   9.387   28.999  1.00 17.68  ? 659 HOH A O   1 
HETATM 13800 O O   . HOH I 3 .   ? 16.054  19.912  15.978  1.00 23.99  ? 660 HOH A O   1 
HETATM 13801 O O   . HOH I 3 .   ? -12.082 16.023  8.054   1.00 42.10  ? 661 HOH A O   1 
HETATM 13802 O O   . HOH I 3 .   ? 6.430   13.604  19.382  1.00 23.66  ? 662 HOH A O   1 
HETATM 13803 O O   . HOH I 3 .   ? 17.847  8.646   22.014  1.00 22.36  ? 663 HOH A O   1 
HETATM 13804 O O   . HOH I 3 .   ? 27.400  8.231   26.497  1.00 30.02  ? 664 HOH A O   1 
HETATM 13805 O O   . HOH I 3 .   ? 20.357  17.255  -11.489 1.00 58.42  ? 665 HOH A O   1 
HETATM 13806 O O   . HOH I 3 .   ? 4.429   26.396  14.085  1.00 28.15  ? 666 HOH A O   1 
HETATM 13807 O O   . HOH I 3 .   ? 17.272  26.959  -0.850  1.00 51.46  ? 667 HOH A O   1 
HETATM 13808 O O   . HOH I 3 .   ? 40.057  6.234   8.428   1.00 27.11  ? 668 HOH A O   1 
HETATM 13809 O O   . HOH I 3 .   ? 2.435   9.519   4.330   1.00 27.33  ? 669 HOH A O   1 
HETATM 13810 O O   . HOH I 3 .   ? 20.615  7.667   27.918  1.00 19.99  ? 670 HOH A O   1 
HETATM 13811 O O   . HOH I 3 .   ? 5.417   30.888  11.534  1.00 39.46  ? 671 HOH A O   1 
HETATM 13812 O O   . HOH I 3 .   ? 2.646   0.569   -3.743  1.00 54.61  ? 672 HOH A O   1 
HETATM 13813 O O   . HOH I 3 .   ? 30.339  20.640  3.729   1.00 34.64  ? 673 HOH A O   1 
HETATM 13814 O O   . HOH I 3 .   ? 3.007   14.977  41.234  1.00 28.50  ? 674 HOH A O   1 
HETATM 13815 O O   . HOH I 3 .   ? 6.645   -17.939 11.383  1.00 44.38  ? 675 HOH A O   1 
HETATM 13816 O O   . HOH I 3 .   ? -9.084  21.335  5.412   1.00 45.57  ? 676 HOH A O   1 
HETATM 13817 O O   . HOH I 3 .   ? -19.484 23.268  -8.786  1.00 55.83  ? 677 HOH A O   1 
HETATM 13818 O O   . HOH I 3 .   ? -1.621  -2.023  -0.318  1.00 43.80  ? 678 HOH A O   1 
HETATM 13819 O O   . HOH I 3 .   ? 24.386  -10.905 18.218  1.00 44.59  ? 679 HOH A O   1 
HETATM 13820 O O   . HOH I 3 .   ? 0.688   2.431   6.450   1.00 51.69  ? 680 HOH A O   1 
HETATM 13821 O O   . HOH I 3 .   ? -14.455 21.675  8.054   1.00 39.09  ? 681 HOH A O   1 
HETATM 13822 O O   . HOH I 3 .   ? 2.244   13.713  12.109  1.00 20.47  ? 682 HOH A O   1 
HETATM 13823 O O   . HOH I 3 .   ? 27.271  0.717   30.235  1.00 42.87  ? 683 HOH A O   1 
HETATM 13824 O O   . HOH I 3 .   ? -1.621  14.701  11.603  1.00 34.84  ? 684 HOH A O   1 
HETATM 13825 O O   . HOH I 3 .   ? 33.303  14.808  -5.229  1.00 42.77  ? 685 HOH A O   1 
HETATM 13826 O O   . HOH I 3 .   ? 8.933   -10.105 11.980  1.00 43.78  ? 686 HOH A O   1 
HETATM 13827 O O   . HOH I 3 .   ? 32.455  -0.317  17.521  1.00 36.35  ? 687 HOH A O   1 
HETATM 13828 O O   . HOH I 3 .   ? 19.034  -5.054  1.784   1.00 20.90  ? 688 HOH A O   1 
HETATM 13829 O O   . HOH I 3 .   ? 15.013  13.812  25.346  1.00 22.36  ? 689 HOH A O   1 
HETATM 13830 O O   . HOH I 3 .   ? 15.659  29.036  35.318  1.00 44.98  ? 690 HOH A O   1 
HETATM 13831 O O   . HOH I 3 .   ? 28.067  -1.847  24.994  1.00 48.14  ? 691 HOH A O   1 
HETATM 13832 O O   . HOH I 3 .   ? 13.024  13.110  12.084  1.00 20.83  ? 692 HOH A O   1 
HETATM 13833 O O   . HOH I 3 .   ? 11.232  14.435  6.086   1.00 23.82  ? 693 HOH A O   1 
HETATM 13834 O O   . HOH I 3 .   ? 17.420  12.253  25.854  1.00 19.80  ? 694 HOH A O   1 
HETATM 13835 O O   . HOH I 3 .   ? 17.744  17.534  -7.178  1.00 49.38  ? 695 HOH A O   1 
HETATM 13836 O O   . HOH I 3 .   ? 24.438  12.116  -1.881  1.00 22.30  ? 696 HOH A O   1 
HETATM 13837 O O   . HOH I 3 .   ? 20.850  20.919  12.176  1.00 28.42  ? 697 HOH A O   1 
HETATM 13838 O O   . HOH I 3 .   ? 13.658  18.186  -3.617  1.00 40.46  ? 698 HOH A O   1 
HETATM 13839 O O   . HOH I 3 .   ? -2.721  1.654   5.259   1.00 28.39  ? 699 HOH A O   1 
HETATM 13840 O O   . HOH I 3 .   ? 9.045   26.288  24.546  1.00 34.68  ? 700 HOH A O   1 
HETATM 13841 O O   . HOH I 3 .   ? 3.917   -0.993  12.660  1.00 23.78  ? 701 HOH A O   1 
HETATM 13842 O O   . HOH I 3 .   ? 27.221  -1.964  30.157  1.00 32.52  ? 702 HOH A O   1 
HETATM 13843 O O   . HOH I 3 .   ? 3.196   10.533  -15.702 1.00 56.98  ? 703 HOH A O   1 
HETATM 13844 O O   . HOH I 3 .   ? -0.861  27.941  25.527  1.00 35.78  ? 704 HOH A O   1 
HETATM 13845 O O   . HOH I 3 .   ? 14.102  22.778  2.508   1.00 28.91  ? 705 HOH A O   1 
HETATM 13846 O O   . HOH I 3 .   ? 24.575  0.584   -1.746  1.00 30.17  ? 706 HOH A O   1 
HETATM 13847 O O   . HOH I 3 .   ? 12.865  18.706  -7.093  1.00 30.73  ? 707 HOH A O   1 
HETATM 13848 O O   . HOH I 3 .   ? 36.106  15.065  11.577  1.00 35.43  ? 708 HOH A O   1 
HETATM 13849 O O   . HOH I 3 .   ? 5.051   8.756   -2.104  1.00 45.32  ? 709 HOH A O   1 
HETATM 13850 O O   . HOH I 3 .   ? 18.022  10.053  19.565  1.00 19.54  ? 710 HOH A O   1 
HETATM 13851 O O   . HOH I 3 .   ? 4.690   8.645   2.393   1.00 41.36  ? 711 HOH A O   1 
HETATM 13852 O O   . HOH I 3 .   ? -2.400  -5.581  10.264  1.00 27.17  ? 712 HOH A O   1 
HETATM 13853 O O   . HOH I 3 .   ? 19.223  22.406  10.185  1.00 28.12  ? 713 HOH A O   1 
HETATM 13854 O O   . HOH I 3 .   ? -11.975 32.173  -3.874  1.00 35.86  ? 714 HOH A O   1 
HETATM 13855 O O   . HOH I 3 .   ? 21.686  -4.932  26.230  1.00 22.35  ? 715 HOH A O   1 
HETATM 13856 O O   . HOH I 3 .   ? 8.365   19.736  -18.530 1.00 42.66  ? 716 HOH A O   1 
HETATM 13857 O O   . HOH I 3 .   ? 18.656  -16.867 12.750  1.00 42.86  ? 717 HOH A O   1 
HETATM 13858 O O   . HOH I 3 .   ? 9.692   20.806  5.608   1.00 31.93  ? 718 HOH A O   1 
HETATM 13859 O O   . HOH I 3 .   ? 25.034  4.969   31.470  1.00 37.31  ? 719 HOH A O   1 
HETATM 13860 O O   . HOH I 3 .   ? 20.857  -2.499  24.686  1.00 22.10  ? 720 HOH A O   1 
HETATM 13861 O O   . HOH I 3 .   ? 31.941  5.268   -11.919 1.00 42.94  ? 721 HOH A O   1 
HETATM 13862 O O   . HOH I 3 .   ? 20.147  -12.029 3.327   1.00 35.21  ? 722 HOH A O   1 
HETATM 13863 O O   . HOH I 3 .   ? 32.594  2.240   9.179   1.00 24.50  ? 723 HOH A O   1 
HETATM 13864 O O   . HOH I 3 .   ? 29.208  7.340   23.700  1.00 23.73  ? 724 HOH A O   1 
HETATM 13865 O O   . HOH I 3 .   ? -5.391  27.958  47.382  1.00 41.32  ? 725 HOH A O   1 
HETATM 13866 O O   . HOH I 3 .   ? 9.830   0.730   1.476   1.00 48.33  ? 726 HOH A O   1 
HETATM 13867 O O   . HOH I 3 .   ? 29.723  7.427   3.218   1.00 49.54  ? 727 HOH A O   1 
HETATM 13868 O O   . HOH I 3 .   ? 0.994   -11.286 -4.552  1.00 35.60  ? 728 HOH A O   1 
HETATM 13869 O O   . HOH I 3 .   ? 1.109   16.666  26.279  1.00 22.33  ? 729 HOH A O   1 
HETATM 13870 O O   . HOH I 3 .   ? 10.748  25.522  1.638   1.00 69.30  ? 730 HOH A O   1 
HETATM 13871 O O   . HOH I 3 .   ? -4.728  -14.493 8.772   1.00 36.47  ? 731 HOH A O   1 
HETATM 13872 O O   . HOH I 3 .   ? 12.748  -8.348  5.215   1.00 36.61  ? 732 HOH A O   1 
HETATM 13873 O O   . HOH I 3 .   ? 25.792  16.767  16.337  1.00 27.81  ? 733 HOH A O   1 
HETATM 13874 O O   . HOH I 3 .   ? 12.875  21.467  -4.444  1.00 39.39  ? 734 HOH A O   1 
HETATM 13875 O O   . HOH I 3 .   ? 11.779  -17.088 13.241  1.00 26.02  ? 735 HOH A O   1 
HETATM 13876 O O   . HOH I 3 .   ? 19.833  8.623   32.246  1.00 26.98  ? 736 HOH A O   1 
HETATM 13877 O O   . HOH I 3 .   ? 28.966  17.693  26.777  1.00 33.23  ? 737 HOH A O   1 
HETATM 13878 O O   . HOH I 3 .   ? -10.848 25.577  -15.331 1.00 44.42  ? 738 HOH A O   1 
HETATM 13879 O O   . HOH I 3 .   ? 19.213  -1.841  14.170  1.00 49.25  ? 739 HOH A O   1 
HETATM 13880 O O   . HOH I 3 .   ? -2.698  -2.641  -6.598  1.00 40.17  ? 740 HOH A O   1 
HETATM 13881 O O   . HOH I 3 .   ? 21.143  -16.934 9.324   1.00 36.27  ? 741 HOH A O   1 
HETATM 13882 O O   . HOH I 3 .   ? -3.524  15.366  45.882  1.00 37.50  ? 742 HOH A O   1 
HETATM 13883 O O   . HOH I 3 .   ? 8.406   27.731  2.631   1.00 39.71  ? 743 HOH A O   1 
HETATM 13884 O O   . HOH I 3 .   ? -1.270  29.612  41.188  1.00 38.00  ? 744 HOH A O   1 
HETATM 13885 O O   . HOH I 3 .   ? -15.831 19.050  -13.949 1.00 51.63  ? 745 HOH A O   1 
HETATM 13886 O O   . HOH I 3 .   ? 15.097  25.614  4.622   1.00 42.09  ? 746 HOH A O   1 
HETATM 13887 O O   . HOH I 3 .   ? -8.083  7.683   6.515   1.00 37.53  ? 747 HOH A O   1 
HETATM 13888 O O   . HOH I 3 .   ? 8.645   13.606  -0.033  1.00 42.79  ? 748 HOH A O   1 
HETATM 13889 O O   . HOH I 3 .   ? 4.563   13.769  13.821  1.00 17.90  ? 749 HOH A O   1 
HETATM 13890 O O   . HOH I 3 .   ? 9.763   8.376   3.759   1.00 40.18  ? 750 HOH A O   1 
HETATM 13891 O O   . HOH I 3 .   ? 11.112  4.503   0.112   1.00 51.22  ? 751 HOH A O   1 
HETATM 13892 O O   . HOH I 3 .   ? 18.233  -7.838  23.456  1.00 29.82  ? 752 HOH A O   1 
HETATM 13893 O O   . HOH I 3 .   ? -2.688  22.917  9.988   1.00 31.03  ? 753 HOH A O   1 
HETATM 13894 O O   . HOH I 3 .   ? 4.192   14.104  -11.865 1.00 47.19  ? 754 HOH A O   1 
HETATM 13895 O O   . HOH I 3 .   ? 20.451  5.016   -12.164 1.00 34.95  ? 755 HOH A O   1 
HETATM 13896 O O   . HOH I 3 .   ? 23.660  8.316   26.387  1.00 33.26  ? 756 HOH A O   1 
HETATM 13897 O O   . HOH I 3 .   ? 3.638   13.748  -19.150 1.00 36.06  ? 757 HOH A O   1 
HETATM 13898 O O   . HOH I 3 .   ? 20.004  27.470  7.771   1.00 51.00  ? 758 HOH A O   1 
HETATM 13899 O O   . HOH I 3 .   ? 41.680  16.675  14.696  1.00 39.49  ? 759 HOH A O   1 
HETATM 13900 O O   . HOH I 3 .   ? 10.800  12.336  -4.085  1.00 44.60  ? 760 HOH A O   1 
HETATM 13901 O O   . HOH I 3 .   ? -0.610  -13.564 -9.479  1.00 34.07  ? 761 HOH A O   1 
HETATM 13902 O O   . HOH I 3 .   ? -8.210  10.459  -9.142  1.00 59.78  ? 762 HOH A O   1 
HETATM 13903 O O   . HOH I 3 .   ? 2.876   -11.686 3.818   1.00 29.07  ? 763 HOH A O   1 
HETATM 13904 O O   . HOH I 3 .   ? 42.444  11.802  13.576  1.00 27.86  ? 764 HOH A O   1 
HETATM 13905 O O   . HOH I 3 .   ? 24.186  23.307  -4.025  1.00 48.21  ? 765 HOH A O   1 
HETATM 13906 O O   . HOH I 3 .   ? 25.959  10.682  12.836  1.00 43.79  ? 766 HOH A O   1 
HETATM 13907 O O   . HOH I 3 .   ? 29.015  15.106  26.156  1.00 37.18  ? 767 HOH A O   1 
HETATM 13908 O O   . HOH I 3 .   ? 26.792  -8.169  -2.947  1.00 37.64  ? 768 HOH A O   1 
HETATM 13909 O O   . HOH I 3 .   ? 22.523  -2.408  1.014   1.00 36.70  ? 769 HOH A O   1 
HETATM 13910 O O   . HOH I 3 .   ? -3.867  -0.970  7.236   1.00 36.17  ? 770 HOH A O   1 
HETATM 13911 O O   . HOH I 3 .   ? -9.428  26.460  46.756  1.00 46.03  ? 771 HOH A O   1 
HETATM 13912 O O   . HOH I 3 .   ? -2.775  31.388  8.368   1.00 54.68  ? 772 HOH A O   1 
HETATM 13913 O O   . HOH I 3 .   ? -0.985  15.480  39.352  1.00 24.56  ? 773 HOH A O   1 
HETATM 13914 O O   . HOH I 3 .   ? 22.514  7.752   -16.646 1.00 44.89  ? 774 HOH A O   1 
HETATM 13915 O O   . HOH I 3 .   ? 33.519  0.247   23.835  1.00 52.96  ? 775 HOH A O   1 
HETATM 13916 O O   . HOH I 3 .   ? 14.641  -3.729  7.353   1.00 52.05  ? 776 HOH A O   1 
HETATM 13917 O O   . HOH I 3 .   ? 20.792  15.369  5.259   1.00 48.55  ? 777 HOH A O   1 
HETATM 13918 O O   . HOH I 3 .   ? 36.386  6.738   15.665  1.00 35.69  ? 778 HOH A O   1 
HETATM 13919 O O   . HOH I 3 .   ? -4.012  24.981  -13.352 1.00 44.99  ? 779 HOH A O   1 
HETATM 13920 O O   . HOH I 3 .   ? 16.879  1.033   4.013   1.00 49.97  ? 780 HOH A O   1 
HETATM 13921 O O   . HOH I 3 .   ? 3.201   4.812   -2.982  1.00 47.82  ? 781 HOH A O   1 
HETATM 13922 O O   . HOH I 3 .   ? 40.423  10.760  11.533  1.00 29.73  ? 782 HOH A O   1 
HETATM 13923 O O   . HOH I 3 .   ? 28.024  14.146  28.563  1.00 36.87  ? 783 HOH A O   1 
HETATM 13924 O O   . HOH I 3 .   ? 7.850   -2.913  -2.575  1.00 38.82  ? 784 HOH A O   1 
HETATM 13925 O O   . HOH I 3 .   ? 9.431   -4.100  5.364   1.00 44.98  ? 785 HOH A O   1 
HETATM 13926 O O   . HOH I 3 .   ? -0.473  -0.324  10.126  1.00 37.11  ? 786 HOH A O   1 
HETATM 13927 O O   . HOH I 3 .   ? 16.244  -8.233  0.076   1.00 50.25  ? 787 HOH A O   1 
HETATM 13928 O O   . HOH I 3 .   ? -11.219 15.613  -9.463  1.00 54.14  ? 788 HOH A O   1 
HETATM 13929 O O   . HOH I 3 .   ? 4.250   23.992  16.907  1.00 37.15  ? 789 HOH A O   1 
HETATM 13930 O O   . HOH I 3 .   ? 22.410  27.501  8.153   1.00 41.41  ? 790 HOH A O   1 
HETATM 13931 O O   . HOH I 3 .   ? -1.678  19.087  12.404  1.00 43.71  ? 791 HOH A O   1 
HETATM 13932 O O   . HOH I 3 .   ? -19.181 18.424  -0.666  1.00 39.49  ? 792 HOH A O   1 
HETATM 13933 O O   . HOH I 3 .   ? 18.921  -5.074  -12.634 1.00 44.95  ? 793 HOH A O   1 
HETATM 13934 O O   . HOH I 3 .   ? 18.505  10.568  24.055  1.00 22.61  ? 794 HOH A O   1 
HETATM 13935 O O   . HOH I 3 .   ? 1.531   -15.538 -3.272  1.00 48.03  ? 795 HOH A O   1 
HETATM 13936 O O   . HOH I 3 .   ? 25.252  -11.346 15.922  1.00 35.40  ? 796 HOH A O   1 
HETATM 13937 O O   . HOH I 3 .   ? 33.919  16.320  7.658   1.00 36.16  ? 797 HOH A O   1 
HETATM 13938 O O   . HOH I 3 .   ? -2.517  14.062  41.793  1.00 34.46  ? 798 HOH A O   1 
HETATM 13939 O O   . HOH I 3 .   ? 38.493  14.465  10.833  1.00 36.17  ? 799 HOH A O   1 
HETATM 13940 O O   . HOH I 3 .   ? 39.476  19.123  17.517  1.00 41.95  ? 800 HOH A O   1 
HETATM 13941 O O   . HOH I 3 .   ? -4.275  1.158   7.180   1.00 31.91  ? 801 HOH A O   1 
HETATM 13942 O O   . HOH I 3 .   ? -15.772 26.907  -14.490 1.00 39.39  ? 802 HOH A O   1 
HETATM 13943 O O   . HOH I 3 .   ? 13.080  2.935   0.910   1.00 64.27  ? 803 HOH A O   1 
HETATM 13944 O O   . HOH I 3 .   ? 33.880  -2.111  10.134  1.00 44.91  ? 804 HOH A O   1 
HETATM 13945 O O   . HOH I 3 .   ? -11.393 27.608  -15.667 1.00 35.48  ? 805 HOH A O   1 
HETATM 13946 O O   . HOH I 3 .   ? 18.746  24.798  10.782  1.00 31.70  ? 806 HOH A O   1 
HETATM 13947 O O   . HOH I 3 .   ? 3.055   32.138  11.673  1.00 38.20  ? 807 HOH A O   1 
HETATM 13948 O O   . HOH I 3 .   ? 33.802  15.428  -7.665  1.00 41.07  ? 808 HOH A O   1 
HETATM 13949 O O   . HOH I 3 .   ? -10.518 28.341  47.932  1.00 37.87  ? 809 HOH A O   1 
HETATM 13950 O O   . HOH I 3 .   ? -3.905  15.754  13.725  1.00 25.29  ? 810 HOH A O   1 
HETATM 13951 O O   . HOH I 3 .   ? 21.775  6.351   34.845  1.00 27.27  ? 811 HOH A O   1 
HETATM 13952 O O   . HOH J 3 .   ? 12.494  -3.754  47.520  1.00 57.13  ? 601 HOH B O   1 
HETATM 13953 O O   . HOH J 3 .   ? 36.506  -2.774  38.469  1.00 27.22  ? 602 HOH B O   1 
HETATM 13954 O O   . HOH J 3 .   ? -1.996  -22.664 26.159  1.00 44.79  ? 603 HOH B O   1 
HETATM 13955 O O   . HOH J 3 .   ? 4.398   -15.224 49.495  1.00 47.24  ? 604 HOH B O   1 
HETATM 13956 O O   . HOH J 3 .   ? -14.556 10.487  33.307  1.00 39.07  ? 605 HOH B O   1 
HETATM 13957 O O   . HOH J 3 .   ? 11.957  0.319   52.107  1.00 41.16  ? 606 HOH B O   1 
HETATM 13958 O O   . HOH J 3 .   ? -2.428  -11.468 45.588  1.00 51.39  ? 607 HOH B O   1 
HETATM 13959 O O   . HOH J 3 .   ? 38.448  -11.364 39.621  1.00 40.46  ? 608 HOH B O   1 
HETATM 13960 O O   . HOH J 3 .   ? 10.990  14.832  35.195  1.00 22.85  ? 609 HOH B O   1 
HETATM 13961 O O   . HOH J 3 .   ? -4.868  -22.174 34.506  1.00 24.49  ? 610 HOH B O   1 
HETATM 13962 O O   . HOH J 3 .   ? -8.559  3.264   32.114  1.00 41.28  ? 611 HOH B O   1 
HETATM 13963 O O   . HOH J 3 .   ? 6.688   -11.958 17.486  1.00 52.84  ? 612 HOH B O   1 
HETATM 13964 O O   . HOH J 3 .   ? 11.938  14.667  41.664  1.00 37.13  ? 613 HOH B O   1 
HETATM 13965 O O   . HOH J 3 .   ? -6.314  -13.421 30.102  1.00 40.55  ? 614 HOH B O   1 
HETATM 13966 O O   . HOH J 3 .   ? -11.976 -2.188  49.827  1.00 35.53  ? 615 HOH B O   1 
HETATM 13967 O O   . HOH J 3 .   ? 0.558   -19.649 26.399  1.00 34.06  ? 616 HOH B O   1 
HETATM 13968 O O   . HOH J 3 .   ? 7.410   -1.466  39.150  1.00 53.72  ? 617 HOH B O   1 
HETATM 13969 O O   . HOH J 3 .   ? -17.137 -5.015  28.567  1.00 33.35  ? 618 HOH B O   1 
HETATM 13970 O O   . HOH J 3 .   ? -17.282 22.094  30.289  1.00 41.79  ? 619 HOH B O   1 
HETATM 13971 O O   . HOH J 3 .   ? -0.149  31.755  29.063  1.00 36.19  ? 620 HOH B O   1 
HETATM 13972 O O   . HOH J 3 .   ? 26.449  10.505  51.407  1.00 53.35  ? 621 HOH B O   1 
HETATM 13973 O O   . HOH J 3 .   ? -4.505  -12.738 46.948  1.00 27.72  ? 622 HOH B O   1 
HETATM 13974 O O   . HOH J 3 .   ? 9.108   3.213   51.125  1.00 48.68  ? 623 HOH B O   1 
HETATM 13975 O O   . HOH J 3 .   ? -20.942 -2.725  35.748  1.00 28.17  ? 624 HOH B O   1 
HETATM 13976 O O   . HOH J 3 .   ? -17.442 -5.367  25.815  1.00 39.78  ? 625 HOH B O   1 
HETATM 13977 O O   . HOH J 3 .   ? 11.058  -5.244  38.340  1.00 25.43  ? 626 HOH B O   1 
HETATM 13978 O O   . HOH J 3 .   ? 16.690  -13.765 46.151  1.00 45.37  ? 627 HOH B O   1 
HETATM 13979 O O   . HOH J 3 .   ? 0.040   11.676  35.964  1.00 23.45  ? 628 HOH B O   1 
HETATM 13980 O O   . HOH J 3 .   ? -9.832  -7.588  33.539  1.00 52.17  ? 629 HOH B O   1 
HETATM 13981 O O   . HOH J 3 .   ? -18.061 17.070  35.306  1.00 34.91  ? 630 HOH B O   1 
HETATM 13982 O O   . HOH J 3 .   ? 16.667  -15.657 24.375  1.00 26.68  ? 631 HOH B O   1 
HETATM 13983 O O   . HOH J 3 .   ? -7.955  15.102  19.291  1.00 32.53  ? 632 HOH B O   1 
HETATM 13984 O O   . HOH J 3 .   ? -8.725  -14.653 35.007  1.00 26.62  ? 633 HOH B O   1 
HETATM 13985 O O   . HOH J 3 .   ? 19.261  -3.358  47.119  1.00 26.87  ? 634 HOH B O   1 
HETATM 13986 O O   . HOH J 3 .   ? -14.081 -3.518  47.573  1.00 32.89  ? 635 HOH B O   1 
HETATM 13987 O O   . HOH J 3 .   ? 24.429  -12.654 51.494  1.00 31.13  ? 636 HOH B O   1 
HETATM 13988 O O   . HOH J 3 .   ? 7.136   -1.810  53.435  1.00 50.66  ? 637 HOH B O   1 
HETATM 13989 O O   . HOH J 3 .   ? -0.879  4.887   27.421  1.00 23.21  ? 638 HOH B O   1 
HETATM 13990 O O   . HOH J 3 .   ? -0.321  18.557  18.731  1.00 34.78  ? 639 HOH B O   1 
HETATM 13991 O O   . HOH J 3 .   ? -25.290 -10.613 34.849  1.00 33.97  ? 640 HOH B O   1 
HETATM 13992 O O   . HOH J 3 .   ? 2.901   4.214   33.739  1.00 22.03  ? 641 HOH B O   1 
HETATM 13993 O O   . HOH J 3 .   ? -20.114 -2.011  23.689  1.00 36.94  ? 642 HOH B O   1 
HETATM 13994 O O   . HOH J 3 .   ? -9.723  8.182   42.769  1.00 37.38  ? 643 HOH B O   1 
HETATM 13995 O O   . HOH J 3 .   ? -11.373 10.955  20.689  1.00 32.39  ? 644 HOH B O   1 
HETATM 13996 O O   . HOH J 3 .   ? 4.573   0.642   38.719  1.00 20.76  ? 645 HOH B O   1 
HETATM 13997 O O   . HOH J 3 .   ? 38.446  -6.378  47.618  1.00 37.31  ? 646 HOH B O   1 
HETATM 13998 O O   . HOH J 3 .   ? 36.857  -1.345  43.529  1.00 28.89  ? 647 HOH B O   1 
HETATM 13999 O O   . HOH J 3 .   ? 19.795  24.580  35.442  1.00 48.17  ? 648 HOH B O   1 
HETATM 14000 O O   . HOH J 3 .   ? 26.077  8.971   41.951  1.00 29.16  ? 649 HOH B O   1 
HETATM 14001 O O   . HOH J 3 .   ? 13.008  23.768  15.464  1.00 42.44  ? 650 HOH B O   1 
HETATM 14002 O O   . HOH J 3 .   ? 21.229  -13.644 39.947  1.00 73.25  ? 651 HOH B O   1 
HETATM 14003 O O   . HOH J 3 .   ? 18.888  -3.253  54.274  1.00 36.30  ? 652 HOH B O   1 
HETATM 14004 O O   . HOH J 3 .   ? 14.392  -9.423  30.870  1.00 29.84  ? 653 HOH B O   1 
HETATM 14005 O O   . HOH J 3 .   ? -9.414  -9.589  34.881  1.00 51.98  ? 654 HOH B O   1 
HETATM 14006 O O   . HOH J 3 .   ? -2.109  7.453   26.263  1.00 16.51  ? 655 HOH B O   1 
HETATM 14007 O O   . HOH J 3 .   ? -10.120 15.928  41.401  1.00 30.05  ? 656 HOH B O   1 
HETATM 14008 O O   . HOH J 3 .   ? 3.971   -1.677  51.209  1.00 34.28  ? 657 HOH B O   1 
HETATM 14009 O O   . HOH J 3 .   ? 16.903  -18.780 41.148  1.00 58.06  ? 658 HOH B O   1 
HETATM 14010 O O   . HOH J 3 .   ? -9.425  9.489   20.762  1.00 60.83  ? 659 HOH B O   1 
HETATM 14011 O O   . HOH J 3 .   ? -4.999  -20.845 18.812  1.00 41.43  ? 660 HOH B O   1 
HETATM 14012 O O   . HOH J 3 .   ? 19.391  -15.871 34.181  1.00 39.87  ? 661 HOH B O   1 
HETATM 14013 O O   . HOH J 3 .   ? -4.446  13.326  33.205  1.00 53.46  ? 662 HOH B O   1 
HETATM 14014 O O   . HOH J 3 .   ? 14.124  5.601   44.559  1.00 33.30  ? 663 HOH B O   1 
HETATM 14015 O O   . HOH J 3 .   ? 2.662   -20.973 41.432  1.00 26.55  ? 664 HOH B O   1 
HETATM 14016 O O   . HOH J 3 .   ? 5.094   21.844  18.601  1.00 26.08  ? 665 HOH B O   1 
HETATM 14017 O O   . HOH J 3 .   ? 37.799  -12.674 42.206  1.00 36.20  ? 666 HOH B O   1 
HETATM 14018 O O   . HOH J 3 .   ? 1.202   14.303  24.800  1.00 30.96  ? 667 HOH B O   1 
HETATM 14019 O O   . HOH J 3 .   ? 15.059  16.514  26.352  1.00 27.80  ? 668 HOH B O   1 
HETATM 14020 O O   . HOH J 3 .   ? 13.668  4.302   33.539  1.00 23.70  ? 669 HOH B O   1 
HETATM 14021 O O   . HOH J 3 .   ? 0.181   -21.708 39.623  1.00 23.92  ? 670 HOH B O   1 
HETATM 14022 O O   . HOH J 3 .   ? 20.262  -0.824  34.564  1.00 27.42  ? 671 HOH B O   1 
HETATM 14023 O O   . HOH J 3 .   ? 12.496  -8.140  50.947  1.00 51.98  ? 672 HOH B O   1 
HETATM 14024 O O   . HOH J 3 .   ? -7.874  -6.319  43.396  1.00 21.23  ? 673 HOH B O   1 
HETATM 14025 O O   . HOH J 3 .   ? 11.862  -25.573 23.335  1.00 56.81  ? 674 HOH B O   1 
HETATM 14026 O O   . HOH J 3 .   ? 33.667  4.283   49.512  1.00 35.09  ? 675 HOH B O   1 
HETATM 14027 O O   . HOH J 3 .   ? 21.827  -10.066 45.917  1.00 43.05  ? 676 HOH B O   1 
HETATM 14028 O O   . HOH J 3 .   ? -14.946 10.791  36.472  1.00 43.55  ? 677 HOH B O   1 
HETATM 14029 O O   . HOH J 3 .   ? -5.484  -18.690 44.745  1.00 43.68  ? 678 HOH B O   1 
HETATM 14030 O O   . HOH J 3 .   ? -4.239  -4.631  42.596  1.00 38.62  ? 679 HOH B O   1 
HETATM 14031 O O   . HOH J 3 .   ? -9.239  29.660  36.303  1.00 55.83  ? 680 HOH B O   1 
HETATM 14032 O O   . HOH J 3 .   ? 14.356  -3.894  50.034  1.00 37.51  ? 681 HOH B O   1 
HETATM 14033 O O   . HOH J 3 .   ? 14.730  37.589  23.669  1.00 40.78  ? 682 HOH B O   1 
HETATM 14034 O O   . HOH J 3 .   ? -8.243  8.389   45.831  1.00 42.08  ? 683 HOH B O   1 
HETATM 14035 O O   . HOH J 3 .   ? -20.365 -4.370  42.426  1.00 30.24  ? 684 HOH B O   1 
HETATM 14036 O O   . HOH J 3 .   ? 11.341  -9.839  36.944  1.00 54.54  ? 685 HOH B O   1 
HETATM 14037 O O   . HOH J 3 .   ? 2.665   -11.811 29.247  1.00 49.83  ? 686 HOH B O   1 
HETATM 14038 O O   . HOH J 3 .   ? -12.233 -15.971 36.657  1.00 30.95  ? 687 HOH B O   1 
HETATM 14039 O O   . HOH J 3 .   ? 28.533  2.944   51.763  1.00 32.17  ? 688 HOH B O   1 
HETATM 14040 O O   . HOH J 3 .   ? 15.869  -23.027 32.997  1.00 28.47  ? 689 HOH B O   1 
HETATM 14041 O O   . HOH J 3 .   ? -8.641  -7.066  19.532  1.00 27.76  ? 690 HOH B O   1 
HETATM 14042 O O   . HOH J 3 .   ? 7.637   -4.658  17.130  1.00 27.10  ? 691 HOH B O   1 
HETATM 14043 O O   . HOH J 3 .   ? 0.613   11.173  43.589  1.00 34.87  ? 692 HOH B O   1 
HETATM 14044 O O   . HOH J 3 .   ? 13.890  6.489   51.483  1.00 28.38  ? 693 HOH B O   1 
HETATM 14045 O O   . HOH J 3 .   ? -2.319  -6.940  50.918  1.00 31.90  ? 694 HOH B O   1 
HETATM 14046 O O   . HOH J 3 .   ? 9.215   -16.678 13.775  1.00 28.50  ? 695 HOH B O   1 
HETATM 14047 O O   . HOH J 3 .   ? 16.028  -8.042  58.632  1.00 47.85  ? 696 HOH B O   1 
HETATM 14048 O O   . HOH J 3 .   ? 22.632  -0.255  36.005  1.00 33.06  ? 697 HOH B O   1 
HETATM 14049 O O   . HOH J 3 .   ? -3.066  1.067   14.235  1.00 27.17  ? 698 HOH B O   1 
HETATM 14050 O O   . HOH J 3 .   ? -1.382  13.675  23.699  1.00 22.28  ? 699 HOH B O   1 
HETATM 14051 O O   . HOH J 3 .   ? -13.066 18.198  27.243  1.00 34.15  ? 700 HOH B O   1 
HETATM 14052 O O   . HOH J 3 .   ? -3.826  -16.311 12.432  1.00 36.88  ? 701 HOH B O   1 
HETATM 14053 O O   . HOH J 3 .   ? -4.404  9.574   39.435  1.00 25.38  ? 702 HOH B O   1 
HETATM 14054 O O   . HOH J 3 .   ? 9.850   12.379  51.042  1.00 35.82  ? 703 HOH B O   1 
HETATM 14055 O O   . HOH J 3 .   ? 13.501  1.427   35.033  1.00 34.28  ? 704 HOH B O   1 
HETATM 14056 O O   . HOH J 3 .   ? 0.800   -8.265  34.699  1.00 34.49  ? 705 HOH B O   1 
HETATM 14057 O O   . HOH J 3 .   ? -24.674 -3.074  32.932  1.00 36.71  ? 706 HOH B O   1 
HETATM 14058 O O   . HOH J 3 .   ? 26.333  6.576   38.845  1.00 28.35  ? 707 HOH B O   1 
HETATM 14059 O O   . HOH J 3 .   ? 16.733  -15.429 45.308  1.00 22.27  ? 708 HOH B O   1 
HETATM 14060 O O   . HOH J 3 .   ? -13.608 3.965   45.497  1.00 31.07  ? 709 HOH B O   1 
HETATM 14061 O O   . HOH J 3 .   ? -10.907 10.342  29.278  1.00 47.97  ? 710 HOH B O   1 
HETATM 14062 O O   . HOH J 3 .   ? 15.323  0.667   36.122  1.00 24.85  ? 711 HOH B O   1 
HETATM 14063 O O   . HOH J 3 .   ? 8.301   -7.205  40.551  1.00 38.95  ? 712 HOH B O   1 
HETATM 14064 O O   . HOH J 3 .   ? 2.723   3.916   47.064  1.00 22.19  ? 713 HOH B O   1 
HETATM 14065 O O   . HOH J 3 .   ? 17.743  -10.659 21.115  1.00 28.65  ? 714 HOH B O   1 
HETATM 14066 O O   . HOH J 3 .   ? -13.109 -7.723  20.819  1.00 41.46  ? 715 HOH B O   1 
HETATM 14067 O O   . HOH J 3 .   ? 17.125  -4.844  25.323  1.00 21.71  ? 716 HOH B O   1 
HETATM 14068 O O   . HOH J 3 .   ? -5.170  31.077  37.091  1.00 50.91  ? 717 HOH B O   1 
HETATM 14069 O O   . HOH J 3 .   ? 12.660  -3.542  22.673  1.00 44.43  ? 718 HOH B O   1 
HETATM 14070 O O   . HOH J 3 .   ? -18.644 21.458  26.036  1.00 38.76  ? 719 HOH B O   1 
HETATM 14071 O O   . HOH J 3 .   ? 19.517  -4.966  44.593  1.00 30.63  ? 720 HOH B O   1 
HETATM 14072 O O   . HOH J 3 .   ? 5.813   -2.936  46.354  1.00 39.80  ? 721 HOH B O   1 
HETATM 14073 O O   . HOH J 3 .   ? 22.191  -6.177  32.175  1.00 33.48  ? 722 HOH B O   1 
HETATM 14074 O O   . HOH J 3 .   ? -5.213  2.690   13.945  1.00 22.10  ? 723 HOH B O   1 
HETATM 14075 O O   . HOH J 3 .   ? -4.769  11.871  18.810  1.00 18.30  ? 724 HOH B O   1 
HETATM 14076 O O   . HOH J 3 .   ? 40.081  -0.355  54.434  1.00 31.03  ? 725 HOH B O   1 
HETATM 14077 O O   . HOH J 3 .   ? 13.394  6.969   36.474  1.00 24.51  ? 726 HOH B O   1 
HETATM 14078 O O   . HOH J 3 .   ? 6.186   -23.953 41.890  1.00 32.01  ? 727 HOH B O   1 
HETATM 14079 O O   . HOH J 3 .   ? -15.660 16.159  37.001  1.00 36.84  ? 728 HOH B O   1 
HETATM 14080 O O   . HOH J 3 .   ? 15.464  12.705  33.244  1.00 31.86  ? 729 HOH B O   1 
HETATM 14081 O O   . HOH J 3 .   ? 11.369  -5.337  23.149  1.00 22.13  ? 730 HOH B O   1 
HETATM 14082 O O   . HOH J 3 .   ? 21.733  -8.441  54.878  1.00 33.50  ? 731 HOH B O   1 
HETATM 14083 O O   . HOH J 3 .   ? 13.268  -19.189 12.444  1.00 37.38  ? 732 HOH B O   1 
HETATM 14084 O O   . HOH J 3 .   ? 2.516   -23.138 14.340  1.00 45.49  ? 733 HOH B O   1 
HETATM 14085 O O   . HOH J 3 .   ? 0.930   -14.155 50.353  1.00 33.82  ? 734 HOH B O   1 
HETATM 14086 O O   . HOH J 3 .   ? 14.845  4.551   37.309  1.00 30.39  ? 735 HOH B O   1 
HETATM 14087 O O   . HOH J 3 .   ? 19.988  -8.327  27.605  1.00 27.81  ? 736 HOH B O   1 
HETATM 14088 O O   . HOH J 3 .   ? 14.604  -12.619 47.510  1.00 36.82  ? 737 HOH B O   1 
HETATM 14089 O O   . HOH J 3 .   ? -3.549  -15.847 27.834  1.00 35.87  ? 738 HOH B O   1 
HETATM 14090 O O   . HOH J 3 .   ? -13.497 21.712  36.183  1.00 34.25  ? 739 HOH B O   1 
HETATM 14091 O O   . HOH J 3 .   ? -3.318  -15.736 32.511  1.00 31.47  ? 740 HOH B O   1 
HETATM 14092 O O   . HOH J 3 .   ? 7.902   -21.877 43.398  1.00 27.71  ? 741 HOH B O   1 
HETATM 14093 O O   . HOH J 3 .   ? 4.072   -27.820 36.743  1.00 34.37  ? 742 HOH B O   1 
HETATM 14094 O O   . HOH J 3 .   ? 4.026   -6.528  50.547  1.00 34.37  ? 743 HOH B O   1 
HETATM 14095 O O   . HOH J 3 .   ? 19.634  -3.109  42.864  1.00 55.72  ? 744 HOH B O   1 
HETATM 14096 O O   . HOH J 3 .   ? 11.497  5.695   32.618  1.00 19.95  ? 745 HOH B O   1 
HETATM 14097 O O   . HOH J 3 .   ? -16.561 -6.039  47.791  1.00 29.52  ? 746 HOH B O   1 
HETATM 14098 O O   . HOH J 3 .   ? -15.333 -17.076 40.015  1.00 44.20  ? 747 HOH B O   1 
HETATM 14099 O O   . HOH J 3 .   ? 16.318  -19.993 47.370  1.00 39.47  ? 748 HOH B O   1 
HETATM 14100 O O   . HOH J 3 .   ? -1.096  14.280  27.670  1.00 22.23  ? 749 HOH B O   1 
HETATM 14101 O O   . HOH J 3 .   ? 17.233  24.625  16.299  1.00 28.42  ? 750 HOH B O   1 
HETATM 14102 O O   . HOH J 3 .   ? 23.264  30.721  10.530  1.00 45.89  ? 751 HOH B O   1 
HETATM 14103 O O   . HOH J 3 .   ? -12.380 15.825  26.410  1.00 30.09  ? 752 HOH B O   1 
HETATM 14104 O O   . HOH J 3 .   ? 18.642  15.386  33.394  1.00 34.01  ? 753 HOH B O   1 
HETATM 14105 O O   . HOH J 3 .   ? 32.555  3.928   53.000  1.00 43.35  ? 754 HOH B O   1 
HETATM 14106 O O   . HOH J 3 .   ? -11.365 16.896  35.566  1.00 49.21  ? 755 HOH B O   1 
HETATM 14107 O O   . HOH J 3 .   ? 6.684   4.704   43.489  1.00 21.57  ? 756 HOH B O   1 
HETATM 14108 O O   . HOH J 3 .   ? -19.973 -4.554  26.426  1.00 33.09  ? 757 HOH B O   1 
HETATM 14109 O O   . HOH J 3 .   ? -4.017  15.666  16.763  1.00 19.76  ? 758 HOH B O   1 
HETATM 14110 O O   . HOH J 3 .   ? -13.396 8.479   22.050  1.00 21.19  ? 759 HOH B O   1 
HETATM 14111 O O   . HOH J 3 .   ? 23.869  21.961  16.299  1.00 30.91  ? 760 HOH B O   1 
HETATM 14112 O O   . HOH J 3 .   ? 13.959  -17.752 54.397  1.00 40.78  ? 761 HOH B O   1 
HETATM 14113 O O   . HOH J 3 .   ? 6.448   -6.790  46.674  1.00 40.74  ? 762 HOH B O   1 
HETATM 14114 O O   . HOH J 3 .   ? -2.805  9.423   41.699  1.00 24.75  ? 763 HOH B O   1 
HETATM 14115 O O   . HOH J 3 .   ? -10.370 -1.128  34.270  1.00 42.62  ? 764 HOH B O   1 
HETATM 14116 O O   . HOH J 3 .   ? 16.463  -16.250 31.442  1.00 41.41  ? 765 HOH B O   1 
HETATM 14117 O O   . HOH J 3 .   ? 3.553   -15.621 11.418  1.00 28.19  ? 766 HOH B O   1 
HETATM 14118 O O   . HOH J 3 .   ? 17.794  4.308   35.046  1.00 28.59  ? 767 HOH B O   1 
HETATM 14119 O O   . HOH J 3 .   ? -16.970 -11.811 32.335  1.00 30.49  ? 768 HOH B O   1 
HETATM 14120 O O   . HOH J 3 .   ? -14.986 -1.033  46.742  1.00 40.11  ? 769 HOH B O   1 
HETATM 14121 O O   . HOH J 3 .   ? -8.620  12.495  16.122  1.00 34.64  ? 770 HOH B O   1 
HETATM 14122 O O   . HOH J 3 .   ? 26.057  0.490   32.848  1.00 34.07  ? 771 HOH B O   1 
HETATM 14123 O O   . HOH J 3 .   ? -8.954  16.870  26.752  1.00 27.42  ? 772 HOH B O   1 
HETATM 14124 O O   . HOH J 3 .   ? 21.493  -3.739  42.647  1.00 27.55  ? 773 HOH B O   1 
HETATM 14125 O O   . HOH J 3 .   ? 8.064   -1.959  18.980  1.00 39.24  ? 774 HOH B O   1 
HETATM 14126 O O   . HOH J 3 .   ? 0.282   0.808   24.953  1.00 86.28  ? 775 HOH B O   1 
HETATM 14127 O O   . HOH J 3 .   ? -6.902  -7.906  52.942  1.00 40.47  ? 776 HOH B O   1 
HETATM 14128 O O   . HOH J 3 .   ? -12.533 -1.569  17.778  1.00 37.61  ? 777 HOH B O   1 
HETATM 14129 O O   . HOH J 3 .   ? -2.160  -11.811 16.018  1.00 39.61  ? 778 HOH B O   1 
HETATM 14130 O O   . HOH J 3 .   ? 16.131  16.341  38.929  1.00 49.45  ? 779 HOH B O   1 
HETATM 14131 O O   . HOH J 3 .   ? 14.657  -26.840 31.599  1.00 37.82  ? 780 HOH B O   1 
HETATM 14132 O O   . HOH J 3 .   ? -4.236  -18.244 23.991  1.00 56.83  ? 781 HOH B O   1 
HETATM 14133 O O   . HOH J 3 .   ? -4.829  -6.211  54.405  1.00 42.00  ? 782 HOH B O   1 
HETATM 14134 O O   . HOH J 3 .   ? 12.114  -19.371 21.378  1.00 28.26  ? 783 HOH B O   1 
HETATM 14135 O O   . HOH J 3 .   ? 5.968   -14.360 17.607  1.00 53.21  ? 784 HOH B O   1 
HETATM 14136 O O   . HOH J 3 .   ? 22.646  9.947   45.917  1.00 73.39  ? 785 HOH B O   1 
HETATM 14137 O O   . HOH J 3 .   ? -2.390  35.335  26.173  1.00 41.71  ? 786 HOH B O   1 
HETATM 14138 O O   . HOH J 3 .   ? 24.622  7.631   37.205  1.00 37.13  ? 787 HOH B O   1 
HETATM 14139 O O   . HOH J 3 .   ? -4.479  -10.149 18.730  1.00 50.43  ? 788 HOH B O   1 
HETATM 14140 O O   . HOH J 3 .   ? 5.025   0.240   50.186  1.00 31.82  ? 789 HOH B O   1 
HETATM 14141 O O   . HOH J 3 .   ? 6.624   19.394  28.992  1.00 52.95  ? 790 HOH B O   1 
HETATM 14142 O O   . HOH J 3 .   ? -12.918 -6.451  13.418  1.00 51.37  ? 791 HOH B O   1 
HETATM 14143 O O   . HOH J 3 .   ? 18.130  16.632  37.478  1.00 44.38  ? 792 HOH B O   1 
HETATM 14144 O O   . HOH J 3 .   ? -7.031  -1.670  9.288   1.00 49.45  ? 793 HOH B O   1 
HETATM 14145 O O   . HOH J 3 .   ? 19.737  30.147  12.329  1.00 42.23  ? 794 HOH B O   1 
HETATM 14146 O O   . HOH J 3 .   ? -5.986  2.425   11.147  1.00 29.56  ? 795 HOH B O   1 
HETATM 14147 O O   . HOH J 3 .   ? -15.264 10.143  23.362  1.00 33.84  ? 796 HOH B O   1 
HETATM 14148 O O   . HOH J 3 .   ? 7.462   22.565  17.463  1.00 45.41  ? 797 HOH B O   1 
HETATM 14149 O O   . HOH J 3 .   ? 26.533  -6.443  42.642  1.00 51.19  ? 798 HOH B O   1 
HETATM 14150 O O   . HOH J 3 .   ? -14.110 20.554  39.249  1.00 49.12  ? 799 HOH B O   1 
HETATM 14151 O O   . HOH J 3 .   ? -0.735  -12.710 54.979  1.00 58.56  ? 800 HOH B O   1 
HETATM 14152 O O   . HOH J 3 .   ? 18.361  -13.717 25.321  1.00 49.35  ? 801 HOH B O   1 
HETATM 14153 O O   . HOH J 3 .   ? -6.531  -15.164 33.050  1.00 30.47  ? 802 HOH B O   1 
HETATM 14154 O O   . HOH J 3 .   ? -8.031  11.245  20.741  1.00 26.38  ? 803 HOH B O   1 
HETATM 14155 O O   . HOH J 3 .   ? 25.764  -1.093  55.664  1.00 52.33  ? 804 HOH B O   1 
HETATM 14156 O O   . HOH J 3 .   ? -11.656 23.923  38.383  1.00 60.65  ? 805 HOH B O   1 
HETATM 14157 O O   . HOH J 3 .   ? -2.760  10.955  23.843  1.00 25.87  ? 806 HOH B O   1 
HETATM 14158 O O   . HOH J 3 .   ? 3.707   18.633  38.731  1.00 43.67  ? 807 HOH B O   1 
HETATM 14159 O O   . HOH J 3 .   ? 19.767  -11.602 25.043  1.00 36.10  ? 808 HOH B O   1 
HETATM 14160 O O   . HOH J 3 .   ? -6.570  -19.558 11.859  1.00 36.69  ? 809 HOH B O   1 
HETATM 14161 O O   . HOH J 3 .   ? 6.109   -12.499 26.431  1.00 52.98  ? 810 HOH B O   1 
HETATM 14162 O O   . HOH J 3 .   ? 1.273   -1.308  43.384  1.00 36.82  ? 811 HOH B O   1 
HETATM 14163 O O   . HOH J 3 .   ? -10.847 28.607  25.713  1.00 39.62  ? 812 HOH B O   1 
HETATM 14164 O O   . HOH J 3 .   ? -6.345  -19.792 14.658  1.00 35.98  ? 813 HOH B O   1 
HETATM 14165 O O   . HOH J 3 .   ? 15.966  -6.743  24.869  1.00 30.20  ? 814 HOH B O   1 
HETATM 14166 O O   . HOH J 3 .   ? 19.832  10.672  34.457  1.00 40.27  ? 815 HOH B O   1 
HETATM 14167 O O   . HOH J 3 .   ? 5.726   -10.303 56.637  1.00 61.05  ? 816 HOH B O   1 
HETATM 14168 O O   . HOH J 3 .   ? 9.301   26.121  17.491  1.00 45.97  ? 817 HOH B O   1 
HETATM 14169 O O   . HOH J 3 .   ? -3.258  -1.768  10.545  1.00 27.93  ? 818 HOH B O   1 
HETATM 14170 O O   . HOH J 3 .   ? -3.802  15.038  28.193  1.00 41.75  ? 819 HOH B O   1 
HETATM 14171 O O   . HOH J 3 .   ? 1.729   13.867  43.749  1.00 38.39  ? 820 HOH B O   1 
HETATM 14172 O O   . HOH J 3 .   ? 14.080  17.194  38.556  1.00 35.08  ? 821 HOH B O   1 
HETATM 14173 O O   . HOH J 3 .   ? -7.550  -4.790  34.235  1.00 37.38  ? 822 HOH B O   1 
HETATM 14174 O O   . HOH J 3 .   ? -3.111  -18.631 27.438  1.00 36.04  ? 823 HOH B O   1 
HETATM 14175 O O   . HOH J 3 .   ? 1.673   -20.989 24.040  1.00 51.74  ? 824 HOH B O   1 
HETATM 14176 O O   . HOH J 3 .   ? -6.815  -4.365  31.842  1.00 39.34  ? 825 HOH B O   1 
HETATM 14177 O O   . HOH J 3 .   ? -3.059  -20.689 44.596  1.00 38.11  ? 826 HOH B O   1 
HETATM 14178 O O   . HOH J 3 .   ? -3.531  12.034  45.412  1.00 35.47  ? 827 HOH B O   1 
HETATM 14179 O O   . HOH J 3 .   ? 11.943  16.568  43.669  1.00 46.59  ? 828 HOH B O   1 
HETATM 14180 O O   . HOH J 3 .   ? -1.816  11.596  43.362  1.00 25.31  ? 829 HOH B O   1 
HETATM 14181 O O   . HOH J 3 .   ? 21.108  -6.596  44.181  1.00 62.60  ? 830 HOH B O   1 
HETATM 14182 O O   . HOH J 3 .   ? 13.962  -26.030 21.785  1.00 48.20  ? 831 HOH B O   1 
HETATM 14183 O O   . HOH J 3 .   ? 32.529  7.885   49.233  1.00 43.73  ? 832 HOH B O   1 
HETATM 14184 O O   . HOH J 3 .   ? 10.094  15.513  39.305  1.00 46.12  ? 833 HOH B O   1 
HETATM 14185 O O   . HOH J 3 .   ? 40.677  1.829   54.786  1.00 38.54  ? 834 HOH B O   1 
HETATM 14186 O O   . HOH J 3 .   ? 18.930  6.645   34.288  1.00 32.38  ? 835 HOH B O   1 
HETATM 14187 O O   . HOH J 3 .   ? -5.358  -17.022 9.277   1.00 43.41  ? 836 HOH B O   1 
HETATM 14188 O O   . HOH J 3 .   ? -13.434 -3.382  52.208  1.00 34.59  ? 837 HOH B O   1 
HETATM 14189 O O   . HOH J 3 .   ? 33.661  4.615   55.881  1.00 38.37  ? 838 HOH B O   1 
HETATM 14190 O O   . HOH J 3 .   ? 17.025  -27.978 32.022  1.00 34.27  ? 839 HOH B O   1 
HETATM 14191 O O   . HOH K 3 .   ? 20.162  39.753  57.099  1.00 54.38  ? 601 HOH C O   1 
HETATM 14192 O O   . HOH K 3 .   ? -1.119  58.750  60.905  1.00 44.32  ? 602 HOH C O   1 
HETATM 14193 O O   . HOH K 3 .   ? 30.676  41.923  55.408  1.00 38.03  ? 603 HOH C O   1 
HETATM 14194 O O   . HOH K 3 .   ? 18.824  68.038  40.053  1.00 47.83  ? 604 HOH C O   1 
HETATM 14195 O O   . HOH K 3 .   ? 16.502  36.654  49.479  1.00 59.46  ? 605 HOH C O   1 
HETATM 14196 O O   . HOH K 3 .   ? 2.363   41.218  54.187  1.00 61.09  ? 606 HOH C O   1 
HETATM 14197 O O   . HOH K 3 .   ? 0.798   66.881  29.733  1.00 41.68  ? 607 HOH C O   1 
HETATM 14198 O O   . HOH K 3 .   ? -0.450  33.780  58.117  1.00 34.46  ? 608 HOH C O   1 
HETATM 14199 O O   . HOH K 3 .   ? -7.345  49.366  37.833  1.00 34.86  ? 609 HOH C O   1 
HETATM 14200 O O   . HOH K 3 .   ? 0.953   67.896  49.100  1.00 42.41  ? 610 HOH C O   1 
HETATM 14201 O O   . HOH K 3 .   ? 36.373  30.328  42.783  1.00 36.86  ? 611 HOH C O   1 
HETATM 14202 O O   . HOH K 3 .   ? 24.043  71.363  39.207  1.00 26.58  ? 612 HOH C O   1 
HETATM 14203 O O   . HOH K 3 .   ? 25.774  42.750  68.382  1.00 38.93  ? 613 HOH C O   1 
HETATM 14204 O O   . HOH K 3 .   ? 27.868  42.207  46.551  1.00 33.89  ? 614 HOH C O   1 
HETATM 14205 O O   . HOH K 3 .   ? 11.006  47.145  45.871  1.00 55.79  ? 615 HOH C O   1 
HETATM 14206 O O   . HOH K 3 .   ? 1.825   58.475  65.442  1.00 37.18  ? 616 HOH C O   1 
HETATM 14207 O O   . HOH K 3 .   ? 17.044  30.582  57.646  1.00 45.22  ? 617 HOH C O   1 
HETATM 14208 O O   . HOH K 3 .   ? 28.714  58.146  31.120  1.00 40.94  ? 618 HOH C O   1 
HETATM 14209 O O   . HOH K 3 .   ? 3.687   42.872  63.199  1.00 31.15  ? 619 HOH C O   1 
HETATM 14210 O O   . HOH K 3 .   ? 16.358  46.791  46.753  1.00 22.12  ? 620 HOH C O   1 
HETATM 14211 O O   . HOH K 3 .   ? 38.643  40.122  20.257  1.00 51.70  ? 621 HOH C O   1 
HETATM 14212 O O   . HOH K 3 .   ? -0.767  39.600  38.448  1.00 30.53  ? 622 HOH C O   1 
HETATM 14213 O O   . HOH K 3 .   ? 24.808  60.525  29.414  1.00 48.49  ? 623 HOH C O   1 
HETATM 14214 O O   . HOH K 3 .   ? 27.273  46.589  47.035  1.00 27.79  ? 624 HOH C O   1 
HETATM 14215 O O   . HOH K 3 .   ? -7.445  47.414  33.965  1.00 33.62  ? 625 HOH C O   1 
HETATM 14216 O O   . HOH K 3 .   ? 31.192  58.194  46.444  1.00 27.60  ? 626 HOH C O   1 
HETATM 14217 O O   . HOH K 3 .   ? 17.694  76.834  47.793  1.00 31.17  ? 627 HOH C O   1 
HETATM 14218 O O   . HOH K 3 .   ? 8.877   54.446  31.493  1.00 22.60  ? 628 HOH C O   1 
HETATM 14219 O O   . HOH K 3 .   ? 2.171   51.782  60.936  1.00 34.66  ? 629 HOH C O   1 
HETATM 14220 O O   . HOH K 3 .   ? 21.180  33.718  54.938  1.00 33.02  ? 630 HOH C O   1 
HETATM 14221 O O   . HOH K 3 .   ? 31.530  40.523  30.906  1.00 25.09  ? 631 HOH C O   1 
HETATM 14222 O O   . HOH K 3 .   ? 21.457  66.300  23.205  1.00 35.84  ? 632 HOH C O   1 
HETATM 14223 O O   . HOH K 3 .   ? 24.925  39.745  49.209  1.00 40.55  ? 633 HOH C O   1 
HETATM 14224 O O   . HOH K 3 .   ? -0.373  44.734  54.844  1.00 44.70  ? 634 HOH C O   1 
HETATM 14225 O O   . HOH K 3 .   ? 18.161  65.060  31.591  1.00 46.19  ? 635 HOH C O   1 
HETATM 14226 O O   . HOH K 3 .   ? 3.346   54.120  52.641  1.00 45.63  ? 636 HOH C O   1 
HETATM 14227 O O   . HOH K 3 .   ? 8.562   39.528  46.737  1.00 31.37  ? 637 HOH C O   1 
HETATM 14228 O O   . HOH K 3 .   ? 12.145  74.896  40.789  1.00 43.80  ? 638 HOH C O   1 
HETATM 14229 O O   . HOH K 3 .   ? -3.467  44.367  37.770  1.00 34.93  ? 639 HOH C O   1 
HETATM 14230 O O   . HOH K 3 .   ? 14.983  45.077  22.707  1.00 37.17  ? 640 HOH C O   1 
HETATM 14231 O O   . HOH K 3 .   ? 31.740  58.430  40.196  1.00 32.67  ? 641 HOH C O   1 
HETATM 14232 O O   . HOH K 3 .   ? -5.933  42.951  59.310  1.00 39.63  ? 642 HOH C O   1 
HETATM 14233 O O   . HOH K 3 .   ? 24.611  48.862  36.557  1.00 23.17  ? 643 HOH C O   1 
HETATM 14234 O O   . HOH K 3 .   ? 32.325  62.124  28.383  1.00 38.70  ? 644 HOH C O   1 
HETATM 14235 O O   . HOH K 3 .   ? 10.531  42.489  27.025  1.00 42.75  ? 645 HOH C O   1 
HETATM 14236 O O   . HOH K 3 .   ? 18.186  45.516  40.760  1.00 19.91  ? 646 HOH C O   1 
HETATM 14237 O O   . HOH K 3 .   ? 30.929  66.904  39.552  1.00 29.33  ? 647 HOH C O   1 
HETATM 14238 O O   . HOH K 3 .   ? 10.868  63.291  58.002  1.00 22.94  ? 648 HOH C O   1 
HETATM 14239 O O   . HOH K 3 .   ? 8.576   49.555  25.725  1.00 26.23  ? 649 HOH C O   1 
HETATM 14240 O O   . HOH K 3 .   ? 7.590   64.946  60.903  1.00 24.94  ? 650 HOH C O   1 
HETATM 14241 O O   . HOH K 3 .   ? 11.375  51.473  56.796  1.00 17.36  ? 651 HOH C O   1 
HETATM 14242 O O   . HOH K 3 .   ? 29.737  62.121  24.561  1.00 39.08  ? 652 HOH C O   1 
HETATM 14243 O O   . HOH K 3 .   ? 8.648   77.075  44.180  1.00 35.05  ? 653 HOH C O   1 
HETATM 14244 O O   . HOH K 3 .   ? 27.300  30.631  79.134  1.00 39.70  ? 654 HOH C O   1 
HETATM 14245 O O   . HOH K 3 .   ? 30.443  44.739  73.923  1.00 27.94  ? 655 HOH C O   1 
HETATM 14246 O O   . HOH K 3 .   ? -3.557  59.842  45.223  1.00 32.03  ? 656 HOH C O   1 
HETATM 14247 O O   . HOH K 3 .   ? 10.148  37.834  44.946  1.00 27.90  ? 657 HOH C O   1 
HETATM 14248 O O   . HOH K 3 .   ? 31.229  52.763  33.415  1.00 58.11  ? 658 HOH C O   1 
HETATM 14249 O O   . HOH K 3 .   ? 2.372   46.006  26.109  1.00 35.67  ? 659 HOH C O   1 
HETATM 14250 O O   . HOH K 3 .   ? 5.604   65.314  48.478  1.00 25.35  ? 660 HOH C O   1 
HETATM 14251 O O   . HOH K 3 .   ? 4.622   35.439  24.921  1.00 43.33  ? 661 HOH C O   1 
HETATM 14252 O O   . HOH K 3 .   ? 26.561  37.297  39.642  1.00 26.41  ? 662 HOH C O   1 
HETATM 14253 O O   . HOH K 3 .   ? 2.791   37.929  51.657  1.00 33.06  ? 663 HOH C O   1 
HETATM 14254 O O   . HOH K 3 .   ? 16.927  41.351  27.720  1.00 30.74  ? 664 HOH C O   1 
HETATM 14255 O O   . HOH K 3 .   ? 13.319  40.050  50.774  1.00 24.85  ? 665 HOH C O   1 
HETATM 14256 O O   . HOH K 3 .   ? 15.790  53.774  16.899  1.00 31.78  ? 666 HOH C O   1 
HETATM 14257 O O   . HOH K 3 .   ? 38.363  42.384  19.018  1.00 38.02  ? 667 HOH C O   1 
HETATM 14258 O O   . HOH K 3 .   ? 23.732  35.884  29.918  1.00 31.97  ? 668 HOH C O   1 
HETATM 14259 O O   . HOH K 3 .   ? 20.004  60.320  33.666  1.00 44.86  ? 669 HOH C O   1 
HETATM 14260 O O   . HOH K 3 .   ? 7.939   38.326  22.556  1.00 47.42  ? 670 HOH C O   1 
HETATM 14261 O O   . HOH K 3 .   ? 11.315  49.959  54.263  1.00 20.54  ? 671 HOH C O   1 
HETATM 14262 O O   . HOH K 3 .   ? 31.442  44.290  60.161  1.00 30.51  ? 672 HOH C O   1 
HETATM 14263 O O   . HOH K 3 .   ? 27.975  39.865  27.625  1.00 38.89  ? 673 HOH C O   1 
HETATM 14264 O O   . HOH K 3 .   ? 29.193  67.149  27.413  1.00 44.58  ? 674 HOH C O   1 
HETATM 14265 O O   . HOH K 3 .   ? 3.288   64.382  66.469  1.00 43.84  ? 675 HOH C O   1 
HETATM 14266 O O   . HOH K 3 .   ? -6.421  56.572  40.238  1.00 52.29  ? 676 HOH C O   1 
HETATM 14267 O O   . HOH K 3 .   ? 8.678   52.422  62.817  1.00 23.56  ? 677 HOH C O   1 
HETATM 14268 O O   . HOH K 3 .   ? -7.629  38.165  66.266  1.00 35.34  ? 678 HOH C O   1 
HETATM 14269 O O   . HOH K 3 .   ? 25.334  60.928  47.297  1.00 27.13  ? 679 HOH C O   1 
HETATM 14270 O O   . HOH K 3 .   ? 5.233   47.783  32.608  1.00 27.62  ? 680 HOH C O   1 
HETATM 14271 O O   . HOH K 3 .   ? 12.484  51.059  52.022  1.00 20.07  ? 681 HOH C O   1 
HETATM 14272 O O   . HOH K 3 .   ? 14.346  43.548  60.794  1.00 28.17  ? 682 HOH C O   1 
HETATM 14273 O O   . HOH K 3 .   ? 12.794  27.431  61.808  1.00 60.16  ? 683 HOH C O   1 
HETATM 14274 O O   . HOH K 3 .   ? 11.779  47.641  60.619  1.00 21.56  ? 684 HOH C O   1 
HETATM 14275 O O   . HOH K 3 .   ? 5.521   67.304  45.748  1.00 53.75  ? 685 HOH C O   1 
HETATM 14276 O O   . HOH K 3 .   ? 29.061  58.163  40.674  1.00 43.62  ? 686 HOH C O   1 
HETATM 14277 O O   . HOH K 3 .   ? -7.068  55.399  37.697  1.00 48.53  ? 687 HOH C O   1 
HETATM 14278 O O   . HOH K 3 .   ? 16.169  67.652  32.170  1.00 49.09  ? 688 HOH C O   1 
HETATM 14279 O O   . HOH K 3 .   ? 9.152   67.797  37.172  1.00 55.42  ? 689 HOH C O   1 
HETATM 14280 O O   . HOH K 3 .   ? 27.502  35.176  76.408  1.00 38.37  ? 690 HOH C O   1 
HETATM 14281 O O   . HOH K 3 .   ? 29.987  35.364  25.191  1.00 31.44  ? 691 HOH C O   1 
HETATM 14282 O O   . HOH K 3 .   ? 27.145  63.146  26.262  1.00 34.47  ? 692 HOH C O   1 
HETATM 14283 O O   . HOH K 3 .   ? 28.965  34.768  55.896  1.00 43.52  ? 693 HOH C O   1 
HETATM 14284 O O   . HOH K 3 .   ? 15.498  37.441  37.324  1.00 24.79  ? 694 HOH C O   1 
HETATM 14285 O O   . HOH K 3 .   ? 14.284  46.345  60.095  1.00 28.32  ? 695 HOH C O   1 
HETATM 14286 O O   . HOH K 3 .   ? 6.043   57.436  25.267  1.00 40.45  ? 696 HOH C O   1 
HETATM 14287 O O   . HOH K 3 .   ? 42.847  53.658  30.356  1.00 48.86  ? 697 HOH C O   1 
HETATM 14288 O O   . HOH K 3 .   ? 0.564   45.247  60.582  1.00 33.52  ? 698 HOH C O   1 
HETATM 14289 O O   . HOH K 3 .   ? 44.365  36.979  48.677  1.00 43.27  ? 699 HOH C O   1 
HETATM 14290 O O   . HOH K 3 .   ? 20.792  75.961  35.267  1.00 48.04  ? 700 HOH C O   1 
HETATM 14291 O O   . HOH K 3 .   ? 6.075   53.146  63.517  1.00 29.96  ? 701 HOH C O   1 
HETATM 14292 O O   . HOH K 3 .   ? 8.707   51.287  59.370  1.00 27.01  ? 702 HOH C O   1 
HETATM 14293 O O   . HOH K 3 .   ? 24.683  33.477  48.913  1.00 35.00  ? 703 HOH C O   1 
HETATM 14294 O O   . HOH K 3 .   ? 12.301  44.279  58.250  1.00 23.14  ? 704 HOH C O   1 
HETATM 14295 O O   . HOH K 3 .   ? 29.263  36.722  22.304  1.00 33.59  ? 705 HOH C O   1 
HETATM 14296 O O   . HOH K 3 .   ? 31.447  62.180  34.416  1.00 42.13  ? 706 HOH C O   1 
HETATM 14297 O O   . HOH K 3 .   ? 48.243  32.449  36.621  1.00 41.07  ? 707 HOH C O   1 
HETATM 14298 O O   . HOH K 3 .   ? 23.688  75.518  45.967  1.00 27.62  ? 708 HOH C O   1 
HETATM 14299 O O   . HOH K 3 .   ? 13.611  30.677  41.399  1.00 48.95  ? 709 HOH C O   1 
HETATM 14300 O O   . HOH K 3 .   ? 36.603  33.729  24.945  1.00 61.82  ? 710 HOH C O   1 
HETATM 14301 O O   . HOH K 3 .   ? 10.393  64.817  36.379  1.00 50.53  ? 711 HOH C O   1 
HETATM 14302 O O   . HOH K 3 .   ? 2.440   54.740  29.336  1.00 31.03  ? 712 HOH C O   1 
HETATM 14303 O O   . HOH K 3 .   ? 4.297   54.764  65.883  1.00 40.05  ? 713 HOH C O   1 
HETATM 14304 O O   . HOH K 3 .   ? 19.653  39.150  40.329  1.00 28.64  ? 714 HOH C O   1 
HETATM 14305 O O   . HOH K 3 .   ? 17.376  37.704  32.666  1.00 32.69  ? 715 HOH C O   1 
HETATM 14306 O O   . HOH K 3 .   ? 5.833   39.308  48.291  1.00 27.70  ? 716 HOH C O   1 
HETATM 14307 O O   . HOH K 3 .   ? 13.920  71.330  26.502  1.00 38.28  ? 717 HOH C O   1 
HETATM 14308 O O   . HOH K 3 .   ? -5.011  37.535  61.641  1.00 36.61  ? 718 HOH C O   1 
HETATM 14309 O O   . HOH K 3 .   ? 8.026   49.560  16.888  1.00 34.04  ? 719 HOH C O   1 
HETATM 14310 O O   . HOH K 3 .   ? 8.645   62.611  59.642  1.00 22.67  ? 720 HOH C O   1 
HETATM 14311 O O   . HOH K 3 .   ? 29.116  34.457  74.031  1.00 59.34  ? 721 HOH C O   1 
HETATM 14312 O O   . HOH K 3 .   ? 17.496  57.189  31.407  1.00 54.06  ? 722 HOH C O   1 
HETATM 14313 O O   . HOH K 3 .   ? 0.247   52.836  58.168  1.00 20.52  ? 723 HOH C O   1 
HETATM 14314 O O   . HOH K 3 .   ? 13.324  31.063  70.194  1.00 42.72  ? 724 HOH C O   1 
HETATM 14315 O O   . HOH K 3 .   ? -0.384  30.589  66.354  1.00 84.12  ? 725 HOH C O   1 
HETATM 14316 O O   . HOH K 3 .   ? 12.589  61.353  21.054  1.00 43.62  ? 726 HOH C O   1 
HETATM 14317 O O   . HOH K 3 .   ? 30.859  28.173  44.152  1.00 50.25  ? 727 HOH C O   1 
HETATM 14318 O O   . HOH K 3 .   ? 23.411  28.866  39.874  1.00 56.82  ? 728 HOH C O   1 
HETATM 14319 O O   . HOH K 3 .   ? 31.859  41.144  50.798  1.00 31.68  ? 729 HOH C O   1 
HETATM 14320 O O   . HOH K 3 .   ? -3.128  40.947  50.549  1.00 45.63  ? 730 HOH C O   1 
HETATM 14321 O O   . HOH K 3 .   ? 24.948  46.374  48.643  1.00 18.47  ? 731 HOH C O   1 
HETATM 14322 O O   . HOH K 3 .   ? -0.218  57.324  29.655  1.00 35.13  ? 732 HOH C O   1 
HETATM 14323 O O   . HOH K 3 .   ? 0.208   66.641  55.120  1.00 36.43  ? 733 HOH C O   1 
HETATM 14324 O O   . HOH K 3 .   ? 34.192  29.832  74.723  1.00 54.13  ? 734 HOH C O   1 
HETATM 14325 O O   . HOH K 3 .   ? 24.867  27.656  64.515  1.00 43.70  ? 735 HOH C O   1 
HETATM 14326 O O   . HOH K 3 .   ? -5.146  47.938  26.148  1.00 36.51  ? 736 HOH C O   1 
HETATM 14327 O O   . HOH K 3 .   ? 25.956  31.061  36.143  1.00 28.68  ? 737 HOH C O   1 
HETATM 14328 O O   . HOH K 3 .   ? 9.398   51.430  66.981  1.00 25.03  ? 738 HOH C O   1 
HETATM 14329 O O   . HOH K 3 .   ? 34.119  36.946  22.771  1.00 48.24  ? 739 HOH C O   1 
HETATM 14330 O O   . HOH K 3 .   ? 7.743   60.352  55.211  1.00 38.67  ? 740 HOH C O   1 
HETATM 14331 O O   . HOH K 3 .   ? 21.207  40.755  15.961  1.00 38.79  ? 741 HOH C O   1 
HETATM 14332 O O   . HOH K 3 .   ? 48.294  33.794  25.328  1.00 73.40  ? 742 HOH C O   1 
HETATM 14333 O O   . HOH K 3 .   ? 49.086  38.185  44.564  1.00 29.99  ? 743 HOH C O   1 
HETATM 14334 O O   . HOH K 3 .   ? 51.729  39.520  35.640  1.00 42.20  ? 744 HOH C O   1 
HETATM 14335 O O   . HOH K 3 .   ? 18.202  58.899  55.939  1.00 39.75  ? 745 HOH C O   1 
HETATM 14336 O O   . HOH K 3 .   ? 6.876   61.527  33.315  1.00 32.01  ? 746 HOH C O   1 
HETATM 14337 O O   . HOH K 3 .   ? 16.050  34.133  49.314  1.00 33.13  ? 747 HOH C O   1 
HETATM 14338 O O   . HOH K 3 .   ? -2.822  60.982  52.121  1.00 34.68  ? 748 HOH C O   1 
HETATM 14339 O O   . HOH K 3 .   ? 3.228   43.074  51.088  1.00 30.04  ? 749 HOH C O   1 
HETATM 14340 O O   . HOH K 3 .   ? 21.332  31.063  59.925  1.00 46.76  ? 750 HOH C O   1 
HETATM 14341 O O   . HOH K 3 .   ? 37.726  54.424  20.955  1.00 42.05  ? 751 HOH C O   1 
HETATM 14342 O O   . HOH K 3 .   ? -2.066  47.192  46.484  1.00 48.97  ? 752 HOH C O   1 
HETATM 14343 O O   . HOH K 3 .   ? -5.102  42.283  41.525  1.00 45.92  ? 753 HOH C O   1 
HETATM 14344 O O   . HOH K 3 .   ? 26.944  71.681  38.561  1.00 26.10  ? 754 HOH C O   1 
HETATM 14345 O O   . HOH K 3 .   ? 7.276   44.223  65.911  1.00 46.11  ? 755 HOH C O   1 
HETATM 14346 O O   . HOH K 3 .   ? 26.133  44.851  74.576  1.00 46.64  ? 756 HOH C O   1 
HETATM 14347 O O   . HOH K 3 .   ? -6.951  55.920  51.221  1.00 47.14  ? 757 HOH C O   1 
HETATM 14348 O O   . HOH K 3 .   ? 31.747  31.562  36.045  1.00 41.92  ? 758 HOH C O   1 
HETATM 14349 O O   . HOH K 3 .   ? 12.990  43.280  21.655  1.00 39.16  ? 759 HOH C O   1 
HETATM 14350 O O   . HOH K 3 .   ? 18.063  27.891  61.071  1.00 51.36  ? 760 HOH C O   1 
HETATM 14351 O O   . HOH K 3 .   ? 1.068   39.670  32.760  1.00 53.26  ? 761 HOH C O   1 
HETATM 14352 O O   . HOH K 3 .   ? -5.610  37.167  56.231  1.00 51.31  ? 762 HOH C O   1 
HETATM 14353 O O   . HOH K 3 .   ? 37.164  33.748  59.530  1.00 41.72  ? 763 HOH C O   1 
HETATM 14354 O O   . HOH K 3 .   ? 33.313  43.965  78.169  1.00 50.51  ? 764 HOH C O   1 
HETATM 14355 O O   . HOH K 3 .   ? -2.437  64.577  60.240  1.00 46.03  ? 765 HOH C O   1 
HETATM 14356 O O   . HOH K 3 .   ? 13.689  30.958  36.686  1.00 44.24  ? 766 HOH C O   1 
HETATM 14357 O O   . HOH K 3 .   ? 6.705   40.011  25.733  1.00 34.73  ? 767 HOH C O   1 
HETATM 14358 O O   . HOH K 3 .   ? 8.761   54.078  20.792  1.00 42.69  ? 768 HOH C O   1 
HETATM 14359 O O   . HOH K 3 .   ? 3.413   43.582  37.266  1.00 71.94  ? 769 HOH C O   1 
HETATM 14360 O O   . HOH K 3 .   ? 23.651  76.075  34.661  1.00 42.31  ? 770 HOH C O   1 
HETATM 14361 O O   . HOH K 3 .   ? 0.676   61.748  59.527  1.00 36.78  ? 771 HOH C O   1 
HETATM 14362 O O   . HOH K 3 .   ? -3.221  33.724  69.479  1.00 42.95  ? 772 HOH C O   1 
HETATM 14363 O O   . HOH K 3 .   ? -2.214  59.295  29.054  1.00 45.84  ? 773 HOH C O   1 
HETATM 14364 O O   . HOH K 3 .   ? 0.823   70.025  54.456  1.00 45.80  ? 774 HOH C O   1 
HETATM 14365 O O   . HOH K 3 .   ? -1.319  66.292  58.670  1.00 44.93  ? 775 HOH C O   1 
HETATM 14366 O O   . HOH K 3 .   ? 31.554  45.965  76.438  1.00 30.79  ? 776 HOH C O   1 
HETATM 14367 O O   . HOH K 3 .   ? 21.952  65.222  21.130  1.00 50.14  ? 777 HOH C O   1 
HETATM 14368 O O   . HOH K 3 .   ? -8.596  44.003  47.899  1.00 40.55  ? 778 HOH C O   1 
HETATM 14369 O O   . HOH K 3 .   ? 29.648  60.366  45.497  1.00 29.55  ? 779 HOH C O   1 
HETATM 14370 O O   . HOH K 3 .   ? 18.959  67.927  23.721  1.00 33.65  ? 780 HOH C O   1 
HETATM 14371 O O   . HOH K 3 .   ? 48.589  42.024  33.798  1.00 44.82  ? 781 HOH C O   1 
HETATM 14372 O O   . HOH K 3 .   ? 10.684  49.517  58.744  1.00 24.14  ? 782 HOH C O   1 
HETATM 14373 O O   . HOH K 3 .   ? 24.763  66.193  22.661  1.00 33.69  ? 783 HOH C O   1 
HETATM 14374 O O   . HOH K 3 .   ? 18.927  31.939  55.393  1.00 31.59  ? 784 HOH C O   1 
HETATM 14375 O O   . HOH K 3 .   ? 48.005  43.548  36.019  1.00 37.59  ? 785 HOH C O   1 
HETATM 14376 O O   . HOH K 3 .   ? 2.668   69.829  49.541  1.00 47.23  ? 786 HOH C O   1 
HETATM 14377 O O   . HOH K 3 .   ? 32.842  47.837  80.276  1.00 29.96  ? 787 HOH C O   1 
HETATM 14378 O O   . HOH K 3 .   ? 32.963  59.412  44.631  1.00 35.89  ? 788 HOH C O   1 
HETATM 14379 O O   . HOH K 3 .   ? 23.012  58.579  32.839  1.00 37.00  ? 789 HOH C O   1 
HETATM 14380 O O   . HOH K 3 .   ? 10.843  35.268  45.573  1.00 32.39  ? 790 HOH C O   1 
HETATM 14381 O O   . HOH K 3 .   ? 26.346  33.211  76.611  1.00 38.41  ? 791 HOH C O   1 
HETATM 14382 O O   . HOH K 3 .   ? -1.296  69.609  52.909  1.00 33.24  ? 792 HOH C O   1 
HETATM 14383 O O   . HOH K 3 .   ? 9.981   66.514  60.304  1.00 19.49  ? 793 HOH C O   1 
HETATM 14384 O O   . HOH K 3 .   ? 34.153  41.684  51.705  1.00 41.82  ? 794 HOH C O   1 
HETATM 14385 O O   . HOH K 3 .   ? 14.653  30.061  50.147  1.00 44.64  ? 795 HOH C O   1 
HETATM 14386 O O   . HOH L 3 .   ? 55.054  67.203  2.809   1.00 43.13  ? 601 HOH D O   1 
HETATM 14387 O O   . HOH L 3 .   ? 36.705  60.324  -16.090 1.00 37.37  ? 602 HOH D O   1 
HETATM 14388 O O   . HOH L 3 .   ? 3.792   64.613  16.691  1.00 54.28  ? 603 HOH D O   1 
HETATM 14389 O O   . HOH L 3 .   ? 28.161  66.268  -5.530  1.00 43.23  ? 604 HOH D O   1 
HETATM 14390 O O   . HOH L 3 .   ? 38.419  60.915  -0.622  1.00 38.00  ? 605 HOH D O   1 
HETATM 14391 O O   . HOH L 3 .   ? -0.153  61.250  22.255  1.00 35.90  ? 606 HOH D O   1 
HETATM 14392 O O   . HOH L 3 .   ? 43.821  63.695  12.604  1.00 33.93  ? 607 HOH D O   1 
HETATM 14393 O O   . HOH L 3 .   ? 25.004  83.222  -12.770 1.00 35.13  ? 608 HOH D O   1 
HETATM 14394 O O   . HOH L 3 .   ? 24.883  71.817  17.259  1.00 36.63  ? 609 HOH D O   1 
HETATM 14395 O O   . HOH L 3 .   ? 18.614  65.835  -13.153 1.00 56.48  ? 610 HOH D O   1 
HETATM 14396 O O   . HOH L 3 .   ? -0.360  66.012  -1.060  1.00 43.52  ? 611 HOH D O   1 
HETATM 14397 O O   . HOH L 3 .   ? 38.646  74.408  -0.266  1.00 26.43  ? 612 HOH D O   1 
HETATM 14398 O O   . HOH L 3 .   ? 38.804  65.499  18.274  1.00 54.61  ? 613 HOH D O   1 
HETATM 14399 O O   . HOH L 3 .   ? 18.681  65.438  3.665   1.00 26.07  ? 614 HOH D O   1 
HETATM 14400 O O   . HOH L 3 .   ? 26.752  55.712  -0.789  1.00 23.54  ? 615 HOH D O   1 
HETATM 14401 O O   . HOH L 3 .   ? 4.960   67.301  15.652  1.00 49.07  ? 616 HOH D O   1 
HETATM 14402 O O   . HOH L 3 .   ? 42.038  76.136  1.750   1.00 35.42  ? 617 HOH D O   1 
HETATM 14403 O O   . HOH L 3 .   ? -7.077  61.642  8.993   1.00 31.14  ? 618 HOH D O   1 
HETATM 14404 O O   . HOH L 3 .   ? 15.524  68.682  3.047   1.00 54.93  ? 619 HOH D O   1 
HETATM 14405 O O   . HOH L 3 .   ? 14.604  59.572  1.169   1.00 32.39  ? 620 HOH D O   1 
HETATM 14406 O O   . HOH L 3 .   ? 40.490  49.729  -5.621  1.00 45.41  ? 621 HOH D O   1 
HETATM 14407 O O   . HOH L 3 .   ? 34.712  72.066  4.423   1.00 26.25  ? 622 HOH D O   1 
HETATM 14408 O O   . HOH L 3 .   ? -9.205  71.224  16.194  1.00 44.19  ? 623 HOH D O   1 
HETATM 14409 O O   . HOH L 3 .   ? 13.314  64.658  18.808  1.00 34.77  ? 624 HOH D O   1 
HETATM 14410 O O   . HOH L 3 .   ? 7.057   61.739  -1.280  1.00 26.88  ? 625 HOH D O   1 
HETATM 14411 O O   . HOH L 3 .   ? 25.324  59.464  4.049   1.00 21.84  ? 626 HOH D O   1 
HETATM 14412 O O   . HOH L 3 .   ? 39.988  68.264  -1.025  1.00 41.32  ? 627 HOH D O   1 
HETATM 14413 O O   . HOH L 3 .   ? 34.564  72.582  12.324  1.00 29.04  ? 628 HOH D O   1 
HETATM 14414 O O   . HOH L 3 .   ? 18.619  52.347  -3.310  1.00 42.82  ? 629 HOH D O   1 
HETATM 14415 O O   . HOH L 3 .   ? -6.521  53.562  7.321   1.00 35.68  ? 630 HOH D O   1 
HETATM 14416 O O   . HOH L 3 .   ? 30.254  54.793  18.005  1.00 35.06  ? 631 HOH D O   1 
HETATM 14417 O O   . HOH L 3 .   ? 22.336  64.918  -16.891 1.00 27.84  ? 632 HOH D O   1 
HETATM 14418 O O   . HOH L 3 .   ? 48.070  71.395  0.384   1.00 46.67  ? 633 HOH D O   1 
HETATM 14419 O O   . HOH L 3 .   ? -6.020  55.687  13.204  1.00 47.13  ? 634 HOH D O   1 
HETATM 14420 O O   . HOH L 3 .   ? 43.708  45.320  -17.922 1.00 50.55  ? 635 HOH D O   1 
HETATM 14421 O O   . HOH L 3 .   ? 43.797  83.847  1.366   1.00 36.17  ? 636 HOH D O   1 
HETATM 14422 O O   . HOH L 3 .   ? 32.890  58.977  -20.566 1.00 29.80  ? 637 HOH D O   1 
HETATM 14423 O O   . HOH L 3 .   ? 32.306  50.595  7.227   1.00 27.53  ? 638 HOH D O   1 
HETATM 14424 O O   . HOH L 3 .   ? 31.986  69.965  18.327  1.00 47.45  ? 639 HOH D O   1 
HETATM 14425 O O   . HOH L 3 .   ? 14.462  83.152  -2.098  1.00 29.82  ? 640 HOH D O   1 
HETATM 14426 O O   . HOH L 3 .   ? 30.769  54.923  -7.250  1.00 22.21  ? 641 HOH D O   1 
HETATM 14427 O O   . HOH L 3 .   ? 31.987  52.572  -8.358  1.00 20.41  ? 642 HOH D O   1 
HETATM 14428 O O   . HOH L 3 .   ? -3.747  59.038  13.511  1.00 45.03  ? 643 HOH D O   1 
HETATM 14429 O O   . HOH L 3 .   ? 42.736  82.914  -1.189  1.00 34.82  ? 644 HOH D O   1 
HETATM 14430 O O   . HOH L 3 .   ? 12.563  30.576  -17.758 1.00 40.71  ? 645 HOH D O   1 
HETATM 14431 O O   . HOH L 3 .   ? 5.606   66.264  0.479   1.00 28.26  ? 646 HOH D O   1 
HETATM 14432 O O   . HOH L 3 .   ? 32.324  72.187  0.680   1.00 63.82  ? 647 HOH D O   1 
HETATM 14433 O O   . HOH L 3 .   ? 34.029  62.911  -22.068 1.00 41.69  ? 648 HOH D O   1 
HETATM 14434 O O   . HOH L 3 .   ? 9.453   60.968  -0.025  1.00 29.75  ? 649 HOH D O   1 
HETATM 14435 O O   . HOH L 3 .   ? 18.644  45.266  0.460   1.00 23.96  ? 650 HOH D O   1 
HETATM 14436 O O   . HOH L 3 .   ? 37.835  66.295  8.660   1.00 23.95  ? 651 HOH D O   1 
HETATM 14437 O O   . HOH L 3 .   ? 28.708  45.847  -9.845  1.00 21.61  ? 652 HOH D O   1 
HETATM 14438 O O   . HOH L 3 .   ? -6.872  62.393  0.821   1.00 37.19  ? 653 HOH D O   1 
HETATM 14439 O O   . HOH L 3 .   ? 12.589  50.450  1.745   1.00 43.92  ? 654 HOH D O   1 
HETATM 14440 O O   . HOH L 3 .   ? 51.269  69.085  3.217   1.00 39.45  ? 655 HOH D O   1 
HETATM 14441 O O   . HOH L 3 .   ? 24.785  38.184  -15.964 1.00 22.79  ? 656 HOH D O   1 
HETATM 14442 O O   . HOH L 3 .   ? 23.500  46.562  -15.428 1.00 20.56  ? 657 HOH D O   1 
HETATM 14443 O O   . HOH L 3 .   ? 29.544  48.397  1.407   1.00 22.04  ? 658 HOH D O   1 
HETATM 14444 O O   . HOH L 3 .   ? 25.598  45.771  14.954  1.00 41.89  ? 659 HOH D O   1 
HETATM 14445 O O   . HOH L 3 .   ? 16.539  68.981  21.249  1.00 44.85  ? 660 HOH D O   1 
HETATM 14446 O O   . HOH L 3 .   ? 42.574  41.753  -7.241  1.00 34.42  ? 661 HOH D O   1 
HETATM 14447 O O   . HOH L 3 .   ? 17.966  78.923  -22.215 1.00 58.82  ? 662 HOH D O   1 
HETATM 14448 O O   . HOH L 3 .   ? 47.377  65.427  -9.062  1.00 30.18  ? 663 HOH D O   1 
HETATM 14449 O O   . HOH L 3 .   ? 11.419  45.146  -8.599  1.00 27.21  ? 664 HOH D O   1 
HETATM 14450 O O   . HOH L 3 .   ? 4.621   60.051  -0.796  1.00 42.83  ? 665 HOH D O   1 
HETATM 14451 O O   . HOH L 3 .   ? 18.185  69.274  3.424   1.00 26.76  ? 666 HOH D O   1 
HETATM 14452 O O   . HOH L 3 .   ? 47.786  71.948  11.601  1.00 33.03  ? 667 HOH D O   1 
HETATM 14453 O O   . HOH L 3 .   ? 50.774  51.910  -15.329 1.00 39.37  ? 668 HOH D O   1 
HETATM 14454 O O   . HOH L 3 .   ? 43.164  51.372  -12.862 1.00 22.05  ? 669 HOH D O   1 
HETATM 14455 O O   . HOH L 3 .   ? 37.425  46.598  2.493   1.00 29.73  ? 670 HOH D O   1 
HETATM 14456 O O   . HOH L 3 .   ? 40.792  74.447  16.516  1.00 49.84  ? 671 HOH D O   1 
HETATM 14457 O O   . HOH L 3 .   ? 30.837  81.308  8.650   1.00 39.82  ? 672 HOH D O   1 
HETATM 14458 O O   . HOH L 3 .   ? 15.785  54.710  9.699   1.00 32.01  ? 673 HOH D O   1 
HETATM 14459 O O   . HOH L 3 .   ? -5.254  67.280  6.396   1.00 56.02  ? 674 HOH D O   1 
HETATM 14460 O O   . HOH L 3 .   ? 20.156  50.533  -5.788  1.00 18.54  ? 675 HOH D O   1 
HETATM 14461 O O   . HOH L 3 .   ? 13.255  76.162  -3.511  1.00 28.86  ? 676 HOH D O   1 
HETATM 14462 O O   . HOH L 3 .   ? 17.602  82.118  -17.674 1.00 35.10  ? 677 HOH D O   1 
HETATM 14463 O O   . HOH L 3 .   ? 2.150   58.701  4.598   1.00 44.79  ? 678 HOH D O   1 
HETATM 14464 O O   . HOH L 3 .   ? 33.660  75.682  -2.115  1.00 33.70  ? 679 HOH D O   1 
HETATM 14465 O O   . HOH L 3 .   ? 13.408  75.848  10.635  1.00 27.67  ? 680 HOH D O   1 
HETATM 14466 O O   . HOH L 3 .   ? 25.708  79.548  1.938   1.00 61.79  ? 681 HOH D O   1 
HETATM 14467 O O   . HOH L 3 .   ? 3.960   61.903  5.360   1.00 43.44  ? 682 HOH D O   1 
HETATM 14468 O O   . HOH L 3 .   ? 1.026   57.460  16.789  1.00 32.25  ? 683 HOH D O   1 
HETATM 14469 O O   . HOH L 3 .   ? 11.900  55.844  0.351   1.00 31.78  ? 684 HOH D O   1 
HETATM 14470 O O   . HOH L 3 .   ? 0.889   66.789  2.203   1.00 32.25  ? 685 HOH D O   1 
HETATM 14471 O O   . HOH L 3 .   ? 34.539  48.153  -15.765 1.00 21.67  ? 686 HOH D O   1 
HETATM 14472 O O   . HOH L 3 .   ? 31.403  46.431  -10.953 1.00 25.63  ? 687 HOH D O   1 
HETATM 14473 O O   . HOH L 3 .   ? 35.931  58.167  -23.738 1.00 34.66  ? 688 HOH D O   1 
HETATM 14474 O O   . HOH L 3 .   ? 23.993  84.013  7.014   1.00 28.46  ? 689 HOH D O   1 
HETATM 14475 O O   . HOH L 3 .   ? 8.112   68.952  20.251  1.00 35.56  ? 690 HOH D O   1 
HETATM 14476 O O   . HOH L 3 .   ? 20.619  77.688  6.486   1.00 47.88  ? 691 HOH D O   1 
HETATM 14477 O O   . HOH L 3 .   ? 37.490  48.453  -13.893 1.00 29.34  ? 692 HOH D O   1 
HETATM 14478 O O   . HOH L 3 .   ? 10.596  63.778  12.405  1.00 28.81  ? 693 HOH D O   1 
HETATM 14479 O O   . HOH L 3 .   ? 33.839  44.265  -17.724 1.00 22.58  ? 694 HOH D O   1 
HETATM 14480 O O   . HOH L 3 .   ? 16.299  53.166  1.585   1.00 26.73  ? 695 HOH D O   1 
HETATM 14481 O O   . HOH L 3 .   ? 13.341  75.606  -10.425 1.00 35.44  ? 696 HOH D O   1 
HETATM 14482 O O   . HOH L 3 .   ? 28.401  43.265  -8.319  1.00 22.07  ? 697 HOH D O   1 
HETATM 14483 O O   . HOH L 3 .   ? -7.675  59.294  6.755   1.00 23.14  ? 698 HOH D O   1 
HETATM 14484 O O   . HOH L 3 .   ? 27.454  81.314  6.572   1.00 27.30  ? 699 HOH D O   1 
HETATM 14485 O O   . HOH L 3 .   ? 10.227  65.083  9.676   1.00 24.02  ? 700 HOH D O   1 
HETATM 14486 O O   . HOH L 3 .   ? 29.928  86.431  9.608   1.00 42.87  ? 701 HOH D O   1 
HETATM 14487 O O   . HOH L 3 .   ? 5.368   56.164  4.592   1.00 32.76  ? 702 HOH D O   1 
HETATM 14488 O O   . HOH L 3 .   ? 12.217  70.662  -13.692 1.00 26.17  ? 703 HOH D O   1 
HETATM 14489 O O   . HOH L 3 .   ? 15.489  69.591  -4.022  1.00 27.47  ? 704 HOH D O   1 
HETATM 14490 O O   . HOH L 3 .   ? 23.926  87.927  1.098   1.00 36.02  ? 705 HOH D O   1 
HETATM 14491 O O   . HOH L 3 .   ? 26.824  56.161  12.447  1.00 25.94  ? 706 HOH D O   1 
HETATM 14492 O O   . HOH L 3 .   ? 29.153  74.424  15.523  1.00 30.74  ? 707 HOH D O   1 
HETATM 14493 O O   . HOH L 3 .   ? 34.566  82.033  -0.379  1.00 48.46  ? 708 HOH D O   1 
HETATM 14494 O O   . HOH L 3 .   ? 2.398   59.511  12.758  1.00 40.54  ? 709 HOH D O   1 
HETATM 14495 O O   . HOH L 3 .   ? -7.821  54.548  1.528   1.00 33.53  ? 710 HOH D O   1 
HETATM 14496 O O   . HOH L 3 .   ? 20.907  70.880  3.384   1.00 37.38  ? 711 HOH D O   1 
HETATM 14497 O O   . HOH L 3 .   ? 21.755  33.757  -17.126 1.00 45.63  ? 712 HOH D O   1 
HETATM 14498 O O   . HOH L 3 .   ? 16.052  55.796  -0.829  1.00 25.46  ? 713 HOH D O   1 
HETATM 14499 O O   . HOH L 3 .   ? 9.916   68.406  -7.245  1.00 26.57  ? 714 HOH D O   1 
HETATM 14500 O O   . HOH L 3 .   ? 28.195  52.660  13.004  1.00 37.16  ? 715 HOH D O   1 
HETATM 14501 O O   . HOH L 3 .   ? 42.850  55.818  11.142  1.00 33.47  ? 716 HOH D O   1 
HETATM 14502 O O   . HOH L 3 .   ? 12.540  35.385  -18.256 1.00 27.76  ? 717 HOH D O   1 
HETATM 14503 O O   . HOH L 3 .   ? 41.309  73.078  5.978   1.00 30.73  ? 718 HOH D O   1 
HETATM 14504 O O   . HOH L 3 .   ? 10.983  44.947  -1.375  1.00 33.15  ? 719 HOH D O   1 
HETATM 14505 O O   . HOH L 3 .   ? 29.118  68.406  -0.005  1.00 39.91  ? 720 HOH D O   1 
HETATM 14506 O O   . HOH L 3 .   ? 37.322  70.420  -15.312 1.00 41.25  ? 721 HOH D O   1 
HETATM 14507 O O   . HOH L 3 .   ? 43.863  79.348  6.420   1.00 37.17  ? 722 HOH D O   1 
HETATM 14508 O O   . HOH L 3 .   ? 1.884   67.196  18.668  1.00 36.81  ? 723 HOH D O   1 
HETATM 14509 O O   . HOH L 3 .   ? 6.710   62.969  7.271   1.00 72.08  ? 724 HOH D O   1 
HETATM 14510 O O   . HOH L 3 .   ? 10.165  75.471  -0.798  1.00 44.29  ? 725 HOH D O   1 
HETATM 14511 O O   . HOH L 3 .   ? 37.366  48.933  4.028   1.00 27.04  ? 726 HOH D O   1 
HETATM 14512 O O   . HOH L 3 .   ? 18.262  54.476  -1.954  1.00 18.95  ? 727 HOH D O   1 
HETATM 14513 O O   . HOH L 3 .   ? 32.410  65.880  -24.039 1.00 21.23  ? 728 HOH D O   1 
HETATM 14514 O O   . HOH L 3 .   ? 34.213  50.151  4.996   1.00 32.77  ? 729 HOH D O   1 
HETATM 14515 O O   . HOH L 3 .   ? 28.859  48.534  9.088   1.00 28.77  ? 730 HOH D O   1 
HETATM 14516 O O   . HOH L 3 .   ? 42.504  53.280  10.065  1.00 41.84  ? 731 HOH D O   1 
HETATM 14517 O O   . HOH L 3 .   ? 3.945   62.295  22.235  1.00 35.25  ? 732 HOH D O   1 
HETATM 14518 O O   . HOH L 3 .   ? 33.794  76.359  -22.369 1.00 24.96  ? 733 HOH D O   1 
HETATM 14519 O O   . HOH L 3 .   ? 13.343  70.979  22.091  1.00 41.28  ? 734 HOH D O   1 
HETATM 14520 O O   . HOH L 3 .   ? 37.164  60.310  18.059  1.00 89.85  ? 735 HOH D O   1 
HETATM 14521 O O   . HOH L 3 .   ? 9.839   73.752  5.032   1.00 39.74  ? 736 HOH D O   1 
HETATM 14522 O O   . HOH L 3 .   ? 34.944  62.880  23.976  1.00 48.88  ? 737 HOH D O   1 
HETATM 14523 O O   . HOH L 3 .   ? 27.317  84.007  -13.088 1.00 45.95  ? 738 HOH D O   1 
HETATM 14524 O O   . HOH L 3 .   ? -0.893  56.024  19.113  1.00 38.09  ? 739 HOH D O   1 
HETATM 14525 O O   . HOH L 3 .   ? 2.678   62.279  -1.701  1.00 37.92  ? 740 HOH D O   1 
HETATM 14526 O O   . HOH L 3 .   ? 30.261  84.891  -3.182  1.00 36.67  ? 741 HOH D O   1 
HETATM 14527 O O   . HOH L 3 .   ? 10.552  35.449  -0.042  1.00 49.56  ? 742 HOH D O   1 
HETATM 14528 O O   . HOH L 3 .   ? 20.720  76.696  -21.213 1.00 31.95  ? 743 HOH D O   1 
HETATM 14529 O O   . HOH L 3 .   ? 12.293  59.380  2.686   1.00 34.49  ? 744 HOH D O   1 
HETATM 14530 O O   . HOH L 3 .   ? 10.814  51.025  5.798   1.00 31.99  ? 745 HOH D O   1 
HETATM 14531 O O   . HOH L 3 .   ? 35.043  57.315  -21.060 1.00 28.22  ? 746 HOH D O   1 
HETATM 14532 O O   . HOH L 3 .   ? 30.999  45.583  -7.033  1.00 26.92  ? 747 HOH D O   1 
HETATM 14533 O O   . HOH L 3 .   ? 43.120  78.112  -5.603  1.00 35.45  ? 748 HOH D O   1 
HETATM 14534 O O   . HOH L 3 .   ? 11.693  21.692  -11.925 1.00 45.92  ? 749 HOH D O   1 
HETATM 14535 O O   . HOH L 3 .   ? 27.389  63.442  13.416  1.00 58.48  ? 750 HOH D O   1 
HETATM 14536 O O   . HOH L 3 .   ? -1.184  78.303  13.437  1.00 42.69  ? 751 HOH D O   1 
HETATM 14537 O O   . HOH L 3 .   ? 46.247  66.481  13.357  1.00 40.55  ? 752 HOH D O   1 
HETATM 14538 O O   . HOH L 3 .   ? 5.074   29.035  -11.657 1.00 37.73  ? 753 HOH D O   1 
HETATM 14539 O O   . HOH L 3 .   ? 10.738  48.931  15.903  1.00 33.91  ? 754 HOH D O   1 
HETATM 14540 O O   . HOH L 3 .   ? 22.927  55.322  8.762   1.00 22.73  ? 755 HOH D O   1 
HETATM 14541 O O   . HOH L 3 .   ? 9.021   80.032  13.464  1.00 39.39  ? 756 HOH D O   1 
HETATM 14542 O O   . HOH L 3 .   ? 20.190  53.943  16.129  1.00 41.30  ? 757 HOH D O   1 
HETATM 14543 O O   . HOH L 3 .   ? 48.148  57.498  -27.451 1.00 35.73  ? 758 HOH D O   1 
HETATM 14544 O O   . HOH L 3 .   ? -8.620  63.609  20.046  1.00 43.07  ? 759 HOH D O   1 
HETATM 14545 O O   . HOH L 3 .   ? -5.941  53.917  11.677  1.00 54.40  ? 760 HOH D O   1 
HETATM 14546 O O   . HOH L 3 .   ? 7.095   25.588  -16.754 1.00 40.69  ? 761 HOH D O   1 
HETATM 14547 O O   . HOH L 3 .   ? 23.601  70.345  -6.600  1.00 43.18  ? 762 HOH D O   1 
HETATM 14548 O O   . HOH L 3 .   ? 19.478  47.964  16.322  1.00 41.20  ? 763 HOH D O   1 
HETATM 14549 O O   . HOH L 3 .   ? 17.976  79.476  -13.427 1.00 22.74  ? 764 HOH D O   1 
HETATM 14550 O O   . HOH L 3 .   ? 34.582  59.198  6.494   1.00 66.74  ? 765 HOH D O   1 
HETATM 14551 O O   . HOH L 3 .   ? 21.673  57.189  16.614  1.00 34.94  ? 766 HOH D O   1 
HETATM 14552 O O   . HOH L 3 .   ? 25.163  70.208  11.015  1.00 58.86  ? 767 HOH D O   1 
HETATM 14553 O O   . HOH L 3 .   ? 54.121  69.073  0.707   1.00 34.92  ? 768 HOH D O   1 
HETATM 14554 O O   . HOH L 3 .   ? 44.861  33.215  -6.377  1.00 35.45  ? 769 HOH D O   1 
HETATM 14555 O O   . HOH L 3 .   ? 0.622   65.944  11.111  1.00 43.26  ? 770 HOH D O   1 
HETATM 14556 O O   . HOH L 3 .   ? 47.790  68.645  13.687  1.00 36.66  ? 771 HOH D O   1 
HETATM 14557 O O   . HOH L 3 .   ? -3.947  51.174  13.316  1.00 42.13  ? 772 HOH D O   1 
HETATM 14558 O O   . HOH L 3 .   ? 49.542  71.056  4.720   1.00 35.27  ? 773 HOH D O   1 
HETATM 14559 O O   . HOH L 3 .   ? 23.410  67.349  7.592   1.00 56.10  ? 774 HOH D O   1 
HETATM 14560 O O   . HOH L 3 .   ? -5.012  60.326  17.736  1.00 41.26  ? 775 HOH D O   1 
HETATM 14561 O O   . HOH L 3 .   ? 32.595  26.848  -2.221  1.00 39.35  ? 776 HOH D O   1 
HETATM 14562 O O   . HOH L 3 .   ? 39.634  49.807  -0.745  1.00 29.17  ? 777 HOH D O   1 
HETATM 14563 O O   . HOH L 3 .   ? 27.107  51.616  14.317  1.00 50.80  ? 778 HOH D O   1 
HETATM 14564 O O   . HOH L 3 .   ? 40.679  61.105  -0.193  1.00 61.75  ? 779 HOH D O   1 
HETATM 14565 O O   . HOH L 3 .   ? 40.308  69.184  15.699  1.00 42.58  ? 780 HOH D O   1 
HETATM 14566 O O   . HOH L 3 .   ? 38.691  48.562  -21.199 1.00 27.89  ? 781 HOH D O   1 
HETATM 14567 O O   . HOH L 3 .   ? 46.154  70.223  14.565  1.00 48.38  ? 782 HOH D O   1 
HETATM 14568 O O   . HOH L 3 .   ? 6.158   70.215  9.693   1.00 38.48  ? 783 HOH D O   1 
HETATM 14569 O O   . HOH L 3 .   ? 3.891   69.919  18.142  1.00 45.56  ? 784 HOH D O   1 
HETATM 14570 O O   . HOH L 3 .   ? 28.644  68.610  -5.306  1.00 46.59  ? 785 HOH D O   1 
HETATM 14571 O O   . HOH L 3 .   ? 41.834  49.462  0.283   1.00 47.05  ? 786 HOH D O   1 
HETATM 14572 O O   . HOH L 3 .   ? 47.871  56.314  4.239   1.00 53.09  ? 787 HOH D O   1 
HETATM 14573 O O   . HOH L 3 .   ? 13.792  79.406  20.025  1.00 43.60  ? 788 HOH D O   1 
HETATM 14574 O O   . HOH L 3 .   ? 21.139  84.226  3.544   1.00 47.59  ? 789 HOH D O   1 
HETATM 14575 O O   . HOH L 3 .   ? 16.492  78.476  19.282  1.00 37.17  ? 790 HOH D O   1 
HETATM 14576 O O   . HOH L 3 .   ? 13.947  65.840  16.516  1.00 44.49  ? 791 HOH D O   1 
HETATM 14577 O O   . HOH L 3 .   ? 31.050  78.734  -10.884 1.00 49.83  ? 792 HOH D O   1 
HETATM 14578 O O   . HOH L 3 .   ? 32.137  60.315  20.452  1.00 35.73  ? 793 HOH D O   1 
HETATM 14579 O O   . HOH L 3 .   ? 23.037  76.452  8.661   1.00 35.00  ? 794 HOH D O   1 
HETATM 14580 O O   . HOH L 3 .   ? 26.107  55.345  14.611  1.00 38.34  ? 795 HOH D O   1 
HETATM 14581 O O   . HOH L 3 .   ? 6.342   45.173  8.191   1.00 48.86  ? 796 HOH D O   1 
HETATM 14582 O O   . HOH L 3 .   ? 32.233  48.923  -11.175 1.00 26.58  ? 797 HOH D O   1 
HETATM 14583 O O   . HOH L 3 .   ? 47.684  39.401  -10.453 1.00 48.38  ? 798 HOH D O   1 
HETATM 14584 O O   . HOH L 3 .   ? 30.655  70.928  -1.504  1.00 43.26  ? 799 HOH D O   1 
HETATM 14585 O O   . HOH L 3 .   ? 32.981  80.986  10.223  1.00 33.86  ? 800 HOH D O   1 
HETATM 14586 O O   . HOH L 3 .   ? 31.510  48.405  8.675   1.00 37.47  ? 801 HOH D O   1 
HETATM 14587 O O   . HOH L 3 .   ? 24.635  57.539  16.456  1.00 38.09  ? 802 HOH D O   1 
HETATM 14588 O O   . HOH L 3 .   ? 9.800   72.458  7.779   1.00 46.34  ? 803 HOH D O   1 
HETATM 14589 O O   . HOH L 3 .   ? 32.312  68.232  20.224  1.00 38.63  ? 804 HOH D O   1 
HETATM 14590 O O   . HOH L 3 .   ? 12.320  33.100  -23.629 1.00 42.29  ? 805 HOH D O   1 
HETATM 14591 O O   . HOH L 3 .   ? 36.064  59.845  20.301  1.00 47.77  ? 806 HOH D O   1 
HETATM 14592 O O   . HOH L 3 .   ? 3.171   59.909  9.836   1.00 44.07  ? 807 HOH D O   1 
HETATM 14593 O O   . HOH L 3 .   ? 29.235  72.424  -0.990  1.00 44.41  ? 808 HOH D O   1 
HETATM 14594 O O   . HOH L 3 .   ? 21.291  93.534  -8.328  1.00 37.89  ? 809 HOH D O   1 
HETATM 14595 O O   . HOH L 3 .   ? 38.414  59.264  20.566  1.00 39.47  ? 810 HOH D O   1 
# 
