data_8ZW1
# 
_entry.id   8ZW1 
# 
_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   8ZW1         pdb_00008zw1 10.2210/pdb8zw1/pdb 
WWPDB D_1300048629 ?            ?                   
# 
_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                        8ZW1 
_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                     'citrate synthases complexed with oxaloacetate and acetyl-CoA' 
_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 2   2.3.3.1 ? ? ? 
2 non-polymer syn 'COENZYME A'                      767.534   1   ?       ? ? ? 
3 non-polymer syn 'CITRIC ACID'                     192.124   1   ?       ? ? ? 
4 non-polymer syn 'OXALOACETATE ION'                131.064   1   ?       ? ? ? 
5 non-polymer syn 'ACETYL COENZYME *A'              809.571   1   ?       ? ? ? 
6 water       nat water                             18.015    142 ?       ? ? ? 
# 
_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 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'COENZYME A'         COA 
3 'CITRIC ACID'        CIT 
4 'OXALOACETATE ION'   OAA 
5 'ACETYL COENZYME *A' ACO 
6 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 
ACO non-polymer         . 'ACETYL COENZYME *A' ? 'C23 H38 N7 O17 P3 S' 809.571 
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 
COA non-polymer         . 'COENZYME A'         ? 'C21 H36 N7 O16 P3 S' 767.534 
CYS 'L-peptide linking' y CYSTEINE             ? 'C3 H7 N O2 S'        121.158 
GLN 'L-peptide linking' y GLUTAMINE            ? 'C5 H10 N2 O3'        146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'      ? 'C5 H9 N O4'          147.129 
GLY 'peptide linking'   y GLYCINE              ? 'C2 H5 N O2'          75.067  
HIS 'L-peptide linking' y HISTIDINE            ? 'C6 H10 N3 O2 1'      156.162 
HOH non-polymer         . WATER                ? 'H2 O'                18.015  
ILE 'L-peptide linking' y ISOLEUCINE           ? 'C6 H13 N O2'         131.173 
LEU 'L-peptide linking' y LEUCINE              ? 'C6 H13 N O2'         131.173 
LYS 'L-peptide linking' y LYSINE               ? 'C6 H15 N2 O2 1'      147.195 
MET 'L-peptide linking' y METHIONINE           ? 'C5 H11 N O2 S'       149.211 
OAA non-polymer         . 'OXALOACETATE ION'   ? 'C4 H3 O5 -1'         131.064 
PHE 'L-peptide linking' y PHENYLALANINE        ? 'C9 H11 N O2'         165.189 
PRO 'L-peptide linking' y PROLINE              ? 'C5 H9 N O2'          115.130 
SER 'L-peptide linking' y SERINE               ? 'C3 H7 N O3'          105.093 
THR 'L-peptide linking' y THREONINE            ? 'C4 H9 N O3'          119.119 
TRP 'L-peptide linking' y TRYPTOPHAN           ? 'C11 H12 N2 O2'       204.225 
TYR 'L-peptide linking' y TYROSINE             ? 'C9 H11 N O3'         181.189 
VAL 'L-peptide linking' y VALINE               ? 'C5 H11 N O2'         117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   30  30  SER SER A . n 
A 1 2   THR 2   31  31  THR THR A . n 
A 1 3   ASN 3   32  32  ASN ASN A . n 
A 1 4   LEU 4   33  33  LEU LEU A . n 
A 1 5   LYS 5   34  34  LYS LYS A . n 
A 1 6   ASP 6   35  35  ASP ASP A . n 
A 1 7   ILE 7   36  36  ILE ILE A . n 
A 1 8   LEU 8   37  37  LEU LEU A . n 
A 1 9   ALA 9   38  38  ALA ALA A . n 
A 1 10  ASP 10  39  39  ASP ASP A . n 
A 1 11  LEU 11  40  40  LEU LEU A . n 
A 1 12  ILE 12  41  41  ILE ILE A . n 
A 1 13  PRO 13  42  42  PRO PRO A . n 
A 1 14  LYS 14  43  43  LYS LYS A . n 
A 1 15  GLU 15  44  44  GLU GLU A . n 
A 1 16  GLN 16  45  45  GLN GLN A . n 
A 1 17  ALA 17  46  46  ALA ALA A . n 
A 1 18  ARG 18  47  47  ARG ARG A . n 
A 1 19  ILE 19  48  48  ILE ILE A . n 
A 1 20  LYS 20  49  49  LYS LYS A . n 
A 1 21  THR 21  50  50  THR THR A . n 
A 1 22  PHE 22  51  51  PHE PHE A . n 
A 1 23  ARG 23  52  52  ARG ARG A . n 
A 1 24  GLN 24  53  53  GLN GLN A . n 
A 1 25  GLN 25  54  54  GLN GLN A . n 
A 1 26  HIS 26  55  55  HIS HIS A . n 
A 1 27  GLY 27  56  56  GLY GLY A . n 
A 1 28  LYS 28  57  57  LYS LYS A . n 
A 1 29  THR 29  58  58  THR THR A . n 
A 1 30  VAL 30  59  59  VAL VAL A . n 
A 1 31  VAL 31  60  60  VAL VAL A . n 
A 1 32  GLY 32  61  61  GLY GLY A . n 
A 1 33  GLN 33  62  62  GLN GLN A . n 
A 1 34  ILE 34  63  63  ILE ILE A . n 
A 1 35  THR 35  64  64  THR THR A . n 
A 1 36  VAL 36  65  65  VAL VAL A . n 
A 1 37  ASP 37  66  66  ASP ASP A . n 
A 1 38  MET 38  67  67  MET MET A . n 
A 1 39  MET 39  68  68  MET MET A . n 
A 1 40  TYR 40  69  69  TYR TYR A . n 
A 1 41  GLY 41  70  70  GLY GLY A . n 
A 1 42  GLY 42  71  71  GLY GLY A . n 
A 1 43  MET 43  72  72  MET MET A . n 
A 1 44  ARG 44  73  73  ARG ARG A . n 
A 1 45  GLY 45  74  74  GLY GLY A . n 
A 1 46  MET 46  75  75  MET MET A . n 
A 1 47  LYS 47  76  76  LYS LYS A . n 
A 1 48  GLY 48  77  77  GLY GLY A . n 
A 1 49  LEU 49  78  78  LEU LEU A . n 
A 1 50  VAL 50  79  79  VAL VAL A . n 
A 1 51  TYR 51  80  80  TYR TYR A . n 
A 1 52  GLU 52  81  81  GLU GLU A . n 
A 1 53  THR 53  82  82  THR THR A . n 
A 1 54  SER 54  83  83  SER SER A . n 
A 1 55  VAL 55  84  84  VAL VAL A . n 
A 1 56  LEU 56  85  85  LEU LEU A . n 
A 1 57  ASP 57  86  86  ASP ASP A . n 
A 1 58  PRO 58  87  87  PRO PRO A . n 
A 1 59  ASP 59  88  88  ASP ASP A . n 
A 1 60  GLU 60  89  89  GLU GLU A . n 
A 1 61  GLY 61  90  90  GLY GLY A . n 
A 1 62  ILE 62  91  91  ILE ILE A . n 
A 1 63  ARG 63  92  92  ARG ARG A . n 
A 1 64  PHE 64  93  93  PHE PHE A . n 
A 1 65  ARG 65  94  94  ARG ARG A . n 
A 1 66  GLY 66  95  95  GLY GLY A . n 
A 1 67  PHE 67  96  96  PHE PHE A . n 
A 1 68  SER 68  97  97  SER SER A . n 
A 1 69  ILE 69  98  98  ILE ILE A . n 
A 1 70  PRO 70  99  99  PRO PRO A . n 
A 1 71  GLU 71  100 100 GLU GLU A . n 
A 1 72  CYS 72  101 101 CYS CYS A . n 
A 1 73  GLN 73  102 102 GLN GLN A . n 
A 1 74  LYS 74  103 103 LYS LYS A . n 
A 1 75  LEU 75  104 104 LEU LEU A . n 
A 1 76  LEU 76  105 105 LEU LEU A . n 
A 1 77  PRO 77  106 106 PRO PRO A . n 
A 1 78  LYS 78  107 107 LYS LYS A . n 
A 1 79  ALA 79  108 108 ALA ALA A . n 
A 1 80  LYS 80  109 109 LYS LYS A . n 
A 1 81  GLY 81  110 110 GLY GLY A . n 
A 1 82  GLY 82  111 111 GLY GLY A . n 
A 1 83  GLU 83  112 112 GLU GLU A . n 
A 1 84  GLU 84  113 113 GLU GLU A . n 
A 1 85  PRO 85  114 114 PRO PRO A . n 
A 1 86  LEU 86  115 115 LEU LEU A . n 
A 1 87  PRO 87  116 116 PRO PRO A . n 
A 1 88  GLU 88  117 117 GLU GLU A . n 
A 1 89  GLY 89  118 118 GLY GLY A . n 
A 1 90  LEU 90  119 119 LEU LEU A . n 
A 1 91  PHE 91  120 120 PHE PHE A . n 
A 1 92  TRP 92  121 121 TRP TRP A . n 
A 1 93  LEU 93  122 122 LEU LEU A . n 
A 1 94  LEU 94  123 123 LEU LEU A . n 
A 1 95  VAL 95  124 124 VAL VAL A . n 
A 1 96  THR 96  125 125 THR THR A . n 
A 1 97  GLY 97  126 126 GLY GLY A . n 
A 1 98  HIS 98  127 127 HIS HIS A . n 
A 1 99  ILE 99  128 128 ILE ILE A . n 
A 1 100 PRO 100 129 129 PRO PRO A . n 
A 1 101 THR 101 130 130 THR THR A . n 
A 1 102 GLU 102 131 131 GLU GLU A . n 
A 1 103 GLU 103 132 132 GLU GLU A . n 
A 1 104 GLN 104 133 133 GLN GLN A . n 
A 1 105 VAL 105 134 134 VAL VAL A . n 
A 1 106 SER 106 135 135 SER SER A . n 
A 1 107 TRP 107 136 136 TRP TRP A . n 
A 1 108 LEU 108 137 137 LEU LEU A . n 
A 1 109 SER 109 138 138 SER SER A . n 
A 1 110 LYS 110 139 139 LYS LYS A . n 
A 1 111 GLU 111 140 140 GLU GLU A . n 
A 1 112 TRP 112 141 141 TRP TRP A . n 
A 1 113 ALA 113 142 142 ALA ALA A . n 
A 1 114 LYS 114 143 143 LYS LYS A . n 
A 1 115 ARG 115 144 144 ARG ARG A . n 
A 1 116 ALA 116 145 145 ALA ALA A . n 
A 1 117 ALA 117 146 146 ALA ALA A . n 
A 1 118 LEU 118 147 147 LEU LEU A . n 
A 1 119 PRO 119 148 148 PRO PRO A . n 
A 1 120 SER 120 149 149 SER SER A . n 
A 1 121 HIS 121 150 150 HIS HIS A . n 
A 1 122 VAL 122 151 151 VAL VAL A . n 
A 1 123 VAL 123 152 152 VAL VAL A . n 
A 1 124 THR 124 153 153 THR THR A . n 
A 1 125 MET 125 154 154 MET MET A . n 
A 1 126 LEU 126 155 155 LEU LEU A . n 
A 1 127 ASP 127 156 156 ASP ASP A . n 
A 1 128 ASN 128 157 157 ASN ASN A . n 
A 1 129 PHE 129 158 158 PHE PHE A . n 
A 1 130 PRO 130 159 159 PRO PRO A . n 
A 1 131 THR 131 160 160 THR THR A . n 
A 1 132 ASN 132 161 161 ASN ASN A . n 
A 1 133 LEU 133 162 162 LEU LEU A . n 
A 1 134 HIS 134 163 163 HIS HIS A . n 
A 1 135 PRO 135 164 164 PRO PRO A . n 
A 1 136 MET 136 165 165 MET MET A . n 
A 1 137 SER 137 166 166 SER SER A . n 
A 1 138 GLN 138 167 167 GLN GLN A . n 
A 1 139 LEU 139 168 168 LEU LEU A . n 
A 1 140 SER 140 169 169 SER SER A . n 
A 1 141 ALA 141 170 170 ALA ALA A . n 
A 1 142 ALA 142 171 171 ALA ALA A . n 
A 1 143 VAL 143 172 172 VAL VAL A . n 
A 1 144 THR 144 173 173 THR THR A . n 
A 1 145 ALA 145 174 174 ALA ALA A . n 
A 1 146 LEU 146 175 175 LEU LEU A . n 
A 1 147 ASN 147 176 176 ASN ASN A . n 
A 1 148 SER 148 177 177 SER SER A . n 
A 1 149 GLU 149 178 178 GLU GLU A . n 
A 1 150 SER 150 179 179 SER SER A . n 
A 1 151 ASN 151 180 180 ASN ASN A . n 
A 1 152 PHE 152 181 181 PHE PHE A . n 
A 1 153 ALA 153 182 182 ALA ALA A . n 
A 1 154 ARG 154 183 183 ARG ARG A . n 
A 1 155 ALA 155 184 184 ALA ALA A . n 
A 1 156 TYR 156 185 185 TYR TYR A . n 
A 1 157 ALA 157 186 186 ALA ALA A . n 
A 1 158 GLN 158 187 187 GLN GLN A . n 
A 1 159 GLY 159 188 188 GLY GLY A . n 
A 1 160 ILE 160 189 189 ILE ILE A . n 
A 1 161 SER 161 190 190 SER SER A . n 
A 1 162 ARG 162 191 191 ARG ARG A . n 
A 1 163 THR 163 192 192 THR THR A . n 
A 1 164 LYS 164 193 193 LYS LYS A . n 
A 1 165 TYR 165 194 194 TYR TYR A . n 
A 1 166 TRP 166 195 195 TRP TRP A . n 
A 1 167 GLU 167 196 196 GLU GLU A . n 
A 1 168 LEU 168 197 197 LEU LEU A . n 
A 1 169 ILE 169 198 198 ILE ILE A . n 
A 1 170 TYR 170 199 199 TYR TYR A . n 
A 1 171 GLU 171 200 200 GLU GLU A . n 
A 1 172 ASP 172 201 201 ASP ASP A . n 
A 1 173 SER 173 202 202 SER SER A . n 
A 1 174 MET 174 203 203 MET MET A . n 
A 1 175 ASP 175 204 204 ASP ASP A . n 
A 1 176 LEU 176 205 205 LEU LEU A . n 
A 1 177 ILE 177 206 206 ILE ILE A . n 
A 1 178 ALA 178 207 207 ALA ALA A . n 
A 1 179 LYS 179 208 208 LYS LYS A . n 
A 1 180 LEU 180 209 209 LEU LEU A . n 
A 1 181 PRO 181 210 210 PRO PRO A . n 
A 1 182 CYS 182 211 211 CYS CYS A . n 
A 1 183 VAL 183 212 212 VAL VAL A . n 
A 1 184 ALA 184 213 213 ALA ALA A . n 
A 1 185 ALA 185 214 214 ALA ALA A . n 
A 1 186 LYS 186 215 215 LYS LYS A . n 
A 1 187 ILE 187 216 216 ILE ILE A . n 
A 1 188 TYR 188 217 217 TYR TYR A . n 
A 1 189 ARG 189 218 218 ARG ARG A . n 
A 1 190 ASN 190 219 219 ASN ASN A . n 
A 1 191 LEU 191 220 220 LEU LEU A . n 
A 1 192 TYR 192 221 221 TYR TYR A . n 
A 1 193 ARG 193 222 222 ARG ARG A . n 
A 1 194 GLU 194 223 223 GLU GLU A . n 
A 1 195 GLY 195 224 224 GLY GLY A . n 
A 1 196 SER 196 225 225 SER SER A . n 
A 1 197 GLY 197 226 226 GLY GLY A . n 
A 1 198 ILE 198 227 227 ILE ILE A . n 
A 1 199 GLY 199 228 228 GLY GLY A . n 
A 1 200 ALA 200 229 229 ALA ALA A . n 
A 1 201 ILE 201 230 230 ILE ILE A . n 
A 1 202 ASP 202 231 231 ASP ASP A . n 
A 1 203 SER 203 232 232 SER SER A . n 
A 1 204 ASN 204 233 233 ASN ASN A . n 
A 1 205 LEU 205 234 234 LEU LEU A . n 
A 1 206 ASP 206 235 235 ASP ASP A . n 
A 1 207 TRP 207 236 236 TRP TRP A . n 
A 1 208 SER 208 237 237 SER SER A . n 
A 1 209 HIS 209 238 238 HIS HIS A . n 
A 1 210 ASN 210 239 239 ASN ASN A . n 
A 1 211 PHE 211 240 240 PHE PHE A . n 
A 1 212 THR 212 241 241 THR THR A . n 
A 1 213 ASN 213 242 242 ASN ASN A . n 
A 1 214 MET 214 243 243 MET MET A . n 
A 1 215 LEU 215 244 244 LEU LEU A . n 
A 1 216 GLY 216 245 245 GLY GLY A . n 
A 1 217 TYR 217 246 246 TYR TYR A . n 
A 1 218 THR 218 247 247 THR THR A . n 
A 1 219 ASP 219 248 248 ASP ASP A . n 
A 1 220 HIS 220 249 249 HIS HIS A . n 
A 1 221 GLN 221 250 250 GLN GLN A . n 
A 1 222 PHE 222 251 251 PHE PHE A . n 
A 1 223 THR 223 252 252 THR THR A . n 
A 1 224 GLU 224 253 253 GLU GLU A . n 
A 1 225 LEU 225 254 254 LEU LEU A . n 
A 1 226 THR 226 255 255 THR THR A . n 
A 1 227 ARG 227 256 256 ARG ARG A . n 
A 1 228 LEU 228 257 257 LEU LEU A . n 
A 1 229 TYR 229 258 258 TYR TYR A . n 
A 1 230 LEU 230 259 259 LEU LEU A . n 
A 1 231 THR 231 260 260 THR THR A . n 
A 1 232 ILE 232 261 261 ILE ILE A . n 
A 1 233 HIS 233 262 262 HIS HIS A . n 
A 1 234 SER 234 263 263 SER SER A . n 
A 1 235 ASP 235 264 264 ASP ASP A . n 
A 1 236 HIS 236 265 265 HIS HIS A . n 
A 1 237 GLU 237 266 266 GLU GLU A . n 
A 1 238 GLY 238 267 267 GLY GLY A . n 
A 1 239 GLY 239 268 268 GLY GLY A . n 
A 1 240 ASN 240 269 269 ASN ASN A . n 
A 1 241 VAL 241 270 270 VAL VAL A . n 
A 1 242 SER 242 271 271 SER SER A . n 
A 1 243 ALA 243 272 272 ALA ALA A . n 
A 1 244 HIS 244 273 273 HIS HIS A . n 
A 1 245 THR 245 274 274 THR THR A . n 
A 1 246 SER 246 275 275 SER SER A . n 
A 1 247 HIS 247 276 276 HIS HIS A . n 
A 1 248 LEU 248 277 277 LEU LEU A . n 
A 1 249 VAL 249 278 278 VAL VAL A . n 
A 1 250 GLY 250 279 279 GLY GLY A . n 
A 1 251 SER 251 280 280 SER SER A . n 
A 1 252 ALA 252 281 281 ALA ALA A . n 
A 1 253 LEU 253 282 282 LEU LEU A . n 
A 1 254 SER 254 283 283 SER SER A . n 
A 1 255 ASP 255 284 284 ASP ASP A . n 
A 1 256 PRO 256 285 285 PRO PRO A . n 
A 1 257 TYR 257 286 286 TYR TYR A . n 
A 1 258 LEU 258 287 287 LEU LEU A . n 
A 1 259 SER 259 288 288 SER SER A . n 
A 1 260 PHE 260 289 289 PHE PHE A . n 
A 1 261 ALA 261 290 290 ALA ALA A . n 
A 1 262 ALA 262 291 291 ALA ALA A . n 
A 1 263 ALA 263 292 292 ALA ALA A . n 
A 1 264 MET 264 293 293 MET MET A . n 
A 1 265 ASN 265 294 294 ASN ASN A . n 
A 1 266 GLY 266 295 295 GLY GLY A . n 
A 1 267 LEU 267 296 296 LEU LEU A . n 
A 1 268 ALA 268 297 297 ALA ALA A . n 
A 1 269 GLY 269 298 298 GLY GLY A . n 
A 1 270 PRO 270 299 299 PRO PRO A . n 
A 1 271 LEU 271 300 300 LEU LEU A . n 
A 1 272 HIS 272 301 301 HIS HIS A . n 
A 1 273 GLY 273 302 302 GLY GLY A . n 
A 1 274 LEU 274 303 303 LEU LEU A . n 
A 1 275 ALA 275 304 304 ALA ALA A . n 
A 1 276 ASN 276 305 305 ASN ASN A . n 
A 1 277 GLN 277 306 306 GLN GLN A . n 
A 1 278 GLU 278 307 307 GLU GLU A . n 
A 1 279 VAL 279 308 308 VAL VAL A . n 
A 1 280 LEU 280 309 309 LEU LEU A . n 
A 1 281 VAL 281 310 310 VAL VAL A . n 
A 1 282 TRP 282 311 311 TRP TRP A . n 
A 1 283 LEU 283 312 312 LEU LEU A . n 
A 1 284 THR 284 313 313 THR THR A . n 
A 1 285 GLN 285 314 314 GLN GLN A . n 
A 1 286 LEU 286 315 315 LEU LEU A . n 
A 1 287 GLN 287 316 316 GLN GLN A . n 
A 1 288 LYS 288 317 317 LYS LYS A . n 
A 1 289 GLU 289 318 318 GLU GLU A . n 
A 1 290 VAL 290 319 319 VAL VAL A . n 
A 1 291 GLY 291 320 320 GLY GLY A . n 
A 1 292 LYS 292 321 321 LYS LYS A . n 
A 1 293 ASP 293 322 322 ASP ASP A . n 
A 1 294 VAL 294 323 323 VAL VAL A . n 
A 1 295 SER 295 324 324 SER SER A . n 
A 1 296 ASP 296 325 325 ASP ASP A . n 
A 1 297 GLU 297 326 326 GLU GLU A . n 
A 1 298 LYS 298 327 327 LYS LYS A . n 
A 1 299 LEU 299 328 328 LEU LEU A . n 
A 1 300 ARG 300 329 329 ARG ARG A . n 
A 1 301 ASP 301 330 330 ASP ASP A . n 
A 1 302 TYR 302 331 331 TYR TYR A . n 
A 1 303 ILE 303 332 332 ILE ILE A . n 
A 1 304 TRP 304 333 333 TRP TRP A . n 
A 1 305 ASN 305 334 334 ASN ASN A . n 
A 1 306 THR 306 335 335 THR THR A . n 
A 1 307 LEU 307 336 336 LEU LEU A . n 
A 1 308 ASN 308 337 337 ASN ASN A . n 
A 1 309 SER 309 338 338 SER SER A . n 
A 1 310 GLY 310 339 339 GLY GLY A . n 
A 1 311 ARG 311 340 340 ARG ARG A . n 
A 1 312 VAL 312 341 341 VAL VAL A . n 
A 1 313 VAL 313 342 342 VAL VAL A . n 
A 1 314 PRO 314 343 343 PRO PRO A . n 
A 1 315 GLY 315 344 344 GLY GLY A . n 
A 1 316 TYR 316 345 345 TYR TYR A . n 
A 1 317 GLY 317 346 346 GLY GLY A . n 
A 1 318 HIS 318 347 347 HIS HIS A . n 
A 1 319 ALA 319 348 348 ALA ALA A . n 
A 1 320 VAL 320 349 349 VAL VAL A . n 
A 1 321 LEU 321 350 350 LEU LEU A . n 
A 1 322 ARG 322 351 351 ARG ARG A . n 
A 1 323 LYS 323 352 352 LYS LYS A . n 
A 1 324 THR 324 353 353 THR THR A . n 
A 1 325 ASP 325 354 354 ASP ASP A . n 
A 1 326 PRO 326 355 355 PRO PRO A . n 
A 1 327 ARG 327 356 356 ARG ARG A . n 
A 1 328 TYR 328 357 357 TYR TYR A . n 
A 1 329 THR 329 358 358 THR THR A . n 
A 1 330 CYS 330 359 359 CYS CYS A . n 
A 1 331 GLN 331 360 360 GLN GLN A . n 
A 1 332 ARG 332 361 361 ARG ARG A . n 
A 1 333 GLU 333 362 362 GLU GLU A . n 
A 1 334 PHE 334 363 363 PHE PHE A . n 
A 1 335 ALA 335 364 364 ALA ALA A . n 
A 1 336 LEU 336 365 365 LEU LEU A . n 
A 1 337 LYS 337 366 366 LYS LYS A . n 
A 1 338 HIS 338 367 367 HIS HIS A . n 
A 1 339 LEU 339 368 368 LEU LEU A . n 
A 1 340 PRO 340 369 369 PRO PRO A . n 
A 1 341 ASN 341 370 370 ASN ASN A . n 
A 1 342 ASP 342 371 371 ASP ASP A . n 
A 1 343 PRO 343 372 372 PRO PRO A . n 
A 1 344 MET 344 373 373 MET MET A . n 
A 1 345 PHE 345 374 374 PHE PHE A . n 
A 1 346 LYS 346 375 375 LYS LYS A . n 
A 1 347 LEU 347 376 376 LEU LEU A . n 
A 1 348 VAL 348 377 377 VAL VAL A . n 
A 1 349 ALA 349 378 378 ALA ALA A . n 
A 1 350 GLN 350 379 379 GLN GLN A . n 
A 1 351 LEU 351 380 380 LEU LEU A . n 
A 1 352 TYR 352 381 381 TYR TYR A . n 
A 1 353 LYS 353 382 382 LYS LYS A . n 
A 1 354 ILE 354 383 383 ILE ILE A . n 
A 1 355 VAL 355 384 384 VAL VAL A . n 
A 1 356 PRO 356 385 385 PRO PRO A . n 
A 1 357 ASN 357 386 386 ASN ASN A . n 
A 1 358 VAL 358 387 387 VAL VAL A . n 
A 1 359 LEU 359 388 388 LEU LEU A . n 
A 1 360 LEU 360 389 389 LEU LEU A . n 
A 1 361 GLU 361 390 390 GLU GLU A . n 
A 1 362 GLN 362 391 391 GLN GLN A . n 
A 1 363 GLY 363 392 392 GLY GLY A . n 
A 1 364 LYS 364 393 393 LYS LYS A . n 
A 1 365 ALA 365 394 394 ALA ALA A . n 
A 1 366 LYS 366 395 395 LYS LYS A . n 
A 1 367 ASN 367 396 396 ASN ASN A . n 
A 1 368 PRO 368 397 397 PRO PRO A . n 
A 1 369 TRP 369 398 398 TRP TRP A . n 
A 1 370 PRO 370 399 399 PRO PRO A . n 
A 1 371 ASN 371 400 400 ASN ASN A . n 
A 1 372 VAL 372 401 401 VAL VAL A . n 
A 1 373 ASP 373 402 402 ASP ASP A . n 
A 1 374 ALA 374 403 403 ALA ALA A . n 
A 1 375 HIS 375 404 404 HIS HIS A . n 
A 1 376 SER 376 405 405 SER SER A . n 
A 1 377 GLY 377 406 406 GLY GLY A . n 
A 1 378 VAL 378 407 407 VAL VAL A . n 
A 1 379 LEU 379 408 408 LEU LEU A . n 
A 1 380 LEU 380 409 409 LEU LEU A . n 
A 1 381 GLN 381 410 410 GLN GLN A . n 
A 1 382 TYR 382 411 411 TYR TYR A . n 
A 1 383 TYR 383 412 412 TYR TYR A . n 
A 1 384 GLY 384 413 413 GLY GLY A . n 
A 1 385 MET 385 414 414 MET MET A . n 
A 1 386 THR 386 415 415 THR THR A . n 
A 1 387 GLU 387 416 416 GLU GLU A . n 
A 1 388 MET 388 417 417 MET MET A . n 
A 1 389 ASN 389 418 418 ASN ASN A . n 
A 1 390 TYR 390 419 419 TYR TYR A . n 
A 1 391 TYR 391 420 420 TYR TYR A . n 
A 1 392 THR 392 421 421 THR THR A . n 
A 1 393 VAL 393 422 422 VAL VAL A . n 
A 1 394 LEU 394 423 423 LEU LEU A . n 
A 1 395 PHE 395 424 424 PHE PHE A . n 
A 1 396 GLY 396 425 425 GLY GLY A . n 
A 1 397 VAL 397 426 426 VAL VAL A . n 
A 1 398 SER 398 427 427 SER SER A . n 
A 1 399 ARG 399 428 428 ARG ARG A . n 
A 1 400 ALA 400 429 429 ALA ALA A . n 
A 1 401 LEU 401 430 430 LEU LEU A . n 
A 1 402 GLY 402 431 431 GLY GLY A . n 
A 1 403 VAL 403 432 432 VAL VAL A . n 
A 1 404 LEU 404 433 433 LEU LEU A . n 
A 1 405 ALA 405 434 434 ALA ALA A . n 
A 1 406 GLN 406 435 435 GLN GLN A . n 
A 1 407 LEU 407 436 436 LEU LEU A . n 
A 1 408 ILE 408 437 437 ILE ILE A . n 
A 1 409 TRP 409 438 438 TRP TRP A . n 
A 1 410 SER 410 439 439 SER SER A . n 
A 1 411 ARG 411 440 440 ARG ARG A . n 
A 1 412 ALA 412 441 441 ALA ALA A . n 
A 1 413 LEU 413 442 442 LEU LEU A . n 
A 1 414 GLY 414 443 443 GLY GLY A . n 
A 1 415 PHE 415 444 444 PHE PHE A . n 
A 1 416 PRO 416 445 445 PRO PRO A . n 
A 1 417 LEU 417 446 446 LEU LEU A . n 
A 1 418 GLU 418 447 447 GLU GLU A . n 
A 1 419 ARG 419 448 448 ARG ARG A . n 
A 1 420 PRO 420 449 449 PRO PRO A . n 
A 1 421 LYS 421 450 450 LYS LYS A . n 
A 1 422 SER 422 451 451 SER SER A . n 
A 1 423 MET 423 452 452 MET MET A . n 
A 1 424 SER 424 453 453 SER SER A . n 
A 1 425 THR 425 454 454 THR THR A . n 
A 1 426 GLU 426 455 455 GLU GLU A . n 
A 1 427 GLY 427 456 456 GLY GLY A . n 
A 1 428 LEU 428 457 457 LEU LEU A . n 
A 1 429 MET 429 458 458 MET MET A . n 
A 1 430 LYS 430 459 459 LYS LYS A . n 
A 1 431 PHE 431 460 460 PHE PHE A . n 
A 1 432 VAL 432 461 461 VAL VAL A . n 
A 1 433 ASP 433 462 462 ASP ASP A . n 
A 1 434 SER 434 463 463 SER SER A . n 
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 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 COA 1  501 502 COA COA A . 
D 3 CIT 1  502 503 CIT CIT A . 
E 4 OAA 1  501 503 OAA OAA B . 
F 5 ACO 1  502 504 ACO ACO B . 
G 6 HOH 1  601 112 HOH HOH A . 
G 6 HOH 2  602 99  HOH HOH A . 
G 6 HOH 3  603 22  HOH HOH A . 
G 6 HOH 4  604 43  HOH HOH A . 
G 6 HOH 5  605 27  HOH HOH A . 
G 6 HOH 6  606 94  HOH HOH A . 
G 6 HOH 7  607 65  HOH HOH A . 
G 6 HOH 8  608 19  HOH HOH A . 
G 6 HOH 9  609 1   HOH HOH A . 
G 6 HOH 10 610 151 HOH HOH A . 
G 6 HOH 11 611 3   HOH HOH A . 
G 6 HOH 12 612 29  HOH HOH A . 
G 6 HOH 13 613 37  HOH HOH A . 
G 6 HOH 14 614 103 HOH HOH A . 
G 6 HOH 15 615 63  HOH HOH A . 
G 6 HOH 16 616 112 HOH HOH A . 
G 6 HOH 17 617 48  HOH HOH A . 
G 6 HOH 18 618 16  HOH HOH A . 
G 6 HOH 19 619 54  HOH HOH A . 
G 6 HOH 20 620 13  HOH HOH A . 
G 6 HOH 21 621 10  HOH HOH A . 
G 6 HOH 22 622 5   HOH HOH A . 
G 6 HOH 23 623 45  HOH HOH A . 
G 6 HOH 24 624 118 HOH HOH A . 
G 6 HOH 25 625 81  HOH HOH A . 
G 6 HOH 26 626 49  HOH HOH A . 
G 6 HOH 27 627 106 HOH HOH A . 
G 6 HOH 28 628 114 HOH HOH A . 
G 6 HOH 29 629 100 HOH HOH A . 
G 6 HOH 30 630 47  HOH HOH A . 
G 6 HOH 31 631 2   HOH HOH A . 
G 6 HOH 32 632 40  HOH HOH A . 
G 6 HOH 33 633 2   HOH HOH A . 
G 6 HOH 34 634 102 HOH HOH A . 
G 6 HOH 35 635 84  HOH HOH A . 
G 6 HOH 36 636 59  HOH HOH A . 
G 6 HOH 37 637 35  HOH HOH A . 
G 6 HOH 38 638 49  HOH HOH A . 
G 6 HOH 39 639 45  HOH HOH A . 
G 6 HOH 40 640 115 HOH HOH A . 
G 6 HOH 41 641 44  HOH HOH A . 
G 6 HOH 42 642 91  HOH HOH A . 
G 6 HOH 43 643 53  HOH HOH A . 
G 6 HOH 44 644 97  HOH HOH A . 
G 6 HOH 45 645 69  HOH HOH A . 
G 6 HOH 46 646 113 HOH HOH A . 
G 6 HOH 47 647 87  HOH HOH A . 
G 6 HOH 48 648 76  HOH HOH A . 
G 6 HOH 49 649 42  HOH HOH A . 
G 6 HOH 50 650 99  HOH HOH A . 
G 6 HOH 51 651 41  HOH HOH A . 
G 6 HOH 52 652 159 HOH HOH A . 
G 6 HOH 53 653 63  HOH HOH A . 
G 6 HOH 54 654 7   HOH HOH A . 
G 6 HOH 55 655 101 HOH HOH A . 
G 6 HOH 56 656 65  HOH HOH A . 
G 6 HOH 57 657 83  HOH HOH A . 
G 6 HOH 58 658 75  HOH HOH A . 
G 6 HOH 59 659 36  HOH HOH A . 
G 6 HOH 60 660 108 HOH HOH A . 
G 6 HOH 61 661 145 HOH HOH A . 
G 6 HOH 62 662 56  HOH HOH A . 
G 6 HOH 63 663 58  HOH HOH A . 
G 6 HOH 64 664 110 HOH HOH A . 
G 6 HOH 65 665 86  HOH HOH A . 
G 6 HOH 66 666 117 HOH HOH A . 
G 6 HOH 67 667 160 HOH HOH A . 
G 6 HOH 68 668 56  HOH HOH A . 
H 6 HOH 1  601 50  HOH HOH B . 
H 6 HOH 2  602 18  HOH HOH B . 
H 6 HOH 3  603 1   HOH HOH B . 
H 6 HOH 4  604 6   HOH HOH B . 
H 6 HOH 5  605 70  HOH HOH B . 
H 6 HOH 6  606 24  HOH HOH B . 
H 6 HOH 7  607 22  HOH HOH B . 
H 6 HOH 8  608 7   HOH HOH B . 
H 6 HOH 9  609 61  HOH HOH B . 
H 6 HOH 10 610 89  HOH HOH B . 
H 6 HOH 11 611 39  HOH HOH B . 
H 6 HOH 12 612 52  HOH HOH B . 
H 6 HOH 13 613 89  HOH HOH B . 
H 6 HOH 14 614 98  HOH HOH B . 
H 6 HOH 15 615 12  HOH HOH B . 
H 6 HOH 16 616 30  HOH HOH B . 
H 6 HOH 17 617 52  HOH HOH B . 
H 6 HOH 18 618 93  HOH HOH B . 
H 6 HOH 19 619 42  HOH HOH B . 
H 6 HOH 20 620 16  HOH HOH B . 
H 6 HOH 21 621 12  HOH HOH B . 
H 6 HOH 22 622 2   HOH HOH B . 
H 6 HOH 23 623 36  HOH HOH B . 
H 6 HOH 24 624 100 HOH HOH B . 
H 6 HOH 25 625 11  HOH HOH B . 
H 6 HOH 26 626 3   HOH HOH B . 
H 6 HOH 27 627 57  HOH HOH B . 
H 6 HOH 28 628 155 HOH HOH B . 
H 6 HOH 29 629 79  HOH HOH B . 
H 6 HOH 30 630 33  HOH HOH B . 
H 6 HOH 31 631 26  HOH HOH B . 
H 6 HOH 32 632 57  HOH HOH B . 
H 6 HOH 33 633 51  HOH HOH B . 
H 6 HOH 34 634 12  HOH HOH B . 
H 6 HOH 35 635 28  HOH HOH B . 
H 6 HOH 36 636 31  HOH HOH B . 
H 6 HOH 37 637 6   HOH HOH B . 
H 6 HOH 38 638 6   HOH HOH B . 
H 6 HOH 39 639 59  HOH HOH B . 
H 6 HOH 40 640 15  HOH HOH B . 
H 6 HOH 41 641 32  HOH HOH B . 
H 6 HOH 42 642 66  HOH HOH B . 
H 6 HOH 43 643 142 HOH HOH B . 
H 6 HOH 44 644 23  HOH HOH B . 
H 6 HOH 45 645 25  HOH HOH B . 
H 6 HOH 46 646 73  HOH HOH B . 
H 6 HOH 47 647 66  HOH HOH B . 
H 6 HOH 48 648 27  HOH HOH B . 
H 6 HOH 49 649 72  HOH HOH B . 
H 6 HOH 50 650 41  HOH HOH B . 
H 6 HOH 51 651 18  HOH HOH B . 
H 6 HOH 52 652 68  HOH HOH B . 
H 6 HOH 53 653 74  HOH HOH B . 
H 6 HOH 54 654 101 HOH HOH B . 
H 6 HOH 55 655 10  HOH HOH B . 
H 6 HOH 56 656 43  HOH HOH B . 
H 6 HOH 57 657 98  HOH HOH B . 
H 6 HOH 58 658 43  HOH HOH B . 
H 6 HOH 59 659 34  HOH HOH B . 
H 6 HOH 60 660 77  HOH HOH B . 
H 6 HOH 61 661 35  HOH HOH B . 
H 6 HOH 62 662 44  HOH HOH B . 
H 6 HOH 63 663 33  HOH HOH B . 
H 6 HOH 64 664 17  HOH HOH B . 
H 6 HOH 65 665 20  HOH HOH B . 
H 6 HOH 66 666 37  HOH HOH B . 
H 6 HOH 67 667 24  HOH HOH B . 
H 6 HOH 68 668 92  HOH HOH B . 
H 6 HOH 69 669 14  HOH HOH B . 
H 6 HOH 70 670 82  HOH HOH B . 
H 6 HOH 71 671 104 HOH HOH B . 
H 6 HOH 72 672 9   HOH HOH B . 
H 6 HOH 73 673 119 HOH HOH B . 
H 6 HOH 74 674 38  HOH HOH B . 
# 
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 ? CG  ? A LYS 186 CG  
2  1 Y 1 A LYS 215 ? CD  ? A LYS 186 CD  
3  1 Y 1 A LYS 215 ? CE  ? A LYS 186 CE  
4  1 Y 1 A LYS 215 ? NZ  ? A LYS 186 NZ  
5  1 Y 1 A LYS 317 ? CG  ? A LYS 288 CG  
6  1 Y 1 A LYS 317 ? CD  ? A LYS 288 CD  
7  1 Y 1 A LYS 317 ? CE  ? A LYS 288 CE  
8  1 Y 1 A LYS 317 ? NZ  ? A LYS 288 NZ  
9  1 Y 1 B LYS 109 ? CG  ? B LYS 80  CG  
10 1 Y 1 B LYS 109 ? CD  ? B LYS 80  CD  
11 1 Y 1 B LYS 109 ? CE  ? B LYS 80  CE  
12 1 Y 1 B LYS 109 ? NZ  ? B LYS 80  NZ  
13 1 Y 1 B LYS 215 ? NZ  ? B LYS 186 NZ  
14 1 Y 1 B LYS 317 ? CG  ? B LYS 288 CG  
15 1 Y 1 B LYS 317 ? CD  ? B LYS 288 CD  
16 1 Y 1 B LYS 317 ? CE  ? B LYS 288 CE  
17 1 Y 1 B LYS 317 ? NZ  ? B LYS 288 NZ  
18 1 Y 1 B LYS 321 ? CG  ? B LYS 292 CG  
19 1 Y 1 B LYS 321 ? CD  ? B LYS 292 CD  
20 1 Y 1 B LYS 321 ? CE  ? B LYS 292 CE  
21 1 Y 1 B LYS 321 ? NZ  ? B LYS 292 NZ  
22 1 Y 1 B ARG 329 ? CG  ? B ARG 300 CG  
23 1 Y 1 B ARG 329 ? CD  ? B ARG 300 CD  
24 1 Y 1 B ARG 329 ? NE  ? B ARG 300 NE  
25 1 Y 1 B ARG 329 ? CZ  ? B ARG 300 CZ  
26 1 Y 1 B ARG 329 ? NH1 ? B ARG 300 NH1 
27 1 Y 1 B ARG 329 ? NH2 ? B ARG 300 NH2 
28 1 Y 1 B LYS 393 ? CG  ? B LYS 364 CG  
29 1 Y 1 B LYS 393 ? CD  ? B LYS 364 CD  
30 1 Y 1 B LYS 393 ? CE  ? B LYS 364 CE  
31 1 Y 1 B LYS 393 ? NZ  ? B LYS 364 NZ  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? 5.8.0419 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .        4 
# 
_cell.angle_alpha                  102.52 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   98.23 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  118.76 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8ZW1 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     57.523 
_cell.length_a_esd                 ? 
_cell.length_b                     59.789 
_cell.length_b_esd                 ? 
_cell.length_c                     72.582 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        2 
_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                         8ZW1 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8ZW1 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.10 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          41.50 
_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         2023-10-26 
_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                                       8ZW1 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.03 
_reflns.d_resolution_low                               67.83 
_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                                     48136 
_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                           94.2 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                2.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          1.6 
_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                                0.151 
_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                                   0.978 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.114 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.03 
_reflns_shell.d_res_low                                     2.14 
_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                             7190 
_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                               1.134 
_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                                  0.223 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.841 
_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]                            -0.00 
_refine.aniso_B[1][2]                            -0.01 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            -0.00 
_refine.aniso_B[2][3]                            0.01 
_refine.aniso_B[3][3]                            0.00 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               48.895 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.940 
_refine.correlation_coeff_Fo_to_Fc_free          0.894 
_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                                 8ZW1 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.10 
_refine.ls_d_res_low                             41.12 
_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                     41416 
_refine.ls_number_reflns_R_free                  2024 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    93.89 
_refine.ls_percent_reflns_R_free                 4.7 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.23601 
_refine.ls_R_factor_R_free                       0.29869 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.23298 
_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                       0.374 
_refine.pdbx_overall_ESU_R_Free                  0.269 
_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                             16.362 
_refine.overall_SU_ML                            0.409 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.10 
_refine_hist.d_res_low                        41.12 
_refine_hist.number_atoms_solvent             142 
_refine_hist.number_atoms_total               7076 
_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        6813 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         121 
_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' ? 0.003  0.012  7114  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  6637  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.118  1.827  9683  ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.398  1.743  15285 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.201  5.000  870   ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 6.495  5.000  43    ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 13.539 10.000 1163  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.054  0.200  1067  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.004  0.020  8333  ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  1613  ? 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' ? 2.564  4.896  3475  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.562  4.895  3474  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 4.170  8.800  4340  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 4.170  8.801  4341  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 2.538  5.241  3639  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.537  5.242  3640  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 4.249  9.557  5342  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 7.641  49.41  8413  ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 7.637  49.43  8402  ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.100 
_refine_ls_shell.d_res_low                        2.154 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             137 
_refine_ls_shell.number_reflns_R_work             3161 
_refine_ls_shell.percent_reflns_obs               95.76 
_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                  0.380 
_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                  0.365 
# 
_struct.entry_id                     8ZW1 
_struct.title                        'citrate synthases complexed with oxaloacetate and acetyl-CoA' 
_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        8ZW1 
_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 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 5 ? 
G N N 6 ? 
H N N 6 ? 
# 
_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 8ZW1 A 1 ? 434 ? O75390 30 ? 463 ? 30 463 
2 1 8ZW1 B 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   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 12110 ? 
1 MORE         -53   ? 
1 'SSA (A^2)'  29520 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASN A 3   ? GLY A 27  ? ASN A 32  GLY A 56  1 ? 25 
HELX_P HELX_P2  AA2 VAL A 36  ? GLY A 41  ? VAL A 65  GLY A 70  1 ? 6  
HELX_P HELX_P3  AA3 ILE A 69  ? LEU A 76  ? ILE A 98  LEU A 105 1 ? 8  
HELX_P HELX_P4  AA4 LEU A 86  ? GLY A 97  ? LEU A 115 GLY A 126 1 ? 12 
HELX_P HELX_P5  AA5 THR A 101 ? ARG A 115 ? THR A 130 ARG A 144 1 ? 15 
HELX_P HELX_P6  AA6 PRO A 119 ? ASN A 128 ? PRO A 148 ASN A 157 1 ? 10 
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 GLY A 269 ? LEU A 274 ? GLY A 298 LEU A 303 1 ? 6  
HELX_P HELX_P17 AB8 LEU A 274 ? VAL A 290 ? LEU A 303 VAL A 319 1 ? 17 
HELX_P HELX_P18 AB9 SER A 295 ? SER A 309 ? SER A 324 SER A 338 1 ? 15 
HELX_P HELX_P19 AC1 ASP A 325 ? LEU A 339 ? ASP A 354 LEU A 368 1 ? 15 
HELX_P HELX_P20 AC2 ASP A 342 ? GLY A 363 ? ASP A 371 GLY A 392 1 ? 22 
HELX_P HELX_P21 AC3 VAL A 372 ? TYR A 383 ? VAL A 401 TYR A 412 1 ? 12 
HELX_P HELX_P22 AC4 GLU A 387 ? ASN A 389 ? GLU A 416 ASN A 418 5 ? 3  
HELX_P HELX_P23 AC5 TYR A 390 ? LEU A 413 ? TYR A 419 LEU A 442 1 ? 24 
HELX_P HELX_P24 AC6 SER A 424 ? SER A 434 ? SER A 453 SER A 463 1 ? 11 
HELX_P HELX_P25 AC7 ASN B 3   ? ASP B 10  ? ASN B 32  ASP B 39  1 ? 8  
HELX_P HELX_P26 AC8 LEU B 11  ? GLY B 27  ? LEU B 40  GLY B 56  1 ? 17 
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 ? ASN B 128 ? PRO B 148 ASN B 157 1 ? 10 
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 ? SER B 251 ? ASN B 269 SER B 280 1 ? 12 
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 ? VAL B 290 ? LEU B 303 VAL B 319 1 ? 17 
HELX_P HELX_P42 AE6 ASP B 296 ? LEU B 307 ? ASP B 325 LEU B 336 1 ? 12 
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 ? GLY B 363 ? ASP B 371 GLY B 392 1 ? 22 
HELX_P HELX_P45 AE9 VAL B 372 ? TYR B 383 ? VAL B 401 TYR B 412 1 ? 12 
HELX_P HELX_P46 AF1 GLU B 387 ? ASN B 389 ? GLU B 416 ASN B 418 5 ? 3  
HELX_P HELX_P47 AF2 TYR B 390 ? LEU B 413 ? TYR B 419 LEU B 442 1 ? 24 
HELX_P HELX_P48 AF3 SER B 424 ? ASP B 433 ? SER B 453 ASP B 462 1 ? 10 
# 
_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 ? 
# 
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 
# 
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  
# 
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 VAL A 55  ? N VAL A 84  O ARG A 63  ? O ARG A 92  
AA3 2 3 N PHE A 64  ? N PHE A 93  O PHE A 67  ? O PHE A 96  
AA4 1 2 N LYS A 421 ? N LYS A 450 O GLY B 48  ? O GLY B 77  
AA5 1 2 N VAL B 55  ? N VAL B 84  O ARG B 63  ? O ARG B 92  
# 
_pdbx_entry_details.entry_id                   8ZW1 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ARG A 222 ? ? -143.61 35.26   
2  1 THR A 247 ? ? -146.68 43.33   
3  1 HIS A 265 ? ? -162.98 51.12   
4  1 GLU A 266 ? ? 83.16   179.38  
5  1 GLN A 316 ? ? -100.52 45.16   
6  1 LYS A 317 ? ? -149.41 -43.13  
7  1 VAL A 349 ? ? -140.09 -29.29  
8  1 LEU A 368 ? ? -160.79 58.20   
9  1 ILE A 383 ? ? -93.93  -61.72  
10 1 ARG A 448 ? ? -160.61 77.44   
11 1 ASP A 462 ? ? -59.38  -70.09  
12 1 ARG B 94  ? ? 34.77   46.10   
13 1 ASN B 157 ? ? -102.80 43.29   
14 1 ARG B 222 ? ? -144.53 39.93   
15 1 THR B 247 ? ? -141.60 52.50   
16 1 HIS B 265 ? ? -159.49 61.22   
17 1 GLU B 266 ? ? 71.25   177.48  
18 1 HIS B 301 ? ? -115.48 -104.25 
19 1 SER B 324 ? ? -85.09  -128.47 
20 1 VAL B 349 ? ? -142.29 -40.37  
21 1 THR B 353 ? ? -38.46  131.89  
22 1 ALA B 394 ? ? -170.75 -177.37 
23 1 LYS B 395 ? ? -135.70 -45.45  
24 1 LEU B 446 ? ? -39.84  124.93  
25 1 ARG B 448 ? ? -159.60 73.73   
26 1 ASP B 462 ? ? -78.22  45.79   
# 
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 B 73  ? ? 0.299 'SIDE CHAIN' 
2 1 ARG B 428 ? ? 0.090 'SIDE CHAIN' 
# 
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 
ACO N1A  N Y N 1   
ACO C2A  C Y N 2   
ACO N3A  N Y N 3   
ACO C4A  C Y N 4   
ACO C5A  C Y N 5   
ACO C6A  C Y N 6   
ACO N6A  N N N 7   
ACO N7A  N Y N 8   
ACO C8A  C Y N 9   
ACO N9A  N Y N 10  
ACO C1B  C N R 11  
ACO C2B  C N R 12  
ACO O2B  O N N 13  
ACO C3B  C N S 14  
ACO O3B  O N N 15  
ACO P3B  P N N 16  
ACO O7A  O N N 17  
ACO O8A  O N N 18  
ACO O9A  O N N 19  
ACO C4B  C N R 20  
ACO O4B  O N N 21  
ACO C5B  C N N 22  
ACO O5B  O N N 23  
ACO P1A  P N S 24  
ACO O1A  O N N 25  
ACO O2A  O N N 26  
ACO O3A  O N N 27  
ACO P2A  P N S 28  
ACO O4A  O N N 29  
ACO O5A  O N N 30  
ACO O6A  O N N 31  
ACO CBP  C N N 32  
ACO CCP  C N N 33  
ACO CDP  C N N 34  
ACO CEP  C N N 35  
ACO CAP  C N R 36  
ACO OAP  O N N 37  
ACO C9P  C N N 38  
ACO O9P  O N N 39  
ACO N8P  N N N 40  
ACO C7P  C N N 41  
ACO C6P  C N N 42  
ACO C5P  C N N 43  
ACO O5P  O N N 44  
ACO N4P  N N N 45  
ACO C3P  C N N 46  
ACO C2P  C N N 47  
ACO S1P  S N N 48  
ACO C    C N N 49  
ACO O    O N N 50  
ACO CH3  C N N 51  
ACO H2A  H N N 52  
ACO H61A H N N 53  
ACO H62A H N N 54  
ACO H8A  H N N 55  
ACO H1B  H N N 56  
ACO H2B  H N N 57  
ACO HO2A H N N 58  
ACO H3B  H N N 59  
ACO HOA8 H N N 60  
ACO HOA9 H N N 61  
ACO H4B  H N N 62  
ACO H51A H N N 63  
ACO H52A H N N 64  
ACO HOA2 H N N 65  
ACO HOA5 H N N 66  
ACO H121 H N N 67  
ACO H122 H N N 68  
ACO H131 H N N 69  
ACO H132 H N N 70  
ACO H133 H N N 71  
ACO H141 H N N 72  
ACO H142 H N N 73  
ACO H143 H N N 74  
ACO H10  H N N 75  
ACO HO1  H N N 76  
ACO HN8  H N N 77  
ACO H71  H N N 78  
ACO H72  H N N 79  
ACO H61  H N N 80  
ACO H62  H N N 81  
ACO HN4  H N N 82  
ACO H31  H N N 83  
ACO H32  H N N 84  
ACO H21  H N N 85  
ACO H22  H N N 86  
ACO HH31 H N N 87  
ACO HH32 H N N 88  
ACO HH33 H N N 89  
ALA N    N N N 90  
ALA CA   C N S 91  
ALA C    C N N 92  
ALA O    O N N 93  
ALA CB   C N N 94  
ALA OXT  O N N 95  
ALA H    H N N 96  
ALA H2   H N N 97  
ALA HA   H N N 98  
ALA HB1  H N N 99  
ALA HB2  H N N 100 
ALA HB3  H N N 101 
ALA HXT  H N N 102 
ARG N    N N N 103 
ARG CA   C N S 104 
ARG C    C N N 105 
ARG O    O N N 106 
ARG CB   C N N 107 
ARG CG   C N N 108 
ARG CD   C N N 109 
ARG NE   N N N 110 
ARG CZ   C N N 111 
ARG NH1  N N N 112 
ARG NH2  N N N 113 
ARG OXT  O N N 114 
ARG H    H N N 115 
ARG H2   H N N 116 
ARG HA   H N N 117 
ARG HB2  H N N 118 
ARG HB3  H N N 119 
ARG HG2  H N N 120 
ARG HG3  H N N 121 
ARG HD2  H N N 122 
ARG HD3  H N N 123 
ARG HE   H N N 124 
ARG HH11 H N N 125 
ARG HH12 H N N 126 
ARG HH21 H N N 127 
ARG HH22 H N N 128 
ARG HXT  H N N 129 
ASN N    N N N 130 
ASN CA   C N S 131 
ASN C    C N N 132 
ASN O    O N N 133 
ASN CB   C N N 134 
ASN CG   C N N 135 
ASN OD1  O N N 136 
ASN ND2  N N N 137 
ASN OXT  O N N 138 
ASN H    H N N 139 
ASN H2   H N N 140 
ASN HA   H N N 141 
ASN HB2  H N N 142 
ASN HB3  H N N 143 
ASN HD21 H N N 144 
ASN HD22 H N N 145 
ASN HXT  H N N 146 
ASP N    N N N 147 
ASP CA   C N S 148 
ASP C    C N N 149 
ASP O    O N N 150 
ASP CB   C N N 151 
ASP CG   C N N 152 
ASP OD1  O N N 153 
ASP OD2  O N N 154 
ASP OXT  O N N 155 
ASP H    H N N 156 
ASP H2   H N N 157 
ASP HA   H N N 158 
ASP HB2  H N N 159 
ASP HB3  H N N 160 
ASP HD2  H N N 161 
ASP HXT  H N N 162 
CIT C1   C N N 163 
CIT O1   O N N 164 
CIT O2   O N N 165 
CIT C2   C N N 166 
CIT C3   C N N 167 
CIT O7   O N N 168 
CIT C4   C N N 169 
CIT C5   C N N 170 
CIT O3   O N N 171 
CIT O4   O N N 172 
CIT C6   C N N 173 
CIT O5   O N N 174 
CIT O6   O N N 175 
CIT HO2  H N N 176 
CIT H21  H N N 177 
CIT H22  H N N 178 
CIT HO7  H N N 179 
CIT H41  H N N 180 
CIT H42  H N N 181 
CIT HO4  H N N 182 
CIT HO6  H N N 183 
COA N1A  N Y N 184 
COA C2A  C Y N 185 
COA N3A  N Y N 186 
COA C4A  C Y N 187 
COA C5A  C Y N 188 
COA C6A  C Y N 189 
COA N6A  N N N 190 
COA N7A  N Y N 191 
COA C8A  C Y N 192 
COA N9A  N Y N 193 
COA C1B  C N R 194 
COA C2B  C N R 195 
COA O2B  O N N 196 
COA C3B  C N S 197 
COA O3B  O N N 198 
COA P3B  P N N 199 
COA O7A  O N N 200 
COA O8A  O N N 201 
COA O9A  O N N 202 
COA C4B  C N R 203 
COA O4B  O N N 204 
COA C5B  C N N 205 
COA O5B  O N N 206 
COA P1A  P N S 207 
COA O1A  O N N 208 
COA O2A  O N N 209 
COA O3A  O N N 210 
COA P2A  P N S 211 
COA O4A  O N N 212 
COA O5A  O N N 213 
COA O6A  O N N 214 
COA CBP  C N N 215 
COA CCP  C N N 216 
COA CDP  C N N 217 
COA CEP  C N N 218 
COA CAP  C N R 219 
COA OAP  O N N 220 
COA C9P  C N N 221 
COA O9P  O N N 222 
COA N8P  N N N 223 
COA C7P  C N N 224 
COA C6P  C N N 225 
COA C5P  C N N 226 
COA O5P  O N N 227 
COA N4P  N N N 228 
COA C3P  C N N 229 
COA C2P  C N N 230 
COA S1P  S N N 231 
COA H2A  H N N 232 
COA H61A H N N 233 
COA H62A H N N 234 
COA H8A  H N N 235 
COA H1B  H N N 236 
COA H2B  H N N 237 
COA HO2A H N N 238 
COA H3B  H N N 239 
COA HOA8 H N N 240 
COA HOA9 H N N 241 
COA H4B  H N N 242 
COA H51A H N N 243 
COA H52A H N N 244 
COA HOA2 H N N 245 
COA HOA5 H N N 246 
COA H121 H N N 247 
COA H122 H N N 248 
COA H131 H N N 249 
COA H132 H N N 250 
COA H133 H N N 251 
COA H141 H N N 252 
COA H142 H N N 253 
COA H143 H N N 254 
COA H10  H N N 255 
COA HO1  H N N 256 
COA HN8  H N N 257 
COA H71  H N N 258 
COA H72  H N N 259 
COA H61  H N N 260 
COA H62  H N N 261 
COA HN4  H N N 262 
COA H31  H N N 263 
COA H32  H N N 264 
COA H21  H N N 265 
COA H22  H N N 266 
COA HS1  H N N 267 
CYS N    N N N 268 
CYS CA   C N R 269 
CYS C    C N N 270 
CYS O    O N N 271 
CYS CB   C N N 272 
CYS SG   S N N 273 
CYS OXT  O N N 274 
CYS H    H N N 275 
CYS H2   H N N 276 
CYS HA   H N N 277 
CYS HB2  H N N 278 
CYS HB3  H N N 279 
CYS HG   H N N 280 
CYS HXT  H N N 281 
GLN N    N N N 282 
GLN CA   C N S 283 
GLN C    C N N 284 
GLN O    O N N 285 
GLN CB   C N N 286 
GLN CG   C N N 287 
GLN CD   C N N 288 
GLN OE1  O N N 289 
GLN NE2  N N N 290 
GLN OXT  O N N 291 
GLN H    H N N 292 
GLN H2   H N N 293 
GLN HA   H N N 294 
GLN HB2  H N N 295 
GLN HB3  H N N 296 
GLN HG2  H N N 297 
GLN HG3  H N N 298 
GLN HE21 H N N 299 
GLN HE22 H N N 300 
GLN HXT  H N N 301 
GLU N    N N N 302 
GLU CA   C N S 303 
GLU C    C N N 304 
GLU O    O N N 305 
GLU CB   C N N 306 
GLU CG   C N N 307 
GLU CD   C N N 308 
GLU OE1  O N N 309 
GLU OE2  O N N 310 
GLU OXT  O N N 311 
GLU H    H N N 312 
GLU H2   H N N 313 
GLU HA   H N N 314 
GLU HB2  H N N 315 
GLU HB3  H N N 316 
GLU HG2  H N N 317 
GLU HG3  H N N 318 
GLU HE2  H N N 319 
GLU HXT  H N N 320 
GLY N    N N N 321 
GLY CA   C N N 322 
GLY C    C N N 323 
GLY O    O N N 324 
GLY OXT  O N N 325 
GLY H    H N N 326 
GLY H2   H N N 327 
GLY HA2  H N N 328 
GLY HA3  H N N 329 
GLY HXT  H N N 330 
HIS N    N N N 331 
HIS CA   C N S 332 
HIS C    C N N 333 
HIS O    O N N 334 
HIS CB   C N N 335 
HIS CG   C Y N 336 
HIS ND1  N Y N 337 
HIS CD2  C Y N 338 
HIS CE1  C Y N 339 
HIS NE2  N Y N 340 
HIS OXT  O N N 341 
HIS H    H N N 342 
HIS H2   H N N 343 
HIS HA   H N N 344 
HIS HB2  H N N 345 
HIS HB3  H N N 346 
HIS HD1  H N N 347 
HIS HD2  H N N 348 
HIS HE1  H N N 349 
HIS HE2  H N N 350 
HIS HXT  H N N 351 
HOH O    O N N 352 
HOH H1   H N N 353 
HOH H2   H N N 354 
ILE N    N N N 355 
ILE CA   C N S 356 
ILE C    C N N 357 
ILE O    O N N 358 
ILE CB   C N S 359 
ILE CG1  C N N 360 
ILE CG2  C N N 361 
ILE CD1  C N N 362 
ILE OXT  O N N 363 
ILE H    H N N 364 
ILE H2   H N N 365 
ILE HA   H N N 366 
ILE HB   H N N 367 
ILE HG12 H N N 368 
ILE HG13 H N N 369 
ILE HG21 H N N 370 
ILE HG22 H N N 371 
ILE HG23 H N N 372 
ILE HD11 H N N 373 
ILE HD12 H N N 374 
ILE HD13 H N N 375 
ILE HXT  H N N 376 
LEU N    N N N 377 
LEU CA   C N S 378 
LEU C    C N N 379 
LEU O    O N N 380 
LEU CB   C N N 381 
LEU CG   C N N 382 
LEU CD1  C N N 383 
LEU CD2  C N N 384 
LEU OXT  O N N 385 
LEU H    H N N 386 
LEU H2   H N N 387 
LEU HA   H N N 388 
LEU HB2  H N N 389 
LEU HB3  H N N 390 
LEU HG   H N N 391 
LEU HD11 H N N 392 
LEU HD12 H N N 393 
LEU HD13 H N N 394 
LEU HD21 H N N 395 
LEU HD22 H N N 396 
LEU HD23 H N N 397 
LEU HXT  H N N 398 
LYS N    N N N 399 
LYS CA   C N S 400 
LYS C    C N N 401 
LYS O    O N N 402 
LYS CB   C N N 403 
LYS CG   C N N 404 
LYS CD   C N N 405 
LYS CE   C N N 406 
LYS NZ   N N N 407 
LYS OXT  O N N 408 
LYS H    H N N 409 
LYS H2   H N N 410 
LYS HA   H N N 411 
LYS HB2  H N N 412 
LYS HB3  H N N 413 
LYS HG2  H N N 414 
LYS HG3  H N N 415 
LYS HD2  H N N 416 
LYS HD3  H N N 417 
LYS HE2  H N N 418 
LYS HE3  H N N 419 
LYS HZ1  H N N 420 
LYS HZ2  H N N 421 
LYS HZ3  H N N 422 
LYS HXT  H N N 423 
MET N    N N N 424 
MET CA   C N S 425 
MET C    C N N 426 
MET O    O N N 427 
MET CB   C N N 428 
MET CG   C N N 429 
MET SD   S N N 430 
MET CE   C N N 431 
MET OXT  O N N 432 
MET H    H N N 433 
MET H2   H N N 434 
MET HA   H N N 435 
MET HB2  H N N 436 
MET HB3  H N N 437 
MET HG2  H N N 438 
MET HG3  H N N 439 
MET HE1  H N N 440 
MET HE2  H N N 441 
MET HE3  H N N 442 
MET HXT  H N N 443 
OAA O1   O N N 444 
OAA O2   O N N 445 
OAA O4   O N N 446 
OAA O5   O N N 447 
OAA O3   O N N 448 
OAA C1   C N N 449 
OAA C2   C N N 450 
OAA C3   C N N 451 
OAA C4   C N N 452 
OAA HO5  H N N 453 
OAA H21  H N N 454 
OAA H22  H N N 455 
PHE N    N N N 456 
PHE CA   C N S 457 
PHE C    C N N 458 
PHE O    O N N 459 
PHE CB   C N N 460 
PHE CG   C Y N 461 
PHE CD1  C Y N 462 
PHE CD2  C Y N 463 
PHE CE1  C Y N 464 
PHE CE2  C Y N 465 
PHE CZ   C Y N 466 
PHE OXT  O N N 467 
PHE H    H N N 468 
PHE H2   H N N 469 
PHE HA   H N N 470 
PHE HB2  H N N 471 
PHE HB3  H N N 472 
PHE HD1  H N N 473 
PHE HD2  H N N 474 
PHE HE1  H N N 475 
PHE HE2  H N N 476 
PHE HZ   H N N 477 
PHE HXT  H N N 478 
PRO N    N N N 479 
PRO CA   C N S 480 
PRO C    C N N 481 
PRO O    O N N 482 
PRO CB   C N N 483 
PRO CG   C N N 484 
PRO CD   C N N 485 
PRO OXT  O N N 486 
PRO H    H N N 487 
PRO HA   H N N 488 
PRO HB2  H N N 489 
PRO HB3  H N N 490 
PRO HG2  H N N 491 
PRO HG3  H N N 492 
PRO HD2  H N N 493 
PRO HD3  H N N 494 
PRO HXT  H N N 495 
SER N    N N N 496 
SER CA   C N S 497 
SER C    C N N 498 
SER O    O N N 499 
SER CB   C N N 500 
SER OG   O N N 501 
SER OXT  O N N 502 
SER H    H N N 503 
SER H2   H N N 504 
SER HA   H N N 505 
SER HB2  H N N 506 
SER HB3  H N N 507 
SER HG   H N N 508 
SER HXT  H N N 509 
THR N    N N N 510 
THR CA   C N S 511 
THR C    C N N 512 
THR O    O N N 513 
THR CB   C N R 514 
THR OG1  O N N 515 
THR CG2  C N N 516 
THR OXT  O N N 517 
THR H    H N N 518 
THR H2   H N N 519 
THR HA   H N N 520 
THR HB   H N N 521 
THR HG1  H N N 522 
THR HG21 H N N 523 
THR HG22 H N N 524 
THR HG23 H N N 525 
THR HXT  H N N 526 
TRP N    N N N 527 
TRP CA   C N S 528 
TRP C    C N N 529 
TRP O    O N N 530 
TRP CB   C N N 531 
TRP CG   C Y N 532 
TRP CD1  C Y N 533 
TRP CD2  C Y N 534 
TRP NE1  N Y N 535 
TRP CE2  C Y N 536 
TRP CE3  C Y N 537 
TRP CZ2  C Y N 538 
TRP CZ3  C Y N 539 
TRP CH2  C Y N 540 
TRP OXT  O N N 541 
TRP H    H N N 542 
TRP H2   H N N 543 
TRP HA   H N N 544 
TRP HB2  H N N 545 
TRP HB3  H N N 546 
TRP HD1  H N N 547 
TRP HE1  H N N 548 
TRP HE3  H N N 549 
TRP HZ2  H N N 550 
TRP HZ3  H N N 551 
TRP HH2  H N N 552 
TRP HXT  H N N 553 
TYR N    N N N 554 
TYR CA   C N S 555 
TYR C    C N N 556 
TYR O    O N N 557 
TYR CB   C N N 558 
TYR CG   C Y N 559 
TYR CD1  C Y N 560 
TYR CD2  C Y N 561 
TYR CE1  C Y N 562 
TYR CE2  C Y N 563 
TYR CZ   C Y N 564 
TYR OH   O N N 565 
TYR OXT  O N N 566 
TYR H    H N N 567 
TYR H2   H N N 568 
TYR HA   H N N 569 
TYR HB2  H N N 570 
TYR HB3  H N N 571 
TYR HD1  H N N 572 
TYR HD2  H N N 573 
TYR HE1  H N N 574 
TYR HE2  H N N 575 
TYR HH   H N N 576 
TYR HXT  H N N 577 
VAL N    N N N 578 
VAL CA   C N S 579 
VAL C    C N N 580 
VAL O    O N N 581 
VAL CB   C N N 582 
VAL CG1  C N N 583 
VAL CG2  C N N 584 
VAL OXT  O N N 585 
VAL H    H N N 586 
VAL H2   H N N 587 
VAL HA   H N N 588 
VAL HB   H N N 589 
VAL HG11 H N N 590 
VAL HG12 H N N 591 
VAL HG13 H N N 592 
VAL HG21 H N N 593 
VAL HG22 H N N 594 
VAL HG23 H N N 595 
VAL HXT  H N N 596 
# 
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 
ACO N1A C2A  sing Y N 1   
ACO N1A C6A  doub Y N 2   
ACO C2A N3A  doub Y N 3   
ACO C2A H2A  sing N N 4   
ACO N3A C4A  sing Y N 5   
ACO C4A C5A  doub Y N 6   
ACO C4A N9A  sing Y N 7   
ACO C5A C6A  sing Y N 8   
ACO C5A N7A  sing Y N 9   
ACO C6A N6A  sing N N 10  
ACO N6A H61A sing N N 11  
ACO N6A H62A sing N N 12  
ACO N7A C8A  doub Y N 13  
ACO C8A N9A  sing Y N 14  
ACO C8A H8A  sing N N 15  
ACO N9A C1B  sing N N 16  
ACO C1B C2B  sing N N 17  
ACO C1B O4B  sing N N 18  
ACO C1B H1B  sing N N 19  
ACO C2B O2B  sing N N 20  
ACO C2B C3B  sing N N 21  
ACO C2B H2B  sing N N 22  
ACO O2B HO2A sing N N 23  
ACO C3B O3B  sing N N 24  
ACO C3B C4B  sing N N 25  
ACO C3B H3B  sing N N 26  
ACO O3B P3B  sing N N 27  
ACO P3B O7A  doub N N 28  
ACO P3B O8A  sing N N 29  
ACO P3B O9A  sing N N 30  
ACO O8A HOA8 sing N N 31  
ACO O9A HOA9 sing N N 32  
ACO C4B O4B  sing N N 33  
ACO C4B C5B  sing N N 34  
ACO C4B H4B  sing N N 35  
ACO C5B O5B  sing N N 36  
ACO C5B H51A sing N N 37  
ACO C5B H52A sing N N 38  
ACO O5B P1A  sing N N 39  
ACO P1A O1A  doub N N 40  
ACO P1A O2A  sing N N 41  
ACO P1A O3A  sing N N 42  
ACO O2A HOA2 sing N N 43  
ACO O3A P2A  sing N N 44  
ACO P2A O4A  doub N N 45  
ACO P2A O5A  sing N N 46  
ACO P2A O6A  sing N N 47  
ACO O5A HOA5 sing N N 48  
ACO O6A CCP  sing N N 49  
ACO CBP CCP  sing N N 50  
ACO CBP CDP  sing N N 51  
ACO CBP CEP  sing N N 52  
ACO CBP CAP  sing N N 53  
ACO CCP H121 sing N N 54  
ACO CCP H122 sing N N 55  
ACO CDP H131 sing N N 56  
ACO CDP H132 sing N N 57  
ACO CDP H133 sing N N 58  
ACO CEP H141 sing N N 59  
ACO CEP H142 sing N N 60  
ACO CEP H143 sing N N 61  
ACO CAP OAP  sing N N 62  
ACO CAP C9P  sing N N 63  
ACO CAP H10  sing N N 64  
ACO OAP HO1  sing N N 65  
ACO C9P O9P  doub N N 66  
ACO C9P N8P  sing N N 67  
ACO N8P C7P  sing N N 68  
ACO N8P HN8  sing N N 69  
ACO C7P C6P  sing N N 70  
ACO C7P H71  sing N N 71  
ACO C7P H72  sing N N 72  
ACO C6P C5P  sing N N 73  
ACO C6P H61  sing N N 74  
ACO C6P H62  sing N N 75  
ACO C5P O5P  doub N N 76  
ACO C5P N4P  sing N N 77  
ACO N4P C3P  sing N N 78  
ACO N4P HN4  sing N N 79  
ACO C3P C2P  sing N N 80  
ACO C3P H31  sing N N 81  
ACO C3P H32  sing N N 82  
ACO C2P S1P  sing N N 83  
ACO C2P H21  sing N N 84  
ACO C2P H22  sing N N 85  
ACO S1P C    sing N N 86  
ACO C   O    doub N N 87  
ACO C   CH3  sing N N 88  
ACO CH3 HH31 sing N N 89  
ACO CH3 HH32 sing N N 90  
ACO CH3 HH33 sing N N 91  
ALA N   CA   sing N N 92  
ALA N   H    sing N N 93  
ALA N   H2   sing N N 94  
ALA CA  C    sing N N 95  
ALA CA  CB   sing N N 96  
ALA CA  HA   sing N N 97  
ALA C   O    doub N N 98  
ALA C   OXT  sing N N 99  
ALA CB  HB1  sing N N 100 
ALA CB  HB2  sing N N 101 
ALA CB  HB3  sing N N 102 
ALA OXT HXT  sing N N 103 
ARG N   CA   sing N N 104 
ARG N   H    sing N N 105 
ARG N   H2   sing N N 106 
ARG CA  C    sing N N 107 
ARG CA  CB   sing N N 108 
ARG CA  HA   sing N N 109 
ARG C   O    doub N N 110 
ARG C   OXT  sing N N 111 
ARG CB  CG   sing N N 112 
ARG CB  HB2  sing N N 113 
ARG CB  HB3  sing N N 114 
ARG CG  CD   sing N N 115 
ARG CG  HG2  sing N N 116 
ARG CG  HG3  sing N N 117 
ARG CD  NE   sing N N 118 
ARG CD  HD2  sing N N 119 
ARG CD  HD3  sing N N 120 
ARG NE  CZ   sing N N 121 
ARG NE  HE   sing N N 122 
ARG CZ  NH1  sing N N 123 
ARG CZ  NH2  doub N N 124 
ARG NH1 HH11 sing N N 125 
ARG NH1 HH12 sing N N 126 
ARG NH2 HH21 sing N N 127 
ARG NH2 HH22 sing N N 128 
ARG OXT HXT  sing N N 129 
ASN N   CA   sing N N 130 
ASN N   H    sing N N 131 
ASN N   H2   sing N N 132 
ASN CA  C    sing N N 133 
ASN CA  CB   sing N N 134 
ASN CA  HA   sing N N 135 
ASN C   O    doub N N 136 
ASN C   OXT  sing N N 137 
ASN CB  CG   sing N N 138 
ASN CB  HB2  sing N N 139 
ASN CB  HB3  sing N N 140 
ASN CG  OD1  doub N N 141 
ASN CG  ND2  sing N N 142 
ASN ND2 HD21 sing N N 143 
ASN ND2 HD22 sing N N 144 
ASN OXT HXT  sing N N 145 
ASP N   CA   sing N N 146 
ASP N   H    sing N N 147 
ASP N   H2   sing N N 148 
ASP CA  C    sing N N 149 
ASP CA  CB   sing N N 150 
ASP CA  HA   sing N N 151 
ASP C   O    doub N N 152 
ASP C   OXT  sing N N 153 
ASP CB  CG   sing N N 154 
ASP CB  HB2  sing N N 155 
ASP CB  HB3  sing N N 156 
ASP CG  OD1  doub N N 157 
ASP CG  OD2  sing N N 158 
ASP OD2 HD2  sing N N 159 
ASP OXT HXT  sing N N 160 
CIT C1  O1   doub N N 161 
CIT C1  O2   sing N N 162 
CIT C1  C2   sing N N 163 
CIT O2  HO2  sing N N 164 
CIT C2  C3   sing N N 165 
CIT C2  H21  sing N N 166 
CIT C2  H22  sing N N 167 
CIT C3  O7   sing N N 168 
CIT C3  C4   sing N N 169 
CIT C3  C6   sing N N 170 
CIT O7  HO7  sing N N 171 
CIT C4  C5   sing N N 172 
CIT C4  H41  sing N N 173 
CIT C4  H42  sing N N 174 
CIT C5  O3   doub N N 175 
CIT C5  O4   sing N N 176 
CIT O4  HO4  sing N N 177 
CIT C6  O5   doub N N 178 
CIT C6  O6   sing N N 179 
CIT O6  HO6  sing N N 180 
COA N1A C2A  sing Y N 181 
COA N1A C6A  doub Y N 182 
COA C2A N3A  doub Y N 183 
COA C2A H2A  sing N N 184 
COA N3A C4A  sing Y N 185 
COA C4A C5A  doub Y N 186 
COA C4A N9A  sing Y N 187 
COA C5A C6A  sing Y N 188 
COA C5A N7A  sing Y N 189 
COA C6A N6A  sing N N 190 
COA N6A H61A sing N N 191 
COA N6A H62A sing N N 192 
COA N7A C8A  doub Y N 193 
COA C8A N9A  sing Y N 194 
COA C8A H8A  sing N N 195 
COA N9A C1B  sing N N 196 
COA C1B C2B  sing N N 197 
COA C1B O4B  sing N N 198 
COA C1B H1B  sing N N 199 
COA C2B O2B  sing N N 200 
COA C2B C3B  sing N N 201 
COA C2B H2B  sing N N 202 
COA O2B HO2A sing N N 203 
COA C3B O3B  sing N N 204 
COA C3B C4B  sing N N 205 
COA C3B H3B  sing N N 206 
COA O3B P3B  sing N N 207 
COA P3B O7A  doub N N 208 
COA P3B O8A  sing N N 209 
COA P3B O9A  sing N N 210 
COA O8A HOA8 sing N N 211 
COA O9A HOA9 sing N N 212 
COA C4B O4B  sing N N 213 
COA C4B C5B  sing N N 214 
COA C4B H4B  sing N N 215 
COA C5B O5B  sing N N 216 
COA C5B H51A sing N N 217 
COA C5B H52A sing N N 218 
COA O5B P1A  sing N N 219 
COA P1A O1A  doub N N 220 
COA P1A O2A  sing N N 221 
COA P1A O3A  sing N N 222 
COA O2A HOA2 sing N N 223 
COA O3A P2A  sing N N 224 
COA P2A O4A  doub N N 225 
COA P2A O5A  sing N N 226 
COA P2A O6A  sing N N 227 
COA O5A HOA5 sing N N 228 
COA O6A CCP  sing N N 229 
COA CBP CCP  sing N N 230 
COA CBP CDP  sing N N 231 
COA CBP CEP  sing N N 232 
COA CBP CAP  sing N N 233 
COA CCP H121 sing N N 234 
COA CCP H122 sing N N 235 
COA CDP H131 sing N N 236 
COA CDP H132 sing N N 237 
COA CDP H133 sing N N 238 
COA CEP H141 sing N N 239 
COA CEP H142 sing N N 240 
COA CEP H143 sing N N 241 
COA CAP OAP  sing N N 242 
COA CAP C9P  sing N N 243 
COA CAP H10  sing N N 244 
COA OAP HO1  sing N N 245 
COA C9P O9P  doub N N 246 
COA C9P N8P  sing N N 247 
COA N8P C7P  sing N N 248 
COA N8P HN8  sing N N 249 
COA C7P C6P  sing N N 250 
COA C7P H71  sing N N 251 
COA C7P H72  sing N N 252 
COA C6P C5P  sing N N 253 
COA C6P H61  sing N N 254 
COA C6P H62  sing N N 255 
COA C5P O5P  doub N N 256 
COA C5P N4P  sing N N 257 
COA N4P C3P  sing N N 258 
COA N4P HN4  sing N N 259 
COA C3P C2P  sing N N 260 
COA C3P H31  sing N N 261 
COA C3P H32  sing N N 262 
COA C2P S1P  sing N N 263 
COA C2P H21  sing N N 264 
COA C2P H22  sing N N 265 
COA S1P HS1  sing N N 266 
CYS N   CA   sing N N 267 
CYS N   H    sing N N 268 
CYS N   H2   sing N N 269 
CYS CA  C    sing N N 270 
CYS CA  CB   sing N N 271 
CYS CA  HA   sing N N 272 
CYS C   O    doub N N 273 
CYS C   OXT  sing N N 274 
CYS CB  SG   sing N N 275 
CYS CB  HB2  sing N N 276 
CYS CB  HB3  sing N N 277 
CYS SG  HG   sing N N 278 
CYS OXT HXT  sing N N 279 
GLN N   CA   sing N N 280 
GLN N   H    sing N N 281 
GLN N   H2   sing N N 282 
GLN CA  C    sing N N 283 
GLN CA  CB   sing N N 284 
GLN CA  HA   sing N N 285 
GLN C   O    doub N N 286 
GLN C   OXT  sing N N 287 
GLN CB  CG   sing N N 288 
GLN CB  HB2  sing N N 289 
GLN CB  HB3  sing N N 290 
GLN CG  CD   sing N N 291 
GLN CG  HG2  sing N N 292 
GLN CG  HG3  sing N N 293 
GLN CD  OE1  doub N N 294 
GLN CD  NE2  sing N N 295 
GLN NE2 HE21 sing N N 296 
GLN NE2 HE22 sing N N 297 
GLN OXT HXT  sing N N 298 
GLU N   CA   sing N N 299 
GLU N   H    sing N N 300 
GLU N   H2   sing N N 301 
GLU CA  C    sing N N 302 
GLU CA  CB   sing N N 303 
GLU CA  HA   sing N N 304 
GLU C   O    doub N N 305 
GLU C   OXT  sing N N 306 
GLU CB  CG   sing N N 307 
GLU CB  HB2  sing N N 308 
GLU CB  HB3  sing N N 309 
GLU CG  CD   sing N N 310 
GLU CG  HG2  sing N N 311 
GLU CG  HG3  sing N N 312 
GLU CD  OE1  doub N N 313 
GLU CD  OE2  sing N N 314 
GLU OE2 HE2  sing N N 315 
GLU OXT HXT  sing N N 316 
GLY N   CA   sing N N 317 
GLY N   H    sing N N 318 
GLY N   H2   sing N N 319 
GLY CA  C    sing N N 320 
GLY CA  HA2  sing N N 321 
GLY CA  HA3  sing N N 322 
GLY C   O    doub N N 323 
GLY C   OXT  sing N N 324 
GLY OXT HXT  sing N N 325 
HIS N   CA   sing N N 326 
HIS N   H    sing N N 327 
HIS N   H2   sing N N 328 
HIS CA  C    sing N N 329 
HIS CA  CB   sing N N 330 
HIS CA  HA   sing N N 331 
HIS C   O    doub N N 332 
HIS C   OXT  sing N N 333 
HIS CB  CG   sing N N 334 
HIS CB  HB2  sing N N 335 
HIS CB  HB3  sing N N 336 
HIS CG  ND1  sing Y N 337 
HIS CG  CD2  doub Y N 338 
HIS ND1 CE1  doub Y N 339 
HIS ND1 HD1  sing N N 340 
HIS CD2 NE2  sing Y N 341 
HIS CD2 HD2  sing N N 342 
HIS CE1 NE2  sing Y N 343 
HIS CE1 HE1  sing N N 344 
HIS NE2 HE2  sing N N 345 
HIS OXT HXT  sing N N 346 
HOH O   H1   sing N N 347 
HOH O   H2   sing N N 348 
ILE N   CA   sing N N 349 
ILE N   H    sing N N 350 
ILE N   H2   sing N N 351 
ILE CA  C    sing N N 352 
ILE CA  CB   sing N N 353 
ILE CA  HA   sing N N 354 
ILE C   O    doub N N 355 
ILE C   OXT  sing N N 356 
ILE CB  CG1  sing N N 357 
ILE CB  CG2  sing N N 358 
ILE CB  HB   sing N N 359 
ILE CG1 CD1  sing N N 360 
ILE CG1 HG12 sing N N 361 
ILE CG1 HG13 sing N N 362 
ILE CG2 HG21 sing N N 363 
ILE CG2 HG22 sing N N 364 
ILE CG2 HG23 sing N N 365 
ILE CD1 HD11 sing N N 366 
ILE CD1 HD12 sing N N 367 
ILE CD1 HD13 sing N N 368 
ILE OXT HXT  sing N N 369 
LEU N   CA   sing N N 370 
LEU N   H    sing N N 371 
LEU N   H2   sing N N 372 
LEU CA  C    sing N N 373 
LEU CA  CB   sing N N 374 
LEU CA  HA   sing N N 375 
LEU C   O    doub N N 376 
LEU C   OXT  sing N N 377 
LEU CB  CG   sing N N 378 
LEU CB  HB2  sing N N 379 
LEU CB  HB3  sing N N 380 
LEU CG  CD1  sing N N 381 
LEU CG  CD2  sing N N 382 
LEU CG  HG   sing N N 383 
LEU CD1 HD11 sing N N 384 
LEU CD1 HD12 sing N N 385 
LEU CD1 HD13 sing N N 386 
LEU CD2 HD21 sing N N 387 
LEU CD2 HD22 sing N N 388 
LEU CD2 HD23 sing N N 389 
LEU OXT HXT  sing N N 390 
LYS N   CA   sing N N 391 
LYS N   H    sing N N 392 
LYS N   H2   sing N N 393 
LYS CA  C    sing N N 394 
LYS CA  CB   sing N N 395 
LYS CA  HA   sing N N 396 
LYS C   O    doub N N 397 
LYS C   OXT  sing N N 398 
LYS CB  CG   sing N N 399 
LYS CB  HB2  sing N N 400 
LYS CB  HB3  sing N N 401 
LYS CG  CD   sing N N 402 
LYS CG  HG2  sing N N 403 
LYS CG  HG3  sing N N 404 
LYS CD  CE   sing N N 405 
LYS CD  HD2  sing N N 406 
LYS CD  HD3  sing N N 407 
LYS CE  NZ   sing N N 408 
LYS CE  HE2  sing N N 409 
LYS CE  HE3  sing N N 410 
LYS NZ  HZ1  sing N N 411 
LYS NZ  HZ2  sing N N 412 
LYS NZ  HZ3  sing N N 413 
LYS OXT HXT  sing N N 414 
MET N   CA   sing N N 415 
MET N   H    sing N N 416 
MET N   H2   sing N N 417 
MET CA  C    sing N N 418 
MET CA  CB   sing N N 419 
MET CA  HA   sing N N 420 
MET C   O    doub N N 421 
MET C   OXT  sing N N 422 
MET CB  CG   sing N N 423 
MET CB  HB2  sing N N 424 
MET CB  HB3  sing N N 425 
MET CG  SD   sing N N 426 
MET CG  HG2  sing N N 427 
MET CG  HG3  sing N N 428 
MET SD  CE   sing N N 429 
MET CE  HE1  sing N N 430 
MET CE  HE2  sing N N 431 
MET CE  HE3  sing N N 432 
MET OXT HXT  sing N N 433 
OAA O1  C1   doub N N 434 
OAA O2  C1   sing N N 435 
OAA O4  C4   doub N N 436 
OAA O5  C4   sing N N 437 
OAA O5  HO5  sing N N 438 
OAA O3  C3   doub N N 439 
OAA C1  C2   sing N N 440 
OAA C2  C3   sing N N 441 
OAA C2  H21  sing N N 442 
OAA C2  H22  sing N N 443 
OAA C3  C4   sing N N 444 
PHE N   CA   sing N N 445 
PHE N   H    sing N N 446 
PHE N   H2   sing N N 447 
PHE CA  C    sing N N 448 
PHE CA  CB   sing N N 449 
PHE CA  HA   sing N N 450 
PHE C   O    doub N N 451 
PHE C   OXT  sing N N 452 
PHE CB  CG   sing N N 453 
PHE CB  HB2  sing N N 454 
PHE CB  HB3  sing N N 455 
PHE CG  CD1  doub Y N 456 
PHE CG  CD2  sing Y N 457 
PHE CD1 CE1  sing Y N 458 
PHE CD1 HD1  sing N N 459 
PHE CD2 CE2  doub Y N 460 
PHE CD2 HD2  sing N N 461 
PHE CE1 CZ   doub Y N 462 
PHE CE1 HE1  sing N N 463 
PHE CE2 CZ   sing Y N 464 
PHE CE2 HE2  sing N N 465 
PHE CZ  HZ   sing N N 466 
PHE OXT HXT  sing N N 467 
PRO N   CA   sing N N 468 
PRO N   CD   sing N N 469 
PRO N   H    sing N N 470 
PRO CA  C    sing N N 471 
PRO CA  CB   sing N N 472 
PRO CA  HA   sing N N 473 
PRO C   O    doub N N 474 
PRO C   OXT  sing N N 475 
PRO CB  CG   sing N N 476 
PRO CB  HB2  sing N N 477 
PRO CB  HB3  sing N N 478 
PRO CG  CD   sing N N 479 
PRO CG  HG2  sing N N 480 
PRO CG  HG3  sing N N 481 
PRO CD  HD2  sing N N 482 
PRO CD  HD3  sing N N 483 
PRO OXT HXT  sing N N 484 
SER N   CA   sing N N 485 
SER N   H    sing N N 486 
SER N   H2   sing N N 487 
SER CA  C    sing N N 488 
SER CA  CB   sing N N 489 
SER CA  HA   sing N N 490 
SER C   O    doub N N 491 
SER C   OXT  sing N N 492 
SER CB  OG   sing N N 493 
SER CB  HB2  sing N N 494 
SER CB  HB3  sing N N 495 
SER OG  HG   sing N N 496 
SER OXT HXT  sing N N 497 
THR N   CA   sing N N 498 
THR N   H    sing N N 499 
THR N   H2   sing N N 500 
THR CA  C    sing N N 501 
THR CA  CB   sing N N 502 
THR CA  HA   sing N N 503 
THR C   O    doub N N 504 
THR C   OXT  sing N N 505 
THR CB  OG1  sing N N 506 
THR CB  CG2  sing N N 507 
THR CB  HB   sing N N 508 
THR OG1 HG1  sing N N 509 
THR CG2 HG21 sing N N 510 
THR CG2 HG22 sing N N 511 
THR CG2 HG23 sing N N 512 
THR OXT HXT  sing N N 513 
TRP N   CA   sing N N 514 
TRP N   H    sing N N 515 
TRP N   H2   sing N N 516 
TRP CA  C    sing N N 517 
TRP CA  CB   sing N N 518 
TRP CA  HA   sing N N 519 
TRP C   O    doub N N 520 
TRP C   OXT  sing N N 521 
TRP CB  CG   sing N N 522 
TRP CB  HB2  sing N N 523 
TRP CB  HB3  sing N N 524 
TRP CG  CD1  doub Y N 525 
TRP CG  CD2  sing Y N 526 
TRP CD1 NE1  sing Y N 527 
TRP CD1 HD1  sing N N 528 
TRP CD2 CE2  doub Y N 529 
TRP CD2 CE3  sing Y N 530 
TRP NE1 CE2  sing Y N 531 
TRP NE1 HE1  sing N N 532 
TRP CE2 CZ2  sing Y N 533 
TRP CE3 CZ3  doub Y N 534 
TRP CE3 HE3  sing N N 535 
TRP CZ2 CH2  doub Y N 536 
TRP CZ2 HZ2  sing N N 537 
TRP CZ3 CH2  sing Y N 538 
TRP CZ3 HZ3  sing N N 539 
TRP CH2 HH2  sing N N 540 
TRP OXT HXT  sing N N 541 
TYR N   CA   sing N N 542 
TYR N   H    sing N N 543 
TYR N   H2   sing N N 544 
TYR CA  C    sing N N 545 
TYR CA  CB   sing N N 546 
TYR CA  HA   sing N N 547 
TYR C   O    doub N N 548 
TYR C   OXT  sing N N 549 
TYR CB  CG   sing N N 550 
TYR CB  HB2  sing N N 551 
TYR CB  HB3  sing N N 552 
TYR CG  CD1  doub Y N 553 
TYR CG  CD2  sing Y N 554 
TYR CD1 CE1  sing Y N 555 
TYR CD1 HD1  sing N N 556 
TYR CD2 CE2  doub Y N 557 
TYR CD2 HD2  sing N N 558 
TYR CE1 CZ   doub Y N 559 
TYR CE1 HE1  sing N N 560 
TYR CE2 CZ   sing Y N 561 
TYR CE2 HE2  sing N N 562 
TYR CZ  OH   sing N N 563 
TYR OH  HH   sing N N 564 
TYR OXT HXT  sing N N 565 
VAL N   CA   sing N N 566 
VAL N   H    sing N N 567 
VAL N   H2   sing N N 568 
VAL CA  C    sing N N 569 
VAL CA  CB   sing N N 570 
VAL CA  HA   sing N N 571 
VAL C   O    doub N N 572 
VAL C   OXT  sing N N 573 
VAL CB  CG1  sing N N 574 
VAL CB  CG2  sing N N 575 
VAL CB  HB   sing N N 576 
VAL CG1 HG11 sing N N 577 
VAL CG1 HG12 sing N N 578 
VAL CG1 HG13 sing N N 579 
VAL CG2 HG21 sing N N 580 
VAL CG2 HG22 sing N N 581 
VAL CG2 HG23 sing N N 582 
VAL OXT HXT  sing N N 583 
# 
_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                    8ZW1 
_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]   0.017384 
_atom_sites.fract_transf_matrix[1][2]   0.009540 
_atom_sites.fract_transf_matrix[1][3]   0.005989 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.019078 
_atom_sites.fract_transf_matrix[2][3]   0.006653 
_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]   0.014743 
_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 
P 
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   ? 48.751  3.817   -13.392 1.00 86.35  ? 30  SER A N   1 
ATOM   2    C CA  . SER A 1 1   ? 48.656  3.948   -14.873 1.00 91.23  ? 30  SER A CA  1 
ATOM   3    C C   . SER A 1 1   ? 47.288  3.468   -15.354 1.00 93.28  ? 30  SER A C   1 
ATOM   4    O O   . SER A 1 1   ? 46.510  4.250   -15.899 1.00 95.24  ? 30  SER A O   1 
ATOM   5    C CB  . SER A 1 1   ? 49.778  3.205   -15.572 1.00 93.93  ? 30  SER A CB  1 
ATOM   6    O OG  . SER A 1 1   ? 49.631  3.257   -16.987 1.00 94.23  ? 30  SER A OG  1 
ATOM   7    N N   . THR A 1 2   ? 47.017  2.172   -15.160 1.00 87.44  ? 31  THR A N   1 
ATOM   8    C CA  . THR A 1 2   ? 45.718  1.604   -15.479 1.00 81.09  ? 31  THR A CA  1 
ATOM   9    C C   . THR A 1 2   ? 44.971  1.256   -14.192 1.00 75.14  ? 31  THR A C   1 
ATOM   10   O O   . THR A 1 2   ? 43.814  0.849   -14.257 1.00 82.32  ? 31  THR A O   1 
ATOM   11   C CB  . THR A 1 2   ? 45.878  0.381   -16.383 1.00 78.89  ? 31  THR A CB  1 
ATOM   12   O OG1 . THR A 1 2   ? 46.680  -0.549  -15.659 1.00 81.27  ? 31  THR A OG1 1 
ATOM   13   C CG2 . THR A 1 2   ? 46.517  0.725   -17.717 1.00 77.56  ? 31  THR A CG2 1 
ATOM   14   N N   . ASN A 1 3   ? 45.617  1.419   -13.028 1.00 64.70  ? 32  ASN A N   1 
ATOM   15   C CA  . ASN A 1 3   ? 44.960  1.131   -11.764 1.00 56.58  ? 32  ASN A CA  1 
ATOM   16   C C   . ASN A 1 3   ? 44.148  2.348   -11.321 1.00 47.41  ? 32  ASN A C   1 
ATOM   17   O O   . ASN A 1 3   ? 44.694  3.351   -10.863 1.00 41.06  ? 32  ASN A O   1 
ATOM   18   C CB  . ASN A 1 3   ? 45.937  0.666   -10.690 1.00 59.72  ? 32  ASN A CB  1 
ATOM   19   C CG  . ASN A 1 3   ? 45.214  0.204   -9.444  1.00 59.88  ? 32  ASN A CG  1 
ATOM   20   O OD1 . ASN A 1 3   ? 44.765  1.034   -8.646  1.00 64.70  ? 32  ASN A OD1 1 
ATOM   21   N ND2 . ASN A 1 3   ? 45.081  -1.101  -9.261  1.00 56.92  ? 32  ASN A ND2 1 
ATOM   22   N N   . LEU A 1 4   ? 42.825  2.218   -11.434 1.00 43.58  ? 33  LEU A N   1 
ATOM   23   C CA  . LEU A 1 4   ? 41.888  3.283   -11.117 1.00 41.97  ? 33  LEU A CA  1 
ATOM   24   C C   . LEU A 1 4   ? 42.049  3.741   -9.671  1.00 38.36  ? 33  LEU A C   1 
ATOM   25   O O   . LEU A 1 4   ? 41.919  4.929   -9.392  1.00 39.76  ? 33  LEU A O   1 
ATOM   26   C CB  . LEU A 1 4   ? 40.476  2.761   -11.387 1.00 45.20  ? 33  LEU A CB  1 
ATOM   27   C CG  . LEU A 1 4   ? 39.318  3.678   -10.985 1.00 44.50  ? 33  LEU A CG  1 
ATOM   28   C CD1 . LEU A 1 4   ? 39.392  5.000   -11.730 1.00 44.68  ? 33  LEU A CD1 1 
ATOM   29   C CD2 . LEU A 1 4   ? 37.986  2.976   -11.212 1.00 44.20  ? 33  LEU A CD2 1 
ATOM   30   N N   . LYS A 1 5   ? 42.318  2.804   -8.755  1.00 37.76  ? 34  LYS A N   1 
ATOM   31   C CA  . LYS A 1 5   ? 42.419  3.143   -7.343  1.00 40.65  ? 34  LYS A CA  1 
ATOM   32   C C   . LYS A 1 5   ? 43.550  4.141   -7.090  1.00 43.41  ? 34  LYS A C   1 
ATOM   33   O O   . LYS A 1 5   ? 43.418  5.018   -6.235  1.00 48.12  ? 34  LYS A O   1 
ATOM   34   C CB  . LYS A 1 5   ? 42.618  1.913   -6.452  1.00 39.56  ? 34  LYS A CB  1 
ATOM   35   C CG  . LYS A 1 5   ? 42.245  2.191   -5.011  1.00 40.68  ? 34  LYS A CG  1 
ATOM   36   C CD  . LYS A 1 5   ? 42.316  0.981   -4.094  1.00 42.92  ? 34  LYS A CD  1 
ATOM   37   C CE  . LYS A 1 5   ? 41.804  1.297   -2.729  1.00 40.88  ? 34  LYS A CE  1 
ATOM   38   N NZ  . LYS A 1 5   ? 42.016  0.142   -1.857  1.00 42.91  ? 34  LYS A NZ  1 
ATOM   39   N N   . ASP A 1 6   ? 44.658  4.007   -7.829  1.00 44.93  ? 35  ASP A N   1 
ATOM   40   C CA  . ASP A 1 6   ? 45.834  4.839   -7.615  1.00 47.74  ? 35  ASP A CA  1 
ATOM   41   C C   . ASP A 1 6   ? 45.624  6.220   -8.233  1.00 44.03  ? 35  ASP A C   1 
ATOM   42   O O   . ASP A 1 6   ? 46.051  7.222   -7.661  1.00 41.57  ? 35  ASP A O   1 
ATOM   43   C CB  . ASP A 1 6   ? 47.095  4.128   -8.089  1.00 50.15  ? 35  ASP A CB  1 
ATOM   44   C CG  . ASP A 1 6   ? 47.404  2.830   -7.353  1.00 53.00  ? 35  ASP A CG  1 
ATOM   45   O OD1 . ASP A 1 6   ? 47.495  2.879   -6.106  1.00 52.37  ? 35  ASP A OD1 1 
ATOM   46   O OD2 . ASP A 1 6   ? 47.542  1.778   -8.027  1.00 53.97  ? 35  ASP A OD2 1 
ATOM   47   N N   . ILE A 1 7   ? 44.938  6.265   -9.385  1.00 43.24  ? 36  ILE A N   1 
ATOM   48   C CA  . ILE A 1 7   ? 44.641  7.517   -10.070 1.00 42.08  ? 36  ILE A CA  1 
ATOM   49   C C   . ILE A 1 7   ? 43.667  8.327   -9.215  1.00 41.69  ? 36  ILE A C   1 
ATOM   50   O O   . ILE A 1 7   ? 43.819  9.538   -9.046  1.00 40.46  ? 36  ILE A O   1 
ATOM   51   C CB  . ILE A 1 7   ? 44.080  7.259   -11.481 1.00 43.36  ? 36  ILE A CB  1 
ATOM   52   C CG1 . ILE A 1 7   ? 44.984  6.339   -12.304 1.00 44.28  ? 36  ILE A CG1 1 
ATOM   53   C CG2 . ILE A 1 7   ? 43.823  8.578   -12.209 1.00 44.92  ? 36  ILE A CG2 1 
ATOM   54   C CD1 . ILE A 1 7   ? 44.274  5.651   -13.454 1.00 44.34  ? 36  ILE A CD1 1 
ATOM   55   N N   . LEU A 1 8   ? 42.667  7.635   -8.661  1.00 42.61  ? 37  LEU A N   1 
ATOM   56   C CA  . LEU A 1 8   ? 41.729  8.248   -7.738  1.00 40.22  ? 37  LEU A CA  1 
ATOM   57   C C   . LEU A 1 8   ? 42.483  8.817   -6.540  1.00 38.74  ? 37  LEU A C   1 
ATOM   58   O O   . LEU A 1 8   ? 42.199  9.926   -6.097  1.00 42.57  ? 37  LEU A O   1 
ATOM   59   C CB  . LEU A 1 8   ? 40.710  7.186   -7.336  1.00 41.52  ? 37  LEU A CB  1 
ATOM   60   C CG  . LEU A 1 8   ? 39.555  7.657   -6.448  1.00 42.53  ? 37  LEU A CG  1 
ATOM   61   C CD1 . LEU A 1 8   ? 38.890  8.918   -6.973  1.00 41.33  ? 37  LEU A CD1 1 
ATOM   62   C CD2 . LEU A 1 8   ? 38.543  6.535   -6.314  1.00 41.97  ? 37  LEU A CD2 1 
ATOM   63   N N   . ALA A 1 9   ? 43.465  8.059   -6.038  1.00 38.12  ? 38  ALA A N   1 
ATOM   64   C CA  . ALA A 1 9   ? 44.261  8.481   -4.895  1.00 40.38  ? 38  ALA A CA  1 
ATOM   65   C C   . ALA A 1 9   ? 44.978  9.797   -5.183  1.00 41.33  ? 38  ALA A C   1 
ATOM   66   O O   . ALA A 1 9   ? 45.136  10.619  -4.281  1.00 43.20  ? 38  ALA A O   1 
ATOM   67   C CB  . ALA A 1 9   ? 45.252  7.396   -4.511  1.00 40.51  ? 38  ALA A CB  1 
ATOM   68   N N   . ASP A 1 10  ? 45.429  9.974   -6.431  1.00 42.96  ? 39  ASP A N   1 
ATOM   69   C CA  . ASP A 1 10  ? 46.155  11.168  -6.842  1.00 44.34  ? 39  ASP A CA  1 
ATOM   70   C C   . ASP A 1 10  ? 45.217  12.375  -6.918  1.00 42.86  ? 39  ASP A C   1 
ATOM   71   O O   . ASP A 1 10  ? 45.621  13.495  -6.606  1.00 39.26  ? 39  ASP A O   1 
ATOM   72   C CB  . ASP A 1 10  ? 46.876  10.940  -8.165  1.00 47.67  ? 39  ASP A CB  1 
ATOM   73   C CG  . ASP A 1 10  ? 48.144  10.095  -8.120  1.00 49.36  ? 39  ASP A CG  1 
ATOM   74   O OD1 . ASP A 1 10  ? 48.645  9.843   -7.002  1.00 49.75  ? 39  ASP A OD1 1 
ATOM   75   O OD2 . ASP A 1 10  ? 48.629  9.705   -9.210  1.00 52.08  ? 39  ASP A OD2 1 
ATOM   76   N N   . LEU A 1 11  ? 43.965  12.140  -7.340  1.00 42.79  ? 40  LEU A N   1 
ATOM   77   C CA  . LEU A 1 11  ? 43.006  13.208  -7.582  1.00 40.50  ? 40  LEU A CA  1 
ATOM   78   C C   . LEU A 1 11  ? 42.396  13.714  -6.278  1.00 40.81  ? 40  LEU A C   1 
ATOM   79   O O   . LEU A 1 11  ? 42.020  14.878  -6.204  1.00 42.38  ? 40  LEU A O   1 
ATOM   80   C CB  . LEU A 1 11  ? 41.914  12.710  -8.526  1.00 43.96  ? 40  LEU A CB  1 
ATOM   81   C CG  . LEU A 1 11  ? 42.357  12.324  -9.940  1.00 44.41  ? 40  LEU A CG  1 
ATOM   82   C CD1 . LEU A 1 11  ? 41.285  11.496  -10.607 1.00 45.39  ? 40  LEU A CD1 1 
ATOM   83   C CD2 . LEU A 1 11  ? 42.682  13.548  -10.779 1.00 44.90  ? 40  LEU A CD2 1 
ATOM   84   N N   . ILE A 1 12  ? 42.269  12.847  -5.262  1.00 41.31  ? 41  ILE A N   1 
ATOM   85   C CA  . ILE A 1 12  ? 41.543  13.206  -4.051  1.00 39.73  ? 41  ILE A CA  1 
ATOM   86   C C   . ILE A 1 12  ? 42.152  14.456  -3.428  1.00 41.10  ? 41  ILE A C   1 
ATOM   87   O O   . ILE A 1 12  ? 41.419  15.394  -3.130  1.00 38.65  ? 41  ILE A O   1 
ATOM   88   C CB  . ILE A 1 12  ? 41.469  12.034  -3.053  1.00 39.31  ? 41  ILE A CB  1 
ATOM   89   C CG1 . ILE A 1 12  ? 40.440  11.007  -3.507  1.00 39.20  ? 41  ILE A CG1 1 
ATOM   90   C CG2 . ILE A 1 12  ? 41.169  12.519  -1.633  1.00 39.03  ? 41  ILE A CG2 1 
ATOM   91   C CD1 . ILE A 1 12  ? 40.583  9.656   -2.840  1.00 40.16  ? 41  ILE A CD1 1 
ATOM   92   N N   . PRO A 1 13  ? 43.486  14.502  -3.184  1.00 44.50  ? 42  PRO A N   1 
ATOM   93   C CA  . PRO A 1 13  ? 44.112  15.659  -2.538  1.00 44.30  ? 42  PRO A CA  1 
ATOM   94   C C   . PRO A 1 13  ? 43.789  16.972  -3.244  1.00 46.36  ? 42  PRO A C   1 
ATOM   95   O O   . PRO A 1 13  ? 43.432  17.956  -2.595  1.00 47.07  ? 42  PRO A O   1 
ATOM   96   C CB  . PRO A 1 13  ? 45.614  15.342  -2.591  1.00 45.14  ? 42  PRO A CB  1 
ATOM   97   C CG  . PRO A 1 13  ? 45.675  13.841  -2.697  1.00 45.76  ? 42  PRO A CG  1 
ATOM   98   C CD  . PRO A 1 13  ? 44.449  13.433  -3.482  1.00 42.88  ? 42  PRO A CD  1 
ATOM   99   N N   . LYS A 1 14  ? 43.914  16.959  -4.578  1.00 47.21  ? 43  LYS A N   1 
ATOM   100  C CA  . LYS A 1 14  ? 43.623  18.123  -5.398  1.00 50.32  ? 43  LYS A CA  1 
ATOM   101  C C   . LYS A 1 14  ? 42.187  18.582  -5.159  1.00 51.06  ? 43  LYS A C   1 
ATOM   102  O O   . LYS A 1 14  ? 41.941  19.768  -4.943  1.00 53.62  ? 43  LYS A O   1 
ATOM   103  C CB  . LYS A 1 14  ? 43.870  17.830  -6.883  1.00 51.67  ? 43  LYS A CB  1 
ATOM   104  C CG  . LYS A 1 14  ? 45.321  17.550  -7.243  1.00 50.93  ? 43  LYS A CG  1 
ATOM   105  C CD  . LYS A 1 14  ? 45.615  17.730  -8.726  1.00 54.76  ? 43  LYS A CD  1 
ATOM   106  C CE  . LYS A 1 14  ? 46.913  17.118  -9.164  1.00 58.07  ? 43  LYS A CE  1 
ATOM   107  N NZ  . LYS A 1 14  ? 46.856  15.653  -9.220  1.00 56.06  ? 43  LYS A NZ  1 
ATOM   108  N N   . GLU A 1 15  ? 41.248  17.630  -5.167  1.00 50.96  ? 44  GLU A N   1 
ATOM   109  C CA  . GLU A 1 15  ? 39.841  17.956  -4.983  1.00 50.97  ? 44  GLU A CA  1 
ATOM   110  C C   . GLU A 1 15  ? 39.587  18.458  -3.560  1.00 49.13  ? 44  GLU A C   1 
ATOM   111  O O   . GLU A 1 15  ? 38.751  19.336  -3.357  1.00 49.79  ? 44  GLU A O   1 
ATOM   112  C CB  . GLU A 1 15  ? 38.953  16.758  -5.314  1.00 51.14  ? 44  GLU A CB  1 
ATOM   113  C CG  . GLU A 1 15  ? 37.556  17.163  -5.773  1.00 52.88  ? 44  GLU A CG  1 
ATOM   114  C CD  . GLU A 1 15  ? 37.548  17.938  -7.078  1.00 53.03  ? 44  GLU A CD  1 
ATOM   115  O OE1 . GLU A 1 15  ? 38.103  17.418  -8.075  1.00 54.81  ? 44  GLU A OE1 1 
ATOM   116  O OE2 . GLU A 1 15  ? 36.982  19.052  -7.096  1.00 50.57  ? 44  GLU A OE2 1 
ATOM   117  N N   . GLN A 1 16  ? 40.301  17.901  -2.575  1.00 49.56  ? 45  GLN A N   1 
ATOM   118  C CA  . GLN A 1 16  ? 40.176  18.362  -1.198  1.00 53.23  ? 45  GLN A CA  1 
ATOM   119  C C   . GLN A 1 16  ? 40.611  19.826  -1.102  1.00 50.40  ? 45  GLN A C   1 
ATOM   120  O O   . GLN A 1 16  ? 39.916  20.647  -0.509  1.00 46.46  ? 45  GLN A O   1 
ATOM   121  C CB  . GLN A 1 16  ? 40.983  17.470  -0.255  1.00 51.67  ? 45  GLN A CB  1 
ATOM   122  C CG  . GLN A 1 16  ? 40.398  16.075  -0.081  1.00 53.60  ? 45  GLN A CG  1 
ATOM   123  C CD  . GLN A 1 16  ? 41.288  15.152  0.724   1.00 58.67  ? 45  GLN A CD  1 
ATOM   124  O OE1 . GLN A 1 16  ? 42.462  15.444  0.974   1.00 62.36  ? 45  GLN A OE1 1 
ATOM   125  N NE2 . GLN A 1 16  ? 40.742  14.015  1.130   1.00 58.75  ? 45  GLN A NE2 1 
ATOM   126  N N   . ALA A 1 17  ? 41.759  20.140  -1.714  1.00 49.56  ? 46  ALA A N   1 
ATOM   127  C CA  . ALA A 1 17  ? 42.287  21.495  -1.731  1.00 49.12  ? 46  ALA A CA  1 
ATOM   128  C C   . ALA A 1 17  ? 41.275  22.456  -2.356  1.00 47.71  ? 46  ALA A C   1 
ATOM   129  O O   . ALA A 1 17  ? 41.035  23.536  -1.826  1.00 48.67  ? 46  ALA A O   1 
ATOM   130  C CB  . ALA A 1 17  ? 43.611  21.516  -2.473  1.00 47.77  ? 46  ALA A CB  1 
ATOM   131  N N   . ARG A 1 18  ? 40.662  22.039  -3.469  1.00 47.63  ? 47  ARG A N   1 
ATOM   132  C CA  . ARG A 1 18  ? 39.752  22.888  -4.223  1.00 47.60  ? 47  ARG A CA  1 
ATOM   133  C C   . ARG A 1 18  ? 38.524  23.249  -3.388  1.00 42.87  ? 47  ARG A C   1 
ATOM   134  O O   . ARG A 1 18  ? 38.128  24.411  -3.326  1.00 39.09  ? 47  ARG A O   1 
ATOM   135  C CB  . ARG A 1 18  ? 39.374  22.176  -5.525  1.00 51.31  ? 47  ARG A CB  1 
ATOM   136  C CG  . ARG A 1 18  ? 38.568  23.015  -6.508  1.00 57.57  ? 47  ARG A CG  1 
ATOM   137  C CD  . ARG A 1 18  ? 38.511  22.350  -7.880  1.00 61.34  ? 47  ARG A CD  1 
ATOM   138  N NE  . ARG A 1 18  ? 37.395  22.842  -8.696  1.00 67.99  ? 47  ARG A NE  1 
ATOM   139  C CZ  . ARG A 1 18  ? 36.843  22.203  -9.729  1.00 74.40  ? 47  ARG A CZ  1 
ATOM   140  N NH1 . ARG A 1 18  ? 37.317  21.035  -10.139 1.00 77.62  ? 47  ARG A NH1 1 
ATOM   141  N NH2 . ARG A 1 18  ? 35.811  22.742  -10.357 1.00 74.07  ? 47  ARG A NH2 1 
ATOM   142  N N   . ILE A 1 19  ? 37.922  22.243  -2.745  1.00 43.89  ? 48  ILE A N   1 
ATOM   143  C CA  . ILE A 1 19  ? 36.721  22.454  -1.950  1.00 42.77  ? 48  ILE A CA  1 
ATOM   144  C C   . ILE A 1 19  ? 37.058  23.293  -0.725  1.00 45.81  ? 48  ILE A C   1 
ATOM   145  O O   . ILE A 1 19  ? 36.290  24.189  -0.378  1.00 48.31  ? 48  ILE A O   1 
ATOM   146  C CB  . ILE A 1 19  ? 36.060  21.113  -1.580  1.00 40.84  ? 48  ILE A CB  1 
ATOM   147  C CG1 . ILE A 1 19  ? 35.221  20.597  -2.754  1.00 40.01  ? 48  ILE A CG1 1 
ATOM   148  C CG2 . ILE A 1 19  ? 35.233  21.214  -0.294  1.00 38.14  ? 48  ILE A CG2 1 
ATOM   149  C CD1 . ILE A 1 19  ? 34.869  19.125  -2.664  1.00 40.56  ? 48  ILE A CD1 1 
ATOM   150  N N   . LYS A 1 20  ? 38.187  22.970  -0.074  1.00 50.02  ? 49  LYS A N   1 
ATOM   151  C CA  . LYS A 1 20  ? 38.660  23.706  1.090   1.00 52.15  ? 49  LYS A CA  1 
ATOM   152  C C   . LYS A 1 20  ? 38.906  25.166  0.701   1.00 48.54  ? 49  LYS A C   1 
ATOM   153  O O   . LYS A 1 20  ? 38.387  26.068  1.350   1.00 46.92  ? 49  LYS A O   1 
ATOM   154  C CB  . LYS A 1 20  ? 39.904  23.010  1.663   1.00 56.23  ? 49  LYS A CB  1 
ATOM   155  C CG  . LYS A 1 20  ? 40.557  23.674  2.873   1.00 58.43  ? 49  LYS A CG  1 
ATOM   156  C CD  . LYS A 1 20  ? 41.987  23.206  3.115   1.00 63.72  ? 49  LYS A CD  1 
ATOM   157  C CE  . LYS A 1 20  ? 42.751  24.066  4.078   1.00 66.93  ? 49  LYS A CE  1 
ATOM   158  N NZ  . LYS A 1 20  ? 42.209  24.011  5.439   1.00 68.73  ? 49  LYS A NZ  1 
ATOM   159  N N   . THR A 1 21  ? 39.678  25.386  -0.374  1.00 49.13  ? 50  THR A N   1 
ATOM   160  C CA  . THR A 1 21  ? 39.941  26.725  -0.889  1.00 51.37  ? 50  THR A CA  1 
ATOM   161  C C   . THR A 1 21  ? 38.619  27.464  -1.098  1.00 50.24  ? 50  THR A C   1 
ATOM   162  O O   . THR A 1 21  ? 38.501  28.624  -0.718  1.00 55.04  ? 50  THR A O   1 
ATOM   163  C CB  . THR A 1 21  ? 40.739  26.659  -2.194  1.00 52.06  ? 50  THR A CB  1 
ATOM   164  O OG1 . THR A 1 21  ? 41.930  25.920  -1.963  1.00 53.95  ? 50  THR A OG1 1 
ATOM   165  C CG2 . THR A 1 21  ? 41.164  28.026  -2.695  1.00 54.41  ? 50  THR A CG2 1 
ATOM   166  N N   . PHE A 1 22  ? 37.636  26.781  -1.701  1.00 46.66  ? 51  PHE A N   1 
ATOM   167  C CA  . PHE A 1 22  ? 36.344  27.374  -2.014  1.00 48.21  ? 51  PHE A CA  1 
ATOM   168  C C   . PHE A 1 22  ? 35.523  27.636  -0.752  1.00 49.82  ? 51  PHE A C   1 
ATOM   169  O O   . PHE A 1 22  ? 34.783  28.615  -0.695  1.00 51.78  ? 51  PHE A O   1 
ATOM   170  C CB  . PHE A 1 22  ? 35.574  26.445  -2.954  1.00 48.31  ? 51  PHE A CB  1 
ATOM   171  C CG  . PHE A 1 22  ? 34.179  26.930  -3.326  1.00 47.21  ? 51  PHE A CG  1 
ATOM   172  C CD1 . PHE A 1 22  ? 33.990  28.147  -3.968  1.00 47.79  ? 51  PHE A CD1 1 
ATOM   173  C CD2 . PHE A 1 22  ? 33.053  26.183  -2.996  1.00 48.15  ? 51  PHE A CD2 1 
ATOM   174  C CE1 . PHE A 1 22  ? 32.715  28.585  -4.295  1.00 47.26  ? 51  PHE A CE1 1 
ATOM   175  C CE2 . PHE A 1 22  ? 31.782  26.628  -3.326  1.00 47.69  ? 51  PHE A CE2 1 
ATOM   176  C CZ  . PHE A 1 22  ? 31.615  27.830  -3.966  1.00 47.26  ? 51  PHE A CZ  1 
ATOM   177  N N   . ARG A 1 23  ? 35.622  26.743  0.240   1.00 52.62  ? 52  ARG A N   1 
ATOM   178  C CA  . ARG A 1 23  ? 34.929  26.926  1.508   1.00 58.77  ? 52  ARG A CA  1 
ATOM   179  C C   . ARG A 1 23  ? 35.623  28.014  2.328   1.00 60.83  ? 52  ARG A C   1 
ATOM   180  O O   . ARG A 1 23  ? 34.967  28.783  3.027   1.00 57.26  ? 52  ARG A O   1 
ATOM   181  C CB  . ARG A 1 23  ? 34.848  25.613  2.297   1.00 60.27  ? 52  ARG A CB  1 
ATOM   182  C CG  . ARG A 1 23  ? 33.918  24.586  1.665   1.00 60.97  ? 52  ARG A CG  1 
ATOM   183  C CD  . ARG A 1 23  ? 33.853  23.295  2.463   1.00 60.36  ? 52  ARG A CD  1 
ATOM   184  N NE  . ARG A 1 23  ? 33.137  23.474  3.730   1.00 58.75  ? 52  ARG A NE  1 
ATOM   185  C CZ  . ARG A 1 23  ? 32.767  22.499  4.554   1.00 60.11  ? 52  ARG A CZ  1 
ATOM   186  N NH1 . ARG A 1 23  ? 33.037  21.234  4.272   1.00 59.50  ? 52  ARG A NH1 1 
ATOM   187  N NH2 . ARG A 1 23  ? 32.111  22.797  5.662   1.00 63.13  ? 52  ARG A NH2 1 
ATOM   188  N N   . GLN A 1 24  ? 36.956  28.081  2.214   1.00 62.71  ? 53  GLN A N   1 
ATOM   189  C CA  . GLN A 1 24  ? 37.745  29.114  2.868   1.00 64.69  ? 53  GLN A CA  1 
ATOM   190  C C   . GLN A 1 24  ? 37.563  30.467  2.174   1.00 63.08  ? 53  GLN A C   1 
ATOM   191  O O   . GLN A 1 24  ? 38.204  31.438  2.570   1.00 66.31  ? 53  GLN A O   1 
ATOM   192  C CB  . GLN A 1 24  ? 39.222  28.710  2.903   1.00 64.62  ? 53  GLN A CB  1 
ATOM   193  C CG  . GLN A 1 24  ? 39.577  27.736  4.023   1.00 64.16  ? 53  GLN A CG  1 
ATOM   194  C CD  . GLN A 1 24  ? 41.042  27.351  4.046   1.00 66.14  ? 53  GLN A CD  1 
ATOM   195  O OE1 . GLN A 1 24  ? 41.766  27.474  3.051   1.00 62.28  ? 53  GLN A OE1 1 
ATOM   196  N NE2 . GLN A 1 24  ? 41.497  26.865  5.192   1.00 67.58  ? 53  GLN A NE2 1 
ATOM   197  N N   . GLN A 1 25  ? 36.696  30.524  1.150   1.00 61.31  ? 54  GLN A N   1 
ATOM   198  C CA  . GLN A 1 25  ? 36.420  31.746  0.408   1.00 61.50  ? 54  GLN A CA  1 
ATOM   199  C C   . GLN A 1 25  ? 34.964  32.171  0.572   1.00 59.78  ? 54  GLN A C   1 
ATOM   200  O O   . GLN A 1 25  ? 34.691  33.317  0.929   1.00 62.32  ? 54  GLN A O   1 
ATOM   201  C CB  . GLN A 1 25  ? 36.666  31.560  -1.087  1.00 62.88  ? 54  GLN A CB  1 
ATOM   202  C CG  . GLN A 1 25  ? 38.126  31.687  -1.502  1.00 64.07  ? 54  GLN A CG  1 
ATOM   203  C CD  . GLN A 1 25  ? 38.356  31.311  -2.949  1.00 64.03  ? 54  GLN A CD  1 
ATOM   204  O OE1 . GLN A 1 25  ? 39.234  30.505  -3.270  1.00 68.30  ? 54  GLN A OE1 1 
ATOM   205  N NE2 . GLN A 1 25  ? 37.566  31.893  -3.839  1.00 64.52  ? 54  GLN A NE2 1 
ATOM   206  N N   . HIS A 1 26  ? 34.042  31.246  0.270   1.00 59.36  ? 55  HIS A N   1 
ATOM   207  C CA  . HIS A 1 26  ? 32.622  31.552  0.196   1.00 59.25  ? 55  HIS A CA  1 
ATOM   208  C C   . HIS A 1 26  ? 31.850  30.669  1.173   1.00 53.48  ? 55  HIS A C   1 
ATOM   209  O O   . HIS A 1 26  ? 30.649  30.469  1.015   1.00 51.38  ? 55  HIS A O   1 
ATOM   210  C CB  . HIS A 1 26  ? 32.117  31.366  -1.243  1.00 63.21  ? 55  HIS A CB  1 
ATOM   211  C CG  . HIS A 1 26  ? 32.733  32.281  -2.253  1.00 65.82  ? 55  HIS A CG  1 
ATOM   212  N ND1 . HIS A 1 26  ? 32.688  33.655  -2.154  1.00 66.87  ? 55  HIS A ND1 1 
ATOM   213  C CD2 . HIS A 1 26  ? 33.362  32.018  -3.409  1.00 67.31  ? 55  HIS A CD2 1 
ATOM   214  C CE1 . HIS A 1 26  ? 33.293  34.192  -3.205  1.00 65.22  ? 55  HIS A CE1 1 
ATOM   215  N NE2 . HIS A 1 26  ? 33.713  33.216  -3.979  1.00 67.27  ? 55  HIS A NE2 1 
ATOM   216  N N   . GLY A 1 27  ? 32.541  30.176  2.205   1.00 54.37  ? 56  GLY A N   1 
ATOM   217  C CA  . GLY A 1 27  ? 31.962  29.235  3.150   1.00 55.46  ? 56  GLY A CA  1 
ATOM   218  C C   . GLY A 1 27  ? 30.631  29.722  3.719   1.00 55.47  ? 56  GLY A C   1 
ATOM   219  O O   . GLY A 1 27  ? 29.709  28.928  3.882   1.00 55.13  ? 56  GLY A O   1 
ATOM   220  N N   . LYS A 1 28  ? 30.542  31.028  4.012   1.00 56.16  ? 57  LYS A N   1 
ATOM   221  C CA  . LYS A 1 28  ? 29.389  31.579  4.707   1.00 57.67  ? 57  LYS A CA  1 
ATOM   222  C C   . LYS A 1 28  ? 28.352  32.145  3.734   1.00 56.40  ? 57  LYS A C   1 
ATOM   223  O O   . LYS A 1 28  ? 27.302  32.608  4.173   1.00 56.63  ? 57  LYS A O   1 
ATOM   224  C CB  . LYS A 1 28  ? 29.885  32.619  5.716   1.00 59.92  ? 57  LYS A CB  1 
ATOM   225  C CG  . LYS A 1 28  ? 30.830  32.042  6.759   1.00 61.92  ? 57  LYS A CG  1 
ATOM   226  C CD  . LYS A 1 28  ? 30.824  32.766  8.099   1.00 64.34  ? 57  LYS A CD  1 
ATOM   227  C CE  . LYS A 1 28  ? 31.468  31.940  9.167   1.00 67.41  ? 57  LYS A CE  1 
ATOM   228  N NZ  . LYS A 1 28  ? 31.216  32.489  10.501  1.00 70.12  ? 57  LYS A NZ  1 
ATOM   229  N N   . THR A 1 29  ? 28.629  32.074  2.423   1.00 54.78  ? 58  THR A N   1 
ATOM   230  C CA  . THR A 1 29  ? 27.808  32.734  1.416   1.00 56.10  ? 58  THR A CA  1 
ATOM   231  C C   . THR A 1 29  ? 26.435  32.073  1.344   1.00 53.13  ? 58  THR A C   1 
ATOM   232  O O   . THR A 1 29  ? 26.327  30.866  1.521   1.00 61.78  ? 58  THR A O   1 
ATOM   233  C CB  . THR A 1 29  ? 28.516  32.666  0.062   1.00 60.50  ? 58  THR A CB  1 
ATOM   234  O OG1 . THR A 1 29  ? 29.752  33.359  0.219   1.00 62.59  ? 58  THR A OG1 1 
ATOM   235  C CG2 . THR A 1 29  ? 27.704  33.286  -1.063  1.00 58.66  ? 58  THR A CG2 1 
ATOM   236  N N   . VAL A 1 30  ? 25.412  32.875  1.028   1.00 50.88  ? 59  VAL A N   1 
ATOM   237  C CA  . VAL A 1 30  ? 24.033  32.427  0.897   1.00 48.52  ? 59  VAL A CA  1 
ATOM   238  C C   . VAL A 1 30  ? 23.785  31.996  -0.549  1.00 50.61  ? 59  VAL A C   1 
ATOM   239  O O   . VAL A 1 30  ? 24.039  32.769  -1.473  1.00 49.38  ? 59  VAL A O   1 
ATOM   240  C CB  . VAL A 1 30  ? 23.074  33.568  1.293   1.00 48.68  ? 59  VAL A CB  1 
ATOM   241  C CG1 . VAL A 1 30  ? 21.609  33.163  1.161   1.00 49.80  ? 59  VAL A CG1 1 
ATOM   242  C CG2 . VAL A 1 30  ? 23.356  34.109  2.692   1.00 49.25  ? 59  VAL A CG2 1 
ATOM   243  N N   . VAL A 1 31  ? 23.247  30.781  -0.733  1.00 50.67  ? 60  VAL A N   1 
ATOM   244  C CA  . VAL A 1 31  ? 23.005  30.237  -2.065  1.00 51.84  ? 60  VAL A CA  1 
ATOM   245  C C   . VAL A 1 31  ? 21.505  30.124  -2.352  1.00 47.28  ? 60  VAL A C   1 
ATOM   246  O O   . VAL A 1 31  ? 21.127  29.837  -3.485  1.00 43.99  ? 60  VAL A O   1 
ATOM   247  C CB  . VAL A 1 31  ? 23.712  28.885  -2.304  1.00 49.92  ? 60  VAL A CB  1 
ATOM   248  C CG1 . VAL A 1 31  ? 25.224  29.038  -2.382  1.00 51.45  ? 60  VAL A CG1 1 
ATOM   249  C CG2 . VAL A 1 31  ? 23.342  27.835  -1.265  1.00 51.28  ? 60  VAL A CG2 1 
ATOM   250  N N   . GLY A 1 32  ? 20.645  30.325  -1.345  1.00 48.67  ? 61  GLY A N   1 
ATOM   251  C CA  . GLY A 1 32  ? 19.207  30.285  -1.577  1.00 48.03  ? 61  GLY A CA  1 
ATOM   252  C C   . GLY A 1 32  ? 18.403  30.413  -0.285  1.00 49.19  ? 61  GLY A C   1 
ATOM   253  O O   . GLY A 1 32  ? 18.967  30.406  0.808   1.00 48.93  ? 61  GLY A O   1 
ATOM   254  N N   . GLN A 1 33  ? 17.076  30.508  -0.445  1.00 53.30  ? 62  GLN A N   1 
ATOM   255  C CA  . GLN A 1 33  ? 16.149  30.724  0.656   1.00 58.32  ? 62  GLN A CA  1 
ATOM   256  C C   . GLN A 1 33  ? 15.427  29.414  0.959   1.00 59.23  ? 62  GLN A C   1 
ATOM   257  O O   . GLN A 1 33  ? 15.390  28.525  0.113   1.00 59.39  ? 62  GLN A O   1 
ATOM   258  C CB  . GLN A 1 33  ? 15.101  31.783  0.304   1.00 61.15  ? 62  GLN A CB  1 
ATOM   259  C CG  . GLN A 1 33  ? 15.662  33.046  -0.341  1.00 64.68  ? 62  GLN A CG  1 
ATOM   260  C CD  . GLN A 1 33  ? 16.461  33.901  0.618   1.00 70.33  ? 62  GLN A CD  1 
ATOM   261  O OE1 . GLN A 1 33  ? 17.697  33.935  0.581   1.00 77.78  ? 62  GLN A OE1 1 
ATOM   262  N NE2 . GLN A 1 33  ? 15.760  34.603  1.494   1.00 67.43  ? 62  GLN A NE2 1 
ATOM   263  N N   . ILE A 1 34  ? 14.854  29.312  2.169   1.00 62.84  ? 63  ILE A N   1 
ATOM   264  C CA  . ILE A 1 34  ? 14.013  28.186  2.553   1.00 61.55  ? 63  ILE A CA  1 
ATOM   265  C C   . ILE A 1 34  ? 12.634  28.722  2.921   1.00 61.03  ? 63  ILE A C   1 
ATOM   266  O O   . ILE A 1 34  ? 12.513  29.493  3.871   1.00 61.93  ? 63  ILE A O   1 
ATOM   267  C CB  . ILE A 1 34  ? 14.608  27.403  3.738   1.00 64.15  ? 63  ILE A CB  1 
ATOM   268  C CG1 . ILE A 1 34  ? 16.072  27.013  3.515   1.00 64.30  ? 63  ILE A CG1 1 
ATOM   269  C CG2 . ILE A 1 34  ? 13.741  26.183  4.054   1.00 63.16  ? 63  ILE A CG2 1 
ATOM   270  C CD1 . ILE A 1 34  ? 16.830  26.696  4.793   1.00 63.20  ? 63  ILE A CD1 1 
ATOM   271  N N   . THR A 1 35  ? 11.606  28.280  2.187   1.00 57.15  ? 64  THR A N   1 
ATOM   272  C CA  . THR A 1 35  ? 10.244  28.719  2.439   1.00 58.07  ? 64  THR A CA  1 
ATOM   273  C C   . THR A 1 35  ? 9.442   27.603  3.105   1.00 62.11  ? 64  THR A C   1 
ATOM   274  O O   . THR A 1 35  ? 9.857   26.443  3.129   1.00 62.00  ? 64  THR A O   1 
ATOM   275  C CB  . THR A 1 35  ? 9.585   29.146  1.129   1.00 57.51  ? 64  THR A CB  1 
ATOM   276  O OG1 . THR A 1 35  ? 9.526   27.941  0.378   1.00 56.14  ? 64  THR A OG1 1 
ATOM   277  C CG2 . THR A 1 35  ? 10.367  30.215  0.387   1.00 58.90  ? 64  THR A CG2 1 
ATOM   278  N N   . VAL A 1 36  ? 8.266   27.989  3.618   1.00 59.76  ? 65  VAL A N   1 
ATOM   279  C CA  . VAL A 1 36  ? 7.270   27.067  4.137   1.00 56.19  ? 65  VAL A CA  1 
ATOM   280  C C   . VAL A 1 36  ? 6.835   26.107  3.029   1.00 54.90  ? 65  VAL A C   1 
ATOM   281  O O   . VAL A 1 36  ? 6.583   24.935  3.301   1.00 54.81  ? 65  VAL A O   1 
ATOM   282  C CB  . VAL A 1 36  ? 6.081   27.853  4.734   1.00 53.16  ? 65  VAL A CB  1 
ATOM   283  C CG1 . VAL A 1 36  ? 4.818   27.012  4.900   1.00 53.75  ? 65  VAL A CG1 1 
ATOM   284  C CG2 . VAL A 1 36  ? 6.453   28.508  6.057   1.00 51.09  ? 65  VAL A CG2 1 
ATOM   285  N N   . ASP A 1 37  ? 6.748   26.608  1.790   1.00 56.38  ? 66  ASP A N   1 
ATOM   286  C CA  . ASP A 1 37  ? 6.319   25.802  0.653   1.00 59.31  ? 66  ASP A CA  1 
ATOM   287  C C   . ASP A 1 37  ? 7.311   24.674  0.377   1.00 51.42  ? 66  ASP A C   1 
ATOM   288  O O   . ASP A 1 37  ? 6.911   23.553  0.095   1.00 44.93  ? 66  ASP A O   1 
ATOM   289  C CB  . ASP A 1 37  ? 6.127   26.641  -0.601  1.00 65.78  ? 66  ASP A CB  1 
ATOM   290  C CG  . ASP A 1 37  ? 4.760   27.291  -0.743  1.00 74.47  ? 66  ASP A CG  1 
ATOM   291  O OD1 . ASP A 1 37  ? 3.751   26.554  -0.648  1.00 74.33  ? 66  ASP A OD1 1 
ATOM   292  O OD2 . ASP A 1 37  ? 4.718   28.522  -0.968  1.00 83.87  ? 66  ASP A OD2 1 
ATOM   293  N N   . MET A 1 38  ? 8.606   24.988  0.456   1.00 55.66  ? 67  MET A N   1 
ATOM   294  C CA  . MET A 1 38  ? 9.663   24.021  0.214   1.00 53.06  ? 67  MET A CA  1 
ATOM   295  C C   . MET A 1 38  ? 9.638   22.940  1.295   1.00 49.95  ? 67  MET A C   1 
ATOM   296  O O   . MET A 1 38  ? 10.079  21.820  1.056   1.00 46.46  ? 67  MET A O   1 
ATOM   297  C CB  . MET A 1 38  ? 11.030  24.715  0.189   1.00 56.03  ? 67  MET A CB  1 
ATOM   298  C CG  . MET A 1 38  ? 11.198  25.723  -0.940  1.00 59.53  ? 67  MET A CG  1 
ATOM   299  S SD  . MET A 1 38  ? 12.759  26.626  -0.860  1.00 67.66  ? 67  MET A SD  1 
ATOM   300  C CE  . MET A 1 38  ? 12.708  27.621  -2.357  1.00 67.54  ? 67  MET A CE  1 
ATOM   301  N N   . MET A 1 39  ? 9.113   23.283  2.480   1.00 49.16  ? 68  MET A N   1 
ATOM   302  C CA  . MET A 1 39  ? 9.070   22.356  3.599   1.00 49.49  ? 68  MET A CA  1 
ATOM   303  C C   . MET A 1 39  ? 7.973   21.317  3.378   1.00 50.98  ? 68  MET A C   1 
ATOM   304  O O   . MET A 1 39  ? 8.221   20.122  3.530   1.00 50.94  ? 68  MET A O   1 
ATOM   305  C CB  . MET A 1 39  ? 8.865   23.101  4.921   1.00 50.55  ? 68  MET A CB  1 
ATOM   306  C CG  . MET A 1 39  ? 10.042  23.980  5.313   1.00 51.81  ? 68  MET A CG  1 
ATOM   307  S SD  . MET A 1 39  ? 9.901   24.650  6.982   1.00 55.34  ? 68  MET A SD  1 
ATOM   308  C CE  . MET A 1 39  ? 10.251  23.172  7.948   1.00 57.35  ? 68  MET A CE  1 
ATOM   309  N N   . TYR A 1 40  ? 6.772   21.782  3.005   1.00 51.31  ? 69  TYR A N   1 
ATOM   310  C CA  . TYR A 1 40  ? 5.645   20.907  2.723   1.00 47.29  ? 69  TYR A CA  1 
ATOM   311  C C   . TYR A 1 40  ? 5.757   20.341  1.308   1.00 45.96  ? 69  TYR A C   1 
ATOM   312  O O   . TYR A 1 40  ? 5.036   19.399  0.979   1.00 46.82  ? 69  TYR A O   1 
ATOM   313  C CB  . TYR A 1 40  ? 4.289   21.619  2.842   1.00 50.14  ? 69  TYR A CB  1 
ATOM   314  C CG  . TYR A 1 40  ? 3.787   21.942  4.246   1.00 50.37  ? 69  TYR A CG  1 
ATOM   315  C CD1 . TYR A 1 40  ? 4.174   23.111  4.891   1.00 53.27  ? 69  TYR A CD1 1 
ATOM   316  C CD2 . TYR A 1 40  ? 2.899   21.103  4.913   1.00 50.88  ? 69  TYR A CD2 1 
ATOM   317  C CE1 . TYR A 1 40  ? 3.715   23.426  6.161   1.00 54.59  ? 69  TYR A CE1 1 
ATOM   318  C CE2 . TYR A 1 40  ? 2.426   21.410  6.181   1.00 51.44  ? 69  TYR A CE2 1 
ATOM   319  C CZ  . TYR A 1 40  ? 2.837   22.576  6.808   1.00 54.08  ? 69  TYR A CZ  1 
ATOM   320  O OH  . TYR A 1 40  ? 2.403   22.912  8.060   1.00 53.78  ? 69  TYR A OH  1 
ATOM   321  N N   . GLY A 1 41  ? 6.628   20.936  0.474   1.00 44.81  ? 70  GLY A N   1 
ATOM   322  C CA  . GLY A 1 41  ? 6.713   20.621  -0.948  1.00 44.59  ? 70  GLY A CA  1 
ATOM   323  C C   . GLY A 1 41  ? 7.872   19.679  -1.285  1.00 44.79  ? 70  GLY A C   1 
ATOM   324  O O   . GLY A 1 41  ? 8.169   19.454  -2.456  1.00 42.14  ? 70  GLY A O   1 
ATOM   325  N N   . GLY A 1 42  ? 8.538   19.146  -0.253  1.00 46.36  ? 71  GLY A N   1 
ATOM   326  C CA  . GLY A 1 42  ? 9.527   18.093  -0.421  1.00 46.25  ? 71  GLY A CA  1 
ATOM   327  C C   . GLY A 1 42  ? 10.854  18.641  -0.924  1.00 44.30  ? 71  GLY A C   1 
ATOM   328  O O   . GLY A 1 42  ? 11.480  18.044  -1.800  1.00 49.09  ? 71  GLY A O   1 
ATOM   329  N N   . MET A 1 43  ? 11.247  19.791  -0.369  1.00 41.44  ? 72  MET A N   1 
ATOM   330  C CA  . MET A 1 43  ? 12.513  20.434  -0.678  1.00 43.94  ? 72  MET A CA  1 
ATOM   331  C C   . MET A 1 43  ? 12.613  20.792  -2.162  1.00 45.41  ? 72  MET A C   1 
ATOM   332  O O   . MET A 1 43  ? 13.718  20.905  -2.691  1.00 44.37  ? 72  MET A O   1 
ATOM   333  C CB  . MET A 1 43  ? 13.703  19.539  -0.320  1.00 46.47  ? 72  MET A CB  1 
ATOM   334  C CG  . MET A 1 43  ? 13.656  18.933  1.067   1.00 50.25  ? 72  MET A CG  1 
ATOM   335  S SD  . MET A 1 43  ? 15.144  17.972  1.409   1.00 51.97  ? 72  MET A SD  1 
ATOM   336  C CE  . MET A 1 43  ? 14.782  17.474  3.100   1.00 51.80  ? 72  MET A CE  1 
ATOM   337  N N   . ARG A 1 44  ? 11.472  20.996  -2.828  1.00 43.88  ? 73  ARG A N   1 
ATOM   338  C CA  . ARG A 1 44  ? 11.475  21.391  -4.226  1.00 47.08  ? 73  ARG A CA  1 
ATOM   339  C C   . ARG A 1 44  ? 12.128  22.767  -4.365  1.00 46.40  ? 73  ARG A C   1 
ATOM   340  O O   . ARG A 1 44  ? 11.840  23.674  -3.588  1.00 49.42  ? 73  ARG A O   1 
ATOM   341  C CB  . ARG A 1 44  ? 10.029  21.410  -4.728  1.00 52.39  ? 73  ARG A CB  1 
ATOM   342  C CG  . ARG A 1 44  ? 9.863   21.800  -6.189  1.00 57.86  ? 73  ARG A CG  1 
ATOM   343  C CD  . ARG A 1 44  ? 8.401   22.088  -6.493  1.00 64.12  ? 73  ARG A CD  1 
ATOM   344  N NE  . ARG A 1 44  ? 7.553   20.934  -6.167  1.00 67.53  ? 73  ARG A NE  1 
ATOM   345  C CZ  . ARG A 1 44  ? 6.754   20.820  -5.101  1.00 70.91  ? 73  ARG A CZ  1 
ATOM   346  N NH1 . ARG A 1 44  ? 6.662   21.796  -4.209  1.00 73.27  ? 73  ARG A NH1 1 
ATOM   347  N NH2 . ARG A 1 44  ? 6.041   19.717  -4.928  1.00 67.58  ? 73  ARG A NH2 1 
ATOM   348  N N   . GLY A 1 45  ? 13.027  22.910  -5.345  1.00 44.71  ? 74  GLY A N   1 
ATOM   349  C CA  . GLY A 1 45  ? 13.702  24.172  -5.600  1.00 44.24  ? 74  GLY A CA  1 
ATOM   350  C C   . GLY A 1 45  ? 14.848  24.434  -4.622  1.00 46.38  ? 74  GLY A C   1 
ATOM   351  O O   . GLY A 1 45  ? 15.680  25.304  -4.863  1.00 49.69  ? 74  GLY A O   1 
ATOM   352  N N   . MET A 1 46  ? 14.907  23.662  -3.531  1.00 47.28  ? 75  MET A N   1 
ATOM   353  C CA  . MET A 1 46  ? 15.883  23.891  -2.481  1.00 46.96  ? 75  MET A CA  1 
ATOM   354  C C   . MET A 1 46  ? 17.226  23.289  -2.893  1.00 45.66  ? 75  MET A C   1 
ATOM   355  O O   . MET A 1 46  ? 17.296  22.138  -3.335  1.00 40.94  ? 75  MET A O   1 
ATOM   356  C CB  . MET A 1 46  ? 15.395  23.267  -1.169  1.00 50.94  ? 75  MET A CB  1 
ATOM   357  C CG  . MET A 1 46  ? 16.180  23.685  0.060   1.00 55.01  ? 75  MET A CG  1 
ATOM   358  S SD  . MET A 1 46  ? 15.701  22.738  1.521   1.00 61.15  ? 75  MET A SD  1 
ATOM   359  C CE  . MET A 1 46  ? 13.937  23.060  1.647   1.00 60.92  ? 75  MET A CE  1 
ATOM   360  N N   . LYS A 1 47  ? 18.290  24.089  -2.748  1.00 47.06  ? 76  LYS A N   1 
ATOM   361  C CA  . LYS A 1 47  ? 19.642  23.623  -2.999  1.00 50.14  ? 76  LYS A CA  1 
ATOM   362  C C   . LYS A 1 47  ? 20.099  22.822  -1.787  1.00 50.16  ? 76  LYS A C   1 
ATOM   363  O O   . LYS A 1 47  ? 20.627  23.379  -0.828  1.00 55.50  ? 76  LYS A O   1 
ATOM   364  C CB  . LYS A 1 47  ? 20.574  24.788  -3.340  1.00 53.97  ? 76  LYS A CB  1 
ATOM   365  C CG  . LYS A 1 47  ? 20.392  25.310  -4.752  1.00 58.06  ? 76  LYS A CG  1 
ATOM   366  C CD  . LYS A 1 47  ? 21.559  26.149  -5.254  1.00 63.25  ? 76  LYS A CD  1 
ATOM   367  C CE  . LYS A 1 47  ? 21.478  26.378  -6.732  1.00 65.92  ? 76  LYS A CE  1 
ATOM   368  N NZ  . LYS A 1 47  ? 20.288  27.146  -7.107  1.00 66.35  ? 76  LYS A NZ  1 
ATOM   369  N N   . GLY A 1 48  ? 19.883  21.506  -1.858  1.00 47.04  ? 77  GLY A N   1 
ATOM   370  C CA  . GLY A 1 48  ? 19.909  20.655  -0.682  1.00 45.05  ? 77  GLY A CA  1 
ATOM   371  C C   . GLY A 1 48  ? 21.312  20.168  -0.339  1.00 39.03  ? 77  GLY A C   1 
ATOM   372  O O   . GLY A 1 48  ? 21.666  20.116  0.833   1.00 34.71  ? 77  GLY A O   1 
ATOM   373  N N   . LEU A 1 49  ? 22.091  19.791  -1.360  1.00 36.45  ? 78  LEU A N   1 
ATOM   374  C CA  . LEU A 1 49  ? 23.314  19.046  -1.122  1.00 36.50  ? 78  LEU A CA  1 
ATOM   375  C C   . LEU A 1 49  ? 24.301  19.220  -2.275  1.00 34.19  ? 78  LEU A C   1 
ATOM   376  O O   . LEU A 1 49  ? 23.938  19.538  -3.412  1.00 30.23  ? 78  LEU A O   1 
ATOM   377  C CB  . LEU A 1 49  ? 22.975  17.567  -0.921  1.00 36.92  ? 78  LEU A CB  1 
ATOM   378  C CG  . LEU A 1 49  ? 22.448  16.832  -2.161  1.00 37.89  ? 78  LEU A CG  1 
ATOM   379  C CD1 . LEU A 1 49  ? 22.606  15.338  -2.014  1.00 39.01  ? 78  LEU A CD1 1 
ATOM   380  C CD2 . LEU A 1 49  ? 20.994  17.170  -2.446  1.00 38.83  ? 78  LEU A CD2 1 
ATOM   381  N N   . VAL A 1 50  ? 25.568  18.964  -1.950  1.00 34.09  ? 79  VAL A N   1 
ATOM   382  C CA  . VAL A 1 50  ? 26.617  18.896  -2.948  1.00 33.72  ? 79  VAL A CA  1 
ATOM   383  C C   . VAL A 1 50  ? 26.719  17.454  -3.444  1.00 33.03  ? 79  VAL A C   1 
ATOM   384  O O   . VAL A 1 50  ? 26.813  16.516  -2.650  1.00 31.94  ? 79  VAL A O   1 
ATOM   385  C CB  . VAL A 1 50  ? 27.948  19.414  -2.372  1.00 35.90  ? 79  VAL A CB  1 
ATOM   386  C CG1 . VAL A 1 50  ? 29.098  19.280  -3.365  1.00 36.36  ? 79  VAL A CG1 1 
ATOM   387  C CG2 . VAL A 1 50  ? 27.825  20.861  -1.900  1.00 37.68  ? 79  VAL A CG2 1 
ATOM   388  N N   . TYR A 1 51  ? 26.685  17.304  -4.773  1.00 33.71  ? 80  TYR A N   1 
ATOM   389  C CA  . TYR A 1 51  ? 26.835  16.030  -5.453  1.00 32.69  ? 80  TYR A CA  1 
ATOM   390  C C   . TYR A 1 51  ? 27.674  16.275  -6.706  1.00 34.51  ? 80  TYR A C   1 
ATOM   391  O O   . TYR A 1 51  ? 27.320  17.136  -7.511  1.00 37.31  ? 80  TYR A O   1 
ATOM   392  C CB  . TYR A 1 51  ? 25.398  15.551  -5.683  1.00 33.26  ? 80  TYR A CB  1 
ATOM   393  C CG  . TYR A 1 51  ? 25.230  14.091  -6.082  1.00 32.56  ? 80  TYR A CG  1 
ATOM   394  C CD1 . TYR A 1 51  ? 25.282  13.708  -7.414  1.00 32.55  ? 80  TYR A CD1 1 
ATOM   395  C CD2 . TYR A 1 51  ? 25.015  13.097  -5.132  1.00 33.55  ? 80  TYR A CD2 1 
ATOM   396  C CE1 . TYR A 1 51  ? 25.137  12.383  -7.790  1.00 32.93  ? 80  TYR A CE1 1 
ATOM   397  C CE2 . TYR A 1 51  ? 24.867  11.765  -5.499  1.00 32.91  ? 80  TYR A CE2 1 
ATOM   398  C CZ  . TYR A 1 51  ? 24.934  11.409  -6.832  1.00 31.55  ? 80  TYR A CZ  1 
ATOM   399  O OH  . TYR A 1 51  ? 24.784  10.111  -7.224  1.00 33.96  ? 80  TYR A OH  1 
ATOM   400  N N   . GLU A 1 52  ? 28.762  15.505  -6.867  1.00 34.69  ? 81  GLU A N   1 
ATOM   401  C CA  . GLU A 1 52  ? 29.858  15.849  -7.767  1.00 37.36  ? 81  GLU A CA  1 
ATOM   402  C C   . GLU A 1 52  ? 29.788  15.104  -9.103  1.00 36.87  ? 81  GLU A C   1 
ATOM   403  O O   . GLU A 1 52  ? 30.256  15.621  -10.113 1.00 39.41  ? 81  GLU A O   1 
ATOM   404  C CB  . GLU A 1 52  ? 31.229  15.513  -7.173  1.00 40.36  ? 81  GLU A CB  1 
ATOM   405  C CG  . GLU A 1 52  ? 31.523  16.160  -5.821  1.00 42.28  ? 81  GLU A CG  1 
ATOM   406  C CD  . GLU A 1 52  ? 31.767  17.660  -5.804  1.00 43.68  ? 81  GLU A CD  1 
ATOM   407  O OE1 . GLU A 1 52  ? 31.744  18.325  -6.862  1.00 46.08  ? 81  GLU A OE1 1 
ATOM   408  O OE2 . GLU A 1 52  ? 31.994  18.168  -4.685  1.00 44.94  ? 81  GLU A OE2 1 
ATOM   409  N N   . THR A 1 53  ? 29.246  13.884  -9.125  1.00 35.43  ? 82  THR A N   1 
ATOM   410  C CA  . THR A 1 53  ? 29.388  13.029  -10.296 1.00 35.23  ? 82  THR A CA  1 
ATOM   411  C C   . THR A 1 53  ? 28.594  13.573  -11.488 1.00 35.52  ? 82  THR A C   1 
ATOM   412  O O   . THR A 1 53  ? 29.067  13.513  -12.622 1.00 36.50  ? 82  THR A O   1 
ATOM   413  C CB  . THR A 1 53  ? 28.997  11.596  -9.940  1.00 35.52  ? 82  THR A CB  1 
ATOM   414  O OG1 . THR A 1 53  ? 27.742  11.664  -9.272  1.00 33.74  ? 82  THR A OG1 1 
ATOM   415  C CG2 . THR A 1 53  ? 30.022  10.930  -9.039  1.00 35.14  ? 82  THR A CG2 1 
ATOM   416  N N   . SER A 1 54  ? 27.389  14.097  -11.250 1.00 34.80  ? 83  SER A N   1 
ATOM   417  C CA  . SER A 1 54  ? 26.587  14.636  -12.338 1.00 37.11  ? 83  SER A CA  1 
ATOM   418  C C   . SER A 1 54  ? 25.744  15.825  -11.879 1.00 38.91  ? 83  SER A C   1 
ATOM   419  O O   . SER A 1 54  ? 25.458  15.983  -10.689 1.00 37.80  ? 83  SER A O   1 
ATOM   420  C CB  . SER A 1 54  ? 25.724  13.567  -12.958 1.00 39.25  ? 83  SER A CB  1 
ATOM   421  O OG  . SER A 1 54  ? 24.725  13.120  -12.054 1.00 37.93  ? 83  SER A OG  1 
ATOM   422  N N   . VAL A 1 55  ? 25.372  16.662  -12.860 1.00 40.40  ? 84  VAL A N   1 
ATOM   423  C CA  . VAL A 1 55  ? 24.575  17.858  -12.642 1.00 40.27  ? 84  VAL A CA  1 
ATOM   424  C C   . VAL A 1 55  ? 23.536  17.961  -13.758 1.00 38.22  ? 84  VAL A C   1 
ATOM   425  O O   . VAL A 1 55  ? 23.830  17.743  -14.927 1.00 38.02  ? 84  VAL A O   1 
ATOM   426  C CB  . VAL A 1 55  ? 25.433  19.136  -12.559 1.00 42.52  ? 84  VAL A CB  1 
ATOM   427  C CG1 . VAL A 1 55  ? 24.578  20.389  -12.370 1.00 43.08  ? 84  VAL A CG1 1 
ATOM   428  C CG2 . VAL A 1 55  ? 26.475  19.036  -11.454 1.00 43.72  ? 84  VAL A CG2 1 
ATOM   429  N N   . LEU A 1 56  ? 22.322  18.345  -13.371 1.00 40.34  ? 85  LEU A N   1 
ATOM   430  C CA  . LEU A 1 56  ? 21.186  18.401  -14.269 1.00 45.06  ? 85  LEU A CA  1 
ATOM   431  C C   . LEU A 1 56  ? 20.706  19.844  -14.338 1.00 47.21  ? 85  LEU A C   1 
ATOM   432  O O   . LEU A 1 56  ? 19.906  20.262  -13.513 1.00 49.27  ? 85  LEU A O   1 
ATOM   433  C CB  . LEU A 1 56  ? 20.125  17.463  -13.699 1.00 45.66  ? 85  LEU A CB  1 
ATOM   434  C CG  . LEU A 1 56  ? 18.721  17.565  -14.297 1.00 49.65  ? 85  LEU A CG  1 
ATOM   435  C CD1 . LEU A 1 56  ? 18.726  17.238  -15.779 1.00 50.77  ? 85  LEU A CD1 1 
ATOM   436  C CD2 . LEU A 1 56  ? 17.774  16.656  -13.524 1.00 50.66  ? 85  LEU A CD2 1 
ATOM   437  N N   . ASP A 1 57  ? 21.218  20.612  -15.301 1.00 51.52  ? 86  ASP A N   1 
ATOM   438  C CA  . ASP A 1 57  ? 20.652  21.924  -15.560 1.00 58.68  ? 86  ASP A CA  1 
ATOM   439  C C   . ASP A 1 57  ? 19.331  21.712  -16.295 1.00 57.17  ? 86  ASP A C   1 
ATOM   440  O O   . ASP A 1 57  ? 19.262  20.950  -17.256 1.00 51.73  ? 86  ASP A O   1 
ATOM   441  C CB  . ASP A 1 57  ? 21.625  22.848  -16.274 1.00 64.08  ? 86  ASP A CB  1 
ATOM   442  C CG  . ASP A 1 57  ? 21.974  22.447  -17.697 1.00 67.47  ? 86  ASP A CG  1 
ATOM   443  O OD1 . ASP A 1 57  ? 22.257  21.251  -17.906 1.00 68.90  ? 86  ASP A OD1 1 
ATOM   444  O OD2 . ASP A 1 57  ? 21.979  23.335  -18.571 1.00 74.45  ? 86  ASP A OD2 1 
ATOM   445  N N   . PRO A 1 58  ? 18.234  22.357  -15.845 1.00 63.44  ? 87  PRO A N   1 
ATOM   446  C CA  . PRO A 1 58  ? 16.908  22.091  -16.408 1.00 66.74  ? 87  PRO A CA  1 
ATOM   447  C C   . PRO A 1 58  ? 16.745  22.464  -17.881 1.00 69.24  ? 87  PRO A C   1 
ATOM   448  O O   . PRO A 1 58  ? 15.746  22.100  -18.498 1.00 67.34  ? 87  PRO A O   1 
ATOM   449  C CB  . PRO A 1 58  ? 15.971  22.905  -15.488 1.00 68.32  ? 87  PRO A CB  1 
ATOM   450  C CG  . PRO A 1 58  ? 16.847  23.990  -14.897 1.00 67.39  ? 87  PRO A CG  1 
ATOM   451  C CD  . PRO A 1 58  ? 18.219  23.358  -14.765 1.00 64.45  ? 87  PRO A CD  1 
ATOM   452  N N   . ASP A 1 59  ? 17.738  23.176  -18.434 1.00 73.41  ? 88  ASP A N   1 
ATOM   453  C CA  . ASP A 1 59  ? 17.689  23.650  -19.810 1.00 76.26  ? 88  ASP A CA  1 
ATOM   454  C C   . ASP A 1 59  ? 18.193  22.566  -20.762 1.00 73.87  ? 88  ASP A C   1 
ATOM   455  O O   . ASP A 1 59  ? 17.496  22.224  -21.714 1.00 73.70  ? 88  ASP A O   1 
ATOM   456  C CB  . ASP A 1 59  ? 18.385  24.997  -19.965 1.00 82.66  ? 88  ASP A CB  1 
ATOM   457  C CG  . ASP A 1 59  ? 19.710  25.177  -19.231 1.00 89.79  ? 88  ASP A CG  1 
ATOM   458  O OD1 . ASP A 1 59  ? 19.777  24.813  -18.032 1.00 86.16  ? 88  ASP A OD1 1 
ATOM   459  O OD2 . ASP A 1 59  ? 20.658  25.713  -19.850 1.00 91.30  ? 88  ASP A OD2 1 
ATOM   460  N N   . GLU A 1 60  ? 19.392  22.024  -20.499 1.00 74.27  ? 89  GLU A N   1 
ATOM   461  C CA  . GLU A 1 60  ? 20.060  21.139  -21.445 1.00 71.94  ? 89  GLU A CA  1 
ATOM   462  C C   . GLU A 1 60  ? 20.245  19.726  -20.887 1.00 63.98  ? 89  GLU A C   1 
ATOM   463  O O   . GLU A 1 60  ? 20.940  18.914  -21.496 1.00 60.45  ? 89  GLU A O   1 
ATOM   464  C CB  . GLU A 1 60  ? 21.402  21.747  -21.849 1.00 78.37  ? 89  GLU A CB  1 
ATOM   465  C CG  . GLU A 1 60  ? 21.256  23.130  -22.478 1.00 86.76  ? 89  GLU A CG  1 
ATOM   466  C CD  . GLU A 1 60  ? 22.437  23.537  -23.339 1.00 93.51  ? 89  GLU A CD  1 
ATOM   467  O OE1 . GLU A 1 60  ? 22.218  23.907  -24.514 1.00 100.56 ? 89  GLU A OE1 1 
ATOM   468  O OE2 . GLU A 1 60  ? 23.579  23.463  -22.839 1.00 93.97  ? 89  GLU A OE2 1 
ATOM   469  N N   . GLY A 1 61  ? 19.627  19.430  -19.736 1.00 55.46  ? 90  GLY A N   1 
ATOM   470  C CA  . GLY A 1 61  ? 19.595  18.076  -19.207 1.00 49.86  ? 90  GLY A CA  1 
ATOM   471  C C   . GLY A 1 61  ? 20.900  17.676  -18.521 1.00 43.79  ? 90  GLY A C   1 
ATOM   472  O O   . GLY A 1 61  ? 21.713  18.525  -18.168 1.00 41.98  ? 90  GLY A O   1 
ATOM   473  N N   . ILE A 1 62  ? 21.080  16.363  -18.343 1.00 38.16  ? 91  ILE A N   1 
ATOM   474  C CA  . ILE A 1 62  ? 22.119  15.827  -17.478 1.00 35.75  ? 91  ILE A CA  1 
ATOM   475  C C   . ILE A 1 62  ? 23.486  16.038  -18.123 1.00 36.99  ? 91  ILE A C   1 
ATOM   476  O O   . ILE A 1 62  ? 23.621  15.915  -19.337 1.00 38.53  ? 91  ILE A O   1 
ATOM   477  C CB  . ILE A 1 62  ? 21.868  14.340  -17.161 1.00 32.38  ? 91  ILE A CB  1 
ATOM   478  C CG1 . ILE A 1 62  ? 22.804  13.818  -16.073 1.00 31.75  ? 91  ILE A CG1 1 
ATOM   479  C CG2 . ILE A 1 62  ? 21.966  13.475  -18.417 1.00 32.58  ? 91  ILE A CG2 1 
ATOM   480  C CD1 . ILE A 1 62  ? 22.664  14.518  -14.736 1.00 31.48  ? 91  ILE A CD1 1 
ATOM   481  N N   . ARG A 1 63  ? 24.481  16.362  -17.286 1.00 38.13  ? 92  ARG A N   1 
ATOM   482  C CA  . ARG A 1 63  ? 25.887  16.317  -17.663 1.00 39.73  ? 92  ARG A CA  1 
ATOM   483  C C   . ARG A 1 63  ? 26.638  15.427  -16.676 1.00 38.93  ? 92  ARG A C   1 
ATOM   484  O O   . ARG A 1 63  ? 26.502  15.593  -15.465 1.00 39.18  ? 92  ARG A O   1 
ATOM   485  C CB  . ARG A 1 63  ? 26.565  17.694  -17.681 1.00 43.85  ? 92  ARG A CB  1 
ATOM   486  C CG  . ARG A 1 63  ? 26.396  18.457  -18.988 1.00 47.93  ? 92  ARG A CG  1 
ATOM   487  C CD  . ARG A 1 63  ? 27.069  19.832  -19.002 1.00 48.33  ? 92  ARG A CD  1 
ATOM   488  N NE  . ARG A 1 63  ? 26.601  20.607  -20.159 1.00 51.53  ? 92  ARG A NE  1 
ATOM   489  C CZ  . ARG A 1 63  ? 26.919  20.414  -21.442 1.00 54.86  ? 92  ARG A CZ  1 
ATOM   490  N NH1 . ARG A 1 63  ? 27.953  19.660  -21.785 1.00 55.71  ? 92  ARG A NH1 1 
ATOM   491  N NH2 . ARG A 1 63  ? 26.226  21.030  -22.386 1.00 53.85  ? 92  ARG A NH2 1 
ATOM   492  N N   . PHE A 1 64  ? 27.429  14.492  -17.219 1.00 37.33  ? 93  PHE A N   1 
ATOM   493  C CA  . PHE A 1 64  ? 28.327  13.667  -16.430 1.00 37.13  ? 93  PHE A CA  1 
ATOM   494  C C   . PHE A 1 64  ? 29.701  14.325  -16.399 1.00 37.64  ? 93  PHE A C   1 
ATOM   495  O O   . PHE A 1 64  ? 30.437  14.241  -17.379 1.00 39.49  ? 93  PHE A O   1 
ATOM   496  C CB  . PHE A 1 64  ? 28.409  12.251  -17.015 1.00 36.14  ? 93  PHE A CB  1 
ATOM   497  C CG  . PHE A 1 64  ? 27.056  11.589  -17.212 1.00 34.01  ? 93  PHE A CG  1 
ATOM   498  C CD1 . PHE A 1 64  ? 26.282  11.210  -16.123 1.00 34.34  ? 93  PHE A CD1 1 
ATOM   499  C CD2 . PHE A 1 64  ? 26.559  11.345  -18.487 1.00 35.26  ? 93  PHE A CD2 1 
ATOM   500  C CE1 . PHE A 1 64  ? 25.039  10.621  -16.307 1.00 33.26  ? 93  PHE A CE1 1 
ATOM   501  C CE2 . PHE A 1 64  ? 25.319  10.746  -18.662 1.00 33.51  ? 93  PHE A CE2 1 
ATOM   502  C CZ  . PHE A 1 64  ? 24.563  10.391  -17.576 1.00 32.42  ? 93  PHE A CZ  1 
ATOM   503  N N   . ARG A 1 65  ? 30.033  14.980  -15.277 1.00 37.76  ? 94  ARG A N   1 
ATOM   504  C CA  . ARG A 1 65  ? 31.310  15.663  -15.114 1.00 38.82  ? 94  ARG A CA  1 
ATOM   505  C C   . ARG A 1 65  ? 31.487  16.742  -16.185 1.00 42.59  ? 94  ARG A C   1 
ATOM   506  O O   . ARG A 1 65  ? 32.557  16.883  -16.780 1.00 43.32  ? 94  ARG A O   1 
ATOM   507  C CB  . ARG A 1 65  ? 32.451  14.638  -15.170 1.00 37.42  ? 94  ARG A CB  1 
ATOM   508  C CG  . ARG A 1 65  ? 32.439  13.652  -14.013 1.00 37.54  ? 94  ARG A CG  1 
ATOM   509  C CD  . ARG A 1 65  ? 32.635  14.353  -12.683 1.00 36.74  ? 94  ARG A CD  1 
ATOM   510  N NE  . ARG A 1 65  ? 33.116  13.427  -11.654 1.00 36.06  ? 94  ARG A NE  1 
ATOM   511  C CZ  . ARG A 1 65  ? 33.587  13.791  -10.469 1.00 35.38  ? 94  ARG A CZ  1 
ATOM   512  N NH1 . ARG A 1 65  ? 33.610  15.061  -10.100 1.00 34.32  ? 94  ARG A NH1 1 
ATOM   513  N NH2 . ARG A 1 65  ? 34.048  12.870  -9.646  1.00 37.45  ? 94  ARG A NH2 1 
ATOM   514  N N   . GLY A 1 66  ? 30.413  17.491  -16.453 1.00 44.45  ? 95  GLY A N   1 
ATOM   515  C CA  . GLY A 1 66  ? 30.449  18.554  -17.444 1.00 40.58  ? 95  GLY A CA  1 
ATOM   516  C C   . GLY A 1 66  ? 30.338  18.037  -18.876 1.00 39.93  ? 95  GLY A C   1 
ATOM   517  O O   . GLY A 1 66  ? 30.424  18.836  -19.802 1.00 41.22  ? 95  GLY A O   1 
ATOM   518  N N   . PHE A 1 67  ? 30.157  16.718  -19.056 1.00 38.21  ? 96  PHE A N   1 
ATOM   519  C CA  . PHE A 1 67  ? 29.984  16.123  -20.376 1.00 36.97  ? 96  PHE A CA  1 
ATOM   520  C C   . PHE A 1 67  ? 28.517  15.735  -20.584 1.00 37.25  ? 96  PHE A C   1 
ATOM   521  O O   . PHE A 1 67  ? 27.883  15.162  -19.702 1.00 37.57  ? 96  PHE A O   1 
ATOM   522  C CB  . PHE A 1 67  ? 30.856  14.879  -20.581 1.00 36.87  ? 96  PHE A CB  1 
ATOM   523  C CG  . PHE A 1 67  ? 32.363  15.097  -20.627 1.00 39.89  ? 96  PHE A CG  1 
ATOM   524  C CD1 . PHE A 1 67  ? 33.008  15.382  -21.827 1.00 41.63  ? 96  PHE A CD1 1 
ATOM   525  C CD2 . PHE A 1 67  ? 33.141  14.989  -19.479 1.00 40.73  ? 96  PHE A CD2 1 
ATOM   526  C CE1 . PHE A 1 67  ? 34.384  15.567  -21.872 1.00 42.72  ? 96  PHE A CE1 1 
ATOM   527  C CE2 . PHE A 1 67  ? 34.518  15.177  -19.531 1.00 43.14  ? 96  PHE A CE2 1 
ATOM   528  C CZ  . PHE A 1 67  ? 35.138  15.465  -20.726 1.00 41.75  ? 96  PHE A CZ  1 
ATOM   529  N N   . SER A 1 68  ? 27.985  16.023  -21.776 1.00 37.26  ? 97  SER A N   1 
ATOM   530  C CA  . SER A 1 68  ? 26.616  15.668  -22.121 1.00 36.62  ? 97  SER A CA  1 
ATOM   531  C C   . SER A 1 68  ? 26.572  14.247  -22.670 1.00 39.00  ? 97  SER A C   1 
ATOM   532  O O   . SER A 1 68  ? 27.610  13.689  -23.022 1.00 40.12  ? 97  SER A O   1 
ATOM   533  C CB  . SER A 1 68  ? 26.052  16.640  -23.111 1.00 33.58  ? 97  SER A CB  1 
ATOM   534  O OG  . SER A 1 68  ? 26.895  16.700  -24.252 1.00 33.62  ? 97  SER A OG  1 
ATOM   535  N N   . ILE A 1 69  ? 25.355  13.695  -22.769 1.00 41.46  ? 98  ILE A N   1 
ATOM   536  C CA  . ILE A 1 69  ? 25.139  12.368  -23.330 1.00 43.70  ? 98  ILE A CA  1 
ATOM   537  C C   . ILE A 1 69  ? 25.733  12.280  -24.740 1.00 42.07  ? 98  ILE A C   1 
ATOM   538  O O   . ILE A 1 69  ? 26.377  11.285  -25.059 1.00 43.43  ? 98  ILE A O   1 
ATOM   539  C CB  . ILE A 1 69  ? 23.644  11.984  -23.329 1.00 46.51  ? 98  ILE A CB  1 
ATOM   540  C CG1 . ILE A 1 69  ? 23.041  11.903  -21.909 1.00 47.89  ? 98  ILE A CG1 1 
ATOM   541  C CG2 . ILE A 1 69  ? 23.422  10.686  -24.115 1.00 48.18  ? 98  ILE A CG2 1 
ATOM   542  C CD1 . ILE A 1 69  ? 23.010  10.513  -21.304 1.00 46.85  ? 98  ILE A CD1 1 
ATOM   543  N N   . PRO A 1 70  ? 25.494  13.243  -25.666 1.00 42.68  ? 99  PRO A N   1 
ATOM   544  C CA  . PRO A 1 70  ? 26.065  13.143  -27.016 1.00 42.69  ? 99  PRO A CA  1 
ATOM   545  C C   . PRO A 1 70  ? 27.595  13.082  -27.008 1.00 40.45  ? 99  PRO A C   1 
ATOM   546  O O   . PRO A 1 70  ? 28.197  12.234  -27.666 1.00 36.05  ? 99  PRO A O   1 
ATOM   547  C CB  . PRO A 1 70  ? 25.522  14.385  -27.752 1.00 42.14  ? 99  PRO A CB  1 
ATOM   548  C CG  . PRO A 1 70  ? 24.305  14.800  -26.948 1.00 42.62  ? 99  PRO A CG  1 
ATOM   549  C CD  . PRO A 1 70  ? 24.634  14.429  -25.507 1.00 41.20  ? 99  PRO A CD  1 
ATOM   550  N N   . GLU A 1 71  ? 28.224  13.961  -26.223 1.00 41.77  ? 100 GLU A N   1 
ATOM   551  C CA  . GLU A 1 71  ? 29.671  13.954  -26.074 1.00 42.60  ? 100 GLU A CA  1 
ATOM   552  C C   . GLU A 1 71  ? 30.158  12.584  -25.607 1.00 42.49  ? 100 GLU A C   1 
ATOM   553  O O   . GLU A 1 71  ? 31.124  12.049  -26.144 1.00 45.05  ? 100 GLU A O   1 
ATOM   554  C CB  . GLU A 1 71  ? 30.105  15.057  -25.117 1.00 45.15  ? 100 GLU A CB  1 
ATOM   555  C CG  . GLU A 1 71  ? 29.918  16.441  -25.724 1.00 49.56  ? 100 GLU A CG  1 
ATOM   556  C CD  . GLU A 1 71  ? 30.015  17.571  -24.721 1.00 57.58  ? 100 GLU A CD  1 
ATOM   557  O OE1 . GLU A 1 71  ? 30.855  18.477  -24.936 1.00 65.06  ? 100 GLU A OE1 1 
ATOM   558  O OE2 . GLU A 1 71  ? 29.258  17.536  -23.724 1.00 59.49  ? 100 GLU A OE2 1 
ATOM   559  N N   . CYS A 1 72  ? 29.471  12.011  -24.617 1.00 41.23  ? 101 CYS A N   1 
ATOM   560  C CA  . CYS A 1 72  ? 29.834  10.712  -24.077 1.00 38.66  ? 101 CYS A CA  1 
ATOM   561  C C   . CYS A 1 72  ? 29.758  9.626   -25.145 1.00 38.44  ? 101 CYS A C   1 
ATOM   562  O O   . CYS A 1 72  ? 30.677  8.827   -25.274 1.00 38.06  ? 101 CYS A O   1 
ATOM   563  C CB  . CYS A 1 72  ? 28.949  10.356  -22.892 1.00 38.72  ? 101 CYS A CB  1 
ATOM   564  S SG  . CYS A 1 72  ? 29.277  11.406  -21.457 1.00 40.28  ? 101 CYS A SG  1 
ATOM   565  N N   . GLN A 1 73  ? 28.650  9.588   -25.891 1.00 40.01  ? 102 GLN A N   1 
ATOM   566  C CA  . GLN A 1 73  ? 28.497  8.633   -26.976 1.00 42.95  ? 102 GLN A CA  1 
ATOM   567  C C   . GLN A 1 73  ? 29.660  8.754   -27.959 1.00 45.11  ? 102 GLN A C   1 
ATOM   568  O O   . GLN A 1 73  ? 30.134  7.748   -28.478 1.00 46.58  ? 102 GLN A O   1 
ATOM   569  C CB  . GLN A 1 73  ? 27.155  8.845   -27.677 1.00 45.70  ? 102 GLN A CB  1 
ATOM   570  C CG  . GLN A 1 73  ? 25.956  8.419   -26.837 1.00 47.07  ? 102 GLN A CG  1 
ATOM   571  C CD  . GLN A 1 73  ? 24.639  8.757   -27.495 1.00 51.35  ? 102 GLN A CD  1 
ATOM   572  O OE1 . GLN A 1 73  ? 24.276  9.929   -27.640 1.00 55.26  ? 102 GLN A OE1 1 
ATOM   573  N NE2 . GLN A 1 73  ? 23.909  7.729   -27.900 1.00 54.61  ? 102 GLN A NE2 1 
ATOM   574  N N   . LYS A 1 74  ? 30.110  9.989   -28.209 1.00 47.61  ? 103 LYS A N   1 
ATOM   575  C CA  . LYS A 1 74  ? 31.212  10.232  -29.123 1.00 51.61  ? 103 LYS A CA  1 
ATOM   576  C C   . LYS A 1 74  ? 32.555  9.900   -28.469 1.00 49.79  ? 103 LYS A C   1 
ATOM   577  O O   . LYS A 1 74  ? 33.413  9.319   -29.128 1.00 47.00  ? 103 LYS A O   1 
ATOM   578  C CB  . LYS A 1 74  ? 31.189  11.677  -29.635 1.00 58.14  ? 103 LYS A CB  1 
ATOM   579  C CG  . LYS A 1 74  ? 30.042  11.994  -30.589 1.00 63.80  ? 103 LYS A CG  1 
ATOM   580  C CD  . LYS A 1 74  ? 30.216  13.289  -31.374 1.00 68.29  ? 103 LYS A CD  1 
ATOM   581  C CE  . LYS A 1 74  ? 28.914  13.892  -31.818 1.00 69.62  ? 103 LYS A CE  1 
ATOM   582  N NZ  . LYS A 1 74  ? 28.174  14.511  -30.710 1.00 67.07  ? 103 LYS A NZ  1 
ATOM   583  N N   . LEU A 1 75  ? 32.729  10.261  -27.186 1.00 47.68  ? 104 LEU A N   1 
ATOM   584  C CA  . LEU A 1 75  ? 34.045  10.272  -26.556 1.00 45.12  ? 104 LEU A CA  1 
ATOM   585  C C   . LEU A 1 75  ? 34.336  8.957   -25.833 1.00 44.59  ? 104 LEU A C   1 
ATOM   586  O O   . LEU A 1 75  ? 35.451  8.452   -25.918 1.00 46.74  ? 104 LEU A O   1 
ATOM   587  C CB  . LEU A 1 75  ? 34.160  11.464  -25.605 1.00 43.83  ? 104 LEU A CB  1 
ATOM   588  C CG  . LEU A 1 75  ? 34.219  12.848  -26.261 1.00 43.88  ? 104 LEU A CG  1 
ATOM   589  C CD1 . LEU A 1 75  ? 34.051  13.945  -25.231 1.00 43.43  ? 104 LEU A CD1 1 
ATOM   590  C CD2 . LEU A 1 75  ? 35.517  13.046  -27.025 1.00 45.93  ? 104 LEU A CD2 1 
ATOM   591  N N   . LEU A 1 76  ? 33.351  8.416   -25.103 1.00 44.58  ? 105 LEU A N   1 
ATOM   592  C CA  . LEU A 1 76  ? 33.553  7.200   -24.327 1.00 42.57  ? 105 LEU A CA  1 
ATOM   593  C C   . LEU A 1 76  ? 33.908  6.050   -25.267 1.00 42.46  ? 105 LEU A C   1 
ATOM   594  O O   . LEU A 1 76  ? 33.372  5.973   -26.370 1.00 40.69  ? 105 LEU A O   1 
ATOM   595  C CB  . LEU A 1 76  ? 32.321  6.844   -23.493 1.00 41.37  ? 105 LEU A CB  1 
ATOM   596  C CG  . LEU A 1 76  ? 32.084  7.674   -22.228 1.00 42.57  ? 105 LEU A CG  1 
ATOM   597  C CD1 . LEU A 1 76  ? 30.739  7.349   -21.601 1.00 43.54  ? 105 LEU A CD1 1 
ATOM   598  C CD2 . LEU A 1 76  ? 33.194  7.451   -21.217 1.00 43.92  ? 105 LEU A CD2 1 
ATOM   599  N N   . PRO A 1 77  ? 34.815  5.128   -24.865 1.00 40.28  ? 106 PRO A N   1 
ATOM   600  C CA  . PRO A 1 77  ? 35.085  3.917   -25.643 1.00 42.04  ? 106 PRO A CA  1 
ATOM   601  C C   . PRO A 1 77  ? 33.870  3.019   -25.858 1.00 44.61  ? 106 PRO A C   1 
ATOM   602  O O   . PRO A 1 77  ? 32.882  3.117   -25.132 1.00 44.35  ? 106 PRO A O   1 
ATOM   603  C CB  . PRO A 1 77  ? 36.178  3.203   -24.828 1.00 40.26  ? 106 PRO A CB  1 
ATOM   604  C CG  . PRO A 1 77  ? 36.852  4.313   -24.064 1.00 40.31  ? 106 PRO A CG  1 
ATOM   605  C CD  . PRO A 1 77  ? 35.707  5.251   -23.701 1.00 41.50  ? 106 PRO A CD  1 
ATOM   606  N N   . LYS A 1 78  ? 33.994  2.124   -26.847 1.00 42.85  ? 107 LYS A N   1 
ATOM   607  C CA  . LYS A 1 78  ? 32.938  1.208   -27.244 1.00 43.37  ? 107 LYS A CA  1 
ATOM   608  C C   . LYS A 1 78  ? 33.486  -0.218  -27.236 1.00 43.62  ? 107 LYS A C   1 
ATOM   609  O O   . LYS A 1 78  ? 34.671  -0.426  -26.979 1.00 43.44  ? 107 LYS A O   1 
ATOM   610  C CB  . LYS A 1 78  ? 32.458  1.626   -28.639 1.00 44.01  ? 107 LYS A CB  1 
ATOM   611  C CG  . LYS A 1 78  ? 31.823  3.021   -28.706 1.00 45.35  ? 107 LYS A CG  1 
ATOM   612  C CD  . LYS A 1 78  ? 32.126  3.793   -29.985 1.00 43.84  ? 107 LYS A CD  1 
ATOM   613  C CE  . LYS A 1 78  ? 31.468  5.139   -30.077 1.00 43.74  ? 107 LYS A CE  1 
ATOM   614  N NZ  . LYS A 1 78  ? 31.632  5.941   -28.866 1.00 43.35  ? 107 LYS A NZ  1 
ATOM   615  N N   . ALA A 1 79  ? 32.615  -1.195  -27.513 1.00 45.00  ? 108 ALA A N   1 
ATOM   616  C CA  . ALA A 1 79  ? 33.045  -2.572  -27.695 1.00 49.53  ? 108 ALA A CA  1 
ATOM   617  C C   . ALA A 1 79  ? 33.662  -2.733  -29.083 1.00 54.66  ? 108 ALA A C   1 
ATOM   618  O O   . ALA A 1 79  ? 33.236  -2.086  -30.040 1.00 54.60  ? 108 ALA A O   1 
ATOM   619  C CB  . ALA A 1 79  ? 31.879  -3.518  -27.498 1.00 49.77  ? 108 ALA A CB  1 
ATOM   620  N N   . LYS A 1 80  ? 34.684  -3.592  -29.174 1.00 58.71  ? 109 LYS A N   1 
ATOM   621  C CA  . LYS A 1 80  ? 35.256  -3.985  -30.450 1.00 60.31  ? 109 LYS A CA  1 
ATOM   622  C C   . LYS A 1 80  ? 34.107  -4.359  -31.385 1.00 58.77  ? 109 LYS A C   1 
ATOM   623  O O   . LYS A 1 80  ? 33.312  -5.238  -31.059 1.00 54.28  ? 109 LYS A O   1 
ATOM   624  C CB  . LYS A 1 80  ? 36.257  -5.120  -30.197 1.00 66.44  ? 109 LYS A CB  1 
ATOM   625  C CG  . LYS A 1 80  ? 36.741  -5.916  -31.406 1.00 69.81  ? 109 LYS A CG  1 
ATOM   626  C CD  . LYS A 1 80  ? 37.773  -6.979  -31.042 1.00 73.20  ? 109 LYS A CD  1 
ATOM   627  C CE  . LYS A 1 80  ? 37.904  -8.075  -32.061 1.00 75.75  ? 109 LYS A CE  1 
ATOM   628  N NZ  . LYS A 1 80  ? 38.286  -7.583  -33.389 1.00 76.61  ? 109 LYS A NZ  1 
ATOM   629  N N   . GLY A 1 81  ? 34.014  -3.647  -32.519 1.00 59.07  ? 110 GLY A N   1 
ATOM   630  C CA  . GLY A 1 81  ? 32.914  -3.797  -33.461 1.00 59.18  ? 110 GLY A CA  1 
ATOM   631  C C   . GLY A 1 81  ? 31.575  -3.379  -32.851 1.00 61.58  ? 110 GLY A C   1 
ATOM   632  O O   . GLY A 1 81  ? 30.634  -4.170  -32.841 1.00 61.37  ? 110 GLY A O   1 
ATOM   633  N N   . GLY A 1 82  ? 31.497  -2.131  -32.358 1.00 59.71  ? 111 GLY A N   1 
ATOM   634  C CA  . GLY A 1 82  ? 30.302  -1.624  -31.696 1.00 58.32  ? 111 GLY A CA  1 
ATOM   635  C C   . GLY A 1 82  ? 30.170  -0.104  -31.819 1.00 56.93  ? 111 GLY A C   1 
ATOM   636  O O   . GLY A 1 82  ? 31.044  0.560   -32.371 1.00 59.82  ? 111 GLY A O   1 
ATOM   637  N N   . GLU A 1 83  ? 29.061  0.439   -31.301 1.00 54.29  ? 112 GLU A N   1 
ATOM   638  C CA  . GLU A 1 83  ? 28.726  1.845   -31.483 1.00 53.46  ? 112 GLU A CA  1 
ATOM   639  C C   . GLU A 1 83  ? 28.281  2.512   -30.175 1.00 48.18  ? 112 GLU A C   1 
ATOM   640  O O   . GLU A 1 83  ? 28.319  3.737   -30.064 1.00 44.75  ? 112 GLU A O   1 
ATOM   641  C CB  . GLU A 1 83  ? 27.618  1.955   -32.532 1.00 56.51  ? 112 GLU A CB  1 
ATOM   642  C CG  . GLU A 1 83  ? 27.766  0.965   -33.685 1.00 59.80  ? 112 GLU A CG  1 
ATOM   643  C CD  . GLU A 1 83  ? 26.779  1.162   -34.821 1.00 62.20  ? 112 GLU A CD  1 
ATOM   644  O OE1 . GLU A 1 83  ? 27.045  2.017   -35.695 1.00 61.74  ? 112 GLU A OE1 1 
ATOM   645  O OE2 . GLU A 1 83  ? 25.733  0.474   -34.816 1.00 64.14  ? 112 GLU A OE2 1 
ATOM   646  N N   . GLU A 1 84  ? 27.845  1.717   -29.188 1.00 44.12  ? 113 GLU A N   1 
ATOM   647  C CA  . GLU A 1 84  ? 27.230  2.256   -27.984 1.00 38.61  ? 113 GLU A CA  1 
ATOM   648  C C   . GLU A 1 84  ? 28.265  2.340   -26.864 1.00 36.63  ? 113 GLU A C   1 
ATOM   649  O O   . GLU A 1 84  ? 29.062  1.423   -26.677 1.00 35.93  ? 113 GLU A O   1 
ATOM   650  C CB  . GLU A 1 84  ? 26.006  1.410   -27.639 1.00 38.33  ? 113 GLU A CB  1 
ATOM   651  C CG  . GLU A 1 84  ? 24.896  1.486   -28.687 1.00 37.28  ? 113 GLU A CG  1 
ATOM   652  C CD  . GLU A 1 84  ? 24.308  2.867   -28.924 1.00 39.01  ? 113 GLU A CD  1 
ATOM   653  O OE1 . GLU A 1 84  ? 24.545  3.783   -28.107 1.00 38.97  ? 113 GLU A OE1 1 
ATOM   654  O OE2 . GLU A 1 84  ? 23.625  3.040   -29.956 1.00 42.41  ? 113 GLU A OE2 1 
ATOM   655  N N   . PRO A 1 85  ? 28.321  3.461   -26.104 1.00 36.97  ? 114 PRO A N   1 
ATOM   656  C CA  . PRO A 1 85  ? 29.353  3.633   -25.076 1.00 36.67  ? 114 PRO A CA  1 
ATOM   657  C C   . PRO A 1 85  ? 29.255  2.563   -23.990 1.00 37.14  ? 114 PRO A C   1 
ATOM   658  O O   . PRO A 1 85  ? 28.156  2.183   -23.595 1.00 40.16  ? 114 PRO A O   1 
ATOM   659  C CB  . PRO A 1 85  ? 29.108  5.065   -24.537 1.00 37.09  ? 114 PRO A CB  1 
ATOM   660  C CG  . PRO A 1 85  ? 27.684  5.392   -24.926 1.00 35.27  ? 114 PRO A CG  1 
ATOM   661  C CD  . PRO A 1 85  ? 27.426  4.626   -26.213 1.00 36.24  ? 114 PRO A CD  1 
ATOM   662  N N   . LEU A 1 86  ? 30.412  2.058   -23.540 1.00 37.73  ? 115 LEU A N   1 
ATOM   663  C CA  . LEU A 1 86  ? 30.455  1.042   -22.499 1.00 36.65  ? 115 LEU A CA  1 
ATOM   664  C C   . LEU A 1 86  ? 30.225  1.729   -21.157 1.00 35.21  ? 115 LEU A C   1 
ATOM   665  O O   . LEU A 1 86  ? 30.870  2.729   -20.876 1.00 36.26  ? 115 LEU A O   1 
ATOM   666  C CB  . LEU A 1 86  ? 31.782  0.284   -22.489 1.00 34.87  ? 115 LEU A CB  1 
ATOM   667  C CG  . LEU A 1 86  ? 32.106  -0.558  -23.727 1.00 36.58  ? 115 LEU A CG  1 
ATOM   668  C CD1 . LEU A 1 86  ? 33.501  -1.151  -23.615 1.00 37.78  ? 115 LEU A CD1 1 
ATOM   669  C CD2 . LEU A 1 86  ? 31.102  -1.666  -23.931 1.00 35.38  ? 115 LEU A CD2 1 
ATOM   670  N N   . PRO A 1 87  ? 29.283  1.252   -20.311 1.00 35.51  ? 116 PRO A N   1 
ATOM   671  C CA  . PRO A 1 87  ? 29.112  1.792   -18.954 1.00 34.42  ? 116 PRO A CA  1 
ATOM   672  C C   . PRO A 1 87  ? 30.378  1.797   -18.099 1.00 33.03  ? 116 PRO A C   1 
ATOM   673  O O   . PRO A 1 87  ? 30.551  2.676   -17.259 1.00 33.72  ? 116 PRO A O   1 
ATOM   674  C CB  . PRO A 1 87  ? 27.993  0.935   -18.327 1.00 33.47  ? 116 PRO A CB  1 
ATOM   675  C CG  . PRO A 1 87  ? 27.812  -0.233  -19.268 1.00 34.53  ? 116 PRO A CG  1 
ATOM   676  C CD  . PRO A 1 87  ? 28.275  0.237   -20.639 1.00 34.53  ? 116 PRO A CD  1 
ATOM   677  N N   . GLU A 1 88  ? 31.276  0.833   -18.327 1.00 31.72  ? 117 GLU A N   1 
ATOM   678  C CA  . GLU A 1 88  ? 32.595  0.879   -17.718 1.00 31.91  ? 117 GLU A CA  1 
ATOM   679  C C   . GLU A 1 88  ? 33.179  2.277   -17.883 1.00 31.15  ? 117 GLU A C   1 
ATOM   680  O O   . GLU A 1 88  ? 33.604  2.888   -16.903 1.00 33.61  ? 117 GLU A O   1 
ATOM   681  C CB  . GLU A 1 88  ? 33.572  -0.113  -18.349 1.00 33.34  ? 117 GLU A CB  1 
ATOM   682  C CG  . GLU A 1 88  ? 33.328  -1.561  -17.940 1.00 34.60  ? 117 GLU A CG  1 
ATOM   683  C CD  . GLU A 1 88  ? 32.449  -2.376  -18.862 1.00 35.29  ? 117 GLU A CD  1 
ATOM   684  O OE1 . GLU A 1 88  ? 31.464  -1.846  -19.416 1.00 37.33  ? 117 GLU A OE1 1 
ATOM   685  O OE2 . GLU A 1 88  ? 32.749  -3.580  -18.989 1.00 35.75  ? 117 GLU A OE2 1 
ATOM   686  N N   . GLY A 1 89  ? 33.205  2.751   -19.139 1.00 29.07  ? 118 GLY A N   1 
ATOM   687  C CA  . GLY A 1 89  ? 33.709  4.068   -19.481 1.00 29.68  ? 118 GLY A CA  1 
ATOM   688  C C   . GLY A 1 89  ? 33.021  5.177   -18.689 1.00 31.15  ? 118 GLY A C   1 
ATOM   689  O O   . GLY A 1 89  ? 33.683  6.074   -18.182 1.00 30.49  ? 118 GLY A O   1 
ATOM   690  N N   . LEU A 1 90  ? 31.686  5.113   -18.611 1.00 31.82  ? 119 LEU A N   1 
ATOM   691  C CA  . LEU A 1 90  ? 30.908  6.062   -17.836 1.00 30.78  ? 119 LEU A CA  1 
ATOM   692  C C   . LEU A 1 90  ? 31.397  6.045   -16.390 1.00 30.44  ? 119 LEU A C   1 
ATOM   693  O O   . LEU A 1 90  ? 31.637  7.097   -15.807 1.00 31.33  ? 119 LEU A O   1 
ATOM   694  C CB  . LEU A 1 90  ? 29.420  5.728   -17.963 1.00 31.77  ? 119 LEU A CB  1 
ATOM   695  C CG  . LEU A 1 90  ? 28.416  6.577   -17.164 1.00 33.00  ? 119 LEU A CG  1 
ATOM   696  C CD1 . LEU A 1 90  ? 28.427  6.252   -15.662 1.00 34.35  ? 119 LEU A CD1 1 
ATOM   697  C CD2 . LEU A 1 90  ? 28.619  8.072   -17.383 1.00 31.39  ? 119 LEU A CD2 1 
ATOM   698  N N   . PHE A 1 91  ? 31.552  4.850   -15.817 1.00 32.78  ? 120 PHE A N   1 
ATOM   699  C CA  . PHE A 1 91  ? 31.937  4.732   -14.419 1.00 33.67  ? 120 PHE A CA  1 
ATOM   700  C C   . PHE A 1 91  ? 33.302  5.381   -14.203 1.00 35.53  ? 120 PHE A C   1 
ATOM   701  O O   . PHE A 1 91  ? 33.503  6.040   -13.184 1.00 31.02  ? 120 PHE A O   1 
ATOM   702  C CB  . PHE A 1 91  ? 31.957  3.285   -13.916 1.00 33.88  ? 120 PHE A CB  1 
ATOM   703  C CG  . PHE A 1 91  ? 32.347  3.172   -12.448 1.00 34.08  ? 120 PHE A CG  1 
ATOM   704  C CD1 . PHE A 1 91  ? 31.418  3.430   -11.444 1.00 35.41  ? 120 PHE A CD1 1 
ATOM   705  C CD2 . PHE A 1 91  ? 33.645  2.843   -12.077 1.00 33.92  ? 120 PHE A CD2 1 
ATOM   706  C CE1 . PHE A 1 91  ? 31.778  3.342   -10.108 1.00 36.13  ? 120 PHE A CE1 1 
ATOM   707  C CE2 . PHE A 1 91  ? 34.001  2.754   -10.740 1.00 35.03  ? 120 PHE A CE2 1 
ATOM   708  C CZ  . PHE A 1 91  ? 33.068  2.997   -9.759  1.00 37.20  ? 120 PHE A CZ  1 
ATOM   709  N N   . TRP A 1 92  ? 34.223  5.183   -15.163 1.00 34.92  ? 121 TRP A N   1 
ATOM   710  C CA  . TRP A 1 92  ? 35.562  5.749   -15.086 1.00 34.99  ? 121 TRP A CA  1 
ATOM   711  C C   . TRP A 1 92  ? 35.490  7.267   -15.004 1.00 31.68  ? 121 TRP A C   1 
ATOM   712  O O   . TRP A 1 92  ? 36.203  7.870   -14.213 1.00 33.93  ? 121 TRP A O   1 
ATOM   713  C CB  . TRP A 1 92  ? 36.426  5.343   -16.290 1.00 38.09  ? 121 TRP A CB  1 
ATOM   714  C CG  . TRP A 1 92  ? 37.857  5.797   -16.158 1.00 40.92  ? 121 TRP A CG  1 
ATOM   715  C CD1 . TRP A 1 92  ? 38.359  7.043   -16.398 1.00 42.10  ? 121 TRP A CD1 1 
ATOM   716  C CD2 . TRP A 1 92  ? 38.973  5.001   -15.706 1.00 40.30  ? 121 TRP A CD2 1 
ATOM   717  N NE1 . TRP A 1 92  ? 39.703  7.077   -16.137 1.00 41.25  ? 121 TRP A NE1 1 
ATOM   718  C CE2 . TRP A 1 92  ? 40.108  5.842   -15.709 1.00 39.86  ? 121 TRP A CE2 1 
ATOM   719  C CE3 . TRP A 1 92  ? 39.120  3.671   -15.302 1.00 39.18  ? 121 TRP A CE3 1 
ATOM   720  C CZ2 . TRP A 1 92  ? 41.368  5.388   -15.329 1.00 40.18  ? 121 TRP A CZ2 1 
ATOM   721  C CZ3 . TRP A 1 92  ? 40.367  3.228   -14.918 1.00 38.73  ? 121 TRP A CZ3 1 
ATOM   722  C CH2 . TRP A 1 92  ? 41.470  4.075   -14.927 1.00 38.65  ? 121 TRP A CH2 1 
ATOM   723  N N   . LEU A 1 93  ? 34.637  7.863   -15.840 1.00 32.18  ? 122 LEU A N   1 
ATOM   724  C CA  . LEU A 1 93  ? 34.517  9.309   -15.958 1.00 32.26  ? 122 LEU A CA  1 
ATOM   725  C C   . LEU A 1 93  ? 33.934  9.920   -14.685 1.00 32.96  ? 122 LEU A C   1 
ATOM   726  O O   . LEU A 1 93  ? 34.325  11.017  -14.299 1.00 34.19  ? 122 LEU A O   1 
ATOM   727  C CB  . LEU A 1 93  ? 33.651  9.664   -17.166 1.00 31.21  ? 122 LEU A CB  1 
ATOM   728  C CG  . LEU A 1 93  ? 33.137  11.106  -17.224 1.00 30.56  ? 122 LEU A CG  1 
ATOM   729  C CD1 . LEU A 1 93  ? 34.302  12.085  -17.281 1.00 31.58  ? 122 LEU A CD1 1 
ATOM   730  C CD2 . LEU A 1 93  ? 32.190  11.299  -18.404 1.00 30.62  ? 122 LEU A CD2 1 
ATOM   731  N N   . LEU A 1 94  ? 32.960  9.238   -14.072 1.00 34.73  ? 123 LEU A N   1 
ATOM   732  C CA  . LEU A 1 94  ? 32.311  9.742   -12.871 1.00 31.87  ? 123 LEU A CA  1 
ATOM   733  C C   . LEU A 1 94  ? 33.285  9.696   -11.700 1.00 32.08  ? 123 LEU A C   1 
ATOM   734  O O   . LEU A 1 94  ? 33.292  10.606  -10.878 1.00 30.25  ? 123 LEU A O   1 
ATOM   735  C CB  . LEU A 1 94  ? 31.028  8.970   -12.576 1.00 31.30  ? 123 LEU A CB  1 
ATOM   736  C CG  . LEU A 1 94  ? 29.895  9.141   -13.595 1.00 31.55  ? 123 LEU A CG  1 
ATOM   737  C CD1 . LEU A 1 94  ? 28.624  8.430   -13.150 1.00 30.29  ? 123 LEU A CD1 1 
ATOM   738  C CD2 . LEU A 1 94  ? 29.616  10.618  -13.855 1.00 31.39  ? 123 LEU A CD2 1 
ATOM   739  N N   . VAL A 1 95  ? 34.121  8.656   -11.646 1.00 33.97  ? 124 VAL A N   1 
ATOM   740  C CA  . VAL A 1 95  ? 35.060  8.498   -10.545 1.00 37.38  ? 124 VAL A CA  1 
ATOM   741  C C   . VAL A 1 95  ? 36.245  9.451   -10.709 1.00 37.87  ? 124 VAL A C   1 
ATOM   742  O O   . VAL A 1 95  ? 36.616  10.108  -9.741  1.00 34.99  ? 124 VAL A O   1 
ATOM   743  C CB  . VAL A 1 95  ? 35.528  7.042   -10.377 1.00 38.98  ? 124 VAL A CB  1 
ATOM   744  C CG1 . VAL A 1 95  ? 36.634  6.921   -9.336  1.00 41.09  ? 124 VAL A CG1 1 
ATOM   745  C CG2 . VAL A 1 95  ? 34.366  6.136   -9.996  1.00 40.24  ? 124 VAL A CG2 1 
ATOM   746  N N   . THR A 1 96  ? 36.814  9.548   -11.921 1.00 39.20  ? 125 THR A N   1 
ATOM   747  C CA  . THR A 1 96  ? 38.042  10.310  -12.130 1.00 41.57  ? 125 THR A CA  1 
ATOM   748  C C   . THR A 1 96  ? 37.763  11.739  -12.609 1.00 41.56  ? 125 THR A C   1 
ATOM   749  O O   . THR A 1 96  ? 38.525  12.655  -12.298 1.00 40.77  ? 125 THR A O   1 
ATOM   750  C CB  . THR A 1 96  ? 38.945  9.574   -13.118 1.00 41.23  ? 125 THR A CB  1 
ATOM   751  O OG1 . THR A 1 96  ? 38.250  9.541   -14.360 1.00 39.01  ? 125 THR A OG1 1 
ATOM   752  C CG2 . THR A 1 96  ? 39.277  8.170   -12.647 1.00 44.25  ? 125 THR A CG2 1 
ATOM   753  N N   . GLY A 1 97  ? 36.713  11.922  -13.415 1.00 39.70  ? 126 GLY A N   1 
ATOM   754  C CA  . GLY A 1 97  ? 36.452  13.201  -14.055 1.00 37.62  ? 126 GLY A CA  1 
ATOM   755  C C   . GLY A 1 97  ? 37.081  13.285  -15.444 1.00 39.02  ? 126 GLY A C   1 
ATOM   756  O O   . GLY A 1 97  ? 36.909  14.285  -16.130 1.00 40.58  ? 126 GLY A O   1 
ATOM   757  N N   . HIS A 1 98  ? 37.786  12.225  -15.866 1.00 39.37  ? 127 HIS A N   1 
ATOM   758  C CA  . HIS A 1 98  ? 38.450  12.200  -17.160 1.00 40.10  ? 127 HIS A CA  1 
ATOM   759  C C   . HIS A 1 98  ? 37.842  11.088  -18.009 1.00 39.56  ? 127 HIS A C   1 
ATOM   760  O O   . HIS A 1 98  ? 37.359  10.093  -17.477 1.00 40.64  ? 127 HIS A O   1 
ATOM   761  C CB  . HIS A 1 98  ? 39.965  12.001  -16.996 1.00 43.19  ? 127 HIS A CB  1 
ATOM   762  C CG  . HIS A 1 98  ? 40.613  12.986  -16.077 1.00 48.43  ? 127 HIS A CG  1 
ATOM   763  N ND1 . HIS A 1 98  ? 40.434  14.352  -16.167 1.00 47.76  ? 127 HIS A ND1 1 
ATOM   764  C CD2 . HIS A 1 98  ? 41.439  12.789  -15.041 1.00 51.81  ? 127 HIS A CD2 1 
ATOM   765  C CE1 . HIS A 1 98  ? 41.128  14.948  -15.208 1.00 51.58  ? 127 HIS A CE1 1 
ATOM   766  N NE2 . HIS A 1 98  ? 41.746  14.019  -14.509 1.00 52.44  ? 127 HIS A NE2 1 
ATOM   767  N N   . ILE A 1 99  ? 37.896  11.275  -19.333 1.00 38.54  ? 128 ILE A N   1 
ATOM   768  C CA  . ILE A 1 99  ? 37.457  10.297  -20.315 1.00 36.66  ? 128 ILE A CA  1 
ATOM   769  C C   . ILE A 1 99  ? 38.486  9.173   -20.377 1.00 39.65  ? 128 ILE A C   1 
ATOM   770  O O   . ILE A 1 99  ? 39.664  9.439   -20.602 1.00 44.27  ? 128 ILE A O   1 
ATOM   771  C CB  . ILE A 1 99  ? 37.291  10.989  -21.683 1.00 35.81  ? 128 ILE A CB  1 
ATOM   772  C CG1 . ILE A 1 99  ? 36.182  12.036  -21.655 1.00 34.39  ? 128 ILE A CG1 1 
ATOM   773  C CG2 . ILE A 1 99  ? 37.066  9.978   -22.808 1.00 35.57  ? 128 ILE A CG2 1 
ATOM   774  C CD1 . ILE A 1 99  ? 34.781  11.454  -21.648 1.00 32.79  ? 128 ILE A CD1 1 
ATOM   775  N N   . PRO A 1 100 ? 38.099  7.890   -20.188 1.00 41.39  ? 129 PRO A N   1 
ATOM   776  C CA  . PRO A 1 100 ? 39.072  6.798   -20.182 1.00 40.71  ? 129 PRO A CA  1 
ATOM   777  C C   . PRO A 1 100 ? 39.510  6.394   -21.584 1.00 41.51  ? 129 PRO A C   1 
ATOM   778  O O   . PRO A 1 100 ? 38.783  6.633   -22.544 1.00 42.53  ? 129 PRO A O   1 
ATOM   779  C CB  . PRO A 1 100 ? 38.304  5.678   -19.488 1.00 39.70  ? 129 PRO A CB  1 
ATOM   780  C CG  . PRO A 1 100 ? 36.879  5.898   -19.942 1.00 40.86  ? 129 PRO A CG  1 
ATOM   781  C CD  . PRO A 1 100 ? 36.722  7.416   -19.965 1.00 40.08  ? 129 PRO A CD  1 
ATOM   782  N N   . THR A 1 101 ? 40.682  5.746   -21.670 1.00 42.39  ? 130 THR A N   1 
ATOM   783  C CA  . THR A 1 101 ? 41.217  5.248   -22.931 1.00 43.34  ? 130 THR A CA  1 
ATOM   784  C C   . THR A 1 101 ? 40.647  3.861   -23.218 1.00 42.35  ? 130 THR A C   1 
ATOM   785  O O   . THR A 1 101 ? 39.964  3.285   -22.374 1.00 40.81  ? 130 THR A O   1 
ATOM   786  C CB  . THR A 1 101 ? 42.747  5.214   -22.886 1.00 42.96  ? 130 THR A CB  1 
ATOM   787  O OG1 . THR A 1 101 ? 43.068  4.033   -22.157 1.00 39.74  ? 130 THR A OG1 1 
ATOM   788  C CG2 . THR A 1 101 ? 43.341  6.475   -22.279 1.00 42.49  ? 130 THR A CG2 1 
ATOM   789  N N   . GLU A 1 102 ? 40.950  3.334   -24.414 1.00 45.95  ? 131 GLU A N   1 
ATOM   790  C CA  . GLU A 1 102 ? 40.619  1.963   -24.769 1.00 48.57  ? 131 GLU A CA  1 
ATOM   791  C C   . GLU A 1 102 ? 41.130  1.034   -23.670 1.00 49.28  ? 131 GLU A C   1 
ATOM   792  O O   . GLU A 1 102 ? 40.389  0.186   -23.180 1.00 49.86  ? 131 GLU A O   1 
ATOM   793  C CB  . GLU A 1 102 ? 41.248  1.454   -26.069 1.00 53.63  ? 131 GLU A CB  1 
ATOM   794  C CG  . GLU A 1 102 ? 41.150  2.387   -27.276 1.00 60.32  ? 131 GLU A CG  1 
ATOM   795  C CD  . GLU A 1 102 ? 39.761  2.750   -27.775 1.00 66.43  ? 131 GLU A CD  1 
ATOM   796  O OE1 . GLU A 1 102 ? 38.751  2.233   -27.254 1.00 63.81  ? 131 GLU A OE1 1 
ATOM   797  O OE2 . GLU A 1 102 ? 39.700  3.572   -28.715 1.00 73.67  ? 131 GLU A OE2 1 
ATOM   798  N N   . GLU A 1 103 ? 42.404  1.213   -23.295 1.00 48.58  ? 132 GLU A N   1 
ATOM   799  C CA  . GLU A 1 103 ? 43.094  0.321   -22.375 1.00 50.58  ? 132 GLU A CA  1 
ATOM   800  C C   . GLU A 1 103 ? 42.440  0.394   -20.996 1.00 46.97  ? 132 GLU A C   1 
ATOM   801  O O   . GLU A 1 103 ? 42.150  -0.630  -20.378 1.00 46.99  ? 132 GLU A O   1 
ATOM   802  C CB  . GLU A 1 103 ? 44.579  0.683   -22.261 1.00 55.73  ? 132 GLU A CB  1 
ATOM   803  C CG  . GLU A 1 103 ? 45.394  0.426   -23.530 1.00 62.62  ? 132 GLU A CG  1 
ATOM   804  C CD  . GLU A 1 103 ? 45.220  1.403   -24.690 1.00 69.66  ? 132 GLU A CD  1 
ATOM   805  O OE1 . GLU A 1 103 ? 44.648  2.501   -24.492 1.00 75.76  ? 132 GLU A OE1 1 
ATOM   806  O OE2 . GLU A 1 103 ? 45.650  1.060   -25.814 1.00 70.66  ? 132 GLU A OE2 1 
ATOM   807  N N   . GLN A 1 104 ? 42.229  1.625   -20.522 1.00 42.29  ? 133 GLN A N   1 
ATOM   808  C CA  . GLN A 1 104 ? 41.704  1.872   -19.190 1.00 39.89  ? 133 GLN A CA  1 
ATOM   809  C C   . GLN A 1 104 ? 40.348  1.198   -18.989 1.00 36.88  ? 133 GLN A C   1 
ATOM   810  O O   . GLN A 1 104 ? 40.118  0.595   -17.946 1.00 34.67  ? 133 GLN A O   1 
ATOM   811  C CB  . GLN A 1 104 ? 41.632  3.376   -18.956 1.00 39.47  ? 133 GLN A CB  1 
ATOM   812  C CG  . GLN A 1 104 ? 42.968  3.986   -18.554 1.00 40.00  ? 133 GLN A CG  1 
ATOM   813  C CD  . GLN A 1 104 ? 42.888  5.483   -18.371 1.00 40.29  ? 133 GLN A CD  1 
ATOM   814  O OE1 . GLN A 1 104 ? 41.987  6.148   -18.896 1.00 41.43  ? 133 GLN A OE1 1 
ATOM   815  N NE2 . GLN A 1 104 ? 43.842  6.026   -17.634 1.00 40.29  ? 133 GLN A NE2 1 
ATOM   816  N N   . VAL A 1 105 ? 39.466  1.290   -19.991 1.00 35.92  ? 134 VAL A N   1 
ATOM   817  C CA  . VAL A 1 105 ? 38.165  0.641   -19.932 1.00 36.65  ? 134 VAL A CA  1 
ATOM   818  C C   . VAL A 1 105 ? 38.333  -0.881  -19.955 1.00 37.94  ? 134 VAL A C   1 
ATOM   819  O O   . VAL A 1 105 ? 37.689  -1.579  -19.176 1.00 37.04  ? 134 VAL A O   1 
ATOM   820  C CB  . VAL A 1 105 ? 37.257  1.149   -21.072 1.00 37.09  ? 134 VAL A CB  1 
ATOM   821  C CG1 . VAL A 1 105 ? 36.085  0.213   -21.355 1.00 36.85  ? 134 VAL A CG1 1 
ATOM   822  C CG2 . VAL A 1 105 ? 36.760  2.567   -20.798 1.00 35.16  ? 134 VAL A CG2 1 
ATOM   823  N N   . SER A 1 106 ? 39.207  -1.386  -20.838 1.00 38.92  ? 135 SER A N   1 
ATOM   824  C CA  A SER A 1 106 ? 39.452  -2.816  -20.947 0.50 38.99  ? 135 SER A CA  1 
ATOM   825  C CA  B SER A 1 106 ? 39.483  -2.812  -20.953 0.50 39.26  ? 135 SER A CA  1 
ATOM   826  C C   . SER A 1 106 ? 39.788  -3.395  -19.574 1.00 40.12  ? 135 SER A C   1 
ATOM   827  O O   . SER A 1 106 ? 39.172  -4.368  -19.146 1.00 41.54  ? 135 SER A O   1 
ATOM   828  C CB  A SER A 1 106 ? 40.538  -3.112  -21.950 0.50 39.25  ? 135 SER A CB  1 
ATOM   829  C CB  B SER A 1 106 ? 40.632  -3.080  -21.909 0.50 39.81  ? 135 SER A CB  1 
ATOM   830  O OG  A SER A 1 106 ? 40.591  -4.501  -22.239 0.50 37.30  ? 135 SER A OG  1 
ATOM   831  O OG  B SER A 1 106 ? 40.578  -2.251  -23.064 0.50 38.45  ? 135 SER A OG  1 
ATOM   832  N N   . TRP A 1 107 ? 40.763  -2.781  -18.894 1.00 39.77  ? 136 TRP A N   1 
ATOM   833  C CA  . TRP A 1 107 ? 41.153  -3.157  -17.545 1.00 43.44  ? 136 TRP A CA  1 
ATOM   834  C C   . TRP A 1 107 ? 39.930  -3.216  -16.623 1.00 44.81  ? 136 TRP A C   1 
ATOM   835  O O   . TRP A 1 107 ? 39.735  -4.193  -15.899 1.00 44.07  ? 136 TRP A O   1 
ATOM   836  C CB  . TRP A 1 107 ? 42.200  -2.155  -17.034 1.00 43.88  ? 136 TRP A CB  1 
ATOM   837  C CG  . TRP A 1 107 ? 42.655  -2.369  -15.615 1.00 46.18  ? 136 TRP A CG  1 
ATOM   838  C CD1 . TRP A 1 107 ? 43.699  -3.139  -15.201 1.00 47.83  ? 136 TRP A CD1 1 
ATOM   839  C CD2 . TRP A 1 107 ? 42.096  -1.779  -14.420 1.00 49.25  ? 136 TRP A CD2 1 
ATOM   840  N NE1 . TRP A 1 107 ? 43.824  -3.084  -13.840 1.00 49.04  ? 136 TRP A NE1 1 
ATOM   841  C CE2 . TRP A 1 107 ? 42.859  -2.257  -13.332 1.00 51.16  ? 136 TRP A CE2 1 
ATOM   842  C CE3 . TRP A 1 107 ? 41.034  -0.905  -14.161 1.00 51.68  ? 136 TRP A CE3 1 
ATOM   843  C CZ2 . TRP A 1 107 ? 42.584  -1.894  -12.013 1.00 50.97  ? 136 TRP A CZ2 1 
ATOM   844  C CZ3 . TRP A 1 107 ? 40.766  -0.543  -12.857 1.00 48.86  ? 136 TRP A CZ3 1 
ATOM   845  C CH2 . TRP A 1 107 ? 41.528  -1.036  -11.799 1.00 49.22  ? 136 TRP A CH2 1 
ATOM   846  N N   . LEU A 1 108 ? 39.094  -2.172  -16.665 1.00 42.73  ? 137 LEU A N   1 
ATOM   847  C CA  . LEU A 1 108 ? 37.988  -2.055  -15.731 1.00 40.27  ? 137 LEU A CA  1 
ATOM   848  C C   . LEU A 1 108 ? 37.046  -3.241  -15.911 1.00 39.57  ? 137 LEU A C   1 
ATOM   849  O O   . LEU A 1 108 ? 36.505  -3.752  -14.933 1.00 36.03  ? 137 LEU A O   1 
ATOM   850  C CB  . LEU A 1 108 ? 37.264  -0.719  -15.891 1.00 40.75  ? 137 LEU A CB  1 
ATOM   851  C CG  . LEU A 1 108 ? 36.118  -0.458  -14.905 1.00 41.07  ? 137 LEU A CG  1 
ATOM   852  C CD1 . LEU A 1 108 ? 36.515  -0.800  -13.482 1.00 39.78  ? 137 LEU A CD1 1 
ATOM   853  C CD2 . LEU A 1 108 ? 35.659  0.985   -14.976 1.00 41.39  ? 137 LEU A CD2 1 
ATOM   854  N N   . SER A 1 109 ? 36.879  -3.681  -17.165 1.00 41.01  ? 138 SER A N   1 
ATOM   855  C CA  . SER A 1 109 ? 36.023  -4.807  -17.489 1.00 42.03  ? 138 SER A CA  1 
ATOM   856  C C   . SER A 1 109 ? 36.536  -6.074  -16.813 1.00 44.45  ? 138 SER A C   1 
ATOM   857  O O   . SER A 1 109 ? 35.746  -6.839  -16.264 1.00 44.70  ? 138 SER A O   1 
ATOM   858  C CB  . SER A 1 109 ? 35.904  -5.001  -18.981 1.00 43.93  ? 138 SER A CB  1 
ATOM   859  O OG  . SER A 1 109 ? 35.270  -3.888  -19.592 1.00 44.09  ? 138 SER A OG  1 
ATOM   860  N N   . LYS A 1 110 ? 37.859  -6.278  -16.854 1.00 47.83  ? 139 LYS A N   1 
ATOM   861  C CA  . LYS A 1 110 ? 38.468  -7.477  -16.299 1.00 52.02  ? 139 LYS A CA  1 
ATOM   862  C C   . LYS A 1 110 ? 38.295  -7.493  -14.781 1.00 48.09  ? 139 LYS A C   1 
ATOM   863  O O   . LYS A 1 110 ? 37.966  -8.528  -14.205 1.00 49.47  ? 139 LYS A O   1 
ATOM   864  C CB  . LYS A 1 110 ? 39.941  -7.560  -16.715 1.00 56.99  ? 139 LYS A CB  1 
ATOM   865  C CG  . LYS A 1 110 ? 40.148  -7.739  -18.209 1.00 60.66  ? 139 LYS A CG  1 
ATOM   866  C CD  . LYS A 1 110 ? 41.575  -7.504  -18.685 1.00 65.34  ? 139 LYS A CD  1 
ATOM   867  C CE  . LYS A 1 110 ? 41.646  -7.343  -20.175 1.00 67.47  ? 139 LYS A CE  1 
ATOM   868  N NZ  . LYS A 1 110 ? 43.020  -7.083  -20.608 1.00 69.12  ? 139 LYS A NZ  1 
ATOM   869  N N   . GLU A 1 111 ? 38.499  -6.334  -14.153 1.00 47.37  ? 140 GLU A N   1 
ATOM   870  C CA  . GLU A 1 111 ? 38.428  -6.208  -12.705 1.00 51.46  ? 140 GLU A CA  1 
ATOM   871  C C   . GLU A 1 111 ? 37.026  -6.548  -12.205 1.00 51.14  ? 140 GLU A C   1 
ATOM   872  O O   . GLU A 1 111 ? 36.890  -7.162  -11.152 1.00 53.03  ? 140 GLU A O   1 
ATOM   873  C CB  . GLU A 1 111 ? 38.820  -4.802  -12.251 1.00 53.38  ? 140 GLU A CB  1 
ATOM   874  C CG  . GLU A 1 111 ? 40.275  -4.450  -12.556 1.00 56.86  ? 140 GLU A CG  1 
ATOM   875  C CD  . GLU A 1 111 ? 41.312  -5.065  -11.631 1.00 57.34  ? 140 GLU A CD  1 
ATOM   876  O OE1 . GLU A 1 111 ? 41.392  -4.600  -10.475 1.00 57.90  ? 140 GLU A OE1 1 
ATOM   877  O OE2 . GLU A 1 111 ? 42.029  -5.999  -12.057 1.00 58.13  ? 140 GLU A OE2 1 
ATOM   878  N N   . TRP A 1 112 ? 35.993  -6.144  -12.957 1.00 51.82  ? 141 TRP A N   1 
ATOM   879  C CA  . TRP A 1 112 ? 34.617  -6.399  -12.558 1.00 50.10  ? 141 TRP A CA  1 
ATOM   880  C C   . TRP A 1 112 ? 34.263  -7.862  -12.805 1.00 51.12  ? 141 TRP A C   1 
ATOM   881  O O   . TRP A 1 112 ? 33.551  -8.467  -12.006 1.00 52.52  ? 141 TRP A O   1 
ATOM   882  C CB  . TRP A 1 112 ? 33.640  -5.451  -13.274 1.00 48.97  ? 141 TRP A CB  1 
ATOM   883  C CG  . TRP A 1 112 ? 33.660  -4.031  -12.761 1.00 44.79  ? 141 TRP A CG  1 
ATOM   884  C CD1 . TRP A 1 112 ? 34.338  -3.543  -11.680 1.00 44.56  ? 141 TRP A CD1 1 
ATOM   885  C CD2 . TRP A 1 112 ? 32.930  -2.915  -13.312 1.00 40.71  ? 141 TRP A CD2 1 
ATOM   886  N NE1 . TRP A 1 112 ? 34.101  -2.203  -11.537 1.00 46.27  ? 141 TRP A NE1 1 
ATOM   887  C CE2 . TRP A 1 112 ? 33.242  -1.789  -12.522 1.00 42.62  ? 141 TRP A CE2 1 
ATOM   888  C CE3 . TRP A 1 112 ? 32.062  -2.754  -14.396 1.00 41.92  ? 141 TRP A CE3 1 
ATOM   889  C CZ2 . TRP A 1 112 ? 32.711  -0.528  -12.785 1.00 39.74  ? 141 TRP A CZ2 1 
ATOM   890  C CZ3 . TRP A 1 112 ? 31.536  -1.506  -14.652 1.00 41.42  ? 141 TRP A CZ3 1 
ATOM   891  C CH2 . TRP A 1 112 ? 31.852  -0.410  -13.852 1.00 39.92  ? 141 TRP A CH2 1 
ATOM   892  N N   . ALA A 1 113 ? 34.776  -8.420  -13.906 1.00 49.82  ? 142 ALA A N   1 
ATOM   893  C CA  . ALA A 1 113 ? 34.679  -9.848  -14.165 1.00 50.45  ? 142 ALA A CA  1 
ATOM   894  C C   . ALA A 1 113 ? 35.383  -10.646 -13.066 1.00 48.37  ? 142 ALA A C   1 
ATOM   895  O O   . ALA A 1 113 ? 34.894  -11.695 -12.661 1.00 46.49  ? 142 ALA A O   1 
ATOM   896  C CB  . ALA A 1 113 ? 35.258  -10.168 -15.525 1.00 51.57  ? 142 ALA A CB  1 
ATOM   897  N N   . LYS A 1 114 ? 36.531  -10.148 -12.587 1.00 48.42  ? 143 LYS A N   1 
ATOM   898  C CA  . LYS A 1 114 ? 37.287  -10.834 -11.549 1.00 49.74  ? 143 LYS A CA  1 
ATOM   899  C C   . LYS A 1 114 ? 36.460  -10.955 -10.272 1.00 51.26  ? 143 LYS A C   1 
ATOM   900  O O   . LYS A 1 114 ? 36.577  -11.954 -9.566  1.00 51.63  ? 143 LYS A O   1 
ATOM   901  C CB  . LYS A 1 114 ? 38.579  -10.106 -11.158 1.00 50.36  ? 143 LYS A CB  1 
ATOM   902  C CG  . LYS A 1 114 ? 39.778  -10.317 -12.059 1.00 52.95  ? 143 LYS A CG  1 
ATOM   903  C CD  . LYS A 1 114 ? 40.984  -9.481  -11.642 1.00 54.87  ? 143 LYS A CD  1 
ATOM   904  C CE  . LYS A 1 114 ? 42.080  -9.517  -12.662 1.00 54.54  ? 143 LYS A CE  1 
ATOM   905  N NZ  . LYS A 1 114 ? 43.143  -8.563  -12.344 1.00 54.56  ? 143 LYS A NZ  1 
ATOM   906  N N   . ARG A 1 115 ? 35.640  -9.929  -9.986  1.00 50.21  ? 144 ARG A N   1 
ATOM   907  C CA  . ARG A 1 115 ? 34.981  -9.779  -8.698  1.00 45.10  ? 144 ARG A CA  1 
ATOM   908  C C   . ARG A 1 115 ? 33.526  -10.256 -8.734  1.00 44.11  ? 144 ARG A C   1 
ATOM   909  O O   . ARG A 1 115 ? 32.760  -9.963  -7.817  1.00 45.45  ? 144 ARG A O   1 
ATOM   910  C CB  . ARG A 1 115 ? 35.054  -8.297  -8.308  1.00 45.74  ? 144 ARG A CB  1 
ATOM   911  C CG  . ARG A 1 115 ? 36.438  -7.713  -8.065  1.00 44.39  ? 144 ARG A CG  1 
ATOM   912  C CD  . ARG A 1 115 ? 36.387  -6.188  -8.045  1.00 44.46  ? 144 ARG A CD  1 
ATOM   913  N NE  . ARG A 1 115 ? 37.653  -5.545  -7.670  1.00 44.37  ? 144 ARG A NE  1 
ATOM   914  C CZ  . ARG A 1 115 ? 37.940  -4.949  -6.505  1.00 44.18  ? 144 ARG A CZ  1 
ATOM   915  N NH1 . ARG A 1 115 ? 37.129  -5.051  -5.465  1.00 41.13  ? 144 ARG A NH1 1 
ATOM   916  N NH2 . ARG A 1 115 ? 39.072  -4.274  -6.374  1.00 43.17  ? 144 ARG A NH2 1 
ATOM   917  N N   . ALA A 1 116 ? 33.146  -11.045 -9.746  1.00 45.59  ? 145 ALA A N   1 
ATOM   918  C CA  . ALA A 1 116 ? 31.740  -11.330 -10.002 1.00 48.11  ? 145 ALA A CA  1 
ATOM   919  C C   . ALA A 1 116 ? 31.196  -12.492 -9.160  1.00 51.20  ? 145 ALA A C   1 
ATOM   920  O O   . ALA A 1 116 ? 30.040  -12.873 -9.331  1.00 50.93  ? 145 ALA A O   1 
ATOM   921  C CB  . ALA A 1 116 ? 31.544  -11.597 -11.476 1.00 46.22  ? 145 ALA A CB  1 
ATOM   922  N N   . ALA A 1 117 ? 31.995  -13.050 -8.242  1.00 53.13  ? 146 ALA A N   1 
ATOM   923  C CA  . ALA A 1 117 ? 31.564  -14.217 -7.485  1.00 56.33  ? 146 ALA A CA  1 
ATOM   924  C C   . ALA A 1 117 ? 30.483  -13.825 -6.482  1.00 53.52  ? 146 ALA A C   1 
ATOM   925  O O   . ALA A 1 117 ? 30.646  -12.841 -5.771  1.00 54.35  ? 146 ALA A O   1 
ATOM   926  C CB  . ALA A 1 117 ? 32.743  -14.854 -6.782  1.00 57.16  ? 146 ALA A CB  1 
ATOM   927  N N   . LEU A 1 118 ? 29.404  -14.620 -6.428  1.00 51.81  ? 147 LEU A N   1 
ATOM   928  C CA  . LEU A 1 118 ? 28.316  -14.426 -5.477  1.00 51.51  ? 147 LEU A CA  1 
ATOM   929  C C   . LEU A 1 118 ? 28.481  -15.369 -4.288  1.00 50.48  ? 147 LEU A C   1 
ATOM   930  O O   . LEU A 1 118 ? 28.537  -16.582 -4.470  1.00 52.49  ? 147 LEU A O   1 
ATOM   931  C CB  . LEU A 1 118 ? 26.967  -14.685 -6.145  1.00 51.22  ? 147 LEU A CB  1 
ATOM   932  C CG  . LEU A 1 118 ? 26.430  -13.592 -7.072  1.00 50.32  ? 147 LEU A CG  1 
ATOM   933  C CD1 . LEU A 1 118 ? 25.164  -14.098 -7.724  1.00 51.86  ? 147 LEU A CD1 1 
ATOM   934  C CD2 . LEU A 1 118 ? 26.166  -12.282 -6.346  1.00 49.50  ? 147 LEU A CD2 1 
ATOM   935  N N   . PRO A 1 119 ? 28.493  -14.868 -3.031  1.00 50.00  ? 148 PRO A N   1 
ATOM   936  C CA  . PRO A 1 119 ? 28.472  -15.753 -1.866  1.00 48.19  ? 148 PRO A CA  1 
ATOM   937  C C   . PRO A 1 119 ? 27.289  -16.712 -1.957  1.00 48.64  ? 148 PRO A C   1 
ATOM   938  O O   . PRO A 1 119 ? 26.232  -16.357 -2.479  1.00 46.49  ? 148 PRO A O   1 
ATOM   939  C CB  . PRO A 1 119 ? 28.392  -14.817 -0.647  1.00 47.59  ? 148 PRO A CB  1 
ATOM   940  C CG  . PRO A 1 119 ? 28.035  -13.462 -1.223  1.00 47.53  ? 148 PRO A CG  1 
ATOM   941  C CD  . PRO A 1 119 ? 28.527  -13.445 -2.660  1.00 48.46  ? 148 PRO A CD  1 
ATOM   942  N N   . SER A 1 120 ? 27.485  -17.934 -1.448  1.00 51.29  ? 149 SER A N   1 
ATOM   943  C CA  . SER A 1 120 ? 26.522  -19.009 -1.639  1.00 49.87  ? 149 SER A CA  1 
ATOM   944  C C   . SER A 1 120 ? 25.235  -18.747 -0.853  1.00 43.70  ? 149 SER A C   1 
ATOM   945  O O   . SER A 1 120 ? 24.157  -19.151 -1.283  1.00 43.76  ? 149 SER A O   1 
ATOM   946  C CB  . SER A 1 120 ? 27.128  -20.356 -1.299  1.00 53.26  ? 149 SER A CB  1 
ATOM   947  O OG  . SER A 1 120 ? 27.915  -20.309 -0.114  1.00 52.48  ? 149 SER A OG  1 
ATOM   948  N N   . HIS A 1 121 ? 25.328  -18.055 0.286   1.00 42.09  ? 150 HIS A N   1 
ATOM   949  C CA  . HIS A 1 121 ? 24.127  -17.784 1.066   1.00 42.95  ? 150 HIS A CA  1 
ATOM   950  C C   . HIS A 1 121 ? 23.192  -16.893 0.250   1.00 38.83  ? 150 HIS A C   1 
ATOM   951  O O   . HIS A 1 121 ? 21.977  -17.025 0.346   1.00 39.49  ? 150 HIS A O   1 
ATOM   952  C CB  . HIS A 1 121 ? 24.456  -17.267 2.474   1.00 41.17  ? 150 HIS A CB  1 
ATOM   953  C CG  . HIS A 1 121 ? 24.691  -15.797 2.586   1.00 42.92  ? 150 HIS A CG  1 
ATOM   954  N ND1 . HIS A 1 121 ? 25.933  -15.220 2.434   1.00 40.52  ? 150 HIS A ND1 1 
ATOM   955  C CD2 . HIS A 1 121 ? 23.847  -14.790 2.883   1.00 43.36  ? 150 HIS A CD2 1 
ATOM   956  C CE1 . HIS A 1 121 ? 25.824  -13.908 2.597   1.00 42.12  ? 150 HIS A CE1 1 
ATOM   957  N NE2 . HIS A 1 121 ? 24.569  -13.624 2.879   1.00 39.84  ? 150 HIS A NE2 1 
ATOM   958  N N   . VAL A 1 122 ? 23.763  -16.021 -0.588  1.00 40.00  ? 151 VAL A N   1 
ATOM   959  C CA  . VAL A 1 122 ? 22.963  -15.136 -1.419  1.00 39.46  ? 151 VAL A CA  1 
ATOM   960  C C   . VAL A 1 122 ? 22.315  -15.959 -2.529  1.00 39.25  ? 151 VAL A C   1 
ATOM   961  O O   . VAL A 1 122 ? 21.149  -15.753 -2.847  1.00 36.82  ? 151 VAL A O   1 
ATOM   962  C CB  . VAL A 1 122 ? 23.768  -13.947 -1.979  1.00 41.09  ? 151 VAL A CB  1 
ATOM   963  C CG1 . VAL A 1 122 ? 22.902  -13.028 -2.835  1.00 41.43  ? 151 VAL A CG1 1 
ATOM   964  C CG2 . VAL A 1 122 ? 24.439  -13.137 -0.873  1.00 39.13  ? 151 VAL A CG2 1 
ATOM   965  N N   . VAL A 1 123 ? 23.070  -16.903 -3.100  1.00 45.80  ? 152 VAL A N   1 
ATOM   966  C CA  . VAL A 1 123 ? 22.558  -17.767 -4.156  1.00 46.56  ? 152 VAL A CA  1 
ATOM   967  C C   . VAL A 1 123 ? 21.387  -18.571 -3.598  1.00 44.99  ? 152 VAL A C   1 
ATOM   968  O O   . VAL A 1 123 ? 20.315  -18.606 -4.198  1.00 45.86  ? 152 VAL A O   1 
ATOM   969  C CB  . VAL A 1 123 ? 23.653  -18.682 -4.740  1.00 48.30  ? 152 VAL A CB  1 
ATOM   970  C CG1 . VAL A 1 123 ? 23.104  -19.650 -5.782  1.00 49.68  ? 152 VAL A CG1 1 
ATOM   971  C CG2 . VAL A 1 123 ? 24.801  -17.878 -5.334  1.00 46.77  ? 152 VAL A CG2 1 
ATOM   972  N N   . THR A 1 124 ? 21.610  -19.212 -2.444  1.00 46.76  ? 153 THR A N   1 
ATOM   973  C CA  . THR A 1 124 ? 20.563  -19.937 -1.742  1.00 45.26  ? 153 THR A CA  1 
ATOM   974  C C   . THR A 1 124 ? 19.357  -19.013 -1.603  1.00 45.59  ? 153 THR A C   1 
ATOM   975  O O   . THR A 1 124 ? 18.284  -19.283 -2.143  1.00 46.01  ? 153 THR A O   1 
ATOM   976  C CB  . THR A 1 124 ? 21.078  -20.397 -0.375  1.00 46.52  ? 153 THR A CB  1 
ATOM   977  O OG1 . THR A 1 124 ? 22.286  -21.134 -0.547  1.00 46.85  ? 153 THR A OG1 1 
ATOM   978  C CG2 . THR A 1 124 ? 20.073  -21.259 0.367   1.00 44.86  ? 153 THR A CG2 1 
ATOM   979  N N   . MET A 1 125 ? 19.581  -17.897 -0.899  1.00 47.06  ? 154 MET A N   1 
ATOM   980  C CA  . MET A 1 125 ? 18.546  -16.929 -0.576  1.00 47.07  ? 154 MET A CA  1 
ATOM   981  C C   . MET A 1 125 ? 17.741  -16.557 -1.820  1.00 46.09  ? 154 MET A C   1 
ATOM   982  O O   . MET A 1 125 ? 16.518  -16.484 -1.754  1.00 47.96  ? 154 MET A O   1 
ATOM   983  C CB  . MET A 1 125 ? 19.180  -15.675 0.034   1.00 49.28  ? 154 MET A CB  1 
ATOM   984  C CG  . MET A 1 125 ? 18.211  -14.542 0.291   1.00 51.88  ? 154 MET A CG  1 
ATOM   985  S SD  . MET A 1 125 ? 19.093  -13.033 0.730   1.00 53.68  ? 154 MET A SD  1 
ATOM   986  C CE  . MET A 1 125 ? 17.757  -11.872 0.438   1.00 55.29  ? 154 MET A CE  1 
ATOM   987  N N   . LEU A 1 126 ? 18.423  -16.305 -2.945  1.00 45.80  ? 155 LEU A N   1 
ATOM   988  C CA  . LEU A 1 126 ? 17.740  -15.919 -4.173  1.00 48.36  ? 155 LEU A CA  1 
ATOM   989  C C   . LEU A 1 126 ? 16.903  -17.077 -4.709  1.00 50.20  ? 155 LEU A C   1 
ATOM   990  O O   . LEU A 1 126 ? 15.803  -16.859 -5.210  1.00 56.76  ? 155 LEU A O   1 
ATOM   991  C CB  . LEU A 1 126 ? 18.723  -15.423 -5.233  1.00 49.39  ? 155 LEU A CB  1 
ATOM   992  C CG  . LEU A 1 126 ? 19.195  -13.972 -5.096  1.00 48.16  ? 155 LEU A CG  1 
ATOM   993  C CD1 . LEU A 1 126 ? 20.301  -13.702 -6.094  1.00 48.23  ? 155 LEU A CD1 1 
ATOM   994  C CD2 . LEU A 1 126 ? 18.062  -12.977 -5.279  1.00 47.41  ? 155 LEU A CD2 1 
ATOM   995  N N   . ASP A 1 127 ? 17.425  -18.305 -4.611  1.00 53.03  ? 156 ASP A N   1 
ATOM   996  C CA  . ASP A 1 127 ? 16.746  -19.459 -5.181  1.00 56.21  ? 156 ASP A CA  1 
ATOM   997  C C   . ASP A 1 127 ? 15.507  -19.815 -4.365  1.00 56.43  ? 156 ASP A C   1 
ATOM   998  O O   . ASP A 1 127 ? 14.551  -20.360 -4.910  1.00 53.92  ? 156 ASP A O   1 
ATOM   999  C CB  . ASP A 1 127 ? 17.684  -20.640 -5.358  1.00 57.84  ? 156 ASP A CB  1 
ATOM   1000 C CG  . ASP A 1 127 ? 18.598  -20.551 -6.572  1.00 62.24  ? 156 ASP A CG  1 
ATOM   1001 O OD1 . ASP A 1 127 ? 18.906  -19.414 -7.000  1.00 60.59  ? 156 ASP A OD1 1 
ATOM   1002 O OD2 . ASP A 1 127 ? 18.954  -21.621 -7.109  1.00 70.44  ? 156 ASP A OD2 1 
ATOM   1003 N N   . ASN A 1 128 ? 15.522  -19.484 -3.070  1.00 55.20  ? 157 ASN A N   1 
ATOM   1004 C CA  . ASN A 1 128 ? 14.417  -19.805 -2.184  1.00 56.89  ? 157 ASN A CA  1 
ATOM   1005 C C   . ASN A 1 128 ? 13.344  -18.718 -2.225  1.00 57.25  ? 157 ASN A C   1 
ATOM   1006 O O   . ASN A 1 128 ? 12.331  -18.849 -1.544  1.00 57.18  ? 157 ASN A O   1 
ATOM   1007 C CB  . ASN A 1 128 ? 14.911  -20.044 -0.760  1.00 55.77  ? 157 ASN A CB  1 
ATOM   1008 C CG  . ASN A 1 128 ? 15.942  -21.145 -0.686  1.00 53.85  ? 157 ASN A CG  1 
ATOM   1009 O OD1 . ASN A 1 128 ? 16.053  -21.964 -1.605  1.00 52.33  ? 157 ASN A OD1 1 
ATOM   1010 N ND2 . ASN A 1 128 ? 16.704  -21.189 0.396   1.00 56.21  ? 157 ASN A ND2 1 
ATOM   1011 N N   . PHE A 1 129 ? 13.552  -17.654 -3.016  1.00 58.90  ? 158 PHE A N   1 
ATOM   1012 C CA  . PHE A 1 129 ? 12.562  -16.591 -3.127  1.00 59.68  ? 158 PHE A CA  1 
ATOM   1013 C C   . PHE A 1 129 ? 11.349  -17.080 -3.916  1.00 60.36  ? 158 PHE A C   1 
ATOM   1014 O O   . PHE A 1 129 ? 11.497  -17.807 -4.896  1.00 61.42  ? 158 PHE A O   1 
ATOM   1015 C CB  . PHE A 1 129 ? 13.081  -15.327 -3.824  1.00 60.36  ? 158 PHE A CB  1 
ATOM   1016 C CG  . PHE A 1 129 ? 13.773  -14.310 -2.930  1.00 59.05  ? 158 PHE A CG  1 
ATOM   1017 C CD1 . PHE A 1 129 ? 13.320  -14.062 -1.639  1.00 62.13  ? 158 PHE A CD1 1 
ATOM   1018 C CD2 . PHE A 1 129 ? 14.882  -13.606 -3.384  1.00 61.36  ? 158 PHE A CD2 1 
ATOM   1019 C CE1 . PHE A 1 129 ? 13.963  -13.141 -0.829  1.00 63.19  ? 158 PHE A CE1 1 
ATOM   1020 C CE2 . PHE A 1 129 ? 15.520  -12.684 -2.569  1.00 61.44  ? 158 PHE A CE2 1 
ATOM   1021 C CZ  . PHE A 1 129 ? 15.058  -12.455 -1.296  1.00 61.90  ? 158 PHE A CZ  1 
ATOM   1022 N N   . PRO A 1 130 ? 10.119  -16.664 -3.528  1.00 59.81  ? 159 PRO A N   1 
ATOM   1023 C CA  . PRO A 1 130 ? 8.910   -16.951 -4.303  1.00 59.44  ? 159 PRO A CA  1 
ATOM   1024 C C   . PRO A 1 130 ? 8.632   -15.893 -5.369  1.00 61.07  ? 159 PRO A C   1 
ATOM   1025 O O   . PRO A 1 130 ? 9.189   -14.799 -5.313  1.00 59.93  ? 159 PRO A O   1 
ATOM   1026 C CB  . PRO A 1 130 ? 7.856   -16.947 -3.190  1.00 60.12  ? 159 PRO A CB  1 
ATOM   1027 C CG  . PRO A 1 130 ? 8.301   -15.818 -2.292  1.00 60.00  ? 159 PRO A CG  1 
ATOM   1028 C CD  . PRO A 1 130 ? 9.826   -15.889 -2.312  1.00 61.19  ? 159 PRO A CD  1 
ATOM   1029 N N   . THR A 1 131 ? 7.721   -16.212 -6.301  1.00 60.40  ? 160 THR A N   1 
ATOM   1030 C CA  . THR A 1 131 ? 7.536   -15.419 -7.508  1.00 59.39  ? 160 THR A CA  1 
ATOM   1031 C C   . THR A 1 131 ? 6.643   -14.210 -7.224  1.00 54.89  ? 160 THR A C   1 
ATOM   1032 O O   . THR A 1 131 ? 6.642   -13.250 -7.990  1.00 54.15  ? 160 THR A O   1 
ATOM   1033 C CB  . THR A 1 131 ? 6.978   -16.278 -8.647  1.00 62.36  ? 160 THR A CB  1 
ATOM   1034 O OG1 . THR A 1 131 ? 5.616   -16.567 -8.348  1.00 67.15  ? 160 THR A OG1 1 
ATOM   1035 C CG2 . THR A 1 131 ? 7.757   -17.566 -8.860  1.00 61.75  ? 160 THR A CG2 1 
ATOM   1036 N N   . ASN A 1 132 ? 5.893   -14.243 -6.118  1.00 52.18  ? 161 ASN A N   1 
ATOM   1037 C CA  . ASN A 1 132 ? 5.033   -13.126 -5.751  1.00 50.01  ? 161 ASN A CA  1 
ATOM   1038 C C   . ASN A 1 132 ? 5.829   -12.051 -4.998  1.00 45.13  ? 161 ASN A C   1 
ATOM   1039 O O   . ASN A 1 132 ? 5.260   -11.027 -4.618  1.00 41.79  ? 161 ASN A O   1 
ATOM   1040 C CB  . ASN A 1 132 ? 3.797   -13.609 -4.994  1.00 50.13  ? 161 ASN A CB  1 
ATOM   1041 C CG  . ASN A 1 132 ? 4.123   -14.179 -3.632  1.00 51.86  ? 161 ASN A CG  1 
ATOM   1042 O OD1 . ASN A 1 132 ? 5.129   -14.880 -3.474  1.00 54.58  ? 161 ASN A OD1 1 
ATOM   1043 N ND2 . ASN A 1 132 ? 3.298   -13.879 -2.636  1.00 52.10  ? 161 ASN A ND2 1 
ATOM   1044 N N   . LEU A 1 133 ? 7.132   -12.283 -4.771  1.00 41.43  ? 162 LEU A N   1 
ATOM   1045 C CA  . LEU A 1 133 ? 8.033   -11.233 -4.316  1.00 38.64  ? 162 LEU A CA  1 
ATOM   1046 C C   . LEU A 1 133 ? 8.610   -10.511 -5.536  1.00 36.96  ? 162 LEU A C   1 
ATOM   1047 O O   . LEU A 1 133 ? 9.287   -11.119 -6.363  1.00 36.21  ? 162 LEU A O   1 
ATOM   1048 C CB  . LEU A 1 133 ? 9.127   -11.831 -3.432  1.00 37.93  ? 162 LEU A CB  1 
ATOM   1049 C CG  . LEU A 1 133 ? 10.028  -10.822 -2.712  1.00 39.15  ? 162 LEU A CG  1 
ATOM   1050 C CD1 . LEU A 1 133 ? 9.230   -10.055 -1.663  1.00 38.98  ? 162 LEU A CD1 1 
ATOM   1051 C CD2 . LEU A 1 133 ? 11.251  -11.486 -2.084  1.00 37.82  ? 162 LEU A CD2 1 
ATOM   1052 N N   . HIS A 1 134 ? 8.336   -9.205  -5.626  1.00 37.15  ? 163 HIS A N   1 
ATOM   1053 C CA  . HIS A 1 134 ? 8.664   -8.377  -6.779  1.00 40.07  ? 163 HIS A CA  1 
ATOM   1054 C C   . HIS A 1 134 ? 10.170  -8.399  -7.060  1.00 38.78  ? 163 HIS A C   1 
ATOM   1055 O O   . HIS A 1 134 ? 10.978  -8.463  -6.135  1.00 37.16  ? 163 HIS A O   1 
ATOM   1056 C CB  . HIS A 1 134 ? 8.144   -6.952  -6.530  1.00 43.79  ? 163 HIS A CB  1 
ATOM   1057 C CG  . HIS A 1 134 ? 8.279   -5.993  -7.671  1.00 45.40  ? 163 HIS A CG  1 
ATOM   1058 N ND1 . HIS A 1 134 ? 9.474   -5.409  -8.037  1.00 45.05  ? 163 HIS A ND1 1 
ATOM   1059 C CD2 . HIS A 1 134 ? 7.362   -5.516  -8.522  1.00 46.92  ? 163 HIS A CD2 1 
ATOM   1060 C CE1 . HIS A 1 134 ? 9.273   -4.608  -9.074  1.00 45.56  ? 163 HIS A CE1 1 
ATOM   1061 N NE2 . HIS A 1 134 ? 7.998   -4.663  -9.389  1.00 47.14  ? 163 HIS A NE2 1 
ATOM   1062 N N   . PRO A 1 135 ? 10.604  -8.312  -8.343  1.00 37.40  ? 164 PRO A N   1 
ATOM   1063 C CA  . PRO A 1 135 ? 12.031  -8.314  -8.686  1.00 36.20  ? 164 PRO A CA  1 
ATOM   1064 C C   . PRO A 1 135 ? 12.913  -7.381  -7.858  1.00 37.65  ? 164 PRO A C   1 
ATOM   1065 O O   . PRO A 1 135 ? 14.056  -7.719  -7.567  1.00 39.50  ? 164 PRO A O   1 
ATOM   1066 C CB  . PRO A 1 135 ? 12.021  -7.881  -10.159 1.00 35.11  ? 164 PRO A CB  1 
ATOM   1067 C CG  . PRO A 1 135 ? 10.718  -8.383  -10.684 1.00 36.66  ? 164 PRO A CG  1 
ATOM   1068 C CD  . PRO A 1 135 ? 9.744   -8.224  -9.532  1.00 37.14  ? 164 PRO A CD  1 
ATOM   1069 N N   . MET A 1 136 ? 12.363  -6.208  -7.509  1.00 38.54  ? 165 MET A N   1 
ATOM   1070 C CA  . MET A 1 136 ? 13.098  -5.135  -6.863  1.00 37.49  ? 165 MET A CA  1 
ATOM   1071 C C   . MET A 1 136 ? 13.326  -5.455  -5.389  1.00 37.82  ? 165 MET A C   1 
ATOM   1072 O O   . MET A 1 136 ? 14.384  -5.125  -4.851  1.00 39.01  ? 165 MET A O   1 
ATOM   1073 C CB  . MET A 1 136 ? 12.364  -3.796  -7.018  1.00 37.00  ? 165 MET A CB  1 
ATOM   1074 C CG  . MET A 1 136 ? 12.579  -3.125  -8.369  1.00 37.12  ? 165 MET A CG  1 
ATOM   1075 S SD  . MET A 1 136 ? 14.308  -2.742  -8.733  1.00 40.94  ? 165 MET A SD  1 
ATOM   1076 C CE  . MET A 1 136 ? 14.798  -1.721  -7.336  1.00 42.73  ? 165 MET A CE  1 
ATOM   1077 N N   . SER A 1 137 ? 12.341  -6.098  -4.747  1.00 38.40  ? 166 SER A N   1 
ATOM   1078 C CA  . SER A 1 137 ? 12.475  -6.531  -3.361  1.00 38.09  ? 166 SER A CA  1 
ATOM   1079 C C   . SER A 1 137 ? 13.564  -7.596  -3.247  1.00 38.67  ? 166 SER A C   1 
ATOM   1080 O O   . SER A 1 137 ? 14.288  -7.662  -2.252  1.00 38.16  ? 166 SER A O   1 
ATOM   1081 C CB  . SER A 1 137 ? 11.168  -7.054  -2.810  1.00 37.80  ? 166 SER A CB  1 
ATOM   1082 O OG  . SER A 1 137 ? 10.089  -6.175  -3.094  1.00 36.47  ? 166 SER A OG  1 
ATOM   1083 N N   . GLN A 1 138 ? 13.662  -8.441  -4.276  1.00 39.01  ? 167 GLN A N   1 
ATOM   1084 C CA  . GLN A 1 138 ? 14.650  -9.505  -4.307  1.00 36.43  ? 167 GLN A CA  1 
ATOM   1085 C C   . GLN A 1 138 ? 16.035  -8.900  -4.491  1.00 35.74  ? 167 GLN A C   1 
ATOM   1086 O O   . GLN A 1 138 ? 16.966  -9.284  -3.790  1.00 36.63  ? 167 GLN A O   1 
ATOM   1087 C CB  . GLN A 1 138 ? 14.326  -10.500 -5.419  1.00 37.30  ? 167 GLN A CB  1 
ATOM   1088 C CG  . GLN A 1 138 ? 13.088  -11.343 -5.144  1.00 37.87  ? 167 GLN A CG  1 
ATOM   1089 C CD  . GLN A 1 138 ? 12.983  -12.542 -6.058  1.00 37.52  ? 167 GLN A CD  1 
ATOM   1090 O OE1 . GLN A 1 138 ? 13.975  -13.224 -6.336  1.00 37.59  ? 167 GLN A OE1 1 
ATOM   1091 N NE2 . GLN A 1 138 ? 11.781  -12.802 -6.549  1.00 36.92  ? 167 GLN A NE2 1 
ATOM   1092 N N   . LEU A 1 139 ? 16.152  -7.950  -5.427  1.00 34.14  ? 168 LEU A N   1 
ATOM   1093 C CA  . LEU A 1 139 ? 17.404  -7.237  -5.629  1.00 36.21  ? 168 LEU A CA  1 
ATOM   1094 C C   . LEU A 1 139 ? 17.836  -6.571  -4.325  1.00 33.70  ? 168 LEU A C   1 
ATOM   1095 O O   . LEU A 1 139 ? 18.961  -6.750  -3.884  1.00 38.90  ? 168 LEU A O   1 
ATOM   1096 C CB  . LEU A 1 139 ? 17.285  -6.190  -6.732  1.00 37.38  ? 168 LEU A CB  1 
ATOM   1097 C CG  . LEU A 1 139 ? 18.557  -5.378  -6.998  1.00 38.58  ? 168 LEU A CG  1 
ATOM   1098 C CD1 . LEU A 1 139 ? 19.594  -6.247  -7.683  1.00 38.99  ? 168 LEU A CD1 1 
ATOM   1099 C CD2 . LEU A 1 139 ? 18.265  -4.127  -7.810  1.00 39.45  ? 168 LEU A CD2 1 
ATOM   1100 N N   . SER A 1 140 ? 16.945  -5.780  -3.727  1.00 31.87  ? 169 SER A N   1 
ATOM   1101 C CA  . SER A 1 140 ? 17.284  -5.038  -2.525  1.00 32.27  ? 169 SER A CA  1 
ATOM   1102 C C   . SER A 1 140 ? 17.639  -5.991  -1.389  1.00 34.25  ? 169 SER A C   1 
ATOM   1103 O O   . SER A 1 140 ? 18.624  -5.787  -0.677  1.00 33.71  ? 169 SER A O   1 
ATOM   1104 C CB  . SER A 1 140 ? 16.170  -4.110  -2.116  1.00 31.01  ? 169 SER A CB  1 
ATOM   1105 O OG  . SER A 1 140 ? 16.438  -3.561  -0.835  1.00 31.47  ? 169 SER A OG  1 
ATOM   1106 N N   . ALA A 1 141 ? 16.803  -7.018  -1.218  1.00 36.46  ? 170 ALA A N   1 
ATOM   1107 C CA  . ALA A 1 141 ? 16.998  -8.009  -0.171  1.00 36.37  ? 170 ALA A CA  1 
ATOM   1108 C C   . ALA A 1 141 ? 18.375  -8.660  -0.306  1.00 37.73  ? 170 ALA A C   1 
ATOM   1109 O O   . ALA A 1 141 ? 19.095  -8.798  0.684   1.00 34.67  ? 170 ALA A O   1 
ATOM   1110 C CB  . ALA A 1 141 ? 15.880  -9.033  -0.240  1.00 38.05  ? 170 ALA A CB  1 
ATOM   1111 N N   . ALA A 1 142 ? 18.733  -9.038  -1.543  1.00 37.69  ? 171 ALA A N   1 
ATOM   1112 C CA  . ALA A 1 142 ? 20.005  -9.683  -1.837  1.00 38.78  ? 171 ALA A CA  1 
ATOM   1113 C C   . ALA A 1 142 ? 21.181  -8.748  -1.563  1.00 37.64  ? 171 ALA A C   1 
ATOM   1114 O O   . ALA A 1 142 ? 22.195  -9.178  -1.015  1.00 40.47  ? 171 ALA A O   1 
ATOM   1115 C CB  . ALA A 1 142 ? 20.017  -10.150 -3.278  1.00 40.13  ? 171 ALA A CB  1 
ATOM   1116 N N   . VAL A 1 143 ? 21.059  -7.477  -1.965  1.00 37.85  ? 172 VAL A N   1 
ATOM   1117 C CA  . VAL A 1 143 ? 22.159  -6.533  -1.804  1.00 37.59  ? 172 VAL A CA  1 
ATOM   1118 C C   . VAL A 1 143 ? 22.464  -6.367  -0.317  1.00 33.22  ? 172 VAL A C   1 
ATOM   1119 O O   . VAL A 1 143 ? 23.622  -6.277  0.072   1.00 33.23  ? 172 VAL A O   1 
ATOM   1120 C CB  . VAL A 1 143 ? 21.926  -5.159  -2.464  1.00 37.46  ? 172 VAL A CB  1 
ATOM   1121 C CG1 . VAL A 1 143 ? 22.974  -4.140  -2.026  1.00 37.06  ? 172 VAL A CG1 1 
ATOM   1122 C CG2 . VAL A 1 143 ? 21.888  -5.255  -3.979  1.00 37.34  ? 172 VAL A CG2 1 
ATOM   1123 N N   . THR A 1 144 ? 21.423  -6.305  0.516   1.00 31.93  ? 173 THR A N   1 
ATOM   1124 C CA  . THR A 1 144 ? 21.617  -6.186  1.955   1.00 30.79  ? 173 THR A CA  1 
ATOM   1125 C C   . THR A 1 144 ? 22.407  -7.383  2.481   1.00 31.48  ? 173 THR A C   1 
ATOM   1126 O O   . THR A 1 144 ? 23.355  -7.208  3.238   1.00 29.36  ? 173 THR A O   1 
ATOM   1127 C CB  . THR A 1 144 ? 20.260  -6.059  2.632   1.00 28.99  ? 173 THR A CB  1 
ATOM   1128 O OG1 . THR A 1 144 ? 19.726  -4.907  1.987   1.00 28.90  ? 173 THR A OG1 1 
ATOM   1129 C CG2 . THR A 1 144 ? 20.375  -5.874  4.134   1.00 30.69  ? 173 THR A CG2 1 
ATOM   1130 N N   . ALA A 1 145 ? 22.015  -8.590  2.053   1.00 35.16  ? 174 ALA A N   1 
ATOM   1131 C CA  . ALA A 1 145 ? 22.630  -9.836  2.494   1.00 35.97  ? 174 ALA A CA  1 
ATOM   1132 C C   . ALA A 1 145 ? 24.109  -9.864  2.129   1.00 36.44  ? 174 ALA A C   1 
ATOM   1133 O O   . ALA A 1 145 ? 24.915  -10.416 2.879   1.00 34.57  ? 174 ALA A O   1 
ATOM   1134 C CB  . ALA A 1 145 ? 21.912  -11.015 1.869   1.00 36.51  ? 174 ALA A CB  1 
ATOM   1135 N N   . LEU A 1 146 ? 24.436  -9.253  0.977   1.00 36.49  ? 175 LEU A N   1 
ATOM   1136 C CA  . LEU A 1 146 ? 25.795  -9.188  0.458   1.00 36.15  ? 175 LEU A CA  1 
ATOM   1137 C C   . LEU A 1 146 ? 26.734  -8.407  1.383   1.00 34.81  ? 175 LEU A C   1 
ATOM   1138 O O   . LEU A 1 146 ? 27.948  -8.509  1.233   1.00 35.32  ? 175 LEU A O   1 
ATOM   1139 C CB  . LEU A 1 146 ? 25.786  -8.573  -0.944  1.00 37.83  ? 175 LEU A CB  1 
ATOM   1140 C CG  . LEU A 1 146 ? 25.534  -9.522  -2.123  1.00 41.31  ? 175 LEU A CG  1 
ATOM   1141 C CD1 . LEU A 1 146 ? 25.346  -8.737  -3.412  1.00 42.24  ? 175 LEU A CD1 1 
ATOM   1142 C CD2 . LEU A 1 146 ? 26.672  -10.515 -2.301  1.00 41.29  ? 175 LEU A CD2 1 
ATOM   1143 N N   . ASN A 1 147 ? 26.207  -7.638  2.344   1.00 34.05  ? 176 ASN A N   1 
ATOM   1144 C CA  . ASN A 1 147 ? 27.057  -6.787  3.165   1.00 35.96  ? 176 ASN A CA  1 
ATOM   1145 C C   . ASN A 1 147 ? 27.806  -7.619  4.212   1.00 36.58  ? 176 ASN A C   1 
ATOM   1146 O O   . ASN A 1 147 ? 28.558  -7.075  5.025   1.00 37.63  ? 176 ASN A O   1 
ATOM   1147 C CB  . ASN A 1 147 ? 26.281  -5.612  3.762   1.00 36.90  ? 176 ASN A CB  1 
ATOM   1148 C CG  . ASN A 1 147 ? 26.072  -5.714  5.255   1.00 36.72  ? 176 ASN A CG  1 
ATOM   1149 O OD1 . ASN A 1 147 ? 25.388  -6.621  5.741   1.00 38.36  ? 176 ASN A OD1 1 
ATOM   1150 N ND2 . ASN A 1 147 ? 26.649  -4.784  5.998   1.00 35.22  ? 176 ASN A ND2 1 
ATOM   1151 N N   . SER A 1 148 ? 27.627  -8.943  4.181   1.00 35.29  ? 177 SER A N   1 
ATOM   1152 C CA  . SER A 1 148 ? 28.538  -9.830  4.878   1.00 38.16  ? 177 SER A CA  1 
ATOM   1153 C C   . SER A 1 148 ? 29.941  -9.727  4.267   1.00 42.13  ? 177 SER A C   1 
ATOM   1154 O O   . SER A 1 148 ? 30.931  -9.934  4.965   1.00 43.62  ? 177 SER A O   1 
ATOM   1155 C CB  . SER A 1 148 ? 28.009  -11.247 4.908   1.00 38.52  ? 177 SER A CB  1 
ATOM   1156 O OG  . SER A 1 148 ? 27.804  -11.775 3.605   1.00 36.88  ? 177 SER A OG  1 
ATOM   1157 N N   . GLU A 1 149 ? 30.027  -9.319  2.991   1.00 45.98  ? 178 GLU A N   1 
ATOM   1158 C CA  . GLU A 1 149 ? 31.295  -9.210  2.280   1.00 47.47  ? 178 GLU A CA  1 
ATOM   1159 C C   . GLU A 1 149 ? 31.888  -7.802  2.325   1.00 43.62  ? 178 GLU A C   1 
ATOM   1160 O O   . GLU A 1 149 ? 32.840  -7.532  1.600   1.00 45.25  ? 178 GLU A O   1 
ATOM   1161 C CB  . GLU A 1 149 ? 31.096  -9.586  0.811   1.00 52.61  ? 178 GLU A CB  1 
ATOM   1162 C CG  . GLU A 1 149 ? 30.715  -11.051 0.622   1.00 59.40  ? 178 GLU A CG  1 
ATOM   1163 C CD  . GLU A 1 149 ? 31.738  -12.005 1.213   1.00 64.74  ? 178 GLU A CD  1 
ATOM   1164 O OE1 . GLU A 1 149 ? 32.835  -12.149 0.627   1.00 70.73  ? 178 GLU A OE1 1 
ATOM   1165 O OE2 . GLU A 1 149 ? 31.446  -12.573 2.287   1.00 70.08  ? 178 GLU A OE2 1 
ATOM   1166 N N   . SER A 1 150 ? 31.345  -6.915  3.170   1.00 40.72  ? 179 SER A N   1 
ATOM   1167 C CA  . SER A 1 150 ? 31.762  -5.519  3.210   1.00 36.86  ? 179 SER A CA  1 
ATOM   1168 C C   . SER A 1 150 ? 33.092  -5.360  3.948   1.00 37.34  ? 179 SER A C   1 
ATOM   1169 O O   . SER A 1 150 ? 33.157  -5.540  5.164   1.00 37.92  ? 179 SER A O   1 
ATOM   1170 C CB  . SER A 1 150 ? 30.705  -4.669  3.860   1.00 36.60  ? 179 SER A CB  1 
ATOM   1171 O OG  . SER A 1 150 ? 31.183  -3.349  4.077   1.00 35.88  ? 179 SER A OG  1 
ATOM   1172 N N   . ASN A 1 151 ? 34.138  -4.964  3.216   1.00 37.10  ? 180 ASN A N   1 
ATOM   1173 C CA  . ASN A 1 151 ? 35.441  -4.715  3.810   1.00 39.70  ? 180 ASN A CA  1 
ATOM   1174 C C   . ASN A 1 151 ? 35.386  -3.452  4.668   1.00 39.82  ? 180 ASN A C   1 
ATOM   1175 O O   . ASN A 1 151 ? 36.107  -3.346  5.654   1.00 40.52  ? 180 ASN A O   1 
ATOM   1176 C CB  . ASN A 1 151 ? 36.532  -4.549  2.758   1.00 43.46  ? 180 ASN A CB  1 
ATOM   1177 C CG  . ASN A 1 151 ? 36.565  -5.683  1.762   1.00 47.65  ? 180 ASN A CG  1 
ATOM   1178 O OD1 . ASN A 1 151 ? 36.125  -5.509  0.619   1.00 50.95  ? 180 ASN A OD1 1 
ATOM   1179 N ND2 . ASN A 1 151 ? 37.066  -6.842  2.171   1.00 47.67  ? 180 ASN A ND2 1 
ATOM   1180 N N   . PHE A 1 152 ? 34.547  -2.488  4.267   1.00 39.57  ? 181 PHE A N   1 
ATOM   1181 C CA  . PHE A 1 152 ? 34.412  -1.228  4.985   1.00 36.92  ? 181 PHE A CA  1 
ATOM   1182 C C   . PHE A 1 152 ? 33.793  -1.459  6.364   1.00 37.93  ? 181 PHE A C   1 
ATOM   1183 O O   . PHE A 1 152 ? 34.262  -0.885  7.349   1.00 39.28  ? 181 PHE A O   1 
ATOM   1184 C CB  . PHE A 1 152 ? 33.581  -0.205  4.205   1.00 34.73  ? 181 PHE A CB  1 
ATOM   1185 C CG  . PHE A 1 152 ? 33.343  1.088   4.973   1.00 31.57  ? 181 PHE A CG  1 
ATOM   1186 C CD1 . PHE A 1 152 ? 34.346  2.045   5.089   1.00 30.67  ? 181 PHE A CD1 1 
ATOM   1187 C CD2 . PHE A 1 152 ? 32.128  1.333   5.601   1.00 30.61  ? 181 PHE A CD2 1 
ATOM   1188 C CE1 . PHE A 1 152 ? 34.135  3.213   5.814   1.00 31.14  ? 181 PHE A CE1 1 
ATOM   1189 C CE2 . PHE A 1 152 ? 31.923  2.504   6.320   1.00 29.89  ? 181 PHE A CE2 1 
ATOM   1190 C CZ  . PHE A 1 152 ? 32.925  3.438   6.427   1.00 30.29  ? 181 PHE A CZ  1 
ATOM   1191 N N   . ALA A 1 153 ? 32.741  -2.283  6.434   1.00 37.36  ? 182 ALA A N   1 
ATOM   1192 C CA  . ALA A 1 153 ? 32.040  -2.511  7.694   1.00 39.49  ? 182 ALA A CA  1 
ATOM   1193 C C   . ALA A 1 153 ? 32.948  -3.231  8.694   1.00 42.21  ? 182 ALA A C   1 
ATOM   1194 O O   . ALA A 1 153 ? 32.933  -2.911  9.880   1.00 38.74  ? 182 ALA A O   1 
ATOM   1195 C CB  . ALA A 1 153 ? 30.752  -3.275  7.462   1.00 37.67  ? 182 ALA A CB  1 
ATOM   1196 N N   . ARG A 1 154 ? 33.746  -4.195  8.212   1.00 46.21  ? 183 ARG A N   1 
ATOM   1197 C CA  . ARG A 1 154 ? 34.727  -4.861  9.057   1.00 50.94  ? 183 ARG A CA  1 
ATOM   1198 C C   . ARG A 1 154 ? 35.776  -3.850  9.505   1.00 45.19  ? 183 ARG A C   1 
ATOM   1199 O O   . ARG A 1 154 ? 35.973  -3.666  10.701  1.00 45.98  ? 183 ARG A O   1 
ATOM   1200 C CB  . ARG A 1 154 ? 35.401  -6.060  8.375   1.00 58.95  ? 183 ARG A CB  1 
ATOM   1201 C CG  . ARG A 1 154 ? 34.585  -7.342  8.460   1.00 65.36  ? 183 ARG A CG  1 
ATOM   1202 C CD  . ARG A 1 154 ? 35.326  -8.561  7.921   1.00 69.83  ? 183 ARG A CD  1 
ATOM   1203 N NE  . ARG A 1 154 ? 35.553  -8.521  6.471   1.00 73.23  ? 183 ARG A NE  1 
ATOM   1204 C CZ  . ARG A 1 154 ? 34.607  -8.540  5.531   1.00 74.84  ? 183 ARG A CZ  1 
ATOM   1205 N NH1 . ARG A 1 154 ? 34.949  -8.565  4.253   1.00 72.47  ? 183 ARG A NH1 1 
ATOM   1206 N NH2 . ARG A 1 154 ? 33.324  -8.548  5.860   1.00 75.67  ? 183 ARG A NH2 1 
ATOM   1207 N N   . ALA A 1 155 ? 36.417  -3.188  8.536   1.00 41.77  ? 184 ALA A N   1 
ATOM   1208 C CA  . ALA A 1 155 ? 37.488  -2.245  8.822   1.00 43.62  ? 184 ALA A CA  1 
ATOM   1209 C C   . ALA A 1 155 ? 37.036  -1.198  9.840   1.00 43.94  ? 184 ALA A C   1 
ATOM   1210 O O   . ALA A 1 155 ? 37.746  -0.951  10.812  1.00 44.84  ? 184 ALA A O   1 
ATOM   1211 C CB  . ALA A 1 155 ? 37.978  -1.595  7.550   1.00 42.74  ? 184 ALA A CB  1 
ATOM   1212 N N   . TYR A 1 156 ? 35.857  -0.597  9.621   1.00 42.54  ? 185 TYR A N   1 
ATOM   1213 C CA  . TYR A 1 156 ? 35.358  0.447   10.507  1.00 38.90  ? 185 TYR A CA  1 
ATOM   1214 C C   . TYR A 1 156 ? 35.294  -0.107  11.926  1.00 38.09  ? 185 TYR A C   1 
ATOM   1215 O O   . TYR A 1 156 ? 35.811  0.503   12.852  1.00 37.29  ? 185 TYR A O   1 
ATOM   1216 C CB  . TYR A 1 156 ? 33.989  1.039   10.139  1.00 38.70  ? 185 TYR A CB  1 
ATOM   1217 C CG  . TYR A 1 156 ? 33.595  2.209   11.036  1.00 36.25  ? 185 TYR A CG  1 
ATOM   1218 C CD1 . TYR A 1 156 ? 33.002  1.994   12.275  1.00 34.97  ? 185 TYR A CD1 1 
ATOM   1219 C CD2 . TYR A 1 156 ? 33.881  3.522   10.680  1.00 36.17  ? 185 TYR A CD2 1 
ATOM   1220 C CE1 . TYR A 1 156 ? 32.678  3.047   13.112  1.00 35.10  ? 185 TYR A CE1 1 
ATOM   1221 C CE2 . TYR A 1 156 ? 33.565  4.586   11.511  1.00 34.82  ? 185 TYR A CE2 1 
ATOM   1222 C CZ  . TYR A 1 156 ? 32.953  4.346   12.728  1.00 36.24  ? 185 TYR A CZ  1 
ATOM   1223 O OH  . TYR A 1 156 ? 32.632  5.380   13.565  1.00 40.04  ? 185 TYR A OH  1 
ATOM   1224 N N   . ALA A 1 157 ? 34.659  -1.266  12.096  1.00 43.01  ? 186 ALA A N   1 
ATOM   1225 C CA  . ALA A 1 157 ? 34.561  -1.900  13.402  1.00 45.19  ? 186 ALA A CA  1 
ATOM   1226 C C   . ALA A 1 157 ? 35.938  -1.979  14.065  1.00 52.15  ? 186 ALA A C   1 
ATOM   1227 O O   . ALA A 1 157 ? 36.071  -1.628  15.236  1.00 58.84  ? 186 ALA A O   1 
ATOM   1228 C CB  . ALA A 1 157 ? 33.931  -3.264  13.262  1.00 44.41  ? 186 ALA A CB  1 
ATOM   1229 N N   . GLN A 1 158 ? 36.962  -2.384  13.295  1.00 54.01  ? 187 GLN A N   1 
ATOM   1230 C CA  . GLN A 1 158 ? 38.321  -2.555  13.798  1.00 52.92  ? 187 GLN A CA  1 
ATOM   1231 C C   . GLN A 1 158 ? 39.009  -1.216  14.070  1.00 50.49  ? 187 GLN A C   1 
ATOM   1232 O O   . GLN A 1 158 ? 40.145  -1.193  14.538  1.00 51.08  ? 187 GLN A O   1 
ATOM   1233 C CB  . GLN A 1 158 ? 39.150  -3.363  12.799  1.00 53.11  ? 187 GLN A CB  1 
ATOM   1234 C CG  . GLN A 1 158 ? 38.763  -4.835  12.735  1.00 55.04  ? 187 GLN A CG  1 
ATOM   1235 C CD  . GLN A 1 158 ? 39.333  -5.551  11.529  1.00 61.80  ? 187 GLN A CD  1 
ATOM   1236 O OE1 . GLN A 1 158 ? 39.758  -4.927  10.549  1.00 63.21  ? 187 GLN A OE1 1 
ATOM   1237 N NE2 . GLN A 1 158 ? 39.317  -6.876  11.573  1.00 61.91  ? 187 GLN A NE2 1 
ATOM   1238 N N   . GLY A 1 159 ? 38.340  -0.106  13.743  1.00 51.06  ? 188 GLY A N   1 
ATOM   1239 C CA  . GLY A 1 159 ? 38.808  1.221   14.107  1.00 49.22  ? 188 GLY A CA  1 
ATOM   1240 C C   . GLY A 1 159 ? 39.836  1.756   13.114  1.00 50.33  ? 188 GLY A C   1 
ATOM   1241 O O   . GLY A 1 159 ? 41.017  1.859   13.441  1.00 53.33  ? 188 GLY A O   1 
ATOM   1242 N N   . ILE A 1 160 ? 39.374  2.116   11.912  1.00 50.38  ? 189 ILE A N   1 
ATOM   1243 C CA  . ILE A 1 160 ? 40.244  2.690   10.896  1.00 50.83  ? 189 ILE A CA  1 
ATOM   1244 C C   . ILE A 1 160 ? 40.081  4.210   10.881  1.00 49.42  ? 189 ILE A C   1 
ATOM   1245 O O   . ILE A 1 160 ? 39.005  4.727   11.163  1.00 48.35  ? 189 ILE A O   1 
ATOM   1246 C CB  . ILE A 1 160 ? 39.961  2.059   9.521   1.00 51.56  ? 189 ILE A CB  1 
ATOM   1247 C CG1 . ILE A 1 160 ? 41.052  2.403   8.497   1.00 55.35  ? 189 ILE A CG1 1 
ATOM   1248 C CG2 . ILE A 1 160 ? 38.565  2.430   9.017   1.00 52.92  ? 189 ILE A CG2 1 
ATOM   1249 C CD1 . ILE A 1 160 ? 42.416  1.795   8.791   1.00 56.50  ? 189 ILE A CD1 1 
ATOM   1250 N N   . SER A 1 161 ? 41.173  4.910   10.550  1.00 49.21  ? 190 SER A N   1 
ATOM   1251 C CA  . SER A 1 161 ? 41.192  6.358   10.389  1.00 47.57  ? 190 SER A CA  1 
ATOM   1252 C C   . SER A 1 161 ? 40.241  6.786   9.271   1.00 45.31  ? 190 SER A C   1 
ATOM   1253 O O   . SER A 1 161 ? 40.080  6.065   8.289   1.00 43.18  ? 190 SER A O   1 
ATOM   1254 C CB  . SER A 1 161 ? 42.610  6.835   10.121  1.00 47.10  ? 190 SER A CB  1 
ATOM   1255 O OG  . SER A 1 161 ? 42.643  8.089   9.450   1.00 47.18  ? 190 SER A OG  1 
ATOM   1256 N N   . ARG A 1 162 ? 39.643  7.977   9.421   1.00 46.71  ? 191 ARG A N   1 
ATOM   1257 C CA  . ARG A 1 162 ? 38.667  8.492   8.470   1.00 47.52  ? 191 ARG A CA  1 
ATOM   1258 C C   . ARG A 1 162 ? 39.272  8.598   7.071   1.00 46.62  ? 191 ARG A C   1 
ATOM   1259 O O   . ARG A 1 162 ? 38.579  8.382   6.075   1.00 37.97  ? 191 ARG A O   1 
ATOM   1260 C CB  . ARG A 1 162 ? 38.176  9.902   8.811   1.00 52.63  ? 191 ARG A CB  1 
ATOM   1261 C CG  . ARG A 1 162 ? 37.423  10.084  10.119  1.00 57.79  ? 191 ARG A CG  1 
ATOM   1262 C CD  . ARG A 1 162 ? 37.026  11.550  10.262  1.00 60.27  ? 191 ARG A CD  1 
ATOM   1263 N NE  . ARG A 1 162 ? 36.295  11.827  11.503  1.00 64.12  ? 191 ARG A NE  1 
ATOM   1264 C CZ  . ARG A 1 162 ? 35.882  13.028  11.904  1.00 65.73  ? 191 ARG A CZ  1 
ATOM   1265 N NH1 . ARG A 1 162 ? 36.098  14.102  11.157  1.00 65.39  ? 191 ARG A NH1 1 
ATOM   1266 N NH2 . ARG A 1 162 ? 35.251  13.149  13.061  1.00 64.51  ? 191 ARG A NH2 1 
ATOM   1267 N N   . THR A 1 163 ? 40.569  8.936   7.011   1.00 44.83  ? 192 THR A N   1 
ATOM   1268 C CA  . THR A 1 163 ? 41.215  9.289   5.757   1.00 42.68  ? 192 THR A CA  1 
ATOM   1269 C C   . THR A 1 163 ? 41.331  8.054   4.867   1.00 38.01  ? 192 THR A C   1 
ATOM   1270 O O   . THR A 1 163 ? 41.617  8.180   3.682   1.00 40.89  ? 192 THR A O   1 
ATOM   1271 C CB  . THR A 1 163 ? 42.575  9.942   6.030   1.00 45.03  ? 192 THR A CB  1 
ATOM   1272 O OG1 . THR A 1 163 ? 43.406  9.018   6.728   1.00 41.27  ? 192 THR A OG1 1 
ATOM   1273 C CG2 . THR A 1 163 ? 42.463  11.197  6.880   1.00 47.95  ? 192 THR A CG2 1 
ATOM   1274 N N   . LYS A 1 164 ? 41.093  6.867   5.437   1.00 36.23  ? 193 LYS A N   1 
ATOM   1275 C CA  . LYS A 1 164 ? 41.136  5.619   4.688   1.00 36.70  ? 193 LYS A CA  1 
ATOM   1276 C C   . LYS A 1 164 ? 39.742  5.161   4.248   1.00 33.29  ? 193 LYS A C   1 
ATOM   1277 O O   . LYS A 1 164 ? 39.639  4.226   3.453   1.00 30.23  ? 193 LYS A O   1 
ATOM   1278 C CB  . LYS A 1 164 ? 41.809  4.548   5.551   1.00 39.49  ? 193 LYS A CB  1 
ATOM   1279 C CG  . LYS A 1 164 ? 43.298  4.778   5.807   1.00 45.06  ? 193 LYS A CG  1 
ATOM   1280 C CD  . LYS A 1 164 ? 44.207  4.463   4.622   1.00 48.50  ? 193 LYS A CD  1 
ATOM   1281 C CE  . LYS A 1 164 ? 44.302  2.988   4.369   1.00 53.44  ? 193 LYS A CE  1 
ATOM   1282 N NZ  . LYS A 1 164 ? 45.285  2.657   3.334   1.00 57.22  ? 193 LYS A NZ  1 
ATOM   1283 N N   . TYR A 1 165 ? 38.683  5.814   4.759   1.00 30.80  ? 194 TYR A N   1 
ATOM   1284 C CA  . TYR A 1 165 ? 37.312  5.422   4.460   1.00 31.20  ? 194 TYR A CA  1 
ATOM   1285 C C   . TYR A 1 165 ? 37.164  5.170   2.961   1.00 31.89  ? 194 TYR A C   1 
ATOM   1286 O O   . TYR A 1 165 ? 36.887  4.044   2.553   1.00 32.93  ? 194 TYR A O   1 
ATOM   1287 C CB  . TYR A 1 165 ? 36.300  6.482   4.908   1.00 30.32  ? 194 TYR A CB  1 
ATOM   1288 C CG  . TYR A 1 165 ? 36.028  6.621   6.400   1.00 29.16  ? 194 TYR A CG  1 
ATOM   1289 C CD1 . TYR A 1 165 ? 36.516  5.710   7.334   1.00 29.97  ? 194 TYR A CD1 1 
ATOM   1290 C CD2 . TYR A 1 165 ? 35.254  7.676   6.874   1.00 29.71  ? 194 TYR A CD2 1 
ATOM   1291 C CE1 . TYR A 1 165 ? 36.246  5.843   8.689   1.00 28.90  ? 194 TYR A CE1 1 
ATOM   1292 C CE2 . TYR A 1 165 ? 34.983  7.826   8.225   1.00 29.58  ? 194 TYR A CE2 1 
ATOM   1293 C CZ  . TYR A 1 165 ? 35.473  6.902   9.132   1.00 30.48  ? 194 TYR A CZ  1 
ATOM   1294 O OH  . TYR A 1 165 ? 35.201  7.049   10.461  1.00 31.03  ? 194 TYR A OH  1 
ATOM   1295 N N   . TRP A 1 166 ? 37.430  6.205   2.155   1.00 30.95  ? 195 TRP A N   1 
ATOM   1296 C CA  . TRP A 1 166 ? 37.191  6.175   0.720   1.00 35.32  ? 195 TRP A CA  1 
ATOM   1297 C C   . TRP A 1 166 ? 37.728  4.903   0.067   1.00 36.58  ? 195 TRP A C   1 
ATOM   1298 O O   . TRP A 1 166 ? 37.116  4.395   -0.878  1.00 38.12  ? 195 TRP A O   1 
ATOM   1299 C CB  . TRP A 1 166 ? 37.762  7.426   0.036   1.00 38.47  ? 195 TRP A CB  1 
ATOM   1300 C CG  . TRP A 1 166 ? 39.261  7.489   -0.113  1.00 42.49  ? 195 TRP A CG  1 
ATOM   1301 C CD1 . TRP A 1 166 ? 40.141  8.104   0.728   1.00 43.88  ? 195 TRP A CD1 1 
ATOM   1302 C CD2 . TRP A 1 166 ? 40.057  6.961   -1.200  1.00 42.98  ? 195 TRP A CD2 1 
ATOM   1303 N NE1 . TRP A 1 166 ? 41.421  7.980   0.256   1.00 43.61  ? 195 TRP A NE1 1 
ATOM   1304 C CE2 . TRP A 1 166 ? 41.404  7.288   -0.925  1.00 41.12  ? 195 TRP A CE2 1 
ATOM   1305 C CE3 . TRP A 1 166 ? 39.768  6.248   -2.369  1.00 45.25  ? 195 TRP A CE3 1 
ATOM   1306 C CZ2 . TRP A 1 166 ? 42.451  6.924   -1.768  1.00 40.45  ? 195 TRP A CZ2 1 
ATOM   1307 C CZ3 . TRP A 1 166 ? 40.806  5.891   -3.205  1.00 46.88  ? 195 TRP A CZ3 1 
ATOM   1308 C CH2 . TRP A 1 166 ? 42.129  6.221   -2.905  1.00 42.70  ? 195 TRP A CH2 1 
ATOM   1309 N N   . GLU A 1 167 ? 38.860  4.393   0.568   1.00 36.70  ? 196 GLU A N   1 
ATOM   1310 C CA  . GLU A 1 167 ? 39.547  3.280   -0.068  1.00 37.66  ? 196 GLU A CA  1 
ATOM   1311 C C   . GLU A 1 167 ? 38.756  1.986   0.120   1.00 35.38  ? 196 GLU A C   1 
ATOM   1312 O O   . GLU A 1 167 ? 38.753  1.135   -0.759  1.00 35.62  ? 196 GLU A O   1 
ATOM   1313 C CB  . GLU A 1 167 ? 40.965  3.124   0.485   1.00 41.06  ? 196 GLU A CB  1 
ATOM   1314 C CG  . GLU A 1 167 ? 41.866  4.336   0.271   1.00 42.77  ? 196 GLU A CG  1 
ATOM   1315 C CD  . GLU A 1 167 ? 43.240  4.223   0.914   1.00 46.00  ? 196 GLU A CD  1 
ATOM   1316 O OE1 . GLU A 1 167 ? 44.031  5.192   0.835   1.00 50.01  ? 196 GLU A OE1 1 
ATOM   1317 O OE2 . GLU A 1 167 ? 43.527  3.160   1.496   1.00 45.05  ? 196 GLU A OE2 1 
ATOM   1318 N N   . LEU A 1 168 ? 38.101  1.834   1.276   1.00 34.51  ? 197 LEU A N   1 
ATOM   1319 C CA  . LEU A 1 168 ? 37.310  0.649   1.570   1.00 37.29  ? 197 LEU A CA  1 
ATOM   1320 C C   . LEU A 1 168 ? 35.998  0.722   0.787   1.00 36.08  ? 197 LEU A C   1 
ATOM   1321 O O   . LEU A 1 168 ? 35.528  -0.275  0.243   1.00 36.16  ? 197 LEU A O   1 
ATOM   1322 C CB  . LEU A 1 168 ? 37.026  0.540   3.070   1.00 39.57  ? 197 LEU A CB  1 
ATOM   1323 C CG  . LEU A 1 168 ? 38.131  0.005   3.987   1.00 41.66  ? 197 LEU A CG  1 
ATOM   1324 C CD1 . LEU A 1 168 ? 38.814  -1.237  3.417   1.00 42.78  ? 197 LEU A CD1 1 
ATOM   1325 C CD2 . LEU A 1 168 ? 39.129  1.082   4.341   1.00 42.46  ? 197 LEU A CD2 1 
ATOM   1326 N N   . ILE A 1 169 ? 35.433  1.930   0.752   1.00 32.04  ? 198 ILE A N   1 
ATOM   1327 C CA  . ILE A 1 169 ? 34.244  2.249   -0.010  1.00 33.98  ? 198 ILE A CA  1 
ATOM   1328 C C   . ILE A 1 169 ? 34.443  1.874   -1.478  1.00 35.05  ? 198 ILE A C   1 
ATOM   1329 O O   . ILE A 1 169 ? 33.528  1.347   -2.106  1.00 28.16  ? 198 ILE A O   1 
ATOM   1330 C CB  . ILE A 1 169 ? 33.938  3.749   0.145   1.00 35.70  ? 198 ILE A CB  1 
ATOM   1331 C CG1 . ILE A 1 169 ? 33.574  4.101   1.592   1.00 33.19  ? 198 ILE A CG1 1 
ATOM   1332 C CG2 . ILE A 1 169 ? 32.871  4.201   -0.854  1.00 35.47  ? 198 ILE A CG2 1 
ATOM   1333 C CD1 . ILE A 1 169 ? 32.241  3.540   2.058   1.00 34.49  ? 198 ILE A CD1 1 
ATOM   1334 N N   . TYR A 1 170 ? 35.625  2.212   -2.019  1.00 36.52  ? 199 TYR A N   1 
ATOM   1335 C CA  . TYR A 1 170 ? 35.965  1.935   -3.407  1.00 35.14  ? 199 TYR A CA  1 
ATOM   1336 C C   . TYR A 1 170 ? 35.916  0.427   -3.653  1.00 34.10  ? 199 TYR A C   1 
ATOM   1337 O O   . TYR A 1 170 ? 35.374  -0.019  -4.660  1.00 31.80  ? 199 TYR A O   1 
ATOM   1338 C CB  . TYR A 1 170 ? 37.340  2.535   -3.732  1.00 35.36  ? 199 TYR A CB  1 
ATOM   1339 C CG  . TYR A 1 170 ? 37.966  2.022   -5.022  1.00 34.00  ? 199 TYR A CG  1 
ATOM   1340 C CD1 . TYR A 1 170 ? 38.731  0.864   -5.030  1.00 35.83  ? 199 TYR A CD1 1 
ATOM   1341 C CD2 . TYR A 1 170 ? 37.780  2.682   -6.227  1.00 32.25  ? 199 TYR A CD2 1 
ATOM   1342 C CE1 . TYR A 1 170 ? 39.288  0.375   -6.200  1.00 35.84  ? 199 TYR A CE1 1 
ATOM   1343 C CE2 . TYR A 1 170 ? 38.335  2.208   -7.402  1.00 33.39  ? 199 TYR A CE2 1 
ATOM   1344 C CZ  . TYR A 1 170 ? 39.097  1.055   -7.387  1.00 34.91  ? 199 TYR A CZ  1 
ATOM   1345 O OH  . TYR A 1 170 ? 39.644  0.569   -8.537  1.00 38.99  ? 199 TYR A OH  1 
ATOM   1346 N N   . GLU A 1 171 ? 36.485  -0.349  -2.719  1.00 34.72  ? 200 GLU A N   1 
ATOM   1347 C CA  . GLU A 1 171 ? 36.596  -1.792  -2.879  1.00 34.59  ? 200 GLU A CA  1 
ATOM   1348 C C   . GLU A 1 171 ? 35.209  -2.427  -2.907  1.00 35.48  ? 200 GLU A C   1 
ATOM   1349 O O   . GLU A 1 171 ? 34.889  -3.187  -3.823  1.00 34.33  ? 200 GLU A O   1 
ATOM   1350 C CB  . GLU A 1 171 ? 37.470  -2.397  -1.775  1.00 34.85  ? 200 GLU A CB  1 
ATOM   1351 C CG  . GLU A 1 171 ? 38.937  -1.969  -1.852  1.00 34.86  ? 200 GLU A CG  1 
ATOM   1352 C CD  . GLU A 1 171 ? 39.679  -2.359  -3.125  1.00 35.30  ? 200 GLU A CD  1 
ATOM   1353 O OE1 . GLU A 1 171 ? 40.700  -1.707  -3.419  1.00 37.74  ? 200 GLU A OE1 1 
ATOM   1354 O OE2 . GLU A 1 171 ? 39.271  -3.320  -3.812  1.00 37.04  ? 200 GLU A OE2 1 
ATOM   1355 N N   . ASP A 1 172 ? 34.405  -2.119  -1.880  1.00 37.14  ? 201 ASP A N   1 
ATOM   1356 C CA  . ASP A 1 172 ? 33.048  -2.631  -1.767  1.00 37.92  ? 201 ASP A CA  1 
ATOM   1357 C C   . ASP A 1 172 ? 32.234  -2.229  -2.996  1.00 34.48  ? 201 ASP A C   1 
ATOM   1358 O O   . ASP A 1 172 ? 31.539  -3.073  -3.552  1.00 34.13  ? 201 ASP A O   1 
ATOM   1359 C CB  . ASP A 1 172 ? 32.396  -2.189  -0.464  1.00 41.04  ? 201 ASP A CB  1 
ATOM   1360 C CG  . ASP A 1 172 ? 32.885  -2.881  0.799   1.00 40.11  ? 201 ASP A CG  1 
ATOM   1361 O OD1 . ASP A 1 172 ? 33.504  -3.965  0.671   1.00 40.53  ? 201 ASP A OD1 1 
ATOM   1362 O OD2 . ASP A 1 172 ? 32.643  -2.327  1.900   1.00 38.15  ? 201 ASP A OD2 1 
ATOM   1363 N N   . SER A 1 173 ? 32.361  -0.960  -3.426  1.00 34.09  ? 202 SER A N   1 
ATOM   1364 C CA  . SER A 1 173 ? 31.683  -0.442  -4.614  1.00 33.30  ? 202 SER A CA  1 
ATOM   1365 C C   . SER A 1 173 ? 31.983  -1.290  -5.848  1.00 32.52  ? 202 SER A C   1 
ATOM   1366 O O   . SER A 1 173 ? 31.085  -1.615  -6.621  1.00 32.26  ? 202 SER A O   1 
ATOM   1367 C CB  . SER A 1 173 ? 32.032  1.016   -4.882  1.00 32.82  ? 202 SER A CB  1 
ATOM   1368 O OG  . SER A 1 173 ? 31.358  1.896   -3.988  1.00 31.68  ? 202 SER A OG  1 
ATOM   1369 N N   . MET A 1 174 ? 33.259  -1.621  -6.045  1.00 35.68  ? 203 MET A N   1 
ATOM   1370 C CA  . MET A 1 174 ? 33.687  -2.388  -7.208  1.00 36.25  ? 203 MET A CA  1 
ATOM   1371 C C   . MET A 1 174 ? 33.107  -3.798  -7.137  1.00 35.71  ? 203 MET A C   1 
ATOM   1372 O O   . MET A 1 174 ? 32.659  -4.335  -8.145  1.00 34.73  ? 203 MET A O   1 
ATOM   1373 C CB  . MET A 1 174 ? 35.215  -2.453  -7.275  1.00 37.92  ? 203 MET A CB  1 
ATOM   1374 C CG  . MET A 1 174 ? 35.877  -1.105  -7.476  1.00 38.93  ? 203 MET A CG  1 
ATOM   1375 S SD  . MET A 1 174 ? 35.820  -0.538  -9.186  1.00 44.25  ? 203 MET A SD  1 
ATOM   1376 C CE  . MET A 1 174 ? 36.857  -1.813  -9.921  1.00 46.84  ? 203 MET A CE  1 
ATOM   1377 N N   . ASP A 1 175 ? 33.086  -4.382  -5.932  1.00 38.50  ? 204 ASP A N   1 
ATOM   1378 C CA  . ASP A 1 175 ? 32.487  -5.696  -5.735  1.00 37.05  ? 204 ASP A CA  1 
ATOM   1379 C C   . ASP A 1 175 ? 30.988  -5.664  -6.002  1.00 35.94  ? 204 ASP A C   1 
ATOM   1380 O O   . ASP A 1 175 ? 30.444  -6.605  -6.576  1.00 38.50  ? 204 ASP A O   1 
ATOM   1381 C CB  . ASP A 1 175 ? 32.708  -6.220  -4.328  1.00 36.82  ? 204 ASP A CB  1 
ATOM   1382 C CG  . ASP A 1 175 ? 34.116  -6.713  -4.051  1.00 37.79  ? 204 ASP A CG  1 
ATOM   1383 O OD1 . ASP A 1 175 ? 34.923  -6.743  -5.003  1.00 38.56  ? 204 ASP A OD1 1 
ATOM   1384 O OD2 . ASP A 1 175 ? 34.380  -7.060  -2.890  1.00 40.96  ? 204 ASP A OD2 1 
ATOM   1385 N N   . LEU A 1 176 ? 30.317  -4.606  -5.537  1.00 32.70  ? 205 LEU A N   1 
ATOM   1386 C CA  . LEU A 1 176 ? 28.880  -4.508  -5.703  1.00 31.41  ? 205 LEU A CA  1 
ATOM   1387 C C   . LEU A 1 176 ? 28.555  -4.415  -7.192  1.00 30.25  ? 205 LEU A C   1 
ATOM   1388 O O   . LEU A 1 176 ? 27.720  -5.158  -7.689  1.00 29.73  ? 205 LEU A O   1 
ATOM   1389 C CB  . LEU A 1 176 ? 28.352  -3.311  -4.913  1.00 31.65  ? 205 LEU A CB  1 
ATOM   1390 C CG  . LEU A 1 176 ? 26.846  -3.042  -5.021  1.00 31.84  ? 205 LEU A CG  1 
ATOM   1391 C CD1 . LEU A 1 176 ? 25.992  -4.295  -4.929  1.00 34.08  ? 205 LEU A CD1 1 
ATOM   1392 C CD2 . LEU A 1 176 ? 26.433  -2.067  -3.936  1.00 29.84  ? 205 LEU A CD2 1 
ATOM   1393 N N   . ILE A 1 177 ? 29.230  -3.503  -7.899  1.00 33.14  ? 206 ILE A N   1 
ATOM   1394 C CA  . ILE A 1 177 ? 29.002  -3.300  -9.323  1.00 32.77  ? 206 ILE A CA  1 
ATOM   1395 C C   . ILE A 1 177 ? 29.316  -4.601  -10.052 1.00 30.99  ? 206 ILE A C   1 
ATOM   1396 O O   . ILE A 1 177 ? 28.554  -5.031  -10.920 1.00 29.40  ? 206 ILE A O   1 
ATOM   1397 C CB  . ILE A 1 177 ? 29.839  -2.122  -9.858  1.00 35.84  ? 206 ILE A CB  1 
ATOM   1398 C CG1 . ILE A 1 177 ? 29.436  -0.806  -9.209  1.00 36.90  ? 206 ILE A CG1 1 
ATOM   1399 C CG2 . ILE A 1 177 ? 29.752  -2.024  -11.383 1.00 37.44  ? 206 ILE A CG2 1 
ATOM   1400 C CD1 . ILE A 1 177 ? 30.516  0.258   -9.268  1.00 39.68  ? 206 ILE A CD1 1 
ATOM   1401 N N   . ALA A 1 178 ? 30.427  -5.228  -9.653  1.00 31.45  ? 207 ALA A N   1 
ATOM   1402 C CA  . ALA A 1 178 ? 30.871  -6.484  -10.236 1.00 33.00  ? 207 ALA A CA  1 
ATOM   1403 C C   . ALA A 1 178 ? 29.802  -7.565  -10.104 1.00 34.20  ? 207 ALA A C   1 
ATOM   1404 O O   . ALA A 1 178 ? 29.661  -8.385  -11.004 1.00 33.44  ? 207 ALA A O   1 
ATOM   1405 C CB  . ALA A 1 178 ? 32.162  -6.922  -9.595  1.00 33.07  ? 207 ALA A CB  1 
ATOM   1406 N N   . LYS A 1 179 ? 29.044  -7.552  -8.998  1.00 35.76  ? 208 LYS A N   1 
ATOM   1407 C CA  . LYS A 1 179 ? 28.137  -8.645  -8.671  1.00 37.94  ? 208 LYS A CA  1 
ATOM   1408 C C   . LYS A 1 179 ? 26.688  -8.385  -9.096  1.00 39.31  ? 208 LYS A C   1 
ATOM   1409 O O   . LYS A 1 179 ? 25.892  -9.324  -9.104  1.00 39.96  ? 208 LYS A O   1 
ATOM   1410 C CB  . LYS A 1 179 ? 28.204  -8.926  -7.165  1.00 38.20  ? 208 LYS A CB  1 
ATOM   1411 C CG  . LYS A 1 179 ? 29.510  -9.553  -6.714  1.00 38.89  ? 208 LYS A CG  1 
ATOM   1412 C CD  . LYS A 1 179 ? 29.788  -9.430  -5.221  1.00 41.42  ? 208 LYS A CD  1 
ATOM   1413 C CE  . LYS A 1 179 ? 31.226  -9.702  -4.904  1.00 43.04  ? 208 LYS A CE  1 
ATOM   1414 N NZ  . LYS A 1 179 ? 31.488  -9.592  -3.465  1.00 47.41  ? 208 LYS A NZ  1 
ATOM   1415 N N   . LEU A 1 180 ? 26.341  -7.140  -9.461  1.00 39.69  ? 209 LEU A N   1 
ATOM   1416 C CA  . LEU A 1 180 ? 24.949  -6.763  -9.686  1.00 37.03  ? 209 LEU A CA  1 
ATOM   1417 C C   . LEU A 1 180 ? 24.354  -7.512  -10.876 1.00 36.18  ? 209 LEU A C   1 
ATOM   1418 O O   . LEU A 1 180 ? 23.211  -7.966  -10.802 1.00 35.26  ? 209 LEU A O   1 
ATOM   1419 C CB  . LEU A 1 180 ? 24.790  -5.255  -9.867  1.00 37.71  ? 209 LEU A CB  1 
ATOM   1420 C CG  . LEU A 1 180 ? 24.554  -4.451  -8.587  1.00 38.98  ? 209 LEU A CG  1 
ATOM   1421 C CD1 . LEU A 1 180 ? 24.764  -2.965  -8.829  1.00 39.10  ? 209 LEU A CD1 1 
ATOM   1422 C CD2 . LEU A 1 180 ? 23.161  -4.719  -8.038  1.00 39.04  ? 209 LEU A CD2 1 
ATOM   1423 N N   . PRO A 1 181 ? 25.057  -7.630  -12.025 1.00 37.41  ? 210 PRO A N   1 
ATOM   1424 C CA  . PRO A 1 181 ? 24.544  -8.431  -13.140 1.00 39.68  ? 210 PRO A CA  1 
ATOM   1425 C C   . PRO A 1 181 ? 24.264  -9.879  -12.728 1.00 40.44  ? 210 PRO A C   1 
ATOM   1426 O O   . PRO A 1 181 ? 23.257  -10.463 -13.127 1.00 39.43  ? 210 PRO A O   1 
ATOM   1427 C CB  . PRO A 1 181 ? 25.649  -8.308  -14.200 1.00 38.85  ? 210 PRO A CB  1 
ATOM   1428 C CG  . PRO A 1 181 ? 26.329  -7.002  -13.867 1.00 38.10  ? 210 PRO A CG  1 
ATOM   1429 C CD  . PRO A 1 181 ? 26.328  -6.963  -12.347 1.00 38.17  ? 210 PRO A CD  1 
ATOM   1430 N N   . CYS A 1 182 ? 25.132  -10.432 -11.878 1.00 42.54  ? 211 CYS A N   1 
ATOM   1431 C CA  . CYS A 1 182 ? 24.970  -11.802 -11.420 1.00 47.08  ? 211 CYS A CA  1 
ATOM   1432 C C   . CYS A 1 182 ? 23.691  -11.942 -10.602 1.00 45.70  ? 211 CYS A C   1 
ATOM   1433 O O   . CYS A 1 182 ? 22.956  -12.915 -10.791 1.00 46.72  ? 211 CYS A O   1 
ATOM   1434 C CB  . CYS A 1 182 ? 26.200  -12.293 -10.666 1.00 48.56  ? 211 CYS A CB  1 
ATOM   1435 S SG  . CYS A 1 182 ? 27.633  -12.485 -11.756 1.00 52.35  ? 211 CYS A SG  1 
ATOM   1436 N N   . VAL A 1 183 ? 23.421  -10.965 -9.722  1.00 40.75  ? 212 VAL A N   1 
ATOM   1437 C CA  . VAL A 1 183 ? 22.197  -10.980 -8.931  1.00 37.33  ? 212 VAL A CA  1 
ATOM   1438 C C   . VAL A 1 183 ? 21.003  -10.747 -9.850  1.00 34.83  ? 212 VAL A C   1 
ATOM   1439 O O   . VAL A 1 183 ? 20.022  -11.477 -9.780  1.00 34.08  ? 212 VAL A O   1 
ATOM   1440 C CB  . VAL A 1 183 ? 22.179  -9.959  -7.780  1.00 37.36  ? 212 VAL A CB  1 
ATOM   1441 C CG1 . VAL A 1 183 ? 20.811  -9.902  -7.107  1.00 37.39  ? 212 VAL A CG1 1 
ATOM   1442 C CG2 . VAL A 1 183 ? 23.280  -10.220 -6.760  1.00 35.52  ? 212 VAL A CG2 1 
ATOM   1443 N N   . ALA A 1 184 ? 21.081  -9.706  -10.686 1.00 35.74  ? 213 ALA A N   1 
ATOM   1444 C CA  . ALA A 1 184 ? 19.952  -9.294  -11.505 1.00 36.97  ? 213 ALA A CA  1 
ATOM   1445 C C   . ALA A 1 184 ? 19.556  -10.414 -12.456 1.00 37.51  ? 213 ALA A C   1 
ATOM   1446 O O   . ALA A 1 184 ? 18.369  -10.584 -12.736 1.00 40.30  ? 213 ALA A O   1 
ATOM   1447 C CB  . ALA A 1 184 ? 20.283  -8.035  -12.278 1.00 38.70  ? 213 ALA A CB  1 
ATOM   1448 N N   . ALA A 1 185 ? 20.566  -11.139 -12.958 1.00 37.92  ? 214 ALA A N   1 
ATOM   1449 C CA  . ALA A 1 185 ? 20.361  -12.260 -13.865 1.00 38.80  ? 214 ALA A CA  1 
ATOM   1450 C C   . ALA A 1 185 ? 19.713  -13.438 -13.137 1.00 39.92  ? 214 ALA A C   1 
ATOM   1451 O O   . ALA A 1 185 ? 18.787  -14.055 -13.661 1.00 44.13  ? 214 ALA A O   1 
ATOM   1452 C CB  . ALA A 1 185 ? 21.677  -12.668 -14.485 1.00 40.63  ? 214 ALA A CB  1 
ATOM   1453 N N   . LYS A 1 186 ? 20.207  -13.751 -11.933 1.00 40.87  ? 215 LYS A N   1 
ATOM   1454 C CA  . LYS A 1 186 ? 19.667  -14.852 -11.146 1.00 41.05  ? 215 LYS A CA  1 
ATOM   1455 C C   . LYS A 1 186 ? 18.181  -14.604 -10.881 1.00 40.99  ? 215 LYS A C   1 
ATOM   1456 O O   . LYS A 1 186 ? 17.388  -15.532 -11.001 1.00 42.85  ? 215 LYS A O   1 
ATOM   1457 C CB  . LYS A 1 186 ? 20.497  -15.102 -9.877  1.00 39.96  ? 215 LYS A CB  1 
ATOM   1458 N N   . ILE A 1 187 ? 17.811  -13.346 -10.574 1.00 41.29  ? 216 ILE A N   1 
ATOM   1459 C CA  . ILE A 1 187 ? 16.428  -12.948 -10.343 1.00 39.58  ? 216 ILE A CA  1 
ATOM   1460 C C   . ILE A 1 187 ? 15.606  -13.114 -11.618 1.00 41.01  ? 216 ILE A C   1 
ATOM   1461 O O   . ILE A 1 187 ? 14.448  -13.526 -11.553 1.00 41.61  ? 216 ILE A O   1 
ATOM   1462 C CB  . ILE A 1 187 ? 16.314  -11.489 -9.860  1.00 40.77  ? 216 ILE A CB  1 
ATOM   1463 C CG1 . ILE A 1 187 ? 17.067  -11.228 -8.559  1.00 40.98  ? 216 ILE A CG1 1 
ATOM   1464 C CG2 . ILE A 1 187 ? 14.842  -11.084 -9.738  1.00 40.22  ? 216 ILE A CG2 1 
ATOM   1465 C CD1 . ILE A 1 187 ? 17.242  -9.754  -8.239  1.00 40.51  ? 216 ILE A CD1 1 
ATOM   1466 N N   . TYR A 1 188 ? 16.183  -12.710 -12.757 1.00 40.18  ? 217 TYR A N   1 
ATOM   1467 C CA  . TYR A 1 188 ? 15.497  -12.778 -14.036 1.00 39.99  ? 217 TYR A CA  1 
ATOM   1468 C C   . TYR A 1 188 ? 15.214  -14.235 -14.387 1.00 41.97  ? 217 TYR A C   1 
ATOM   1469 O O   . TYR A 1 188 ? 14.137  -14.553 -14.880 1.00 41.45  ? 217 TYR A O   1 
ATOM   1470 C CB  . TYR A 1 188 ? 16.300  -12.136 -15.175 1.00 39.22  ? 217 TYR A CB  1 
ATOM   1471 C CG  . TYR A 1 188 ? 15.556  -12.138 -16.506 1.00 38.21  ? 217 TYR A CG  1 
ATOM   1472 C CD1 . TYR A 1 188 ? 14.462  -11.305 -16.711 1.00 38.41  ? 217 TYR A CD1 1 
ATOM   1473 C CD2 . TYR A 1 188 ? 15.928  -12.977 -17.550 1.00 37.22  ? 217 TYR A CD2 1 
ATOM   1474 C CE1 . TYR A 1 188 ? 13.759  -11.306 -17.903 1.00 36.81  ? 217 TYR A CE1 1 
ATOM   1475 C CE2 . TYR A 1 188 ? 15.237  -12.981 -18.752 1.00 36.77  ? 217 TYR A CE2 1 
ATOM   1476 C CZ  . TYR A 1 188 ? 14.151  -12.145 -18.930 1.00 36.72  ? 217 TYR A CZ  1 
ATOM   1477 O OH  . TYR A 1 188 ? 13.457  -12.119 -20.107 1.00 37.47  ? 217 TYR A OH  1 
ATOM   1478 N N   . ARG A 1 189 ? 16.185  -15.117 -14.133 1.00 46.07  ? 218 ARG A N   1 
ATOM   1479 C CA  . ARG A 1 189 ? 16.101  -16.484 -14.626 1.00 50.69  ? 218 ARG A CA  1 
ATOM   1480 C C   . ARG A 1 189 ? 15.237  -17.347 -13.708 1.00 51.29  ? 218 ARG A C   1 
ATOM   1481 O O   . ARG A 1 189 ? 14.572  -18.263 -14.181 1.00 51.86  ? 218 ARG A O   1 
ATOM   1482 C CB  . ARG A 1 189 ? 17.502  -17.053 -14.870 1.00 53.17  ? 218 ARG A CB  1 
ATOM   1483 C CG  . ARG A 1 189 ? 18.074  -16.536 -16.182 1.00 57.71  ? 218 ARG A CG  1 
ATOM   1484 C CD  . ARG A 1 189 ? 19.183  -17.421 -16.728 1.00 63.65  ? 218 ARG A CD  1 
ATOM   1485 N NE  . ARG A 1 189 ? 19.099  -17.583 -18.185 1.00 65.27  ? 218 ARG A NE  1 
ATOM   1486 C CZ  . ARG A 1 189 ? 20.020  -18.160 -18.952 1.00 68.69  ? 218 ARG A CZ  1 
ATOM   1487 N NH1 . ARG A 1 189 ? 21.215  -18.462 -18.470 1.00 68.51  ? 218 ARG A NH1 1 
ATOM   1488 N NH2 . ARG A 1 189 ? 19.754  -18.396 -20.226 1.00 69.90  ? 218 ARG A NH2 1 
ATOM   1489 N N   . ASN A 1 190 ? 15.233  -17.041 -12.408 1.00 51.48  ? 219 ASN A N   1 
ATOM   1490 C CA  . ASN A 1 190 ? 14.360  -17.726 -11.468 1.00 49.66  ? 219 ASN A CA  1 
ATOM   1491 C C   . ASN A 1 190 ? 12.905  -17.354 -11.737 1.00 48.69  ? 219 ASN A C   1 
ATOM   1492 O O   . ASN A 1 190 ? 12.010  -18.168 -11.530 1.00 49.42  ? 219 ASN A O   1 
ATOM   1493 C CB  . ASN A 1 190 ? 14.734  -17.420 -10.022 1.00 48.22  ? 219 ASN A CB  1 
ATOM   1494 C CG  . ASN A 1 190 ? 16.120  -17.901 -9.661  1.00 47.87  ? 219 ASN A CG  1 
ATOM   1495 O OD1 . ASN A 1 190 ? 16.862  -18.391 -10.520 1.00 49.49  ? 219 ASN A OD1 1 
ATOM   1496 N ND2 . ASN A 1 190 ? 16.497  -17.750 -8.401  1.00 48.32  ? 219 ASN A ND2 1 
ATOM   1497 N N   . LEU A 1 191 ? 12.676  -16.120 -12.194 1.00 49.99  ? 220 LEU A N   1 
ATOM   1498 C CA  . LEU A 1 191 ? 11.330  -15.585 -12.316 1.00 51.21  ? 220 LEU A CA  1 
ATOM   1499 C C   . LEU A 1 191 ? 10.744  -15.874 -13.698 1.00 52.51  ? 220 LEU A C   1 
ATOM   1500 O O   . LEU A 1 191 ? 9.522   -15.875 -13.851 1.00 48.77  ? 220 LEU A O   1 
ATOM   1501 C CB  . LEU A 1 191 ? 11.322  -14.080 -12.041 1.00 52.49  ? 220 LEU A CB  1 
ATOM   1502 C CG  . LEU A 1 191 ? 11.229  -13.642 -10.576 1.00 53.91  ? 220 LEU A CG  1 
ATOM   1503 C CD1 . LEU A 1 191 ? 11.375  -12.130 -10.463 1.00 54.40  ? 220 LEU A CD1 1 
ATOM   1504 C CD2 . LEU A 1 191 ? 9.924   -14.078 -9.939  1.00 52.79  ? 220 LEU A CD2 1 
ATOM   1505 N N   . TYR A 1 192 ? 11.604  -16.067 -14.707 1.00 52.19  ? 221 TYR A N   1 
ATOM   1506 C CA  . TYR A 1 192 ? 11.139  -16.096 -16.086 1.00 53.76  ? 221 TYR A CA  1 
ATOM   1507 C C   . TYR A 1 192 ? 11.815  -17.199 -16.902 1.00 53.87  ? 221 TYR A C   1 
ATOM   1508 O O   . TYR A 1 192 ? 11.607  -17.260 -18.110 1.00 55.40  ? 221 TYR A O   1 
ATOM   1509 C CB  . TYR A 1 192 ? 11.364  -14.712 -16.711 1.00 53.72  ? 221 TYR A CB  1 
ATOM   1510 C CG  . TYR A 1 192 ? 10.898  -13.556 -15.834 1.00 52.14  ? 221 TYR A CG  1 
ATOM   1511 C CD1 . TYR A 1 192 ? 9.545   -13.332 -15.593 1.00 49.79  ? 221 TYR A CD1 1 
ATOM   1512 C CD2 . TYR A 1 192 ? 11.812  -12.696 -15.238 1.00 51.49  ? 221 TYR A CD2 1 
ATOM   1513 C CE1 . TYR A 1 192 ? 9.117   -12.286 -14.794 1.00 47.79  ? 221 TYR A CE1 1 
ATOM   1514 C CE2 . TYR A 1 192 ? 11.398  -11.645 -14.437 1.00 52.17  ? 221 TYR A CE2 1 
ATOM   1515 C CZ  . TYR A 1 192 ? 10.048  -11.443 -14.212 1.00 49.49  ? 221 TYR A CZ  1 
ATOM   1516 O OH  . TYR A 1 192 ? 9.661   -10.404 -13.421 1.00 51.53  ? 221 TYR A OH  1 
ATOM   1517 N N   . ARG A 1 193 ? 12.602  -18.071 -16.258 1.00 53.63  ? 222 ARG A N   1 
ATOM   1518 C CA  . ARG A 1 193 ? 13.291  -19.144 -16.961 1.00 57.21  ? 222 ARG A CA  1 
ATOM   1519 C C   . ARG A 1 193 ? 13.327  -20.397 -16.087 1.00 59.30  ? 222 ARG A C   1 
ATOM   1520 O O   . ARG A 1 193 ? 14.313  -21.130 -16.086 1.00 57.82  ? 222 ARG A O   1 
ATOM   1521 C CB  . ARG A 1 193 ? 14.713  -18.728 -17.359 1.00 56.39  ? 222 ARG A CB  1 
ATOM   1522 C CG  . ARG A 1 193 ? 14.832  -17.516 -18.276 1.00 56.22  ? 222 ARG A CG  1 
ATOM   1523 C CD  . ARG A 1 193 ? 14.233  -17.728 -19.656 1.00 56.25  ? 222 ARG A CD  1 
ATOM   1524 N NE  . ARG A 1 193 ? 14.405  -16.538 -20.499 1.00 59.03  ? 222 ARG A NE  1 
ATOM   1525 C CZ  . ARG A 1 193 ? 13.511  -15.578 -20.726 1.00 56.72  ? 222 ARG A CZ  1 
ATOM   1526 N NH1 . ARG A 1 193 ? 12.348  -15.566 -20.094 1.00 58.37  ? 222 ARG A NH1 1 
ATOM   1527 N NH2 . ARG A 1 193 ? 13.802  -14.606 -21.574 1.00 56.86  ? 222 ARG A NH2 1 
ATOM   1528 N N   . GLU A 1 194 ? 12.254  -20.611 -15.317 1.00 64.59  ? 223 GLU A N   1 
ATOM   1529 C CA  . GLU A 1 194 ? 12.056  -21.847 -14.578 1.00 70.14  ? 223 GLU A CA  1 
ATOM   1530 C C   . GLU A 1 194 ? 13.263  -22.177 -13.695 1.00 69.98  ? 223 GLU A C   1 
ATOM   1531 O O   . GLU A 1 194 ? 13.490  -23.345 -13.389 1.00 73.22  ? 223 GLU A O   1 
ATOM   1532 C CB  . GLU A 1 194 ? 11.779  -22.976 -15.572 1.00 74.47  ? 223 GLU A CB  1 
ATOM   1533 C CG  . GLU A 1 194 ? 10.610  -22.693 -16.513 1.00 76.85  ? 223 GLU A CG  1 
ATOM   1534 C CD  . GLU A 1 194 ? 10.360  -23.766 -17.563 1.00 76.62  ? 223 GLU A CD  1 
ATOM   1535 O OE1 . GLU A 1 194 ? 10.267  -23.397 -18.751 1.00 77.22  ? 223 GLU A OE1 1 
ATOM   1536 O OE2 . GLU A 1 194 ? 10.258  -24.961 -17.206 1.00 73.09  ? 223 GLU A OE2 1 
ATOM   1537 N N   . GLY A 1 195 ? 14.028  -21.155 -13.286 1.00 66.22  ? 224 GLY A N   1 
ATOM   1538 C CA  . GLY A 1 195 ? 15.073  -21.319 -12.286 1.00 64.65  ? 224 GLY A CA  1 
ATOM   1539 C C   . GLY A 1 195 ? 16.373  -21.885 -12.854 1.00 66.24  ? 224 GLY A C   1 
ATOM   1540 O O   . GLY A 1 195 ? 17.195  -22.390 -12.090 1.00 62.07  ? 224 GLY A O   1 
ATOM   1541 N N   . SER A 1 196 ? 16.570  -21.766 -14.176 1.00 69.82  ? 225 SER A N   1 
ATOM   1542 C CA  . SER A 1 196 ? 17.753  -22.304 -14.835 1.00 71.12  ? 225 SER A CA  1 
ATOM   1543 C C   . SER A 1 196 ? 18.980  -21.468 -14.479 1.00 74.50  ? 225 SER A C   1 
ATOM   1544 O O   . SER A 1 196 ? 18.856  -20.310 -14.084 1.00 72.98  ? 225 SER A O   1 
ATOM   1545 C CB  . SER A 1 196 ? 17.576  -22.384 -16.334 1.00 72.79  ? 225 SER A CB  1 
ATOM   1546 O OG  . SER A 1 196 ? 17.450  -21.095 -16.919 1.00 75.16  ? 225 SER A OG  1 
ATOM   1547 N N   . GLY A 1 197 ? 20.162  -22.075 -14.642 1.00 75.86  ? 226 GLY A N   1 
ATOM   1548 C CA  . GLY A 1 197 ? 21.422  -21.430 -14.315 1.00 76.90  ? 226 GLY A CA  1 
ATOM   1549 C C   . GLY A 1 197 ? 21.636  -20.170 -15.150 1.00 79.13  ? 226 GLY A C   1 
ATOM   1550 O O   . GLY A 1 197 ? 20.995  -19.992 -16.184 1.00 78.43  ? 226 GLY A O   1 
ATOM   1551 N N   . ILE A 1 198 ? 22.544  -19.306 -14.680 1.00 80.29  ? 227 ILE A N   1 
ATOM   1552 C CA  . ILE A 1 198 ? 22.846  -18.046 -15.344 1.00 79.73  ? 227 ILE A CA  1 
ATOM   1553 C C   . ILE A 1 198 ? 24.021  -18.235 -16.307 1.00 76.82  ? 227 ILE A C   1 
ATOM   1554 O O   . ILE A 1 198 ? 24.135  -17.518 -17.298 1.00 79.39  ? 227 ILE A O   1 
ATOM   1555 C CB  . ILE A 1 198 ? 23.091  -16.911 -14.326 1.00 80.76  ? 227 ILE A CB  1 
ATOM   1556 C CG1 . ILE A 1 198 ? 24.093  -17.300 -13.224 1.00 83.34  ? 227 ILE A CG1 1 
ATOM   1557 C CG2 . ILE A 1 198 ? 21.762  -16.429 -13.738 1.00 80.01  ? 227 ILE A CG2 1 
ATOM   1558 C CD1 . ILE A 1 198 ? 24.505  -16.152 -12.317 1.00 84.12  ? 227 ILE A CD1 1 
ATOM   1559 N N   . GLY A 1 199 ? 24.890  -19.209 -16.026 1.00 71.32  ? 228 GLY A N   1 
ATOM   1560 C CA  . GLY A 1 199 ? 26.053  -19.444 -16.863 1.00 70.36  ? 228 GLY A CA  1 
ATOM   1561 C C   . GLY A 1 199 ? 27.248  -18.640 -16.363 1.00 71.05  ? 228 GLY A C   1 
ATOM   1562 O O   . GLY A 1 199 ? 27.086  -17.696 -15.593 1.00 72.37  ? 228 GLY A O   1 
ATOM   1563 N N   . ALA A 1 200 ? 28.442  -19.025 -16.823 1.00 70.52  ? 229 ALA A N   1 
ATOM   1564 C CA  . ALA A 1 200 ? 29.688  -18.515 -16.276 1.00 72.17  ? 229 ALA A CA  1 
ATOM   1565 C C   . ALA A 1 200 ? 29.979  -17.118 -16.819 1.00 72.81  ? 229 ALA A C   1 
ATOM   1566 O O   . ALA A 1 200 ? 29.386  -16.688 -17.810 1.00 68.06  ? 229 ALA A O   1 
ATOM   1567 C CB  . ALA A 1 200 ? 30.817  -19.473 -16.592 1.00 70.85  ? 229 ALA A CB  1 
ATOM   1568 N N   . ILE A 1 201 ? 30.893  -16.424 -16.133 1.00 72.19  ? 230 ILE A N   1 
ATOM   1569 C CA  . ILE A 1 201 ? 31.400  -15.132 -16.565 1.00 73.95  ? 230 ILE A CA  1 
ATOM   1570 C C   . ILE A 1 201 ? 32.562  -15.380 -17.522 1.00 68.26  ? 230 ILE A C   1 
ATOM   1571 O O   . ILE A 1 201 ? 33.283  -16.364 -17.381 1.00 69.56  ? 230 ILE A O   1 
ATOM   1572 C CB  . ILE A 1 201 ? 31.820  -14.280 -15.348 1.00 79.58  ? 230 ILE A CB  1 
ATOM   1573 C CG1 . ILE A 1 201 ? 30.622  -13.906 -14.462 1.00 81.53  ? 230 ILE A CG1 1 
ATOM   1574 C CG2 . ILE A 1 201 ? 32.601  -13.035 -15.774 1.00 80.88  ? 230 ILE A CG2 1 
ATOM   1575 C CD1 . ILE A 1 201 ? 29.681  -12.877 -15.070 1.00 81.67  ? 230 ILE A CD1 1 
ATOM   1576 N N   . ASP A 1 202 ? 32.721  -14.480 -18.499 1.00 64.24  ? 231 ASP A N   1 
ATOM   1577 C CA  . ASP A 1 202 ? 33.858  -14.493 -19.403 1.00 60.38  ? 231 ASP A CA  1 
ATOM   1578 C C   . ASP A 1 202 ? 34.675  -13.222 -19.172 1.00 58.10  ? 231 ASP A C   1 
ATOM   1579 O O   . ASP A 1 202 ? 34.193  -12.124 -19.441 1.00 53.78  ? 231 ASP A O   1 
ATOM   1580 C CB  . ASP A 1 202 ? 33.400  -14.618 -20.847 1.00 57.66  ? 231 ASP A CB  1 
ATOM   1581 C CG  . ASP A 1 202 ? 34.499  -14.946 -21.847 1.00 58.81  ? 231 ASP A CG  1 
ATOM   1582 O OD1 . ASP A 1 202 ? 35.548  -14.265 -21.820 1.00 59.78  ? 231 ASP A OD1 1 
ATOM   1583 O OD2 . ASP A 1 202 ? 34.294  -15.881 -22.646 1.00 61.24  ? 231 ASP A OD2 1 
ATOM   1584 N N   . SER A 1 203 ? 35.926  -13.383 -18.718 1.00 56.25  ? 232 SER A N   1 
ATOM   1585 C CA  . SER A 1 203 ? 36.730  -12.265 -18.245 1.00 54.28  ? 232 SER A CA  1 
ATOM   1586 C C   . SER A 1 203 ? 37.278  -11.417 -19.394 1.00 55.17  ? 232 SER A C   1 
ATOM   1587 O O   . SER A 1 203 ? 37.973  -10.434 -19.149 1.00 54.82  ? 232 SER A O   1 
ATOM   1588 C CB  . SER A 1 203 ? 37.851  -12.748 -17.361 1.00 53.60  ? 232 SER A CB  1 
ATOM   1589 O OG  . SER A 1 203 ? 38.488  -11.656 -16.710 1.00 54.32  ? 232 SER A OG  1 
ATOM   1590 N N   . ASN A 1 204 ? 36.966  -11.779 -20.642 1.00 56.59  ? 233 ASN A N   1 
ATOM   1591 C CA  . ASN A 1 204 ? 37.419  -11.000 -21.782 1.00 59.56  ? 233 ASN A CA  1 
ATOM   1592 C C   . ASN A 1 204 ? 36.260  -10.212 -22.393 1.00 57.40  ? 233 ASN A C   1 
ATOM   1593 O O   . ASN A 1 204 ? 36.489  -9.359  -23.249 1.00 54.59  ? 233 ASN A O   1 
ATOM   1594 C CB  . ASN A 1 204 ? 38.152  -11.890 -22.779 1.00 65.84  ? 233 ASN A CB  1 
ATOM   1595 C CG  . ASN A 1 204 ? 39.425  -12.462 -22.192 1.00 64.68  ? 233 ASN A CG  1 
ATOM   1596 O OD1 . ASN A 1 204 ? 40.345  -11.711 -21.845 1.00 63.18  ? 233 ASN A OD1 1 
ATOM   1597 N ND2 . ASN A 1 204 ? 39.501  -13.779 -22.066 1.00 62.43  ? 233 ASN A ND2 1 
ATOM   1598 N N   . LEU A 1 205 ? 35.024  -10.478 -21.948 1.00 55.95  ? 234 LEU A N   1 
ATOM   1599 C CA  . LEU A 1 205 ? 33.868  -9.734  -22.431 1.00 55.25  ? 234 LEU A CA  1 
ATOM   1600 C C   . LEU A 1 205 ? 33.638  -8.520  -21.533 1.00 53.27  ? 234 LEU A C   1 
ATOM   1601 O O   . LEU A 1 205 ? 34.318  -8.351  -20.524 1.00 51.38  ? 234 LEU A O   1 
ATOM   1602 C CB  . LEU A 1 205 ? 32.644  -10.648 -22.490 1.00 55.75  ? 234 LEU A CB  1 
ATOM   1603 C CG  . LEU A 1 205 ? 32.780  -11.904 -23.361 1.00 56.18  ? 234 LEU A CG  1 
ATOM   1604 C CD1 . LEU A 1 205 ? 31.443  -12.620 -23.497 1.00 54.58  ? 234 LEU A CD1 1 
ATOM   1605 C CD2 . LEU A 1 205 ? 33.355  -11.602 -24.740 1.00 56.76  ? 234 LEU A CD2 1 
ATOM   1606 N N   . ASP A 1 206 ? 32.689  -7.661  -21.920 1.00 51.02  ? 235 ASP A N   1 
ATOM   1607 C CA  . ASP A 1 206 ? 32.387  -6.470  -21.141 1.00 48.64  ? 235 ASP A CA  1 
ATOM   1608 C C   . ASP A 1 206 ? 31.236  -6.776  -20.186 1.00 44.20  ? 235 ASP A C   1 
ATOM   1609 O O   . ASP A 1 206 ? 30.587  -7.813  -20.297 1.00 42.65  ? 235 ASP A O   1 
ATOM   1610 C CB  . ASP A 1 206 ? 32.171  -5.250  -22.028 1.00 50.39  ? 235 ASP A CB  1 
ATOM   1611 C CG  . ASP A 1 206 ? 30.952  -5.271  -22.942 1.00 49.39  ? 235 ASP A CG  1 
ATOM   1612 O OD1 . ASP A 1 206 ? 29.817  -5.214  -22.423 1.00 47.85  ? 235 ASP A OD1 1 
ATOM   1613 O OD2 . ASP A 1 206 ? 31.147  -5.321  -24.171 1.00 47.67  ? 235 ASP A OD2 1 
ATOM   1614 N N   . TRP A 1 207 ? 31.013  -5.841  -19.252 1.00 44.26  ? 236 TRP A N   1 
ATOM   1615 C CA  . TRP A 1 207 ? 30.030  -5.947  -18.182 1.00 40.58  ? 236 TRP A CA  1 
ATOM   1616 C C   . TRP A 1 207 ? 28.639  -6.202  -18.758 1.00 41.51  ? 236 TRP A C   1 
ATOM   1617 O O   . TRP A 1 207 ? 27.936  -7.110  -18.316 1.00 42.62  ? 236 TRP A O   1 
ATOM   1618 C CB  . TRP A 1 207 ? 30.092  -4.650  -17.362 1.00 40.93  ? 236 TRP A CB  1 
ATOM   1619 C CG  . TRP A 1 207 ? 29.320  -4.602  -16.069 1.00 41.94  ? 236 TRP A CG  1 
ATOM   1620 C CD1 . TRP A 1 207 ? 29.496  -5.382  -14.963 1.00 43.34  ? 236 TRP A CD1 1 
ATOM   1621 C CD2 . TRP A 1 207 ? 28.328  -3.615  -15.704 1.00 42.40  ? 236 TRP A CD2 1 
ATOM   1622 N NE1 . TRP A 1 207 ? 28.643  -4.991  -13.962 1.00 42.82  ? 236 TRP A NE1 1 
ATOM   1623 C CE2 . TRP A 1 207 ? 27.922  -3.905  -14.382 1.00 41.74  ? 236 TRP A CE2 1 
ATOM   1624 C CE3 . TRP A 1 207 ? 27.735  -2.534  -16.366 1.00 42.26  ? 236 TRP A CE3 1 
ATOM   1625 C CZ2 . TRP A 1 207 ? 26.958  -3.149  -13.720 1.00 40.63  ? 236 TRP A CZ2 1 
ATOM   1626 C CZ3 . TRP A 1 207 ? 26.787  -1.782  -15.705 1.00 40.52  ? 236 TRP A CZ3 1 
ATOM   1627 C CH2 . TRP A 1 207 ? 26.414  -2.082  -14.398 1.00 40.28  ? 236 TRP A CH2 1 
ATOM   1628 N N   . SER A 1 208 ? 28.267  -5.406  -19.768 1.00 41.17  ? 237 SER A N   1 
ATOM   1629 C CA  . SER A 1 208 ? 26.959  -5.507  -20.392 1.00 42.38  ? 237 SER A CA  1 
ATOM   1630 C C   . SER A 1 208 ? 26.854  -6.790  -21.212 1.00 43.62  ? 237 SER A C   1 
ATOM   1631 O O   . SER A 1 208 ? 25.754  -7.298  -21.425 1.00 42.26  ? 237 SER A O   1 
ATOM   1632 C CB  . SER A 1 208 ? 26.669  -4.296  -21.246 1.00 43.33  ? 237 SER A CB  1 
ATOM   1633 O OG  . SER A 1 208 ? 26.750  -3.102  -20.479 1.00 44.67  ? 237 SER A OG  1 
ATOM   1634 N N   . HIS A 1 209 ? 28.001  -7.288  -21.690 1.00 43.90  ? 238 HIS A N   1 
ATOM   1635 C CA  . HIS A 1 209 ? 28.027  -8.481  -22.519 1.00 46.85  ? 238 HIS A CA  1 
ATOM   1636 C C   . HIS A 1 209 ? 27.790  -9.696  -21.624 1.00 44.35  ? 238 HIS A C   1 
ATOM   1637 O O   . HIS A 1 209 ? 26.950  -10.536 -21.930 1.00 43.02  ? 238 HIS A O   1 
ATOM   1638 C CB  . HIS A 1 209 ? 29.322  -8.547  -23.342 1.00 48.18  ? 238 HIS A CB  1 
ATOM   1639 C CG  . HIS A 1 209 ? 29.243  -9.434  -24.544 1.00 50.19  ? 238 HIS A CG  1 
ATOM   1640 N ND1 . HIS A 1 209 ? 30.215  -9.439  -25.521 1.00 49.59  ? 238 HIS A ND1 1 
ATOM   1641 C CD2 . HIS A 1 209 ? 28.330  -10.348 -24.927 1.00 50.78  ? 238 HIS A CD2 1 
ATOM   1642 C CE1 . HIS A 1 209 ? 29.887  -10.317 -26.461 1.00 49.12  ? 238 HIS A CE1 1 
ATOM   1643 N NE2 . HIS A 1 209 ? 28.746  -10.881 -26.120 1.00 50.17  ? 238 HIS A NE2 1 
ATOM   1644 N N   . ASN A 1 210 ? 28.511  -9.766  -20.499 1.00 47.30  ? 239 ASN A N   1 
ATOM   1645 C CA  . ASN A 1 210 ? 28.297  -10.833 -19.531 1.00 47.38  ? 239 ASN A CA  1 
ATOM   1646 C C   . ASN A 1 210 ? 26.852  -10.811 -19.046 1.00 45.82  ? 239 ASN A C   1 
ATOM   1647 O O   . ASN A 1 210 ? 26.209  -11.856 -19.001 1.00 47.43  ? 239 ASN A O   1 
ATOM   1648 C CB  . ASN A 1 210 ? 29.277  -10.771 -18.366 1.00 48.53  ? 239 ASN A CB  1 
ATOM   1649 C CG  . ASN A 1 210 ? 30.630  -11.331 -18.739 1.00 51.71  ? 239 ASN A CG  1 
ATOM   1650 O OD1 . ASN A 1 210 ? 30.710  -12.366 -19.411 1.00 54.02  ? 239 ASN A OD1 1 
ATOM   1651 N ND2 . ASN A 1 210 ? 31.701  -10.672 -18.319 1.00 51.91  ? 239 ASN A ND2 1 
ATOM   1652 N N   . PHE A 1 211 ? 26.341  -9.613  -18.731 1.00 43.03  ? 240 PHE A N   1 
ATOM   1653 C CA  . PHE A 1 211 ? 25.003  -9.461  -18.183 1.00 41.33  ? 240 PHE A CA  1 
ATOM   1654 C C   . PHE A 1 211 ? 23.977  -10.139 -19.087 1.00 42.75  ? 240 PHE A C   1 
ATOM   1655 O O   . PHE A 1 211 ? 23.216  -10.974 -18.605 1.00 45.30  ? 240 PHE A O   1 
ATOM   1656 C CB  . PHE A 1 211 ? 24.633  -7.985  -18.001 1.00 41.22  ? 240 PHE A CB  1 
ATOM   1657 C CG  . PHE A 1 211 ? 23.365  -7.730  -17.196 1.00 41.60  ? 240 PHE A CG  1 
ATOM   1658 C CD1 . PHE A 1 211 ? 22.864  -8.680  -16.307 1.00 41.12  ? 240 PHE A CD1 1 
ATOM   1659 C CD2 . PHE A 1 211 ? 22.698  -6.516  -17.300 1.00 42.02  ? 240 PHE A CD2 1 
ATOM   1660 C CE1 . PHE A 1 211 ? 21.725  -8.425  -15.563 1.00 40.70  ? 240 PHE A CE1 1 
ATOM   1661 C CE2 . PHE A 1 211 ? 21.558  -6.269  -16.552 1.00 43.74  ? 240 PHE A CE2 1 
ATOM   1662 C CZ  . PHE A 1 211 ? 21.080  -7.222  -15.679 1.00 41.84  ? 240 PHE A CZ  1 
ATOM   1663 N N   . THR A 1 212 ? 23.969  -9.768  -20.381 1.00 42.89  ? 241 THR A N   1 
ATOM   1664 C CA  . THR A 1 212 ? 22.982  -10.254 -21.339 1.00 43.99  ? 241 THR A CA  1 
ATOM   1665 C C   . THR A 1 212 ? 23.210  -11.735 -21.660 1.00 44.72  ? 241 THR A C   1 
ATOM   1666 O O   . THR A 1 212 ? 22.277  -12.413 -22.089 1.00 44.67  ? 241 THR A O   1 
ATOM   1667 C CB  . THR A 1 212 ? 22.970  -9.414  -22.624 1.00 44.52  ? 241 THR A CB  1 
ATOM   1668 O OG1 . THR A 1 212 ? 24.242  -9.494  -23.262 1.00 43.74  ? 241 THR A OG1 1 
ATOM   1669 C CG2 . THR A 1 212 ? 22.621  -7.957  -22.374 1.00 46.71  ? 241 THR A CG2 1 
ATOM   1670 N N   . ASN A 1 213 ? 24.446  -12.228 -21.486 1.00 47.36  ? 242 ASN A N   1 
ATOM   1671 C CA  . ASN A 1 213 ? 24.739  -13.646 -21.654 1.00 52.06  ? 242 ASN A CA  1 
ATOM   1672 C C   . ASN A 1 213 ? 24.071  -14.440 -20.532 1.00 53.73  ? 242 ASN A C   1 
ATOM   1673 O O   . ASN A 1 213 ? 23.587  -15.543 -20.759 1.00 53.96  ? 242 ASN A O   1 
ATOM   1674 C CB  . ASN A 1 213 ? 26.240  -13.926 -21.704 1.00 53.42  ? 242 ASN A CB  1 
ATOM   1675 C CG  . ASN A 1 213 ? 26.871  -13.568 -23.031 1.00 54.63  ? 242 ASN A CG  1 
ATOM   1676 O OD1 . ASN A 1 213 ? 26.172  -13.333 -24.026 1.00 54.19  ? 242 ASN A OD1 1 
ATOM   1677 N ND2 . ASN A 1 213 ? 28.195  -13.536 -23.069 1.00 55.20  ? 242 ASN A ND2 1 
ATOM   1678 N N   . MET A 1 214 ? 24.033  -13.858 -19.328 1.00 53.14  ? 243 MET A N   1 
ATOM   1679 C CA  . MET A 1 214 ? 23.424  -14.504 -18.177 1.00 50.85  ? 243 MET A CA  1 
ATOM   1680 C C   . MET A 1 214 ? 21.909  -14.332 -18.214 1.00 49.91  ? 243 MET A C   1 
ATOM   1681 O O   . MET A 1 214 ? 21.176  -15.202 -17.747 1.00 53.22  ? 243 MET A O   1 
ATOM   1682 C CB  . MET A 1 214 ? 23.981  -13.927 -16.875 1.00 49.80  ? 243 MET A CB  1 
ATOM   1683 C CG  . MET A 1 214 ? 25.475  -14.113 -16.738 1.00 49.45  ? 243 MET A CG  1 
ATOM   1684 S SD  . MET A 1 214 ? 26.065  -13.690 -15.090 1.00 50.29  ? 243 MET A SD  1 
ATOM   1685 C CE  . MET A 1 214 ? 25.890  -11.900 -15.100 1.00 49.60  ? 243 MET A CE  1 
ATOM   1686 N N   . LEU A 1 215 ? 21.446  -13.204 -18.760 1.00 46.46  ? 244 LEU A N   1 
ATOM   1687 C CA  . LEU A 1 215 ? 20.029  -13.013 -18.997 1.00 46.44  ? 244 LEU A CA  1 
ATOM   1688 C C   . LEU A 1 215 ? 19.579  -13.998 -20.073 1.00 51.69  ? 244 LEU A C   1 
ATOM   1689 O O   . LEU A 1 215 ? 18.405  -14.347 -20.136 1.00 57.88  ? 244 LEU A O   1 
ATOM   1690 C CB  . LEU A 1 215 ? 19.722  -11.570 -19.395 1.00 45.84  ? 244 LEU A CB  1 
ATOM   1691 C CG  . LEU A 1 215 ? 19.846  -10.508 -18.295 1.00 43.49  ? 244 LEU A CG  1 
ATOM   1692 C CD1 . LEU A 1 215 ? 19.688  -9.122  -18.892 1.00 42.05  ? 244 LEU A CD1 1 
ATOM   1693 C CD2 . LEU A 1 215 ? 18.837  -10.702 -17.179 1.00 44.07  ? 244 LEU A CD2 1 
ATOM   1694 N N   . GLY A 1 216 ? 20.524  -14.435 -20.915 1.00 56.00  ? 245 GLY A N   1 
ATOM   1695 C CA  . GLY A 1 216 ? 20.267  -15.462 -21.913 1.00 55.73  ? 245 GLY A CA  1 
ATOM   1696 C C   . GLY A 1 216 ? 19.839  -14.863 -23.250 1.00 57.37  ? 245 GLY A C   1 
ATOM   1697 O O   . GLY A 1 216 ? 19.211  -15.539 -24.064 1.00 61.44  ? 245 GLY A O   1 
ATOM   1698 N N   . TYR A 1 217 ? 20.182  -13.587 -23.457 1.00 56.65  ? 246 TYR A N   1 
ATOM   1699 C CA  . TYR A 1 217 ? 19.987  -12.922 -24.732 1.00 54.92  ? 246 TYR A CA  1 
ATOM   1700 C C   . TYR A 1 217 ? 21.315  -12.927 -25.482 1.00 60.27  ? 246 TYR A C   1 
ATOM   1701 O O   . TYR A 1 217 ? 22.377  -12.778 -24.877 1.00 64.58  ? 246 TYR A O   1 
ATOM   1702 C CB  . TYR A 1 217 ? 19.463  -11.509 -24.466 1.00 52.24  ? 246 TYR A CB  1 
ATOM   1703 C CG  . TYR A 1 217 ? 18.047  -11.414 -23.909 1.00 47.74  ? 246 TYR A CG  1 
ATOM   1704 C CD1 . TYR A 1 217 ? 17.757  -11.729 -22.584 1.00 45.03  ? 246 TYR A CD1 1 
ATOM   1705 C CD2 . TYR A 1 217 ? 17.005  -10.961 -24.707 1.00 47.10  ? 246 TYR A CD2 1 
ATOM   1706 C CE1 . TYR A 1 217 ? 16.469  -11.627 -22.084 1.00 42.95  ? 246 TYR A CE1 1 
ATOM   1707 C CE2 . TYR A 1 217 ? 15.715  -10.843 -24.216 1.00 46.47  ? 246 TYR A CE2 1 
ATOM   1708 C CZ  . TYR A 1 217 ? 15.447  -11.175 -22.902 1.00 44.41  ? 246 TYR A CZ  1 
ATOM   1709 O OH  . TYR A 1 217 ? 14.163  -11.038 -22.459 1.00 46.99  ? 246 TYR A OH  1 
ATOM   1710 N N   . THR A 1 218 ? 21.250  -13.118 -26.803 1.00 60.69  ? 247 THR A N   1 
ATOM   1711 C CA  . THR A 1 218 ? 22.437  -13.042 -27.639 1.00 62.05  ? 247 THR A CA  1 
ATOM   1712 C C   . THR A 1 218 ? 22.075  -12.484 -29.009 1.00 57.89  ? 247 THR A C   1 
ATOM   1713 O O   . THR A 1 218 ? 22.524  -12.995 -30.031 1.00 63.02  ? 247 THR A O   1 
ATOM   1714 C CB  . THR A 1 218 ? 23.090  -14.417 -27.730 1.00 68.49  ? 247 THR A CB  1 
ATOM   1715 O OG1 . THR A 1 218 ? 21.995  -15.301 -27.971 1.00 66.41  ? 247 THR A OG1 1 
ATOM   1716 C CG2 . THR A 1 218 ? 23.884  -14.737 -26.473 1.00 69.25  ? 247 THR A CG2 1 
ATOM   1717 N N   . ASP A 1 219 ? 21.245  -11.439 -29.001 1.00 55.79  ? 248 ASP A N   1 
ATOM   1718 C CA  . ASP A 1 219 ? 21.152  -10.518 -30.115 1.00 52.45  ? 248 ASP A CA  1 
ATOM   1719 C C   . ASP A 1 219 ? 22.130  -9.382  -29.848 1.00 52.98  ? 248 ASP A C   1 
ATOM   1720 O O   . ASP A 1 219 ? 22.020  -8.694  -28.836 1.00 54.63  ? 248 ASP A O   1 
ATOM   1721 C CB  . ASP A 1 219 ? 19.733  -10.014 -30.319 1.00 50.67  ? 248 ASP A CB  1 
ATOM   1722 C CG  . ASP A 1 219 ? 19.570  -9.038  -31.475 1.00 52.82  ? 248 ASP A CG  1 
ATOM   1723 O OD1 . ASP A 1 219 ? 20.612  -8.604  -32.025 1.00 53.46  ? 248 ASP A OD1 1 
ATOM   1724 O OD2 . ASP A 1 219 ? 18.410  -8.732  -31.829 1.00 51.86  ? 248 ASP A OD2 1 
ATOM   1725 N N   . HIS A 1 220 ? 23.079  -9.197  -30.771 1.00 52.83  ? 249 HIS A N   1 
ATOM   1726 C CA  . HIS A 1 220 ? 24.087  -8.157  -30.665 1.00 51.70  ? 249 HIS A CA  1 
ATOM   1727 C C   . HIS A 1 220 ? 23.420  -6.823  -30.334 1.00 52.06  ? 249 HIS A C   1 
ATOM   1728 O O   . HIS A 1 220 ? 23.925  -6.064  -29.512 1.00 53.26  ? 249 HIS A O   1 
ATOM   1729 C CB  . HIS A 1 220 ? 24.889  -8.073  -31.970 1.00 53.26  ? 249 HIS A CB  1 
ATOM   1730 C CG  . HIS A 1 220 ? 25.968  -7.044  -31.959 1.00 57.01  ? 249 HIS A CG  1 
ATOM   1731 N ND1 . HIS A 1 220 ? 26.885  -6.926  -30.934 1.00 59.19  ? 249 HIS A ND1 1 
ATOM   1732 C CD2 . HIS A 1 220 ? 26.280  -6.093  -32.852 1.00 57.54  ? 249 HIS A CD2 1 
ATOM   1733 C CE1 . HIS A 1 220 ? 27.714  -5.927  -31.202 1.00 57.39  ? 249 HIS A CE1 1 
ATOM   1734 N NE2 . HIS A 1 220 ? 27.361  -5.404  -32.361 1.00 59.99  ? 249 HIS A NE2 1 
ATOM   1735 N N   . GLN A 1 221 ? 22.278  -6.562  -30.981 1.00 53.45  ? 250 GLN A N   1 
ATOM   1736 C CA  . GLN A 1 221 ? 21.584  -5.289  -30.883 1.00 53.84  ? 250 GLN A CA  1 
ATOM   1737 C C   . GLN A 1 221 ? 21.073  -5.041  -29.467 1.00 51.75  ? 250 GLN A C   1 
ATOM   1738 O O   . GLN A 1 221 ? 20.977  -3.891  -29.045 1.00 54.72  ? 250 GLN A O   1 
ATOM   1739 C CB  . GLN A 1 221 ? 20.424  -5.241  -31.877 1.00 58.02  ? 250 GLN A CB  1 
ATOM   1740 C CG  . GLN A 1 221 ? 20.855  -4.925  -33.304 1.00 64.67  ? 250 GLN A CG  1 
ATOM   1741 C CD  . GLN A 1 221 ? 21.616  -3.620  -33.394 1.00 72.55  ? 250 GLN A CD  1 
ATOM   1742 O OE1 . GLN A 1 221 ? 21.239  -2.619  -32.772 1.00 79.28  ? 250 GLN A OE1 1 
ATOM   1743 N NE2 . GLN A 1 221 ? 22.719  -3.630  -34.128 1.00 75.98  ? 250 GLN A NE2 1 
ATOM   1744 N N   . PHE A 1 222 ? 20.729  -6.118  -28.752 1.00 48.17  ? 251 PHE A N   1 
ATOM   1745 C CA  . PHE A 1 222 ? 20.223  -6.002  -27.396 1.00 44.49  ? 251 PHE A CA  1 
ATOM   1746 C C   . PHE A 1 222 ? 21.378  -5.755  -26.426 1.00 44.52  ? 251 PHE A C   1 
ATOM   1747 O O   . PHE A 1 222 ? 21.227  -5.013  -25.455 1.00 43.43  ? 251 PHE A O   1 
ATOM   1748 C CB  . PHE A 1 222 ? 19.424  -7.243  -27.001 1.00 42.10  ? 251 PHE A CB  1 
ATOM   1749 C CG  . PHE A 1 222 ? 18.776  -7.087  -25.635 1.00 42.18  ? 251 PHE A CG  1 
ATOM   1750 C CD1 . PHE A 1 222 ? 17.763  -6.158  -25.437 1.00 43.86  ? 251 PHE A CD1 1 
ATOM   1751 C CD2 . PHE A 1 222 ? 19.195  -7.850  -24.553 1.00 43.89  ? 251 PHE A CD2 1 
ATOM   1752 C CE1 . PHE A 1 222 ? 17.172  -6.009  -24.195 1.00 45.38  ? 251 PHE A CE1 1 
ATOM   1753 C CE2 . PHE A 1 222 ? 18.610  -7.689  -23.307 1.00 44.93  ? 251 PHE A CE2 1 
ATOM   1754 C CZ  . PHE A 1 222 ? 17.596  -6.775  -23.132 1.00 45.05  ? 251 PHE A CZ  1 
ATOM   1755 N N   . THR A 1 223 ? 22.529  -6.384  -26.691 1.00 41.30  ? 252 THR A N   1 
ATOM   1756 C CA  . THR A 1 223 ? 23.743  -6.086  -25.950 1.00 40.99  ? 252 THR A CA  1 
ATOM   1757 C C   . THR A 1 223 ? 24.084  -4.604  -26.124 1.00 40.53  ? 252 THR A C   1 
ATOM   1758 O O   . THR A 1 223 ? 24.433  -3.940  -25.150 1.00 40.41  ? 252 THR A O   1 
ATOM   1759 C CB  . THR A 1 223 ? 24.874  -7.010  -26.407 1.00 40.25  ? 252 THR A CB  1 
ATOM   1760 O OG1 . THR A 1 223 ? 24.363  -8.329  -26.266 1.00 38.60  ? 252 THR A OG1 1 
ATOM   1761 C CG2 . THR A 1 223 ? 26.135  -6.884  -25.569 1.00 42.16  ? 252 THR A CG2 1 
ATOM   1762 N N   . GLU A 1 224 ? 23.958  -4.085  -27.357 1.00 39.36  ? 253 GLU A N   1 
ATOM   1763 C CA  . GLU A 1 224 ? 24.216  -2.677  -27.630 1.00 38.39  ? 253 GLU A CA  1 
ATOM   1764 C C   . GLU A 1 224 ? 23.202  -1.791  -26.899 1.00 38.40  ? 253 GLU A C   1 
ATOM   1765 O O   . GLU A 1 224 ? 23.558  -0.732  -26.389 1.00 38.31  ? 253 GLU A O   1 
ATOM   1766 C CB  . GLU A 1 224 ? 24.207  -2.394  -29.132 1.00 39.33  ? 253 GLU A CB  1 
ATOM   1767 C CG  . GLU A 1 224 ? 25.476  -2.865  -29.839 1.00 40.42  ? 253 GLU A CG  1 
ATOM   1768 C CD  . GLU A 1 224 ? 26.703  -2.039  -29.489 1.00 40.21  ? 253 GLU A CD  1 
ATOM   1769 O OE1 . GLU A 1 224 ? 27.497  -2.497  -28.649 1.00 40.96  ? 253 GLU A OE1 1 
ATOM   1770 O OE2 . GLU A 1 224 ? 26.875  -0.939  -30.057 1.00 43.94  ? 253 GLU A OE2 1 
ATOM   1771 N N   . LEU A 1 225 ? 21.934  -2.217  -26.867 1.00 38.14  ? 254 LEU A N   1 
ATOM   1772 C CA  . LEU A 1 225 ? 20.897  -1.473  -26.173 1.00 36.99  ? 254 LEU A CA  1 
ATOM   1773 C C   . LEU A 1 225 ? 21.243  -1.392  -24.688 1.00 35.71  ? 254 LEU A C   1 
ATOM   1774 O O   . LEU A 1 225 ? 21.231  -0.310  -24.110 1.00 36.19  ? 254 LEU A O   1 
ATOM   1775 C CB  . LEU A 1 225 ? 19.521  -2.095  -26.400 1.00 35.22  ? 254 LEU A CB  1 
ATOM   1776 C CG  . LEU A 1 225 ? 18.375  -1.493  -25.583 1.00 35.73  ? 254 LEU A CG  1 
ATOM   1777 C CD1 . LEU A 1 225 ? 18.344  0.021   -25.698 1.00 38.48  ? 254 LEU A CD1 1 
ATOM   1778 C CD2 . LEU A 1 225 ? 17.040  -2.074  -26.022 1.00 36.44  ? 254 LEU A CD2 1 
ATOM   1779 N N   . THR A 1 226 ? 21.547  -2.546  -24.091 1.00 35.45  ? 255 THR A N   1 
ATOM   1780 C CA  . THR A 1 226 ? 21.947  -2.630  -22.697 1.00 36.32  ? 255 THR A CA  1 
ATOM   1781 C C   . THR A 1 226 ? 23.053  -1.623  -22.409 1.00 38.57  ? 255 THR A C   1 
ATOM   1782 O O   . THR A 1 226 ? 22.973  -0.881  -21.433 1.00 38.28  ? 255 THR A O   1 
ATOM   1783 C CB  . THR A 1 226 ? 22.433  -4.044  -22.397 1.00 36.77  ? 255 THR A CB  1 
ATOM   1784 O OG1 . THR A 1 226 ? 21.302  -4.865  -22.662 1.00 36.03  ? 255 THR A OG1 1 
ATOM   1785 C CG2 . THR A 1 226 ? 22.916  -4.196  -20.967 1.00 36.65  ? 255 THR A CG2 1 
ATOM   1786 N N   . ARG A 1 227 ? 24.091  -1.631  -23.255 1.00 36.29  ? 256 ARG A N   1 
ATOM   1787 C CA  . ARG A 1 227 ? 25.236  -0.757  -23.071 1.00 37.06  ? 256 ARG A CA  1 
ATOM   1788 C C   . ARG A 1 227 ? 24.769  0.694   -22.988 1.00 37.26  ? 256 ARG A C   1 
ATOM   1789 O O   . ARG A 1 227 ? 25.187  1.435   -22.104 1.00 36.89  ? 256 ARG A O   1 
ATOM   1790 C CB  . ARG A 1 227 ? 26.264  -0.944  -24.196 1.00 37.78  ? 256 ARG A CB  1 
ATOM   1791 C CG  . ARG A 1 227 ? 27.125  -2.192  -24.067 1.00 37.25  ? 256 ARG A CG  1 
ATOM   1792 C CD  . ARG A 1 227 ? 27.955  -2.412  -25.314 1.00 37.62  ? 256 ARG A CD  1 
ATOM   1793 N NE  . ARG A 1 227 ? 28.790  -3.618  -25.255 1.00 38.67  ? 256 ARG A NE  1 
ATOM   1794 C CZ  . ARG A 1 227 ? 28.879  -4.556  -26.191 1.00 42.72  ? 256 ARG A CZ  1 
ATOM   1795 N NH1 . ARG A 1 227 ? 28.106  -4.528  -27.265 1.00 43.33  ? 256 ARG A NH1 1 
ATOM   1796 N NH2 . ARG A 1 227 ? 29.746  -5.542  -26.049 1.00 45.45  ? 256 ARG A NH2 1 
ATOM   1797 N N   . LEU A 1 228 ? 23.907  1.093   -23.925 1.00 37.79  ? 257 LEU A N   1 
ATOM   1798 C CA  . LEU A 1 228 ? 23.392  2.448   -23.943 1.00 37.97  ? 257 LEU A CA  1 
ATOM   1799 C C   . LEU A 1 228 ? 22.556  2.697   -22.689 1.00 37.24  ? 257 LEU A C   1 
ATOM   1800 O O   . LEU A 1 228 ? 22.683  3.742   -22.052 1.00 35.06  ? 257 LEU A O   1 
ATOM   1801 C CB  . LEU A 1 228 ? 22.579  2.660   -25.218 1.00 39.37  ? 257 LEU A CB  1 
ATOM   1802 C CG  . LEU A 1 228 ? 21.973  4.054   -25.407 1.00 37.87  ? 257 LEU A CG  1 
ATOM   1803 C CD1 . LEU A 1 228 ? 23.061  5.110   -25.370 1.00 37.71  ? 257 LEU A CD1 1 
ATOM   1804 C CD2 . LEU A 1 228 ? 21.176  4.125   -26.698 1.00 37.30  ? 257 LEU A CD2 1 
ATOM   1805 N N   . TYR A 1 229 ? 21.705  1.724   -22.355 1.00 37.81  ? 258 TYR A N   1 
ATOM   1806 C CA  . TYR A 1 229 ? 20.690  1.883   -21.324 1.00 36.36  ? 258 TYR A CA  1 
ATOM   1807 C C   . TYR A 1 229 ? 21.382  2.072   -19.978 1.00 33.37  ? 258 TYR A C   1 
ATOM   1808 O O   . TYR A 1 229 ? 20.999  2.928   -19.184 1.00 33.43  ? 258 TYR A O   1 
ATOM   1809 C CB  . TYR A 1 229 ? 19.726  0.690   -21.346 1.00 36.38  ? 258 TYR A CB  1 
ATOM   1810 C CG  . TYR A 1 229 ? 18.704  0.724   -20.220 1.00 38.06  ? 258 TYR A CG  1 
ATOM   1811 C CD1 . TYR A 1 229 ? 19.097  0.490   -18.908 1.00 38.76  ? 258 TYR A CD1 1 
ATOM   1812 C CD2 . TYR A 1 229 ? 17.364  1.017   -20.456 1.00 38.25  ? 258 TYR A CD2 1 
ATOM   1813 C CE1 . TYR A 1 229 ? 18.198  0.556   -17.860 1.00 38.44  ? 258 TYR A CE1 1 
ATOM   1814 C CE2 . TYR A 1 229 ? 16.450  1.075   -19.415 1.00 38.04  ? 258 TYR A CE2 1 
ATOM   1815 C CZ  . TYR A 1 229 ? 16.872  0.843   -18.117 1.00 38.70  ? 258 TYR A CZ  1 
ATOM   1816 O OH  . TYR A 1 229 ? 16.024  0.884   -17.056 1.00 45.17  ? 258 TYR A OH  1 
ATOM   1817 N N   . LEU A 1 230 ? 22.423  1.279   -19.744 1.00 33.92  ? 259 LEU A N   1 
ATOM   1818 C CA  . LEU A 1 230 ? 23.146  1.310   -18.485 1.00 35.49  ? 259 LEU A CA  1 
ATOM   1819 C C   . LEU A 1 230 ? 23.976  2.583   -18.349 1.00 34.81  ? 259 LEU A C   1 
ATOM   1820 O O   . LEU A 1 230 ? 24.162  3.065   -17.233 1.00 35.95  ? 259 LEU A O   1 
ATOM   1821 C CB  . LEU A 1 230 ? 23.996  0.051   -18.389 1.00 36.65  ? 259 LEU A CB  1 
ATOM   1822 C CG  . LEU A 1 230 ? 23.222  -1.268  -18.318 1.00 38.32  ? 259 LEU A CG  1 
ATOM   1823 C CD1 . LEU A 1 230 ? 24.196  -2.439  -18.380 1.00 40.16  ? 259 LEU A CD1 1 
ATOM   1824 C CD2 . LEU A 1 230 ? 22.374  -1.350  -17.069 1.00 37.98  ? 259 LEU A CD2 1 
ATOM   1825 N N   . THR A 1 231 ? 24.467  3.130   -19.471 1.00 33.18  ? 260 THR A N   1 
ATOM   1826 C CA  . THR A 1 231 ? 25.179  4.398   -19.440 1.00 34.46  ? 260 THR A CA  1 
ATOM   1827 C C   . THR A 1 231 ? 24.213  5.528   -19.075 1.00 35.18  ? 260 THR A C   1 
ATOM   1828 O O   . THR A 1 231 ? 24.439  6.251   -18.108 1.00 37.05  ? 260 THR A O   1 
ATOM   1829 C CB  . THR A 1 231 ? 25.877  4.694   -20.768 1.00 34.56  ? 260 THR A CB  1 
ATOM   1830 O OG1 . THR A 1 231 ? 26.866  3.698   -21.015 1.00 33.46  ? 260 THR A OG1 1 
ATOM   1831 C CG2 . THR A 1 231 ? 26.578  6.040   -20.740 1.00 34.31  ? 260 THR A CG2 1 
ATOM   1832 N N   . ILE A 1 232 ? 23.134  5.679   -19.848 1.00 33.43  ? 261 ILE A N   1 
ATOM   1833 C CA  . ILE A 1 232 ? 22.310  6.875   -19.756 1.00 33.72  ? 261 ILE A CA  1 
ATOM   1834 C C   . ILE A 1 232 ? 21.535  6.909   -18.438 1.00 33.38  ? 261 ILE A C   1 
ATOM   1835 O O   . ILE A 1 232 ? 21.248  7.996   -17.945 1.00 30.89  ? 261 ILE A O   1 
ATOM   1836 C CB  . ILE A 1 232 ? 21.390  7.022   -20.982 1.00 34.64  ? 261 ILE A CB  1 
ATOM   1837 C CG1 . ILE A 1 232 ? 20.325  5.921   -21.048 1.00 36.59  ? 261 ILE A CG1 1 
ATOM   1838 C CG2 . ILE A 1 232 ? 22.230  7.111   -22.261 1.00 34.90  ? 261 ILE A CG2 1 
ATOM   1839 C CD1 . ILE A 1 232 ? 19.403  6.009   -22.255 1.00 36.05  ? 261 ILE A CD1 1 
ATOM   1840 N N   . HIS A 1 233 ? 21.210  5.737   -17.867 1.00 33.02  ? 262 HIS A N   1 
ATOM   1841 C CA  . HIS A 1 233 ? 20.483  5.673   -16.601 1.00 31.72  ? 262 HIS A CA  1 
ATOM   1842 C C   . HIS A 1 233 ? 21.429  5.763   -15.396 1.00 30.72  ? 262 HIS A C   1 
ATOM   1843 O O   . HIS A 1 233 ? 20.977  5.663   -14.252 1.00 29.03  ? 262 HIS A O   1 
ATOM   1844 C CB  . HIS A 1 233 ? 19.664  4.377   -16.489 1.00 30.79  ? 262 HIS A CB  1 
ATOM   1845 C CG  . HIS A 1 233 ? 18.418  4.329   -17.306 1.00 30.14  ? 262 HIS A CG  1 
ATOM   1846 N ND1 . HIS A 1 233 ? 18.410  4.057   -18.658 1.00 32.09  ? 262 HIS A ND1 1 
ATOM   1847 C CD2 . HIS A 1 233 ? 17.141  4.530   -16.959 1.00 30.67  ? 262 HIS A CD2 1 
ATOM   1848 C CE1 . HIS A 1 233 ? 17.160  4.090   -19.097 1.00 31.88  ? 262 HIS A CE1 1 
ATOM   1849 N NE2 . HIS A 1 233 ? 16.375  4.372   -18.076 1.00 30.53  ? 262 HIS A NE2 1 
ATOM   1850 N N   . SER A 1 234 ? 22.732  5.954   -15.647 1.00 30.66  ? 263 SER A N   1 
ATOM   1851 C CA  . SER A 1 234 ? 23.753  5.756   -14.626 1.00 31.26  ? 263 SER A CA  1 
ATOM   1852 C C   . SER A 1 234 ? 23.584  6.713   -13.448 1.00 30.42  ? 263 SER A C   1 
ATOM   1853 O O   . SER A 1 234 ? 23.688  6.274   -12.308 1.00 31.99  ? 263 SER A O   1 
ATOM   1854 C CB  . SER A 1 234 ? 25.155  5.848   -15.204 1.00 31.57  ? 263 SER A CB  1 
ATOM   1855 O OG  . SER A 1 234 ? 25.387  7.091   -15.861 1.00 32.49  ? 263 SER A OG  1 
ATOM   1856 N N   . ASP A 1 235 ? 23.350  8.006   -13.717 1.00 30.39  ? 264 ASP A N   1 
ATOM   1857 C CA  . ASP A 1 235 ? 23.258  9.032   -12.678 1.00 31.95  ? 264 ASP A CA  1 
ATOM   1858 C C   . ASP A 1 235 ? 22.304  10.124  -13.160 1.00 32.56  ? 264 ASP A C   1 
ATOM   1859 O O   . ASP A 1 235 ? 22.003  10.202  -14.347 1.00 33.18  ? 264 ASP A O   1 
ATOM   1860 C CB  . ASP A 1 235 ? 24.634  9.591   -12.331 1.00 33.99  ? 264 ASP A CB  1 
ATOM   1861 C CG  . ASP A 1 235 ? 24.845  10.123  -10.915 1.00 37.34  ? 264 ASP A CG  1 
ATOM   1862 O OD1 . ASP A 1 235 ? 24.336  9.499   -9.964  1.00 39.60  ? 264 ASP A OD1 1 
ATOM   1863 O OD2 . ASP A 1 235 ? 25.572  11.132  -10.758 1.00 39.68  ? 264 ASP A OD2 1 
ATOM   1864 N N   . HIS A 1 236 ? 21.808  10.952  -12.231 1.00 33.15  ? 265 HIS A N   1 
ATOM   1865 C CA  . HIS A 1 236 ? 20.948  12.072  -12.574 1.00 31.52  ? 265 HIS A CA  1 
ATOM   1866 C C   . HIS A 1 236 ? 20.885  13.058  -11.414 1.00 31.55  ? 265 HIS A C   1 
ATOM   1867 O O   . HIS A 1 236 ? 19.793  13.424  -10.968 1.00 30.11  ? 265 HIS A O   1 
ATOM   1868 C CB  . HIS A 1 236 ? 19.526  11.598  -12.895 1.00 35.24  ? 265 HIS A CB  1 
ATOM   1869 C CG  . HIS A 1 236 ? 18.847  12.405  -13.957 1.00 36.68  ? 265 HIS A CG  1 
ATOM   1870 N ND1 . HIS A 1 236 ? 17.561  12.886  -13.858 1.00 38.72  ? 265 HIS A ND1 1 
ATOM   1871 C CD2 . HIS A 1 236 ? 19.300  12.804  -15.153 1.00 37.24  ? 265 HIS A CD2 1 
ATOM   1872 C CE1 . HIS A 1 236 ? 17.258  13.545  -14.972 1.00 41.82  ? 265 HIS A CE1 1 
ATOM   1873 N NE2 . HIS A 1 236 ? 18.303  13.514  -15.770 1.00 38.68  ? 265 HIS A NE2 1 
ATOM   1874 N N   . GLU A 1 237 ? 22.061  13.457  -10.916 1.00 30.75  ? 266 GLU A N   1 
ATOM   1875 C CA  . GLU A 1 237 ? 22.154  14.441  -9.846  1.00 33.96  ? 266 GLU A CA  1 
ATOM   1876 C C   . GLU A 1 237 ? 21.965  13.779  -8.485  1.00 32.80  ? 266 GLU A C   1 
ATOM   1877 O O   . GLU A 1 237 ? 21.742  12.577  -8.376  1.00 35.86  ? 266 GLU A O   1 
ATOM   1878 C CB  . GLU A 1 237 ? 21.126  15.570  -9.969  1.00 35.60  ? 266 GLU A CB  1 
ATOM   1879 C CG  . GLU A 1 237 ? 21.732  16.876  -10.461 1.00 39.82  ? 266 GLU A CG  1 
ATOM   1880 C CD  . GLU A 1 237 ? 20.929  18.105  -10.081 1.00 41.40  ? 266 GLU A CD  1 
ATOM   1881 O OE1 . GLU A 1 237 ? 19.861  17.982  -9.430  1.00 41.98  ? 266 GLU A OE1 1 
ATOM   1882 O OE2 . GLU A 1 237 ? 21.407  19.199  -10.445 1.00 48.60  ? 266 GLU A OE2 1 
ATOM   1883 N N   . GLY A 1 238 ? 22.046  14.598  -7.435  1.00 31.14  ? 267 GLY A N   1 
ATOM   1884 C CA  . GLY A 1 238 ? 21.982  14.094  -6.080  1.00 29.35  ? 267 GLY A CA  1 
ATOM   1885 C C   . GLY A 1 238 ? 20.554  14.053  -5.571  1.00 27.63  ? 267 GLY A C   1 
ATOM   1886 O O   . GLY A 1 238 ? 20.274  13.355  -4.603  1.00 28.28  ? 267 GLY A O   1 
ATOM   1887 N N   . GLY A 1 239 ? 19.663  14.787  -6.248  1.00 28.46  ? 268 GLY A N   1 
ATOM   1888 C CA  . GLY A 1 239 ? 18.382  15.164  -5.677  1.00 28.39  ? 268 GLY A CA  1 
ATOM   1889 C C   . GLY A 1 239 ? 17.293  14.134  -5.941  1.00 26.08  ? 268 GLY A C   1 
ATOM   1890 O O   . GLY A 1 239 ? 16.235  14.202  -5.315  1.00 24.38  ? 268 GLY A O   1 
ATOM   1891 N N   . ASN A 1 240 ? 17.554  13.198  -6.871  1.00 25.77  ? 269 ASN A N   1 
ATOM   1892 C CA  . ASN A 1 240 ? 16.610  12.126  -7.157  1.00 25.46  ? 269 ASN A CA  1 
ATOM   1893 C C   . ASN A 1 240 ? 16.617  11.159  -5.978  1.00 24.95  ? 269 ASN A C   1 
ATOM   1894 O O   . ASN A 1 240 ? 17.616  11.083  -5.270  1.00 25.89  ? 269 ASN A O   1 
ATOM   1895 C CB  . ASN A 1 240 ? 16.902  11.431  -8.482  1.00 25.46  ? 269 ASN A CB  1 
ATOM   1896 C CG  . ASN A 1 240 ? 18.146  10.572  -8.438  1.00 24.47  ? 269 ASN A CG  1 
ATOM   1897 O OD1 . ASN A 1 240 ? 18.170  9.537   -7.763  1.00 26.17  ? 269 ASN A OD1 1 
ATOM   1898 N ND2 . ASN A 1 240 ? 19.179  10.976  -9.159  1.00 23.43  ? 269 ASN A ND2 1 
ATOM   1899 N N   . VAL A 1 241 ? 15.507  10.428  -5.795  1.00 24.15  ? 270 VAL A N   1 
ATOM   1900 C CA  . VAL A 1 241 ? 15.248  9.674   -4.571  1.00 25.51  ? 270 VAL A CA  1 
ATOM   1901 C C   . VAL A 1 241 ? 16.280  8.566   -4.376  1.00 22.79  ? 270 VAL A C   1 
ATOM   1902 O O   . VAL A 1 241 ? 16.726  8.357   -3.257  1.00 20.05  ? 270 VAL A O   1 
ATOM   1903 C CB  . VAL A 1 241 ? 13.804  9.129   -4.492  1.00 26.53  ? 270 VAL A CB  1 
ATOM   1904 C CG1 . VAL A 1 241 ? 13.664  7.934   -3.553  1.00 26.46  ? 270 VAL A CG1 1 
ATOM   1905 C CG2 . VAL A 1 241 ? 12.826  10.217  -4.071  1.00 27.60  ? 270 VAL A CG2 1 
ATOM   1906 N N   . SER A 1 242 ? 16.674  7.870   -5.453  1.00 23.58  ? 271 SER A N   1 
ATOM   1907 C CA  . SER A 1 242 ? 17.641  6.786   -5.340  1.00 22.85  ? 271 SER A CA  1 
ATOM   1908 C C   . SER A 1 242 ? 19.022  7.332   -4.957  1.00 22.47  ? 271 SER A C   1 
ATOM   1909 O O   . SER A 1 242 ? 19.651  6.830   -4.022  1.00 22.55  ? 271 SER A O   1 
ATOM   1910 C CB  . SER A 1 242 ? 17.694  5.935   -6.600  1.00 23.56  ? 271 SER A CB  1 
ATOM   1911 O OG  . SER A 1 242 ? 17.954  6.710   -7.770  1.00 24.72  ? 271 SER A OG  1 
ATOM   1912 N N   . ALA A 1 243 ? 19.489  8.382   -5.645  1.00 20.34  ? 272 ALA A N   1 
ATOM   1913 C CA  . ALA A 1 243 ? 20.793  8.944   -5.338  1.00 21.73  ? 272 ALA A CA  1 
ATOM   1914 C C   . ALA A 1 243 ? 20.806  9.563   -3.941  1.00 22.34  ? 272 ALA A C   1 
ATOM   1915 O O   . ALA A 1 243 ? 21.830  9.561   -3.267  1.00 22.69  ? 272 ALA A O   1 
ATOM   1916 C CB  . ALA A 1 243 ? 21.198  9.965   -6.378  1.00 22.67  ? 272 ALA A CB  1 
ATOM   1917 N N   . HIS A 1 244 ? 19.661  10.090  -3.506  1.00 23.27  ? 273 HIS A N   1 
ATOM   1918 C CA  . HIS A 1 244 ? 19.608  10.882  -2.288  1.00 23.03  ? 273 HIS A CA  1 
ATOM   1919 C C   . HIS A 1 244 ? 19.528  9.943   -1.087  1.00 23.53  ? 273 HIS A C   1 
ATOM   1920 O O   . HIS A 1 244 ? 20.211  10.159  -0.084  1.00 23.40  ? 273 HIS A O   1 
ATOM   1921 C CB  . HIS A 1 244 ? 18.488  11.922  -2.402  1.00 22.55  ? 273 HIS A CB  1 
ATOM   1922 C CG  . HIS A 1 244 ? 18.311  12.778  -1.195  1.00 21.72  ? 273 HIS A CG  1 
ATOM   1923 N ND1 . HIS A 1 244 ? 17.118  13.417  -0.937  1.00 22.81  ? 273 HIS A ND1 1 
ATOM   1924 C CD2 . HIS A 1 244 ? 19.132  13.109  -0.194  1.00 22.38  ? 273 HIS A CD2 1 
ATOM   1925 C CE1 . HIS A 1 244 ? 17.221  14.100  0.199   1.00 22.65  ? 273 HIS A CE1 1 
ATOM   1926 N NE2 . HIS A 1 244 ? 18.433  13.928  0.673   1.00 22.47  ? 273 HIS A NE2 1 
ATOM   1927 N N   . THR A 1 245 ? 18.724  8.875   -1.204  1.00 23.39  ? 274 THR A N   1 
ATOM   1928 C CA  . THR A 1 245 ? 18.696  7.827   -0.192  1.00 23.37  ? 274 THR A CA  1 
ATOM   1929 C C   . THR A 1 245 ? 20.117  7.311   0.055   1.00 25.87  ? 274 THR A C   1 
ATOM   1930 O O   . THR A 1 245 ? 20.577  7.231   1.204   1.00 24.51  ? 274 THR A O   1 
ATOM   1931 C CB  . THR A 1 245 ? 17.758  6.707   -0.638  1.00 24.98  ? 274 THR A CB  1 
ATOM   1932 O OG1 . THR A 1 245 ? 16.469  7.257   -0.917  1.00 25.64  ? 274 THR A OG1 1 
ATOM   1933 C CG2 . THR A 1 245 ? 17.627  5.615   0.409   1.00 25.31  ? 274 THR A CG2 1 
ATOM   1934 N N   . SER A 1 246 ? 20.827  6.961   -1.027  1.00 27.10  ? 275 SER A N   1 
ATOM   1935 C CA  . SER A 1 246 ? 22.168  6.403   -0.891  1.00 29.75  ? 275 SER A CA  1 
ATOM   1936 C C   . SER A 1 246 ? 23.082  7.415   -0.216  1.00 29.32  ? 275 SER A C   1 
ATOM   1937 O O   . SER A 1 246 ? 23.925  7.049   0.604   1.00 31.61  ? 275 SER A O   1 
ATOM   1938 C CB  . SER A 1 246 ? 22.750  5.991   -2.213  1.00 31.79  ? 275 SER A CB  1 
ATOM   1939 O OG  . SER A 1 246 ? 23.098  7.135   -2.982  1.00 36.84  ? 275 SER A OG  1 
ATOM   1940 N N   . HIS A 1 247 ? 22.924  8.685   -0.610  1.00 29.08  ? 276 HIS A N   1 
ATOM   1941 C CA  . HIS A 1 247 ? 23.721  9.769   -0.069  1.00 28.14  ? 276 HIS A CA  1 
ATOM   1942 C C   . HIS A 1 247 ? 23.463  9.822   1.427   1.00 25.79  ? 276 HIS A C   1 
ATOM   1943 O O   . HIS A 1 247 ? 24.381  9.719   2.224   1.00 26.51  ? 276 HIS A O   1 
ATOM   1944 C CB  . HIS A 1 247 ? 23.389  11.083  -0.788  1.00 29.61  ? 276 HIS A CB  1 
ATOM   1945 C CG  . HIS A 1 247 ? 24.314  12.198  -0.458  1.00 30.48  ? 276 HIS A CG  1 
ATOM   1946 N ND1 . HIS A 1 247 ? 25.595  12.275  -0.968  1.00 33.08  ? 276 HIS A ND1 1 
ATOM   1947 C CD2 . HIS A 1 247 ? 24.158  13.254  0.344   1.00 32.55  ? 276 HIS A CD2 1 
ATOM   1948 C CE1 . HIS A 1 247 ? 26.184  13.362  -0.494  1.00 34.86  ? 276 HIS A CE1 1 
ATOM   1949 N NE2 . HIS A 1 247 ? 25.328  13.973  0.309   1.00 36.66  ? 276 HIS A NE2 1 
ATOM   1950 N N   . LEU A 1 248 ? 22.178  9.923   1.761   1.00 26.54  ? 277 LEU A N   1 
ATOM   1951 C CA  . LEU A 1 248 ? 21.710  10.053  3.124   1.00 27.60  ? 277 LEU A CA  1 
ATOM   1952 C C   . LEU A 1 248 ? 22.156  8.850   3.951   1.00 27.68  ? 277 LEU A C   1 
ATOM   1953 O O   . LEU A 1 248 ? 22.769  9.005   5.004   1.00 24.46  ? 277 LEU A O   1 
ATOM   1954 C CB  . LEU A 1 248 ? 20.192  10.169  3.000   1.00 27.71  ? 277 LEU A CB  1 
ATOM   1955 C CG  . LEU A 1 248 ? 19.405  10.341  4.296   1.00 28.35  ? 277 LEU A CG  1 
ATOM   1956 C CD1 . LEU A 1 248 ? 19.973  11.440  5.145   1.00 31.38  ? 277 LEU A CD1 1 
ATOM   1957 C CD2 . LEU A 1 248 ? 17.962  10.639  3.976   1.00 28.96  ? 277 LEU A CD2 1 
ATOM   1958 N N   . VAL A 1 249 ? 21.871  7.644   3.444   1.00 29.20  ? 278 VAL A N   1 
ATOM   1959 C CA  . VAL A 1 249 ? 22.241  6.426   4.146   1.00 27.76  ? 278 VAL A CA  1 
ATOM   1960 C C   . VAL A 1 249 ? 23.761  6.313   4.206   1.00 27.57  ? 278 VAL A C   1 
ATOM   1961 O O   . VAL A 1 249 ? 24.301  5.863   5.215   1.00 25.86  ? 278 VAL A O   1 
ATOM   1962 C CB  . VAL A 1 249 ? 21.612  5.171   3.517   1.00 26.79  ? 278 VAL A CB  1 
ATOM   1963 C CG1 . VAL A 1 249 ? 22.176  3.892   4.127   1.00 28.47  ? 278 VAL A CG1 1 
ATOM   1964 C CG2 . VAL A 1 249 ? 20.094  5.194   3.640   1.00 26.31  ? 278 VAL A CG2 1 
ATOM   1965 N N   . GLY A 1 250 ? 24.439  6.716   3.124   1.00 25.90  ? 279 GLY A N   1 
ATOM   1966 C CA  . GLY A 1 250 ? 25.893  6.662   3.073   1.00 26.12  ? 279 GLY A CA  1 
ATOM   1967 C C   . GLY A 1 250 ? 26.549  7.570   4.111   1.00 25.81  ? 279 GLY A C   1 
ATOM   1968 O O   . GLY A 1 250 ? 27.627  7.267   4.599   1.00 27.57  ? 279 GLY A O   1 
ATOM   1969 N N   . SER A 1 251 ? 25.889  8.681   4.452   1.00 27.77  ? 280 SER A N   1 
ATOM   1970 C CA  . SER A 1 251 ? 26.459  9.690   5.330   1.00 28.58  ? 280 SER A CA  1 
ATOM   1971 C C   . SER A 1 251 ? 26.556  9.209   6.780   1.00 30.90  ? 280 SER A C   1 
ATOM   1972 O O   . SER A 1 251 ? 27.278  9.813   7.568   1.00 33.08  ? 280 SER A O   1 
ATOM   1973 C CB  . SER A 1 251 ? 25.674  10.966  5.239   1.00 29.49  ? 280 SER A CB  1 
ATOM   1974 O OG  . SER A 1 251 ? 24.458  10.891  5.976   1.00 28.80  ? 280 SER A OG  1 
ATOM   1975 N N   . ALA A 1 252 ? 25.822  8.141   7.133   1.00 33.45  ? 281 ALA A N   1 
ATOM   1976 C CA  . ALA A 1 252 ? 25.865  7.559   8.470   1.00 33.64  ? 281 ALA A CA  1 
ATOM   1977 C C   . ALA A 1 252 ? 26.985  6.528   8.573   1.00 30.25  ? 281 ALA A C   1 
ATOM   1978 O O   . ALA A 1 252 ? 27.190  5.941   9.631   1.00 30.68  ? 281 ALA A O   1 
ATOM   1979 C CB  . ALA A 1 252 ? 24.523  6.933   8.811   1.00 34.56  ? 281 ALA A CB  1 
ATOM   1980 N N   . LEU A 1 253 ? 27.707  6.342   7.466   1.00 30.03  ? 282 LEU A N   1 
ATOM   1981 C CA  . LEU A 1 253 ? 28.832  5.424   7.347   1.00 30.44  ? 282 LEU A CA  1 
ATOM   1982 C C   . LEU A 1 253 ? 28.322  3.985   7.260   1.00 31.46  ? 282 LEU A C   1 
ATOM   1983 O O   . LEU A 1 253 ? 29.040  3.050   7.602   1.00 31.52  ? 282 LEU A O   1 
ATOM   1984 C CB  . LEU A 1 253 ? 29.890  5.619   8.435   1.00 30.21  ? 282 LEU A CB  1 
ATOM   1985 C CG  . LEU A 1 253 ? 30.472  7.034   8.550   1.00 29.88  ? 282 LEU A CG  1 
ATOM   1986 C CD1 . LEU A 1 253 ? 31.661  7.069   9.507   1.00 31.34  ? 282 LEU A CD1 1 
ATOM   1987 C CD2 . LEU A 1 253 ? 30.888  7.596   7.206   1.00 29.70  ? 282 LEU A CD2 1 
ATOM   1988 N N   . SER A 1 254 ? 27.087  3.828   6.760   1.00 31.31  ? 283 SER A N   1 
ATOM   1989 C CA  . SER A 1 254 ? 26.589  2.547   6.297   1.00 32.01  ? 283 SER A CA  1 
ATOM   1990 C C   . SER A 1 254 ? 27.325  2.198   5.010   1.00 33.18  ? 283 SER A C   1 
ATOM   1991 O O   . SER A 1 254 ? 27.647  3.088   4.217   1.00 34.55  ? 283 SER A O   1 
ATOM   1992 C CB  . SER A 1 254 ? 25.092  2.575   6.080   1.00 32.17  ? 283 SER A CB  1 
ATOM   1993 O OG  . SER A 1 254 ? 24.401  2.989   7.255   1.00 34.60  ? 283 SER A OG  1 
ATOM   1994 N N   . ASP A 1 255 ? 27.562  0.904   4.791   1.00 32.87  ? 284 ASP A N   1 
ATOM   1995 C CA  . ASP A 1 255 ? 28.492  0.495   3.751   1.00 34.93  ? 284 ASP A CA  1 
ATOM   1996 C C   . ASP A 1 255 ? 27.803  0.658   2.392   1.00 34.72  ? 284 ASP A C   1 
ATOM   1997 O O   . ASP A 1 255 ? 26.618  0.989   2.329   1.00 33.21  ? 284 ASP A O   1 
ATOM   1998 C CB  . ASP A 1 255 ? 29.089  -0.860  4.100   1.00 34.80  ? 284 ASP A CB  1 
ATOM   1999 C CG  . ASP A 1 255 ? 28.166  -2.047  3.892   1.00 36.67  ? 284 ASP A CG  1 
ATOM   2000 O OD1 . ASP A 1 255 ? 27.622  -2.161  2.778   1.00 34.18  ? 284 ASP A OD1 1 
ATOM   2001 O OD2 . ASP A 1 255 ? 28.030  -2.863  4.833   1.00 41.98  ? 284 ASP A OD2 1 
ATOM   2002 N N   . PRO A 1 256 ? 28.528  0.517   1.259   1.00 34.09  ? 285 PRO A N   1 
ATOM   2003 C CA  . PRO A 1 256 ? 27.905  0.578   -0.071  1.00 32.55  ? 285 PRO A CA  1 
ATOM   2004 C C   . PRO A 1 256 ? 26.761  -0.396  -0.354  1.00 33.90  ? 285 PRO A C   1 
ATOM   2005 O O   . PRO A 1 256 ? 25.890  -0.122  -1.189  1.00 33.75  ? 285 PRO A O   1 
ATOM   2006 C CB  . PRO A 1 256 ? 29.106  0.331   -1.004  1.00 32.13  ? 285 PRO A CB  1 
ATOM   2007 C CG  . PRO A 1 256 ? 30.272  0.896   -0.231  1.00 33.09  ? 285 PRO A CG  1 
ATOM   2008 C CD  . PRO A 1 256 ? 30.000  0.428   1.195   1.00 34.94  ? 285 PRO A CD  1 
ATOM   2009 N N   . TYR A 1 257 ? 26.782  -1.557  0.312   1.00 32.32  ? 286 TYR A N   1 
ATOM   2010 C CA  . TYR A 1 257 ? 25.725  -2.535  0.131   1.00 29.99  ? 286 TYR A CA  1 
ATOM   2011 C C   . TYR A 1 257 ? 24.462  -2.024  0.820   1.00 27.59  ? 286 TYR A C   1 
ATOM   2012 O O   . TYR A 1 257 ? 23.375  -2.081  0.249   1.00 28.88  ? 286 TYR A O   1 
ATOM   2013 C CB  . TYR A 1 257 ? 26.121  -3.929  0.633   1.00 30.14  ? 286 TYR A CB  1 
ATOM   2014 C CG  . TYR A 1 257 ? 27.326  -4.557  -0.057  1.00 29.09  ? 286 TYR A CG  1 
ATOM   2015 C CD1 . TYR A 1 257 ? 27.190  -5.259  -1.250  1.00 29.11  ? 286 TYR A CD1 1 
ATOM   2016 C CD2 . TYR A 1 257 ? 28.597  -4.478  0.507   1.00 29.62  ? 286 TYR A CD2 1 
ATOM   2017 C CE1 . TYR A 1 257 ? 28.285  -5.841  -1.875  1.00 28.90  ? 286 TYR A CE1 1 
ATOM   2018 C CE2 . TYR A 1 257 ? 29.698  -5.063  -0.101  1.00 29.71  ? 286 TYR A CE2 1 
ATOM   2019 C CZ  . TYR A 1 257 ? 29.540  -5.747  -1.293  1.00 30.30  ? 286 TYR A CZ  1 
ATOM   2020 O OH  . TYR A 1 257 ? 30.641  -6.302  -1.877  1.00 33.47  ? 286 TYR A OH  1 
ATOM   2021 N N   . LEU A 1 258 ? 24.588  -1.534  2.054   1.00 25.39  ? 287 LEU A N   1 
ATOM   2022 C CA  . LEU A 1 258 ? 23.415  -1.016  2.742   1.00 26.37  ? 287 LEU A CA  1 
ATOM   2023 C C   . LEU A 1 258 ? 22.922  0.257   2.046   1.00 27.25  ? 287 LEU A C   1 
ATOM   2024 O O   . LEU A 1 258 ? 21.717  0.420   1.853   1.00 27.22  ? 287 LEU A O   1 
ATOM   2025 C CB  . LEU A 1 258 ? 23.685  -0.782  4.224   1.00 25.03  ? 287 LEU A CB  1 
ATOM   2026 C CG  . LEU A 1 258 ? 24.151  -1.996  5.034   1.00 25.05  ? 287 LEU A CG  1 
ATOM   2027 C CD1 . LEU A 1 258 ? 24.334  -1.637  6.505   1.00 23.52  ? 287 LEU A CD1 1 
ATOM   2028 C CD2 . LEU A 1 258 ? 23.223  -3.171  4.900   1.00 23.67  ? 287 LEU A CD2 1 
ATOM   2029 N N   . SER A 1 259 ? 23.841  1.144   1.644   1.00 28.18  ? 288 SER A N   1 
ATOM   2030 C CA  . SER A 1 259 ? 23.459  2.393   0.990   1.00 28.27  ? 288 SER A CA  1 
ATOM   2031 C C   . SER A 1 259 ? 22.695  2.136   -0.311  1.00 28.20  ? 288 SER A C   1 
ATOM   2032 O O   . SER A 1 259 ? 21.717  2.821   -0.610  1.00 26.90  ? 288 SER A O   1 
ATOM   2033 C CB  . SER A 1 259 ? 24.651  3.265   0.737   1.00 30.05  ? 288 SER A CB  1 
ATOM   2034 O OG  . SER A 1 259 ? 25.186  3.741   1.968   1.00 34.19  ? 288 SER A OG  1 
ATOM   2035 N N   . PHE A 1 260 ? 23.156  1.156   -1.091  1.00 27.72  ? 289 PHE A N   1 
ATOM   2036 C CA  . PHE A 1 260 ? 22.595  0.905   -2.409  1.00 27.20  ? 289 PHE A CA  1 
ATOM   2037 C C   . PHE A 1 260 ? 21.265  0.167   -2.278  1.00 26.93  ? 289 PHE A C   1 
ATOM   2038 O O   . PHE A 1 260 ? 20.331  0.444   -3.025  1.00 26.53  ? 289 PHE A O   1 
ATOM   2039 C CB  . PHE A 1 260 ? 23.592  0.128   -3.273  1.00 28.40  ? 289 PHE A CB  1 
ATOM   2040 C CG  . PHE A 1 260 ? 23.044  -0.174  -4.661  1.00 29.02  ? 289 PHE A CG  1 
ATOM   2041 C CD1 . PHE A 1 260 ? 22.851  0.844   -5.587  1.00 29.68  ? 289 PHE A CD1 1 
ATOM   2042 C CD2 . PHE A 1 260 ? 22.723  -1.470  -5.034  1.00 29.30  ? 289 PHE A CD2 1 
ATOM   2043 C CE1 . PHE A 1 260 ? 22.338  0.570   -6.844  1.00 29.44  ? 289 PHE A CE1 1 
ATOM   2044 C CE2 . PHE A 1 260 ? 22.210  -1.736  -6.293  1.00 29.39  ? 289 PHE A CE2 1 
ATOM   2045 C CZ  . PHE A 1 260 ? 22.021  -0.719  -7.190  1.00 29.76  ? 289 PHE A CZ  1 
ATOM   2046 N N   . ALA A 1 261 ? 21.188  -0.776  -1.327  1.00 26.37  ? 290 ALA A N   1 
ATOM   2047 C CA  . ALA A 1 261 ? 19.954  -1.493  -1.054  1.00 25.33  ? 290 ALA A CA  1 
ATOM   2048 C C   . ALA A 1 261 ? 18.858  -0.499  -0.694  1.00 25.02  ? 290 ALA A C   1 
ATOM   2049 O O   . ALA A 1 261 ? 17.732  -0.610  -1.189  1.00 24.89  ? 290 ALA A O   1 
ATOM   2050 C CB  . ALA A 1 261 ? 20.171  -2.499  0.057   1.00 26.58  ? 290 ALA A CB  1 
ATOM   2051 N N   . ALA A 1 262 ? 19.210  0.487   0.143   1.00 23.02  ? 291 ALA A N   1 
ATOM   2052 C CA  . ALA A 1 262 ? 18.259  1.519   0.534   1.00 23.91  ? 291 ALA A CA  1 
ATOM   2053 C C   . ALA A 1 262 ? 17.812  2.311   -0.693  1.00 24.93  ? 291 ALA A C   1 
ATOM   2054 O O   . ALA A 1 262 ? 16.612  2.471   -0.935  1.00 26.18  ? 291 ALA A O   1 
ATOM   2055 C CB  . ALA A 1 262 ? 18.863  2.403   1.594   1.00 23.65  ? 291 ALA A CB  1 
ATOM   2056 N N   . ALA A 1 263 ? 18.781  2.722   -1.518  1.00 25.80  ? 292 ALA A N   1 
ATOM   2057 C CA  . ALA A 1 263 ? 18.494  3.435   -2.751  1.00 24.15  ? 292 ALA A CA  1 
ATOM   2058 C C   . ALA A 1 263 ? 17.530  2.647   -3.642  1.00 24.47  ? 292 ALA A C   1 
ATOM   2059 O O   . ALA A 1 263 ? 16.728  3.249   -4.350  1.00 23.61  ? 292 ALA A O   1 
ATOM   2060 C CB  . ALA A 1 263 ? 19.783  3.747   -3.478  1.00 24.17  ? 292 ALA A CB  1 
ATOM   2061 N N   . MET A 1 264 ? 17.620  1.310   -3.622  1.00 26.98  ? 293 MET A N   1 
ATOM   2062 C CA  . MET A 1 264 ? 16.797  0.472   -4.486  1.00 27.73  ? 293 MET A CA  1 
ATOM   2063 C C   . MET A 1 264 ? 15.362  0.433   -3.968  1.00 28.99  ? 293 MET A C   1 
ATOM   2064 O O   . MET A 1 264 ? 14.430  0.386   -4.765  1.00 33.61  ? 293 MET A O   1 
ATOM   2065 C CB  . MET A 1 264 ? 17.334  -0.963  -4.595  1.00 27.20  ? 293 MET A CB  1 
ATOM   2066 C CG  . MET A 1 264 ? 18.572  -1.139  -5.453  1.00 28.03  ? 293 MET A CG  1 
ATOM   2067 S SD  . MET A 1 264 ? 18.482  -0.454  -7.122  1.00 28.89  ? 293 MET A SD  1 
ATOM   2068 C CE  . MET A 1 264 ? 18.907  1.274   -6.862  1.00 30.06  ? 293 MET A CE  1 
ATOM   2069 N N   . ASN A 1 265 ? 15.194  0.454   -2.641  1.00 30.39  ? 294 ASN A N   1 
ATOM   2070 C CA  . ASN A 1 265 ? 13.881  0.550   -2.020  1.00 31.96  ? 294 ASN A CA  1 
ATOM   2071 C C   . ASN A 1 265 ? 13.220  1.881   -2.371  1.00 33.34  ? 294 ASN A C   1 
ATOM   2072 O O   . ASN A 1 265 ? 12.001  1.950   -2.498  1.00 36.58  ? 294 ASN A O   1 
ATOM   2073 C CB  . ASN A 1 265 ? 13.954  0.355   -0.508  1.00 31.80  ? 294 ASN A CB  1 
ATOM   2074 C CG  . ASN A 1 265 ? 13.941  -1.098  -0.101  1.00 33.67  ? 294 ASN A CG  1 
ATOM   2075 O OD1 . ASN A 1 265 ? 13.793  -1.990  -0.941  1.00 38.09  ? 294 ASN A OD1 1 
ATOM   2076 N ND2 . ASN A 1 265 ? 14.072  -1.364  1.186   1.00 36.80  ? 294 ASN A ND2 1 
ATOM   2077 N N   . GLY A 1 266 ? 14.028  2.939   -2.498  1.00 34.10  ? 295 GLY A N   1 
ATOM   2078 C CA  . GLY A 1 266 ? 13.555  4.220   -2.996  1.00 32.20  ? 295 GLY A CA  1 
ATOM   2079 C C   . GLY A 1 266 ? 13.182  4.112   -4.469  1.00 32.39  ? 295 GLY A C   1 
ATOM   2080 O O   . GLY A 1 266 ? 12.148  4.629   -4.892  1.00 28.74  ? 295 GLY A O   1 
ATOM   2081 N N   . LEU A 1 267 ? 14.015  3.388   -5.228  1.00 31.71  ? 296 LEU A N   1 
ATOM   2082 C CA  . LEU A 1 267 ? 13.819  3.241   -6.661  1.00 32.51  ? 296 LEU A CA  1 
ATOM   2083 C C   . LEU A 1 267 ? 12.591  2.384   -6.972  1.00 34.43  ? 296 LEU A C   1 
ATOM   2084 O O   . LEU A 1 267 ? 12.006  2.519   -8.044  1.00 35.71  ? 296 LEU A O   1 
ATOM   2085 C CB  . LEU A 1 267 ? 15.077  2.661   -7.302  1.00 32.06  ? 296 LEU A CB  1 
ATOM   2086 C CG  . LEU A 1 267 ? 15.063  2.598   -8.830  1.00 33.11  ? 296 LEU A CG  1 
ATOM   2087 C CD1 . LEU A 1 267 ? 14.940  4.012   -9.383  1.00 33.60  ? 296 LEU A CD1 1 
ATOM   2088 C CD2 . LEU A 1 267 ? 16.293  1.889   -9.380  1.00 33.93  ? 296 LEU A CD2 1 
ATOM   2089 N N   . ALA A 1 268 ? 12.202  1.498   -6.049  1.00 36.13  ? 297 ALA A N   1 
ATOM   2090 C CA  . ALA A 1 268 ? 11.086  0.595   -6.287  1.00 39.09  ? 297 ALA A CA  1 
ATOM   2091 C C   . ALA A 1 268 ? 9.757   1.336   -6.139  1.00 39.79  ? 297 ALA A C   1 
ATOM   2092 O O   . ALA A 1 268 ? 8.708   0.804   -6.491  1.00 40.19  ? 297 ALA A O   1 
ATOM   2093 C CB  . ALA A 1 268 ? 11.170  -0.590  -5.347  1.00 40.83  ? 297 ALA A CB  1 
ATOM   2094 N N   . GLY A 1 269 ? 9.821   2.566   -5.616  1.00 42.89  ? 298 GLY A N   1 
ATOM   2095 C CA  . GLY A 1 269 ? 8.655   3.411   -5.433  1.00 41.73  ? 298 GLY A CA  1 
ATOM   2096 C C   . GLY A 1 269 ? 8.012   3.784   -6.765  1.00 42.27  ? 298 GLY A C   1 
ATOM   2097 O O   . GLY A 1 269 ? 8.695   4.238   -7.684  1.00 39.27  ? 298 GLY A O   1 
ATOM   2098 N N   . PRO A 1 270 ? 6.681   3.573   -6.898  1.00 40.34  ? 299 PRO A N   1 
ATOM   2099 C CA  . PRO A 1 270 ? 5.921   3.991   -8.077  1.00 40.58  ? 299 PRO A CA  1 
ATOM   2100 C C   . PRO A 1 270 ? 6.295   5.299   -8.764  1.00 39.81  ? 299 PRO A C   1 
ATOM   2101 O O   . PRO A 1 270 ? 6.347   5.353   -9.989  1.00 40.85  ? 299 PRO A O   1 
ATOM   2102 C CB  . PRO A 1 270 ? 4.520   4.081   -7.444  1.00 42.46  ? 299 PRO A CB  1 
ATOM   2103 C CG  . PRO A 1 270 ? 4.457   2.876   -6.538  1.00 39.97  ? 299 PRO A CG  1 
ATOM   2104 C CD  . PRO A 1 270 ? 5.844   2.850   -5.923  1.00 39.28  ? 299 PRO A CD  1 
ATOM   2105 N N   . LEU A 1 271 ? 6.511   6.349   -7.967  1.00 40.28  ? 300 LEU A N   1 
ATOM   2106 C CA  . LEU A 1 271 ? 6.756   7.684   -8.489  1.00 42.56  ? 300 LEU A CA  1 
ATOM   2107 C C   . LEU A 1 271 ? 8.209   7.858   -8.926  1.00 46.85  ? 300 LEU A C   1 
ATOM   2108 O O   . LEU A 1 271 ? 8.530   8.854   -9.568  1.00 48.04  ? 300 LEU A O   1 
ATOM   2109 C CB  . LEU A 1 271 ? 6.401   8.729   -7.432  1.00 42.23  ? 300 LEU A CB  1 
ATOM   2110 C CG  . LEU A 1 271 ? 4.939   8.773   -6.982  1.00 44.38  ? 300 LEU A CG  1 
ATOM   2111 C CD1 . LEU A 1 271 ? 4.733   10.006  -6.106  1.00 44.80  ? 300 LEU A CD1 1 
ATOM   2112 C CD2 . LEU A 1 271 ? 3.962   8.760   -8.153  1.00 43.78  ? 300 LEU A CD2 1 
ATOM   2113 N N   . HIS A 1 272 ? 9.092   6.925   -8.553  1.00 49.49  ? 301 HIS A N   1 
ATOM   2114 C CA  . HIS A 1 272 ? 10.495  7.052   -8.910  1.00 50.40  ? 301 HIS A CA  1 
ATOM   2115 C C   . HIS A 1 272 ? 10.841  6.163   -10.106 1.00 50.00  ? 301 HIS A C   1 
ATOM   2116 O O   . HIS A 1 272 ? 11.490  6.634   -11.030 1.00 48.02  ? 301 HIS A O   1 
ATOM   2117 C CB  . HIS A 1 272 ? 11.416  6.801   -7.708  1.00 49.81  ? 301 HIS A CB  1 
ATOM   2118 C CG  . HIS A 1 272 ? 12.861  6.986   -8.049  1.00 50.67  ? 301 HIS A CG  1 
ATOM   2119 N ND1 . HIS A 1 272 ? 13.264  7.560   -9.237  1.00 48.71  ? 301 HIS A ND1 1 
ATOM   2120 C CD2 . HIS A 1 272 ? 13.984  6.656   -7.401  1.00 49.11  ? 301 HIS A CD2 1 
ATOM   2121 C CE1 . HIS A 1 272 ? 14.586  7.589   -9.280  1.00 49.26  ? 301 HIS A CE1 1 
ATOM   2122 N NE2 . HIS A 1 272 ? 15.044  7.040   -8.181  1.00 46.30  ? 301 HIS A NE2 1 
ATOM   2123 N N   . GLY A 1 273 ? 10.442  4.883   -10.090 1.00 50.99  ? 302 GLY A N   1 
ATOM   2124 C CA  . GLY A 1 273 ? 10.972  3.944   -11.068 1.00 52.45  ? 302 GLY A CA  1 
ATOM   2125 C C   . GLY A 1 273 ? 9.951   2.921   -11.554 1.00 54.62  ? 302 GLY A C   1 
ATOM   2126 O O   . GLY A 1 273 ? 10.284  1.744   -11.678 1.00 57.70  ? 302 GLY A O   1 
ATOM   2127 N N   . LEU A 1 274 ? 8.724   3.381   -11.843 1.00 56.22  ? 303 LEU A N   1 
ATOM   2128 C CA  . LEU A 1 274 ? 7.709   2.553   -12.482 1.00 53.21  ? 303 LEU A CA  1 
ATOM   2129 C C   . LEU A 1 274 ? 7.192   3.205   -13.766 1.00 49.24  ? 303 LEU A C   1 
ATOM   2130 O O   . LEU A 1 274 ? 6.385   2.604   -14.470 1.00 47.03  ? 303 LEU A O   1 
ATOM   2131 C CB  . LEU A 1 274 ? 6.564   2.269   -11.510 1.00 55.51  ? 303 LEU A CB  1 
ATOM   2132 C CG  . LEU A 1 274 ? 6.709   1.017   -10.635 1.00 60.64  ? 303 LEU A CG  1 
ATOM   2133 C CD1 . LEU A 1 274 ? 7.746   1.158   -9.524  1.00 62.43  ? 303 LEU A CD1 1 
ATOM   2134 C CD2 . LEU A 1 274 ? 5.362   0.629   -10.052 1.00 62.65  ? 303 LEU A CD2 1 
ATOM   2135 N N   . ALA A 1 275 ? 7.676   4.410   -14.094 1.00 45.88  ? 304 ALA A N   1 
ATOM   2136 C CA  . ALA A 1 275 ? 7.104   5.205   -15.169 1.00 42.19  ? 304 ALA A CA  1 
ATOM   2137 C C   . ALA A 1 275 ? 7.301   4.523   -16.522 1.00 42.94  ? 304 ALA A C   1 
ATOM   2138 O O   . ALA A 1 275 ? 6.488   4.711   -17.425 1.00 44.17  ? 304 ALA A O   1 
ATOM   2139 C CB  . ALA A 1 275 ? 7.703   6.584   -15.148 1.00 42.48  ? 304 ALA A CB  1 
ATOM   2140 N N   . ASN A 1 276 ? 8.386   3.745   -16.643 1.00 42.11  ? 305 ASN A N   1 
ATOM   2141 C CA  . ASN A 1 276 ? 8.659   2.887   -17.793 1.00 43.13  ? 305 ASN A CA  1 
ATOM   2142 C C   . ASN A 1 276 ? 7.553   1.837   -17.941 1.00 45.02  ? 305 ASN A C   1 
ATOM   2143 O O   . ASN A 1 276 ? 7.073   1.584   -19.048 1.00 41.14  ? 305 ASN A O   1 
ATOM   2144 C CB  . ASN A 1 276 ? 10.050  2.270   -17.655 1.00 42.42  ? 305 ASN A CB  1 
ATOM   2145 C CG  . ASN A 1 276 ? 10.408  1.243   -18.707 1.00 44.76  ? 305 ASN A CG  1 
ATOM   2146 O OD1 . ASN A 1 276 ? 9.572   0.829   -19.523 1.00 45.28  ? 305 ASN A OD1 1 
ATOM   2147 N ND2 . ASN A 1 276 ? 11.658  0.804   -18.693 1.00 45.13  ? 305 ASN A ND2 1 
ATOM   2148 N N   . GLN A 1 277 ? 7.155   1.222   -16.820 1.00 47.49  ? 306 GLN A N   1 
ATOM   2149 C CA  . GLN A 1 277 ? 6.047   0.275   -16.809 1.00 48.47  ? 306 GLN A CA  1 
ATOM   2150 C C   . GLN A 1 277 ? 4.730   0.981   -17.125 1.00 46.33  ? 306 GLN A C   1 
ATOM   2151 O O   . GLN A 1 277 ? 3.943   0.474   -17.919 1.00 42.87  ? 306 GLN A O   1 
ATOM   2152 C CB  . GLN A 1 277 ? 5.923   -0.469  -15.477 1.00 48.54  ? 306 GLN A CB  1 
ATOM   2153 C CG  . GLN A 1 277 ? 7.028   -1.496  -15.251 1.00 48.99  ? 306 GLN A CG  1 
ATOM   2154 C CD  . GLN A 1 277 ? 8.278   -0.931  -14.606 1.00 49.27  ? 306 GLN A CD  1 
ATOM   2155 O OE1 . GLN A 1 277 ? 8.695   0.205   -14.872 1.00 45.36  ? 306 GLN A OE1 1 
ATOM   2156 N NE2 . GLN A 1 277 ? 8.893   -1.733  -13.745 1.00 48.60  ? 306 GLN A NE2 1 
ATOM   2157 N N   . GLU A 1 278 ? 4.510   2.141   -16.490 1.00 48.43  ? 307 GLU A N   1 
ATOM   2158 C CA  . GLU A 1 278 ? 3.280   2.910   -16.625 1.00 49.75  ? 307 GLU A CA  1 
ATOM   2159 C C   . GLU A 1 278 ? 3.077   3.357   -18.074 1.00 48.73  ? 307 GLU A C   1 
ATOM   2160 O O   . GLU A 1 278 ? 1.947   3.399   -18.562 1.00 45.11  ? 307 GLU A O   1 
ATOM   2161 C CB  . GLU A 1 278 ? 3.310   4.132   -15.700 1.00 53.63  ? 307 GLU A CB  1 
ATOM   2162 C CG  . GLU A 1 278 ? 3.224   3.778   -14.214 1.00 60.24  ? 307 GLU A CG  1 
ATOM   2163 C CD  . GLU A 1 278 ? 3.356   4.923   -13.211 1.00 62.25  ? 307 GLU A CD  1 
ATOM   2164 O OE1 . GLU A 1 278 ? 3.690   6.061   -13.618 1.00 64.12  ? 307 GLU A OE1 1 
ATOM   2165 O OE2 . GLU A 1 278 ? 3.117   4.671   -12.004 1.00 59.76  ? 307 GLU A OE2 1 
ATOM   2166 N N   . VAL A 1 279 ? 4.179   3.728   -18.740 1.00 45.58  ? 308 VAL A N   1 
ATOM   2167 C CA  . VAL A 1 279 ? 4.127   4.189   -20.116 1.00 45.02  ? 308 VAL A CA  1 
ATOM   2168 C C   . VAL A 1 279 ? 3.592   3.062   -20.998 1.00 44.17  ? 308 VAL A C   1 
ATOM   2169 O O   . VAL A 1 279 ? 2.676   3.279   -21.786 1.00 39.42  ? 308 VAL A O   1 
ATOM   2170 C CB  . VAL A 1 279 ? 5.509   4.689   -20.586 1.00 42.67  ? 308 VAL A CB  1 
ATOM   2171 C CG1 . VAL A 1 279 ? 5.703   4.566   -22.091 1.00 40.78  ? 308 VAL A CG1 1 
ATOM   2172 C CG2 . VAL A 1 279 ? 5.770   6.117   -20.132 1.00 41.94  ? 308 VAL A CG2 1 
ATOM   2173 N N   . LEU A 1 280 ? 4.154   1.860   -20.825 1.00 47.50  ? 309 LEU A N   1 
ATOM   2174 C CA  . LEU A 1 280 ? 3.927   0.751   -21.740 1.00 50.31  ? 309 LEU A CA  1 
ATOM   2175 C C   . LEU A 1 280 ? 2.537   0.144   -21.526 1.00 51.40  ? 309 LEU A C   1 
ATOM   2176 O O   . LEU A 1 280 ? 1.973   -0.423  -22.457 1.00 51.27  ? 309 LEU A O   1 
ATOM   2177 C CB  . LEU A 1 280 ? 5.058   -0.257  -21.542 1.00 49.30  ? 309 LEU A CB  1 
ATOM   2178 C CG  . LEU A 1 280 ? 5.282   -1.277  -22.665 1.00 53.61  ? 309 LEU A CG  1 
ATOM   2179 C CD1 . LEU A 1 280 ? 5.598   -0.678  -24.034 1.00 51.64  ? 309 LEU A CD1 1 
ATOM   2180 C CD2 . LEU A 1 280 ? 6.411   -2.191  -22.233 1.00 55.76  ? 309 LEU A CD2 1 
ATOM   2181 N N   . VAL A 1 281 ? 1.994   0.268   -20.302 1.00 49.47  ? 310 VAL A N   1 
ATOM   2182 C CA  . VAL A 1 281 ? 0.597   -0.039  -20.015 1.00 50.30  ? 310 VAL A CA  1 
ATOM   2183 C C   . VAL A 1 281 ? -0.302  0.910   -20.811 1.00 50.40  ? 310 VAL A C   1 
ATOM   2184 O O   . VAL A 1 281 ? -1.315  0.490   -21.369 1.00 50.95  ? 310 VAL A O   1 
ATOM   2185 C CB  . VAL A 1 281 ? 0.281   0.055   -18.503 1.00 48.05  ? 310 VAL A CB  1 
ATOM   2186 C CG1 . VAL A 1 281 ? -1.217  0.045   -18.203 1.00 46.84  ? 310 VAL A CG1 1 
ATOM   2187 C CG2 . VAL A 1 281 ? 0.973   -1.037  -17.700 1.00 47.24  ? 310 VAL A CG2 1 
ATOM   2188 N N   . TRP A 1 282 ? 0.076   2.194   -20.831 1.00 50.25  ? 311 TRP A N   1 
ATOM   2189 C CA  . TRP A 1 282 ? -0.735  3.253   -21.410 1.00 51.32  ? 311 TRP A CA  1 
ATOM   2190 C C   . TRP A 1 282 ? -0.548  3.336   -22.922 1.00 50.92  ? 311 TRP A C   1 
ATOM   2191 O O   . TRP A 1 282 ? -1.407  3.883   -23.606 1.00 52.58  ? 311 TRP A O   1 
ATOM   2192 C CB  . TRP A 1 282 ? -0.386  4.590   -20.747 1.00 54.30  ? 311 TRP A CB  1 
ATOM   2193 C CG  . TRP A 1 282 ? -1.151  5.775   -21.272 1.00 57.32  ? 311 TRP A CG  1 
ATOM   2194 C CD1 . TRP A 1 282 ? -2.381  6.194   -20.865 1.00 58.91  ? 311 TRP A CD1 1 
ATOM   2195 C CD2 . TRP A 1 282 ? -0.714  6.725   -22.270 1.00 62.01  ? 311 TRP A CD2 1 
ATOM   2196 N NE1 . TRP A 1 282 ? -2.747  7.325   -21.544 1.00 62.87  ? 311 TRP A NE1 1 
ATOM   2197 C CE2 . TRP A 1 282 ? -1.746  7.678   -22.409 1.00 62.17  ? 311 TRP A CE2 1 
ATOM   2198 C CE3 . TRP A 1 282 ? 0.437   6.864   -23.055 1.00 65.16  ? 311 TRP A CE3 1 
ATOM   2199 C CZ2 . TRP A 1 282 ? -1.658  8.748   -23.298 1.00 62.13  ? 311 TRP A CZ2 1 
ATOM   2200 C CZ3 . TRP A 1 282 ? 0.525   7.926   -23.930 1.00 63.35  ? 311 TRP A CZ3 1 
ATOM   2201 C CH2 . TRP A 1 282 ? -0.509  8.854   -24.048 1.00 61.90  ? 311 TRP A CH2 1 
ATOM   2202 N N   . LEU A 1 283 ? 0.580   2.824   -23.432 1.00 50.41  ? 312 LEU A N   1 
ATOM   2203 C CA  . LEU A 1 283 ? 0.797   2.716   -24.866 1.00 53.65  ? 312 LEU A CA  1 
ATOM   2204 C C   . LEU A 1 283 ? 0.021   1.525   -25.416 1.00 58.02  ? 312 LEU A C   1 
ATOM   2205 O O   . LEU A 1 283 ? -0.454  1.578   -26.548 1.00 64.22  ? 312 LEU A O   1 
ATOM   2206 C CB  . LEU A 1 283 ? 2.280   2.569   -25.204 1.00 56.30  ? 312 LEU A CB  1 
ATOM   2207 C CG  . LEU A 1 283 ? 3.148   3.821   -25.053 1.00 58.14  ? 312 LEU A CG  1 
ATOM   2208 C CD1 . LEU A 1 283 ? 4.601   3.481   -25.356 1.00 57.39  ? 312 LEU A CD1 1 
ATOM   2209 C CD2 . LEU A 1 283 ? 2.667   4.961   -25.933 1.00 58.40  ? 312 LEU A CD2 1 
ATOM   2210 N N   . THR A 1 284 ? -0.058  0.448   -24.622 1.00 61.07  ? 313 THR A N   1 
ATOM   2211 C CA  . THR A 1 284 ? -0.685  -0.791  -25.054 1.00 65.43  ? 313 THR A CA  1 
ATOM   2212 C C   . THR A 1 284 ? -2.178  -0.551  -25.277 1.00 71.65  ? 313 THR A C   1 
ATOM   2213 O O   . THR A 1 284 ? -2.686  -0.815  -26.367 1.00 70.28  ? 313 THR A O   1 
ATOM   2214 C CB  . THR A 1 284 ? -0.424  -1.900  -24.034 1.00 65.56  ? 313 THR A CB  1 
ATOM   2215 O OG1 . THR A 1 284 ? 0.985   -2.107  -24.016 1.00 63.24  ? 313 THR A OG1 1 
ATOM   2216 C CG2 . THR A 1 284 ? -1.078  -3.219  -24.406 1.00 65.05  ? 313 THR A CG2 1 
ATOM   2217 N N   . GLN A 1 285 ? -2.865  -0.029  -24.249 1.00 72.99  ? 314 GLN A N   1 
ATOM   2218 C CA  . GLN A 1 285 ? -4.301  0.196   -24.332 1.00 74.41  ? 314 GLN A CA  1 
ATOM   2219 C C   . GLN A 1 285 ? -4.601  1.168   -25.474 1.00 75.25  ? 314 GLN A C   1 
ATOM   2220 O O   . GLN A 1 285 ? -5.583  0.984   -26.188 1.00 76.58  ? 314 GLN A O   1 
ATOM   2221 C CB  . GLN A 1 285 ? -4.921  0.668   -23.013 1.00 75.07  ? 314 GLN A CB  1 
ATOM   2222 C CG  . GLN A 1 285 ? -4.699  2.143   -22.685 1.00 77.98  ? 314 GLN A CG  1 
ATOM   2223 C CD  . GLN A 1 285 ? -5.398  2.621   -21.428 1.00 83.96  ? 314 GLN A CD  1 
ATOM   2224 O OE1 . GLN A 1 285 ? -5.184  3.752   -20.975 1.00 85.19  ? 314 GLN A OE1 1 
ATOM   2225 N NE2 . GLN A 1 285 ? -6.242  1.783   -20.840 1.00 86.74  ? 314 GLN A NE2 1 
ATOM   2226 N N   . LEU A 1 286 ? -3.746  2.187   -25.647 1.00 78.40  ? 315 LEU A N   1 
ATOM   2227 C CA  . LEU A 1 286 ? -3.906  3.175   -26.706 1.00 79.35  ? 315 LEU A CA  1 
ATOM   2228 C C   . LEU A 1 286 ? -3.954  2.480   -28.068 1.00 81.22  ? 315 LEU A C   1 
ATOM   2229 O O   . LEU A 1 286 ? -4.615  2.968   -28.982 1.00 75.96  ? 315 LEU A O   1 
ATOM   2230 C CB  . LEU A 1 286 ? -2.781  4.209   -26.629 1.00 78.65  ? 315 LEU A CB  1 
ATOM   2231 C CG  . LEU A 1 286 ? -2.732  5.265   -27.740 1.00 81.45  ? 315 LEU A CG  1 
ATOM   2232 C CD1 . LEU A 1 286 ? -4.036  6.021   -27.905 1.00 82.81  ? 315 LEU A CD1 1 
ATOM   2233 C CD2 . LEU A 1 286 ? -1.608  6.245   -27.460 1.00 82.80  ? 315 LEU A CD2 1 
ATOM   2234 N N   . GLN A 1 287 ? -3.262  1.337   -28.189 1.00 82.16  ? 316 GLN A N   1 
ATOM   2235 C CA  . GLN A 1 287 ? -3.365  0.485   -29.365 1.00 81.18  ? 316 GLN A CA  1 
ATOM   2236 C C   . GLN A 1 287 ? -4.291  -0.702  -29.090 1.00 77.82  ? 316 GLN A C   1 
ATOM   2237 O O   . GLN A 1 287 ? -3.969  -1.844  -29.410 1.00 74.80  ? 316 GLN A O   1 
ATOM   2238 C CB  . GLN A 1 287 ? -1.963  0.069   -29.806 1.00 81.55  ? 316 GLN A CB  1 
ATOM   2239 C CG  . GLN A 1 287 ? -1.150  1.226   -30.376 1.00 82.47  ? 316 GLN A CG  1 
ATOM   2240 C CD  . GLN A 1 287 ? 0.285   0.874   -30.704 1.00 84.88  ? 316 GLN A CD  1 
ATOM   2241 O OE1 . GLN A 1 287 ? 1.054   1.717   -31.177 1.00 82.26  ? 316 GLN A OE1 1 
ATOM   2242 N NE2 . GLN A 1 287 ? 0.672   -0.370  -30.457 1.00 91.10  ? 316 GLN A NE2 1 
ATOM   2243 N N   . LYS A 1 288 ? -5.438  -0.413  -28.469 1.00 76.54  ? 317 LYS A N   1 
ATOM   2244 C CA  . LYS A 1 288 ? -6.598  -1.291  -28.495 1.00 76.41  ? 317 LYS A CA  1 
ATOM   2245 C C   . LYS A 1 288 ? -7.861  -0.435  -28.405 1.00 78.52  ? 317 LYS A C   1 
ATOM   2246 O O   . LYS A 1 288 ? -8.823  -0.678  -29.127 1.00 86.19  ? 317 LYS A O   1 
ATOM   2247 C CB  . LYS A 1 288 ? -6.560  -2.342  -27.379 1.00 75.33  ? 317 LYS A CB  1 
ATOM   2248 N N   . GLU A 1 289 ? -7.835  0.567   -27.517 1.00 80.26  ? 318 GLU A N   1 
ATOM   2249 C CA  . GLU A 1 289 ? -8.930  1.508   -27.336 1.00 81.59  ? 318 GLU A CA  1 
ATOM   2250 C C   . GLU A 1 289 ? -9.025  2.451   -28.535 1.00 86.51  ? 318 GLU A C   1 
ATOM   2251 O O   . GLU A 1 289 ? -10.051 3.096   -28.735 1.00 92.81  ? 318 GLU A O   1 
ATOM   2252 C CB  . GLU A 1 289 ? -8.723  2.292   -26.038 1.00 82.11  ? 318 GLU A CB  1 
ATOM   2253 C CG  . GLU A 1 289 ? -8.635  1.405   -24.798 1.00 84.77  ? 318 GLU A CG  1 
ATOM   2254 C CD  . GLU A 1 289 ? -8.338  2.121   -23.490 1.00 89.95  ? 318 GLU A CD  1 
ATOM   2255 O OE1 . GLU A 1 289 ? -8.143  3.358   -23.499 1.00 94.23  ? 318 GLU A OE1 1 
ATOM   2256 O OE2 . GLU A 1 289 ? -8.297  1.427   -22.451 1.00 84.73  ? 318 GLU A OE2 1 
ATOM   2257 N N   . VAL A 1 290 ? -7.931  2.555   -29.300 1.00 91.02  ? 319 VAL A N   1 
ATOM   2258 C CA  . VAL A 1 290 ? -7.930  3.191   -30.609 1.00 88.51  ? 319 VAL A CA  1 
ATOM   2259 C C   . VAL A 1 290 ? -7.178  2.250   -31.545 1.00 89.99  ? 319 VAL A C   1 
ATOM   2260 O O   . VAL A 1 290 ? -6.378  1.438   -31.084 1.00 93.59  ? 319 VAL A O   1 
ATOM   2261 C CB  . VAL A 1 290 ? -7.287  4.595   -30.604 1.00 87.96  ? 319 VAL A CB  1 
ATOM   2262 C CG1 . VAL A 1 290 ? -7.865  5.493   -31.690 1.00 87.71  ? 319 VAL A CG1 1 
ATOM   2263 C CG2 . VAL A 1 290 ? -7.415  5.283   -29.252 1.00 92.37  ? 319 VAL A CG2 1 
ATOM   2264 N N   . GLY A 1 291 ? -7.439  2.358   -32.852 1.00 93.61  ? 320 GLY A N   1 
ATOM   2265 C CA  . GLY A 1 291 ? -6.767  1.524   -33.837 1.00 93.65  ? 320 GLY A CA  1 
ATOM   2266 C C   . GLY A 1 291 ? -5.250  1.617   -33.694 1.00 93.36  ? 320 GLY A C   1 
ATOM   2267 O O   . GLY A 1 291 ? -4.742  2.588   -33.138 1.00 99.00  ? 320 GLY A O   1 
ATOM   2268 N N   . LYS A 1 292 ? -4.536  0.596   -34.186 1.00 92.64  ? 321 LYS A N   1 
ATOM   2269 C CA  . LYS A 1 292 ? -3.081  0.605   -34.185 1.00 95.73  ? 321 LYS A CA  1 
ATOM   2270 C C   . LYS A 1 292 ? -2.595  1.767   -35.050 1.00 102.06 ? 321 LYS A C   1 
ATOM   2271 O O   . LYS A 1 292 ? -1.782  2.576   -34.606 1.00 105.84 ? 321 LYS A O   1 
ATOM   2272 C CB  . LYS A 1 292 ? -2.502  -0.731  -34.669 1.00 92.21  ? 321 LYS A CB  1 
ATOM   2273 C CG  . LYS A 1 292 ? -0.983  -0.852  -34.568 1.00 90.50  ? 321 LYS A CG  1 
ATOM   2274 C CD  . LYS A 1 292 ? -0.428  -2.241  -34.867 1.00 91.26  ? 321 LYS A CD  1 
ATOM   2275 C CE  . LYS A 1 292 ? -0.451  -2.615  -36.320 1.00 91.71  ? 321 LYS A CE  1 
ATOM   2276 N NZ  . LYS A 1 292 ? 0.569   -1.913  -37.104 1.00 90.08  ? 321 LYS A NZ  1 
ATOM   2277 N N   . ASP A 1 293 ? -3.109  1.832   -36.285 1.00 104.63 ? 322 ASP A N   1 
ATOM   2278 C CA  . ASP A 1 293 ? -2.888  2.959   -37.180 1.00 101.70 ? 322 ASP A CA  1 
ATOM   2279 C C   . ASP A 1 293 ? -3.903  4.052   -36.853 1.00 96.94  ? 322 ASP A C   1 
ATOM   2280 O O   . ASP A 1 293 ? -5.106  3.845   -37.001 1.00 95.38  ? 322 ASP A O   1 
ATOM   2281 C CB  . ASP A 1 293 ? -2.965  2.531   -38.639 1.00 103.86 ? 322 ASP A CB  1 
ATOM   2282 C CG  . ASP A 1 293 ? -4.145  1.642   -39.008 1.00 105.17 ? 322 ASP A CG  1 
ATOM   2283 O OD1 . ASP A 1 293 ? -4.127  0.452   -38.624 1.00 104.96 ? 322 ASP A OD1 1 
ATOM   2284 O OD2 . ASP A 1 293 ? -5.081  2.147   -39.662 1.00 103.86 ? 322 ASP A OD2 1 
ATOM   2285 N N   . VAL A 1 294 ? -3.406  5.211   -36.404 1.00 92.09  ? 323 VAL A N   1 
ATOM   2286 C CA  . VAL A 1 294 ? -4.263  6.261   -35.877 1.00 92.16  ? 323 VAL A CA  1 
ATOM   2287 C C   . VAL A 1 294 ? -3.864  7.590   -36.513 1.00 89.82  ? 323 VAL A C   1 
ATOM   2288 O O   . VAL A 1 294 ? -2.684  7.839   -36.745 1.00 92.45  ? 323 VAL A O   1 
ATOM   2289 C CB  . VAL A 1 294 ? -4.174  6.323   -34.339 1.00 95.22  ? 323 VAL A CB  1 
ATOM   2290 C CG1 . VAL A 1 294 ? -2.873  6.960   -33.858 1.00 94.37  ? 323 VAL A CG1 1 
ATOM   2291 C CG2 . VAL A 1 294 ? -5.371  7.039   -33.724 1.00 96.59  ? 323 VAL A CG2 1 
ATOM   2292 N N   . SER A 1 295 ? -4.863  8.437   -36.785 1.00 86.17  ? 324 SER A N   1 
ATOM   2293 C CA  . SER A 1 295 ? -4.618  9.786   -37.269 1.00 81.17  ? 324 SER A CA  1 
ATOM   2294 C C   . SER A 1 295 ? -4.113  10.650  -36.116 1.00 76.13  ? 324 SER A C   1 
ATOM   2295 O O   . SER A 1 295 ? -4.336  10.329  -34.950 1.00 71.46  ? 324 SER A O   1 
ATOM   2296 C CB  . SER A 1 295 ? -5.855  10.380  -37.902 1.00 78.40  ? 324 SER A CB  1 
ATOM   2297 O OG  . SER A 1 295 ? -6.886  10.575  -36.943 1.00 75.49  ? 324 SER A OG  1 
ATOM   2298 N N   . ASP A 1 296 ? -3.449  11.758  -36.464 1.00 78.25  ? 325 ASP A N   1 
ATOM   2299 C CA  . ASP A 1 296 ? -2.846  12.641  -35.479 1.00 78.63  ? 325 ASP A CA  1 
ATOM   2300 C C   . ASP A 1 296 ? -3.902  13.574  -34.888 1.00 79.53  ? 325 ASP A C   1 
ATOM   2301 O O   . ASP A 1 296 ? -3.617  14.290  -33.931 1.00 81.02  ? 325 ASP A O   1 
ATOM   2302 C CB  . ASP A 1 296 ? -1.616  13.342  -36.041 1.00 78.76  ? 325 ASP A CB  1 
ATOM   2303 C CG  . ASP A 1 296 ? -0.336  12.512  -36.045 1.00 77.68  ? 325 ASP A CG  1 
ATOM   2304 O OD1 . ASP A 1 296 ? 0.066   12.033  -34.955 1.00 78.52  ? 325 ASP A OD1 1 
ATOM   2305 O OD2 . ASP A 1 296 ? 0.260   12.352  -37.132 1.00 71.72  ? 325 ASP A OD2 1 
ATOM   2306 N N   . GLU A 1 297 ? -5.120  13.556  -35.445 1.00 84.11  ? 326 GLU A N   1 
ATOM   2307 C CA  . GLU A 1 297 ? -6.249  14.219  -34.810 1.00 86.64  ? 326 GLU A CA  1 
ATOM   2308 C C   . GLU A 1 297 ? -6.867  13.272  -33.779 1.00 82.05  ? 326 GLU A C   1 
ATOM   2309 O O   . GLU A 1 297 ? -7.064  13.666  -32.632 1.00 86.09  ? 326 GLU A O   1 
ATOM   2310 C CB  . GLU A 1 297 ? -7.259  14.794  -35.810 1.00 91.31  ? 326 GLU A CB  1 
ATOM   2311 C CG  . GLU A 1 297 ? -7.830  13.797  -36.816 1.00 94.71  ? 326 GLU A CG  1 
ATOM   2312 C CD  . GLU A 1 297 ? -8.903  14.388  -37.715 1.00 94.33  ? 326 GLU A CD  1 
ATOM   2313 O OE1 . GLU A 1 297 ? -8.616  15.376  -38.425 1.00 88.30  ? 326 GLU A OE1 1 
ATOM   2314 O OE2 . GLU A 1 297 ? -10.033 13.857  -37.700 1.00 96.39  ? 326 GLU A OE2 1 
ATOM   2315 N N   . LYS A 1 298 ? -7.145  12.022  -34.178 1.00 74.04  ? 327 LYS A N   1 
ATOM   2316 C CA  . LYS A 1 298 ? -7.710  11.036  -33.270 1.00 72.31  ? 327 LYS A CA  1 
ATOM   2317 C C   . LYS A 1 298 ? -6.832  10.924  -32.028 1.00 69.45  ? 327 LYS A C   1 
ATOM   2318 O O   . LYS A 1 298 ? -7.332  10.943  -30.907 1.00 71.74  ? 327 LYS A O   1 
ATOM   2319 C CB  . LYS A 1 298 ? -7.823  9.646   -33.907 1.00 75.82  ? 327 LYS A CB  1 
ATOM   2320 C CG  . LYS A 1 298 ? -9.037  9.421   -34.799 1.00 80.24  ? 327 LYS A CG  1 
ATOM   2321 C CD  . LYS A 1 298 ? -8.979  8.121   -35.593 1.00 80.62  ? 327 LYS A CD  1 
ATOM   2322 C CE  . LYS A 1 298 ? -9.046  6.893   -34.740 1.00 80.52  ? 327 LYS A CE  1 
ATOM   2323 N NZ  . LYS A 1 298 ? -8.599  5.711   -35.483 1.00 80.76  ? 327 LYS A NZ  1 
ATOM   2324 N N   . LEU A 1 299 ? -5.520  10.810  -32.254 1.00 67.26  ? 328 LEU A N   1 
ATOM   2325 C CA  . LEU A 1 299 ? -4.554  10.706  -31.175 1.00 65.50  ? 328 LEU A CA  1 
ATOM   2326 C C   . LEU A 1 299 ? -4.634  11.951  -30.295 1.00 63.68  ? 328 LEU A C   1 
ATOM   2327 O O   . LEU A 1 299 ? -4.774  11.841  -29.080 1.00 60.84  ? 328 LEU A O   1 
ATOM   2328 C CB  . LEU A 1 299 ? -3.156  10.514  -31.761 1.00 67.27  ? 328 LEU A CB  1 
ATOM   2329 C CG  . LEU A 1 299 ? -2.041  10.206  -30.756 1.00 70.08  ? 328 LEU A CG  1 
ATOM   2330 C CD1 . LEU A 1 299 ? -2.348  8.963   -29.939 1.00 69.10  ? 328 LEU A CD1 1 
ATOM   2331 C CD2 . LEU A 1 299 ? -0.714  10.051  -31.482 1.00 70.31  ? 328 LEU A CD2 1 
ATOM   2332 N N   . ARG A 1 300 ? -4.565  13.125  -30.933 1.00 63.81  ? 329 ARG A N   1 
ATOM   2333 C CA  . ARG A 1 300 ? -4.608  14.406  -30.242 1.00 64.54  ? 329 ARG A CA  1 
ATOM   2334 C C   . ARG A 1 300 ? -5.826  14.483  -29.325 1.00 66.51  ? 329 ARG A C   1 
ATOM   2335 O O   . ARG A 1 300 ? -5.712  14.960  -28.195 1.00 67.44  ? 329 ARG A O   1 
ATOM   2336 C CB  . ARG A 1 300 ? -4.603  15.560  -31.255 1.00 64.00  ? 329 ARG A CB  1 
ATOM   2337 C CG  . ARG A 1 300 ? -4.849  16.927  -30.633 1.00 66.01  ? 329 ARG A CG  1 
ATOM   2338 C CD  . ARG A 1 300 ? -4.914  18.038  -31.662 1.00 67.26  ? 329 ARG A CD  1 
ATOM   2339 N NE  . ARG A 1 300 ? -3.585  18.493  -32.083 1.00 66.37  ? 329 ARG A NE  1 
ATOM   2340 C CZ  . ARG A 1 300 ? -3.114  18.477  -33.321 1.00 68.38  ? 329 ARG A CZ  1 
ATOM   2341 N NH1 . ARG A 1 300 ? -3.874  18.081  -34.327 1.00 69.59  ? 329 ARG A NH1 1 
ATOM   2342 N NH2 . ARG A 1 300 ? -1.872  18.864  -33.553 1.00 72.04  ? 329 ARG A NH2 1 
ATOM   2343 N N   . ASP A 1 301 ? -6.983  14.027  -29.827 1.00 71.68  ? 330 ASP A N   1 
ATOM   2344 C CA  . ASP A 1 301 ? -8.209  13.979  -29.043 1.00 74.20  ? 330 ASP A CA  1 
ATOM   2345 C C   . ASP A 1 301 ? -8.021  13.050  -27.844 1.00 71.45  ? 330 ASP A C   1 
ATOM   2346 O O   . ASP A 1 301 ? -8.338  13.420  -26.717 1.00 70.89  ? 330 ASP A O   1 
ATOM   2347 C CB  . ASP A 1 301 ? -9.408  13.523  -29.864 1.00 76.60  ? 330 ASP A CB  1 
ATOM   2348 C CG  . ASP A 1 301 ? -9.770  14.383  -31.068 1.00 79.72  ? 330 ASP A CG  1 
ATOM   2349 O OD1 . ASP A 1 301 ? -9.935  15.615  -30.890 1.00 80.95  ? 330 ASP A OD1 1 
ATOM   2350 O OD2 . ASP A 1 301 ? -9.904  13.808  -32.173 1.00 73.50  ? 330 ASP A OD2 1 
ATOM   2351 N N   . TYR A 1 302 ? -7.504  11.841  -28.099 1.00 72.43  ? 331 TYR A N   1 
ATOM   2352 C CA  . TYR A 1 302 ? -7.272  10.867  -27.043 1.00 74.86  ? 331 TYR A CA  1 
ATOM   2353 C C   . TYR A 1 302 ? -6.515  11.523  -25.891 1.00 70.65  ? 331 TYR A C   1 
ATOM   2354 O O   . TYR A 1 302 ? -6.830  11.285  -24.727 1.00 68.35  ? 331 TYR A O   1 
ATOM   2355 C CB  . TYR A 1 302 ? -6.496  9.642   -27.537 1.00 78.17  ? 331 TYR A CB  1 
ATOM   2356 C CG  . TYR A 1 302 ? -6.243  8.608   -26.447 1.00 84.21  ? 331 TYR A CG  1 
ATOM   2357 C CD1 . TYR A 1 302 ? -7.170  7.608   -26.175 1.00 86.67  ? 331 TYR A CD1 1 
ATOM   2358 C CD2 . TYR A 1 302 ? -5.086  8.645   -25.678 1.00 87.52  ? 331 TYR A CD2 1 
ATOM   2359 C CE1 . TYR A 1 302 ? -6.950  6.673   -25.176 1.00 89.48  ? 331 TYR A CE1 1 
ATOM   2360 C CE2 . TYR A 1 302 ? -4.854  7.714   -24.678 1.00 89.51  ? 331 TYR A CE2 1 
ATOM   2361 C CZ  . TYR A 1 302 ? -5.788  6.726   -24.425 1.00 90.88  ? 331 TYR A CZ  1 
ATOM   2362 O OH  . TYR A 1 302 ? -5.556  5.811   -23.439 1.00 99.27  ? 331 TYR A OH  1 
ATOM   2363 N N   . ILE A 1 303 ? -5.518  12.347  -26.232 1.00 68.68  ? 332 ILE A N   1 
ATOM   2364 C CA  . ILE A 1 303 ? -4.680  12.994  -25.236 1.00 67.77  ? 332 ILE A CA  1 
ATOM   2365 C C   . ILE A 1 303 ? -5.545  13.938  -24.403 1.00 68.45  ? 332 ILE A C   1 
ATOM   2366 O O   . ILE A 1 303 ? -5.435  13.951  -23.180 1.00 72.01  ? 332 ILE A O   1 
ATOM   2367 C CB  . ILE A 1 303 ? -3.483  13.724  -25.881 1.00 66.56  ? 332 ILE A CB  1 
ATOM   2368 C CG1 . ILE A 1 303 ? -2.686  12.833  -26.848 1.00 64.07  ? 332 ILE A CG1 1 
ATOM   2369 C CG2 . ILE A 1 303 ? -2.571  14.324  -24.810 1.00 66.29  ? 332 ILE A CG2 1 
ATOM   2370 C CD1 . ILE A 1 303 ? -2.170  11.539  -26.244 1.00 62.91  ? 332 ILE A CD1 1 
ATOM   2371 N N   . TRP A 1 304 ? -6.407  14.719  -25.065 1.00 65.69  ? 333 TRP A N   1 
ATOM   2372 C CA  . TRP A 1 304 ? -7.286  15.643  -24.363 1.00 63.45  ? 333 TRP A CA  1 
ATOM   2373 C C   . TRP A 1 304 ? -8.326  14.896  -23.531 1.00 63.20  ? 333 TRP A C   1 
ATOM   2374 O O   . TRP A 1 304 ? -8.667  15.348  -22.439 1.00 60.42  ? 333 TRP A O   1 
ATOM   2375 C CB  . TRP A 1 304 ? -7.950  16.629  -25.333 1.00 62.59  ? 333 TRP A CB  1 
ATOM   2376 C CG  . TRP A 1 304 ? -7.398  18.023  -25.209 1.00 64.78  ? 333 TRP A CG  1 
ATOM   2377 C CD1 . TRP A 1 304 ? -7.328  18.773  -24.072 1.00 63.17  ? 333 TRP A CD1 1 
ATOM   2378 C CD2 . TRP A 1 304 ? -6.792  18.813  -26.253 1.00 67.56  ? 333 TRP A CD2 1 
ATOM   2379 N NE1 . TRP A 1 304 ? -6.743  19.982  -24.337 1.00 64.71  ? 333 TRP A NE1 1 
ATOM   2380 C CE2 . TRP A 1 304 ? -6.399  20.035  -25.664 1.00 68.42  ? 333 TRP A CE2 1 
ATOM   2381 C CE3 . TRP A 1 304 ? -6.548  18.610  -27.616 1.00 70.15  ? 333 TRP A CE3 1 
ATOM   2382 C CZ2 . TRP A 1 304 ? -5.781  21.046  -26.398 1.00 68.80  ? 333 TRP A CZ2 1 
ATOM   2383 C CZ3 . TRP A 1 304 ? -5.934  19.611  -28.337 1.00 71.45  ? 333 TRP A CZ3 1 
ATOM   2384 C CH2 . TRP A 1 304 ? -5.556  20.811  -27.735 1.00 68.49  ? 333 TRP A CH2 1 
ATOM   2385 N N   . ASN A 1 305 ? -8.815  13.761  -24.048 1.00 62.84  ? 334 ASN A N   1 
ATOM   2386 C CA  . ASN A 1 305 ? -9.733  12.903  -23.311 1.00 62.23  ? 334 ASN A CA  1 
ATOM   2387 C C   . ASN A 1 305 ? -9.010  12.262  -22.128 1.00 66.18  ? 334 ASN A C   1 
ATOM   2388 O O   . ASN A 1 305 ? -9.646  11.900  -21.138 1.00 65.72  ? 334 ASN A O   1 
ATOM   2389 C CB  . ASN A 1 305 ? -10.366 11.838  -24.204 1.00 61.16  ? 334 ASN A CB  1 
ATOM   2390 C CG  . ASN A 1 305 ? -11.358 12.414  -25.189 1.00 61.58  ? 334 ASN A CG  1 
ATOM   2391 O OD1 . ASN A 1 305 ? -11.528 13.634  -25.266 1.00 68.68  ? 334 ASN A OD1 1 
ATOM   2392 N ND2 . ASN A 1 305 ? -12.021 11.562  -25.956 1.00 59.80  ? 334 ASN A ND2 1 
ATOM   2393 N N   . THR A 1 306 ? -7.684  12.104  -22.254 1.00 66.77  ? 335 THR A N   1 
ATOM   2394 C CA  . THR A 1 306 ? -6.843  11.623  -21.170 1.00 69.46  ? 335 THR A CA  1 
ATOM   2395 C C   . THR A 1 306 ? -6.774  12.677  -20.063 1.00 69.42  ? 335 THR A C   1 
ATOM   2396 O O   . THR A 1 306 ? -7.031  12.379  -18.896 1.00 62.83  ? 335 THR A O   1 
ATOM   2397 C CB  . THR A 1 306 ? -5.461  11.285  -21.731 1.00 72.46  ? 335 THR A CB  1 
ATOM   2398 O OG1 . THR A 1 306 ? -5.706  10.347  -22.775 1.00 73.77  ? 335 THR A OG1 1 
ATOM   2399 C CG2 . THR A 1 306 ? -4.524  10.692  -20.692 1.00 75.14  ? 335 THR A CG2 1 
ATOM   2400 N N   . LEU A 1 307 ? -6.435  13.915  -20.444 1.00 70.08  ? 336 LEU A N   1 
ATOM   2401 C CA  . LEU A 1 307 ? -6.187  14.988  -19.491 1.00 71.68  ? 336 LEU A CA  1 
ATOM   2402 C C   . LEU A 1 307 ? -7.448  15.300  -18.683 1.00 71.21  ? 336 LEU A C   1 
ATOM   2403 O O   . LEU A 1 307 ? -7.372  15.496  -17.472 1.00 65.19  ? 336 LEU A O   1 
ATOM   2404 C CB  . LEU A 1 307 ? -5.669  16.215  -20.244 1.00 72.11  ? 336 LEU A CB  1 
ATOM   2405 C CG  . LEU A 1 307 ? -4.287  16.080  -20.898 1.00 72.61  ? 336 LEU A CG  1 
ATOM   2406 C CD1 . LEU A 1 307 ? -3.979  17.268  -21.794 1.00 72.36  ? 336 LEU A CD1 1 
ATOM   2407 C CD2 . LEU A 1 307 ? -3.184  15.914  -19.868 1.00 72.70  ? 336 LEU A CD2 1 
ATOM   2408 N N   . ASN A 1 308 ? -8.604  15.336  -19.362 1.00 71.61  ? 337 ASN A N   1 
ATOM   2409 C CA  . ASN A 1 308 ? -9.875  15.669  -18.737 1.00 67.64  ? 337 ASN A CA  1 
ATOM   2410 C C   . ASN A 1 308 ? -10.271 14.600  -17.717 1.00 67.49  ? 337 ASN A C   1 
ATOM   2411 O O   . ASN A 1 308 ? -10.828 14.928  -16.672 1.00 71.97  ? 337 ASN A O   1 
ATOM   2412 C CB  . ASN A 1 308 ? -10.960 15.901  -19.787 1.00 69.19  ? 337 ASN A CB  1 
ATOM   2413 C CG  . ASN A 1 308 ? -10.879 17.277  -20.410 1.00 68.22  ? 337 ASN A CG  1 
ATOM   2414 O OD1 . ASN A 1 308 ? -11.209 18.273  -19.757 1.00 71.32  ? 337 ASN A OD1 1 
ATOM   2415 N ND2 . ASN A 1 308 ? -10.462 17.364  -21.664 1.00 66.69  ? 337 ASN A ND2 1 
ATOM   2416 N N   . SER A 1 309 ? -9.953  13.329  -18.003 1.00 63.77  ? 338 SER A N   1 
ATOM   2417 C CA  . SER A 1 309 ? -10.377 12.206  -17.176 1.00 61.97  ? 338 SER A CA  1 
ATOM   2418 C C   . SER A 1 309 ? -9.662  12.173  -15.822 1.00 68.21  ? 338 SER A C   1 
ATOM   2419 O O   . SER A 1 309 ? -9.952  11.304  -15.000 1.00 64.50  ? 338 SER A O   1 
ATOM   2420 C CB  . SER A 1 309 ? -10.171 10.897  -17.899 1.00 60.18  ? 338 SER A CB  1 
ATOM   2421 O OG  . SER A 1 309 ? -10.933 10.829  -19.095 1.00 55.74  ? 338 SER A OG  1 
ATOM   2422 N N   . GLY A 1 310 ? -8.713  13.095  -15.598 1.00 71.33  ? 339 GLY A N   1 
ATOM   2423 C CA  . GLY A 1 310 ? -8.005  13.189  -14.329 1.00 71.30  ? 339 GLY A CA  1 
ATOM   2424 C C   . GLY A 1 310 ? -6.785  12.268  -14.276 1.00 70.13  ? 339 GLY A C   1 
ATOM   2425 O O   . GLY A 1 310 ? -6.259  12.002  -13.195 1.00 71.35  ? 339 GLY A O   1 
ATOM   2426 N N   . ARG A 1 311 ? -6.342  11.797  -15.451 1.00 66.14  ? 340 ARG A N   1 
ATOM   2427 C CA  . ARG A 1 311 ? -5.184  10.924  -15.566 1.00 64.47  ? 340 ARG A CA  1 
ATOM   2428 C C   . ARG A 1 311 ? -4.073  11.675  -16.297 1.00 61.21  ? 340 ARG A C   1 
ATOM   2429 O O   . ARG A 1 311 ? -4.330  12.584  -17.083 1.00 60.43  ? 340 ARG A O   1 
ATOM   2430 C CB  . ARG A 1 311 ? -5.533  9.572   -16.208 1.00 67.16  ? 340 ARG A CB  1 
ATOM   2431 C CG  . ARG A 1 311 ? -6.896  9.478   -16.880 1.00 68.83  ? 340 ARG A CG  1 
ATOM   2432 C CD  . ARG A 1 311 ? -7.152  8.137   -17.556 1.00 71.85  ? 340 ARG A CD  1 
ATOM   2433 N NE  . ARG A 1 311 ? -6.865  8.161   -18.998 1.00 75.44  ? 340 ARG A NE  1 
ATOM   2434 C CZ  . ARG A 1 311 ? -6.139  7.288   -19.701 1.00 75.00  ? 340 ARG A CZ  1 
ATOM   2435 N NH1 . ARG A 1 311 ? -6.068  7.406   -21.018 1.00 72.87  ? 340 ARG A NH1 1 
ATOM   2436 N NH2 . ARG A 1 311 ? -5.507  6.287   -19.108 1.00 76.78  ? 340 ARG A NH2 1 
ATOM   2437 N N   . VAL A 1 312 ? -2.832  11.293  -15.989 1.00 60.68  ? 341 VAL A N   1 
ATOM   2438 C CA  . VAL A 1 312 ? -1.648  11.967  -16.490 1.00 60.61  ? 341 VAL A CA  1 
ATOM   2439 C C   . VAL A 1 312 ? -1.155  11.209  -17.717 1.00 59.18  ? 341 VAL A C   1 
ATOM   2440 O O   . VAL A 1 312 ? -1.422  10.018  -17.850 1.00 58.46  ? 341 VAL A O   1 
ATOM   2441 C CB  . VAL A 1 312 ? -0.578  12.025  -15.381 1.00 62.83  ? 341 VAL A CB  1 
ATOM   2442 C CG1 . VAL A 1 312 ? -0.002  10.649  -15.054 1.00 61.88  ? 341 VAL A CG1 1 
ATOM   2443 C CG2 . VAL A 1 312 ? 0.539   13.003  -15.715 1.00 64.13  ? 341 VAL A CG2 1 
ATOM   2444 N N   . VAL A 1 313 ? -0.448  11.912  -18.609 1.00 59.37  ? 342 VAL A N   1 
ATOM   2445 C CA  . VAL A 1 313 ? 0.205   11.272  -19.740 1.00 59.86  ? 342 VAL A CA  1 
ATOM   2446 C C   . VAL A 1 313 ? 1.569   10.783  -19.262 1.00 57.51  ? 342 VAL A C   1 
ATOM   2447 O O   . VAL A 1 313 ? 2.452   11.599  -19.012 1.00 55.79  ? 342 VAL A O   1 
ATOM   2448 C CB  . VAL A 1 313 ? 0.369   12.193  -20.964 1.00 60.13  ? 342 VAL A CB  1 
ATOM   2449 C CG1 . VAL A 1 313 ? 0.932   11.436  -22.163 1.00 61.69  ? 342 VAL A CG1 1 
ATOM   2450 C CG2 . VAL A 1 313 ? -0.937  12.879  -21.340 1.00 62.58  ? 342 VAL A CG2 1 
ATOM   2451 N N   . PRO A 1 314 ? 1.793   9.456   -19.128 1.00 54.25  ? 343 PRO A N   1 
ATOM   2452 C CA  . PRO A 1 314 ? 3.061   8.947   -18.609 1.00 54.81  ? 343 PRO A CA  1 
ATOM   2453 C C   . PRO A 1 314 ? 4.162   9.120   -19.652 1.00 50.92  ? 343 PRO A C   1 
ATOM   2454 O O   . PRO A 1 314 ? 3.897   9.037   -20.850 1.00 51.41  ? 343 PRO A O   1 
ATOM   2455 C CB  . PRO A 1 314 ? 2.743   7.473   -18.295 1.00 56.06  ? 343 PRO A CB  1 
ATOM   2456 C CG  . PRO A 1 314 ? 1.684   7.107   -19.314 1.00 57.46  ? 343 PRO A CG  1 
ATOM   2457 C CD  . PRO A 1 314 ? 0.864   8.377   -19.500 1.00 57.60  ? 343 PRO A CD  1 
ATOM   2458 N N   . GLY A 1 315 ? 5.385   9.392   -19.178 1.00 47.05  ? 344 GLY A N   1 
ATOM   2459 C CA  . GLY A 1 315 ? 6.534   9.599   -20.044 1.00 44.57  ? 344 GLY A CA  1 
ATOM   2460 C C   . GLY A 1 315 ? 6.847   11.079  -20.264 1.00 43.12  ? 344 GLY A C   1 
ATOM   2461 O O   . GLY A 1 315 ? 7.912   11.403  -20.787 1.00 42.18  ? 344 GLY A O   1 
ATOM   2462 N N   . TYR A 1 316 ? 5.935   11.973  -19.852 1.00 42.07  ? 345 TYR A N   1 
ATOM   2463 C CA  . TYR A 1 316 ? 6.067   13.400  -20.119 1.00 40.45  ? 345 TYR A CA  1 
ATOM   2464 C C   . TYR A 1 316 ? 6.119   14.165  -18.795 1.00 41.54  ? 345 TYR A C   1 
ATOM   2465 O O   . TYR A 1 316 ? 5.405   13.829  -17.853 1.00 44.66  ? 345 TYR A O   1 
ATOM   2466 C CB  . TYR A 1 316 ? 4.925   13.799  -21.063 1.00 39.80  ? 345 TYR A CB  1 
ATOM   2467 C CG  . TYR A 1 316 ? 5.093   13.279  -22.488 1.00 38.22  ? 345 TYR A CG  1 
ATOM   2468 C CD1 . TYR A 1 316 ? 4.905   11.936  -22.783 1.00 39.18  ? 345 TYR A CD1 1 
ATOM   2469 C CD2 . TYR A 1 316 ? 5.444   14.126  -23.536 1.00 38.23  ? 345 TYR A CD2 1 
ATOM   2470 C CE1 . TYR A 1 316 ? 5.060   11.449  -24.070 1.00 41.19  ? 345 TYR A CE1 1 
ATOM   2471 C CE2 . TYR A 1 316 ? 5.612   13.652  -24.828 1.00 40.09  ? 345 TYR A CE2 1 
ATOM   2472 C CZ  . TYR A 1 316 ? 5.413   12.307  -25.096 1.00 43.69  ? 345 TYR A CZ  1 
ATOM   2473 O OH  . TYR A 1 316 ? 5.572   11.784  -26.349 1.00 50.13  ? 345 TYR A OH  1 
ATOM   2474 N N   . GLY A 1 317 ? 6.994   15.180  -18.729 1.00 41.82  ? 346 GLY A N   1 
ATOM   2475 C CA  . GLY A 1 317 ? 7.172   15.989  -17.530 1.00 40.49  ? 346 GLY A CA  1 
ATOM   2476 C C   . GLY A 1 317 ? 8.322   15.482  -16.660 1.00 39.10  ? 346 GLY A C   1 
ATOM   2477 O O   . GLY A 1 317 ? 8.840   14.392  -16.888 1.00 36.40  ? 346 GLY A O   1 
ATOM   2478 N N   . HIS A 1 318 ? 8.714   16.297  -15.668 1.00 40.40  ? 347 HIS A N   1 
ATOM   2479 C CA  . HIS A 1 318 ? 9.797   15.972  -14.747 1.00 41.79  ? 347 HIS A CA  1 
ATOM   2480 C C   . HIS A 1 318 ? 9.842   16.995  -13.610 1.00 42.59  ? 347 HIS A C   1 
ATOM   2481 O O   . HIS A 1 318 ? 9.311   18.094  -13.750 1.00 42.64  ? 347 HIS A O   1 
ATOM   2482 C CB  . HIS A 1 318 ? 11.151  15.966  -15.469 1.00 41.56  ? 347 HIS A CB  1 
ATOM   2483 C CG  . HIS A 1 318 ? 12.274  15.319  -14.710 1.00 41.80  ? 347 HIS A CG  1 
ATOM   2484 N ND1 . HIS A 1 318 ? 12.504  13.961  -14.758 1.00 42.24  ? 347 HIS A ND1 1 
ATOM   2485 C CD2 . HIS A 1 318 ? 13.225  15.815  -13.909 1.00 39.16  ? 347 HIS A CD2 1 
ATOM   2486 C CE1 . HIS A 1 318 ? 13.554  13.672  -14.007 1.00 40.13  ? 347 HIS A CE1 1 
ATOM   2487 N NE2 . HIS A 1 318 ? 14.007  14.780  -13.484 1.00 40.75  ? 347 HIS A NE2 1 
ATOM   2488 N N   . ALA A 1 319 ? 10.525  16.633  -12.513 1.00 44.69  ? 348 ALA A N   1 
ATOM   2489 C CA  . ALA A 1 319 ? 10.631  17.456  -11.313 1.00 44.49  ? 348 ALA A CA  1 
ATOM   2490 C C   . ALA A 1 319 ? 11.533  18.681  -11.499 1.00 44.72  ? 348 ALA A C   1 
ATOM   2491 O O   . ALA A 1 319 ? 11.367  19.660  -10.777 1.00 44.31  ? 348 ALA A O   1 
ATOM   2492 C CB  . ALA A 1 319 ? 11.126  16.611  -10.159 1.00 42.42  ? 348 ALA A CB  1 
ATOM   2493 N N   . VAL A 1 320 ? 12.509  18.630  -12.417 1.00 47.19  ? 349 VAL A N   1 
ATOM   2494 C CA  . VAL A 1 320 ? 13.358  19.792  -12.666 1.00 49.55  ? 349 VAL A CA  1 
ATOM   2495 C C   . VAL A 1 320 ? 13.657  19.981  -14.157 1.00 47.43  ? 349 VAL A C   1 
ATOM   2496 O O   . VAL A 1 320 ? 13.882  21.109  -14.577 1.00 47.95  ? 349 VAL A O   1 
ATOM   2497 C CB  . VAL A 1 320 ? 14.658  19.792  -11.833 1.00 55.93  ? 349 VAL A CB  1 
ATOM   2498 C CG1 . VAL A 1 320 ? 15.604  18.666  -12.220 1.00 55.35  ? 349 VAL A CG1 1 
ATOM   2499 C CG2 . VAL A 1 320 ? 15.379  21.138  -11.899 1.00 60.16  ? 349 VAL A CG2 1 
ATOM   2500 N N   . LEU A 1 321 ? 13.693  18.916  -14.966 1.00 46.39  ? 350 LEU A N   1 
ATOM   2501 C CA  . LEU A 1 321 ? 13.814  19.089  -16.408 1.00 47.90  ? 350 LEU A CA  1 
ATOM   2502 C C   . LEU A 1 321 ? 12.702  20.017  -16.895 1.00 49.59  ? 350 LEU A C   1 
ATOM   2503 O O   . LEU A 1 321 ? 11.583  19.949  -16.393 1.00 50.93  ? 350 LEU A O   1 
ATOM   2504 C CB  . LEU A 1 321 ? 13.758  17.759  -17.156 1.00 45.47  ? 350 LEU A CB  1 
ATOM   2505 C CG  . LEU A 1 321 ? 15.060  16.963  -17.237 1.00 45.84  ? 350 LEU A CG  1 
ATOM   2506 C CD1 . LEU A 1 321 ? 14.770  15.547  -17.709 1.00 46.94  ? 350 LEU A CD1 1 
ATOM   2507 C CD2 . LEU A 1 321 ? 16.040  17.646  -18.169 1.00 46.33  ? 350 LEU A CD2 1 
ATOM   2508 N N   . ARG A 1 322 ? 13.030  20.867  -17.880 1.00 50.12  ? 351 ARG A N   1 
ATOM   2509 C CA  . ARG A 1 322 ? 12.068  21.757  -18.516 1.00 52.13  ? 351 ARG A CA  1 
ATOM   2510 C C   . ARG A 1 322 ? 12.246  21.741  -20.039 1.00 54.22  ? 351 ARG A C   1 
ATOM   2511 O O   . ARG A 1 322 ? 11.951  22.730  -20.707 1.00 56.59  ? 351 ARG A O   1 
ATOM   2512 C CB  . ARG A 1 322 ? 12.231  23.179  -17.960 1.00 52.94  ? 351 ARG A CB  1 
ATOM   2513 C CG  . ARG A 1 322 ? 12.137  23.329  -16.446 1.00 52.75  ? 351 ARG A CG  1 
ATOM   2514 C CD  . ARG A 1 322 ? 10.736  23.060  -15.908 1.00 53.86  ? 351 ARG A CD  1 
ATOM   2515 N NE  . ARG A 1 322 ? 10.685  23.077  -14.441 1.00 56.59  ? 351 ARG A NE  1 
ATOM   2516 C CZ  . ARG A 1 322 ? 10.504  22.028  -13.636 1.00 58.08  ? 351 ARG A CZ  1 
ATOM   2517 N NH1 . ARG A 1 322 ? 10.573  22.198  -12.326 1.00 58.64  ? 351 ARG A NH1 1 
ATOM   2518 N NH2 . ARG A 1 322 ? 10.294  20.811  -14.123 1.00 56.39  ? 351 ARG A NH2 1 
ATOM   2519 N N   . LYS A 1 323 ? 12.706  20.607  -20.589 1.00 52.51  ? 352 LYS A N   1 
ATOM   2520 C CA  . LYS A 1 323 ? 12.891  20.440  -22.026 1.00 52.36  ? 352 LYS A CA  1 
ATOM   2521 C C   . LYS A 1 323 ? 13.011  18.941  -22.308 1.00 45.43  ? 352 LYS A C   1 
ATOM   2522 O O   . LYS A 1 323 ? 13.119  18.158  -21.371 1.00 46.36  ? 352 LYS A O   1 
ATOM   2523 C CB  . LYS A 1 323 ? 14.101  21.275  -22.479 1.00 54.93  ? 352 LYS A CB  1 
ATOM   2524 C CG  . LYS A 1 323 ? 14.324  21.360  -23.981 1.00 58.87  ? 352 LYS A CG  1 
ATOM   2525 C CD  . LYS A 1 323 ? 15.421  22.317  -24.431 1.00 62.11  ? 352 LYS A CD  1 
ATOM   2526 C CE  . LYS A 1 323 ? 15.039  23.758  -24.283 1.00 63.97  ? 352 LYS A CE  1 
ATOM   2527 N NZ  . LYS A 1 323 ? 16.086  24.633  -24.813 1.00 61.81  ? 352 LYS A NZ  1 
ATOM   2528 N N   . THR A 1 324 ? 12.960  18.535  -23.584 1.00 43.79  ? 353 THR A N   1 
ATOM   2529 C CA  . THR A 1 324 ? 13.176  17.140  -23.950 1.00 42.33  ? 353 THR A CA  1 
ATOM   2530 C C   . THR A 1 324 ? 14.407  16.625  -23.206 1.00 41.84  ? 353 THR A C   1 
ATOM   2531 O O   . THR A 1 324 ? 15.479  17.223  -23.280 1.00 42.40  ? 353 THR A O   1 
ATOM   2532 C CB  . THR A 1 324 ? 13.339  16.972  -25.464 1.00 43.06  ? 353 THR A CB  1 
ATOM   2533 O OG1 . THR A 1 324 ? 12.144  17.377  -26.121 1.00 41.76  ? 353 THR A OG1 1 
ATOM   2534 C CG2 . THR A 1 324 ? 13.589  15.531  -25.880 1.00 42.89  ? 353 THR A CG2 1 
ATOM   2535 N N   . ASP A 1 325 ? 14.226  15.526  -22.465 1.00 42.76  ? 354 ASP A N   1 
ATOM   2536 C CA  . ASP A 1 325 ? 15.304  14.854  -21.753 1.00 40.32  ? 354 ASP A CA  1 
ATOM   2537 C C   . ASP A 1 325 ? 16.277  14.276  -22.781 1.00 37.26  ? 354 ASP A C   1 
ATOM   2538 O O   . ASP A 1 325 ? 15.830  13.607  -23.710 1.00 37.54  ? 354 ASP A O   1 
ATOM   2539 C CB  . ASP A 1 325 ? 14.724  13.759  -20.868 1.00 40.36  ? 354 ASP A CB  1 
ATOM   2540 C CG  . ASP A 1 325 ? 15.678  13.005  -19.950 1.00 41.18  ? 354 ASP A CG  1 
ATOM   2541 O OD1 . ASP A 1 325 ? 16.886  13.324  -19.928 1.00 37.97  ? 354 ASP A OD1 1 
ATOM   2542 O OD2 . ASP A 1 325 ? 15.192  12.089  -19.257 1.00 43.47  ? 354 ASP A OD2 1 
ATOM   2543 N N   . PRO A 1 326 ? 17.609  14.527  -22.672 1.00 34.10  ? 355 PRO A N   1 
ATOM   2544 C CA  . PRO A 1 326 ? 18.589  13.938  -23.591 1.00 32.35  ? 355 PRO A CA  1 
ATOM   2545 C C   . PRO A 1 326 ? 18.580  12.409  -23.633 1.00 33.58  ? 355 PRO A C   1 
ATOM   2546 O O   . PRO A 1 326 ? 18.938  11.812  -24.649 1.00 32.78  ? 355 PRO A O   1 
ATOM   2547 C CB  . PRO A 1 326 ? 19.965  14.481  -23.140 1.00 33.75  ? 355 PRO A CB  1 
ATOM   2548 C CG  . PRO A 1 326 ? 19.719  15.217  -21.834 1.00 34.69  ? 355 PRO A CG  1 
ATOM   2549 C CD  . PRO A 1 326 ? 18.226  15.464  -21.720 1.00 34.89  ? 355 PRO A CD  1 
ATOM   2550 N N   . ARG A 1 327 ? 18.173  11.780  -22.525 1.00 32.77  ? 356 ARG A N   1 
ATOM   2551 C CA  . ARG A 1 327 ? 18.092  10.329  -22.443 1.00 33.01  ? 356 ARG A CA  1 
ATOM   2552 C C   . ARG A 1 327 ? 16.950  9.810   -23.320 1.00 34.17  ? 356 ARG A C   1 
ATOM   2553 O O   . ARG A 1 327 ? 17.030  8.699   -23.841 1.00 33.60  ? 356 ARG A O   1 
ATOM   2554 C CB  . ARG A 1 327 ? 17.956  9.901   -20.977 1.00 32.66  ? 356 ARG A CB  1 
ATOM   2555 C CG  . ARG A 1 327 ? 19.124  10.303  -20.083 1.00 32.19  ? 356 ARG A CG  1 
ATOM   2556 C CD  . ARG A 1 327 ? 18.871  9.987   -18.611 1.00 32.55  ? 356 ARG A CD  1 
ATOM   2557 N NE  . ARG A 1 327 ? 17.657  10.660  -18.143 1.00 32.77  ? 356 ARG A NE  1 
ATOM   2558 C CZ  . ARG A 1 327 ? 16.951  10.387  -17.055 1.00 35.29  ? 356 ARG A CZ  1 
ATOM   2559 N NH1 . ARG A 1 327 ? 17.385  9.516   -16.160 1.00 34.57  ? 356 ARG A NH1 1 
ATOM   2560 N NH2 . ARG A 1 327 ? 15.798  11.008  -16.867 1.00 36.37  ? 356 ARG A NH2 1 
ATOM   2561 N N   . TYR A 1 328 ? 15.893  10.612  -23.499 1.00 35.92  ? 357 TYR A N   1 
ATOM   2562 C CA  . TYR A 1 328 ? 14.844  10.280  -24.454 1.00 36.27  ? 357 TYR A CA  1 
ATOM   2563 C C   . TYR A 1 328 ? 15.422  10.321  -25.870 1.00 34.80  ? 357 TYR A C   1 
ATOM   2564 O O   . TYR A 1 328 ? 15.313  9.343   -26.611 1.00 30.98  ? 357 TYR A O   1 
ATOM   2565 C CB  . TYR A 1 328 ? 13.648  11.233  -24.326 1.00 37.02  ? 357 TYR A CB  1 
ATOM   2566 C CG  . TYR A 1 328 ? 12.485  10.968  -25.280 1.00 38.80  ? 357 TYR A CG  1 
ATOM   2567 C CD1 . TYR A 1 328 ? 11.448  10.111  -24.923 1.00 39.34  ? 357 TYR A CD1 1 
ATOM   2568 C CD2 . TYR A 1 328 ? 12.408  11.582  -26.528 1.00 38.32  ? 357 TYR A CD2 1 
ATOM   2569 C CE1 . TYR A 1 328 ? 10.374  9.879   -25.767 1.00 38.28  ? 357 TYR A CE1 1 
ATOM   2570 C CE2 . TYR A 1 328 ? 11.343  11.348  -27.387 1.00 37.77  ? 357 TYR A CE2 1 
ATOM   2571 C CZ  . TYR A 1 328 ? 10.322  10.498  -27.002 1.00 37.36  ? 357 TYR A CZ  1 
ATOM   2572 O OH  . TYR A 1 328 ? 9.263   10.235  -27.819 1.00 38.65  ? 357 TYR A OH  1 
ATOM   2573 N N   . THR A 1 329 ? 16.038  11.463  -26.215 1.00 34.06  ? 358 THR A N   1 
ATOM   2574 C CA  . THR A 1 329 ? 16.557  11.725  -27.553 1.00 34.39  ? 358 THR A CA  1 
ATOM   2575 C C   . THR A 1 329 ? 17.541  10.627  -27.947 1.00 37.76  ? 358 THR A C   1 
ATOM   2576 O O   . THR A 1 329 ? 17.470  10.068  -29.041 1.00 39.58  ? 358 THR A O   1 
ATOM   2577 C CB  . THR A 1 329 ? 17.231  13.096  -27.578 1.00 33.46  ? 358 THR A CB  1 
ATOM   2578 O OG1 . THR A 1 329 ? 16.307  14.026  -27.026 1.00 30.40  ? 358 THR A OG1 1 
ATOM   2579 C CG2 . THR A 1 329 ? 17.610  13.532  -28.979 1.00 34.75  ? 358 THR A CG2 1 
ATOM   2580 N N   . CYS A 1 330 ? 18.467  10.348  -27.028 1.00 38.47  ? 359 CYS A N   1 
ATOM   2581 C CA  . CYS A 1 330 ? 19.438  9.279   -27.161 1.00 41.59  ? 359 CYS A CA  1 
ATOM   2582 C C   . CYS A 1 330 ? 18.773  7.969   -27.593 1.00 40.96  ? 359 CYS A C   1 
ATOM   2583 O O   . CYS A 1 330 ? 19.269  7.295   -28.491 1.00 43.16  ? 359 CYS A O   1 
ATOM   2584 C CB  . CYS A 1 330 ? 20.198  9.146   -25.847 1.00 44.53  ? 359 CYS A CB  1 
ATOM   2585 S SG  . CYS A 1 330 ? 20.733  7.459   -25.501 1.00 53.76  ? 359 CYS A SG  1 
ATOM   2586 N N   . GLN A 1 331 ? 17.662  7.604   -26.940 1.00 41.81  ? 360 GLN A N   1 
ATOM   2587 C CA  . GLN A 1 331 ? 16.951  6.364   -27.222 1.00 40.47  ? 360 GLN A CA  1 
ATOM   2588 C C   . GLN A 1 331 ? 16.154  6.475   -28.518 1.00 42.21  ? 360 GLN A C   1 
ATOM   2589 O O   . GLN A 1 331 ? 16.018  5.491   -29.238 1.00 43.20  ? 360 GLN A O   1 
ATOM   2590 C CB  . GLN A 1 331 ? 15.976  6.002   -26.103 1.00 39.38  ? 360 GLN A CB  1 
ATOM   2591 C CG  . GLN A 1 331 ? 16.654  5.703   -24.773 1.00 39.73  ? 360 GLN A CG  1 
ATOM   2592 C CD  . GLN A 1 331 ? 15.692  5.218   -23.712 1.00 41.27  ? 360 GLN A CD  1 
ATOM   2593 O OE1 . GLN A 1 331 ? 15.733  4.054   -23.293 1.00 44.85  ? 360 GLN A OE1 1 
ATOM   2594 N NE2 . GLN A 1 331 ? 14.805  6.102   -23.278 1.00 40.17  ? 360 GLN A NE2 1 
ATOM   2595 N N   . ARG A 1 332 ? 15.597  7.664   -28.784 1.00 45.30  ? 361 ARG A N   1 
ATOM   2596 C CA  . ARG A 1 332 ? 14.940  7.943   -30.053 1.00 44.83  ? 361 ARG A CA  1 
ATOM   2597 C C   . ARG A 1 332 ? 15.912  7.691   -31.208 1.00 46.02  ? 361 ARG A C   1 
ATOM   2598 O O   . ARG A 1 332 ? 15.531  7.058   -32.192 1.00 47.00  ? 361 ARG A O   1 
ATOM   2599 C CB  . ARG A 1 332 ? 14.373  9.368   -30.100 1.00 43.30  ? 361 ARG A CB  1 
ATOM   2600 C CG  . ARG A 1 332 ? 13.699  9.740   -31.416 1.00 43.78  ? 361 ARG A CG  1 
ATOM   2601 C CD  . ARG A 1 332 ? 13.063  11.128  -31.370 1.00 43.94  ? 361 ARG A CD  1 
ATOM   2602 N NE  . ARG A 1 332 ? 12.722  11.654  -32.698 1.00 43.01  ? 361 ARG A NE  1 
ATOM   2603 C CZ  . ARG A 1 332 ? 11.669  11.320  -33.453 1.00 44.00  ? 361 ARG A CZ  1 
ATOM   2604 N NH1 . ARG A 1 332 ? 10.700  10.557  -32.976 1.00 46.53  ? 361 ARG A NH1 1 
ATOM   2605 N NH2 . ARG A 1 332 ? 11.569  11.783  -34.689 1.00 40.86  ? 361 ARG A NH2 1 
ATOM   2606 N N   . GLU A 1 333 ? 17.155  8.185   -31.085 1.00 42.83  ? 362 GLU A N   1 
ATOM   2607 C CA  . GLU A 1 333 ? 18.171  8.007   -32.114 1.00 43.40  ? 362 GLU A CA  1 
ATOM   2608 C C   . GLU A 1 333 ? 18.453  6.520   -32.329 1.00 44.25  ? 362 GLU A C   1 
ATOM   2609 O O   . GLU A 1 333 ? 18.551  6.070   -33.467 1.00 45.58  ? 362 GLU A O   1 
ATOM   2610 C CB  . GLU A 1 333 ? 19.505  8.662   -31.756 1.00 43.99  ? 362 GLU A CB  1 
ATOM   2611 C CG  . GLU A 1 333 ? 19.487  10.189  -31.719 1.00 45.46  ? 362 GLU A CG  1 
ATOM   2612 C CD  . GLU A 1 333 ? 20.639  10.827  -30.947 1.00 46.36  ? 362 GLU A CD  1 
ATOM   2613 O OE1 . GLU A 1 333 ? 21.354  10.116  -30.206 1.00 49.06  ? 362 GLU A OE1 1 
ATOM   2614 O OE2 . GLU A 1 333 ? 20.838  12.051  -31.089 1.00 46.39  ? 362 GLU A OE2 1 
ATOM   2615 N N   . PHE A 1 334 ? 18.578  5.767   -31.228 1.00 44.35  ? 363 PHE A N   1 
ATOM   2616 C CA  . PHE A 1 334 ? 18.902  4.349   -31.285 1.00 43.28  ? 363 PHE A CA  1 
ATOM   2617 C C   . PHE A 1 334 ? 17.832  3.594   -32.071 1.00 44.69  ? 363 PHE A C   1 
ATOM   2618 O O   . PHE A 1 334 ? 18.151  2.636   -32.765 1.00 45.39  ? 363 PHE A O   1 
ATOM   2619 C CB  . PHE A 1 334 ? 19.063  3.750   -29.881 1.00 41.28  ? 363 PHE A CB  1 
ATOM   2620 C CG  . PHE A 1 334 ? 19.318  2.248   -29.876 1.00 38.53  ? 363 PHE A CG  1 
ATOM   2621 C CD1 . PHE A 1 334 ? 20.613  1.743   -29.927 1.00 37.65  ? 363 PHE A CD1 1 
ATOM   2622 C CD2 . PHE A 1 334 ? 18.263  1.341   -29.843 1.00 39.36  ? 363 PHE A CD2 1 
ATOM   2623 C CE1 . PHE A 1 334 ? 20.845  0.376   -29.931 1.00 37.15  ? 363 PHE A CE1 1 
ATOM   2624 C CE2 . PHE A 1 334 ? 18.500  -0.026  -29.862 1.00 38.50  ? 363 PHE A CE2 1 
ATOM   2625 C CZ  . PHE A 1 334 ? 19.792  -0.504  -29.904 1.00 37.99  ? 363 PHE A CZ  1 
ATOM   2626 N N   . ALA A 1 335 ? 16.569  4.026   -31.943 1.00 47.65  ? 364 ALA A N   1 
ATOM   2627 C CA  . ALA A 1 335 ? 15.430  3.342   -32.538 1.00 49.64  ? 364 ALA A CA  1 
ATOM   2628 C C   . ALA A 1 335 ? 15.341  3.610   -34.039 1.00 52.92  ? 364 ALA A C   1 
ATOM   2629 O O   . ALA A 1 335 ? 14.897  2.746   -34.796 1.00 50.83  ? 364 ALA A O   1 
ATOM   2630 C CB  . ALA A 1 335 ? 14.156  3.779   -31.851 1.00 50.00  ? 364 ALA A CB  1 
ATOM   2631 N N   . LEU A 1 336 ? 15.716  4.827   -34.451 1.00 54.70  ? 365 LEU A N   1 
ATOM   2632 C CA  . LEU A 1 336 ? 15.683  5.202   -35.854 1.00 56.49  ? 365 LEU A CA  1 
ATOM   2633 C C   . LEU A 1 336 ? 16.682  4.348   -36.639 1.00 59.12  ? 365 LEU A C   1 
ATOM   2634 O O   . LEU A 1 336 ? 16.470  4.101   -37.826 1.00 62.91  ? 365 LEU A O   1 
ATOM   2635 C CB  . LEU A 1 336 ? 15.941  6.702   -36.002 1.00 56.85  ? 365 LEU A CB  1 
ATOM   2636 C CG  . LEU A 1 336 ? 14.792  7.624   -35.572 1.00 58.50  ? 365 LEU A CG  1 
ATOM   2637 C CD1 . LEU A 1 336 ? 15.249  9.067   -35.431 1.00 56.78  ? 365 LEU A CD1 1 
ATOM   2638 C CD2 . LEU A 1 336 ? 13.618  7.553   -36.542 1.00 59.34  ? 365 LEU A CD2 1 
ATOM   2639 N N   . LYS A 1 337 ? 17.749  3.883   -35.970 1.00 54.11  ? 366 LYS A N   1 
ATOM   2640 C CA  . LYS A 1 337 ? 18.718  2.981   -36.576 1.00 52.91  ? 366 LYS A CA  1 
ATOM   2641 C C   . LYS A 1 337 ? 18.175  1.554   -36.645 1.00 48.25  ? 366 LYS A C   1 
ATOM   2642 O O   . LYS A 1 337 ? 18.293  0.889   -37.668 1.00 46.93  ? 366 LYS A O   1 
ATOM   2643 C CB  . LYS A 1 337 ? 20.003  2.816   -35.757 1.00 58.76  ? 366 LYS A CB  1 
ATOM   2644 C CG  . LYS A 1 337 ? 20.906  4.020   -35.558 1.00 61.48  ? 366 LYS A CG  1 
ATOM   2645 C CD  . LYS A 1 337 ? 22.029  3.729   -34.565 1.00 68.07  ? 366 LYS A CD  1 
ATOM   2646 C CE  . LYS A 1 337 ? 22.729  4.951   -34.053 1.00 69.97  ? 366 LYS A CE  1 
ATOM   2647 N NZ  . LYS A 1 337 ? 23.578  4.677   -32.890 1.00 70.75  ? 366 LYS A NZ  1 
ATOM   2648 N N   . HIS A 1 338 ? 17.612  1.072   -35.535 1.00 46.02  ? 367 HIS A N   1 
ATOM   2649 C CA  . HIS A 1 338 ? 17.559  -0.358  -35.283 1.00 44.86  ? 367 HIS A CA  1 
ATOM   2650 C C   . HIS A 1 338 ? 16.147  -0.931  -35.376 1.00 46.13  ? 367 HIS A C   1 
ATOM   2651 O O   . HIS A 1 338 ? 16.002  -2.145  -35.463 1.00 48.75  ? 367 HIS A O   1 
ATOM   2652 C CB  . HIS A 1 338 ? 18.207  -0.652  -33.930 1.00 43.48  ? 367 HIS A CB  1 
ATOM   2653 C CG  . HIS A 1 338 ? 19.667  -0.363  -33.915 1.00 44.86  ? 367 HIS A CG  1 
ATOM   2654 N ND1 . HIS A 1 338 ? 20.552  -0.908  -34.820 1.00 45.09  ? 367 HIS A ND1 1 
ATOM   2655 C CD2 . HIS A 1 338 ? 20.403  0.383   -33.085 1.00 45.39  ? 367 HIS A CD2 1 
ATOM   2656 C CE1 . HIS A 1 338 ? 21.775  -0.478  -34.547 1.00 43.68  ? 367 HIS A CE1 1 
ATOM   2657 N NE2 . HIS A 1 338 ? 21.708  0.303   -33.494 1.00 44.10  ? 367 HIS A NE2 1 
ATOM   2658 N N   . LEU A 1 339 ? 15.109  -0.089  -35.344 1.00 49.34  ? 368 LEU A N   1 
ATOM   2659 C CA  . LEU A 1 339 ? 13.748  -0.590  -35.473 1.00 52.18  ? 368 LEU A CA  1 
ATOM   2660 C C   . LEU A 1 339 ? 12.807  0.538   -35.879 1.00 51.46  ? 368 LEU A C   1 
ATOM   2661 O O   . LEU A 1 339 ? 11.821  0.799   -35.192 1.00 57.41  ? 368 LEU A O   1 
ATOM   2662 C CB  . LEU A 1 339 ? 13.287  -1.254  -34.174 1.00 55.43  ? 368 LEU A CB  1 
ATOM   2663 C CG  . LEU A 1 339 ? 13.449  -0.433  -32.890 1.00 58.45  ? 368 LEU A CG  1 
ATOM   2664 C CD1 . LEU A 1 339 ? 12.276  -0.653  -31.948 1.00 58.85  ? 368 LEU A CD1 1 
ATOM   2665 C CD2 . LEU A 1 339 ? 14.756  -0.777  -32.189 1.00 60.24  ? 368 LEU A CD2 1 
ATOM   2666 N N   . PRO A 1 340 ? 13.052  1.212   -37.025 1.00 49.58  ? 369 PRO A N   1 
ATOM   2667 C CA  . PRO A 1 340 ? 12.239  2.366   -37.418 1.00 49.88  ? 369 PRO A CA  1 
ATOM   2668 C C   . PRO A 1 340 ? 10.776  2.045   -37.733 1.00 53.32  ? 369 PRO A C   1 
ATOM   2669 O O   . PRO A 1 340 ? 9.905   2.898   -37.561 1.00 56.07  ? 369 PRO A O   1 
ATOM   2670 C CB  . PRO A 1 340 ? 13.002  2.897   -38.647 1.00 48.77  ? 369 PRO A CB  1 
ATOM   2671 C CG  . PRO A 1 340 ? 13.640  1.659   -39.237 1.00 48.77  ? 369 PRO A CG  1 
ATOM   2672 C CD  . PRO A 1 340 ? 14.087  0.873   -38.016 1.00 47.87  ? 369 PRO A CD  1 
ATOM   2673 N N   . ASN A 1 341 ? 10.506  0.814   -38.184 1.00 53.07  ? 370 ASN A N   1 
ATOM   2674 C CA  . ASN A 1 341 ? 9.174   0.457   -38.646 1.00 58.22  ? 370 ASN A CA  1 
ATOM   2675 C C   . ASN A 1 341 ? 8.399   -0.306  -37.573 1.00 61.26  ? 370 ASN A C   1 
ATOM   2676 O O   . ASN A 1 341 ? 7.289   -0.761  -37.840 1.00 65.51  ? 370 ASN A O   1 
ATOM   2677 C CB  . ASN A 1 341 ? 9.239   -0.317  -39.956 1.00 61.87  ? 370 ASN A CB  1 
ATOM   2678 C CG  . ASN A 1 341 ? 9.870   0.507   -41.054 1.00 62.59  ? 370 ASN A CG  1 
ATOM   2679 O OD1 . ASN A 1 341 ? 9.428   1.631   -41.314 1.00 62.83  ? 370 ASN A OD1 1 
ATOM   2680 N ND2 . ASN A 1 341 ? 10.916  -0.011  -41.683 1.00 62.82  ? 370 ASN A ND2 1 
ATOM   2681 N N   . ASP A 1 342 ? 8.961   -0.426  -36.361 1.00 64.73  ? 371 ASP A N   1 
ATOM   2682 C CA  . ASP A 1 342 ? 8.265   -1.078  -35.261 1.00 62.25  ? 371 ASP A CA  1 
ATOM   2683 C C   . ASP A 1 342 ? 6.998   -0.291  -34.928 1.00 58.24  ? 371 ASP A C   1 
ATOM   2684 O O   . ASP A 1 342 ? 7.073   0.909   -34.689 1.00 53.72  ? 371 ASP A O   1 
ATOM   2685 C CB  . ASP A 1 342 ? 9.133   -1.209  -34.019 1.00 60.93  ? 371 ASP A CB  1 
ATOM   2686 C CG  . ASP A 1 342 ? 8.379   -1.619  -32.762 1.00 60.12  ? 371 ASP A CG  1 
ATOM   2687 O OD1 . ASP A 1 342 ? 8.162   -2.838  -32.575 1.00 54.51  ? 371 ASP A OD1 1 
ATOM   2688 O OD2 . ASP A 1 342 ? 7.969   -0.707  -32.007 1.00 59.17  ? 371 ASP A OD2 1 
ATOM   2689 N N   . PRO A 1 343 ? 5.807   -0.936  -34.899 1.00 60.90  ? 372 PRO A N   1 
ATOM   2690 C CA  . PRO A 1 343 ? 4.554   -0.234  -34.597 1.00 61.78  ? 372 PRO A CA  1 
ATOM   2691 C C   . PRO A 1 343 ? 4.547   0.536   -33.275 1.00 62.95  ? 372 PRO A C   1 
ATOM   2692 O O   . PRO A 1 343 ? 4.133   1.693   -33.235 1.00 62.72  ? 372 PRO A O   1 
ATOM   2693 C CB  . PRO A 1 343 ? 3.510   -1.370  -34.603 1.00 64.00  ? 372 PRO A CB  1 
ATOM   2694 C CG  . PRO A 1 343 ? 4.116   -2.441  -35.482 1.00 63.26  ? 372 PRO A CG  1 
ATOM   2695 C CD  . PRO A 1 343 ? 5.602   -2.366  -35.190 1.00 62.94  ? 372 PRO A CD  1 
ATOM   2696 N N   . MET A 1 344 ? 5.010   -0.109  -32.195 1.00 62.79  ? 373 MET A N   1 
ATOM   2697 C CA  . MET A 1 344 ? 5.074   0.527   -30.887 1.00 63.26  ? 373 MET A CA  1 
ATOM   2698 C C   . MET A 1 344 ? 5.977   1.761   -30.932 1.00 55.63  ? 373 MET A C   1 
ATOM   2699 O O   . MET A 1 344 ? 5.691   2.757   -30.272 1.00 53.35  ? 373 MET A O   1 
ATOM   2700 C CB  . MET A 1 344 ? 5.583   -0.450  -29.819 1.00 71.51  ? 373 MET A CB  1 
ATOM   2701 C CG  . MET A 1 344 ? 4.607   -1.564  -29.479 1.00 76.29  ? 373 MET A CG  1 
ATOM   2702 S SD  . MET A 1 344 ? 3.159   -0.996  -28.563 1.00 84.19  ? 373 MET A SD  1 
ATOM   2703 C CE  . MET A 1 344 ? 3.871   -0.547  -26.974 1.00 85.77  ? 373 MET A CE  1 
ATOM   2704 N N   . PHE A 1 345 ? 7.063   1.699   -31.711 1.00 52.46  ? 374 PHE A N   1 
ATOM   2705 C CA  . PHE A 1 345 ? 7.944   2.847   -31.870 1.00 53.74  ? 374 PHE A CA  1 
ATOM   2706 C C   . PHE A 1 345 ? 7.207   3.989   -32.581 1.00 51.22  ? 374 PHE A C   1 
ATOM   2707 O O   . PHE A 1 345 ? 7.232   5.126   -32.113 1.00 47.79  ? 374 PHE A O   1 
ATOM   2708 C CB  . PHE A 1 345 ? 9.247   2.517   -32.611 1.00 50.61  ? 374 PHE A CB  1 
ATOM   2709 C CG  . PHE A 1 345 ? 10.037  3.769   -32.966 1.00 50.05  ? 374 PHE A CG  1 
ATOM   2710 C CD1 . PHE A 1 345 ? 10.285  4.748   -32.009 1.00 49.66  ? 374 PHE A CD1 1 
ATOM   2711 C CD2 . PHE A 1 345 ? 10.463  4.000   -34.267 1.00 50.61  ? 374 PHE A CD2 1 
ATOM   2712 C CE1 . PHE A 1 345 ? 10.961  5.906   -32.340 1.00 50.37  ? 374 PHE A CE1 1 
ATOM   2713 C CE2 . PHE A 1 345 ? 11.140  5.162   -34.595 1.00 51.28  ? 374 PHE A CE2 1 
ATOM   2714 C CZ  . PHE A 1 345 ? 11.384  6.114   -33.632 1.00 53.26  ? 374 PHE A CZ  1 
ATOM   2715 N N   . LYS A 1 346 ? 6.555   3.685   -33.710 1.00 51.60  ? 375 LYS A N   1 
ATOM   2716 C CA  . LYS A 1 346 ? 5.889   4.700   -34.515 1.00 54.68  ? 375 LYS A CA  1 
ATOM   2717 C C   . LYS A 1 346 ? 4.867   5.475   -33.686 1.00 49.39  ? 375 LYS A C   1 
ATOM   2718 O O   . LYS A 1 346 ? 4.586   6.631   -33.988 1.00 47.85  ? 375 LYS A O   1 
ATOM   2719 C CB  . LYS A 1 346 ? 5.155   4.103   -35.720 1.00 60.65  ? 375 LYS A CB  1 
ATOM   2720 C CG  . LYS A 1 346 ? 6.023   3.473   -36.802 1.00 66.59  ? 375 LYS A CG  1 
ATOM   2721 C CD  . LYS A 1 346 ? 5.183   2.852   -37.915 1.00 71.98  ? 375 LYS A CD  1 
ATOM   2722 C CE  . LYS A 1 346 ? 5.983   2.075   -38.905 1.00 76.16  ? 375 LYS A CE  1 
ATOM   2723 N NZ  . LYS A 1 346 ? 5.147   1.521   -39.973 1.00 80.11  ? 375 LYS A NZ  1 
ATOM   2724 N N   . LEU A 1 347 ? 4.295   4.827   -32.663 1.00 48.69  ? 376 LEU A N   1 
ATOM   2725 C CA  . LEU A 1 347 ? 3.360   5.489   -31.770 1.00 48.89  ? 376 LEU A CA  1 
ATOM   2726 C C   . LEU A 1 347 ? 4.113   6.476   -30.881 1.00 48.13  ? 376 LEU A C   1 
ATOM   2727 O O   . LEU A 1 347 ? 3.743   7.647   -30.804 1.00 48.86  ? 376 LEU A O   1 
ATOM   2728 C CB  . LEU A 1 347 ? 2.592   4.464   -30.939 1.00 52.85  ? 376 LEU A CB  1 
ATOM   2729 C CG  . LEU A 1 347 ? 1.594   5.048   -29.931 1.00 55.58  ? 376 LEU A CG  1 
ATOM   2730 C CD1 . LEU A 1 347 ? 0.471   5.798   -30.638 1.00 56.12  ? 376 LEU A CD1 1 
ATOM   2731 C CD2 . LEU A 1 347 ? 1.035   3.967   -29.029 1.00 56.00  ? 376 LEU A CD2 1 
ATOM   2732 N N   . VAL A 1 348 ? 5.165   5.991   -30.208 1.00 46.02  ? 377 VAL A N   1 
ATOM   2733 C CA  . VAL A 1 348 ? 5.984   6.833   -29.352 1.00 44.40  ? 377 VAL A CA  1 
ATOM   2734 C C   . VAL A 1 348 ? 6.373   8.080   -30.143 1.00 43.64  ? 377 VAL A C   1 
ATOM   2735 O O   . VAL A 1 348 ? 6.158   9.200   -29.684 1.00 41.60  ? 377 VAL A O   1 
ATOM   2736 C CB  . VAL A 1 348 ? 7.217   6.078   -28.805 1.00 45.92  ? 377 VAL A CB  1 
ATOM   2737 C CG1 . VAL A 1 348 ? 8.280   7.012   -28.235 1.00 47.52  ? 377 VAL A CG1 1 
ATOM   2738 C CG2 . VAL A 1 348 ? 6.832   5.031   -27.764 1.00 44.89  ? 377 VAL A CG2 1 
ATOM   2739 N N   . ALA A 1 349 ? 6.915   7.867   -31.349 1.00 45.90  ? 378 ALA A N   1 
ATOM   2740 C CA  . ALA A 1 349 ? 7.311   8.950   -32.241 1.00 44.97  ? 378 ALA A CA  1 
ATOM   2741 C C   . ALA A 1 349 ? 6.129   9.869   -32.547 1.00 47.70  ? 378 ALA A C   1 
ATOM   2742 O O   . ALA A 1 349 ? 6.306   11.088  -32.593 1.00 48.62  ? 378 ALA A O   1 
ATOM   2743 C CB  . ALA A 1 349 ? 7.893   8.382   -33.512 1.00 44.22  ? 378 ALA A CB  1 
ATOM   2744 N N   . GLN A 1 350 ? 4.940   9.281   -32.763 1.00 45.54  ? 379 GLN A N   1 
ATOM   2745 C CA  . GLN A 1 350 ? 3.733   10.054  -33.023 1.00 49.92  ? 379 GLN A CA  1 
ATOM   2746 C C   . GLN A 1 350 ? 3.417   10.979  -31.848 1.00 49.74  ? 379 GLN A C   1 
ATOM   2747 O O   . GLN A 1 350 ? 3.148   12.159  -32.056 1.00 45.95  ? 379 GLN A O   1 
ATOM   2748 C CB  . GLN A 1 350 ? 2.503   9.194   -33.325 1.00 54.01  ? 379 GLN A CB  1 
ATOM   2749 C CG  . GLN A 1 350 ? 2.316   8.854   -34.798 1.00 58.24  ? 379 GLN A CG  1 
ATOM   2750 C CD  . GLN A 1 350 ? 0.944   8.294   -35.106 1.00 63.74  ? 379 GLN A CD  1 
ATOM   2751 O OE1 . GLN A 1 350 ? 0.606   7.160   -34.740 1.00 63.12  ? 379 GLN A OE1 1 
ATOM   2752 N NE2 . GLN A 1 350 ? 0.139   9.087   -35.799 1.00 66.38  ? 379 GLN A NE2 1 
ATOM   2753 N N   . LEU A 1 351 ? 3.455   10.434  -30.623 1.00 50.82  ? 380 LEU A N   1 
ATOM   2754 C CA  . LEU A 1 351 ? 3.103   11.174  -29.415 1.00 48.95  ? 380 LEU A CA  1 
ATOM   2755 C C   . LEU A 1 351 ? 4.046   12.354  -29.195 1.00 48.29  ? 380 LEU A C   1 
ATOM   2756 O O   . LEU A 1 351 ? 3.650   13.358  -28.603 1.00 44.23  ? 380 LEU A O   1 
ATOM   2757 C CB  . LEU A 1 351 ? 3.139   10.243  -28.205 1.00 49.40  ? 380 LEU A CB  1 
ATOM   2758 C CG  . LEU A 1 351 ? 2.135   9.088   -28.210 1.00 49.47  ? 380 LEU A CG  1 
ATOM   2759 C CD1 . LEU A 1 351 ? 2.586   8.004   -27.251 1.00 49.70  ? 380 LEU A CD1 1 
ATOM   2760 C CD2 . LEU A 1 351 ? 0.745   9.577   -27.844 1.00 52.90  ? 380 LEU A CD2 1 
ATOM   2761 N N   . TYR A 1 352 ? 5.299   12.217  -29.649 1.00 53.70  ? 381 TYR A N   1 
ATOM   2762 C CA  . TYR A 1 352 ? 6.300   13.262  -29.484 1.00 56.18  ? 381 TYR A CA  1 
ATOM   2763 C C   . TYR A 1 352 ? 5.909   14.508  -30.283 1.00 59.43  ? 381 TYR A C   1 
ATOM   2764 O O   . TYR A 1 352 ? 6.259   15.619  -29.886 1.00 56.92  ? 381 TYR A O   1 
ATOM   2765 C CB  . TYR A 1 352 ? 7.686   12.737  -29.879 1.00 58.18  ? 381 TYR A CB  1 
ATOM   2766 C CG  . TYR A 1 352 ? 8.841   13.688  -29.583 1.00 61.78  ? 381 TYR A CG  1 
ATOM   2767 C CD1 . TYR A 1 352 ? 8.871   14.443  -28.417 1.00 62.51  ? 381 TYR A CD1 1 
ATOM   2768 C CD2 . TYR A 1 352 ? 9.895   13.846  -30.479 1.00 67.94  ? 381 TYR A CD2 1 
ATOM   2769 C CE1 . TYR A 1 352 ? 9.915   15.311  -28.139 1.00 64.95  ? 381 TYR A CE1 1 
ATOM   2770 C CE2 . TYR A 1 352 ? 10.945  14.713  -30.215 1.00 68.87  ? 381 TYR A CE2 1 
ATOM   2771 C CZ  . TYR A 1 352 ? 10.956  15.449  -29.041 1.00 69.62  ? 381 TYR A CZ  1 
ATOM   2772 O OH  . TYR A 1 352 ? 11.971  16.319  -28.750 1.00 69.81  ? 381 TYR A OH  1 
ATOM   2773 N N   . LYS A 1 353 ? 5.187   14.315  -31.403 1.00 60.26  ? 382 LYS A N   1 
ATOM   2774 C CA  . LYS A 1 353 ? 4.690   15.413  -32.227 1.00 58.75  ? 382 LYS A CA  1 
ATOM   2775 C C   . LYS A 1 353 ? 3.518   16.121  -31.545 1.00 52.74  ? 382 LYS A C   1 
ATOM   2776 O O   . LYS A 1 353 ? 3.411   17.343  -31.606 1.00 46.00  ? 382 LYS A O   1 
ATOM   2777 C CB  . LYS A 1 353 ? 4.181   14.911  -33.584 1.00 62.94  ? 382 LYS A CB  1 
ATOM   2778 C CG  . LYS A 1 353 ? 5.209   14.255  -34.499 1.00 67.63  ? 382 LYS A CG  1 
ATOM   2779 C CD  . LYS A 1 353 ? 4.626   13.248  -35.488 1.00 71.67  ? 382 LYS A CD  1 
ATOM   2780 C CE  . LYS A 1 353 ? 3.503   13.769  -36.340 1.00 71.32  ? 382 LYS A CE  1 
ATOM   2781 N NZ  . LYS A 1 353 ? 2.938   12.713  -37.188 1.00 69.57  ? 382 LYS A NZ  1 
ATOM   2782 N N   . ILE A 1 354 ? 2.647   15.335  -30.897 1.00 52.97  ? 383 ILE A N   1 
ATOM   2783 C CA  . ILE A 1 354 ? 1.346   15.806  -30.443 1.00 52.61  ? 383 ILE A CA  1 
ATOM   2784 C C   . ILE A 1 354 ? 1.419   16.281  -28.993 1.00 51.61  ? 383 ILE A C   1 
ATOM   2785 O O   . ILE A 1 354 ? 1.151   17.447  -28.716 1.00 54.16  ? 383 ILE A O   1 
ATOM   2786 C CB  . ILE A 1 354 ? 0.278   14.707  -30.604 1.00 53.08  ? 383 ILE A CB  1 
ATOM   2787 C CG1 . ILE A 1 354 ? 0.286   14.069  -32.006 1.00 53.41  ? 383 ILE A CG1 1 
ATOM   2788 C CG2 . ILE A 1 354 ? -1.106  15.241  -30.237 1.00 53.59  ? 383 ILE A CG2 1 
ATOM   2789 C CD1 . ILE A 1 354 ? 0.235   15.061  -33.157 1.00 51.67  ? 383 ILE A CD1 1 
ATOM   2790 N N   . VAL A 1 355 ? 1.763   15.366  -28.076 1.00 50.52  ? 384 VAL A N   1 
ATOM   2791 C CA  . VAL A 1 355 ? 1.548   15.574  -26.650 1.00 50.33  ? 384 VAL A CA  1 
ATOM   2792 C C   . VAL A 1 355 ? 2.135   16.920  -26.220 1.00 51.35  ? 384 VAL A C   1 
ATOM   2793 O O   . VAL A 1 355 ? 1.476   17.669  -25.500 1.00 49.11  ? 384 VAL A O   1 
ATOM   2794 C CB  . VAL A 1 355 ? 2.088   14.410  -25.788 1.00 49.72  ? 384 VAL A CB  1 
ATOM   2795 C CG1 . VAL A 1 355 ? 1.999   14.699  -24.291 1.00 49.17  ? 384 VAL A CG1 1 
ATOM   2796 C CG2 . VAL A 1 355 ? 1.387   13.094  -26.110 1.00 49.62  ? 384 VAL A CG2 1 
ATOM   2797 N N   . PRO A 1 356 ? 3.381   17.284  -26.612 1.00 54.67  ? 385 PRO A N   1 
ATOM   2798 C CA  . PRO A 1 356 ? 3.946   18.580  -26.225 1.00 57.54  ? 385 PRO A CA  1 
ATOM   2799 C C   . PRO A 1 356 ? 3.100   19.801  -26.588 1.00 58.37  ? 385 PRO A C   1 
ATOM   2800 O O   . PRO A 1 356 ? 3.074   20.771  -25.831 1.00 56.23  ? 385 PRO A O   1 
ATOM   2801 C CB  . PRO A 1 356 ? 5.303   18.576  -26.941 1.00 57.92  ? 385 PRO A CB  1 
ATOM   2802 C CG  . PRO A 1 356 ? 5.654   17.110  -27.011 1.00 58.40  ? 385 PRO A CG  1 
ATOM   2803 C CD  . PRO A 1 356 ? 4.331   16.470  -27.388 1.00 57.26  ? 385 PRO A CD  1 
ATOM   2804 N N   . ASN A 1 357 ? 2.384   19.737  -27.719 1.00 59.83  ? 386 ASN A N   1 
ATOM   2805 C CA  . ASN A 1 357 ? 1.601   20.875  -28.180 1.00 63.16  ? 386 ASN A CA  1 
ATOM   2806 C C   . ASN A 1 357 ? 0.435   21.120  -27.221 1.00 60.51  ? 386 ASN A C   1 
ATOM   2807 O O   . ASN A 1 357 ? 0.090   22.274  -26.986 1.00 64.14  ? 386 ASN A O   1 
ATOM   2808 C CB  . ASN A 1 357 ? 1.222   20.759  -29.659 1.00 67.05  ? 386 ASN A CB  1 
ATOM   2809 C CG  . ASN A 1 357 ? -0.057  19.996  -29.930 1.00 71.31  ? 386 ASN A CG  1 
ATOM   2810 O OD1 . ASN A 1 357 ? -0.019  18.919  -30.536 1.00 72.32  ? 386 ASN A OD1 1 
ATOM   2811 N ND2 . ASN A 1 357 ? -1.202  20.559  -29.565 1.00 73.08  ? 386 ASN A ND2 1 
ATOM   2812 N N   . VAL A 1 358 ? -0.132  20.054  -26.634 1.00 57.04  ? 387 VAL A N   1 
ATOM   2813 C CA  . VAL A 1 358 ? -1.391  20.152  -25.908 1.00 55.25  ? 387 VAL A CA  1 
ATOM   2814 C C   . VAL A 1 358 ? -1.158  20.467  -24.428 1.00 58.13  ? 387 VAL A C   1 
ATOM   2815 O O   . VAL A 1 358 ? -2.021  21.073  -23.795 1.00 56.19  ? 387 VAL A O   1 
ATOM   2816 C CB  . VAL A 1 358 ? -2.272  18.894  -26.051 1.00 56.50  ? 387 VAL A CB  1 
ATOM   2817 C CG1 . VAL A 1 358 ? -2.522  18.524  -27.507 1.00 57.99  ? 387 VAL A CG1 1 
ATOM   2818 C CG2 . VAL A 1 358 ? -1.717  17.694  -25.299 1.00 58.61  ? 387 VAL A CG2 1 
ATOM   2819 N N   . LEU A 1 359 ? -0.026  20.029  -23.858 1.00 60.10  ? 388 LEU A N   1 
ATOM   2820 C CA  . LEU A 1 359 ? 0.192   20.177  -22.425 1.00 58.60  ? 388 LEU A CA  1 
ATOM   2821 C C   . LEU A 1 359 ? 0.419   21.648  -22.086 1.00 60.26  ? 388 LEU A C   1 
ATOM   2822 O O   . LEU A 1 359 ? -0.062  22.124  -21.061 1.00 63.74  ? 388 LEU A O   1 
ATOM   2823 C CB  . LEU A 1 359 ? 1.348   19.306  -21.930 1.00 58.04  ? 388 LEU A CB  1 
ATOM   2824 C CG  . LEU A 1 359 ? 1.137   17.790  -22.032 1.00 58.54  ? 388 LEU A CG  1 
ATOM   2825 C CD1 . LEU A 1 359 ? 2.392   17.040  -21.622 1.00 58.32  ? 388 LEU A CD1 1 
ATOM   2826 C CD2 . LEU A 1 359 ? -0.045  17.321  -21.203 1.00 56.53  ? 388 LEU A CD2 1 
ATOM   2827 N N   . LEU A 1 360 ? 1.150   22.357  -22.955 1.00 64.61  ? 389 LEU A N   1 
ATOM   2828 C CA  . LEU A 1 360 ? 1.420   23.776  -22.765 1.00 69.79  ? 389 LEU A CA  1 
ATOM   2829 C C   . LEU A 1 360 ? 0.131   24.584  -22.921 1.00 73.95  ? 389 LEU A C   1 
ATOM   2830 O O   . LEU A 1 360 ? -0.059  25.574  -22.215 1.00 74.28  ? 389 LEU A O   1 
ATOM   2831 C CB  . LEU A 1 360 ? 2.531   24.260  -23.700 1.00 70.47  ? 389 LEU A CB  1 
ATOM   2832 C CG  . LEU A 1 360 ? 2.385   23.954  -25.196 1.00 74.08  ? 389 LEU A CG  1 
ATOM   2833 C CD1 . LEU A 1 360 ? 1.595   25.013  -25.951 1.00 75.85  ? 389 LEU A CD1 1 
ATOM   2834 C CD2 . LEU A 1 360 ? 3.759   23.772  -25.823 1.00 76.03  ? 389 LEU A CD2 1 
ATOM   2835 N N   . GLU A 1 361 ? -0.754  24.147  -23.830 1.00 76.40  ? 390 GLU A N   1 
ATOM   2836 C CA  . GLU A 1 361 ? -2.066  24.757  -23.992 1.00 75.88  ? 390 GLU A CA  1 
ATOM   2837 C C   . GLU A 1 361 ? -2.822  24.669  -22.669 1.00 73.76  ? 390 GLU A C   1 
ATOM   2838 O O   . GLU A 1 361 ? -3.100  25.692  -22.050 1.00 72.19  ? 390 GLU A O   1 
ATOM   2839 C CB  . GLU A 1 361 ? -2.865  24.096  -25.116 1.00 79.74  ? 390 GLU A CB  1 
ATOM   2840 C CG  . GLU A 1 361 ? -2.273  24.318  -26.505 1.00 83.21  ? 390 GLU A CG  1 
ATOM   2841 C CD  . GLU A 1 361 ? -2.996  23.567  -27.610 1.00 87.16  ? 390 GLU A CD  1 
ATOM   2842 O OE1 . GLU A 1 361 ? -4.153  23.943  -27.895 1.00 92.09  ? 390 GLU A OE1 1 
ATOM   2843 O OE2 . GLU A 1 361 ? -2.423  22.614  -28.185 1.00 86.75  ? 390 GLU A OE2 1 
ATOM   2844 N N   . GLN A 1 362 ? -3.127  23.436  -22.240 1.00 74.66  ? 391 GLN A N   1 
ATOM   2845 C CA  . GLN A 1 362 ? -3.695  23.190  -20.923 1.00 78.22  ? 391 GLN A CA  1 
ATOM   2846 C C   . GLN A 1 362 ? -3.013  24.120  -19.920 1.00 77.34  ? 391 GLN A C   1 
ATOM   2847 O O   . GLN A 1 362 ? -3.682  24.872  -19.217 1.00 76.12  ? 391 GLN A O   1 
ATOM   2848 C CB  . GLN A 1 362 ? -3.547  21.713  -20.541 1.00 81.32  ? 391 GLN A CB  1 
ATOM   2849 C CG  . GLN A 1 362 ? -3.927  21.389  -19.097 1.00 86.51  ? 391 GLN A CG  1 
ATOM   2850 C CD  . GLN A 1 362 ? -3.352  20.081  -18.589 1.00 91.08  ? 391 GLN A CD  1 
ATOM   2851 O OE1 . GLN A 1 362 ? -4.057  19.247  -18.009 1.00 87.04  ? 391 GLN A OE1 1 
ATOM   2852 N NE2 . GLN A 1 362 ? -2.049  19.901  -18.766 1.00 90.98  ? 391 GLN A NE2 1 
ATOM   2853 N N   . GLY A 1 363 ? -1.676  24.064  -19.873 1.00 76.40  ? 392 GLY A N   1 
ATOM   2854 C CA  . GLY A 1 363 ? -0.887  25.014  -19.107 1.00 76.09  ? 392 GLY A CA  1 
ATOM   2855 C C   . GLY A 1 363 ? -0.266  24.382  -17.866 1.00 73.20  ? 392 GLY A C   1 
ATOM   2856 O O   . GLY A 1 363 ? 0.844   24.742  -17.484 1.00 75.79  ? 392 GLY A O   1 
ATOM   2857 N N   . LYS A 1 364 ? -0.999  23.453  -17.241 1.00 72.36  ? 393 LYS A N   1 
ATOM   2858 C CA  . LYS A 1 364 ? -0.602  22.859  -15.972 1.00 70.05  ? 393 LYS A CA  1 
ATOM   2859 C C   . LYS A 1 364 ? 0.874   22.461  -15.999 1.00 66.93  ? 393 LYS A C   1 
ATOM   2860 O O   . LYS A 1 364 ? 1.659   22.982  -15.212 1.00 66.50  ? 393 LYS A O   1 
ATOM   2861 C CB  . LYS A 1 364 ? -1.546  21.703  -15.611 1.00 69.66  ? 393 LYS A CB  1 
ATOM   2862 C CG  . LYS A 1 364 ? -2.441  21.902  -14.384 1.00 73.18  ? 393 LYS A CG  1 
ATOM   2863 C CD  . LYS A 1 364 ? -3.091  23.267  -14.177 1.00 75.62  ? 393 LYS A CD  1 
ATOM   2864 C CE  . LYS A 1 364 ? -4.108  23.632  -15.207 1.00 74.83  ? 393 LYS A CE  1 
ATOM   2865 N NZ  . LYS A 1 364 ? -4.754  24.901  -14.864 1.00 72.35  ? 393 LYS A NZ  1 
ATOM   2866 N N   . ALA A 1 365 ? 1.247   21.561  -16.917 1.00 64.33  ? 394 ALA A N   1 
ATOM   2867 C CA  . ALA A 1 365 ? 2.599   21.026  -16.980 1.00 63.40  ? 394 ALA A CA  1 
ATOM   2868 C C   . ALA A 1 365 ? 3.616   22.131  -17.263 1.00 63.99  ? 394 ALA A C   1 
ATOM   2869 O O   . ALA A 1 365 ? 3.500   22.840  -18.261 1.00 67.31  ? 394 ALA A O   1 
ATOM   2870 C CB  . ALA A 1 365 ? 2.674   19.946  -18.035 1.00 65.71  ? 394 ALA A CB  1 
ATOM   2871 N N   . LYS A 1 366 ? 4.621   22.248  -16.383 1.00 63.63  ? 395 LYS A N   1 
ATOM   2872 C CA  . LYS A 1 366 ? 5.720   23.182  -16.575 1.00 62.52  ? 395 LYS A CA  1 
ATOM   2873 C C   . LYS A 1 366 ? 6.765   22.573  -17.509 1.00 56.92  ? 395 LYS A C   1 
ATOM   2874 O O   . LYS A 1 366 ? 7.567   23.303  -18.087 1.00 58.71  ? 395 LYS A O   1 
ATOM   2875 C CB  . LYS A 1 366 ? 6.349   23.616  -15.243 1.00 66.52  ? 395 LYS A CB  1 
ATOM   2876 C CG  . LYS A 1 366 ? 5.645   24.782  -14.546 1.00 72.16  ? 395 LYS A CG  1 
ATOM   2877 C CD  . LYS A 1 366 ? 6.474   25.493  -13.480 1.00 75.81  ? 395 LYS A CD  1 
ATOM   2878 C CE  . LYS A 1 366 ? 5.858   26.789  -13.024 1.00 77.27  ? 395 LYS A CE  1 
ATOM   2879 N NZ  . LYS A 1 366 ? 6.704   27.538  -12.088 1.00 74.56  ? 395 LYS A NZ  1 
ATOM   2880 N N   . ASN A 1 367 ? 6.754   21.238  -17.634 1.00 53.07  ? 396 ASN A N   1 
ATOM   2881 C CA  . ASN A 1 367 ? 7.614   20.523  -18.563 1.00 50.73  ? 396 ASN A CA  1 
ATOM   2882 C C   . ASN A 1 367 ? 6.729   19.677  -19.473 1.00 46.56  ? 396 ASN A C   1 
ATOM   2883 O O   . ASN A 1 367 ? 6.376   18.550  -19.125 1.00 45.11  ? 396 ASN A O   1 
ATOM   2884 C CB  . ASN A 1 367 ? 8.673   19.692  -17.841 1.00 50.35  ? 396 ASN A CB  1 
ATOM   2885 C CG  . ASN A 1 367 ? 9.538   18.884  -18.786 1.00 51.78  ? 396 ASN A CG  1 
ATOM   2886 O OD1 . ASN A 1 367 ? 9.764   17.688  -18.559 1.00 50.66  ? 396 ASN A OD1 1 
ATOM   2887 N ND2 . ASN A 1 367 ? 10.054  19.507  -19.835 1.00 50.16  ? 396 ASN A ND2 1 
ATOM   2888 N N   . PRO A 1 368 ? 6.343   20.198  -20.661 1.00 44.63  ? 397 PRO A N   1 
ATOM   2889 C CA  . PRO A 1 368 ? 5.470   19.459  -21.574 1.00 44.60  ? 397 PRO A CA  1 
ATOM   2890 C C   . PRO A 1 368 ? 6.172   18.367  -22.380 1.00 43.93  ? 397 PRO A C   1 
ATOM   2891 O O   . PRO A 1 368 ? 5.529   17.681  -23.171 1.00 49.46  ? 397 PRO A O   1 
ATOM   2892 C CB  . PRO A 1 368 ? 4.925   20.588  -22.474 1.00 45.69  ? 397 PRO A CB  1 
ATOM   2893 C CG  . PRO A 1 368 ? 6.057   21.601  -22.546 1.00 43.96  ? 397 PRO A CG  1 
ATOM   2894 C CD  . PRO A 1 368 ? 6.722   21.524  -21.182 1.00 45.28  ? 397 PRO A CD  1 
ATOM   2895 N N   . TRP A 1 369 ? 7.481   18.195  -22.157 1.00 43.16  ? 398 TRP A N   1 
ATOM   2896 C CA  . TRP A 1 369 ? 8.308   17.359  -23.014 1.00 41.33  ? 398 TRP A CA  1 
ATOM   2897 C C   . TRP A 1 369 ? 8.507   15.983  -22.388 1.00 39.53  ? 398 TRP A C   1 
ATOM   2898 O O   . TRP A 1 369 ? 8.363   15.832  -21.175 1.00 40.70  ? 398 TRP A O   1 
ATOM   2899 C CB  . TRP A 1 369 ? 9.641   18.071  -23.264 1.00 42.06  ? 398 TRP A CB  1 
ATOM   2900 C CG  . TRP A 1 369 ? 9.448   19.439  -23.866 1.00 44.74  ? 398 TRP A CG  1 
ATOM   2901 C CD1 . TRP A 1 369 ? 9.437   20.640  -23.216 1.00 41.41  ? 398 TRP A CD1 1 
ATOM   2902 C CD2 . TRP A 1 369 ? 9.199   19.728  -25.258 1.00 42.06  ? 398 TRP A CD2 1 
ATOM   2903 N NE1 . TRP A 1 369 ? 9.216   21.656  -24.107 1.00 42.93  ? 398 TRP A NE1 1 
ATOM   2904 C CE2 . TRP A 1 369 ? 9.067   21.131  -25.365 1.00 42.29  ? 398 TRP A CE2 1 
ATOM   2905 C CE3 . TRP A 1 369 ? 9.093   18.945  -26.414 1.00 42.21  ? 398 TRP A CE3 1 
ATOM   2906 C CZ2 . TRP A 1 369 ? 8.829   21.762  -26.583 1.00 41.89  ? 398 TRP A CZ2 1 
ATOM   2907 C CZ3 . TRP A 1 369 ? 8.853   19.570  -27.619 1.00 43.29  ? 398 TRP A CZ3 1 
ATOM   2908 C CH2 . TRP A 1 369 ? 8.724   20.959  -27.698 1.00 44.89  ? 398 TRP A CH2 1 
ATOM   2909 N N   . PRO A 1 370 ? 8.838   14.944  -23.193 1.00 38.81  ? 399 PRO A N   1 
ATOM   2910 C CA  . PRO A 1 370 ? 8.989   13.586  -22.668 1.00 37.26  ? 399 PRO A CA  1 
ATOM   2911 C C   . PRO A 1 370 ? 10.265  13.367  -21.851 1.00 39.06  ? 399 PRO A C   1 
ATOM   2912 O O   . PRO A 1 370 ? 11.272  14.061  -22.019 1.00 38.12  ? 399 PRO A O   1 
ATOM   2913 C CB  . PRO A 1 370 ? 8.938   12.679  -23.913 1.00 37.32  ? 399 PRO A CB  1 
ATOM   2914 C CG  . PRO A 1 370 ? 9.349   13.576  -25.068 1.00 39.97  ? 399 PRO A CG  1 
ATOM   2915 C CD  . PRO A 1 370 ? 9.075   15.020  -24.646 1.00 39.04  ? 399 PRO A CD  1 
ATOM   2916 N N   . ASN A 1 371 ? 10.193  12.379  -20.952 1.00 38.09  ? 400 ASN A N   1 
ATOM   2917 C CA  . ASN A 1 371 ? 11.333  11.964  -20.158 1.00 35.93  ? 400 ASN A CA  1 
ATOM   2918 C C   . ASN A 1 371 ? 11.762  10.583  -20.646 1.00 34.26  ? 400 ASN A C   1 
ATOM   2919 O O   . ASN A 1 371 ? 11.170  10.044  -21.576 1.00 32.96  ? 400 ASN A O   1 
ATOM   2920 C CB  . ASN A 1 371 ? 11.046  12.082  -18.663 1.00 37.52  ? 400 ASN A CB  1 
ATOM   2921 C CG  . ASN A 1 371 ? 9.879   11.239  -18.208 1.00 33.74  ? 400 ASN A CG  1 
ATOM   2922 O OD1 . ASN A 1 371 ? 9.867   10.026  -18.432 1.00 35.92  ? 400 ASN A OD1 1 
ATOM   2923 N ND2 . ASN A 1 371 ? 8.887   11.859  -17.587 1.00 31.16  ? 400 ASN A ND2 1 
ATOM   2924 N N   . VAL A 1 372 ? 12.827  10.059  -20.033 1.00 35.52  ? 401 VAL A N   1 
ATOM   2925 C CA  . VAL A 1 372 ? 13.472  8.818   -20.448 1.00 36.81  ? 401 VAL A CA  1 
ATOM   2926 C C   . VAL A 1 372 ? 12.473  7.656   -20.492 1.00 36.90  ? 401 VAL A C   1 
ATOM   2927 O O   . VAL A 1 372 ? 12.567  6.803   -21.375 1.00 35.55  ? 401 VAL A O   1 
ATOM   2928 C CB  . VAL A 1 372 ? 14.664  8.530   -19.509 1.00 36.30  ? 401 VAL A CB  1 
ATOM   2929 C CG1 . VAL A 1 372 ? 14.244  8.362   -18.054 1.00 36.61  ? 401 VAL A CG1 1 
ATOM   2930 C CG2 . VAL A 1 372 ? 15.486  7.326   -19.958 1.00 38.57  ? 401 VAL A CG2 1 
ATOM   2931 N N   . ASP A 1 373 ? 11.509  7.644   -19.557 1.00 36.11  ? 402 ASP A N   1 
ATOM   2932 C CA  . ASP A 1 373 ? 10.630  6.504   -19.324 1.00 38.17  ? 402 ASP A CA  1 
ATOM   2933 C C   . ASP A 1 373 ? 9.633   6.343   -20.479 1.00 37.65  ? 402 ASP A C   1 
ATOM   2934 O O   . ASP A 1 373 ? 9.113   5.255   -20.725 1.00 38.44  ? 402 ASP A O   1 
ATOM   2935 C CB  . ASP A 1 373 ? 9.972   6.612   -17.951 1.00 41.27  ? 402 ASP A CB  1 
ATOM   2936 C CG  . ASP A 1 373 ? 10.902  6.925   -16.778 1.00 44.73  ? 402 ASP A CG  1 
ATOM   2937 O OD1 . ASP A 1 373 ? 11.819  6.111   -16.507 1.00 45.72  ? 402 ASP A OD1 1 
ATOM   2938 O OD2 . ASP A 1 373 ? 10.709  7.987   -16.134 1.00 40.67  ? 402 ASP A OD2 1 
ATOM   2939 N N   . ALA A 1 374 ? 9.400   7.426   -21.220 1.00 39.30  ? 403 ALA A N   1 
ATOM   2940 C CA  . ALA A 1 374 ? 8.581   7.392   -22.419 1.00 38.28  ? 403 ALA A CA  1 
ATOM   2941 C C   . ALA A 1 374 ? 9.107   6.384   -23.441 1.00 39.34  ? 403 ALA A C   1 
ATOM   2942 O O   . ALA A 1 374 ? 8.319   5.805   -24.190 1.00 39.66  ? 403 ALA A O   1 
ATOM   2943 C CB  . ALA A 1 374 ? 8.510   8.782   -23.014 1.00 38.22  ? 403 ALA A CB  1 
ATOM   2944 N N   . HIS A 1 375 ? 10.428  6.164   -23.487 1.00 38.45  ? 404 HIS A N   1 
ATOM   2945 C CA  . HIS A 1 375 ? 11.019  5.534   -24.662 1.00 38.20  ? 404 HIS A CA  1 
ATOM   2946 C C   . HIS A 1 375 ? 11.614  4.156   -24.370 1.00 36.95  ? 404 HIS A C   1 
ATOM   2947 O O   . HIS A 1 375 ? 11.792  3.375   -25.298 1.00 36.90  ? 404 HIS A O   1 
ATOM   2948 C CB  . HIS A 1 375 ? 12.040  6.479   -25.310 1.00 37.21  ? 404 HIS A CB  1 
ATOM   2949 C CG  . HIS A 1 375 ? 12.019  6.465   -26.801 1.00 35.96  ? 404 HIS A CG  1 
ATOM   2950 N ND1 . HIS A 1 375 ? 12.076  5.306   -27.540 1.00 38.02  ? 404 HIS A ND1 1 
ATOM   2951 C CD2 . HIS A 1 375 ? 11.952  7.463   -27.689 1.00 36.77  ? 404 HIS A CD2 1 
ATOM   2952 C CE1 . HIS A 1 375 ? 12.046  5.607   -28.834 1.00 37.78  ? 404 HIS A CE1 1 
ATOM   2953 N NE2 . HIS A 1 375 ? 11.959  6.912   -28.946 1.00 38.05  ? 404 HIS A NE2 1 
ATOM   2954 N N   . SER A 1 376 ? 11.923  3.838   -23.106 1.00 38.57  ? 405 SER A N   1 
ATOM   2955 C CA  . SER A 1 376 ? 12.756  2.672   -22.819 1.00 38.79  ? 405 SER A CA  1 
ATOM   2956 C C   . SER A 1 376 ? 11.982  1.368   -23.009 1.00 38.84  ? 405 SER A C   1 
ATOM   2957 O O   . SER A 1 376 ? 12.543  0.378   -23.485 1.00 35.82  ? 405 SER A O   1 
ATOM   2958 C CB  . SER A 1 376 ? 13.385  2.745   -21.445 1.00 36.66  ? 405 SER A CB  1 
ATOM   2959 O OG  . SER A 1 376 ? 12.434  3.109   -20.460 1.00 37.60  ? 405 SER A OG  1 
ATOM   2960 N N   . GLY A 1 377 ? 10.694  1.387   -22.643 1.00 38.89  ? 406 GLY A N   1 
ATOM   2961 C CA  . GLY A 1 377 ? 9.853   0.201   -22.652 1.00 39.20  ? 406 GLY A CA  1 
ATOM   2962 C C   . GLY A 1 377 ? 9.732   -0.422  -24.041 1.00 37.70  ? 406 GLY A C   1 
ATOM   2963 O O   . GLY A 1 377 ? 9.813   -1.643  -24.172 1.00 35.92  ? 406 GLY A O   1 
ATOM   2964 N N   . VAL A 1 378 ? 9.526   0.420   -25.064 1.00 39.60  ? 407 VAL A N   1 
ATOM   2965 C CA  . VAL A 1 378 ? 9.271   -0.063  -26.417 1.00 41.14  ? 407 VAL A CA  1 
ATOM   2966 C C   . VAL A 1 378 ? 10.556  -0.653  -26.995 1.00 38.89  ? 407 VAL A C   1 
ATOM   2967 O O   . VAL A 1 378 ? 10.498  -1.584  -27.788 1.00 39.85  ? 407 VAL A O   1 
ATOM   2968 C CB  . VAL A 1 378 ? 8.659   0.977   -27.380 1.00 42.01  ? 407 VAL A CB  1 
ATOM   2969 C CG1 . VAL A 1 378 ? 7.276   1.423   -26.924 1.00 43.74  ? 407 VAL A CG1 1 
ATOM   2970 C CG2 . VAL A 1 378 ? 9.559   2.187   -27.593 1.00 42.70  ? 407 VAL A CG2 1 
ATOM   2971 N N   . LEU A 1 379 ? 11.714  -0.126  -26.581 1.00 40.66  ? 408 LEU A N   1 
ATOM   2972 C CA  . LEU A 1 379 ? 12.990  -0.683  -26.999 1.00 40.42  ? 408 LEU A CA  1 
ATOM   2973 C C   . LEU A 1 379 ? 13.204  -2.041  -26.328 1.00 39.87  ? 408 LEU A C   1 
ATOM   2974 O O   . LEU A 1 379 ? 13.670  -2.986  -26.960 1.00 38.39  ? 408 LEU A O   1 
ATOM   2975 C CB  . LEU A 1 379 ? 14.135  0.284   -26.698 1.00 40.09  ? 408 LEU A CB  1 
ATOM   2976 C CG  . LEU A 1 379 ? 14.138  1.615   -27.460 1.00 42.80  ? 408 LEU A CG  1 
ATOM   2977 C CD1 . LEU A 1 379 ? 15.461  2.324   -27.237 1.00 44.60  ? 408 LEU A CD1 1 
ATOM   2978 C CD2 . LEU A 1 379 ? 13.893  1.485   -28.946 1.00 45.79  ? 408 LEU A CD2 1 
ATOM   2979 N N   . LEU A 1 380 ? 12.858  -2.143  -25.044 1.00 38.82  ? 409 LEU A N   1 
ATOM   2980 C CA  . LEU A 1 380 ? 13.066  -3.383  -24.312 1.00 41.19  ? 409 LEU A CA  1 
ATOM   2981 C C   . LEU A 1 380 ? 12.135  -4.472  -24.842 1.00 42.42  ? 409 LEU A C   1 
ATOM   2982 O O   . LEU A 1 380 ? 12.572  -5.581  -25.135 1.00 41.68  ? 409 LEU A O   1 
ATOM   2983 C CB  . LEU A 1 380 ? 12.851  -3.131  -22.820 1.00 41.58  ? 409 LEU A CB  1 
ATOM   2984 C CG  . LEU A 1 380 ? 13.929  -2.296  -22.120 1.00 39.61  ? 409 LEU A CG  1 
ATOM   2985 C CD1 . LEU A 1 380 ? 13.530  -1.903  -20.700 1.00 37.45  ? 409 LEU A CD1 1 
ATOM   2986 C CD2 . LEU A 1 380 ? 15.240  -3.055  -22.127 1.00 37.65  ? 409 LEU A CD2 1 
ATOM   2987 N N   . GLN A 1 381 ? 10.847  -4.139  -24.965 1.00 47.32  ? 410 GLN A N   1 
ATOM   2988 C CA  . GLN A 1 381 ? 9.847   -5.069  -25.463 1.00 49.25  ? 410 GLN A CA  1 
ATOM   2989 C C   . GLN A 1 381 ? 10.268  -5.617  -26.827 1.00 47.31  ? 410 GLN A C   1 
ATOM   2990 O O   . GLN A 1 381 ? 10.157  -6.815  -27.083 1.00 50.75  ? 410 GLN A O   1 
ATOM   2991 C CB  . GLN A 1 381 ? 8.511   -4.328  -25.484 1.00 54.01  ? 410 GLN A CB  1 
ATOM   2992 C CG  . GLN A 1 381 ? 7.353   -5.134  -26.060 1.00 60.56  ? 410 GLN A CG  1 
ATOM   2993 C CD  . GLN A 1 381 ? 6.034   -4.404  -25.950 1.00 65.85  ? 410 GLN A CD  1 
ATOM   2994 O OE1 . GLN A 1 381 ? 5.499   -3.885  -26.935 1.00 70.86  ? 410 GLN A OE1 1 
ATOM   2995 N NE2 . GLN A 1 381 ? 5.514   -4.333  -24.734 1.00 70.46  ? 410 GLN A NE2 1 
ATOM   2996 N N   . TYR A 1 382 ? 10.789  -4.738  -27.687 1.00 44.54  ? 411 TYR A N   1 
ATOM   2997 C CA  . TYR A 1 382 ? 11.173  -5.100  -29.041 1.00 45.32  ? 411 TYR A CA  1 
ATOM   2998 C C   . TYR A 1 382 ? 12.168  -6.260  -29.076 1.00 43.95  ? 411 TYR A C   1 
ATOM   2999 O O   . TYR A 1 382 ? 12.106  -7.086  -29.981 1.00 43.17  ? 411 TYR A O   1 
ATOM   3000 C CB  . TYR A 1 382 ? 11.786  -3.884  -29.733 1.00 46.59  ? 411 TYR A CB  1 
ATOM   3001 C CG  . TYR A 1 382 ? 12.098  -4.145  -31.195 1.00 48.95  ? 411 TYR A CG  1 
ATOM   3002 C CD1 . TYR A 1 382 ? 11.075  -4.197  -32.131 1.00 52.50  ? 411 TYR A CD1 1 
ATOM   3003 C CD2 . TYR A 1 382 ? 13.402  -4.332  -31.636 1.00 50.19  ? 411 TYR A CD2 1 
ATOM   3004 C CE1 . TYR A 1 382 ? 11.333  -4.434  -33.470 1.00 54.25  ? 411 TYR A CE1 1 
ATOM   3005 C CE2 . TYR A 1 382 ? 13.675  -4.575  -32.973 1.00 54.37  ? 411 TYR A CE2 1 
ATOM   3006 C CZ  . TYR A 1 382 ? 12.636  -4.622  -33.890 1.00 55.85  ? 411 TYR A CZ  1 
ATOM   3007 O OH  . TYR A 1 382 ? 12.863  -4.849  -35.213 1.00 55.30  ? 411 TYR A OH  1 
ATOM   3008 N N   . TYR A 1 383 ? 13.098  -6.319  -28.113 1.00 44.46  ? 412 TYR A N   1 
ATOM   3009 C CA  . TYR A 1 383 ? 14.117  -7.360  -28.115 1.00 44.40  ? 412 TYR A CA  1 
ATOM   3010 C C   . TYR A 1 383 ? 13.649  -8.583  -27.327 1.00 46.83  ? 412 TYR A C   1 
ATOM   3011 O O   . TYR A 1 383 ? 14.411  -9.533  -27.170 1.00 49.16  ? 412 TYR A O   1 
ATOM   3012 C CB  . TYR A 1 383 ? 15.449  -6.800  -27.605 1.00 43.23  ? 412 TYR A CB  1 
ATOM   3013 C CG  . TYR A 1 383 ? 16.061  -5.801  -28.577 1.00 44.25  ? 412 TYR A CG  1 
ATOM   3014 C CD1 . TYR A 1 383 ? 16.686  -6.225  -29.746 1.00 43.92  ? 412 TYR A CD1 1 
ATOM   3015 C CD2 . TYR A 1 383 ? 15.975  -4.431  -28.347 1.00 45.23  ? 412 TYR A CD2 1 
ATOM   3016 C CE1 . TYR A 1 383 ? 17.215  -5.315  -30.649 1.00 45.88  ? 412 TYR A CE1 1 
ATOM   3017 C CE2 . TYR A 1 383 ? 16.498  -3.511  -29.243 1.00 44.83  ? 412 TYR A CE2 1 
ATOM   3018 C CZ  . TYR A 1 383 ? 17.119  -3.954  -30.398 1.00 46.25  ? 412 TYR A CZ  1 
ATOM   3019 O OH  . TYR A 1 383 ? 17.641  -3.044  -31.270 1.00 48.73  ? 412 TYR A OH  1 
ATOM   3020 N N   . GLY A 1 384 ? 12.394  -8.573  -26.859 1.00 49.57  ? 413 GLY A N   1 
ATOM   3021 C CA  . GLY A 1 384 ? 11.819  -9.709  -26.152 1.00 52.17  ? 413 GLY A CA  1 
ATOM   3022 C C   . GLY A 1 384 ? 12.044  -9.624  -24.644 1.00 54.57  ? 413 GLY A C   1 
ATOM   3023 O O   . GLY A 1 384 ? 11.989  -10.639 -23.949 1.00 57.66  ? 413 GLY A O   1 
ATOM   3024 N N   . MET A 1 385 ? 12.314  -8.403  -24.165 1.00 53.66  ? 414 MET A N   1 
ATOM   3025 C CA  . MET A 1 385 ? 12.377  -8.093  -22.746 1.00 55.42  ? 414 MET A CA  1 
ATOM   3026 C C   . MET A 1 385 ? 11.018  -7.510  -22.373 1.00 55.17  ? 414 MET A C   1 
ATOM   3027 O O   . MET A 1 385 ? 10.843  -6.293  -22.331 1.00 53.25  ? 414 MET A O   1 
ATOM   3028 C CB  . MET A 1 385 ? 13.540  -7.124  -22.481 1.00 58.03  ? 414 MET A CB  1 
ATOM   3029 C CG  . MET A 1 385 ? 13.609  -6.518  -21.092 1.00 59.13  ? 414 MET A CG  1 
ATOM   3030 S SD  . MET A 1 385 ? 14.014  -7.678  -19.775 1.00 60.31  ? 414 MET A SD  1 
ATOM   3031 C CE  . MET A 1 385 ? 15.741  -8.044  -20.107 1.00 60.22  ? 414 MET A CE  1 
ATOM   3032 N N   . THR A 1 386 ? 10.040  -8.401  -22.177 1.00 55.28  ? 415 THR A N   1 
ATOM   3033 C CA  . THR A 1 386 ? 8.647   -7.990  -22.090 1.00 56.38  ? 415 THR A CA  1 
ATOM   3034 C C   . THR A 1 386 ? 8.135   -8.128  -20.657 1.00 54.50  ? 415 THR A C   1 
ATOM   3035 O O   . THR A 1 386 ? 6.964   -7.847  -20.417 1.00 55.50  ? 415 THR A O   1 
ATOM   3036 C CB  . THR A 1 386 ? 7.795   -8.804  -23.068 1.00 58.56  ? 415 THR A CB  1 
ATOM   3037 O OG1 . THR A 1 386 ? 7.770   -10.139 -22.576 1.00 63.35  ? 415 THR A OG1 1 
ATOM   3038 C CG2 . THR A 1 386 ? 8.352   -8.809  -24.481 1.00 57.36  ? 415 THR A CG2 1 
ATOM   3039 N N   . GLU A 1 387 ? 9.007   -8.538  -19.720 1.00 53.00  ? 416 GLU A N   1 
ATOM   3040 C CA  . GLU A 1 387 ? 8.641   -8.671  -18.314 1.00 54.32  ? 416 GLU A CA  1 
ATOM   3041 C C   . GLU A 1 387 ? 8.722   -7.300  -17.641 1.00 50.36  ? 416 GLU A C   1 
ATOM   3042 O O   . GLU A 1 387 ? 9.778   -6.909  -17.156 1.00 50.25  ? 416 GLU A O   1 
ATOM   3043 C CB  . GLU A 1 387 ? 9.543   -9.663  -17.574 1.00 54.15  ? 416 GLU A CB  1 
ATOM   3044 C CG  . GLU A 1 387 ? 9.535   -11.077 -18.154 1.00 55.34  ? 416 GLU A CG  1 
ATOM   3045 C CD  . GLU A 1 387 ? 10.327  -11.289 -19.438 1.00 54.77  ? 416 GLU A CD  1 
ATOM   3046 O OE1 . GLU A 1 387 ? 10.257  -12.408 -19.991 1.00 56.30  ? 416 GLU A OE1 1 
ATOM   3047 O OE2 . GLU A 1 387 ? 11.020  -10.351 -19.885 1.00 50.73  ? 416 GLU A OE2 1 
ATOM   3048 N N   . MET A 1 388 ? 7.591   -6.583  -17.596 1.00 48.99  ? 417 MET A N   1 
ATOM   3049 C CA  . MET A 1 388 ? 7.574   -5.182  -17.192 1.00 49.20  ? 417 MET A CA  1 
ATOM   3050 C C   . MET A 1 388 ? 8.051   -4.990  -15.752 1.00 46.34  ? 417 MET A C   1 
ATOM   3051 O O   . MET A 1 388 ? 8.670   -3.972  -15.440 1.00 43.29  ? 417 MET A O   1 
ATOM   3052 C CB  . MET A 1 388 ? 6.169   -4.587  -17.314 1.00 50.68  ? 417 MET A CB  1 
ATOM   3053 C CG  . MET A 1 388 ? 5.624   -4.623  -18.720 1.00 55.34  ? 417 MET A CG  1 
ATOM   3054 S SD  . MET A 1 388 ? 4.385   -3.346  -18.998 1.00 58.80  ? 417 MET A SD  1 
ATOM   3055 C CE  . MET A 1 388 ? 3.648   -4.065  -20.472 1.00 66.39  ? 417 MET A CE  1 
ATOM   3056 N N   . ASN A 1 389 ? 7.734   -5.946  -14.872 1.00 44.87  ? 418 ASN A N   1 
ATOM   3057 C CA  . ASN A 1 389 ? 8.092   -5.844  -13.465 1.00 47.12  ? 418 ASN A CA  1 
ATOM   3058 C C   . ASN A 1 389 ? 9.607   -5.760  -13.304 1.00 45.77  ? 418 ASN A C   1 
ATOM   3059 O O   . ASN A 1 389 ? 10.095  -5.054  -12.421 1.00 50.70  ? 418 ASN A O   1 
ATOM   3060 C CB  . ASN A 1 389 ? 7.512   -6.990  -12.645 1.00 46.85  ? 418 ASN A CB  1 
ATOM   3061 C CG  . ASN A 1 389 ? 6.084   -6.712  -12.248 1.00 48.49  ? 418 ASN A CG  1 
ATOM   3062 O OD1 . ASN A 1 389 ? 5.826   -5.745  -11.521 1.00 52.30  ? 418 ASN A OD1 1 
ATOM   3063 N ND2 . ASN A 1 389 ? 5.148   -7.525  -12.713 1.00 51.88  ? 418 ASN A ND2 1 
ATOM   3064 N N   . TYR A 1 390 ? 10.329  -6.461  -14.187 1.00 42.07  ? 419 TYR A N   1 
ATOM   3065 C CA  . TYR A 1 390 ? 11.775  -6.554  -14.121 1.00 39.24  ? 419 TYR A CA  1 
ATOM   3066 C C   . TYR A 1 390 ? 12.451  -5.250  -14.553 1.00 41.19  ? 419 TYR A C   1 
ATOM   3067 O O   . TYR A 1 390 ? 13.586  -4.987  -14.157 1.00 39.26  ? 419 TYR A O   1 
ATOM   3068 C CB  . TYR A 1 390 ? 12.213  -7.733  -14.992 1.00 36.46  ? 419 TYR A CB  1 
ATOM   3069 C CG  . TYR A 1 390 ? 13.698  -8.013  -14.836 1.00 35.04  ? 419 TYR A CG  1 
ATOM   3070 C CD1 . TYR A 1 390 ? 14.197  -8.603  -13.682 1.00 34.61  ? 419 TYR A CD1 1 
ATOM   3071 C CD2 . TYR A 1 390 ? 14.602  -7.635  -15.815 1.00 35.05  ? 419 TYR A CD2 1 
ATOM   3072 C CE1 . TYR A 1 390 ? 15.553  -8.830  -13.518 1.00 35.00  ? 419 TYR A CE1 1 
ATOM   3073 C CE2 . TYR A 1 390 ? 15.960  -7.858  -15.663 1.00 34.44  ? 419 TYR A CE2 1 
ATOM   3074 C CZ  . TYR A 1 390 ? 16.435  -8.461  -14.514 1.00 34.42  ? 419 TYR A CZ  1 
ATOM   3075 O OH  . TYR A 1 390 ? 17.770  -8.689  -14.377 1.00 36.33  ? 419 TYR A OH  1 
ATOM   3076 N N   . TYR A 1 391 ? 11.768  -4.436  -15.370 1.00 40.46  ? 420 TYR A N   1 
ATOM   3077 C CA  . TYR A 1 391 ? 12.390  -3.271  -15.980 1.00 38.50  ? 420 TYR A CA  1 
ATOM   3078 C C   . TYR A 1 391 ? 13.178  -2.479  -14.936 1.00 39.32  ? 420 TYR A C   1 
ATOM   3079 O O   . TYR A 1 391 ? 14.282  -2.032  -15.232 1.00 38.70  ? 420 TYR A O   1 
ATOM   3080 C CB  . TYR A 1 391 ? 11.372  -2.386  -16.710 1.00 38.84  ? 420 TYR A CB  1 
ATOM   3081 C CG  . TYR A 1 391 ? 10.775  -2.961  -17.993 1.00 36.67  ? 420 TYR A CG  1 
ATOM   3082 C CD1 . TYR A 1 391 ? 11.270  -4.126  -18.570 1.00 37.68  ? 420 TYR A CD1 1 
ATOM   3083 C CD2 . TYR A 1 391 ? 9.741   -2.309  -18.654 1.00 34.93  ? 420 TYR A CD2 1 
ATOM   3084 C CE1 . TYR A 1 391 ? 10.739  -4.633  -19.745 1.00 37.64  ? 420 TYR A CE1 1 
ATOM   3085 C CE2 . TYR A 1 391 ? 9.204   -2.801  -19.834 1.00 35.23  ? 420 TYR A CE2 1 
ATOM   3086 C CZ  . TYR A 1 391 ? 9.707   -3.968  -20.382 1.00 36.18  ? 420 TYR A CZ  1 
ATOM   3087 O OH  . TYR A 1 391 ? 9.202   -4.480  -21.541 1.00 38.48  ? 420 TYR A OH  1 
ATOM   3088 N N   . THR A 1 392 ? 12.643  -2.334  -13.714 1.00 37.00  ? 421 THR A N   1 
ATOM   3089 C CA  . THR A 1 392 ? 13.275  -1.471  -12.722 1.00 34.85  ? 421 THR A CA  1 
ATOM   3090 C C   . THR A 1 392 ? 14.602  -2.062  -12.241 1.00 33.35  ? 421 THR A C   1 
ATOM   3091 O O   . THR A 1 392 ? 15.468  -1.324  -11.777 1.00 34.00  ? 421 THR A O   1 
ATOM   3092 C CB  . THR A 1 392 ? 12.345  -1.198  -11.541 1.00 33.91  ? 421 THR A CB  1 
ATOM   3093 O OG1 . THR A 1 392 ? 11.039  -0.951  -12.051 1.00 31.20  ? 421 THR A OG1 1 
ATOM   3094 C CG2 . THR A 1 392 ? 12.811  -0.001  -10.729 1.00 35.97  ? 421 THR A CG2 1 
ATOM   3095 N N   . VAL A 1 393 ? 14.759  -3.386  -12.328 1.00 32.86  ? 422 VAL A N   1 
ATOM   3096 C CA  . VAL A 1 393 ? 16.032  -4.017  -12.018 1.00 31.02  ? 422 VAL A CA  1 
ATOM   3097 C C   . VAL A 1 393 ? 17.116  -3.487  -12.955 1.00 28.65  ? 422 VAL A C   1 
ATOM   3098 O O   . VAL A 1 393 ? 18.239  -3.254  -12.524 1.00 28.08  ? 422 VAL A O   1 
ATOM   3099 C CB  . VAL A 1 393 ? 15.923  -5.552  -12.077 1.00 32.90  ? 422 VAL A CB  1 
ATOM   3100 C CG1 . VAL A 1 393 ? 17.285  -6.234  -12.036 1.00 32.18  ? 422 VAL A CG1 1 
ATOM   3101 C CG2 . VAL A 1 393 ? 15.021  -6.075  -10.968 1.00 33.28  ? 422 VAL A CG2 1 
ATOM   3102 N N   . LEU A 1 394 ? 16.783  -3.264  -14.228 1.00 29.64  ? 423 LEU A N   1 
ATOM   3103 C CA  . LEU A 1 394 ? 17.758  -2.741  -15.174 1.00 32.30  ? 423 LEU A CA  1 
ATOM   3104 C C   . LEU A 1 394 ? 18.176  -1.337  -14.751 1.00 30.65  ? 423 LEU A C   1 
ATOM   3105 O O   . LEU A 1 394 ? 19.364  -1.021  -14.715 1.00 28.59  ? 423 LEU A O   1 
ATOM   3106 C CB  . LEU A 1 394 ? 17.217  -2.733  -16.601 1.00 34.14  ? 423 LEU A CB  1 
ATOM   3107 C CG  . LEU A 1 394 ? 16.993  -4.104  -17.245 1.00 37.41  ? 423 LEU A CG  1 
ATOM   3108 C CD1 . LEU A 1 394 ? 16.363  -3.948  -18.623 1.00 37.67  ? 423 LEU A CD1 1 
ATOM   3109 C CD2 . LEU A 1 394 ? 18.301  -4.875  -17.324 1.00 38.67  ? 423 LEU A CD2 1 
ATOM   3110 N N   . PHE A 1 395 ? 17.174  -0.503  -14.459 1.00 31.81  ? 424 PHE A N   1 
ATOM   3111 C CA  . PHE A 1 395 ? 17.393  0.859   -14.005 1.00 32.15  ? 424 PHE A CA  1 
ATOM   3112 C C   . PHE A 1 395 ? 18.361  0.828   -12.829 1.00 31.44  ? 424 PHE A C   1 
ATOM   3113 O O   . PHE A 1 395 ? 19.371  1.524   -12.849 1.00 32.25  ? 424 PHE A O   1 
ATOM   3114 C CB  . PHE A 1 395 ? 16.022  1.457   -13.669 1.00 35.67  ? 424 PHE A CB  1 
ATOM   3115 C CG  . PHE A 1 395 ? 15.910  2.979   -13.631 1.00 37.32  ? 424 PHE A CG  1 
ATOM   3116 C CD1 . PHE A 1 395 ? 16.940  3.780   -13.142 1.00 36.17  ? 424 PHE A CD1 1 
ATOM   3117 C CD2 . PHE A 1 395 ? 14.750  3.608   -14.085 1.00 38.39  ? 424 PHE A CD2 1 
ATOM   3118 C CE1 . PHE A 1 395 ? 16.806  5.161   -13.099 1.00 36.49  ? 424 PHE A CE1 1 
ATOM   3119 C CE2 . PHE A 1 395 ? 14.628  4.992   -14.043 1.00 39.93  ? 424 PHE A CE2 1 
ATOM   3120 C CZ  . PHE A 1 395 ? 15.658  5.764   -13.553 1.00 37.05  ? 424 PHE A CZ  1 
ATOM   3121 N N   . GLY A 1 396 ? 18.071  -0.041  -11.850 1.00 30.95  ? 425 GLY A N   1 
ATOM   3122 C CA  . GLY A 1 396 ? 18.812  -0.105  -10.599 1.00 31.02  ? 425 GLY A CA  1 
ATOM   3123 C C   . GLY A 1 396 ? 20.281  -0.489  -10.778 1.00 31.19  ? 425 GLY A C   1 
ATOM   3124 O O   . GLY A 1 396 ? 21.154  0.089   -10.128 1.00 29.93  ? 425 GLY A O   1 
ATOM   3125 N N   . VAL A 1 397 ? 20.536  -1.494  -11.628 1.00 30.23  ? 426 VAL A N   1 
ATOM   3126 C CA  . VAL A 1 397 ? 21.887  -1.924  -11.945 1.00 29.14  ? 426 VAL A CA  1 
ATOM   3127 C C   . VAL A 1 397 ? 22.649  -0.751  -12.548 1.00 29.40  ? 426 VAL A C   1 
ATOM   3128 O O   . VAL A 1 397 ? 23.846  -0.613  -12.307 1.00 31.20  ? 426 VAL A O   1 
ATOM   3129 C CB  . VAL A 1 397 ? 21.909  -3.134  -12.901 1.00 30.70  ? 426 VAL A CB  1 
ATOM   3130 C CG1 . VAL A 1 397 ? 23.259  -3.294  -13.605 1.00 30.53  ? 426 VAL A CG1 1 
ATOM   3131 C CG2 . VAL A 1 397 ? 21.510  -4.423  -12.189 1.00 30.74  ? 426 VAL A CG2 1 
ATOM   3132 N N   . SER A 1 398 ? 21.954  0.046   -13.372 1.00 27.84  ? 427 SER A N   1 
ATOM   3133 C CA  . SER A 1 398 ? 22.543  1.214   -14.001 1.00 26.67  ? 427 SER A CA  1 
ATOM   3134 C C   . SER A 1 398 ? 22.904  2.261   -12.957 1.00 27.28  ? 427 SER A C   1 
ATOM   3135 O O   . SER A 1 398 ? 24.015  2.782   -12.973 1.00 28.72  ? 427 SER A O   1 
ATOM   3136 C CB  . SER A 1 398 ? 21.631  1.817   -15.018 1.00 27.21  ? 427 SER A CB  1 
ATOM   3137 O OG  . SER A 1 398 ? 22.186  3.025   -15.511 1.00 26.06  ? 427 SER A OG  1 
ATOM   3138 N N   . ARG A 1 399 ? 21.964  2.537   -12.045 1.00 26.50  ? 428 ARG A N   1 
ATOM   3139 C CA  . ARG A 1 399 ? 22.081  3.662   -11.124 1.00 25.99  ? 428 ARG A CA  1 
ATOM   3140 C C   . ARG A 1 399 ? 23.195  3.397   -10.114 1.00 27.59  ? 428 ARG A C   1 
ATOM   3141 O O   . ARG A 1 399 ? 23.647  4.330   -9.449  1.00 29.74  ? 428 ARG A O   1 
ATOM   3142 C CB  . ARG A 1 399 ? 20.720  3.932   -10.467 1.00 24.10  ? 428 ARG A CB  1 
ATOM   3143 C CG  . ARG A 1 399 ? 20.626  5.091   -9.480  1.00 25.00  ? 428 ARG A CG  1 
ATOM   3144 C CD  . ARG A 1 399 ? 21.088  6.430   -10.022 1.00 24.07  ? 428 ARG A CD  1 
ATOM   3145 N NE  . ARG A 1 399 ? 20.488  6.710   -11.330 1.00 26.15  ? 428 ARG A NE  1 
ATOM   3146 C CZ  . ARG A 1 399 ? 19.517  7.578   -11.598 1.00 27.69  ? 428 ARG A CZ  1 
ATOM   3147 N NH1 . ARG A 1 399 ? 18.940  8.262   -10.626 1.00 28.16  ? 428 ARG A NH1 1 
ATOM   3148 N NH2 . ARG A 1 399 ? 19.130  7.770   -12.849 1.00 28.04  ? 428 ARG A NH2 1 
ATOM   3149 N N   . ALA A 1 400 ? 23.614  2.129   -9.992  1.00 28.89  ? 429 ALA A N   1 
ATOM   3150 C CA  . ALA A 1 400 ? 24.709  1.742   -9.115  1.00 31.77  ? 429 ALA A CA  1 
ATOM   3151 C C   . ALA A 1 400 ? 26.005  2.442   -9.517  1.00 31.19  ? 429 ALA A C   1 
ATOM   3152 O O   . ALA A 1 400 ? 26.831  2.746   -8.662  1.00 31.80  ? 429 ALA A O   1 
ATOM   3153 C CB  . ALA A 1 400 ? 24.888  0.235   -9.142  1.00 34.36  ? 429 ALA A CB  1 
ATOM   3154 N N   . LEU A 1 401 ? 26.182  2.697   -10.816 1.00 31.91  ? 430 LEU A N   1 
ATOM   3155 C CA  . LEU A 1 401 ? 27.391  3.346   -11.299 1.00 33.18  ? 430 LEU A CA  1 
ATOM   3156 C C   . LEU A 1 401 ? 27.469  4.774   -10.772 1.00 33.21  ? 430 LEU A C   1 
ATOM   3157 O O   . LEU A 1 401 ? 28.551  5.221   -10.395 1.00 33.88  ? 430 LEU A O   1 
ATOM   3158 C CB  . LEU A 1 401 ? 27.423  3.322   -12.823 1.00 34.52  ? 430 LEU A CB  1 
ATOM   3159 C CG  . LEU A 1 401 ? 27.441  1.928   -13.449 1.00 36.09  ? 430 LEU A CG  1 
ATOM   3160 C CD1 . LEU A 1 401 ? 27.480  2.060   -14.967 1.00 37.37  ? 430 LEU A CD1 1 
ATOM   3161 C CD2 . LEU A 1 401 ? 28.604  1.103   -12.921 1.00 33.84  ? 430 LEU A CD2 1 
ATOM   3162 N N   . GLY A 1 402 ? 26.324  5.472   -10.750 1.00 28.44  ? 431 GLY A N   1 
ATOM   3163 C CA  . GLY A 1 402 ? 26.288  6.875   -10.367 1.00 29.50  ? 431 GLY A CA  1 
ATOM   3164 C C   . GLY A 1 402 ? 26.402  7.066   -8.854  1.00 30.77  ? 431 GLY A C   1 
ATOM   3165 O O   . GLY A 1 402 ? 27.186  7.883   -8.368  1.00 30.90  ? 431 GLY A O   1 
ATOM   3166 N N   . VAL A 1 403 ? 25.614  6.290   -8.105  1.00 30.34  ? 432 VAL A N   1 
ATOM   3167 C CA  . VAL A 1 403 ? 25.469  6.527   -6.686  1.00 28.64  ? 432 VAL A CA  1 
ATOM   3168 C C   . VAL A 1 403 ? 26.696  6.016   -5.937  1.00 28.68  ? 432 VAL A C   1 
ATOM   3169 O O   . VAL A 1 403 ? 27.008  6.538   -4.879  1.00 28.49  ? 432 VAL A O   1 
ATOM   3170 C CB  . VAL A 1 403 ? 24.147  5.939   -6.161  1.00 27.60  ? 432 VAL A CB  1 
ATOM   3171 C CG1 . VAL A 1 403 ? 22.977  6.484   -6.973  1.00 28.58  ? 432 VAL A CG1 1 
ATOM   3172 C CG2 . VAL A 1 403 ? 24.140  4.415   -6.127  1.00 28.23  ? 432 VAL A CG2 1 
ATOM   3173 N N   . LEU A 1 404 ? 27.415  5.039   -6.502  1.00 28.30  ? 433 LEU A N   1 
ATOM   3174 C CA  . LEU A 1 404 ? 28.616  4.507   -5.872  1.00 28.60  ? 433 LEU A CA  1 
ATOM   3175 C C   . LEU A 1 404 ? 29.851  5.304   -6.293  1.00 28.60  ? 433 LEU A C   1 
ATOM   3176 O O   . LEU A 1 404 ? 30.782  5.454   -5.503  1.00 31.66  ? 433 LEU A O   1 
ATOM   3177 C CB  . LEU A 1 404 ? 28.769  3.014   -6.172  1.00 29.49  ? 433 LEU A CB  1 
ATOM   3178 C CG  . LEU A 1 404 ? 27.674  2.110   -5.597  1.00 30.44  ? 433 LEU A CG  1 
ATOM   3179 C CD1 . LEU A 1 404 ? 27.779  0.709   -6.148  1.00 32.00  ? 433 LEU A CD1 1 
ATOM   3180 C CD2 . LEU A 1 404 ? 27.732  2.079   -4.086  1.00 33.34  ? 433 LEU A CD2 1 
ATOM   3181 N N   . ALA A 1 405 ? 29.879  5.818   -7.526  1.00 27.65  ? 434 ALA A N   1 
ATOM   3182 C CA  . ALA A 1 405 ? 30.864  6.823   -7.870  1.00 28.78  ? 434 ALA A CA  1 
ATOM   3183 C C   . ALA A 1 405 ? 30.808  7.950   -6.841  1.00 30.64  ? 434 ALA A C   1 
ATOM   3184 O O   . ALA A 1 405 ? 31.834  8.338   -6.272  1.00 30.40  ? 434 ALA A O   1 
ATOM   3185 C CB  . ALA A 1 405 ? 30.643  7.356   -9.267  1.00 30.25  ? 434 ALA A CB  1 
ATOM   3186 N N   . GLN A 1 406 ? 29.606  8.472   -6.588  1.00 28.90  ? 435 GLN A N   1 
ATOM   3187 C CA  . GLN A 1 406 ? 29.498  9.623   -5.701  1.00 31.34  ? 435 GLN A CA  1 
ATOM   3188 C C   . GLN A 1 406 ? 29.915  9.230   -4.285  1.00 32.08  ? 435 GLN A C   1 
ATOM   3189 O O   . GLN A 1 406 ? 30.619  9.983   -3.616  1.00 32.40  ? 435 GLN A O   1 
ATOM   3190 C CB  . GLN A 1 406 ? 28.102  10.240  -5.712  1.00 31.80  ? 435 GLN A CB  1 
ATOM   3191 C CG  . GLN A 1 406 ? 27.902  11.356  -4.695  1.00 33.01  ? 435 GLN A CG  1 
ATOM   3192 C CD  . GLN A 1 406 ? 28.882  12.493  -4.865  1.00 35.52  ? 435 GLN A CD  1 
ATOM   3193 O OE1 . GLN A 1 406 ? 29.157  12.938  -5.984  1.00 39.97  ? 435 GLN A OE1 1 
ATOM   3194 N NE2 . GLN A 1 406 ? 29.450  12.947  -3.757  1.00 37.27  ? 435 GLN A NE2 1 
ATOM   3195 N N   . LEU A 1 407 ? 29.494  8.036   -3.853  1.00 32.24  ? 436 LEU A N   1 
ATOM   3196 C CA  . LEU A 1 407 ? 29.681  7.597   -2.478  1.00 30.98  ? 436 LEU A CA  1 
ATOM   3197 C C   . LEU A 1 407 ? 31.170  7.540   -2.119  1.00 29.20  ? 436 LEU A C   1 
ATOM   3198 O O   . LEU A 1 407 ? 31.566  7.888   -1.008  1.00 28.39  ? 436 LEU A O   1 
ATOM   3199 C CB  . LEU A 1 407 ? 28.993  6.243   -2.306  1.00 31.08  ? 436 LEU A CB  1 
ATOM   3200 C CG  . LEU A 1 407 ? 28.925  5.713   -0.873  1.00 33.68  ? 436 LEU A CG  1 
ATOM   3201 C CD1 . LEU A 1 407 ? 28.004  6.614   -0.062  1.00 34.49  ? 436 LEU A CD1 1 
ATOM   3202 C CD2 . LEU A 1 407 ? 28.485  4.251   -0.804  1.00 32.87  ? 436 LEU A CD2 1 
ATOM   3203 N N   . ILE A 1 408 ? 32.001  7.112   -3.074  1.00 28.68  ? 437 ILE A N   1 
ATOM   3204 C CA  . ILE A 1 408 ? 33.444  7.129   -2.902  1.00 28.03  ? 437 ILE A CA  1 
ATOM   3205 C C   . ILE A 1 408 ? 33.918  8.547   -2.599  1.00 30.23  ? 437 ILE A C   1 
ATOM   3206 O O   . ILE A 1 408 ? 34.762  8.728   -1.729  1.00 34.67  ? 437 ILE A O   1 
ATOM   3207 C CB  . ILE A 1 408 ? 34.146  6.579   -4.154  1.00 28.89  ? 437 ILE A CB  1 
ATOM   3208 C CG1 . ILE A 1 408 ? 33.839  5.091   -4.378  1.00 27.31  ? 437 ILE A CG1 1 
ATOM   3209 C CG2 . ILE A 1 408 ? 35.652  6.836   -4.084  1.00 29.27  ? 437 ILE A CG2 1 
ATOM   3210 C CD1 . ILE A 1 408 ? 34.088  4.635   -5.803  1.00 27.46  ? 437 ILE A CD1 1 
ATOM   3211 N N   . TRP A 1 409 ? 33.400  9.532   -3.343  1.00 29.79  ? 438 TRP A N   1 
ATOM   3212 C CA  . TRP A 1 409 ? 33.832  10.913  -3.214  1.00 31.56  ? 438 TRP A CA  1 
ATOM   3213 C C   . TRP A 1 409 ? 33.267  11.572  -1.959  1.00 30.85  ? 438 TRP A C   1 
ATOM   3214 O O   . TRP A 1 409 ? 33.953  12.397  -1.369  1.00 35.36  ? 438 TRP A O   1 
ATOM   3215 C CB  . TRP A 1 409 ? 33.500  11.725  -4.476  1.00 32.40  ? 438 TRP A CB  1 
ATOM   3216 C CG  . TRP A 1 409 ? 34.512  11.512  -5.571  1.00 33.28  ? 438 TRP A CG  1 
ATOM   3217 C CD1 . TRP A 1 409 ? 34.406  10.677  -6.647  1.00 34.80  ? 438 TRP A CD1 1 
ATOM   3218 C CD2 . TRP A 1 409 ? 35.824  12.106  -5.652  1.00 34.78  ? 438 TRP A CD2 1 
ATOM   3219 N NE1 . TRP A 1 409 ? 35.548  10.725  -7.402  1.00 34.96  ? 438 TRP A NE1 1 
ATOM   3220 C CE2 . TRP A 1 409 ? 36.435  11.593  -6.819  1.00 37.52  ? 438 TRP A CE2 1 
ATOM   3221 C CE3 . TRP A 1 409 ? 36.531  13.027  -4.871  1.00 36.93  ? 438 TRP A CE3 1 
ATOM   3222 C CZ2 . TRP A 1 409 ? 37.719  11.972  -7.211  1.00 37.14  ? 438 TRP A CZ2 1 
ATOM   3223 C CZ3 . TRP A 1 409 ? 37.799  13.401  -5.263  1.00 37.25  ? 438 TRP A CZ3 1 
ATOM   3224 C CH2 . TRP A 1 409 ? 38.385  12.873  -6.412  1.00 37.26  ? 438 TRP A CH2 1 
ATOM   3225 N N   . SER A 1 410 ? 32.043  11.223  -1.544  1.00 30.45  ? 439 SER A N   1 
ATOM   3226 C CA  . SER A 1 410 ? 31.493  11.736  -0.292  1.00 29.21  ? 439 SER A CA  1 
ATOM   3227 C C   . SER A 1 410 ? 32.355  11.293  0.894   1.00 29.51  ? 439 SER A C   1 
ATOM   3228 O O   . SER A 1 410 ? 32.518  12.039  1.862   1.00 30.32  ? 439 SER A O   1 
ATOM   3229 C CB  . SER A 1 410 ? 30.056  11.312  -0.086  1.00 29.03  ? 439 SER A CB  1 
ATOM   3230 O OG  . SER A 1 410 ? 29.278  11.555  -1.250  1.00 28.09  ? 439 SER A OG  1 
ATOM   3231 N N   . ARG A 1 411 ? 32.903  10.075  0.826   1.00 29.72  ? 440 ARG A N   1 
ATOM   3232 C CA  . ARG A 1 411 ? 33.733  9.566   1.907   1.00 32.72  ? 440 ARG A CA  1 
ATOM   3233 C C   . ARG A 1 411 ? 35.166  10.084  1.775   1.00 32.98  ? 440 ARG A C   1 
ATOM   3234 O O   . ARG A 1 411 ? 35.830  10.254  2.791   1.00 33.57  ? 440 ARG A O   1 
ATOM   3235 C CB  . ARG A 1 411 ? 33.655  8.038   2.019   1.00 33.44  ? 440 ARG A CB  1 
ATOM   3236 C CG  . ARG A 1 411 ? 32.281  7.497   2.404   1.00 31.31  ? 440 ARG A CG  1 
ATOM   3237 C CD  . ARG A 1 411 ? 31.855  7.849   3.818   1.00 32.59  ? 440 ARG A CD  1 
ATOM   3238 N NE  . ARG A 1 411 ? 31.335  9.218   3.954   1.00 33.21  ? 440 ARG A NE  1 
ATOM   3239 C CZ  . ARG A 1 411 ? 30.176  9.680   3.490   1.00 31.73  ? 440 ARG A CZ  1 
ATOM   3240 N NH1 . ARG A 1 411 ? 29.376  8.910   2.779   1.00 32.80  ? 440 ARG A NH1 1 
ATOM   3241 N NH2 . ARG A 1 411 ? 29.821  10.928  3.733   1.00 32.34  ? 440 ARG A NH2 1 
ATOM   3242 N N   . ALA A 1 412 ? 35.634  10.342  0.544   1.00 33.24  ? 441 ALA A N   1 
ATOM   3243 C CA  . ALA A 1 412 ? 36.981  10.861  0.328   1.00 35.74  ? 441 ALA A CA  1 
ATOM   3244 C C   . ALA A 1 412 ? 37.053  12.329  0.732   1.00 36.60  ? 441 ALA A C   1 
ATOM   3245 O O   . ALA A 1 412 ? 38.092  12.805  1.196   1.00 33.71  ? 441 ALA A O   1 
ATOM   3246 C CB  . ALA A 1 412 ? 37.393  10.697  -1.112  1.00 38.53  ? 441 ALA A CB  1 
ATOM   3247 N N   . LEU A 1 413 ? 35.932  13.039  0.567   1.00 34.06  ? 442 LEU A N   1 
ATOM   3248 C CA  . LEU A 1 413 ? 35.878  14.442  0.935   1.00 34.61  ? 442 LEU A CA  1 
ATOM   3249 C C   . LEU A 1 413 ? 35.365  14.613  2.359   1.00 33.71  ? 442 LEU A C   1 
ATOM   3250 O O   . LEU A 1 413 ? 35.194  15.741  2.811   1.00 34.18  ? 442 LEU A O   1 
ATOM   3251 C CB  . LEU A 1 413 ? 35.000  15.155  -0.084  1.00 34.88  ? 442 LEU A CB  1 
ATOM   3252 C CG  . LEU A 1 413 ? 35.523  15.105  -1.520  1.00 34.08  ? 442 LEU A CG  1 
ATOM   3253 C CD1 . LEU A 1 413 ? 34.484  15.639  -2.485  1.00 33.87  ? 442 LEU A CD1 1 
ATOM   3254 C CD2 . LEU A 1 413 ? 36.842  15.868  -1.618  1.00 35.49  ? 442 LEU A CD2 1 
ATOM   3255 N N   . GLY A 1 414 ? 35.126  13.493  3.053   1.00 33.05  ? 443 GLY A N   1 
ATOM   3256 C CA  . GLY A 1 414 ? 34.636  13.523  4.421   1.00 32.89  ? 443 GLY A CA  1 
ATOM   3257 C C   . GLY A 1 414 ? 33.364  14.354  4.578   1.00 31.89  ? 443 GLY A C   1 
ATOM   3258 O O   . GLY A 1 414 ? 33.265  15.148  5.504   1.00 30.56  ? 443 GLY A O   1 
ATOM   3259 N N   . PHE A 1 415 ? 32.385  14.168  3.680   1.00 33.66  ? 444 PHE A N   1 
ATOM   3260 C CA  . PHE A 1 415 ? 31.073  14.770  3.876   1.00 33.32  ? 444 PHE A CA  1 
ATOM   3261 C C   . PHE A 1 415 ? 30.497  14.177  5.157   1.00 33.62  ? 444 PHE A C   1 
ATOM   3262 O O   . PHE A 1 415 ? 30.673  12.987  5.420   1.00 34.40  ? 444 PHE A O   1 
ATOM   3263 C CB  . PHE A 1 415 ? 30.084  14.554  2.728   1.00 33.28  ? 444 PHE A CB  1 
ATOM   3264 C CG  . PHE A 1 415 ? 30.388  15.267  1.416   1.00 36.92  ? 444 PHE A CG  1 
ATOM   3265 C CD1 . PHE A 1 415 ? 31.548  16.017  1.240   1.00 37.74  ? 444 PHE A CD1 1 
ATOM   3266 C CD2 . PHE A 1 415 ? 29.515  15.147  0.339   1.00 39.79  ? 444 PHE A CD2 1 
ATOM   3267 C CE1 . PHE A 1 415 ? 31.806  16.652  0.035   1.00 38.52  ? 444 PHE A CE1 1 
ATOM   3268 C CE2 . PHE A 1 415 ? 29.780  15.778  -0.867  1.00 40.44  ? 444 PHE A CE2 1 
ATOM   3269 C CZ  . PHE A 1 415 ? 30.926  16.524  -1.017  1.00 41.57  ? 444 PHE A CZ  1 
ATOM   3270 N N   . PRO A 1 416 ? 29.835  14.991  6.008   1.00 33.73  ? 445 PRO A N   1 
ATOM   3271 C CA  . PRO A 1 416 ? 29.306  14.506  7.281   1.00 34.46  ? 445 PRO A CA  1 
ATOM   3272 C C   . PRO A 1 416 ? 27.840  14.091  7.234   1.00 34.59  ? 445 PRO A C   1 
ATOM   3273 O O   . PRO A 1 416 ? 27.173  14.253  6.216   1.00 35.75  ? 445 PRO A O   1 
ATOM   3274 C CB  . PRO A 1 416 ? 29.519  15.762  8.132   1.00 34.05  ? 445 PRO A CB  1 
ATOM   3275 C CG  . PRO A 1 416 ? 29.112  16.875  7.189   1.00 36.02  ? 445 PRO A CG  1 
ATOM   3276 C CD  . PRO A 1 416 ? 29.600  16.431  5.813   1.00 33.89  ? 445 PRO A CD  1 
ATOM   3277 N N   . LEU A 1 417 ? 27.353  13.585  8.373   1.00 35.98  ? 446 LEU A N   1 
ATOM   3278 C CA  . LEU A 1 417 ? 25.993  13.093  8.503   1.00 34.36  ? 446 LEU A CA  1 
ATOM   3279 C C   . LEU A 1 417 ? 25.025  14.108  7.906   1.00 33.61  ? 446 LEU A C   1 
ATOM   3280 O O   . LEU A 1 417 ? 25.035  15.272  8.293   1.00 30.27  ? 446 LEU A O   1 
ATOM   3281 C CB  . LEU A 1 417 ? 25.683  12.829  9.979   1.00 34.64  ? 446 LEU A CB  1 
ATOM   3282 C CG  . LEU A 1 417 ? 24.418  12.011  10.267  1.00 34.99  ? 446 LEU A CG  1 
ATOM   3283 C CD1 . LEU A 1 417 ? 24.654  10.565  9.887   1.00 36.14  ? 446 LEU A CD1 1 
ATOM   3284 C CD2 . LEU A 1 417 ? 23.979  12.095  11.713  1.00 35.96  ? 446 LEU A CD2 1 
ATOM   3285 N N   . GLU A 1 418 ? 24.193  13.657  6.958   1.00 34.04  ? 447 GLU A N   1 
ATOM   3286 C CA  . GLU A 1 418 ? 23.043  14.440  6.530   1.00 34.20  ? 447 GLU A CA  1 
ATOM   3287 C C   . GLU A 1 418 ? 21.992  14.401  7.639   1.00 33.32  ? 447 GLU A C   1 
ATOM   3288 O O   . GLU A 1 418 ? 21.528  13.336  8.045   1.00 31.76  ? 447 GLU A O   1 
ATOM   3289 C CB  . GLU A 1 418 ? 22.490  13.967  5.185   1.00 36.85  ? 447 GLU A CB  1 
ATOM   3290 C CG  . GLU A 1 418 ? 21.403  14.885  4.621   1.00 39.08  ? 447 GLU A CG  1 
ATOM   3291 C CD  . GLU A 1 418 ? 20.913  14.529  3.228   1.00 40.02  ? 447 GLU A CD  1 
ATOM   3292 O OE1 . GLU A 1 418 ? 19.690  14.362  3.027   1.00 42.57  ? 447 GLU A OE1 1 
ATOM   3293 O OE2 . GLU A 1 418 ? 21.767  14.424  2.328   1.00 43.51  ? 447 GLU A OE2 1 
ATOM   3294 N N   . ARG A 1 419 ? 21.650  15.584  8.150   1.00 32.31  ? 448 ARG A N   1 
ATOM   3295 C CA  . ARG A 1 419 ? 20.855  15.696  9.356   1.00 32.85  ? 448 ARG A CA  1 
ATOM   3296 C C   . ARG A 1 419 ? 20.249  17.093  9.392   1.00 34.01  ? 448 ARG A C   1 
ATOM   3297 O O   . ARG A 1 419 ? 20.746  17.971  10.087  1.00 33.84  ? 448 ARG A O   1 
ATOM   3298 C CB  . ARG A 1 419 ? 21.698  15.399  10.601  1.00 34.02  ? 448 ARG A CB  1 
ATOM   3299 C CG  . ARG A 1 419 ? 20.892  14.879  11.786  1.00 38.79  ? 448 ARG A CG  1 
ATOM   3300 C CD  . ARG A 1 419 ? 19.649  15.710  12.145  1.00 41.21  ? 448 ARG A CD  1 
ATOM   3301 N NE  . ARG A 1 419 ? 18.964  15.247  13.361  1.00 43.07  ? 448 ARG A NE  1 
ATOM   3302 C CZ  . ARG A 1 419 ? 17.736  15.614  13.750  1.00 42.42  ? 448 ARG A CZ  1 
ATOM   3303 N NH1 . ARG A 1 419 ? 17.226  15.180  14.893  1.00 40.62  ? 448 ARG A NH1 1 
ATOM   3304 N NH2 . ARG A 1 419 ? 17.021  16.433  13.000  1.00 42.61  ? 448 ARG A NH2 1 
ATOM   3305 N N   . PRO A 1 420 ? 19.180  17.346  8.605   1.00 33.72  ? 449 PRO A N   1 
ATOM   3306 C CA  . PRO A 1 420 ? 18.432  18.596  8.711   1.00 34.70  ? 449 PRO A CA  1 
ATOM   3307 C C   . PRO A 1 420 ? 17.597  18.686  9.983   1.00 37.58  ? 449 PRO A C   1 
ATOM   3308 O O   . PRO A 1 420 ? 17.420  17.704  10.701  1.00 36.54  ? 449 PRO A O   1 
ATOM   3309 C CB  . PRO A 1 420 ? 17.558  18.585  7.440   1.00 34.69  ? 449 PRO A CB  1 
ATOM   3310 C CG  . PRO A 1 420 ? 17.367  17.114  7.140   1.00 33.40  ? 449 PRO A CG  1 
ATOM   3311 C CD  . PRO A 1 420 ? 18.680  16.466  7.541   1.00 31.74  ? 449 PRO A CD  1 
ATOM   3312 N N   . LYS A 1 421 ? 17.123  19.904  10.245  1.00 42.08  ? 450 LYS A N   1 
ATOM   3313 C CA  . LYS A 1 421 ? 16.147  20.187  11.282  1.00 43.16  ? 450 LYS A CA  1 
ATOM   3314 C C   . LYS A 1 421 ? 14.762  20.102  10.642  1.00 45.52  ? 450 LYS A C   1 
ATOM   3315 O O   . LYS A 1 421 ? 14.576  20.565  9.519   1.00 47.27  ? 450 LYS A O   1 
ATOM   3316 C CB  . LYS A 1 421 ? 16.509  21.561  11.868  1.00 44.59  ? 450 LYS A CB  1 
ATOM   3317 C CG  . LYS A 1 421 ? 15.501  22.211  12.813  1.00 46.50  ? 450 LYS A CG  1 
ATOM   3318 C CD  . LYS A 1 421 ? 15.192  21.444  14.094  1.00 47.73  ? 450 LYS A CD  1 
ATOM   3319 C CE  . LYS A 1 421 ? 14.108  22.135  14.867  1.00 49.15  ? 450 LYS A CE  1 
ATOM   3320 N NZ  . LYS A 1 421 ? 13.788  21.479  16.135  1.00 49.30  ? 450 LYS A NZ  1 
ATOM   3321 N N   . SER A 1 422 ? 13.811  19.469  11.346  1.00 44.40  ? 451 SER A N   1 
ATOM   3322 C CA  . SER A 1 422 ? 12.430  19.386  10.897  1.00 41.17  ? 451 SER A CA  1 
ATOM   3323 C C   . SER A 1 422 ? 11.550  20.254  11.793  1.00 42.39  ? 451 SER A C   1 
ATOM   3324 O O   . SER A 1 422 ? 11.999  20.740  12.832  1.00 40.14  ? 451 SER A O   1 
ATOM   3325 C CB  . SER A 1 422 ? 11.930  17.953  10.873  1.00 42.30  ? 451 SER A CB  1 
ATOM   3326 O OG  . SER A 1 422 ? 11.709  17.442  12.184  1.00 41.42  ? 451 SER A OG  1 
ATOM   3327 N N   . MET A 1 423 ? 10.295  20.434  11.365  1.00 42.58  ? 452 MET A N   1 
ATOM   3328 C CA  . MET A 1 423 ? 9.304   21.173  12.131  1.00 45.95  ? 452 MET A CA  1 
ATOM   3329 C C   . MET A 1 423 ? 7.940   20.504  11.971  1.00 42.38  ? 452 MET A C   1 
ATOM   3330 O O   . MET A 1 423 ? 7.654   19.894  10.943  1.00 42.77  ? 452 MET A O   1 
ATOM   3331 C CB  . MET A 1 423 ? 9.203   22.629  11.656  1.00 50.56  ? 452 MET A CB  1 
ATOM   3332 C CG  . MET A 1 423 ? 10.504  23.418  11.726  1.00 54.20  ? 452 MET A CG  1 
ATOM   3333 S SD  . MET A 1 423 ? 11.045  23.778  13.407  1.00 62.17  ? 452 MET A SD  1 
ATOM   3334 C CE  . MET A 1 423 ? 9.853   25.055  13.834  1.00 63.34  ? 452 MET A CE  1 
ATOM   3335 N N   . SER A 1 424 ? 7.108   20.609  13.009  1.00 41.64  ? 453 SER A N   1 
ATOM   3336 C CA  . SER A 1 424 ? 5.704   20.244  12.899  1.00 41.64  ? 453 SER A CA  1 
ATOM   3337 C C   . SER A 1 424 ? 4.921   21.429  12.331  1.00 41.83  ? 453 SER A C   1 
ATOM   3338 O O   . SER A 1 424 ? 5.390   22.564  12.393  1.00 40.25  ? 453 SER A O   1 
ATOM   3339 C CB  . SER A 1 424 ? 5.142   19.812  14.229  1.00 39.77  ? 453 SER A CB  1 
ATOM   3340 O OG  . SER A 1 424 ? 5.103   20.902  15.141  1.00 36.73  ? 453 SER A OG  1 
ATOM   3341 N N   . THR A 1 425 ? 3.740   21.154  11.764  1.00 41.77  ? 454 THR A N   1 
ATOM   3342 C CA  . THR A 1 425 ? 2.804   22.209  11.415  1.00 45.33  ? 454 THR A CA  1 
ATOM   3343 C C   . THR A 1 425 ? 2.702   23.180  12.592  1.00 49.52  ? 454 THR A C   1 
ATOM   3344 O O   . THR A 1 425 ? 3.128   24.333  12.493  1.00 48.30  ? 454 THR A O   1 
ATOM   3345 C CB  . THR A 1 425 ? 1.445   21.605  11.064  1.00 45.51  ? 454 THR A CB  1 
ATOM   3346 O OG1 . THR A 1 425 ? 1.597   20.877  9.848   1.00 43.53  ? 454 THR A OG1 1 
ATOM   3347 C CG2 . THR A 1 425 ? 0.376   22.664  10.872  1.00 46.09  ? 454 THR A CG2 1 
ATOM   3348 N N   . GLU A 1 426 ? 2.178   22.683  13.723  1.00 49.79  ? 455 GLU A N   1 
ATOM   3349 C CA  . GLU A 1 426 ? 1.895   23.524  14.874  1.00 48.33  ? 455 GLU A CA  1 
ATOM   3350 C C   . GLU A 1 426 ? 3.123   24.372  15.198  1.00 46.31  ? 455 GLU A C   1 
ATOM   3351 O O   . GLU A 1 426 ? 2.994   25.562  15.487  1.00 43.60  ? 455 GLU A O   1 
ATOM   3352 C CB  . GLU A 1 426 ? 1.433   22.686  16.066  1.00 50.98  ? 455 GLU A CB  1 
ATOM   3353 C CG  . GLU A 1 426 ? 0.944   23.543  17.232  1.00 57.88  ? 455 GLU A CG  1 
ATOM   3354 C CD  . GLU A 1 426 ? 0.083   22.835  18.266  1.00 61.69  ? 455 GLU A CD  1 
ATOM   3355 O OE1 . GLU A 1 426 ? -0.317  23.484  19.261  1.00 54.63  ? 455 GLU A OE1 1 
ATOM   3356 O OE2 . GLU A 1 426 ? -0.199  21.631  18.070  1.00 67.65  ? 455 GLU A OE2 1 
ATOM   3357 N N   . GLY A 1 427 ? 4.308   23.754  15.113  1.00 42.45  ? 456 GLY A N   1 
ATOM   3358 C CA  . GLY A 1 427 ? 5.569   24.435  15.373  1.00 43.37  ? 456 GLY A CA  1 
ATOM   3359 C C   . GLY A 1 427 ? 5.879   25.516  14.339  1.00 43.72  ? 456 GLY A C   1 
ATOM   3360 O O   . GLY A 1 427 ? 6.410   26.568  14.683  1.00 44.75  ? 456 GLY A O   1 
ATOM   3361 N N   . LEU A 1 428 ? 5.553   25.244  13.070  1.00 45.18  ? 457 LEU A N   1 
ATOM   3362 C CA  . LEU A 1 428 ? 5.762   26.198  11.992  1.00 47.34  ? 457 LEU A CA  1 
ATOM   3363 C C   . LEU A 1 428 ? 4.914   27.449  12.211  1.00 47.05  ? 457 LEU A C   1 
ATOM   3364 O O   . LEU A 1 428 ? 5.370   28.558  11.946  1.00 45.56  ? 457 LEU A O   1 
ATOM   3365 C CB  . LEU A 1 428 ? 5.437   25.579  10.633  1.00 47.57  ? 457 LEU A CB  1 
ATOM   3366 C CG  . LEU A 1 428 ? 6.584   24.889  9.894   1.00 50.38  ? 457 LEU A CG  1 
ATOM   3367 C CD1 . LEU A 1 428 ? 6.075   24.523  8.511   1.00 51.64  ? 457 LEU A CD1 1 
ATOM   3368 C CD2 . LEU A 1 428 ? 7.847   25.739  9.800   1.00 50.26  ? 457 LEU A CD2 1 
ATOM   3369 N N   . MET A 1 429 ? 3.671   27.249  12.660  1.00 48.79  ? 458 MET A N   1 
ATOM   3370 C CA  . MET A 1 429 ? 2.734   28.337  12.895  1.00 48.58  ? 458 MET A CA  1 
ATOM   3371 C C   . MET A 1 429 ? 3.280   29.298  13.947  1.00 50.18  ? 458 MET A C   1 
ATOM   3372 O O   . MET A 1 429 ? 3.160   30.510  13.793  1.00 53.35  ? 458 MET A O   1 
ATOM   3373 C CB  . MET A 1 429 ? 1.373   27.788  13.332  1.00 46.51  ? 458 MET A CB  1 
ATOM   3374 C CG  . MET A 1 429 ? 0.643   27.059  12.224  1.00 46.37  ? 458 MET A CG  1 
ATOM   3375 S SD  . MET A 1 429 ? -0.754  26.086  12.814  1.00 48.70  ? 458 MET A SD  1 
ATOM   3376 C CE  . MET A 1 429 ? -1.642  25.894  11.265  1.00 45.52  ? 458 MET A CE  1 
ATOM   3377 N N   . LYS A 1 430 ? 3.896   28.757  15.003  1.00 52.83  ? 459 LYS A N   1 
ATOM   3378 C CA  . LYS A 1 430 ? 4.464   29.590  16.050  1.00 56.46  ? 459 LYS A CA  1 
ATOM   3379 C C   . LYS A 1 430 ? 5.701   30.325  15.534  1.00 59.28  ? 459 LYS A C   1 
ATOM   3380 O O   . LYS A 1 430 ? 5.987   31.436  15.981  1.00 61.23  ? 459 LYS A O   1 
ATOM   3381 C CB  . LYS A 1 430 ? 4.761   28.770  17.312  1.00 57.53  ? 459 LYS A CB  1 
ATOM   3382 C CG  . LYS A 1 430 ? 3.524   28.217  18.016  1.00 59.82  ? 459 LYS A CG  1 
ATOM   3383 C CD  . LYS A 1 430 ? 3.702   27.936  19.504  1.00 60.22  ? 459 LYS A CD  1 
ATOM   3384 C CE  . LYS A 1 430 ? 4.851   27.029  19.809  1.00 63.20  ? 459 LYS A CE  1 
ATOM   3385 N NZ  . LYS A 1 430 ? 4.710   25.723  19.158  1.00 66.01  ? 459 LYS A NZ  1 
ATOM   3386 N N   . PHE A 1 431 ? 6.421   29.713  14.585  1.00 61.06  ? 460 PHE A N   1 
ATOM   3387 C CA  . PHE A 1 431 ? 7.679   30.259  14.098  1.00 62.83  ? 460 PHE A CA  1 
ATOM   3388 C C   . PHE A 1 431 ? 7.450   31.515  13.257  1.00 64.55  ? 460 PHE A C   1 
ATOM   3389 O O   . PHE A 1 431 ? 8.188   32.488  13.390  1.00 60.16  ? 460 PHE A O   1 
ATOM   3390 C CB  . PHE A 1 431 ? 8.447   29.230  13.265  1.00 62.15  ? 460 PHE A CB  1 
ATOM   3391 C CG  . PHE A 1 431 ? 9.851   29.685  12.895  1.00 63.64  ? 460 PHE A CG  1 
ATOM   3392 C CD1 . PHE A 1 431 ? 10.902  29.547  13.797  1.00 63.35  ? 460 PHE A CD1 1 
ATOM   3393 C CD2 . PHE A 1 431 ? 10.115  30.259  11.655  1.00 63.66  ? 460 PHE A CD2 1 
ATOM   3394 C CE1 . PHE A 1 431 ? 12.181  29.962  13.464  1.00 64.38  ? 460 PHE A CE1 1 
ATOM   3395 C CE2 . PHE A 1 431 ? 11.400  30.669  11.325  1.00 64.77  ? 460 PHE A CE2 1 
ATOM   3396 C CZ  . PHE A 1 431 ? 12.429  30.517  12.226  1.00 65.13  ? 460 PHE A CZ  1 
ATOM   3397 N N   . VAL A 1 432 ? 6.450   31.475  12.369  1.00 70.82  ? 461 VAL A N   1 
ATOM   3398 C CA  . VAL A 1 432 ? 6.241   32.542  11.400  1.00 75.33  ? 461 VAL A CA  1 
ATOM   3399 C C   . VAL A 1 432 ? 5.807   33.818  12.123  1.00 80.51  ? 461 VAL A C   1 
ATOM   3400 O O   . VAL A 1 432 ? 6.112   34.918  11.666  1.00 79.55  ? 461 VAL A O   1 
ATOM   3401 C CB  . VAL A 1 432 ? 5.238   32.155  10.294  1.00 77.29  ? 461 VAL A CB  1 
ATOM   3402 C CG1 . VAL A 1 432 ? 5.763   31.012  9.432   1.00 75.24  ? 461 VAL A CG1 1 
ATOM   3403 C CG2 . VAL A 1 432 ? 3.857   31.817  10.844  1.00 79.11  ? 461 VAL A CG2 1 
ATOM   3404 N N   . ASP A 1 433 ? 5.092   33.661  13.246  1.00 86.07  ? 462 ASP A N   1 
ATOM   3405 C CA  . ASP A 1 433 ? 4.712   34.786  14.085  1.00 87.84  ? 462 ASP A CA  1 
ATOM   3406 C C   . ASP A 1 433 ? 5.971   35.503  14.564  1.00 95.50  ? 462 ASP A C   1 
ATOM   3407 O O   . ASP A 1 433 ? 6.256   36.613  14.119  1.00 104.36 ? 462 ASP A O   1 
ATOM   3408 C CB  . ASP A 1 433 ? 3.824   34.346  15.238  1.00 83.72  ? 462 ASP A CB  1 
ATOM   3409 C CG  . ASP A 1 433 ? 2.406   33.956  14.850  1.00 83.10  ? 462 ASP A CG  1 
ATOM   3410 O OD1 . ASP A 1 433 ? 2.043   34.150  13.670  1.00 86.42  ? 462 ASP A OD1 1 
ATOM   3411 O OD2 . ASP A 1 433 ? 1.679   33.457  15.729  1.00 79.83  ? 462 ASP A OD2 1 
ATOM   3412 N N   . SER A 1 434 ? 6.726   34.848  15.455  1.00 96.53  ? 463 SER A N   1 
ATOM   3413 C CA  . SER A 1 434 ? 7.962   35.408  15.975  1.00 95.28  ? 463 SER A CA  1 
ATOM   3414 C C   . SER A 1 434 ? 9.123   35.057  15.032  1.00 92.65  ? 463 SER A C   1 
ATOM   3415 O O   . SER A 1 434 ? 8.939   35.241  13.807  1.00 91.12  ? 463 SER A O   1 
ATOM   3416 C CB  . SER A 1 434 ? 8.231   34.933  17.383  1.00 95.48  ? 463 SER A CB  1 
ATOM   3417 O OG  . SER A 1 434 ? 8.305   33.516  17.443  1.00 100.86 ? 463 SER A OG  1 
ATOM   3418 N N   . SER B 1 1   ? -14.602 3.989   18.309  1.00 118.79 ? 30  SER B N   1 
ATOM   3419 C CA  . SER B 1 1   ? -14.655 3.733   19.776  1.00 120.67 ? 30  SER B CA  1 
ATOM   3420 C C   . SER B 1 1   ? -13.257 3.407   20.297  1.00 116.77 ? 30  SER B C   1 
ATOM   3421 O O   . SER B 1 1   ? -12.602 4.258   20.896  1.00 115.65 ? 30  SER B O   1 
ATOM   3422 C CB  . SER B 1 1   ? -15.647 2.638   20.111  1.00 122.13 ? 30  SER B CB  1 
ATOM   3423 O OG  . SER B 1 1   ? -15.409 2.101   21.406  1.00 121.84 ? 30  SER B OG  1 
ATOM   3424 N N   . THR B 1 2   ? -12.826 2.161   20.068  1.00 108.93 ? 31  THR B N   1 
ATOM   3425 C CA  . THR B 1 2   ? -11.461 1.742   20.334  1.00 102.63 ? 31  THR B CA  1 
ATOM   3426 C C   . THR B 1 2   ? -10.763 1.443   19.006  1.00 90.23  ? 31  THR B C   1 
ATOM   3427 O O   . THR B 1 2   ? -9.646  0.927   18.997  1.00 91.99  ? 31  THR B O   1 
ATOM   3428 C CB  . THR B 1 2   ? -11.480 0.538   21.278  1.00 105.78 ? 31  THR B CB  1 
ATOM   3429 O OG1 . THR B 1 2   ? -12.401 -0.409  20.743  1.00 107.50 ? 31  THR B OG1 1 
ATOM   3430 C CG2 . THR B 1 2   ? -11.929 0.911   22.679  1.00 106.39 ? 31  THR B CG2 1 
ATOM   3431 N N   . ASN B 1 3   ? -11.420 1.801   17.891  1.00 74.50  ? 32  ASN B N   1 
ATOM   3432 C CA  . ASN B 1 3   ? -10.889 1.572   16.557  1.00 65.91  ? 32  ASN B CA  1 
ATOM   3433 C C   . ASN B 1 3   ? -10.088 2.796   16.118  1.00 57.70  ? 32  ASN B C   1 
ATOM   3434 O O   . ASN B 1 3   ? -10.663 3.832   15.780  1.00 55.73  ? 32  ASN B O   1 
ATOM   3435 C CB  . ASN B 1 3   ? -12.002 1.257   15.564  1.00 64.84  ? 32  ASN B CB  1 
ATOM   3436 C CG  . ASN B 1 3   ? -11.489 0.528   14.345  1.00 65.98  ? 32  ASN B CG  1 
ATOM   3437 O OD1 . ASN B 1 3   ? -10.517 0.965   13.718  1.00 67.88  ? 32  ASN B OD1 1 
ATOM   3438 N ND2 . ASN B 1 3   ? -12.108 -0.593  14.005  1.00 66.01  ? 32  ASN B ND2 1 
ATOM   3439 N N   . LEU B 1 4   ? -8.756  2.651   16.104  1.00 49.99  ? 33  LEU B N   1 
ATOM   3440 C CA  . LEU B 1 4   ? -7.854  3.760   15.828  1.00 45.83  ? 33  LEU B CA  1 
ATOM   3441 C C   . LEU B 1 4   ? -8.083  4.283   14.410  1.00 42.47  ? 33  LEU B C   1 
ATOM   3442 O O   . LEU B 1 4   ? -7.989  5.483   14.169  1.00 44.22  ? 33  LEU B O   1 
ATOM   3443 C CB  . LEU B 1 4   ? -6.416  3.288   16.044  1.00 44.82  ? 33  LEU B CB  1 
ATOM   3444 C CG  . LEU B 1 4   ? -5.305  4.295   15.731  1.00 45.08  ? 33  LEU B CG  1 
ATOM   3445 C CD1 . LEU B 1 4   ? -5.395  5.526   16.605  1.00 45.99  ? 33  LEU B CD1 1 
ATOM   3446 C CD2 . LEU B 1 4   ? -3.942  3.644   15.884  1.00 46.19  ? 33  LEU B CD2 1 
ATOM   3447 N N   . LYS B 1 5   ? -8.397  3.375   13.484  1.00 41.07  ? 34  LYS B N   1 
ATOM   3448 C CA  . LYS B 1 5   ? -8.551  3.719   12.081  1.00 43.43  ? 34  LYS B CA  1 
ATOM   3449 C C   . LYS B 1 5   ? -9.799  4.571   11.865  1.00 43.75  ? 34  LYS B C   1 
ATOM   3450 O O   . LYS B 1 5   ? -9.809  5.419   10.972  1.00 42.19  ? 34  LYS B O   1 
ATOM   3451 C CB  . LYS B 1 5   ? -8.618  2.459   11.213  1.00 43.99  ? 34  LYS B CB  1 
ATOM   3452 C CG  . LYS B 1 5   ? -8.575  2.711   9.712   1.00 44.72  ? 34  LYS B CG  1 
ATOM   3453 C CD  . LYS B 1 5   ? -8.566  1.419   8.902   1.00 45.40  ? 34  LYS B CD  1 
ATOM   3454 C CE  . LYS B 1 5   ? -8.490  1.678   7.436   1.00 46.20  ? 34  LYS B CE  1 
ATOM   3455 N NZ  . LYS B 1 5   ? -8.720  0.450   6.673   1.00 48.10  ? 34  LYS B NZ  1 
ATOM   3456 N N   . ASP B 1 6   ? -10.849 4.325   12.662  1.00 45.87  ? 35  ASP B N   1 
ATOM   3457 C CA  . ASP B 1 6   ? -12.037 5.169   12.640  1.00 48.21  ? 35  ASP B CA  1 
ATOM   3458 C C   . ASP B 1 6   ? -11.723 6.529   13.258  1.00 44.70  ? 35  ASP B C   1 
ATOM   3459 O O   . ASP B 1 6   ? -12.149 7.550   12.728  1.00 44.11  ? 35  ASP B O   1 
ATOM   3460 C CB  . ASP B 1 6   ? -13.232 4.534   13.339  1.00 51.17  ? 35  ASP B CB  1 
ATOM   3461 C CG  . ASP B 1 6   ? -13.833 3.316   12.649  1.00 55.88  ? 35  ASP B CG  1 
ATOM   3462 O OD1 . ASP B 1 6   ? -13.938 3.336   11.401  1.00 52.67  ? 35  ASP B OD1 1 
ATOM   3463 O OD2 . ASP B 1 6   ? -14.220 2.365   13.370  1.00 62.02  ? 35  ASP B OD2 1 
ATOM   3464 N N   . ILE B 1 7   ? -10.974 6.525   14.370  1.00 43.97  ? 36  ILE B N   1 
ATOM   3465 C CA  . ILE B 1 7   ? -10.576 7.745   15.062  1.00 45.26  ? 36  ILE B CA  1 
ATOM   3466 C C   . ILE B 1 7   ? -9.706  8.604   14.151  1.00 44.05  ? 36  ILE B C   1 
ATOM   3467 O O   . ILE B 1 7   ? -9.798  9.826   14.182  1.00 44.04  ? 36  ILE B O   1 
ATOM   3468 C CB  . ILE B 1 7   ? -9.849  7.414   16.381  1.00 49.05  ? 36  ILE B CB  1 
ATOM   3469 C CG1 . ILE B 1 7   ? -10.820 6.821   17.403  1.00 51.51  ? 36  ILE B CG1 1 
ATOM   3470 C CG2 . ILE B 1 7   ? -9.117  8.639   16.941  1.00 48.25  ? 36  ILE B CG2 1 
ATOM   3471 C CD1 . ILE B 1 7   ? -10.163 6.300   18.666  1.00 52.89  ? 36  ILE B CD1 1 
ATOM   3472 N N   . LEU B 1 8   ? -8.860  7.949   13.351  1.00 45.32  ? 37  LEU B N   1 
ATOM   3473 C CA  . LEU B 1 8   ? -7.902  8.639   12.507  1.00 46.88  ? 37  LEU B CA  1 
ATOM   3474 C C   . LEU B 1 8   ? -8.608  9.208   11.277  1.00 45.64  ? 37  LEU B C   1 
ATOM   3475 O O   . LEU B 1 8   ? -8.353  10.340  10.884  1.00 44.39  ? 37  LEU B O   1 
ATOM   3476 C CB  . LEU B 1 8   ? -6.808  7.626   12.169  1.00 48.92  ? 37  LEU B CB  1 
ATOM   3477 C CG  . LEU B 1 8   ? -5.407  8.191   11.922  1.00 48.69  ? 37  LEU B CG  1 
ATOM   3478 C CD1 . LEU B 1 8   ? -4.948  9.034   13.092  1.00 47.18  ? 37  LEU B CD1 1 
ATOM   3479 C CD2 . LEU B 1 8   ? -4.439  7.045   11.670  1.00 49.30  ? 37  LEU B CD2 1 
ATOM   3480 N N   . ALA B 1 9   ? -9.537  8.430   10.705  1.00 50.32  ? 38  ALA B N   1 
ATOM   3481 C CA  . ALA B 1 9   ? -10.358 8.868   9.583   1.00 49.76  ? 38  ALA B CA  1 
ATOM   3482 C C   . ALA B 1 9   ? -11.076 10.177  9.897   1.00 49.38  ? 38  ALA B C   1 
ATOM   3483 O O   . ALA B 1 9   ? -11.220 11.018  9.016   1.00 53.83  ? 38  ALA B O   1 
ATOM   3484 C CB  . ALA B 1 9   ? -11.357 7.792   9.219   1.00 49.85  ? 38  ALA B CB  1 
ATOM   3485 N N   . ASP B 1 10  ? -11.532 10.333  11.146  1.00 47.05  ? 39  ASP B N   1 
ATOM   3486 C CA  . ASP B 1 10  ? -12.269 11.516  11.563  1.00 49.92  ? 39  ASP B CA  1 
ATOM   3487 C C   . ASP B 1 10  ? -11.321 12.676  11.861  1.00 48.57  ? 39  ASP B C   1 
ATOM   3488 O O   . ASP B 1 10  ? -11.767 13.811  12.015  1.00 46.87  ? 39  ASP B O   1 
ATOM   3489 C CB  . ASP B 1 10  ? -13.140 11.234  12.780  1.00 55.92  ? 39  ASP B CB  1 
ATOM   3490 C CG  . ASP B 1 10  ? -14.450 10.501  12.512  1.00 64.54  ? 39  ASP B CG  1 
ATOM   3491 O OD1 . ASP B 1 10  ? -14.411 9.400   11.913  1.00 66.60  ? 39  ASP B OD1 1 
ATOM   3492 O OD2 . ASP B 1 10  ? -15.509 11.030  12.919  1.00 73.68  ? 39  ASP B OD2 1 
ATOM   3493 N N   . LEU B 1 11  ? -10.023 12.387  12.001  1.00 48.62  ? 40  LEU B N   1 
ATOM   3494 C CA  . LEU B 1 11  ? -9.047  13.416  12.318  1.00 46.02  ? 40  LEU B CA  1 
ATOM   3495 C C   . LEU B 1 11  ? -8.448  13.985  11.035  1.00 41.36  ? 40  LEU B C   1 
ATOM   3496 O O   . LEU B 1 11  ? -8.140  15.168  10.972  1.00 36.94  ? 40  LEU B O   1 
ATOM   3497 C CB  . LEU B 1 11  ? -7.957  12.851  13.227  1.00 46.97  ? 40  LEU B CB  1 
ATOM   3498 C CG  . LEU B 1 11  ? -8.332  12.636  14.695  1.00 49.66  ? 40  LEU B CG  1 
ATOM   3499 C CD1 . LEU B 1 11  ? -7.108  12.106  15.422  1.00 52.70  ? 40  LEU B CD1 1 
ATOM   3500 C CD2 . LEU B 1 11  ? -8.834  13.896  15.374  1.00 51.91  ? 40  LEU B CD2 1 
ATOM   3501 N N   . ILE B 1 12  ? -8.285  13.134  10.020  1.00 38.47  ? 41  ILE B N   1 
ATOM   3502 C CA  . ILE B 1 12  ? -7.491  13.483  8.853   1.00 38.56  ? 41  ILE B CA  1 
ATOM   3503 C C   . ILE B 1 12  ? -8.043  14.733  8.160   1.00 39.98  ? 41  ILE B C   1 
ATOM   3504 O O   . ILE B 1 12  ? -7.266  15.636  7.857   1.00 40.39  ? 41  ILE B O   1 
ATOM   3505 C CB  . ILE B 1 12  ? -7.367  12.274  7.909   1.00 36.54  ? 41  ILE B CB  1 
ATOM   3506 C CG1 . ILE B 1 12  ? -6.411  11.227  8.493   1.00 34.34  ? 41  ILE B CG1 1 
ATOM   3507 C CG2 . ILE B 1 12  ? -6.951  12.706  6.503   1.00 35.23  ? 41  ILE B CG2 1 
ATOM   3508 C CD1 . ILE B 1 12  ? -6.444  9.894   7.772   1.00 35.43  ? 41  ILE B CD1 1 
ATOM   3509 N N   . PRO B 1 13  ? -9.365  14.832  7.859   1.00 43.92  ? 42  PRO B N   1 
ATOM   3510 C CA  . PRO B 1 13  ? -9.923  16.016  7.193   1.00 42.48  ? 42  PRO B CA  1 
ATOM   3511 C C   . PRO B 1 13  ? -9.721  17.319  7.964   1.00 41.81  ? 42  PRO B C   1 
ATOM   3512 O O   . PRO B 1 13  ? -9.446  18.355  7.359   1.00 37.26  ? 42  PRO B O   1 
ATOM   3513 C CB  . PRO B 1 13  ? -11.427 15.703  7.013   1.00 43.28  ? 42  PRO B CB  1 
ATOM   3514 C CG  . PRO B 1 13  ? -11.537 14.209  7.199   1.00 44.07  ? 42  PRO B CG  1 
ATOM   3515 C CD  . PRO B 1 13  ? -10.384 13.799  8.099   1.00 43.38  ? 42  PRO B CD  1 
ATOM   3516 N N   . LYS B 1 14  ? -9.884  17.264  9.293   1.00 42.41  ? 43  LYS B N   1 
ATOM   3517 C CA  . LYS B 1 14  ? -9.645  18.425  10.135  1.00 46.90  ? 43  LYS B CA  1 
ATOM   3518 C C   . LYS B 1 14  ? -8.225  18.928  9.892   1.00 46.35  ? 43  LYS B C   1 
ATOM   3519 O O   . LYS B 1 14  ? -8.007  20.107  9.611   1.00 48.07  ? 43  LYS B O   1 
ATOM   3520 C CB  . LYS B 1 14  ? -9.753  18.117  11.633  1.00 53.83  ? 43  LYS B CB  1 
ATOM   3521 C CG  . LYS B 1 14  ? -11.121 17.740  12.186  1.00 59.29  ? 43  LYS B CG  1 
ATOM   3522 C CD  . LYS B 1 14  ? -11.072 17.541  13.699  1.00 65.06  ? 43  LYS B CD  1 
ATOM   3523 C CE  . LYS B 1 14  ? -12.415 17.428  14.358  1.00 69.80  ? 43  LYS B CE  1 
ATOM   3524 N NZ  . LYS B 1 14  ? -13.136 16.221  13.945  1.00 71.14  ? 43  LYS B NZ  1 
ATOM   3525 N N   . GLU B 1 15  ? -7.270  17.999  9.992   1.00 43.42  ? 44  GLU B N   1 
ATOM   3526 C CA  . GLU B 1 15  ? -5.860  18.322  9.874   1.00 43.03  ? 44  GLU B CA  1 
ATOM   3527 C C   . GLU B 1 15  ? -5.549  18.816  8.464   1.00 41.01  ? 44  GLU B C   1 
ATOM   3528 O O   . GLU B 1 15  ? -4.741  19.722  8.300   1.00 40.93  ? 44  GLU B O   1 
ATOM   3529 C CB  . GLU B 1 15  ? -5.006  17.102  10.213  1.00 43.67  ? 44  GLU B CB  1 
ATOM   3530 C CG  . GLU B 1 15  ? -3.604  17.479  10.675  1.00 50.40  ? 44  GLU B CG  1 
ATOM   3531 C CD  . GLU B 1 15  ? -3.538  17.906  12.127  1.00 51.80  ? 44  GLU B CD  1 
ATOM   3532 O OE1 . GLU B 1 15  ? -3.833  17.044  12.977  1.00 56.64  ? 44  GLU B OE1 1 
ATOM   3533 O OE2 . GLU B 1 15  ? -3.208  19.079  12.405  1.00 54.34  ? 44  GLU B OE2 1 
ATOM   3534 N N   . GLN B 1 16  ? -6.172  18.202  7.450   1.00 37.70  ? 45  GLN B N   1 
ATOM   3535 C CA  . GLN B 1 16  ? -5.954  18.605  6.069   1.00 39.44  ? 45  GLN B CA  1 
ATOM   3536 C C   . GLN B 1 16  ? -6.319  20.074  5.864   1.00 39.81  ? 45  GLN B C   1 
ATOM   3537 O O   . GLN B 1 16  ? -5.577  20.798  5.207   1.00 38.14  ? 45  GLN B O   1 
ATOM   3538 C CB  . GLN B 1 16  ? -6.728  17.711  5.103   1.00 38.94  ? 45  GLN B CB  1 
ATOM   3539 C CG  . GLN B 1 16  ? -6.033  16.381  4.843   1.00 39.70  ? 45  GLN B CG  1 
ATOM   3540 C CD  . GLN B 1 16  ? -6.894  15.382  4.109   1.00 38.69  ? 45  GLN B CD  1 
ATOM   3541 O OE1 . GLN B 1 16  ? -8.126  15.479  4.078   1.00 38.53  ? 45  GLN B OE1 1 
ATOM   3542 N NE2 . GLN B 1 16  ? -6.241  14.400  3.513   1.00 38.62  ? 45  GLN B NE2 1 
ATOM   3543 N N   . ALA B 1 17  ? -7.458  20.508  6.422   1.00 42.42  ? 46  ALA B N   1 
ATOM   3544 C CA  . ALA B 1 17  ? -7.927  21.875  6.235   1.00 44.12  ? 46  ALA B CA  1 
ATOM   3545 C C   . ALA B 1 17  ? -6.944  22.855  6.872   1.00 45.13  ? 46  ALA B C   1 
ATOM   3546 O O   . ALA B 1 17  ? -6.538  23.842  6.255   1.00 45.91  ? 46  ALA B O   1 
ATOM   3547 C CB  . ALA B 1 17  ? -9.315  22.037  6.813   1.00 43.42  ? 46  ALA B CB  1 
ATOM   3548 N N   . ARG B 1 18  ? -6.563  22.552  8.115   1.00 47.85  ? 47  ARG B N   1 
ATOM   3549 C CA  . ARG B 1 18  ? -5.646  23.379  8.880   1.00 50.02  ? 47  ARG B CA  1 
ATOM   3550 C C   . ARG B 1 18  ? -4.355  23.599  8.091   1.00 49.63  ? 47  ARG B C   1 
ATOM   3551 O O   . ARG B 1 18  ? -3.839  24.712  8.057   1.00 53.20  ? 47  ARG B O   1 
ATOM   3552 C CB  . ARG B 1 18  ? -5.410  22.712  10.241  1.00 51.47  ? 47  ARG B CB  1 
ATOM   3553 C CG  . ARG B 1 18  ? -4.467  23.437  11.192  1.00 54.42  ? 47  ARG B CG  1 
ATOM   3554 C CD  . ARG B 1 18  ? -4.146  22.560  12.393  1.00 58.39  ? 47  ARG B CD  1 
ATOM   3555 N NE  . ARG B 1 18  ? -3.108  23.097  13.278  1.00 61.32  ? 47  ARG B NE  1 
ATOM   3556 C CZ  . ARG B 1 18  ? -2.627  22.474  14.350  1.00 66.00  ? 47  ARG B CZ  1 
ATOM   3557 N NH1 . ARG B 1 18  ? -3.065  21.266  14.674  1.00 68.81  ? 47  ARG B NH1 1 
ATOM   3558 N NH2 . ARG B 1 18  ? -1.704  23.061  15.097  1.00 64.56  ? 47  ARG B NH2 1 
ATOM   3559 N N   . ILE B 1 19  ? -3.847  22.540  7.451   1.00 47.20  ? 48  ILE B N   1 
ATOM   3560 C CA  . ILE B 1 19  ? -2.594  22.607  6.714   1.00 47.08  ? 48  ILE B CA  1 
ATOM   3561 C C   . ILE B 1 19  ? -2.794  23.361  5.399   1.00 47.86  ? 48  ILE B C   1 
ATOM   3562 O O   . ILE B 1 19  ? -1.957  24.182  5.035   1.00 52.81  ? 48  ILE B O   1 
ATOM   3563 C CB  . ILE B 1 19  ? -2.022  21.192  6.503   1.00 45.97  ? 48  ILE B CB  1 
ATOM   3564 C CG1 . ILE B 1 19  ? -1.398  20.676  7.795   1.00 47.79  ? 48  ILE B CG1 1 
ATOM   3565 C CG2 . ILE B 1 19  ? -1.023  21.155  5.346   1.00 46.61  ? 48  ILE B CG2 1 
ATOM   3566 C CD1 . ILE B 1 19  ? -1.052  19.201  7.773   1.00 47.85  ? 48  ILE B CD1 1 
ATOM   3567 N N   . LYS B 1 20  ? -3.885  23.056  4.684   1.00 49.05  ? 49  LYS B N   1 
ATOM   3568 C CA  . LYS B 1 20  ? -4.179  23.663  3.394   1.00 52.77  ? 49  LYS B CA  1 
ATOM   3569 C C   . LYS B 1 20  ? -4.357  25.171  3.559   1.00 54.32  ? 49  LYS B C   1 
ATOM   3570 O O   . LYS B 1 20  ? -3.918  25.939  2.708   1.00 53.04  ? 49  LYS B O   1 
ATOM   3571 C CB  . LYS B 1 20  ? -5.423  22.987  2.801   1.00 56.13  ? 49  LYS B CB  1 
ATOM   3572 C CG  . LYS B 1 20  ? -6.148  23.696  1.657   1.00 55.78  ? 49  LYS B CG  1 
ATOM   3573 C CD  . LYS B 1 20  ? -7.502  23.058  1.358   1.00 56.51  ? 49  LYS B CD  1 
ATOM   3574 C CE  . LYS B 1 20  ? -8.536  24.002  0.809   1.00 58.58  ? 49  LYS B CE  1 
ATOM   3575 N NZ  . LYS B 1 20  ? -8.301  24.360  -0.590  1.00 59.81  ? 49  LYS B NZ  1 
ATOM   3576 N N   . THR B 1 21  ? -5.014  25.577  4.652   1.00 56.06  ? 50  THR B N   1 
ATOM   3577 C CA  . THR B 1 21  ? -5.179  26.983  4.986   1.00 56.91  ? 50  THR B CA  1 
ATOM   3578 C C   . THR B 1 21  ? -3.815  27.605  5.269   1.00 58.56  ? 50  THR B C   1 
ATOM   3579 O O   . THR B 1 21  ? -3.522  28.700  4.797   1.00 65.65  ? 50  THR B O   1 
ATOM   3580 C CB  . THR B 1 21  ? -6.098  27.121  6.200   1.00 58.85  ? 50  THR B CB  1 
ATOM   3581 O OG1 . THR B 1 21  ? -7.316  26.454  5.880   1.00 60.14  ? 50  THR B OG1 1 
ATOM   3582 C CG2 . THR B 1 21  ? -6.370  28.572  6.555   1.00 59.85  ? 50  THR B CG2 1 
ATOM   3583 N N   . PHE B 1 22  ? -2.990  26.898  6.048   1.00 54.88  ? 51  PHE B N   1 
ATOM   3584 C CA  . PHE B 1 22  ? -1.730  27.439  6.530   1.00 53.59  ? 51  PHE B CA  1 
ATOM   3585 C C   . PHE B 1 22  ? -0.789  27.757  5.366   1.00 56.57  ? 51  PHE B C   1 
ATOM   3586 O O   . PHE B 1 22  ? 0.008   28.687  5.464   1.00 51.90  ? 51  PHE B O   1 
ATOM   3587 C CB  . PHE B 1 22  ? -1.073  26.468  7.518   1.00 48.86  ? 51  PHE B CB  1 
ATOM   3588 C CG  . PHE B 1 22  ? 0.247   26.984  8.063   1.00 43.72  ? 51  PHE B CG  1 
ATOM   3589 C CD1 . PHE B 1 22  ? 0.307   28.201  8.728   1.00 38.98  ? 51  PHE B CD1 1 
ATOM   3590 C CD2 . PHE B 1 22  ? 1.431   26.282  7.844   1.00 40.54  ? 51  PHE B CD2 1 
ATOM   3591 C CE1 . PHE B 1 22  ? 1.517   28.684  9.192   1.00 41.29  ? 51  PHE B CE1 1 
ATOM   3592 C CE2 . PHE B 1 22  ? 2.633   26.762  8.320   1.00 39.21  ? 51  PHE B CE2 1 
ATOM   3593 C CZ  . PHE B 1 22  ? 2.677   27.966  8.985   1.00 43.01  ? 51  PHE B CZ  1 
ATOM   3594 N N   . ARG B 1 23  ? -0.864  26.971  4.282   1.00 61.96  ? 52  ARG B N   1 
ATOM   3595 C CA  . ARG B 1 23  ? -0.031  27.193  3.106   1.00 64.95  ? 52  ARG B CA  1 
ATOM   3596 C C   . ARG B 1 23  ? -0.659  28.268  2.217   1.00 64.24  ? 52  ARG B C   1 
ATOM   3597 O O   . ARG B 1 23  ? 0.039   28.944  1.464   1.00 60.03  ? 52  ARG B O   1 
ATOM   3598 C CB  . ARG B 1 23  ? 0.155   25.884  2.330   1.00 66.12  ? 52  ARG B CB  1 
ATOM   3599 C CG  . ARG B 1 23  ? 0.748   24.752  3.157   1.00 66.01  ? 52  ARG B CG  1 
ATOM   3600 C CD  . ARG B 1 23  ? 0.536   23.400  2.502   1.00 65.04  ? 52  ARG B CD  1 
ATOM   3601 N NE  . ARG B 1 23  ? 1.242   23.323  1.219   1.00 66.69  ? 52  ARG B NE  1 
ATOM   3602 C CZ  . ARG B 1 23  ? 0.693   23.148  0.017   1.00 71.04  ? 52  ARG B CZ  1 
ATOM   3603 N NH1 . ARG B 1 23  ? -0.617  23.056  -0.133  1.00 69.31  ? 52  ARG B NH1 1 
ATOM   3604 N NH2 . ARG B 1 23  ? 1.467   23.067  -1.051  1.00 74.40  ? 52  ARG B NH2 1 
ATOM   3605 N N   . GLN B 1 24  ? -1.986  28.419  2.322   1.00 66.97  ? 53  GLN B N   1 
ATOM   3606 C CA  . GLN B 1 24  ? -2.731  29.446  1.609   1.00 68.23  ? 53  GLN B CA  1 
ATOM   3607 C C   . GLN B 1 24  ? -2.585  30.814  2.280   1.00 70.60  ? 53  GLN B C   1 
ATOM   3608 O O   . GLN B 1 24  ? -3.218  31.780  1.849   1.00 72.14  ? 53  GLN B O   1 
ATOM   3609 C CB  . GLN B 1 24  ? -4.216  29.083  1.554   1.00 66.70  ? 53  GLN B CB  1 
ATOM   3610 C CG  . GLN B 1 24  ? -4.608  28.194  0.381   1.00 66.40  ? 53  GLN B CG  1 
ATOM   3611 C CD  . GLN B 1 24  ? -6.102  27.959  0.311   1.00 66.96  ? 53  GLN B CD  1 
ATOM   3612 O OE1 . GLN B 1 24  ? -6.839  28.162  1.285   1.00 64.62  ? 53  GLN B OE1 1 
ATOM   3613 N NE2 . GLN B 1 24  ? -6.564  27.511  -0.846  1.00 70.08  ? 53  GLN B NE2 1 
ATOM   3614 N N   . GLN B 1 25  ? -1.770  30.894  3.341   1.00 65.90  ? 54  GLN B N   1 
ATOM   3615 C CA  . GLN B 1 25  ? -1.539  32.146  4.041   1.00 59.80  ? 54  GLN B CA  1 
ATOM   3616 C C   . GLN B 1 25  ? -0.055  32.505  4.038   1.00 58.28  ? 54  GLN B C   1 
ATOM   3617 O O   . GLN B 1 25  ? 0.278   33.667  3.820   1.00 59.16  ? 54  GLN B O   1 
ATOM   3618 C CB  . GLN B 1 25  ? -2.034  32.051  5.483   1.00 58.04  ? 54  GLN B CB  1 
ATOM   3619 C CG  . GLN B 1 25  ? -3.552  32.004  5.635   1.00 53.85  ? 54  GLN B CG  1 
ATOM   3620 C CD  . GLN B 1 25  ? -4.007  31.874  7.075   1.00 56.38  ? 54  GLN B CD  1 
ATOM   3621 O OE1 . GLN B 1 25  ? -5.204  31.930  7.379   1.00 57.30  ? 54  GLN B OE1 1 
ATOM   3622 N NE2 . GLN B 1 25  ? -3.063  31.718  7.995   1.00 59.69  ? 54  GLN B NE2 1 
ATOM   3623 N N   . HIS B 1 26  ? 0.821   31.518  4.304   1.00 57.44  ? 55  HIS B N   1 
ATOM   3624 C CA  . HIS B 1 26  ? 2.212   31.792  4.649   1.00 56.78  ? 55  HIS B CA  1 
ATOM   3625 C C   . HIS B 1 26  ? 3.192   30.910  3.876   1.00 56.53  ? 55  HIS B C   1 
ATOM   3626 O O   . HIS B 1 26  ? 4.345   30.780  4.282   1.00 58.80  ? 55  HIS B O   1 
ATOM   3627 C CB  . HIS B 1 26  ? 2.444   31.587  6.152   1.00 54.96  ? 55  HIS B CB  1 
ATOM   3628 C CG  . HIS B 1 26  ? 1.500   32.349  7.011   1.00 56.17  ? 55  HIS B CG  1 
ATOM   3629 N ND1 . HIS B 1 26  ? 1.667   33.684  7.304   1.00 57.41  ? 55  HIS B ND1 1 
ATOM   3630 C CD2 . HIS B 1 26  ? 0.375   31.972  7.621   1.00 59.84  ? 55  HIS B CD2 1 
ATOM   3631 C CE1 . HIS B 1 26  ? 0.674   34.086  8.082   1.00 60.94  ? 55  HIS B CE1 1 
ATOM   3632 N NE2 . HIS B 1 26  ? -0.123  33.061  8.288   1.00 63.49  ? 55  HIS B NE2 1 
ATOM   3633 N N   . GLY B 1 27  ? 2.752   30.352  2.743   1.00 56.37  ? 56  GLY B N   1 
ATOM   3634 C CA  . GLY B 1 27  ? 3.575   29.457  1.944   1.00 61.50  ? 56  GLY B CA  1 
ATOM   3635 C C   . GLY B 1 27  ? 4.942   30.045  1.582   1.00 63.58  ? 56  GLY B C   1 
ATOM   3636 O O   . GLY B 1 27  ? 5.915   29.300  1.468   1.00 59.38  ? 56  GLY B O   1 
ATOM   3637 N N   . LYS B 1 28  ? 5.015   31.375  1.410   1.00 62.32  ? 57  LYS B N   1 
ATOM   3638 C CA  . LYS B 1 28  ? 6.187   32.008  0.822   1.00 63.73  ? 57  LYS B CA  1 
ATOM   3639 C C   . LYS B 1 28  ? 7.011   32.755  1.877   1.00 68.03  ? 57  LYS B C   1 
ATOM   3640 O O   . LYS B 1 28  ? 7.751   33.681  1.541   1.00 70.44  ? 57  LYS B O   1 
ATOM   3641 C CB  . LYS B 1 28  ? 5.703   32.870  -0.352  1.00 62.64  ? 57  LYS B CB  1 
ATOM   3642 C CG  . LYS B 1 28  ? 4.883   32.104  -1.393  1.00 64.67  ? 57  LYS B CG  1 
ATOM   3643 C CD  . LYS B 1 28  ? 4.467   32.892  -2.633  1.00 64.40  ? 57  LYS B CD  1 
ATOM   3644 C CE  . LYS B 1 28  ? 5.612   33.270  -3.529  1.00 62.29  ? 57  LYS B CE  1 
ATOM   3645 N NZ  . LYS B 1 28  ? 5.165   33.878  -4.788  1.00 60.23  ? 57  LYS B NZ  1 
ATOM   3646 N N   . THR B 1 29  ? 6.938   32.308  3.140   1.00 70.40  ? 58  THR B N   1 
ATOM   3647 C CA  . THR B 1 29  ? 7.681   32.920  4.235   1.00 70.69  ? 58  THR B CA  1 
ATOM   3648 C C   . THR B 1 29  ? 9.054   32.255  4.362   1.00 69.58  ? 58  THR B C   1 
ATOM   3649 O O   . THR B 1 29  ? 9.156   31.103  4.780   1.00 66.89  ? 58  THR B O   1 
ATOM   3650 C CB  . THR B 1 29  ? 6.895   32.794  5.543   1.00 70.70  ? 58  THR B CB  1 
ATOM   3651 O OG1 . THR B 1 29  ? 5.554   33.208  5.299   1.00 70.74  ? 58  THR B OG1 1 
ATOM   3652 C CG2 . THR B 1 29  ? 7.491   33.632  6.661   1.00 71.35  ? 58  THR B CG2 1 
ATOM   3653 N N   . VAL B 1 30  ? 10.112  33.003  4.032   1.00 68.45  ? 59  VAL B N   1 
ATOM   3654 C CA  . VAL B 1 30  ? 11.479  32.531  4.192   1.00 66.57  ? 59  VAL B CA  1 
ATOM   3655 C C   . VAL B 1 30  ? 11.735  32.235  5.670   1.00 65.89  ? 59  VAL B C   1 
ATOM   3656 O O   . VAL B 1 30  ? 11.656  33.146  6.491   1.00 69.81  ? 59  VAL B O   1 
ATOM   3657 C CB  . VAL B 1 30  ? 12.477  33.576  3.652   1.00 62.98  ? 59  VAL B CB  1 
ATOM   3658 C CG1 . VAL B 1 30  ? 13.923  33.213  3.972   1.00 62.38  ? 59  VAL B CG1 1 
ATOM   3659 C CG2 . VAL B 1 30  ? 12.297  33.805  2.156   1.00 61.88  ? 59  VAL B CG2 1 
ATOM   3660 N N   . VAL B 1 31  ? 12.056  30.970  5.994   1.00 61.32  ? 60  VAL B N   1 
ATOM   3661 C CA  . VAL B 1 31  ? 12.291  30.554  7.372   1.00 58.63  ? 60  VAL B CA  1 
ATOM   3662 C C   . VAL B 1 31  ? 13.779  30.308  7.617   1.00 59.40  ? 60  VAL B C   1 
ATOM   3663 O O   . VAL B 1 31  ? 14.186  30.110  8.761   1.00 59.71  ? 60  VAL B O   1 
ATOM   3664 C CB  . VAL B 1 31  ? 11.480  29.307  7.777   1.00 56.52  ? 60  VAL B CB  1 
ATOM   3665 C CG1 . VAL B 1 31  ? 9.988   29.499  7.539   1.00 54.90  ? 60  VAL B CG1 1 
ATOM   3666 C CG2 . VAL B 1 31  ? 11.977  28.038  7.090   1.00 57.59  ? 60  VAL B CG2 1 
ATOM   3667 N N   . GLY B 1 32  ? 14.592  30.296  6.554   1.00 60.08  ? 61  GLY B N   1 
ATOM   3668 C CA  . GLY B 1 32  ? 16.012  30.028  6.712   1.00 57.59  ? 61  GLY B CA  1 
ATOM   3669 C C   . GLY B 1 32  ? 16.811  30.375  5.459   1.00 57.00  ? 61  GLY B C   1 
ATOM   3670 O O   . GLY B 1 32  ? 16.272  30.410  4.357   1.00 57.10  ? 61  GLY B O   1 
ATOM   3671 N N   . GLN B 1 33  ? 18.108  30.632  5.659   1.00 58.43  ? 62  GLN B N   1 
ATOM   3672 C CA  . GLN B 1 33  ? 19.054  30.788  4.569   1.00 59.29  ? 62  GLN B CA  1 
ATOM   3673 C C   . GLN B 1 33  ? 19.695  29.427  4.297   1.00 61.17  ? 62  GLN B C   1 
ATOM   3674 O O   . GLN B 1 33  ? 19.542  28.496  5.087   1.00 60.72  ? 62  GLN B O   1 
ATOM   3675 C CB  . GLN B 1 33  ? 20.107  31.843  4.920   1.00 59.87  ? 62  GLN B CB  1 
ATOM   3676 C CG  . GLN B 1 33  ? 19.542  33.165  5.435   1.00 61.63  ? 62  GLN B CG  1 
ATOM   3677 C CD  . GLN B 1 33  ? 18.724  33.918  4.409   1.00 65.39  ? 62  GLN B CD  1 
ATOM   3678 O OE1 . GLN B 1 33  ? 17.490  33.939  4.459   1.00 71.15  ? 62  GLN B OE1 1 
ATOM   3679 N NE2 . GLN B 1 33  ? 19.402  34.547  3.460   1.00 67.18  ? 62  GLN B NE2 1 
ATOM   3680 N N   . ILE B 1 34  ? 20.391  29.323  3.159   1.00 60.68  ? 63  ILE B N   1 
ATOM   3681 C CA  . ILE B 1 34  ? 21.181  28.149  2.820   1.00 60.48  ? 63  ILE B CA  1 
ATOM   3682 C C   . ILE B 1 34  ? 22.587  28.620  2.458   1.00 53.90  ? 63  ILE B C   1 
ATOM   3683 O O   . ILE B 1 34  ? 22.766  29.287  1.450   1.00 51.31  ? 63  ILE B O   1 
ATOM   3684 C CB  . ILE B 1 34  ? 20.537  27.357  1.662   1.00 65.50  ? 63  ILE B CB  1 
ATOM   3685 C CG1 . ILE B 1 34  ? 19.088  26.971  1.963   1.00 64.98  ? 63  ILE B CG1 1 
ATOM   3686 C CG2 . ILE B 1 34  ? 21.378  26.130  1.299   1.00 66.06  ? 63  ILE B CG2 1 
ATOM   3687 C CD1 . ILE B 1 34  ? 18.314  26.470  0.756   1.00 66.33  ? 63  ILE B CD1 1 
ATOM   3688 N N   . THR B 1 35  ? 23.583  28.287  3.283   1.00 55.06  ? 64  THR B N   1 
ATOM   3689 C CA  . THR B 1 35  ? 24.953  28.668  2.984   1.00 55.69  ? 64  THR B CA  1 
ATOM   3690 C C   . THR B 1 35  ? 25.649  27.517  2.264   1.00 56.73  ? 64  THR B C   1 
ATOM   3691 O O   . THR B 1 35  ? 25.194  26.378  2.301   1.00 61.97  ? 64  THR B O   1 
ATOM   3692 C CB  . THR B 1 35  ? 25.712  29.062  4.252   1.00 55.94  ? 64  THR B CB  1 
ATOM   3693 O OG1 . THR B 1 35  ? 25.964  27.840  4.941   1.00 60.71  ? 64  THR B OG1 1 
ATOM   3694 C CG2 . THR B 1 35  ? 24.952  30.062  5.106   1.00 53.87  ? 64  THR B CG2 1 
ATOM   3695 N N   . VAL B 1 36  ? 26.770  27.836  1.613   1.00 56.13  ? 65  VAL B N   1 
ATOM   3696 C CA  . VAL B 1 36  ? 27.636  26.832  1.017   1.00 54.47  ? 65  VAL B CA  1 
ATOM   3697 C C   . VAL B 1 36  ? 27.952  25.763  2.067   1.00 57.69  ? 65  VAL B C   1 
ATOM   3698 O O   . VAL B 1 36  ? 27.940  24.570  1.760   1.00 55.50  ? 65  VAL B O   1 
ATOM   3699 C CB  . VAL B 1 36  ? 28.903  27.511  0.449   1.00 51.48  ? 65  VAL B CB  1 
ATOM   3700 C CG1 . VAL B 1 36  ? 30.035  26.530  0.159   1.00 53.09  ? 65  VAL B CG1 1 
ATOM   3701 C CG2 . VAL B 1 36  ? 28.589  28.322  -0.801  1.00 49.95  ? 65  VAL B CG2 1 
ATOM   3702 N N   . ASP B 1 37  ? 28.212  26.204  3.308   1.00 57.06  ? 66  ASP B N   1 
ATOM   3703 C CA  . ASP B 1 37  ? 28.584  25.308  4.391   1.00 56.92  ? 66  ASP B CA  1 
ATOM   3704 C C   . ASP B 1 37  ? 27.437  24.356  4.731   1.00 52.84  ? 66  ASP B C   1 
ATOM   3705 O O   . ASP B 1 37  ? 27.694  23.217  5.104   1.00 54.60  ? 66  ASP B O   1 
ATOM   3706 C CB  . ASP B 1 37  ? 29.084  26.076  5.606   1.00 57.54  ? 66  ASP B CB  1 
ATOM   3707 C CG  . ASP B 1 37  ? 30.558  26.451  5.589   1.00 58.62  ? 66  ASP B CG  1 
ATOM   3708 O OD1 . ASP B 1 37  ? 31.323  25.820  4.824   1.00 55.32  ? 66  ASP B OD1 1 
ATOM   3709 O OD2 . ASP B 1 37  ? 30.928  27.382  6.338   1.00 61.22  ? 66  ASP B OD2 1 
ATOM   3710 N N   . MET B 1 38  ? 26.185  24.810  4.606   1.00 49.06  ? 67  MET B N   1 
ATOM   3711 C CA  . MET B 1 38  ? 25.038  23.947  4.848   1.00 53.22  ? 67  MET B CA  1 
ATOM   3712 C C   . MET B 1 38  ? 24.976  22.826  3.809   1.00 53.63  ? 67  MET B C   1 
ATOM   3713 O O   . MET B 1 38  ? 24.526  21.724  4.114   1.00 50.77  ? 67  MET B O   1 
ATOM   3714 C CB  . MET B 1 38  ? 23.713  24.719  4.808   1.00 56.77  ? 67  MET B CB  1 
ATOM   3715 C CG  . MET B 1 38  ? 23.472  25.638  6.000   1.00 58.05  ? 67  MET B CG  1 
ATOM   3716 S SD  . MET B 1 38  ? 21.779  26.262  6.059   1.00 57.98  ? 67  MET B SD  1 
ATOM   3717 C CE  . MET B 1 38  ? 21.857  27.358  7.482   1.00 57.92  ? 67  MET B CE  1 
ATOM   3718 N N   . MET B 1 39  ? 25.419  23.111  2.579   1.00 51.80  ? 68  MET B N   1 
ATOM   3719 C CA  . MET B 1 39  ? 25.336  22.149  1.490   1.00 49.38  ? 68  MET B CA  1 
ATOM   3720 C C   . MET B 1 39  ? 26.472  21.132  1.598   1.00 48.12  ? 68  MET B C   1 
ATOM   3721 O O   . MET B 1 39  ? 26.301  19.972  1.224   1.00 44.27  ? 68  MET B O   1 
ATOM   3722 C CB  . MET B 1 39  ? 25.412  22.850  0.128   1.00 48.90  ? 68  MET B CB  1 
ATOM   3723 C CG  . MET B 1 39  ? 24.302  23.844  -0.128  1.00 47.93  ? 68  MET B CG  1 
ATOM   3724 S SD  . MET B 1 39  ? 24.343  24.472  -1.818  1.00 46.76  ? 68  MET B SD  1 
ATOM   3725 C CE  . MET B 1 39  ? 23.702  23.031  -2.681  1.00 47.98  ? 68  MET B CE  1 
ATOM   3726 N N   . TYR B 1 40  ? 27.641  21.595  2.067   1.00 48.65  ? 69  TYR B N   1 
ATOM   3727 C CA  . TYR B 1 40  ? 28.778  20.724  2.321   1.00 46.70  ? 69  TYR B CA  1 
ATOM   3728 C C   . TYR B 1 40  ? 28.656  20.099  3.712   1.00 41.86  ? 69  TYR B C   1 
ATOM   3729 O O   . TYR B 1 40  ? 29.275  19.074  3.975   1.00 45.74  ? 69  TYR B O   1 
ATOM   3730 C CB  . TYR B 1 40  ? 30.118  21.458  2.182   1.00 45.76  ? 69  TYR B CB  1 
ATOM   3731 C CG  . TYR B 1 40  ? 30.544  21.783  0.755   1.00 44.39  ? 69  TYR B CG  1 
ATOM   3732 C CD1 . TYR B 1 40  ? 31.254  20.866  -0.018  1.00 43.02  ? 69  TYR B CD1 1 
ATOM   3733 C CD2 . TYR B 1 40  ? 30.254  23.018  0.185   1.00 45.02  ? 69  TYR B CD2 1 
ATOM   3734 C CE1 . TYR B 1 40  ? 31.650  21.166  -1.313  1.00 41.96  ? 69  TYR B CE1 1 
ATOM   3735 C CE2 . TYR B 1 40  ? 30.640  23.326  -1.109  1.00 43.47  ? 69  TYR B CE2 1 
ATOM   3736 C CZ  . TYR B 1 40  ? 31.342  22.401  -1.857  1.00 41.92  ? 69  TYR B CZ  1 
ATOM   3737 O OH  . TYR B 1 40  ? 31.702  22.746  -3.127  1.00 44.57  ? 69  TYR B OH  1 
ATOM   3738 N N   . GLY B 1 41  ? 27.843  20.696  4.587   1.00 42.60  ? 70  GLY B N   1 
ATOM   3739 C CA  . GLY B 1 41  ? 27.797  20.305  5.989   1.00 43.85  ? 70  GLY B CA  1 
ATOM   3740 C C   . GLY B 1 41  ? 26.599  19.420  6.334   1.00 43.88  ? 70  GLY B C   1 
ATOM   3741 O O   . GLY B 1 41  ? 26.299  19.240  7.510   1.00 39.72  ? 70  GLY B O   1 
ATOM   3742 N N   . GLY B 1 42  ? 25.918  18.886  5.309   1.00 46.32  ? 71  GLY B N   1 
ATOM   3743 C CA  . GLY B 1 42  ? 24.843  17.920  5.494   1.00 45.69  ? 71  GLY B CA  1 
ATOM   3744 C C   . GLY B 1 42  ? 23.556  18.562  6.011   1.00 45.31  ? 71  GLY B C   1 
ATOM   3745 O O   . GLY B 1 42  ? 22.869  17.989  6.858   1.00 46.05  ? 71  GLY B O   1 
ATOM   3746 N N   . MET B 1 43  ? 23.239  19.747  5.481   1.00 42.40  ? 72  MET B N   1 
ATOM   3747 C CA  . MET B 1 43  ? 22.011  20.461  5.793   1.00 43.67  ? 72  MET B CA  1 
ATOM   3748 C C   . MET B 1 43  ? 21.972  20.844  7.271   1.00 42.79  ? 72  MET B C   1 
ATOM   3749 O O   . MET B 1 43  ? 20.899  20.958  7.855   1.00 41.35  ? 72  MET B O   1 
ATOM   3750 C CB  . MET B 1 43  ? 20.775  19.623  5.439   1.00 44.77  ? 72  MET B CB  1 
ATOM   3751 C CG  . MET B 1 43  ? 20.815  19.015  4.055   1.00 45.44  ? 72  MET B CG  1 
ATOM   3752 S SD  . MET B 1 43  ? 19.432  17.891  3.778   1.00 44.66  ? 72  MET B SD  1 
ATOM   3753 C CE  . MET B 1 43  ? 19.814  17.423  2.084   1.00 47.23  ? 72  MET B CE  1 
ATOM   3754 N N   . ARG B 1 44  ? 23.152  21.036  7.845   1.00 47.43  ? 73  ARG B N   1 
ATOM   3755 C CA  . ARG B 1 44  ? 23.225  21.384  9.284   1.00 54.65  ? 73  ARG B CA  1 
ATOM   3756 C C   . ARG B 1 44  ? 22.581  22.758  9.506   1.00 57.04  ? 73  ARG B C   1 
ATOM   3757 O O   . ARG B 1 44  ? 23.105  23.751  8.973   1.00 56.21  ? 73  ARG B O   1 
ATOM   3758 C CB  . ARG B 1 44  ? 24.652  21.322  9.836   1.00 59.81  ? 73  ARG B CB  1 
ATOM   3759 C CG  . ARG B 1 44  ? 24.671  20.882  11.293  1.00 66.45  ? 73  ARG B CG  1 
ATOM   3760 C CD  . ARG B 1 44  ? 25.576  19.688  11.552  1.00 74.50  ? 73  ARG B CD  1 
ATOM   3761 N NE  . ARG B 1 44  ? 24.895  18.400  11.383  1.00 81.24  ? 73  ARG B NE  1 
ATOM   3762 C CZ  . ARG B 1 44  ? 24.980  17.670  10.281  1.00 85.51  ? 73  ARG B CZ  1 
ATOM   3763 N NH1 . ARG B 1 44  ? 26.008  16.865  10.099  1.00 86.71  ? 73  ARG B NH1 1 
ATOM   3764 N NH2 . ARG B 1 44  ? 24.044  17.757  9.358   1.00 84.25  ? 73  ARG B NH2 1 
ATOM   3765 N N   . GLY B 1 45  ? 21.486  22.791  10.262  1.00 56.39  ? 74  GLY B N   1 
ATOM   3766 C CA  . GLY B 1 45  ? 20.762  24.019  10.553  1.00 54.07  ? 74  GLY B CA  1 
ATOM   3767 C C   . GLY B 1 45  ? 19.627  24.265  9.560   1.00 51.77  ? 74  GLY B C   1 
ATOM   3768 O O   . GLY B 1 45  ? 18.796  25.140  9.779   1.00 49.62  ? 74  GLY B O   1 
ATOM   3769 N N   . MET B 1 46  ? 19.601  23.499  8.465   1.00 49.98  ? 75  MET B N   1 
ATOM   3770 C CA  . MET B 1 46  ? 18.596  23.667  7.431   1.00 50.60  ? 75  MET B CA  1 
ATOM   3771 C C   . MET B 1 46  ? 17.266  23.101  7.928   1.00 52.05  ? 75  MET B C   1 
ATOM   3772 O O   . MET B 1 46  ? 17.185  21.932  8.300   1.00 49.03  ? 75  MET B O   1 
ATOM   3773 C CB  . MET B 1 46  ? 19.029  22.944  6.151   1.00 52.16  ? 75  MET B CB  1 
ATOM   3774 C CG  . MET B 1 46  ? 18.260  23.341  4.897   1.00 54.73  ? 75  MET B CG  1 
ATOM   3775 S SD  . MET B 1 46  ? 18.818  22.502  3.396   1.00 54.11  ? 75  MET B SD  1 
ATOM   3776 C CE  . MET B 1 46  ? 20.575  22.887  3.352   1.00 50.75  ? 75  MET B CE  1 
ATOM   3777 N N   . LYS B 1 47  ? 16.230  23.948  7.942   1.00 51.88  ? 76  LYS B N   1 
ATOM   3778 C CA  . LYS B 1 47  ? 14.864  23.488  8.126   1.00 53.47  ? 76  LYS B CA  1 
ATOM   3779 C C   . LYS B 1 47  ? 14.371  22.916  6.801   1.00 51.68  ? 76  LYS B C   1 
ATOM   3780 O O   . LYS B 1 47  ? 14.073  23.670  5.880   1.00 50.36  ? 76  LYS B O   1 
ATOM   3781 C CB  . LYS B 1 47  ? 13.953  24.622  8.612   1.00 58.93  ? 76  LYS B CB  1 
ATOM   3782 C CG  . LYS B 1 47  ? 14.378  25.235  9.942   1.00 61.64  ? 76  LYS B CG  1 
ATOM   3783 C CD  . LYS B 1 47  ? 13.341  26.162  10.562  1.00 66.23  ? 76  LYS B CD  1 
ATOM   3784 C CE  . LYS B 1 47  ? 13.754  26.673  11.908  1.00 67.59  ? 76  LYS B CE  1 
ATOM   3785 N NZ  . LYS B 1 47  ? 14.860  27.628  11.815  1.00 69.18  ? 76  LYS B NZ  1 
ATOM   3786 N N   . GLY B 1 48  ? 14.272  21.583  6.723   1.00 49.61  ? 77  GLY B N   1 
ATOM   3787 C CA  . GLY B 1 48  ? 14.135  20.891  5.450   1.00 46.11  ? 77  GLY B CA  1 
ATOM   3788 C C   . GLY B 1 48  ? 12.732  20.340  5.193   1.00 46.81  ? 77  GLY B C   1 
ATOM   3789 O O   . GLY B 1 48  ? 12.293  20.293  4.041   1.00 48.29  ? 77  GLY B O   1 
ATOM   3790 N N   . LEU B 1 49  ? 12.038  19.884  6.244   1.00 44.11  ? 78  LEU B N   1 
ATOM   3791 C CA  . LEU B 1 49  ? 10.837  19.095  6.029   1.00 43.98  ? 78  LEU B CA  1 
ATOM   3792 C C   . LEU B 1 49  ? 9.880   19.188  7.215   1.00 42.76  ? 78  LEU B C   1 
ATOM   3793 O O   . LEU B 1 49  ? 10.249  19.613  8.307   1.00 38.56  ? 78  LEU B O   1 
ATOM   3794 C CB  . LEU B 1 49  ? 11.195  17.639  5.730   1.00 47.68  ? 78  LEU B CB  1 
ATOM   3795 C CG  . LEU B 1 49  ? 11.768  16.815  6.888   1.00 50.16  ? 78  LEU B CG  1 
ATOM   3796 C CD1 . LEU B 1 49  ? 11.525  15.335  6.646   1.00 51.03  ? 78  LEU B CD1 1 
ATOM   3797 C CD2 . LEU B 1 49  ? 13.253  17.073  7.095   1.00 52.98  ? 78  LEU B CD2 1 
ATOM   3798 N N   . VAL B 1 50  ? 8.638   18.765  6.949   1.00 39.83  ? 79  VAL B N   1 
ATOM   3799 C CA  . VAL B 1 50  ? 7.570   18.736  7.931   1.00 39.70  ? 79  VAL B CA  1 
ATOM   3800 C C   . VAL B 1 50  ? 7.519   17.341  8.543   1.00 36.07  ? 79  VAL B C   1 
ATOM   3801 O O   . VAL B 1 50  ? 7.430   16.350  7.829   1.00 34.96  ? 79  VAL B O   1 
ATOM   3802 C CB  . VAL B 1 50  ? 6.231   19.095  7.258   1.00 42.94  ? 79  VAL B CB  1 
ATOM   3803 C CG1 . VAL B 1 50  ? 5.058   19.082  8.239   1.00 42.91  ? 79  VAL B CG1 1 
ATOM   3804 C CG2 . VAL B 1 50  ? 6.314   20.437  6.540   1.00 45.96  ? 79  VAL B CG2 1 
ATOM   3805 N N   . TYR B 1 51  ? 7.574   17.274  9.870   1.00 34.02  ? 80  TYR B N   1 
ATOM   3806 C CA  . TYR B 1 51  ? 7.405   16.016  10.574  1.00 35.86  ? 80  TYR B CA  1 
ATOM   3807 C C   . TYR B 1 51  ? 6.521   16.299  11.782  1.00 35.81  ? 80  TYR B C   1 
ATOM   3808 O O   . TYR B 1 51  ? 6.892   17.107  12.629  1.00 35.79  ? 80  TYR B O   1 
ATOM   3809 C CB  . TYR B 1 51  ? 8.807   15.498  10.908  1.00 35.77  ? 80  TYR B CB  1 
ATOM   3810 C CG  . TYR B 1 51  ? 8.936   14.010  11.193  1.00 35.63  ? 80  TYR B CG  1 
ATOM   3811 C CD1 . TYR B 1 51  ? 8.821   13.506  12.488  1.00 35.04  ? 80  TYR B CD1 1 
ATOM   3812 C CD2 . TYR B 1 51  ? 9.208   13.108  10.166  1.00 35.93  ? 80  TYR B CD2 1 
ATOM   3813 C CE1 . TYR B 1 51  ? 8.964   12.150  12.748  1.00 32.88  ? 80  TYR B CE1 1 
ATOM   3814 C CE2 . TYR B 1 51  ? 9.355   11.751  10.413  1.00 33.38  ? 80  TYR B CE2 1 
ATOM   3815 C CZ  . TYR B 1 51  ? 9.235   11.274  11.707  1.00 32.62  ? 80  TYR B CZ  1 
ATOM   3816 O OH  . TYR B 1 51  ? 9.369   9.942   11.937  1.00 33.15  ? 80  TYR B OH  1 
ATOM   3817 N N   . GLU B 1 52  ? 5.354   15.649  11.827  1.00 38.86  ? 81  GLU B N   1 
ATOM   3818 C CA  . GLU B 1 52  ? 4.271   16.063  12.706  1.00 43.74  ? 81  GLU B CA  1 
ATOM   3819 C C   . GLU B 1 52  ? 4.370   15.401  14.081  1.00 44.18  ? 81  GLU B C   1 
ATOM   3820 O O   . GLU B 1 52  ? 3.895   15.981  15.056  1.00 48.86  ? 81  GLU B O   1 
ATOM   3821 C CB  . GLU B 1 52  ? 2.896   15.697  12.144  1.00 45.98  ? 81  GLU B CB  1 
ATOM   3822 C CG  . GLU B 1 52  ? 2.601   16.258  10.756  1.00 49.08  ? 81  GLU B CG  1 
ATOM   3823 C CD  . GLU B 1 52  ? 2.304   17.748  10.677  1.00 52.19  ? 81  GLU B CD  1 
ATOM   3824 O OE1 . GLU B 1 52  ? 2.745   18.563  11.522  1.00 51.30  ? 81  GLU B OE1 1 
ATOM   3825 O OE2 . GLU B 1 52  ? 1.571   18.085  9.729   1.00 55.54  ? 81  GLU B OE2 1 
ATOM   3826 N N   . THR B 1 53  ? 4.972   14.203  14.160  1.00 38.96  ? 82  THR B N   1 
ATOM   3827 C CA  . THR B 1 53  ? 4.773   13.328  15.308  1.00 37.45  ? 82  THR B CA  1 
ATOM   3828 C C   . THR B 1 53  ? 5.639   13.760  16.491  1.00 35.14  ? 82  THR B C   1 
ATOM   3829 O O   . THR B 1 53  ? 5.220   13.608  17.633  1.00 35.05  ? 82  THR B O   1 
ATOM   3830 C CB  . THR B 1 53  ? 5.009   11.860  14.939  1.00 38.63  ? 82  THR B CB  1 
ATOM   3831 O OG1 . THR B 1 53  ? 6.330   11.744  14.417  1.00 38.49  ? 82  THR B OG1 1 
ATOM   3832 C CG2 . THR B 1 53  ? 3.990   11.345  13.939  1.00 39.27  ? 82  THR B CG2 1 
ATOM   3833 N N   . SER B 1 54  ? 6.841   14.283  16.236  1.00 37.31  ? 83  SER B N   1 
ATOM   3834 C CA  . SER B 1 54  ? 7.714   14.717  17.319  1.00 36.38  ? 83  SER B CA  1 
ATOM   3835 C C   . SER B 1 54  ? 8.630   15.857  16.882  1.00 37.09  ? 83  SER B C   1 
ATOM   3836 O O   . SER B 1 54  ? 8.927   16.028  15.702  1.00 36.51  ? 83  SER B O   1 
ATOM   3837 C CB  . SER B 1 54  ? 8.527   13.573  17.847  1.00 37.07  ? 83  SER B CB  1 
ATOM   3838 O OG  . SER B 1 54  ? 9.483   13.159  16.884  1.00 38.28  ? 83  SER B OG  1 
ATOM   3839 N N   . VAL B 1 55  ? 9.098   16.617  17.877  1.00 39.92  ? 84  VAL B N   1 
ATOM   3840 C CA  . VAL B 1 55  ? 9.864   17.829  17.653  1.00 39.21  ? 84  VAL B CA  1 
ATOM   3841 C C   . VAL B 1 55  ? 10.963  17.893  18.707  1.00 42.94  ? 84  VAL B C   1 
ATOM   3842 O O   . VAL B 1 55  ? 10.723  17.597  19.875  1.00 42.33  ? 84  VAL B O   1 
ATOM   3843 C CB  . VAL B 1 55  ? 8.968   19.083  17.705  1.00 41.30  ? 84  VAL B CB  1 
ATOM   3844 C CG1 . VAL B 1 55  ? 9.761   20.365  17.464  1.00 41.19  ? 84  VAL B CG1 1 
ATOM   3845 C CG2 . VAL B 1 55  ? 7.792   18.989  16.737  1.00 40.07  ? 84  VAL B CG2 1 
ATOM   3846 N N   . LEU B 1 56  ? 12.161  18.310  18.282  1.00 45.56  ? 85  LEU B N   1 
ATOM   3847 C CA  . LEU B 1 56  ? 13.337  18.274  19.133  1.00 49.95  ? 85  LEU B CA  1 
ATOM   3848 C C   . LEU B 1 56  ? 13.845  19.695  19.352  1.00 53.81  ? 85  LEU B C   1 
ATOM   3849 O O   . LEU B 1 56  ? 14.434  20.291  18.454  1.00 62.24  ? 85  LEU B O   1 
ATOM   3850 C CB  . LEU B 1 56  ? 14.388  17.386  18.471  1.00 49.71  ? 85  LEU B CB  1 
ATOM   3851 C CG  . LEU B 1 56  ? 15.753  17.314  19.156  1.00 52.36  ? 85  LEU B CG  1 
ATOM   3852 C CD1 . LEU B 1 56  ? 15.660  16.615  20.497  1.00 54.66  ? 85  LEU B CD1 1 
ATOM   3853 C CD2 . LEU B 1 56  ? 16.743  16.616  18.246  1.00 52.89  ? 85  LEU B CD2 1 
ATOM   3854 N N   . ASP B 1 57  ? 13.609  20.230  20.553  1.00 54.59  ? 86  ASP B N   1 
ATOM   3855 C CA  . ASP B 1 57  ? 14.176  21.512  20.942  1.00 59.56  ? 86  ASP B CA  1 
ATOM   3856 C C   . ASP B 1 57  ? 15.628  21.289  21.371  1.00 61.34  ? 86  ASP B C   1 
ATOM   3857 O O   . ASP B 1 57  ? 15.925  20.346  22.101  1.00 62.54  ? 86  ASP B O   1 
ATOM   3858 C CB  . ASP B 1 57  ? 13.287  22.258  21.934  1.00 61.20  ? 86  ASP B CB  1 
ATOM   3859 C CG  . ASP B 1 57  ? 12.218  21.442  22.653  1.00 61.69  ? 86  ASP B CG  1 
ATOM   3860 O OD1 . ASP B 1 57  ? 11.413  20.778  21.963  1.00 64.20  ? 86  ASP B OD1 1 
ATOM   3861 O OD2 . ASP B 1 57  ? 12.172  21.501  23.896  1.00 61.97  ? 86  ASP B OD2 1 
ATOM   3862 N N   . PRO B 1 58  ? 16.590  22.127  20.911  1.00 66.30  ? 87  PRO B N   1 
ATOM   3863 C CA  . PRO B 1 58  ? 18.003  21.932  21.255  1.00 70.00  ? 87  PRO B CA  1 
ATOM   3864 C C   . PRO B 1 58  ? 18.383  22.219  22.710  1.00 73.50  ? 87  PRO B C   1 
ATOM   3865 O O   . PRO B 1 58  ? 19.564  22.248  23.043  1.00 75.81  ? 87  PRO B O   1 
ATOM   3866 C CB  . PRO B 1 58  ? 18.729  22.884  20.271  1.00 66.03  ? 87  PRO B CB  1 
ATOM   3867 C CG  . PRO B 1 58  ? 17.722  23.968  19.977  1.00 63.05  ? 87  PRO B CG  1 
ATOM   3868 C CD  . PRO B 1 58  ? 16.372  23.273  20.009  1.00 62.58  ? 87  PRO B CD  1 
ATOM   3869 N N   . ASP B 1 59  ? 17.380  22.411  23.575  1.00 78.18  ? 88  ASP B N   1 
ATOM   3870 C CA  . ASP B 1 59  ? 17.613  22.783  24.962  1.00 80.28  ? 88  ASP B CA  1 
ATOM   3871 C C   . ASP B 1 59  ? 17.066  21.707  25.903  1.00 73.86  ? 88  ASP B C   1 
ATOM   3872 O O   . ASP B 1 59  ? 17.771  21.275  26.812  1.00 70.04  ? 88  ASP B O   1 
ATOM   3873 C CB  . ASP B 1 59  ? 17.088  24.183  25.249  1.00 87.41  ? 88  ASP B CB  1 
ATOM   3874 C CG  . ASP B 1 59  ? 15.696  24.494  24.713  1.00 97.11  ? 88  ASP B CG  1 
ATOM   3875 O OD1 . ASP B 1 59  ? 15.472  24.285  23.499  1.00 98.20  ? 88  ASP B OD1 1 
ATOM   3876 O OD2 . ASP B 1 59  ? 14.854  24.963  25.510  1.00 104.01 ? 88  ASP B OD2 1 
ATOM   3877 N N   . GLU B 1 60  ? 15.816  21.274  25.686  1.00 67.34  ? 89  GLU B N   1 
ATOM   3878 C CA  . GLU B 1 60  ? 15.150  20.381  26.624  1.00 64.47  ? 89  GLU B CA  1 
ATOM   3879 C C   . GLU B 1 60  ? 14.812  19.041  25.971  1.00 56.99  ? 89  GLU B C   1 
ATOM   3880 O O   . GLU B 1 60  ? 14.070  18.243  26.544  1.00 55.27  ? 89  GLU B O   1 
ATOM   3881 C CB  . GLU B 1 60  ? 13.937  21.125  27.185  1.00 70.21  ? 89  GLU B CB  1 
ATOM   3882 C CG  . GLU B 1 60  ? 14.272  22.576  27.519  1.00 77.38  ? 89  GLU B CG  1 
ATOM   3883 C CD  . GLU B 1 60  ? 13.372  23.274  28.515  1.00 85.94  ? 89  GLU B CD  1 
ATOM   3884 O OE1 . GLU B 1 60  ? 13.866  23.606  29.616  1.00 86.63  ? 89  GLU B OE1 1 
ATOM   3885 O OE2 . GLU B 1 60  ? 12.193  23.510  28.181  1.00 98.15  ? 89  GLU B OE2 1 
ATOM   3886 N N   . GLY B 1 61  ? 15.370  18.791  24.780  1.00 51.40  ? 90  GLY B N   1 
ATOM   3887 C CA  . GLY B 1 61  ? 15.230  17.505  24.117  1.00 47.89  ? 90  GLY B CA  1 
ATOM   3888 C C   . GLY B 1 61  ? 13.870  17.345  23.444  1.00 43.85  ? 90  GLY B C   1 
ATOM   3889 O O   . GLY B 1 61  ? 13.213  18.336  23.123  1.00 38.96  ? 90  GLY B O   1 
ATOM   3890 N N   . ILE B 1 62  ? 13.468  16.077  23.265  1.00 40.98  ? 91  ILE B N   1 
ATOM   3891 C CA  . ILE B 1 62  ? 12.358  15.704  22.399  1.00 40.34  ? 91  ILE B CA  1 
ATOM   3892 C C   . ILE B 1 62  ? 11.024  15.967  23.091  1.00 41.80  ? 91  ILE B C   1 
ATOM   3893 O O   . ILE B 1 62  ? 10.910  15.840  24.306  1.00 43.56  ? 91  ILE B O   1 
ATOM   3894 C CB  . ILE B 1 62  ? 12.458  14.225  21.968  1.00 37.12  ? 91  ILE B CB  1 
ATOM   3895 C CG1 . ILE B 1 62  ? 11.578  13.918  20.749  1.00 38.09  ? 91  ILE B CG1 1 
ATOM   3896 C CG2 . ILE B 1 62  ? 12.134  13.279  23.124  1.00 36.87  ? 91  ILE B CG2 1 
ATOM   3897 C CD1 . ILE B 1 62  ? 12.054  14.549  19.449  1.00 38.74  ? 91  ILE B CD1 1 
ATOM   3898 N N   . ARG B 1 63  ? 10.013  16.297  22.281  1.00 44.28  ? 92  ARG B N   1 
ATOM   3899 C CA  . ARG B 1 63  ? 8.624   16.245  22.699  1.00 46.63  ? 92  ARG B CA  1 
ATOM   3900 C C   . ARG B 1 63  ? 7.867   15.383  21.698  1.00 48.52  ? 92  ARG B C   1 
ATOM   3901 O O   . ARG B 1 63  ? 8.036   15.561  20.491  1.00 50.48  ? 92  ARG B O   1 
ATOM   3902 C CB  . ARG B 1 63  ? 7.998   17.642  22.783  1.00 51.06  ? 92  ARG B CB  1 
ATOM   3903 C CG  . ARG B 1 63  ? 8.544   18.470  23.938  1.00 55.03  ? 92  ARG B CG  1 
ATOM   3904 C CD  . ARG B 1 63  ? 7.929   19.860  24.035  1.00 58.05  ? 92  ARG B CD  1 
ATOM   3905 N NE  . ARG B 1 63  ? 8.263   20.489  25.319  1.00 62.34  ? 92  ARG B NE  1 
ATOM   3906 C CZ  . ARG B 1 63  ? 7.749   20.177  26.514  1.00 64.92  ? 92  ARG B CZ  1 
ATOM   3907 N NH1 . ARG B 1 63  ? 6.706   19.368  26.615  1.00 68.12  ? 92  ARG B NH1 1 
ATOM   3908 N NH2 . ARG B 1 63  ? 8.260   20.711  27.614  1.00 62.33  ? 92  ARG B NH2 1 
ATOM   3909 N N   . PHE B 1 64  ? 7.079   14.432  22.225  1.00 46.22  ? 93  PHE B N   1 
ATOM   3910 C CA  . PHE B 1 64  ? 6.137   13.652  21.443  1.00 42.04  ? 93  PHE B CA  1 
ATOM   3911 C C   . PHE B 1 64  ? 4.809   14.397  21.448  1.00 44.09  ? 93  PHE B C   1 
ATOM   3912 O O   . PHE B 1 64  ? 4.210   14.553  22.512  1.00 43.60  ? 93  PHE B O   1 
ATOM   3913 C CB  . PHE B 1 64  ? 5.945   12.253  22.040  1.00 43.16  ? 93  PHE B CB  1 
ATOM   3914 C CG  . PHE B 1 64  ? 7.221   11.440  22.192  1.00 45.28  ? 93  PHE B CG  1 
ATOM   3915 C CD1 . PHE B 1 64  ? 8.087   11.262  21.121  1.00 45.34  ? 93  PHE B CD1 1 
ATOM   3916 C CD2 . PHE B 1 64  ? 7.573   10.886  23.418  1.00 47.47  ? 93  PHE B CD2 1 
ATOM   3917 C CE1 . PHE B 1 64  ? 9.251   10.526  21.266  1.00 44.38  ? 93  PHE B CE1 1 
ATOM   3918 C CE2 . PHE B 1 64  ? 8.746   10.160  23.558  1.00 46.35  ? 93  PHE B CE2 1 
ATOM   3919 C CZ  . PHE B 1 64  ? 9.582   9.984   22.484  1.00 43.19  ? 93  PHE B CZ  1 
ATOM   3920 N N   . ARG B 1 65  ? 4.383   14.867  20.264  1.00 40.91  ? 94  ARG B N   1 
ATOM   3921 C CA  . ARG B 1 65  ? 3.169   15.654  20.089  1.00 40.99  ? 94  ARG B CA  1 
ATOM   3922 C C   . ARG B 1 65  ? 2.912   16.574  21.287  1.00 42.34  ? 94  ARG B C   1 
ATOM   3923 O O   . ARG B 1 65  ? 1.789   16.629  21.781  1.00 44.62  ? 94  ARG B O   1 
ATOM   3924 C CB  . ARG B 1 65  ? 1.956   14.745  19.872  1.00 37.74  ? 94  ARG B CB  1 
ATOM   3925 C CG  . ARG B 1 65  ? 1.963   13.937  18.582  1.00 38.61  ? 94  ARG B CG  1 
ATOM   3926 C CD  . ARG B 1 65  ? 1.486   14.696  17.341  1.00 37.47  ? 94  ARG B CD  1 
ATOM   3927 N NE  . ARG B 1 65  ? 1.203   13.778  16.230  1.00 37.70  ? 94  ARG B NE  1 
ATOM   3928 C CZ  . ARG B 1 65  ? 0.630   14.090  15.069  1.00 38.80  ? 94  ARG B CZ  1 
ATOM   3929 N NH1 . ARG B 1 65  ? 0.222   15.322  14.818  1.00 38.99  ? 94  ARG B NH1 1 
ATOM   3930 N NH2 . ARG B 1 65  ? 0.459   13.154  14.150  1.00 40.73  ? 94  ARG B NH2 1 
ATOM   3931 N N   . GLY B 1 66  ? 3.951   17.279  21.751  1.00 41.37  ? 95  GLY B N   1 
ATOM   3932 C CA  . GLY B 1 66  ? 3.811   18.288  22.791  1.00 44.39  ? 95  GLY B CA  1 
ATOM   3933 C C   . GLY B 1 66  ? 4.356   17.843  24.148  1.00 44.67  ? 95  GLY B C   1 
ATOM   3934 O O   . GLY B 1 66  ? 4.809   18.679  24.929  1.00 41.09  ? 95  GLY B O   1 
ATOM   3935 N N   . PHE B 1 67  ? 4.302   16.535  24.429  1.00 46.12  ? 96  PHE B N   1 
ATOM   3936 C CA  . PHE B 1 67  ? 4.613   16.014  25.754  1.00 46.46  ? 96  PHE B CA  1 
ATOM   3937 C C   . PHE B 1 67  ? 6.088   15.617  25.833  1.00 48.70  ? 96  PHE B C   1 
ATOM   3938 O O   . PHE B 1 67  ? 6.603   14.959  24.934  1.00 48.42  ? 96  PHE B O   1 
ATOM   3939 C CB  . PHE B 1 67  ? 3.700   14.819  26.048  1.00 45.97  ? 96  PHE B CB  1 
ATOM   3940 C CG  . PHE B 1 67  ? 2.208   15.130  25.997  1.00 50.42  ? 96  PHE B CG  1 
ATOM   3941 C CD1 . PHE B 1 67  ? 1.554   15.687  27.093  1.00 51.79  ? 96  PHE B CD1 1 
ATOM   3942 C CD2 . PHE B 1 67  ? 1.460   14.862  24.855  1.00 52.83  ? 96  PHE B CD2 1 
ATOM   3943 C CE1 . PHE B 1 67  ? 0.195   15.962  27.046  1.00 51.85  ? 96  PHE B CE1 1 
ATOM   3944 C CE2 . PHE B 1 67  ? 0.100   15.140  24.814  1.00 54.27  ? 96  PHE B CE2 1 
ATOM   3945 C CZ  . PHE B 1 67  ? -0.530  15.687  25.909  1.00 54.00  ? 96  PHE B CZ  1 
ATOM   3946 N N   . SER B 1 68  ? 6.759   16.000  26.927  1.00 50.17  ? 97  SER B N   1 
ATOM   3947 C CA  . SER B 1 68  ? 8.124   15.565  27.185  1.00 52.05  ? 97  SER B CA  1 
ATOM   3948 C C   . SER B 1 68  ? 8.123   14.117  27.680  1.00 51.16  ? 97  SER B C   1 
ATOM   3949 O O   . SER B 1 68  ? 7.064   13.498  27.808  1.00 49.10  ? 97  SER B O   1 
ATOM   3950 C CB  . SER B 1 68  ? 8.824   16.481  28.167  1.00 53.09  ? 97  SER B CB  1 
ATOM   3951 O OG  . SER B 1 68  ? 8.302   16.318  29.479  1.00 58.29  ? 97  SER B OG  1 
ATOM   3952 N N   . ILE B 1 69  ? 9.324   13.585  27.951  1.00 53.58  ? 98  ILE B N   1 
ATOM   3953 C CA  . ILE B 1 69  ? 9.484   12.213  28.412  1.00 52.93  ? 98  ILE B CA  1 
ATOM   3954 C C   . ILE B 1 69  ? 8.854   12.058  29.800  1.00 47.34  ? 98  ILE B C   1 
ATOM   3955 O O   . ILE B 1 69  ? 8.060   11.145  30.009  1.00 42.74  ? 98  ILE B O   1 
ATOM   3956 C CB  . ILE B 1 69  ? 10.965  11.777  28.375  1.00 53.28  ? 98  ILE B CB  1 
ATOM   3957 C CG1 . ILE B 1 69  ? 11.542  11.825  26.955  1.00 54.05  ? 98  ILE B CG1 1 
ATOM   3958 C CG2 . ILE B 1 69  ? 11.159  10.394  29.005  1.00 52.91  ? 98  ILE B CG2 1 
ATOM   3959 C CD1 . ILE B 1 69  ? 10.963  10.792  26.009  1.00 53.08  ? 98  ILE B CD1 1 
ATOM   3960 N N   . PRO B 1 70  ? 9.159   12.921  30.797  1.00 47.29  ? 99  PRO B N   1 
ATOM   3961 C CA  . PRO B 1 70  ? 8.523   12.801  32.113  1.00 47.86  ? 99  PRO B CA  1 
ATOM   3962 C C   . PRO B 1 70  ? 6.994   12.829  32.041  1.00 44.53  ? 99  PRO B C   1 
ATOM   3963 O O   . PRO B 1 70  ? 6.329   12.077  32.747  1.00 43.34  ? 99  PRO B O   1 
ATOM   3964 C CB  . PRO B 1 70  ? 9.091   13.978  32.938  1.00 46.94  ? 99  PRO B CB  1 
ATOM   3965 C CG  . PRO B 1 70  ? 10.349  14.400  32.202  1.00 47.46  ? 99  PRO B CG  1 
ATOM   3966 C CD  . PRO B 1 70  ? 10.127  14.031  30.736  1.00 47.78  ? 99  PRO B CD  1 
ATOM   3967 N N   . GLU B 1 71  ? 6.443   13.684  31.171  1.00 46.75  ? 100 GLU B N   1 
ATOM   3968 C CA  . GLU B 1 71  ? 4.999   13.819  31.023  1.00 48.09  ? 100 GLU B CA  1 
ATOM   3969 C C   . GLU B 1 71  ? 4.406   12.522  30.483  1.00 45.40  ? 100 GLU B C   1 
ATOM   3970 O O   . GLU B 1 71  ? 3.311   12.132  30.877  1.00 41.81  ? 100 GLU B O   1 
ATOM   3971 C CB  . GLU B 1 71  ? 4.616   14.966  30.088  1.00 50.84  ? 100 GLU B CB  1 
ATOM   3972 C CG  . GLU B 1 71  ? 4.902   16.346  30.671  1.00 54.84  ? 100 GLU B CG  1 
ATOM   3973 C CD  . GLU B 1 71  ? 4.609   17.496  29.722  1.00 60.87  ? 100 GLU B CD  1 
ATOM   3974 O OE1 . GLU B 1 71  ? 3.836   18.402  30.108  1.00 65.92  ? 100 GLU B OE1 1 
ATOM   3975 O OE2 . GLU B 1 71  ? 5.146   17.486  28.592  1.00 59.12  ? 100 GLU B OE2 1 
ATOM   3976 N N   . CYS B 1 72  ? 5.134   11.877  29.562  1.00 44.04  ? 101 CYS B N   1 
ATOM   3977 C CA  . CYS B 1 72  ? 4.694   10.618  28.989  1.00 43.07  ? 101 CYS B CA  1 
ATOM   3978 C C   . CYS B 1 72  ? 4.750   9.528   30.056  1.00 41.45  ? 101 CYS B C   1 
ATOM   3979 O O   . CYS B 1 72  ? 3.858   8.699   30.137  1.00 41.17  ? 101 CYS B O   1 
ATOM   3980 C CB  . CYS B 1 72  ? 5.525   10.262  27.762  1.00 45.52  ? 101 CYS B CB  1 
ATOM   3981 S SG  . CYS B 1 72  ? 5.125   11.256  26.299  1.00 52.64  ? 101 CYS B SG  1 
ATOM   3982 N N   . GLN B 1 73  ? 5.792   9.548   30.893  1.00 44.12  ? 102 GLN B N   1 
ATOM   3983 C CA  . GLN B 1 73  ? 5.933   8.556   31.946  1.00 45.54  ? 102 GLN B CA  1 
ATOM   3984 C C   . GLN B 1 73  ? 4.726   8.586   32.886  1.00 45.33  ? 102 GLN B C   1 
ATOM   3985 O O   . GLN B 1 73  ? 4.292   7.536   33.348  1.00 44.79  ? 102 GLN B O   1 
ATOM   3986 C CB  . GLN B 1 73  ? 7.264   8.733   32.671  1.00 46.64  ? 102 GLN B CB  1 
ATOM   3987 C CG  . GLN B 1 73  ? 8.449   8.154   31.906  1.00 50.52  ? 102 GLN B CG  1 
ATOM   3988 C CD  . GLN B 1 73  ? 9.770   8.374   32.609  1.00 55.21  ? 102 GLN B CD  1 
ATOM   3989 O OE1 . GLN B 1 73  ? 10.266  9.503   32.702  1.00 57.35  ? 102 GLN B OE1 1 
ATOM   3990 N NE2 . GLN B 1 73  ? 10.353  7.295   33.114  1.00 57.60  ? 102 GLN B NE2 1 
ATOM   3991 N N   . LYS B 1 74  ? 4.171   9.780   33.138  1.00 47.41  ? 103 LYS B N   1 
ATOM   3992 C CA  . LYS B 1 74  ? 3.078   9.947   34.086  1.00 49.84  ? 103 LYS B CA  1 
ATOM   3993 C C   . LYS B 1 74  ? 1.737   9.532   33.485  1.00 47.35  ? 103 LYS B C   1 
ATOM   3994 O O   . LYS B 1 74  ? 0.958   8.852   34.151  1.00 48.82  ? 103 LYS B O   1 
ATOM   3995 C CB  . LYS B 1 74  ? 2.951   11.406  34.534  1.00 55.80  ? 103 LYS B CB  1 
ATOM   3996 C CG  . LYS B 1 74  ? 4.155   11.956  35.283  1.00 63.84  ? 103 LYS B CG  1 
ATOM   3997 C CD  . LYS B 1 74  ? 3.976   13.384  35.788  1.00 67.06  ? 103 LYS B CD  1 
ATOM   3998 C CE  . LYS B 1 74  ? 5.175   13.909  36.520  1.00 69.15  ? 103 LYS B CE  1 
ATOM   3999 N NZ  . LYS B 1 74  ? 6.289   14.252  35.630  1.00 71.01  ? 103 LYS B NZ  1 
ATOM   4000 N N   . LEU B 1 75  ? 1.480   9.951   32.235  1.00 45.12  ? 104 LEU B N   1 
ATOM   4001 C CA  . LEU B 1 75  ? 0.144   9.963   31.648  1.00 41.68  ? 104 LEU B CA  1 
ATOM   4002 C C   . LEU B 1 75  ? -0.173  8.671   30.901  1.00 42.30  ? 104 LEU B C   1 
ATOM   4003 O O   . LEU B 1 75  ? -1.320  8.224   30.901  1.00 40.76  ? 104 LEU B O   1 
ATOM   4004 C CB  . LEU B 1 75  ? 0.054   11.151  30.695  1.00 40.82  ? 104 LEU B CB  1 
ATOM   4005 C CG  . LEU B 1 75  ? 0.148   12.533  31.341  1.00 42.19  ? 104 LEU B CG  1 
ATOM   4006 C CD1 . LEU B 1 75  ? 0.411   13.580  30.273  1.00 42.13  ? 104 LEU B CD1 1 
ATOM   4007 C CD2 . LEU B 1 75  ? -1.124  12.842  32.121  1.00 44.22  ? 104 LEU B CD2 1 
ATOM   4008 N N   . LEU B 1 76  ? 0.835   8.107   30.226  1.00 42.10  ? 105 LEU B N   1 
ATOM   4009 C CA  . LEU B 1 76  ? 0.621   6.995   29.317  1.00 43.04  ? 105 LEU B CA  1 
ATOM   4010 C C   . LEU B 1 76  ? 0.280   5.738   30.110  1.00 43.28  ? 105 LEU B C   1 
ATOM   4011 O O   . LEU B 1 76  ? 0.910   5.444   31.123  1.00 40.50  ? 105 LEU B O   1 
ATOM   4012 C CB  . LEU B 1 76  ? 1.857   6.782   28.442  1.00 43.06  ? 105 LEU B CB  1 
ATOM   4013 C CG  . LEU B 1 76  ? 2.015   7.747   27.265  1.00 44.92  ? 105 LEU B CG  1 
ATOM   4014 C CD1 . LEU B 1 76  ? 3.382   7.582   26.623  1.00 46.36  ? 105 LEU B CD1 1 
ATOM   4015 C CD2 . LEU B 1 76  ? 0.923   7.527   26.231  1.00 46.79  ? 105 LEU B CD2 1 
ATOM   4016 N N   . PRO B 1 77  ? -0.715  4.939   29.669  1.00 44.75  ? 106 PRO B N   1 
ATOM   4017 C CA  . PRO B 1 77  ? -1.072  3.719   30.390  1.00 46.13  ? 106 PRO B CA  1 
ATOM   4018 C C   . PRO B 1 77  ? 0.155   2.840   30.606  1.00 45.95  ? 106 PRO B C   1 
ATOM   4019 O O   . PRO B 1 77  ? 1.158   2.980   29.910  1.00 45.33  ? 106 PRO B O   1 
ATOM   4020 C CB  . PRO B 1 77  ? -2.131  3.052   29.496  1.00 46.62  ? 106 PRO B CB  1 
ATOM   4021 C CG  . PRO B 1 77  ? -2.707  4.203   28.699  1.00 47.53  ? 106 PRO B CG  1 
ATOM   4022 C CD  . PRO B 1 77  ? -1.538  5.152   28.469  1.00 46.72  ? 106 PRO B CD  1 
ATOM   4023 N N   . LYS B 1 78  ? 0.051   1.947   31.593  1.00 46.18  ? 107 LYS B N   1 
ATOM   4024 C CA  . LYS B 1 78  ? 1.113   1.013   31.917  1.00 47.14  ? 107 LYS B CA  1 
ATOM   4025 C C   . LYS B 1 78  ? 0.515   -0.387  31.911  1.00 47.99  ? 107 LYS B C   1 
ATOM   4026 O O   . LYS B 1 78  ? -0.693  -0.539  31.745  1.00 47.61  ? 107 LYS B O   1 
ATOM   4027 C CB  . LYS B 1 78  ? 1.705   1.434   33.264  1.00 46.86  ? 107 LYS B CB  1 
ATOM   4028 C CG  . LYS B 1 78  ? 2.336   2.812   33.234  1.00 50.76  ? 107 LYS B CG  1 
ATOM   4029 C CD  . LYS B 1 78  ? 2.232   3.576   34.546  1.00 54.36  ? 107 LYS B CD  1 
ATOM   4030 C CE  . LYS B 1 78  ? 2.782   4.964   34.419  1.00 56.23  ? 107 LYS B CE  1 
ATOM   4031 N NZ  . LYS B 1 78  ? 1.940   5.827   33.585  1.00 56.06  ? 107 LYS B NZ  1 
ATOM   4032 N N   . ALA B 1 79  ? 1.371   -1.404  32.054  1.00 47.98  ? 108 ALA B N   1 
ATOM   4033 C CA  . ALA B 1 79  ? 0.900   -2.766  32.235  1.00 49.81  ? 108 ALA B CA  1 
ATOM   4034 C C   . ALA B 1 79  ? 0.345   -2.909  33.650  1.00 50.14  ? 108 ALA B C   1 
ATOM   4035 O O   . ALA B 1 79  ? 0.763   -2.186  34.553  1.00 48.98  ? 108 ALA B O   1 
ATOM   4036 C CB  . ALA B 1 79  ? 2.017   -3.751  31.971  1.00 47.47  ? 108 ALA B CB  1 
ATOM   4037 N N   . LYS B 1 80  ? -0.606  -3.831  33.829  1.00 53.56  ? 109 LYS B N   1 
ATOM   4038 C CA  . LYS B 1 80  ? -1.106  -4.155  35.156  1.00 53.77  ? 109 LYS B CA  1 
ATOM   4039 C C   . LYS B 1 80  ? 0.096   -4.444  36.045  1.00 56.32  ? 109 LYS B C   1 
ATOM   4040 O O   . LYS B 1 80  ? 0.864   -5.365  35.773  1.00 53.04  ? 109 LYS B O   1 
ATOM   4041 C CB  . LYS B 1 80  ? -2.052  -5.362  35.139  1.00 51.90  ? 109 LYS B CB  1 
ATOM   4042 N N   . GLY B 1 81  ? 0.263   -3.623  37.085  1.00 58.26  ? 110 GLY B N   1 
ATOM   4043 C CA  . GLY B 1 81  ? 1.386   -3.762  37.992  1.00 59.95  ? 110 GLY B CA  1 
ATOM   4044 C C   . GLY B 1 81  ? 2.691   -3.347  37.319  1.00 61.40  ? 110 GLY B C   1 
ATOM   4045 O O   . GLY B 1 81  ? 3.705   -4.025  37.465  1.00 67.63  ? 110 GLY B O   1 
ATOM   4046 N N   . GLY B 1 82  ? 2.641   -2.234  36.576  1.00 59.42  ? 111 GLY B N   1 
ATOM   4047 C CA  . GLY B 1 82  ? 3.816   -1.660  35.941  1.00 53.60  ? 111 GLY B CA  1 
ATOM   4048 C C   . GLY B 1 82  ? 3.983   -0.201  36.350  1.00 50.53  ? 111 GLY B C   1 
ATOM   4049 O O   . GLY B 1 82  ? 3.109   0.364   36.995  1.00 49.74  ? 111 GLY B O   1 
ATOM   4050 N N   . GLU B 1 83  ? 5.126   0.391   35.994  1.00 53.08  ? 112 GLU B N   1 
ATOM   4051 C CA  . GLU B 1 83  ? 5.327   1.820   36.178  1.00 56.74  ? 112 GLU B CA  1 
ATOM   4052 C C   . GLU B 1 83  ? 5.917   2.482   34.929  1.00 52.27  ? 112 GLU B C   1 
ATOM   4053 O O   . GLU B 1 83  ? 5.977   3.710   34.875  1.00 51.57  ? 112 GLU B O   1 
ATOM   4054 C CB  . GLU B 1 83  ? 6.132   2.116   37.446  1.00 60.52  ? 112 GLU B CB  1 
ATOM   4055 C CG  . GLU B 1 83  ? 7.335   1.205   37.668  1.00 64.72  ? 112 GLU B CG  1 
ATOM   4056 C CD  . GLU B 1 83  ? 8.124   1.538   38.923  1.00 67.20  ? 112 GLU B CD  1 
ATOM   4057 O OE1 . GLU B 1 83  ? 7.809   2.562   39.572  1.00 66.92  ? 112 GLU B OE1 1 
ATOM   4058 O OE2 . GLU B 1 83  ? 9.052   0.768   39.260  1.00 70.49  ? 112 GLU B OE2 1 
ATOM   4059 N N   . GLU B 1 84  ? 6.325   1.699   33.919  1.00 48.85  ? 113 GLU B N   1 
ATOM   4060 C CA  . GLU B 1 84  ? 6.863   2.280   32.698  1.00 46.61  ? 113 GLU B CA  1 
ATOM   4061 C C   . GLU B 1 84  ? 5.772   2.304   31.628  1.00 43.17  ? 113 GLU B C   1 
ATOM   4062 O O   . GLU B 1 84  ? 4.953   1.394   31.540  1.00 41.77  ? 113 GLU B O   1 
ATOM   4063 C CB  . GLU B 1 84  ? 8.123   1.563   32.207  1.00 48.59  ? 113 GLU B CB  1 
ATOM   4064 C CG  . GLU B 1 84  ? 9.283   1.603   33.198  1.00 51.66  ? 113 GLU B CG  1 
ATOM   4065 C CD  . GLU B 1 84  ? 9.833   2.973   33.559  1.00 55.71  ? 113 GLU B CD  1 
ATOM   4066 O OE1 . GLU B 1 84  ? 9.529   3.967   32.862  1.00 59.54  ? 113 GLU B OE1 1 
ATOM   4067 O OE2 . GLU B 1 84  ? 10.579  3.049   34.563  1.00 56.77  ? 113 GLU B OE2 1 
ATOM   4068 N N   . PRO B 1 85  ? 5.728   3.351   30.777  1.00 42.60  ? 114 PRO B N   1 
ATOM   4069 C CA  . PRO B 1 85  ? 4.659   3.493   29.788  1.00 41.18  ? 114 PRO B CA  1 
ATOM   4070 C C   . PRO B 1 85  ? 4.781   2.439   28.695  1.00 41.20  ? 114 PRO B C   1 
ATOM   4071 O O   . PRO B 1 85  ? 5.890   2.034   28.358  1.00 43.36  ? 114 PRO B O   1 
ATOM   4072 C CB  . PRO B 1 85  ? 4.858   4.920   29.261  1.00 42.79  ? 114 PRO B CB  1 
ATOM   4073 C CG  . PRO B 1 85  ? 6.338   5.175   29.443  1.00 45.78  ? 114 PRO B CG  1 
ATOM   4074 C CD  . PRO B 1 85  ? 6.706   4.451   30.727  1.00 44.17  ? 114 PRO B CD  1 
ATOM   4075 N N   . LEU B 1 86  ? 3.635   1.992   28.166  1.00 39.43  ? 115 LEU B N   1 
ATOM   4076 C CA  . LEU B 1 86  ? 3.615   0.980   27.121  1.00 39.29  ? 115 LEU B CA  1 
ATOM   4077 C C   . LEU B 1 86  ? 3.888   1.662   25.780  1.00 41.07  ? 115 LEU B C   1 
ATOM   4078 O O   . LEU B 1 86  ? 3.445   2.788   25.551  1.00 39.63  ? 115 LEU B O   1 
ATOM   4079 C CB  . LEU B 1 86  ? 2.283   0.229   27.102  1.00 39.20  ? 115 LEU B CB  1 
ATOM   4080 C CG  . LEU B 1 86  ? 1.965   -0.663  28.310  1.00 38.97  ? 115 LEU B CG  1 
ATOM   4081 C CD1 . LEU B 1 86  ? 0.631   -1.359  28.108  1.00 40.18  ? 115 LEU B CD1 1 
ATOM   4082 C CD2 . LEU B 1 86  ? 3.034   -1.696  28.569  1.00 38.59  ? 115 LEU B CD2 1 
ATOM   4083 N N   . PRO B 1 87  ? 4.666   1.031   24.868  1.00 42.81  ? 116 PRO B N   1 
ATOM   4084 C CA  . PRO B 1 87  ? 4.858   1.576   23.522  1.00 41.11  ? 116 PRO B CA  1 
ATOM   4085 C C   . PRO B 1 87  ? 3.547   1.731   22.754  1.00 37.34  ? 116 PRO B C   1 
ATOM   4086 O O   . PRO B 1 87  ? 3.403   2.651   21.957  1.00 37.27  ? 116 PRO B O   1 
ATOM   4087 C CB  . PRO B 1 87  ? 5.827   0.609   22.822  1.00 42.89  ? 116 PRO B CB  1 
ATOM   4088 C CG  . PRO B 1 87  ? 5.932   -0.602  23.735  1.00 44.84  ? 116 PRO B CG  1 
ATOM   4089 C CD  . PRO B 1 87  ? 5.445   -0.193  25.109  1.00 42.60  ? 116 PRO B CD  1 
ATOM   4090 N N   . GLU B 1 88  ? 2.596   0.827   23.002  1.00 36.97  ? 117 GLU B N   1 
ATOM   4091 C CA  . GLU B 1 88  ? 1.283   0.920   22.386  1.00 36.00  ? 117 GLU B CA  1 
ATOM   4092 C C   . GLU B 1 88  ? 0.724   2.327   22.585  1.00 35.06  ? 117 GLU B C   1 
ATOM   4093 O O   . GLU B 1 88  ? 0.245   2.941   21.635  1.00 32.63  ? 117 GLU B O   1 
ATOM   4094 C CB  . GLU B 1 88  ? 0.315   -0.113  22.960  1.00 35.35  ? 117 GLU B CB  1 
ATOM   4095 C CG  . GLU B 1 88  ? 0.643   -1.545  22.546  1.00 36.73  ? 117 GLU B CG  1 
ATOM   4096 C CD  . GLU B 1 88  ? 1.553   -2.285  23.502  1.00 35.14  ? 117 GLU B CD  1 
ATOM   4097 O OE1 . GLU B 1 88  ? 2.408   -1.620  24.123  1.00 34.58  ? 117 GLU B OE1 1 
ATOM   4098 O OE2 . GLU B 1 88  ? 1.404   -3.524  23.607  1.00 36.11  ? 117 GLU B OE2 1 
ATOM   4099 N N   . GLY B 1 89  ? 0.796   2.824   23.828  1.00 32.47  ? 118 GLY B N   1 
ATOM   4100 C CA  . GLY B 1 89  ? 0.252   4.127   24.162  1.00 33.91  ? 118 GLY B CA  1 
ATOM   4101 C C   . GLY B 1 89  ? 0.973   5.250   23.423  1.00 35.45  ? 118 GLY B C   1 
ATOM   4102 O O   . GLY B 1 89  ? 0.346   6.197   22.961  1.00 38.94  ? 118 GLY B O   1 
ATOM   4103 N N   . LEU B 1 90  ? 2.297   5.118   23.318  1.00 34.09  ? 119 LEU B N   1 
ATOM   4104 C CA  . LEU B 1 90  ? 3.125   6.098   22.643  1.00 35.25  ? 119 LEU B CA  1 
ATOM   4105 C C   . LEU B 1 90  ? 2.663   6.206   21.196  1.00 31.98  ? 119 LEU B C   1 
ATOM   4106 O O   . LEU B 1 90  ? 2.381   7.297   20.716  1.00 31.71  ? 119 LEU B O   1 
ATOM   4107 C CB  . LEU B 1 90  ? 4.584   5.657   22.798  1.00 37.74  ? 119 LEU B CB  1 
ATOM   4108 C CG  . LEU B 1 90  ? 5.660   6.447   22.048  1.00 38.93  ? 119 LEU B CG  1 
ATOM   4109 C CD1 . LEU B 1 90  ? 5.582   6.148   20.557  1.00 41.44  ? 119 LEU B CD1 1 
ATOM   4110 C CD2 . LEU B 1 90  ? 5.585   7.945   22.314  1.00 39.01  ? 119 LEU B CD2 1 
ATOM   4111 N N   . PHE B 1 91  ? 2.530   5.058   20.533  1.00 31.82  ? 120 PHE B N   1 
ATOM   4112 C CA  . PHE B 1 91  ? 2.122   5.012   19.141  1.00 30.96  ? 120 PHE B CA  1 
ATOM   4113 C C   . PHE B 1 91  ? 0.786   5.734   18.977  1.00 30.62  ? 120 PHE B C   1 
ATOM   4114 O O   . PHE B 1 91  ? 0.645   6.573   18.092  1.00 28.02  ? 120 PHE B O   1 
ATOM   4115 C CB  . PHE B 1 91  ? 2.074   3.559   18.655  1.00 30.85  ? 120 PHE B CB  1 
ATOM   4116 C CG  . PHE B 1 91  ? 1.689   3.427   17.189  1.00 31.22  ? 120 PHE B CG  1 
ATOM   4117 C CD1 . PHE B 1 91  ? 2.615   3.681   16.187  1.00 33.39  ? 120 PHE B CD1 1 
ATOM   4118 C CD2 . PHE B 1 91  ? 0.398   3.075   16.819  1.00 31.50  ? 120 PHE B CD2 1 
ATOM   4119 C CE1 . PHE B 1 91  ? 2.263   3.572   14.850  1.00 33.41  ? 120 PHE B CE1 1 
ATOM   4120 C CE2 . PHE B 1 91  ? 0.050   2.967   15.486  1.00 31.83  ? 120 PHE B CE2 1 
ATOM   4121 C CZ  . PHE B 1 91  ? 0.981   3.221   14.503  1.00 34.21  ? 120 PHE B CZ  1 
ATOM   4122 N N   . TRP B 1 92  ? -0.180  5.419   19.847  1.00 32.30  ? 121 TRP B N   1 
ATOM   4123 C CA  . TRP B 1 92  ? -1.479  6.084   19.838  1.00 32.85  ? 121 TRP B CA  1 
ATOM   4124 C C   . TRP B 1 92  ? -1.312  7.601   19.937  1.00 30.99  ? 121 TRP B C   1 
ATOM   4125 O O   . TRP B 1 92  ? -1.962  8.352   19.216  1.00 31.85  ? 121 TRP B O   1 
ATOM   4126 C CB  . TRP B 1 92  ? -2.355  5.562   20.982  1.00 34.48  ? 121 TRP B CB  1 
ATOM   4127 C CG  . TRP B 1 92  ? -3.805  5.943   20.855  1.00 35.94  ? 121 TRP B CG  1 
ATOM   4128 C CD1 . TRP B 1 92  ? -4.359  7.174   21.055  1.00 37.26  ? 121 TRP B CD1 1 
ATOM   4129 C CD2 . TRP B 1 92  ? -4.897  5.061   20.527  1.00 36.82  ? 121 TRP B CD2 1 
ATOM   4130 N NE1 . TRP B 1 92  ? -5.713  7.125   20.862  1.00 37.89  ? 121 TRP B NE1 1 
ATOM   4131 C CE2 . TRP B 1 92  ? -6.072  5.842   20.542  1.00 36.90  ? 121 TRP B CE2 1 
ATOM   4132 C CE3 . TRP B 1 92  ? -4.995  3.697   20.230  1.00 36.16  ? 121 TRP B CE3 1 
ATOM   4133 C CZ2 . TRP B 1 92  ? -7.322  5.300   20.264  1.00 35.73  ? 121 TRP B CZ2 1 
ATOM   4134 C CZ3 . TRP B 1 92  ? -6.232  3.164   19.955  1.00 35.72  ? 121 TRP B CZ3 1 
ATOM   4135 C CH2 . TRP B 1 92  ? -7.378  3.958   19.972  1.00 36.69  ? 121 TRP B CH2 1 
ATOM   4136 N N   . LEU B 1 93  ? -0.425  8.049   20.824  1.00 28.30  ? 122 LEU B N   1 
ATOM   4137 C CA  . LEU B 1 93  ? -0.191  9.471   20.995  1.00 30.54  ? 122 LEU B CA  1 
ATOM   4138 C C   . LEU B 1 93  ? 0.353   10.094  19.707  1.00 36.40  ? 122 LEU B C   1 
ATOM   4139 O O   . LEU B 1 93  ? 0.029   11.244  19.400  1.00 38.54  ? 122 LEU B O   1 
ATOM   4140 C CB  . LEU B 1 93  ? 0.764   9.682   22.164  1.00 29.73  ? 122 LEU B CB  1 
ATOM   4141 C CG  . LEU B 1 93  ? 1.320   11.097  22.327  1.00 30.85  ? 122 LEU B CG  1 
ATOM   4142 C CD1 . LEU B 1 93  ? 0.216   12.141  22.381  1.00 32.52  ? 122 LEU B CD1 1 
ATOM   4143 C CD2 . LEU B 1 93  ? 2.163   11.140  23.593  1.00 30.80  ? 122 LEU B CD2 1 
ATOM   4144 N N   . LEU B 1 94  ? 1.198   9.355   18.970  1.00 34.07  ? 123 LEU B N   1 
ATOM   4145 C CA  . LEU B 1 94  ? 1.844   9.904   17.789  1.00 35.13  ? 123 LEU B CA  1 
ATOM   4146 C C   . LEU B 1 94  ? 0.878   9.904   16.605  1.00 34.00  ? 123 LEU B C   1 
ATOM   4147 O O   . LEU B 1 94  ? 0.939   10.783  15.754  1.00 32.30  ? 123 LEU B O   1 
ATOM   4148 C CB  . LEU B 1 94  ? 3.125   9.127   17.482  1.00 36.40  ? 123 LEU B CB  1 
ATOM   4149 C CG  . LEU B 1 94  ? 4.247   9.255   18.519  1.00 36.84  ? 123 LEU B CG  1 
ATOM   4150 C CD1 . LEU B 1 94  ? 5.413   8.370   18.152  1.00 35.06  ? 123 LEU B CD1 1 
ATOM   4151 C CD2 . LEU B 1 94  ? 4.723   10.691  18.702  1.00 38.25  ? 123 LEU B CD2 1 
ATOM   4152 N N   . VAL B 1 95  ? -0.025  8.924   16.570  1.00 38.18  ? 124 VAL B N   1 
ATOM   4153 C CA  . VAL B 1 95  ? -0.976  8.772   15.481  1.00 39.77  ? 124 VAL B CA  1 
ATOM   4154 C C   . VAL B 1 95  ? -2.132  9.757   15.652  1.00 43.19  ? 124 VAL B C   1 
ATOM   4155 O O   . VAL B 1 95  ? -2.474  10.472  14.715  1.00 43.44  ? 124 VAL B O   1 
ATOM   4156 C CB  . VAL B 1 95  ? -1.440  7.306   15.419  1.00 39.91  ? 124 VAL B CB  1 
ATOM   4157 C CG1 . VAL B 1 95  ? -2.678  7.110   14.553  1.00 42.99  ? 124 VAL B CG1 1 
ATOM   4158 C CG2 . VAL B 1 95  ? -0.315  6.411   14.921  1.00 40.40  ? 124 VAL B CG2 1 
ATOM   4159 N N   . THR B 1 96  ? -2.703  9.816   16.860  1.00 43.49  ? 125 THR B N   1 
ATOM   4160 C CA  . THR B 1 96  ? -3.894  10.613  17.120  1.00 41.50  ? 125 THR B CA  1 
ATOM   4161 C C   . THR B 1 96  ? -3.509  12.023  17.563  1.00 43.67  ? 125 THR B C   1 
ATOM   4162 O O   . THR B 1 96  ? -4.213  12.980  17.249  1.00 50.76  ? 125 THR B O   1 
ATOM   4163 C CB  . THR B 1 96  ? -4.761  9.921   18.174  1.00 38.89  ? 125 THR B CB  1 
ATOM   4164 O OG1 . THR B 1 96  ? -4.073  9.986   19.418  1.00 34.57  ? 125 THR B OG1 1 
ATOM   4165 C CG2 . THR B 1 96  ? -5.043  8.475   17.814  1.00 40.40  ? 125 THR B CG2 1 
ATOM   4166 N N   . GLY B 1 97  ? -2.401  12.145  18.301  1.00 42.41  ? 126 GLY B N   1 
ATOM   4167 C CA  . GLY B 1 97  ? -2.029  13.408  18.916  1.00 41.31  ? 126 GLY B CA  1 
ATOM   4168 C C   . GLY B 1 97  ? -2.640  13.557  20.305  1.00 42.51  ? 126 GLY B C   1 
ATOM   4169 O O   . GLY B 1 97  ? -2.562  14.631  20.897  1.00 42.47  ? 126 GLY B O   1 
ATOM   4170 N N   . HIS B 1 98  ? -3.223  12.467  20.821  1.00 46.96  ? 127 HIS B N   1 
ATOM   4171 C CA  . HIS B 1 98  ? -3.928  12.482  22.093  1.00 52.30  ? 127 HIS B CA  1 
ATOM   4172 C C   . HIS B 1 98  ? -3.534  11.259  22.918  1.00 48.53  ? 127 HIS B C   1 
ATOM   4173 O O   . HIS B 1 98  ? -3.380  10.170  22.366  1.00 44.65  ? 127 HIS B O   1 
ATOM   4174 C CB  . HIS B 1 98  ? -5.447  12.475  21.875  1.00 59.81  ? 127 HIS B CB  1 
ATOM   4175 C CG  . HIS B 1 98  ? -5.968  13.604  21.049  1.00 65.32  ? 127 HIS B CG  1 
ATOM   4176 N ND1 . HIS B 1 98  ? -6.191  14.868  21.552  1.00 69.56  ? 127 HIS B ND1 1 
ATOM   4177 C CD2 . HIS B 1 98  ? -6.313  13.652  19.755  1.00 68.30  ? 127 HIS B CD2 1 
ATOM   4178 C CE1 . HIS B 1 98  ? -6.657  15.646  20.585  1.00 72.92  ? 127 HIS B CE1 1 
ATOM   4179 N NE2 . HIS B 1 98  ? -6.738  14.927  19.485  1.00 72.33  ? 127 HIS B NE2 1 
ATOM   4180 N N   . ILE B 1 99  ? -3.419  11.459  24.241  1.00 46.49  ? 128 ILE B N   1 
ATOM   4181 C CA  . ILE B 1 99  ? -3.106  10.404  25.195  1.00 45.00  ? 128 ILE B CA  1 
ATOM   4182 C C   . ILE B 1 99  ? -4.229  9.372   25.178  1.00 43.71  ? 128 ILE B C   1 
ATOM   4183 O O   . ILE B 1 99  ? -5.384  9.743   25.352  1.00 49.40  ? 128 ILE B O   1 
ATOM   4184 C CB  . ILE B 1 99  ? -2.909  11.005  26.601  1.00 45.52  ? 128 ILE B CB  1 
ATOM   4185 C CG1 . ILE B 1 99  ? -1.672  11.900  26.661  1.00 47.43  ? 128 ILE B CG1 1 
ATOM   4186 C CG2 . ILE B 1 99  ? -2.861  9.924   27.684  1.00 45.12  ? 128 ILE B CG2 1 
ATOM   4187 C CD1 . ILE B 1 99  ? -0.359  11.177  26.426  1.00 46.72  ? 128 ILE B CD1 1 
ATOM   4188 N N   . PRO B 1 100 ? -3.942  8.059   24.986  1.00 42.30  ? 129 PRO B N   1 
ATOM   4189 C CA  . PRO B 1 100 ? -4.986  7.032   24.971  1.00 43.89  ? 129 PRO B CA  1 
ATOM   4190 C C   . PRO B 1 100 ? -5.434  6.594   26.363  1.00 47.13  ? 129 PRO B C   1 
ATOM   4191 O O   . PRO B 1 100 ? -4.701  6.761   27.337  1.00 47.15  ? 129 PRO B O   1 
ATOM   4192 C CB  . PRO B 1 100 ? -4.300  5.877   24.234  1.00 41.34  ? 129 PRO B CB  1 
ATOM   4193 C CG  . PRO B 1 100 ? -2.866  5.980   24.685  1.00 41.07  ? 129 PRO B CG  1 
ATOM   4194 C CD  . PRO B 1 100 ? -2.603  7.480   24.787  1.00 41.46  ? 129 PRO B CD  1 
ATOM   4195 N N   . THR B 1 101 ? -6.632  5.998   26.419  1.00 47.15  ? 130 THR B N   1 
ATOM   4196 C CA  . THR B 1 101 ? -7.155  5.397   27.633  1.00 47.43  ? 130 THR B CA  1 
ATOM   4197 C C   . THR B 1 101 ? -6.512  4.021   27.784  1.00 49.69  ? 130 THR B C   1 
ATOM   4198 O O   . THR B 1 101 ? -5.966  3.484   26.821  1.00 48.87  ? 130 THR B O   1 
ATOM   4199 C CB  . THR B 1 101 ? -8.682  5.301   27.557  1.00 48.93  ? 130 THR B CB  1 
ATOM   4200 O OG1 . THR B 1 101 ? -9.019  4.394   26.512  1.00 48.20  ? 130 THR B OG1 1 
ATOM   4201 C CG2 . THR B 1 101 ? -9.354  6.622   27.229  1.00 48.34  ? 130 THR B CG2 1 
ATOM   4202 N N   . GLU B 1 102 ? -6.594  3.467   28.999  1.00 52.65  ? 131 GLU B N   1 
ATOM   4203 C CA  . GLU B 1 102 ? -6.248  2.080   29.270  1.00 53.74  ? 131 GLU B CA  1 
ATOM   4204 C C   . GLU B 1 102 ? -6.811  1.169   28.180  1.00 53.48  ? 131 GLU B C   1 
ATOM   4205 O O   . GLU B 1 102 ? -6.129  0.266   27.696  1.00 54.44  ? 131 GLU B O   1 
ATOM   4206 C CB  . GLU B 1 102 ? -6.876  1.637   30.593  1.00 57.85  ? 131 GLU B CB  1 
ATOM   4207 C CG  . GLU B 1 102 ? -6.153  2.119   31.848  1.00 62.90  ? 131 GLU B CG  1 
ATOM   4208 C CD  . GLU B 1 102 ? -5.300  1.068   32.540  1.00 63.59  ? 131 GLU B CD  1 
ATOM   4209 O OE1 . GLU B 1 102 ? -4.856  0.127   31.855  1.00 64.17  ? 131 GLU B OE1 1 
ATOM   4210 O OE2 . GLU B 1 102 ? -5.119  1.163   33.774  1.00 62.75  ? 131 GLU B OE2 1 
ATOM   4211 N N   . GLU B 1 103 ? -8.074  1.410   27.816  1.00 51.12  ? 132 GLU B N   1 
ATOM   4212 C CA  . GLU B 1 103 ? -8.851  0.459   27.041  1.00 50.48  ? 132 GLU B CA  1 
ATOM   4213 C C   . GLU B 1 103 ? -8.478  0.564   25.561  1.00 47.25  ? 132 GLU B C   1 
ATOM   4214 O O   . GLU B 1 103 ? -8.533  -0.427  24.833  1.00 50.28  ? 132 GLU B O   1 
ATOM   4215 C CB  . GLU B 1 103 ? -10.333 0.689   27.357  1.00 54.32  ? 132 GLU B CB  1 
ATOM   4216 C CG  . GLU B 1 103 ? -10.718 0.357   28.803  1.00 56.83  ? 132 GLU B CG  1 
ATOM   4217 C CD  . GLU B 1 103 ? -10.572 1.426   29.885  1.00 58.94  ? 132 GLU B CD  1 
ATOM   4218 O OE1 . GLU B 1 103 ? -10.466 2.635   29.574  1.00 56.24  ? 132 GLU B OE1 1 
ATOM   4219 O OE2 . GLU B 1 103 ? -10.559 1.035   31.077  1.00 60.78  ? 132 GLU B OE2 1 
ATOM   4220 N N   . GLN B 1 104 ? -8.093  1.767   25.123  1.00 45.28  ? 133 GLN B N   1 
ATOM   4221 C CA  . GLN B 1 104 ? -7.592  1.978   23.770  1.00 47.70  ? 133 GLN B CA  1 
ATOM   4222 C C   . GLN B 1 104 ? -6.268  1.235   23.576  1.00 47.34  ? 133 GLN B C   1 
ATOM   4223 O O   . GLN B 1 104 ? -6.089  0.551   22.565  1.00 46.38  ? 133 GLN B O   1 
ATOM   4224 C CB  . GLN B 1 104 ? -7.450  3.476   23.492  1.00 47.33  ? 133 GLN B CB  1 
ATOM   4225 C CG  . GLN B 1 104 ? -8.773  4.160   23.158  1.00 47.28  ? 133 GLN B CG  1 
ATOM   4226 C CD  . GLN B 1 104 ? -8.734  5.664   23.320  1.00 47.89  ? 133 GLN B CD  1 
ATOM   4227 O OE1 . GLN B 1 104 ? -7.946  6.211   24.097  1.00 49.43  ? 133 GLN B OE1 1 
ATOM   4228 N NE2 . GLN B 1 104 ? -9.607  6.352   22.601  1.00 49.40  ? 133 GLN B NE2 1 
ATOM   4229 N N   . VAL B 1 105 ? -5.360  1.367   24.557  1.00 42.97  ? 134 VAL B N   1 
ATOM   4230 C CA  . VAL B 1 105 ? -4.086  0.669   24.536  1.00 44.70  ? 134 VAL B CA  1 
ATOM   4231 C C   . VAL B 1 105 ? -4.326  -0.838  24.527  1.00 46.15  ? 134 VAL B C   1 
ATOM   4232 O O   . VAL B 1 105 ? -3.715  -1.559  23.742  1.00 45.23  ? 134 VAL B O   1 
ATOM   4233 C CB  . VAL B 1 105 ? -3.189  1.079   25.715  1.00 47.33  ? 134 VAL B CB  1 
ATOM   4234 C CG1 . VAL B 1 105 ? -2.057  0.084   25.937  1.00 46.15  ? 134 VAL B CG1 1 
ATOM   4235 C CG2 . VAL B 1 105 ? -2.651  2.495   25.544  1.00 48.38  ? 134 VAL B CG2 1 
ATOM   4236 N N   . SER B 1 106 ? -5.216  -1.306  25.407  1.00 46.64  ? 135 SER B N   1 
ATOM   4237 C CA  A SER B 1 106 ? -5.555  -2.717  25.486  0.50 47.59  ? 135 SER B CA  1 
ATOM   4238 C CA  B SER B 1 106 ? -5.535  -2.723  25.482  0.50 47.22  ? 135 SER B CA  1 
ATOM   4239 C C   . SER B 1 106 ? -5.918  -3.245  24.100  1.00 46.67  ? 135 SER B C   1 
ATOM   4240 O O   . SER B 1 106 ? -5.363  -4.239  23.641  1.00 48.66  ? 135 SER B O   1 
ATOM   4241 C CB  A SER B 1 106 ? -6.677  -2.947  26.472  0.50 48.93  ? 135 SER B CB  1 
ATOM   4242 C CB  B SER B 1 106 ? -6.612  -3.009  26.507  0.50 48.16  ? 135 SER B CB  1 
ATOM   4243 O OG  A SER B 1 106 ? -6.880  -4.334  26.700  0.50 49.53  ? 135 SER B OG  1 
ATOM   4244 O OG  B SER B 1 106 ? -6.045  -3.200  27.797  0.50 47.59  ? 135 SER B OG  1 
ATOM   4245 N N   . TRP B 1 107 ? -6.855  -2.559  23.436  1.00 46.58  ? 136 TRP B N   1 
ATOM   4246 C CA  . TRP B 1 107 ? -7.314  -2.968  22.117  1.00 44.16  ? 136 TRP B CA  1 
ATOM   4247 C C   . TRP B 1 107 ? -6.152  -2.999  21.120  1.00 44.71  ? 136 TRP B C   1 
ATOM   4248 O O   . TRP B 1 107 ? -6.116  -3.848  20.226  1.00 40.93  ? 136 TRP B O   1 
ATOM   4249 C CB  . TRP B 1 107 ? -8.431  -2.034  21.636  1.00 43.30  ? 136 TRP B CB  1 
ATOM   4250 C CG  . TRP B 1 107 ? -8.800  -2.235  20.191  1.00 43.18  ? 136 TRP B CG  1 
ATOM   4251 C CD1 . TRP B 1 107 ? -9.807  -3.004  19.690  1.00 42.13  ? 136 TRP B CD1 1 
ATOM   4252 C CD2 . TRP B 1 107 ? -8.127  -1.658  19.052  1.00 42.63  ? 136 TRP B CD2 1 
ATOM   4253 N NE1 . TRP B 1 107 ? -9.814  -2.939  18.320  1.00 44.33  ? 136 TRP B NE1 1 
ATOM   4254 C CE2 . TRP B 1 107 ? -8.796  -2.124  17.901  1.00 43.72  ? 136 TRP B CE2 1 
ATOM   4255 C CE3 . TRP B 1 107 ? -7.034  -0.796  18.898  1.00 44.01  ? 136 TRP B CE3 1 
ATOM   4256 C CZ2 . TRP B 1 107 ? -8.405  -1.754  16.617  1.00 43.66  ? 136 TRP B CZ2 1 
ATOM   4257 C CZ3 . TRP B 1 107 ? -6.647  -0.430  17.627  1.00 43.08  ? 136 TRP B CZ3 1 
ATOM   4258 C CH2 . TRP B 1 107 ? -7.324  -0.908  16.503  1.00 42.85  ? 136 TRP B CH2 1 
ATOM   4259 N N   . LEU B 1 108 ? -5.216  -2.053  21.268  1.00 44.55  ? 137 LEU B N   1 
ATOM   4260 C CA  . LEU B 1 108 ? -4.053  -1.978  20.395  1.00 44.03  ? 137 LEU B CA  1 
ATOM   4261 C C   . LEU B 1 108 ? -3.165  -3.195  20.635  1.00 40.94  ? 137 LEU B C   1 
ATOM   4262 O O   . LEU B 1 108 ? -2.682  -3.803  19.687  1.00 40.42  ? 137 LEU B O   1 
ATOM   4263 C CB  . LEU B 1 108 ? -3.311  -0.660  20.622  1.00 44.48  ? 137 LEU B CB  1 
ATOM   4264 C CG  . LEU B 1 108 ? -2.287  -0.244  19.559  1.00 44.84  ? 137 LEU B CG  1 
ATOM   4265 C CD1 . LEU B 1 108 ? -2.846  -0.244  18.147  1.00 44.75  ? 137 LEU B CD1 1 
ATOM   4266 C CD2 . LEU B 1 108 ? -1.742  1.139   19.892  1.00 45.67  ? 137 LEU B CD2 1 
ATOM   4267 N N   . SER B 1 109 ? -2.986  -3.568  21.908  1.00 43.47  ? 138 SER B N   1 
ATOM   4268 C CA  . SER B 1 109 ? -2.232  -4.762  22.254  1.00 43.94  ? 138 SER B CA  1 
ATOM   4269 C C   . SER B 1 109 ? -2.886  -5.990  21.625  1.00 48.07  ? 138 SER B C   1 
ATOM   4270 O O   . SER B 1 109 ? -2.188  -6.883  21.148  1.00 54.22  ? 138 SER B O   1 
ATOM   4271 C CB  . SER B 1 109 ? -2.090  -4.913  23.744  1.00 41.37  ? 138 SER B CB  1 
ATOM   4272 O OG  . SER B 1 109 ? -1.384  -3.810  24.295  1.00 40.61  ? 138 SER B OG  1 
ATOM   4273 N N   . LYS B 1 110 ? -4.225  -6.007  21.601  1.00 48.50  ? 139 LYS B N   1 
ATOM   4274 C CA  . LYS B 1 110 ? -4.982  -7.090  20.989  1.00 50.21  ? 139 LYS B CA  1 
ATOM   4275 C C   . LYS B 1 110 ? -4.807  -7.099  19.472  1.00 46.61  ? 139 LYS B C   1 
ATOM   4276 O O   . LYS B 1 110 ? -4.711  -8.171  18.884  1.00 52.59  ? 139 LYS B O   1 
ATOM   4277 C CB  . LYS B 1 110 ? -6.470  -7.019  21.361  1.00 54.94  ? 139 LYS B CB  1 
ATOM   4278 C CG  . LYS B 1 110 ? -6.776  -7.552  22.753  1.00 63.17  ? 139 LYS B CG  1 
ATOM   4279 C CD  . LYS B 1 110 ? -8.185  -7.278  23.270  1.00 69.99  ? 139 LYS B CD  1 
ATOM   4280 C CE  . LYS B 1 110 ? -8.342  -7.736  24.695  1.00 75.95  ? 139 LYS B CE  1 
ATOM   4281 N NZ  . LYS B 1 110 ? -9.600  -7.305  25.312  1.00 77.80  ? 139 LYS B NZ  1 
ATOM   4282 N N   . GLU B 1 111 ? -4.789  -5.921  18.833  1.00 46.62  ? 140 GLU B N   1 
ATOM   4283 C CA  . GLU B 1 111 ? -4.683  -5.849  17.380  1.00 47.74  ? 140 GLU B CA  1 
ATOM   4284 C C   . GLU B 1 111 ? -3.326  -6.351  16.899  1.00 43.99  ? 140 GLU B C   1 
ATOM   4285 O O   . GLU B 1 111 ? -3.255  -6.978  15.847  1.00 46.33  ? 140 GLU B O   1 
ATOM   4286 C CB  . GLU B 1 111 ? -4.842  -4.443  16.804  1.00 49.15  ? 140 GLU B CB  1 
ATOM   4287 C CG  . GLU B 1 111 ? -6.280  -4.078  16.460  1.00 53.27  ? 140 GLU B CG  1 
ATOM   4288 C CD  . GLU B 1 111 ? -7.007  -5.025  15.517  1.00 57.16  ? 140 GLU B CD  1 
ATOM   4289 O OE1 . GLU B 1 111 ? -6.522  -5.236  14.380  1.00 54.61  ? 140 GLU B OE1 1 
ATOM   4290 O OE2 . GLU B 1 111 ? -8.072  -5.543  15.932  1.00 58.78  ? 140 GLU B OE2 1 
ATOM   4291 N N   . TRP B 1 112 ? -2.267  -6.059  17.665  1.00 43.73  ? 141 TRP B N   1 
ATOM   4292 C CA  . TRP B 1 112 ? -0.906  -6.375  17.251  1.00 46.44  ? 141 TRP B CA  1 
ATOM   4293 C C   . TRP B 1 112 ? -0.571  -7.849  17.489  1.00 51.33  ? 141 TRP B C   1 
ATOM   4294 O O   . TRP B 1 112 ? 0.373   -8.359  16.892  1.00 55.40  ? 141 TRP B O   1 
ATOM   4295 C CB  . TRP B 1 112 ? 0.115   -5.451  17.937  1.00 43.29  ? 141 TRP B CB  1 
ATOM   4296 C CG  . TRP B 1 112 ? 0.162   -4.041  17.396  1.00 37.34  ? 141 TRP B CG  1 
ATOM   4297 C CD1 . TRP B 1 112 ? -0.427  -3.558  16.264  1.00 37.06  ? 141 TRP B CD1 1 
ATOM   4298 C CD2 . TRP B 1 112 ? 0.879   -2.927  17.968  1.00 34.19  ? 141 TRP B CD2 1 
ATOM   4299 N NE1 . TRP B 1 112 ? -0.150  -2.226  16.103  1.00 37.20  ? 141 TRP B NE1 1 
ATOM   4300 C CE2 . TRP B 1 112 ? 0.655   -1.813  17.128  1.00 35.00  ? 141 TRP B CE2 1 
ATOM   4301 C CE3 . TRP B 1 112 ? 1.681   -2.765  19.101  1.00 35.59  ? 141 TRP B CE3 1 
ATOM   4302 C CZ2 . TRP B 1 112 ? 1.196   -0.559  17.391  1.00 34.49  ? 141 TRP B CZ2 1 
ATOM   4303 C CZ3 . TRP B 1 112 ? 2.233   -1.529  19.352  1.00 36.84  ? 141 TRP B CZ3 1 
ATOM   4304 C CH2 . TRP B 1 112 ? 1.990   -0.442  18.507  1.00 35.74  ? 141 TRP B CH2 1 
ATOM   4305 N N   . ALA B 1 113 ? -1.344  -8.541  18.337  1.00 52.40  ? 142 ALA B N   1 
ATOM   4306 C CA  . ALA B 1 113 ? -1.148  -9.969  18.539  1.00 52.87  ? 142 ALA B CA  1 
ATOM   4307 C C   . ALA B 1 113 ? -1.803  -10.765 17.409  1.00 54.11  ? 142 ALA B C   1 
ATOM   4308 O O   . ALA B 1 113 ? -1.302  -11.826 17.033  1.00 54.20  ? 142 ALA B O   1 
ATOM   4309 C CB  . ALA B 1 113 ? -1.680  -10.375 19.897  1.00 55.45  ? 142 ALA B CB  1 
ATOM   4310 N N   . LYS B 1 114 ? -2.914  -10.240 16.866  1.00 55.90  ? 143 LYS B N   1 
ATOM   4311 C CA  . LYS B 1 114 ? -3.656  -10.896 15.794  1.00 57.28  ? 143 LYS B CA  1 
ATOM   4312 C C   . LYS B 1 114 ? -2.853  -10.911 14.495  1.00 51.42  ? 143 LYS B C   1 
ATOM   4313 O O   . LYS B 1 114 ? -2.887  -11.891 13.756  1.00 46.22  ? 143 LYS B O   1 
ATOM   4314 C CB  . LYS B 1 114 ? -4.977  -10.185 15.472  1.00 61.17  ? 143 LYS B CB  1 
ATOM   4315 C CG  . LYS B 1 114 ? -6.100  -10.360 16.479  1.00 64.37  ? 143 LYS B CG  1 
ATOM   4316 C CD  . LYS B 1 114 ? -7.349  -9.546  16.157  1.00 67.10  ? 143 LYS B CD  1 
ATOM   4317 C CE  . LYS B 1 114 ? -8.248  -9.400  17.350  1.00 71.05  ? 143 LYS B CE  1 
ATOM   4318 N NZ  . LYS B 1 114 ? -9.331  -8.432  17.145  1.00 72.38  ? 143 LYS B NZ  1 
ATOM   4319 N N   . ARG B 1 115 ? -2.156  -9.800  14.225  1.00 51.84  ? 144 ARG B N   1 
ATOM   4320 C CA  . ARG B 1 115 ? -1.501  -9.560  12.948  1.00 50.88  ? 144 ARG B CA  1 
ATOM   4321 C C   . ARG B 1 115 ? -0.038  -10.007 12.988  1.00 53.35  ? 144 ARG B C   1 
ATOM   4322 O O   . ARG B 1 115 ? 0.742   -9.634  12.118  1.00 55.74  ? 144 ARG B O   1 
ATOM   4323 C CB  . ARG B 1 115 ? -1.545  -8.053  12.668  1.00 47.23  ? 144 ARG B CB  1 
ATOM   4324 C CG  . ARG B 1 115 ? -2.917  -7.403  12.743  1.00 46.36  ? 144 ARG B CG  1 
ATOM   4325 C CD  . ARG B 1 115 ? -2.790  -5.895  12.686  1.00 45.12  ? 144 ARG B CD  1 
ATOM   4326 N NE  . ARG B 1 115 ? -4.069  -5.214  12.455  1.00 45.61  ? 144 ARG B NE  1 
ATOM   4327 C CZ  . ARG B 1 115 ? -4.518  -4.771  11.275  1.00 45.81  ? 144 ARG B CZ  1 
ATOM   4328 N NH1 . ARG B 1 115 ? -3.952  -5.157  10.142  1.00 44.58  ? 144 ARG B NH1 1 
ATOM   4329 N NH2 . ARG B 1 115 ? -5.573  -3.973  11.227  1.00 45.84  ? 144 ARG B NH2 1 
ATOM   4330 N N   . ALA B 1 116 ? 0.327   -10.815 13.990  1.00 57.09  ? 145 ALA B N   1 
ATOM   4331 C CA  . ALA B 1 116 ? 1.722   -11.077 14.308  1.00 58.45  ? 145 ALA B CA  1 
ATOM   4332 C C   . ALA B 1 116 ? 2.266   -12.249 13.492  1.00 59.08  ? 145 ALA B C   1 
ATOM   4333 O O   . ALA B 1 116 ? 3.404   -12.665 13.705  1.00 59.91  ? 145 ALA B O   1 
ATOM   4334 C CB  . ALA B 1 116 ? 1.851   -11.343 15.792  1.00 58.67  ? 145 ALA B CB  1 
ATOM   4335 N N   . ALA B 1 117 ? 1.459   -12.771 12.560  1.00 57.50  ? 146 ALA B N   1 
ATOM   4336 C CA  . ALA B 1 117 ? 1.823   -13.965 11.816  1.00 58.51  ? 146 ALA B CA  1 
ATOM   4337 C C   . ALA B 1 117 ? 2.822   -13.608 10.721  1.00 58.65  ? 146 ALA B C   1 
ATOM   4338 O O   . ALA B 1 117 ? 2.723   -12.539 10.123  1.00 62.26  ? 146 ALA B O   1 
ATOM   4339 C CB  . ALA B 1 117 ? 0.583   -14.614 11.240  1.00 60.71  ? 146 ALA B CB  1 
ATOM   4340 N N   . LEU B 1 118 ? 3.770   -14.525 10.472  1.00 56.07  ? 147 LEU B N   1 
ATOM   4341 C CA  . LEU B 1 118 ? 4.786   -14.356 9.447   1.00 52.90  ? 147 LEU B CA  1 
ATOM   4342 C C   . LEU B 1 118 ? 4.449   -15.262 8.270   1.00 54.58  ? 147 LEU B C   1 
ATOM   4343 O O   . LEU B 1 118 ? 4.074   -16.414 8.470   1.00 59.30  ? 147 LEU B O   1 
ATOM   4344 C CB  . LEU B 1 118 ? 6.179   -14.706 9.966   1.00 49.56  ? 147 LEU B CB  1 
ATOM   4345 C CG  . LEU B 1 118 ? 6.710   -13.886 11.143  1.00 48.00  ? 147 LEU B CG  1 
ATOM   4346 C CD1 . LEU B 1 118 ? 8.150   -14.288 11.373  1.00 47.77  ? 147 LEU B CD1 1 
ATOM   4347 C CD2 . LEU B 1 118 ? 6.604   -12.386 10.929  1.00 47.84  ? 147 LEU B CD2 1 
ATOM   4348 N N   . PRO B 1 119 ? 4.599   -14.786 7.013   1.00 52.76  ? 148 PRO B N   1 
ATOM   4349 C CA  . PRO B 1 119 ? 4.606   -15.683 5.859   1.00 53.46  ? 148 PRO B CA  1 
ATOM   4350 C C   . PRO B 1 119 ? 5.784   -16.649 5.945   1.00 51.48  ? 148 PRO B C   1 
ATOM   4351 O O   . PRO B 1 119 ? 6.791   -16.357 6.588   1.00 52.75  ? 148 PRO B O   1 
ATOM   4352 C CB  . PRO B 1 119 ? 4.688   -14.752 4.643   1.00 53.91  ? 148 PRO B CB  1 
ATOM   4353 C CG  . PRO B 1 119 ? 5.235   -13.457 5.205   1.00 53.44  ? 148 PRO B CG  1 
ATOM   4354 C CD  . PRO B 1 119 ? 4.736   -13.371 6.635   1.00 52.22  ? 148 PRO B CD  1 
ATOM   4355 N N   . SER B 1 120 ? 5.632   -17.803 5.291   1.00 48.59  ? 149 SER B N   1 
ATOM   4356 C CA  . SER B 1 120 ? 6.566   -18.906 5.437   1.00 50.05  ? 149 SER B CA  1 
ATOM   4357 C C   . SER B 1 120 ? 7.901   -18.604 4.755   1.00 46.90  ? 149 SER B C   1 
ATOM   4358 O O   . SER B 1 120 ? 8.949   -19.003 5.263   1.00 44.16  ? 149 SER B O   1 
ATOM   4359 C CB  . SER B 1 120 ? 5.953   -20.180 4.920   1.00 50.51  ? 149 SER B CB  1 
ATOM   4360 O OG  . SER B 1 120 ? 5.172   -19.912 3.767   1.00 52.57  ? 149 SER B OG  1 
ATOM   4361 N N   . HIS B 1 121 ? 7.859   -17.907 3.610   1.00 45.97  ? 150 HIS B N   1 
ATOM   4362 C CA  . HIS B 1 121 ? 9.071   -17.597 2.862   1.00 45.05  ? 150 HIS B CA  1 
ATOM   4363 C C   . HIS B 1 121 ? 10.016  -16.769 3.740   1.00 40.26  ? 150 HIS B C   1 
ATOM   4364 O O   . HIS B 1 121 ? 11.228  -16.948 3.689   1.00 37.63  ? 150 HIS B O   1 
ATOM   4365 C CB  . HIS B 1 121 ? 8.731   -16.973 1.497   1.00 46.58  ? 150 HIS B CB  1 
ATOM   4366 C CG  . HIS B 1 121 ? 8.472   -15.499 1.498   1.00 47.33  ? 150 HIS B CG  1 
ATOM   4367 N ND1 . HIS B 1 121 ? 7.266   -14.947 1.872   1.00 47.61  ? 150 HIS B ND1 1 
ATOM   4368 C CD2 . HIS B 1 121 ? 9.267   -14.463 1.169   1.00 46.01  ? 150 HIS B CD2 1 
ATOM   4369 C CE1 . HIS B 1 121 ? 7.342   -13.627 1.780   1.00 46.01  ? 150 HIS B CE1 1 
ATOM   4370 N NE2 . HIS B 1 121 ? 8.548   -13.309 1.357   1.00 44.55  ? 150 HIS B NE2 1 
ATOM   4371 N N   . VAL B 1 122 ? 9.443   -15.898 4.573   1.00 38.93  ? 151 VAL B N   1 
ATOM   4372 C CA  . VAL B 1 122 ? 10.205  -15.042 5.468   1.00 42.48  ? 151 VAL B CA  1 
ATOM   4373 C C   . VAL B 1 122 ? 10.821  -15.863 6.598   1.00 43.69  ? 151 VAL B C   1 
ATOM   4374 O O   . VAL B 1 122 ? 11.960  -15.613 6.992   1.00 44.44  ? 151 VAL B O   1 
ATOM   4375 C CB  . VAL B 1 122 ? 9.293   -13.918 6.001   1.00 42.11  ? 151 VAL B CB  1 
ATOM   4376 C CG1 . VAL B 1 122 ? 9.888   -13.204 7.203   1.00 44.24  ? 151 VAL B CG1 1 
ATOM   4377 C CG2 . VAL B 1 122 ? 8.965   -12.916 4.904   1.00 43.86  ? 151 VAL B CG2 1 
ATOM   4378 N N   . VAL B 1 123 ? 10.060  -16.824 7.132   1.00 45.65  ? 152 VAL B N   1 
ATOM   4379 C CA  . VAL B 1 123 ? 10.566  -17.709 8.174   1.00 46.12  ? 152 VAL B CA  1 
ATOM   4380 C C   . VAL B 1 123 ? 11.745  -18.520 7.634   1.00 43.99  ? 152 VAL B C   1 
ATOM   4381 O O   . VAL B 1 123 ? 12.753  -18.672 8.319   1.00 41.63  ? 152 VAL B O   1 
ATOM   4382 C CB  . VAL B 1 123 ? 9.478   -18.641 8.743   1.00 45.42  ? 152 VAL B CB  1 
ATOM   4383 C CG1 . VAL B 1 123 ? 10.052  -19.623 9.760   1.00 44.42  ? 152 VAL B CG1 1 
ATOM   4384 C CG2 . VAL B 1 123 ? 8.321   -17.860 9.355   1.00 46.15  ? 152 VAL B CG2 1 
ATOM   4385 N N   . THR B 1 124 ? 11.614  -19.055 6.415   1.00 43.07  ? 153 THR B N   1 
ATOM   4386 C CA  . THR B 1 124 ? 12.667  -19.870 5.823   1.00 46.88  ? 153 THR B CA  1 
ATOM   4387 C C   . THR B 1 124 ? 13.923  -19.026 5.597   1.00 49.26  ? 153 THR B C   1 
ATOM   4388 O O   . THR B 1 124 ? 15.041  -19.466 5.872   1.00 48.62  ? 153 THR B O   1 
ATOM   4389 C CB  . THR B 1 124 ? 12.163  -20.474 4.513   1.00 47.59  ? 153 THR B CB  1 
ATOM   4390 O OG1 . THR B 1 124 ? 11.026  -21.260 4.855   1.00 47.70  ? 153 THR B OG1 1 
ATOM   4391 C CG2 . THR B 1 124 ? 13.202  -21.344 3.832   1.00 49.02  ? 153 THR B CG2 1 
ATOM   4392 N N   . MET B 1 125 ? 13.720  -17.809 5.081   1.00 49.45  ? 154 MET B N   1 
ATOM   4393 C CA  . MET B 1 125 ? 14.807  -16.914 4.717   1.00 52.13  ? 154 MET B CA  1 
ATOM   4394 C C   . MET B 1 125 ? 15.669  -16.602 5.940   1.00 51.06  ? 154 MET B C   1 
ATOM   4395 O O   . MET B 1 125 ? 16.898  -16.618 5.848   1.00 50.31  ? 154 MET B O   1 
ATOM   4396 C CB  . MET B 1 125 ? 14.232  -15.625 4.120   1.00 55.04  ? 154 MET B CB  1 
ATOM   4397 C CG  . MET B 1 125 ? 15.257  -14.635 3.610   1.00 58.83  ? 154 MET B CG  1 
ATOM   4398 S SD  . MET B 1 125 ? 14.393  -13.189 2.969   1.00 61.79  ? 154 MET B SD  1 
ATOM   4399 C CE  . MET B 1 125 ? 15.634  -11.910 3.176   1.00 63.07  ? 154 MET B CE  1 
ATOM   4400 N N   . LEU B 1 126 ? 15.011  -16.317 7.074   1.00 48.33  ? 155 LEU B N   1 
ATOM   4401 C CA  . LEU B 1 126 ? 15.697  -16.047 8.330   1.00 48.40  ? 155 LEU B CA  1 
ATOM   4402 C C   . LEU B 1 126 ? 16.443  -17.295 8.799   1.00 50.20  ? 155 LEU B C   1 
ATOM   4403 O O   . LEU B 1 126 ? 17.602  -17.205 9.195   1.00 50.51  ? 155 LEU B O   1 
ATOM   4404 C CB  . LEU B 1 126 ? 14.714  -15.551 9.390   1.00 46.21  ? 155 LEU B CB  1 
ATOM   4405 C CG  . LEU B 1 126 ? 14.201  -14.119 9.201   1.00 44.79  ? 155 LEU B CG  1 
ATOM   4406 C CD1 . LEU B 1 126 ? 12.925  -13.880 9.979   1.00 44.65  ? 155 LEU B CD1 1 
ATOM   4407 C CD2 . LEU B 1 126 ? 15.259  -13.119 9.615   1.00 46.26  ? 155 LEU B CD2 1 
ATOM   4408 N N   . ASP B 1 127 ? 15.781  -18.456 8.734   1.00 52.17  ? 156 ASP B N   1 
ATOM   4409 C CA  . ASP B 1 127 ? 16.402  -19.715 9.122   1.00 54.00  ? 156 ASP B CA  1 
ATOM   4410 C C   . ASP B 1 127 ? 17.699  -19.922 8.340   1.00 51.57  ? 156 ASP B C   1 
ATOM   4411 O O   . ASP B 1 127 ? 18.664  -20.448 8.885   1.00 55.83  ? 156 ASP B O   1 
ATOM   4412 C CB  . ASP B 1 127 ? 15.446  -20.892 8.979   1.00 52.23  ? 156 ASP B CB  1 
ATOM   4413 C CG  . ASP B 1 127 ? 14.391  -21.040 10.070  1.00 52.50  ? 156 ASP B CG  1 
ATOM   4414 O OD1 . ASP B 1 127 ? 14.263  -20.115 10.908  1.00 51.29  ? 156 ASP B OD1 1 
ATOM   4415 O OD2 . ASP B 1 127 ? 13.710  -22.091 10.081  1.00 50.69  ? 156 ASP B OD2 1 
ATOM   4416 N N   . ASN B 1 128 ? 17.727  -19.474 7.080   1.00 51.79  ? 157 ASN B N   1 
ATOM   4417 C CA  . ASN B 1 128 ? 18.875  -19.679 6.209   1.00 53.76  ? 157 ASN B CA  1 
ATOM   4418 C C   . ASN B 1 128 ? 19.705  -18.402 6.088   1.00 57.16  ? 157 ASN B C   1 
ATOM   4419 O O   . ASN B 1 128 ? 20.138  -18.052 4.989   1.00 62.08  ? 157 ASN B O   1 
ATOM   4420 C CB  . ASN B 1 128 ? 18.433  -20.156 4.832   1.00 54.13  ? 157 ASN B CB  1 
ATOM   4421 C CG  . ASN B 1 128 ? 17.571  -21.393 4.910   1.00 56.73  ? 157 ASN B CG  1 
ATOM   4422 O OD1 . ASN B 1 128 ? 17.644  -22.143 5.890   1.00 61.31  ? 157 ASN B OD1 1 
ATOM   4423 N ND2 . ASN B 1 128 ? 16.764  -21.633 3.888   1.00 57.36  ? 157 ASN B ND2 1 
ATOM   4424 N N   . PHE B 1 129 ? 19.929  -17.716 7.218   1.00 49.31  ? 158 PHE B N   1 
ATOM   4425 C CA  . PHE B 1 129 ? 20.848  -16.593 7.257   1.00 45.12  ? 158 PHE B CA  1 
ATOM   4426 C C   . PHE B 1 129 ? 22.091  -17.011 8.033   1.00 44.68  ? 158 PHE B C   1 
ATOM   4427 O O   . PHE B 1 129 ? 21.981  -17.516 9.150   1.00 44.16  ? 158 PHE B O   1 
ATOM   4428 C CB  . PHE B 1 129 ? 20.240  -15.338 7.894   1.00 44.25  ? 158 PHE B CB  1 
ATOM   4429 C CG  . PHE B 1 129 ? 19.489  -14.395 6.965   1.00 42.67  ? 158 PHE B CG  1 
ATOM   4430 C CD1 . PHE B 1 129 ? 19.843  -14.256 5.624   1.00 42.68  ? 158 PHE B CD1 1 
ATOM   4431 C CD2 . PHE B 1 129 ? 18.444  -13.617 7.450   1.00 42.76  ? 158 PHE B CD2 1 
ATOM   4432 C CE1 . PHE B 1 129 ? 19.160  -13.382 4.795   1.00 41.26  ? 158 PHE B CE1 1 
ATOM   4433 C CE2 . PHE B 1 129 ? 17.765  -12.739 6.615   1.00 43.60  ? 158 PHE B CE2 1 
ATOM   4434 C CZ  . PHE B 1 129 ? 18.127  -12.624 5.292   1.00 41.91  ? 158 PHE B CZ  1 
ATOM   4435 N N   . PRO B 1 130 ? 23.306  -16.786 7.481   1.00 44.71  ? 159 PRO B N   1 
ATOM   4436 C CA  . PRO B 1 130 ? 24.544  -17.182 8.153   1.00 45.26  ? 159 PRO B CA  1 
ATOM   4437 C C   . PRO B 1 130 ? 24.832  -16.302 9.360   1.00 47.02  ? 159 PRO B C   1 
ATOM   4438 O O   . PRO B 1 130 ? 24.258  -15.221 9.495   1.00 48.41  ? 159 PRO B O   1 
ATOM   4439 C CB  . PRO B 1 130 ? 25.622  -17.026 7.066   1.00 45.42  ? 159 PRO B CB  1 
ATOM   4440 C CG  . PRO B 1 130 ? 25.066  -15.955 6.156   1.00 45.50  ? 159 PRO B CG  1 
ATOM   4441 C CD  . PRO B 1 130 ? 23.554  -16.128 6.188   1.00 45.57  ? 159 PRO B CD  1 
ATOM   4442 N N   . THR B 1 131 ? 25.773  -16.761 10.189  1.00 47.49  ? 160 THR B N   1 
ATOM   4443 C CA  . THR B 1 131 ? 26.043  -16.150 11.480  1.00 50.51  ? 160 THR B CA  1 
ATOM   4444 C C   . THR B 1 131 ? 27.009  -14.974 11.340  1.00 48.30  ? 160 THR B C   1 
ATOM   4445 O O   . THR B 1 131 ? 27.391  -14.376 12.343  1.00 48.17  ? 160 THR B O   1 
ATOM   4446 C CB  . THR B 1 131 ? 26.593  -17.210 12.436  1.00 52.73  ? 160 THR B CB  1 
ATOM   4447 O OG1 . THR B 1 131 ? 27.802  -17.677 11.840  1.00 58.63  ? 160 THR B OG1 1 
ATOM   4448 C CG2 . THR B 1 131 ? 25.615  -18.349 12.668  1.00 52.95  ? 160 THR B CG2 1 
ATOM   4449 N N   . ASN B 1 132 ? 27.418  -14.654 10.106  1.00 46.19  ? 161 ASN B N   1 
ATOM   4450 C CA  . ASN B 1 132 ? 28.336  -13.550 9.864   1.00 44.06  ? 161 ASN B CA  1 
ATOM   4451 C C   . ASN B 1 132 ? 27.611  -12.433 9.113   1.00 40.12  ? 161 ASN B C   1 
ATOM   4452 O O   . ASN B 1 132 ? 28.246  -11.502 8.626   1.00 43.91  ? 161 ASN B O   1 
ATOM   4453 C CB  . ASN B 1 132 ? 29.586  -14.019 9.122   1.00 44.26  ? 161 ASN B CB  1 
ATOM   4454 C CG  . ASN B 1 132 ? 29.296  -14.369 7.682   1.00 46.35  ? 161 ASN B CG  1 
ATOM   4455 O OD1 . ASN B 1 132 ? 28.360  -15.129 7.404   1.00 46.48  ? 161 ASN B OD1 1 
ATOM   4456 N ND2 . ASN B 1 132 ? 30.053  -13.801 6.755   1.00 47.06  ? 161 ASN B ND2 1 
ATOM   4457 N N   . LEU B 1 133 ? 26.284  -12.547 9.004   1.00 34.81  ? 162 LEU B N   1 
ATOM   4458 C CA  . LEU B 1 133 ? 25.451  -11.485 8.473   1.00 32.91  ? 162 LEU B CA  1 
ATOM   4459 C C   . LEU B 1 133 ? 24.884  -10.717 9.658   1.00 32.17  ? 162 LEU B C   1 
ATOM   4460 O O   . LEU B 1 133 ? 24.136  -11.287 10.453  1.00 32.71  ? 162 LEU B O   1 
ATOM   4461 C CB  . LEU B 1 133 ? 24.335  -12.063 7.600   1.00 31.96  ? 162 LEU B CB  1 
ATOM   4462 C CG  . LEU B 1 133 ? 23.323  -11.057 7.046   1.00 32.01  ? 162 LEU B CG  1 
ATOM   4463 C CD1 . LEU B 1 133 ? 24.013  -10.003 6.201   1.00 31.56  ? 162 LEU B CD1 1 
ATOM   4464 C CD2 . LEU B 1 133 ? 22.222  -11.746 6.242   1.00 32.37  ? 162 LEU B CD2 1 
ATOM   4465 N N   . HIS B 1 134 ? 25.246  -9.430  9.750   1.00 30.58  ? 163 HIS B N   1 
ATOM   4466 C CA  . HIS B 1 134 ? 24.885  -8.584  10.875  1.00 28.12  ? 163 HIS B CA  1 
ATOM   4467 C C   . HIS B 1 134 ? 23.380  -8.649  11.153  1.00 27.37  ? 163 HIS B C   1 
ATOM   4468 O O   . HIS B 1 134 ? 22.562  -8.617  10.230  1.00 27.19  ? 163 HIS B O   1 
ATOM   4469 C CB  . HIS B 1 134 ? 25.357  -7.148  10.624  1.00 28.96  ? 163 HIS B CB  1 
ATOM   4470 C CG  . HIS B 1 134 ? 25.376  -6.296  11.852  1.00 29.54  ? 163 HIS B CG  1 
ATOM   4471 N ND1 . HIS B 1 134 ? 24.251  -5.652  12.331  1.00 30.02  ? 163 HIS B ND1 1 
ATOM   4472 C CD2 . HIS B 1 134 ? 26.368  -6.014  12.712  1.00 29.73  ? 163 HIS B CD2 1 
ATOM   4473 C CE1 . HIS B 1 134 ? 24.561  -4.990  13.446  1.00 30.58  ? 163 HIS B CE1 1 
ATOM   4474 N NE2 . HIS B 1 134 ? 25.849  -5.191  13.696  1.00 31.07  ? 163 HIS B NE2 1 
ATOM   4475 N N   . PRO B 1 135 ? 22.972  -8.712  12.443  1.00 26.58  ? 164 PRO B N   1 
ATOM   4476 C CA  . PRO B 1 135 ? 21.558  -8.635  12.834  1.00 26.78  ? 164 PRO B CA  1 
ATOM   4477 C C   . PRO B 1 135 ? 20.717  -7.640  12.036  1.00 27.78  ? 164 PRO B C   1 
ATOM   4478 O O   . PRO B 1 135 ? 19.615  -7.972  11.587  1.00 26.75  ? 164 PRO B O   1 
ATOM   4479 C CB  . PRO B 1 135 ? 21.656  -8.190  14.302  1.00 26.03  ? 164 PRO B CB  1 
ATOM   4480 C CG  . PRO B 1 135 ? 22.936  -8.788  14.795  1.00 26.12  ? 164 PRO B CG  1 
ATOM   4481 C CD  . PRO B 1 135 ? 23.870  -8.814  13.604  1.00 25.99  ? 164 PRO B CD  1 
ATOM   4482 N N   . MET B 1 136 ? 21.249  -6.412  11.884  1.00 27.79  ? 165 MET B N   1 
ATOM   4483 C CA  . MET B 1 136 ? 20.534  -5.321  11.227  1.00 28.09  ? 165 MET B CA  1 
ATOM   4484 C C   . MET B 1 136 ? 20.293  -5.633  9.752   1.00 26.48  ? 165 MET B C   1 
ATOM   4485 O O   . MET B 1 136 ? 19.225  -5.332  9.216   1.00 25.52  ? 165 MET B O   1 
ATOM   4486 C CB  . MET B 1 136 ? 21.282  -3.993  11.384  1.00 27.48  ? 165 MET B CB  1 
ATOM   4487 C CG  . MET B 1 136 ? 21.160  -3.404  12.780  1.00 29.19  ? 165 MET B CG  1 
ATOM   4488 S SD  . MET B 1 136 ? 19.429  -3.078  13.181  1.00 30.82  ? 165 MET B SD  1 
ATOM   4489 C CE  . MET B 1 136 ? 19.036  -1.755  12.028  1.00 30.51  ? 165 MET B CE  1 
ATOM   4490 N N   . SER B 1 137 ? 21.294  -6.224  9.096   1.00 28.92  ? 166 SER B N   1 
ATOM   4491 C CA  . SER B 1 137 ? 21.152  -6.644  7.711   1.00 29.19  ? 166 SER B CA  1 
ATOM   4492 C C   . SER B 1 137 ? 20.026  -7.673  7.593   1.00 32.19  ? 166 SER B C   1 
ATOM   4493 O O   . SER B 1 137 ? 19.218  -7.625  6.661   1.00 36.82  ? 166 SER B O   1 
ATOM   4494 C CB  . SER B 1 137 ? 22.453  -7.186  7.189   1.00 30.01  ? 166 SER B CB  1 
ATOM   4495 O OG  . SER B 1 137 ? 23.518  -6.270  7.415   1.00 30.52  ? 166 SER B OG  1 
ATOM   4496 N N   . GLN B 1 138 ? 19.990  -8.612  8.544   1.00 32.41  ? 167 GLN B N   1 
ATOM   4497 C CA  . GLN B 1 138 ? 18.961  -9.635  8.575   1.00 31.10  ? 167 GLN B CA  1 
ATOM   4498 C C   . GLN B 1 138 ? 17.602  -8.960  8.760   1.00 30.03  ? 167 GLN B C   1 
ATOM   4499 O O   . GLN B 1 138 ? 16.636  -9.321  8.088   1.00 29.56  ? 167 GLN B O   1 
ATOM   4500 C CB  . GLN B 1 138 ? 19.231  -10.667 9.675   1.00 31.97  ? 167 GLN B CB  1 
ATOM   4501 C CG  . GLN B 1 138 ? 20.410  -11.598 9.404   1.00 34.44  ? 167 GLN B CG  1 
ATOM   4502 C CD  . GLN B 1 138 ? 20.488  -12.748 10.388  1.00 37.55  ? 167 GLN B CD  1 
ATOM   4503 O OE1 . GLN B 1 138 ? 19.590  -13.593 10.454  1.00 44.93  ? 167 GLN B OE1 1 
ATOM   4504 N NE2 . GLN B 1 138 ? 21.546  -12.796 11.183  1.00 37.12  ? 167 GLN B NE2 1 
ATOM   4505 N N   . LEU B 1 139 ? 17.533  -7.977  9.671   1.00 28.38  ? 168 LEU B N   1 
ATOM   4506 C CA  . LEU B 1 139 ? 16.292  -7.259  9.930   1.00 26.85  ? 168 LEU B CA  1 
ATOM   4507 C C   . LEU B 1 139 ? 15.800  -6.602  8.642   1.00 25.81  ? 168 LEU B C   1 
ATOM   4508 O O   . LEU B 1 139 ? 14.684  -6.848  8.201   1.00 26.49  ? 168 LEU B O   1 
ATOM   4509 C CB  . LEU B 1 139 ? 16.477  -6.223  11.039  1.00 26.95  ? 168 LEU B CB  1 
ATOM   4510 C CG  . LEU B 1 139 ? 15.262  -5.336  11.329  1.00 25.91  ? 168 LEU B CG  1 
ATOM   4511 C CD1 . LEU B 1 139 ? 14.174  -6.133  12.004  1.00 26.28  ? 168 LEU B CD1 1 
ATOM   4512 C CD2 . LEU B 1 139 ? 15.621  -4.107  12.147  1.00 23.57  ? 168 LEU B CD2 1 
ATOM   4513 N N   . SER B 1 140 ? 16.648  -5.774  8.028   1.00 26.18  ? 169 SER B N   1 
ATOM   4514 C CA  . SER B 1 140 ? 16.272  -5.042  6.832   1.00 25.87  ? 169 SER B CA  1 
ATOM   4515 C C   . SER B 1 140 ? 15.858  -6.002  5.721   1.00 26.98  ? 169 SER B C   1 
ATOM   4516 O O   . SER B 1 140 ? 14.841  -5.792  5.057   1.00 27.13  ? 169 SER B O   1 
ATOM   4517 C CB  . SER B 1 140 ? 17.394  -4.158  6.377   1.00 25.69  ? 169 SER B CB  1 
ATOM   4518 O OG  . SER B 1 140 ? 17.102  -3.594  5.110   1.00 26.16  ? 169 SER B OG  1 
ATOM   4519 N N   . ALA B 1 141 ? 16.690  -7.026  5.504   1.00 28.55  ? 170 ALA B N   1 
ATOM   4520 C CA  . ALA B 1 141 ? 16.472  -7.998  4.446   1.00 28.85  ? 170 ALA B CA  1 
ATOM   4521 C C   . ALA B 1 141 ? 15.123  -8.691  4.619   1.00 29.45  ? 170 ALA B C   1 
ATOM   4522 O O   . ALA B 1 141 ? 14.380  -8.853  3.658   1.00 26.33  ? 170 ALA B O   1 
ATOM   4523 C CB  . ALA B 1 141 ? 17.591  -9.006  4.469   1.00 30.94  ? 170 ALA B CB  1 
ATOM   4524 N N   . ALA B 1 142 ? 14.821  -9.094  5.860   1.00 31.93  ? 171 ALA B N   1 
ATOM   4525 C CA  . ALA B 1 142 ? 13.584  -9.792  6.167   1.00 33.47  ? 171 ALA B CA  1 
ATOM   4526 C C   . ALA B 1 142 ? 12.382  -8.878  5.941   1.00 34.92  ? 171 ALA B C   1 
ATOM   4527 O O   . ALA B 1 142 ? 11.379  -9.302  5.377   1.00 35.53  ? 171 ALA B O   1 
ATOM   4528 C CB  . ALA B 1 142 ? 13.629  -10.315 7.584   1.00 33.63  ? 171 ALA B CB  1 
ATOM   4529 N N   . VAL B 1 143 ? 12.495  -7.615  6.370   1.00 37.61  ? 172 VAL B N   1 
ATOM   4530 C CA  . VAL B 1 143 ? 11.406  -6.664  6.218   1.00 35.24  ? 172 VAL B CA  1 
ATOM   4531 C C   . VAL B 1 143 ? 11.166  -6.372  4.739   1.00 35.11  ? 172 VAL B C   1 
ATOM   4532 O O   . VAL B 1 143 ? 10.017  -6.302  4.316   1.00 32.93  ? 172 VAL B O   1 
ATOM   4533 C CB  . VAL B 1 143 ? 11.647  -5.368  7.005   1.00 35.29  ? 172 VAL B CB  1 
ATOM   4534 C CG1 . VAL B 1 143 ? 10.601  -4.317  6.674   1.00 36.31  ? 172 VAL B CG1 1 
ATOM   4535 C CG2 . VAL B 1 143 ? 11.688  -5.619  8.506   1.00 35.75  ? 172 VAL B CG2 1 
ATOM   4536 N N   . THR B 1 144 ? 12.238  -6.201  3.952   1.00 35.49  ? 173 THR B N   1 
ATOM   4537 C CA  . THR B 1 144 ? 12.095  -6.018  2.512   1.00 35.74  ? 173 THR B CA  1 
ATOM   4538 C C   . THR B 1 144 ? 11.240  -7.155  1.945   1.00 37.69  ? 173 THR B C   1 
ATOM   4539 O O   . THR B 1 144 ? 10.319  -6.911  1.160   1.00 39.05  ? 173 THR B O   1 
ATOM   4540 C CB  . THR B 1 144 ? 13.472  -5.957  1.839   1.00 34.23  ? 173 THR B CB  1 
ATOM   4541 O OG1 . THR B 1 144 ? 14.157  -4.807  2.323   1.00 33.78  ? 173 THR B OG1 1 
ATOM   4542 C CG2 . THR B 1 144 ? 13.401  -5.841  0.327   1.00 32.73  ? 173 THR B CG2 1 
ATOM   4543 N N   . ALA B 1 145 ? 11.548  -8.393  2.366   1.00 37.52  ? 174 ALA B N   1 
ATOM   4544 C CA  . ALA B 1 145 ? 10.915  -9.596  1.841   1.00 38.22  ? 174 ALA B CA  1 
ATOM   4545 C C   . ALA B 1 145 ? 9.458   -9.704  2.291   1.00 38.50  ? 174 ALA B C   1 
ATOM   4546 O O   . ALA B 1 145 ? 8.645   -10.312 1.596   1.00 36.63  ? 174 ALA B O   1 
ATOM   4547 C CB  . ALA B 1 145 ? 11.705  -10.819 2.258   1.00 39.51  ? 174 ALA B CB  1 
ATOM   4548 N N   . LEU B 1 146 ? 9.130   -9.106  3.445   1.00 38.49  ? 175 LEU B N   1 
ATOM   4549 C CA  . LEU B 1 146 ? 7.754   -9.060  3.916   1.00 39.97  ? 175 LEU B CA  1 
ATOM   4550 C C   . LEU B 1 146 ? 6.877   -8.304  2.927   1.00 42.17  ? 175 LEU B C   1 
ATOM   4551 O O   . LEU B 1 146 ? 5.658   -8.402  3.031   1.00 45.89  ? 175 LEU B O   1 
ATOM   4552 C CB  . LEU B 1 146 ? 7.616   -8.406  5.291   1.00 40.89  ? 175 LEU B CB  1 
ATOM   4553 C CG  . LEU B 1 146 ? 8.024   -9.235  6.510   1.00 40.89  ? 175 LEU B CG  1 
ATOM   4554 C CD1 . LEU B 1 146 ? 8.083   -8.341  7.737   1.00 40.28  ? 175 LEU B CD1 1 
ATOM   4555 C CD2 . LEU B 1 146 ? 7.058   -10.376 6.743   1.00 41.72  ? 175 LEU B CD2 1 
ATOM   4556 N N   . ASN B 1 147 ? 7.476   -7.538  1.999   1.00 41.42  ? 176 ASN B N   1 
ATOM   4557 C CA  . ASN B 1 147 ? 6.708   -6.575  1.221   1.00 41.02  ? 176 ASN B CA  1 
ATOM   4558 C C   . ASN B 1 147 ? 5.740   -7.305  0.290   1.00 40.89  ? 176 ASN B C   1 
ATOM   4559 O O   . ASN B 1 147 ? 4.846   -6.687  -0.274  1.00 45.31  ? 176 ASN B O   1 
ATOM   4560 C CB  . ASN B 1 147 ? 7.595   -5.551  0.511   1.00 40.60  ? 176 ASN B CB  1 
ATOM   4561 C CG  . ASN B 1 147 ? 7.616   -5.671  -0.997  1.00 39.95  ? 176 ASN B CG  1 
ATOM   4562 O OD1 . ASN B 1 147 ? 8.009   -6.707  -1.550  1.00 39.94  ? 176 ASN B OD1 1 
ATOM   4563 N ND2 . ASN B 1 147 ? 7.214   -4.609  -1.679  1.00 38.61  ? 176 ASN B ND2 1 
ATOM   4564 N N   . SER B 1 148 ? 5.906   -8.623  0.148   1.00 43.47  ? 177 SER B N   1 
ATOM   4565 C CA  . SER B 1 148 ? 4.996   -9.437  -0.640  1.00 44.31  ? 177 SER B CA  1 
ATOM   4566 C C   . SER B 1 148 ? 3.602   -9.498  -0.005  1.00 45.80  ? 177 SER B C   1 
ATOM   4567 O O   . SER B 1 148 ? 2.636   -9.782  -0.707  1.00 48.19  ? 177 SER B O   1 
ATOM   4568 C CB  . SER B 1 148 ? 5.580   -10.814 -0.867  1.00 44.24  ? 177 SER B CB  1 
ATOM   4569 O OG  . SER B 1 148 ? 6.105   -11.358 0.337   1.00 44.34  ? 177 SER B OG  1 
ATOM   4570 N N   . GLU B 1 149 ? 3.495   -9.211  1.302   1.00 47.42  ? 178 GLU B N   1 
ATOM   4571 C CA  . GLU B 1 149 ? 2.215   -9.168  1.999   1.00 50.51  ? 178 GLU B CA  1 
ATOM   4572 C C   . GLU B 1 149 ? 1.601   -7.768  1.956   1.00 49.91  ? 178 GLU B C   1 
ATOM   4573 O O   . GLU B 1 149 ? 0.602   -7.522  2.629   1.00 56.32  ? 178 GLU B O   1 
ATOM   4574 C CB  . GLU B 1 149 ? 2.331   -9.494  3.492   1.00 53.52  ? 178 GLU B CB  1 
ATOM   4575 C CG  . GLU B 1 149 ? 2.985   -10.837 3.802   1.00 56.21  ? 178 GLU B CG  1 
ATOM   4576 C CD  . GLU B 1 149 ? 2.264   -12.063 3.267   1.00 56.25  ? 178 GLU B CD  1 
ATOM   4577 O OE1 . GLU B 1 149 ? 1.359   -12.606 3.949   1.00 56.22  ? 178 GLU B OE1 1 
ATOM   4578 O OE2 . GLU B 1 149 ? 2.624   -12.465 2.140   1.00 53.28  ? 178 GLU B OE2 1 
ATOM   4579 N N   . SER B 1 150 ? 2.190   -6.847  1.186   1.00 46.90  ? 179 SER B N   1 
ATOM   4580 C CA  . SER B 1 150 ? 1.808   -5.445  1.259   1.00 46.70  ? 179 SER B CA  1 
ATOM   4581 C C   . SER B 1 150 ? 0.444   -5.216  0.611   1.00 50.28  ? 179 SER B C   1 
ATOM   4582 O O   . SER B 1 150 ? 0.256   -5.542  -0.557  1.00 50.72  ? 179 SER B O   1 
ATOM   4583 C CB  . SER B 1 150 ? 2.848   -4.564  0.614   1.00 45.03  ? 179 SER B CB  1 
ATOM   4584 O OG  . SER B 1 150 ? 2.499   -3.195  0.755   1.00 41.30  ? 179 SER B OG  1 
ATOM   4585 N N   . ASN B 1 151 ? -0.488  -4.620  1.370   1.00 52.66  ? 180 ASN B N   1 
ATOM   4586 C CA  . ASN B 1 151 ? -1.777  -4.212  0.830   1.00 52.07  ? 180 ASN B CA  1 
ATOM   4587 C C   . ASN B 1 151 ? -1.601  -3.021  -0.107  1.00 52.73  ? 180 ASN B C   1 
ATOM   4588 O O   . ASN B 1 151 ? -2.217  -2.977  -1.167  1.00 56.84  ? 180 ASN B O   1 
ATOM   4589 C CB  . ASN B 1 151 ? -2.781  -3.840  1.915   1.00 54.65  ? 180 ASN B CB  1 
ATOM   4590 C CG  . ASN B 1 151 ? -3.251  -5.027  2.723   1.00 56.48  ? 180 ASN B CG  1 
ATOM   4591 O OD1 . ASN B 1 151 ? -3.215  -4.988  3.958   1.00 55.02  ? 180 ASN B OD1 1 
ATOM   4592 N ND2 . ASN B 1 151 ? -3.719  -6.073  2.054   1.00 57.38  ? 180 ASN B ND2 1 
ATOM   4593 N N   . PHE B 1 152 ? -0.763  -2.058  0.300   1.00 49.44  ? 181 PHE B N   1 
ATOM   4594 C CA  . PHE B 1 152 ? -0.580  -0.829  -0.452  1.00 49.80  ? 181 PHE B CA  1 
ATOM   4595 C C   . PHE B 1 152 ? -0.017  -1.144  -1.837  1.00 51.71  ? 181 PHE B C   1 
ATOM   4596 O O   . PHE B 1 152 ? -0.316  -0.429  -2.791  1.00 52.75  ? 181 PHE B O   1 
ATOM   4597 C CB  . PHE B 1 152 ? 0.334   0.133   0.317   1.00 49.04  ? 181 PHE B CB  1 
ATOM   4598 C CG  . PHE B 1 152 ? 0.533   1.500   -0.329  1.00 47.56  ? 181 PHE B CG  1 
ATOM   4599 C CD1 . PHE B 1 152 ? 1.459   1.683   -1.353  1.00 46.16  ? 181 PHE B CD1 1 
ATOM   4600 C CD2 . PHE B 1 152 ? -0.187  2.609   0.107   1.00 47.51  ? 181 PHE B CD2 1 
ATOM   4601 C CE1 . PHE B 1 152 ? 1.640   2.933   -1.930  1.00 46.33  ? 181 PHE B CE1 1 
ATOM   4602 C CE2 . PHE B 1 152 ? -0.003  3.857   -0.476  1.00 44.81  ? 181 PHE B CE2 1 
ATOM   4603 C CZ  . PHE B 1 152 ? 0.909   4.015   -1.494  1.00 46.25  ? 181 PHE B CZ  1 
ATOM   4604 N N   . ALA B 1 153 ? 0.803   -2.201  -1.937  1.00 52.55  ? 182 ALA B N   1 
ATOM   4605 C CA  . ALA B 1 153 ? 1.509   -2.507  -3.172  1.00 56.25  ? 182 ALA B CA  1 
ATOM   4606 C C   . ALA B 1 153 ? 0.534   -3.000  -4.239  1.00 59.18  ? 182 ALA B C   1 
ATOM   4607 O O   . ALA B 1 153 ? 0.523   -2.481  -5.351  1.00 59.59  ? 182 ALA B O   1 
ATOM   4608 C CB  . ALA B 1 153 ? 2.610   -3.512  -2.916  1.00 54.65  ? 182 ALA B CB  1 
ATOM   4609 N N   . ARG B 1 154 ? -0.278  -4.005  -3.898  1.00 63.02  ? 183 ARG B N   1 
ATOM   4610 C CA  . ARG B 1 154 ? -1.283  -4.512  -4.822  1.00 65.37  ? 183 ARG B CA  1 
ATOM   4611 C C   . ARG B 1 154 ? -2.356  -3.454  -5.073  1.00 58.79  ? 183 ARG B C   1 
ATOM   4612 O O   . ARG B 1 154 ? -2.812  -3.307  -6.203  1.00 56.09  ? 183 ARG B O   1 
ATOM   4613 C CB  . ARG B 1 154 ? -1.905  -5.824  -4.330  1.00 71.62  ? 183 ARG B CB  1 
ATOM   4614 C CG  . ARG B 1 154 ? -1.077  -7.045  -4.705  1.00 76.80  ? 183 ARG B CG  1 
ATOM   4615 C CD  . ARG B 1 154 ? -1.716  -8.356  -4.267  1.00 78.58  ? 183 ARG B CD  1 
ATOM   4616 N NE  . ARG B 1 154 ? -1.612  -8.605  -2.824  1.00 81.21  ? 183 ARG B NE  1 
ATOM   4617 C CZ  . ARG B 1 154 ? -0.482  -8.820  -2.150  1.00 82.14  ? 183 ARG B CZ  1 
ATOM   4618 N NH1 . ARG B 1 154 ? -0.523  -9.117  -0.861  1.00 82.91  ? 183 ARG B NH1 1 
ATOM   4619 N NH2 . ARG B 1 154 ? 0.687   -8.760  -2.764  1.00 79.30  ? 183 ARG B NH2 1 
ATOM   4620 N N   . ALA B 1 155 ? -2.752  -2.721  -4.023  1.00 55.55  ? 184 ALA B N   1 
ATOM   4621 C CA  . ALA B 1 155 ? -3.773  -1.689  -4.148  1.00 54.09  ? 184 ALA B CA  1 
ATOM   4622 C C   . ALA B 1 155 ? -3.376  -0.679  -5.225  1.00 51.84  ? 184 ALA B C   1 
ATOM   4623 O O   . ALA B 1 155 ? -4.143  -0.410  -6.148  1.00 51.30  ? 184 ALA B O   1 
ATOM   4624 C CB  . ALA B 1 155 ? -3.996  -1.004  -2.818  1.00 52.80  ? 184 ALA B CB  1 
ATOM   4625 N N   . TYR B 1 156 ? -2.159  -0.139  -5.094  1.00 48.58  ? 185 TYR B N   1 
ATOM   4626 C CA  . TYR B 1 156 ? -1.634  0.846   -6.023  1.00 45.02  ? 185 TYR B CA  1 
ATOM   4627 C C   . TYR B 1 156 ? -1.586  0.269   -7.439  1.00 45.73  ? 185 TYR B C   1 
ATOM   4628 O O   . TYR B 1 156 ? -1.814  0.995   -8.409  1.00 41.63  ? 185 TYR B O   1 
ATOM   4629 C CB  . TYR B 1 156 ? -0.257  1.331   -5.557  1.00 42.15  ? 185 TYR B CB  1 
ATOM   4630 C CG  . TYR B 1 156 ? 0.265   2.477   -6.409  1.00 37.47  ? 185 TYR B CG  1 
ATOM   4631 C CD1 . TYR B 1 156 ? 0.869   2.225   -7.634  1.00 38.35  ? 185 TYR B CD1 1 
ATOM   4632 C CD2 . TYR B 1 156 ? 0.120   3.799   -6.016  1.00 35.47  ? 185 TYR B CD2 1 
ATOM   4633 C CE1 . TYR B 1 156 ? 1.314   3.251   -8.446  1.00 38.16  ? 185 TYR B CE1 1 
ATOM   4634 C CE2 . TYR B 1 156 ? 0.575   4.836   -6.815  1.00 37.53  ? 185 TYR B CE2 1 
ATOM   4635 C CZ  . TYR B 1 156 ? 1.176   4.559   -8.030  1.00 38.25  ? 185 TYR B CZ  1 
ATOM   4636 O OH  . TYR B 1 156 ? 1.642   5.531   -8.862  1.00 45.32  ? 185 TYR B OH  1 
ATOM   4637 N N   . ALA B 1 157 ? -1.299  -1.034  -7.551  1.00 47.61  ? 186 ALA B N   1 
ATOM   4638 C CA  . ALA B 1 157 ? -1.194  -1.696  -8.842  1.00 52.31  ? 186 ALA B CA  1 
ATOM   4639 C C   . ALA B 1 157 ? -2.520  -1.649  -9.599  1.00 55.61  ? 186 ALA B C   1 
ATOM   4640 O O   . ALA B 1 157 ? -2.528  -1.519  -10.819 1.00 62.17  ? 186 ALA B O   1 
ATOM   4641 C CB  . ALA B 1 157 ? -0.725  -3.121  -8.653  1.00 54.75  ? 186 ALA B CB  1 
ATOM   4642 N N   . GLN B 1 158 ? -3.633  -1.751  -8.866  1.00 58.90  ? 187 GLN B N   1 
ATOM   4643 C CA  . GLN B 1 158 ? -4.962  -1.774  -9.455  1.00 58.85  ? 187 GLN B CA  1 
ATOM   4644 C C   . GLN B 1 158 ? -5.494  -0.363  -9.686  1.00 60.66  ? 187 GLN B C   1 
ATOM   4645 O O   . GLN B 1 158 ? -6.563  -0.200  -10.270 1.00 63.97  ? 187 GLN B O   1 
ATOM   4646 C CB  . GLN B 1 158 ? -5.934  -2.477  -8.514  1.00 59.57  ? 187 GLN B CB  1 
ATOM   4647 C CG  . GLN B 1 158 ? -5.583  -3.931  -8.238  1.00 59.67  ? 187 GLN B CG  1 
ATOM   4648 C CD  . GLN B 1 158 ? -6.330  -4.472  -7.043  1.00 62.61  ? 187 GLN B CD  1 
ATOM   4649 O OE1 . GLN B 1 158 ? -6.097  -4.054  -5.902  1.00 65.67  ? 187 GLN B OE1 1 
ATOM   4650 N NE2 . GLN B 1 158 ? -7.241  -5.400  -7.295  1.00 64.02  ? 187 GLN B NE2 1 
ATOM   4651 N N   . GLY B 1 159 ? -4.767  0.646   -9.194  1.00 58.21  ? 188 GLY B N   1 
ATOM   4652 C CA  . GLY B 1 159 ? -5.141  2.034   -9.402  1.00 55.97  ? 188 GLY B CA  1 
ATOM   4653 C C   . GLY B 1 159 ? -6.106  2.516   -8.323  1.00 57.03  ? 188 GLY B C   1 
ATOM   4654 O O   . GLY B 1 159 ? -7.175  3.042   -8.629  1.00 60.08  ? 188 GLY B O   1 
ATOM   4655 N N   . ILE B 1 160 ? -5.712  2.337   -7.058  1.00 55.72  ? 189 ILE B N   1 
ATOM   4656 C CA  . ILE B 1 160 ? -6.464  2.872   -5.935  1.00 56.14  ? 189 ILE B CA  1 
ATOM   4657 C C   . ILE B 1 160 ? -6.344  4.395   -5.976  1.00 53.02  ? 189 ILE B C   1 
ATOM   4658 O O   . ILE B 1 160 ? -5.420  4.924   -6.589  1.00 58.03  ? 189 ILE B O   1 
ATOM   4659 C CB  . ILE B 1 160 ? -5.981  2.263   -4.600  1.00 58.77  ? 189 ILE B CB  1 
ATOM   4660 C CG1 . ILE B 1 160 ? -6.940  2.557   -3.433  1.00 62.16  ? 189 ILE B CG1 1 
ATOM   4661 C CG2 . ILE B 1 160 ? -4.551  2.694   -4.265  1.00 57.72  ? 189 ILE B CG2 1 
ATOM   4662 C CD1 . ILE B 1 160 ? -8.327  1.951   -3.581  1.00 63.70  ? 189 ILE B CD1 1 
ATOM   4663 N N   . SER B 1 161 ? -7.301  5.085   -5.346  1.00 49.78  ? 190 SER B N   1 
ATOM   4664 C CA  . SER B 1 161 ? -7.337  6.538   -5.324  1.00 48.18  ? 190 SER B CA  1 
ATOM   4665 C C   . SER B 1 161 ? -6.362  7.085   -4.280  1.00 46.45  ? 190 SER B C   1 
ATOM   4666 O O   . SER B 1 161 ? -6.160  6.473   -3.233  1.00 48.36  ? 190 SER B O   1 
ATOM   4667 C CB  . SER B 1 161 ? -8.756  7.035   -5.085  1.00 44.93  ? 190 SER B CB  1 
ATOM   4668 O OG  . SER B 1 161 ? -8.807  8.452   -4.968  1.00 42.70  ? 190 SER B OG  1 
ATOM   4669 N N   . ARG B 1 162 ? -5.792  8.261   -4.578  1.00 45.39  ? 191 ARG B N   1 
ATOM   4670 C CA  . ARG B 1 162 ? -4.902  8.990   -3.686  1.00 51.47  ? 191 ARG B CA  1 
ATOM   4671 C C   . ARG B 1 162 ? -5.531  9.212   -2.308  1.00 53.62  ? 191 ARG B C   1 
ATOM   4672 O O   . ARG B 1 162 ? -4.828  9.265   -1.297  1.00 52.07  ? 191 ARG B O   1 
ATOM   4673 C CB  . ARG B 1 162 ? -4.614  10.384  -4.254  1.00 53.44  ? 191 ARG B CB  1 
ATOM   4674 C CG  . ARG B 1 162 ? -3.843  10.430  -5.564  1.00 58.83  ? 191 ARG B CG  1 
ATOM   4675 C CD  . ARG B 1 162 ? -3.504  11.870  -5.917  1.00 63.06  ? 191 ARG B CD  1 
ATOM   4676 N NE  . ARG B 1 162 ? -2.485  11.989  -6.967  1.00 67.78  ? 191 ARG B NE  1 
ATOM   4677 C CZ  . ARG B 1 162 ? -1.961  13.135  -7.412  1.00 70.71  ? 191 ARG B CZ  1 
ATOM   4678 N NH1 . ARG B 1 162 ? -2.286  14.293  -6.858  1.00 69.56  ? 191 ARG B NH1 1 
ATOM   4679 N NH2 . ARG B 1 162 ? -1.098  13.116  -8.415  1.00 73.53  ? 191 ARG B NH2 1 
ATOM   4680 N N   . THR B 1 163 ? -6.859  9.386   -2.282  1.00 50.07  ? 192 THR B N   1 
ATOM   4681 C CA  . THR B 1 163 ? -7.575  9.691   -1.054  1.00 49.19  ? 192 THR B CA  1 
ATOM   4682 C C   . THR B 1 163 ? -7.515  8.509   -0.088  1.00 46.32  ? 192 THR B C   1 
ATOM   4683 O O   . THR B 1 163 ? -7.724  8.697   1.104   1.00 49.39  ? 192 THR B O   1 
ATOM   4684 C CB  . THR B 1 163 ? -9.021  10.069  -1.387  1.00 46.85  ? 192 THR B CB  1 
ATOM   4685 O OG1 . THR B 1 163 ? -9.480  9.087   -2.313  1.00 43.41  ? 192 THR B OG1 1 
ATOM   4686 C CG2 . THR B 1 163 ? -9.140  11.456  -1.992  1.00 44.30  ? 192 THR B CG2 1 
ATOM   4687 N N   . LYS B 1 164 ? -7.249  7.306   -0.611  1.00 47.47  ? 193 LYS B N   1 
ATOM   4688 C CA  . LYS B 1 164 ? -7.305  6.071   0.156   1.00 49.60  ? 193 LYS B CA  1 
ATOM   4689 C C   . LYS B 1 164 ? -5.913  5.558   0.522   1.00 46.70  ? 193 LYS B C   1 
ATOM   4690 O O   . LYS B 1 164 ? -5.804  4.530   1.179   1.00 45.36  ? 193 LYS B O   1 
ATOM   4691 C CB  . LYS B 1 164 ? -7.987  4.982   -0.680  1.00 55.25  ? 193 LYS B CB  1 
ATOM   4692 C CG  . LYS B 1 164 ? -9.482  5.169   -0.902  1.00 61.96  ? 193 LYS B CG  1 
ATOM   4693 C CD  . LYS B 1 164 ? -10.371 4.328   0.004   1.00 67.08  ? 193 LYS B CD  1 
ATOM   4694 C CE  . LYS B 1 164 ? -10.389 2.893   -0.435  1.00 73.26  ? 193 LYS B CE  1 
ATOM   4695 N NZ  . LYS B 1 164 ? -11.187 2.037   0.446   1.00 76.30  ? 193 LYS B NZ  1 
ATOM   4696 N N   . TYR B 1 165 ? -4.855  6.264   0.111   1.00 44.91  ? 194 TYR B N   1 
ATOM   4697 C CA  . TYR B 1 165 ? -3.497  5.794   0.343   1.00 45.47  ? 194 TYR B CA  1 
ATOM   4698 C C   . TYR B 1 165 ? -3.256  5.530   1.828   1.00 42.37  ? 194 TYR B C   1 
ATOM   4699 O O   . TYR B 1 165 ? -2.862  4.427   2.199   1.00 37.96  ? 194 TYR B O   1 
ATOM   4700 C CB  . TYR B 1 165 ? -2.450  6.785   -0.172  1.00 46.11  ? 194 TYR B CB  1 
ATOM   4701 C CG  . TYR B 1 165 ? -2.191  6.770   -1.674  1.00 44.64  ? 194 TYR B CG  1 
ATOM   4702 C CD1 . TYR B 1 165 ? -2.619  5.727   -2.494  1.00 45.37  ? 194 TYR B CD1 1 
ATOM   4703 C CD2 . TYR B 1 165 ? -1.476  7.804   -2.265  1.00 44.55  ? 194 TYR B CD2 1 
ATOM   4704 C CE1 . TYR B 1 165 ? -2.363  5.731   -3.857  1.00 45.59  ? 194 TYR B CE1 1 
ATOM   4705 C CE2 . TYR B 1 165 ? -1.216  7.820   -3.625  1.00 44.26  ? 194 TYR B CE2 1 
ATOM   4706 C CZ  . TYR B 1 165 ? -1.654  6.779   -4.420  1.00 44.53  ? 194 TYR B CZ  1 
ATOM   4707 O OH  . TYR B 1 165 ? -1.392  6.831   -5.754  1.00 45.74  ? 194 TYR B OH  1 
ATOM   4708 N N   . TRP B 1 166 ? -3.510  6.539   2.667   1.00 44.43  ? 195 TRP B N   1 
ATOM   4709 C CA  . TRP B 1 166 ? -3.195  6.462   4.084   1.00 49.64  ? 195 TRP B CA  1 
ATOM   4710 C C   . TRP B 1 166 ? -3.803  5.206   4.711   1.00 50.34  ? 195 TRP B C   1 
ATOM   4711 O O   . TRP B 1 166 ? -3.254  4.679   5.672   1.00 48.81  ? 195 TRP B O   1 
ATOM   4712 C CB  . TRP B 1 166 ? -3.652  7.734   4.817   1.00 51.48  ? 195 TRP B CB  1 
ATOM   4713 C CG  . TRP B 1 166 ? -5.145  7.864   4.953   1.00 58.51  ? 195 TRP B CG  1 
ATOM   4714 C CD1 . TRP B 1 166 ? -5.974  8.652   4.208   1.00 60.78  ? 195 TRP B CD1 1 
ATOM   4715 C CD2 . TRP B 1 166 ? -5.991  7.159   5.887   1.00 60.34  ? 195 TRP B CD2 1 
ATOM   4716 N NE1 . TRP B 1 166 ? -7.270  8.494   4.614   1.00 62.46  ? 195 TRP B NE1 1 
ATOM   4717 C CE2 . TRP B 1 166 ? -7.314  7.585   5.640   1.00 63.60  ? 195 TRP B CE2 1 
ATOM   4718 C CE3 . TRP B 1 166 ? -5.764  6.219   6.900   1.00 63.61  ? 195 TRP B CE3 1 
ATOM   4719 C CZ2 . TRP B 1 166 ? -8.398  7.099   6.371   1.00 64.37  ? 195 TRP B CZ2 1 
ATOM   4720 C CZ3 . TRP B 1 166 ? -6.837  5.734   7.616   1.00 65.55  ? 195 TRP B CZ3 1 
ATOM   4721 C CH2 . TRP B 1 166 ? -8.135  6.172   7.355   1.00 66.30  ? 195 TRP B CH2 1 
ATOM   4722 N N   . GLU B 1 167 ? -4.941  4.747   4.171   1.00 52.25  ? 196 GLU B N   1 
ATOM   4723 C CA  . GLU B 1 167 ? -5.665  3.608   4.712   1.00 51.40  ? 196 GLU B CA  1 
ATOM   4724 C C   . GLU B 1 167 ? -4.869  2.324   4.519   1.00 48.72  ? 196 GLU B C   1 
ATOM   4725 O O   . GLU B 1 167 ? -4.931  1.433   5.362   1.00 48.44  ? 196 GLU B O   1 
ATOM   4726 C CB  . GLU B 1 167 ? -7.023  3.390   4.040   1.00 55.48  ? 196 GLU B CB  1 
ATOM   4727 C CG  . GLU B 1 167 ? -8.084  4.421   4.412   1.00 58.51  ? 196 GLU B CG  1 
ATOM   4728 C CD  . GLU B 1 167 ? -9.445  4.193   3.769   1.00 63.36  ? 196 GLU B CD  1 
ATOM   4729 O OE1 . GLU B 1 167 ? -10.345 5.037   3.965   1.00 64.96  ? 196 GLU B OE1 1 
ATOM   4730 O OE2 . GLU B 1 167 ? -9.623  3.171   3.074   1.00 65.36  ? 196 GLU B OE2 1 
ATOM   4731 N N   . LEU B 1 168 ? -4.170  2.208   3.385   1.00 47.66  ? 197 LEU B N   1 
ATOM   4732 C CA  . LEU B 1 168 ? -3.427  0.993   3.087   1.00 46.52  ? 197 LEU B CA  1 
ATOM   4733 C C   . LEU B 1 168 ? -2.081  1.046   3.803   1.00 43.23  ? 197 LEU B C   1 
ATOM   4734 O O   . LEU B 1 168 ? -1.547  0.013   4.199   1.00 41.92  ? 197 LEU B O   1 
ATOM   4735 C CB  . LEU B 1 168 ? -3.255  0.803   1.581   1.00 46.67  ? 197 LEU B CB  1 
ATOM   4736 C CG  . LEU B 1 168 ? -4.509  0.426   0.783   1.00 50.88  ? 197 LEU B CG  1 
ATOM   4737 C CD1 . LEU B 1 168 ? -5.267  -0.748  1.390   1.00 52.52  ? 197 LEU B CD1 1 
ATOM   4738 C CD2 . LEU B 1 168 ? -5.433  1.614   0.604   1.00 51.81  ? 197 LEU B CD2 1 
ATOM   4739 N N   . ILE B 1 169 ? -1.540  2.263   3.946   1.00 40.71  ? 198 ILE B N   1 
ATOM   4740 C CA  . ILE B 1 169 ? -0.338  2.493   4.729   1.00 39.79  ? 198 ILE B CA  1 
ATOM   4741 C C   . ILE B 1 169 ? -0.607  1.978   6.138   1.00 41.88  ? 198 ILE B C   1 
ATOM   4742 O O   . ILE B 1 169 ? 0.176   1.202   6.683   1.00 39.71  ? 198 ILE B O   1 
ATOM   4743 C CB  . ILE B 1 169 ? 0.049   3.985   4.742   1.00 36.04  ? 198 ILE B CB  1 
ATOM   4744 C CG1 . ILE B 1 169 ? 0.368   4.515   3.348   1.00 35.69  ? 198 ILE B CG1 1 
ATOM   4745 C CG2 . ILE B 1 169 ? 1.200   4.245   5.716   1.00 34.79  ? 198 ILE B CG2 1 
ATOM   4746 C CD1 . ILE B 1 169 ? 1.679   4.012   2.763   1.00 36.98  ? 198 ILE B CD1 1 
ATOM   4747 N N   . TYR B 1 170 ? -1.745  2.425   6.688   1.00 44.01  ? 199 TYR B N   1 
ATOM   4748 C CA  . TYR B 1 170 ? -2.149  2.113   8.046   1.00 41.78  ? 199 TYR B CA  1 
ATOM   4749 C C   . TYR B 1 170 ? -2.128  0.604   8.261   1.00 40.97  ? 199 TYR B C   1 
ATOM   4750 O O   . TYR B 1 170 ? -1.471  0.106   9.173   1.00 40.17  ? 199 TYR B O   1 
ATOM   4751 C CB  . TYR B 1 170 ? -3.542  2.688   8.306   1.00 41.94  ? 199 TYR B CB  1 
ATOM   4752 C CG  . TYR B 1 170 ? -4.118  2.222   9.631   1.00 41.88  ? 199 TYR B CG  1 
ATOM   4753 C CD1 . TYR B 1 170 ? -4.840  1.036   9.715   1.00 40.19  ? 199 TYR B CD1 1 
ATOM   4754 C CD2 . TYR B 1 170 ? -3.903  2.943   10.800  1.00 40.78  ? 199 TYR B CD2 1 
ATOM   4755 C CE1 . TYR B 1 170 ? -5.357  0.595   10.920  1.00 40.91  ? 199 TYR B CE1 1 
ATOM   4756 C CE2 . TYR B 1 170 ? -4.417  2.511   12.010  1.00 40.51  ? 199 TYR B CE2 1 
ATOM   4757 C CZ  . TYR B 1 170 ? -5.147  1.336   12.067  1.00 40.11  ? 199 TYR B CZ  1 
ATOM   4758 O OH  . TYR B 1 170 ? -5.655  0.897   13.250  1.00 39.94  ? 199 TYR B OH  1 
ATOM   4759 N N   . GLU B 1 171 ? -2.851  -0.112  7.401   1.00 42.08  ? 200 GLU B N   1 
ATOM   4760 C CA  . GLU B 1 171 ? -2.952  -1.559  7.503   1.00 45.67  ? 200 GLU B CA  1 
ATOM   4761 C C   . GLU B 1 171 ? -1.562  -2.195  7.396   1.00 43.50  ? 200 GLU B C   1 
ATOM   4762 O O   . GLU B 1 171 ? -1.250  -3.119  8.145   1.00 46.35  ? 200 GLU B O   1 
ATOM   4763 C CB  . GLU B 1 171 ? -3.919  -2.101  6.447   1.00 46.55  ? 200 GLU B CB  1 
ATOM   4764 C CG  . GLU B 1 171 ? -5.351  -1.590  6.599   1.00 51.08  ? 200 GLU B CG  1 
ATOM   4765 C CD  . GLU B 1 171 ? -6.141  -2.084  7.802   1.00 54.26  ? 200 GLU B CD  1 
ATOM   4766 O OE1 . GLU B 1 171 ? -7.276  -1.596  7.977   1.00 55.96  ? 200 GLU B OE1 1 
ATOM   4767 O OE2 . GLU B 1 171 ? -5.654  -2.957  8.551   1.00 59.76  ? 200 GLU B OE2 1 
ATOM   4768 N N   . ASP B 1 172 ? -0.739  -1.706  6.457   1.00 42.02  ? 201 ASP B N   1 
ATOM   4769 C CA  . ASP B 1 172 ? 0.602   -2.238  6.253   1.00 41.50  ? 201 ASP B CA  1 
ATOM   4770 C C   . ASP B 1 172 ? 1.465   -1.963  7.482   1.00 38.40  ? 201 ASP B C   1 
ATOM   4771 O O   . ASP B 1 172 ? 2.291   -2.789  7.857   1.00 38.39  ? 201 ASP B O   1 
ATOM   4772 C CB  . ASP B 1 172 ? 1.249   -1.681  4.994   1.00 42.52  ? 201 ASP B CB  1 
ATOM   4773 C CG  . ASP B 1 172 ? 0.997   -2.451  3.704   1.00 41.79  ? 201 ASP B CG  1 
ATOM   4774 O OD1 . ASP B 1 172 ? 0.430   -3.562  3.776   1.00 41.79  ? 201 ASP B OD1 1 
ATOM   4775 O OD2 . ASP B 1 172 ? 1.372   -1.932  2.635   1.00 43.50  ? 201 ASP B OD2 1 
ATOM   4776 N N   . SER B 1 173 ? 1.246   -0.801  8.101   1.00 36.07  ? 202 SER B N   1 
ATOM   4777 C CA  . SER B 1 173 ? 2.008   -0.370  9.258   1.00 37.24  ? 202 SER B CA  1 
ATOM   4778 C C   . SER B 1 173 ? 1.653   -1.209  10.485  1.00 36.15  ? 202 SER B C   1 
ATOM   4779 O O   . SER B 1 173 ? 2.538   -1.648  11.212  1.00 34.98  ? 202 SER B O   1 
ATOM   4780 C CB  . SER B 1 173 ? 1.784   1.108   9.509   1.00 37.49  ? 202 SER B CB  1 
ATOM   4781 O OG  . SER B 1 173 ? 2.248   1.874   8.405   1.00 35.75  ? 202 SER B OG  1 
ATOM   4782 N N   . MET B 1 174 ? 0.352   -1.409  10.713  1.00 36.06  ? 203 MET B N   1 
ATOM   4783 C CA  . MET B 1 174 ? -0.129  -2.198  11.835  1.00 38.23  ? 203 MET B CA  1 
ATOM   4784 C C   . MET B 1 174 ? 0.386   -3.628  11.705  1.00 37.96  ? 203 MET B C   1 
ATOM   4785 O O   . MET B 1 174 ? 0.708   -4.254  12.708  1.00 38.77  ? 203 MET B O   1 
ATOM   4786 C CB  . MET B 1 174 ? -1.662  -2.218  11.886  1.00 39.43  ? 203 MET B CB  1 
ATOM   4787 C CG  . MET B 1 174 ? -2.300  -0.867  12.169  1.00 42.64  ? 203 MET B CG  1 
ATOM   4788 S SD  . MET B 1 174 ? -2.180  -0.332  13.888  1.00 47.70  ? 203 MET B SD  1 
ATOM   4789 C CE  . MET B 1 174 ? -3.231  -1.589  14.631  1.00 46.12  ? 203 MET B CE  1 
ATOM   4790 N N   . ASP B 1 175 ? 0.473   -4.130  10.466  1.00 38.39  ? 204 ASP B N   1 
ATOM   4791 C CA  . ASP B 1 175 ? 0.958   -5.480  10.215  1.00 40.66  ? 204 ASP B CA  1 
ATOM   4792 C C   . ASP B 1 175 ? 2.464   -5.577  10.476  1.00 40.36  ? 204 ASP B C   1 
ATOM   4793 O O   . ASP B 1 175 ? 2.944   -6.591  10.988  1.00 40.06  ? 204 ASP B O   1 
ATOM   4794 C CB  . ASP B 1 175 ? 0.616   -5.956  8.810   1.00 42.10  ? 204 ASP B CB  1 
ATOM   4795 C CG  . ASP B 1 175 ? -0.822  -6.403  8.556   1.00 44.96  ? 204 ASP B CG  1 
ATOM   4796 O OD1 . ASP B 1 175 ? -1.646  -6.363  9.498   1.00 43.38  ? 204 ASP B OD1 1 
ATOM   4797 O OD2 . ASP B 1 175 ? -1.106  -6.811  7.410   1.00 44.13  ? 204 ASP B OD2 1 
ATOM   4798 N N   . LEU B 1 176 ? 3.214   -4.532  10.104  1.00 38.07  ? 205 LEU B N   1 
ATOM   4799 C CA  . LEU B 1 176 ? 4.665   -4.571  10.200  1.00 34.39  ? 205 LEU B CA  1 
ATOM   4800 C C   . LEU B 1 176 ? 5.064   -4.496  11.669  1.00 32.85  ? 205 LEU B C   1 
ATOM   4801 O O   . LEU B 1 176 ? 5.899   -5.270  12.119  1.00 32.56  ? 205 LEU B O   1 
ATOM   4802 C CB  . LEU B 1 176 ? 5.310   -3.457  9.373   1.00 34.43  ? 205 LEU B CB  1 
ATOM   4803 C CG  . LEU B 1 176 ? 6.822   -3.266  9.547   1.00 32.82  ? 205 LEU B CG  1 
ATOM   4804 C CD1 . LEU B 1 176 ? 7.577   -4.562  9.337   1.00 33.13  ? 205 LEU B CD1 1 
ATOM   4805 C CD2 . LEU B 1 176 ? 7.326   -2.215  8.586   1.00 33.15  ? 205 LEU B CD2 1 
ATOM   4806 N N   . ILE B 1 177 ? 4.444   -3.567  12.404  1.00 32.97  ? 206 ILE B N   1 
ATOM   4807 C CA  . ILE B 1 177 ? 4.735   -3.378  13.816  1.00 33.34  ? 206 ILE B CA  1 
ATOM   4808 C C   . ILE B 1 177 ? 4.472   -4.676  14.573  1.00 33.17  ? 206 ILE B C   1 
ATOM   4809 O O   . ILE B 1 177 ? 5.235   -5.052  15.458  1.00 31.29  ? 206 ILE B O   1 
ATOM   4810 C CB  . ILE B 1 177 ? 3.910   -2.216  14.396  1.00 30.98  ? 206 ILE B CB  1 
ATOM   4811 C CG1 . ILE B 1 177 ? 4.339   -0.881  13.792  1.00 31.17  ? 206 ILE B CG1 1 
ATOM   4812 C CG2 . ILE B 1 177 ? 4.005   -2.210  15.923  1.00 31.02  ? 206 ILE B CG2 1 
ATOM   4813 C CD1 . ILE B 1 177 ? 3.535   0.314   14.268  1.00 32.61  ? 206 ILE B CD1 1 
ATOM   4814 N N   . ALA B 1 178 ? 3.357   -5.323  14.229  1.00 36.39  ? 207 ALA B N   1 
ATOM   4815 C CA  . ALA B 1 178 ? 2.943   -6.562  14.864  1.00 36.70  ? 207 ALA B CA  1 
ATOM   4816 C C   . ALA B 1 178 ? 4.002   -7.642  14.664  1.00 36.29  ? 207 ALA B C   1 
ATOM   4817 O O   . ALA B 1 178 ? 4.283   -8.411  15.581  1.00 40.24  ? 207 ALA B O   1 
ATOM   4818 C CB  . ALA B 1 178 ? 1.602   -6.994  14.301  1.00 36.10  ? 207 ALA B CB  1 
ATOM   4819 N N   . LYS B 1 179 ? 4.598   -7.675  13.467  1.00 36.30  ? 208 LYS B N   1 
ATOM   4820 C CA  . LYS B 1 179 ? 5.457   -8.778  13.055  1.00 35.29  ? 208 LYS B CA  1 
ATOM   4821 C C   . LYS B 1 179 ? 6.916   -8.526  13.440  1.00 35.95  ? 208 LYS B C   1 
ATOM   4822 O O   . LYS B 1 179 ? 7.745   -9.432  13.353  1.00 35.05  ? 208 LYS B O   1 
ATOM   4823 C CB  . LYS B 1 179 ? 5.381   -8.976  11.538  1.00 35.79  ? 208 LYS B CB  1 
ATOM   4824 C CG  . LYS B 1 179 ? 4.045   -9.415  10.938  1.00 36.66  ? 208 LYS B CG  1 
ATOM   4825 C CD  . LYS B 1 179 ? 4.066   -9.268  9.420   1.00 39.97  ? 208 LYS B CD  1 
ATOM   4826 C CE  . LYS B 1 179 ? 2.770   -9.492  8.717   1.00 42.79  ? 208 LYS B CE  1 
ATOM   4827 N NZ  . LYS B 1 179 ? 2.934   -9.062  7.321   1.00 44.61  ? 208 LYS B NZ  1 
ATOM   4828 N N   . LEU B 1 180 ? 7.232   -7.296  13.862  1.00 37.93  ? 209 LEU B N   1 
ATOM   4829 C CA  . LEU B 1 180 ? 8.617   -6.903  14.071  1.00 37.97  ? 209 LEU B CA  1 
ATOM   4830 C C   . LEU B 1 180 ? 9.230   -7.735  15.195  1.00 38.79  ? 209 LEU B C   1 
ATOM   4831 O O   . LEU B 1 180 ? 10.244  -8.395  14.963  1.00 38.68  ? 209 LEU B O   1 
ATOM   4832 C CB  . LEU B 1 180 ? 8.749   -5.399  14.315  1.00 36.35  ? 209 LEU B CB  1 
ATOM   4833 C CG  . LEU B 1 180 ? 8.874   -4.528  13.062  1.00 34.97  ? 209 LEU B CG  1 
ATOM   4834 C CD1 . LEU B 1 180 ? 8.710   -3.064  13.414  1.00 33.14  ? 209 LEU B CD1 1 
ATOM   4835 C CD2 . LEU B 1 180 ? 10.204  -4.766  12.368  1.00 35.94  ? 209 LEU B CD2 1 
ATOM   4836 N N   . PRO B 1 181 ? 8.675   -7.716  16.434  1.00 39.48  ? 210 PRO B N   1 
ATOM   4837 C CA  . PRO B 1 181 ? 9.126   -8.622  17.492  1.00 37.80  ? 210 PRO B CA  1 
ATOM   4838 C C   . PRO B 1 181 ? 9.410   -10.043 17.026  1.00 37.49  ? 210 PRO B C   1 
ATOM   4839 O O   . PRO B 1 181 ? 10.439  -10.601 17.373  1.00 39.31  ? 210 PRO B O   1 
ATOM   4840 C CB  . PRO B 1 181 ? 7.954   -8.546  18.473  1.00 39.17  ? 210 PRO B CB  1 
ATOM   4841 C CG  . PRO B 1 181 ? 7.554   -7.101  18.402  1.00 38.46  ? 210 PRO B CG  1 
ATOM   4842 C CD  . PRO B 1 181 ? 7.641   -6.784  16.918  1.00 39.20  ? 210 PRO B CD  1 
ATOM   4843 N N   . CYS B 1 182 ? 8.520   -10.605 16.207  1.00 39.72  ? 211 CYS B N   1 
ATOM   4844 C CA  . CYS B 1 182 ? 8.690   -11.966 15.718  1.00 40.68  ? 211 CYS B CA  1 
ATOM   4845 C C   . CYS B 1 182 ? 9.957   -12.097 14.873  1.00 38.58  ? 211 CYS B C   1 
ATOM   4846 O O   . CYS B 1 182 ? 10.711  -13.043 15.068  1.00 38.15  ? 211 CYS B O   1 
ATOM   4847 C CB  . CYS B 1 182 ? 7.473   -12.417 14.920  1.00 42.57  ? 211 CYS B CB  1 
ATOM   4848 S SG  . CYS B 1 182 ? 5.928   -12.255 15.851  1.00 50.79  ? 211 CYS B SG  1 
ATOM   4849 N N   . VAL B 1 183 ? 10.165  -11.164 13.927  1.00 36.69  ? 212 VAL B N   1 
ATOM   4850 C CA  . VAL B 1 183 ? 11.357  -11.134 13.084  1.00 35.09  ? 212 VAL B CA  1 
ATOM   4851 C C   . VAL B 1 183 ? 12.583  -10.947 13.967  1.00 32.80  ? 212 VAL B C   1 
ATOM   4852 O O   . VAL B 1 183 ? 13.589  -11.627 13.814  1.00 32.64  ? 212 VAL B O   1 
ATOM   4853 C CB  . VAL B 1 183 ? 11.338  -10.015 12.020  1.00 34.55  ? 212 VAL B CB  1 
ATOM   4854 C CG1 . VAL B 1 183 ? 12.696  -9.856  11.340  1.00 36.24  ? 212 VAL B CG1 1 
ATOM   4855 C CG2 . VAL B 1 183 ? 10.244  -10.204 10.981  1.00 31.81  ? 212 VAL B CG2 1 
ATOM   4856 N N   . ALA B 1 184 ? 12.489  -9.975  14.872  1.00 33.02  ? 213 ALA B N   1 
ATOM   4857 C CA  . ALA B 1 184 ? 13.601  -9.586  15.718  1.00 33.18  ? 213 ALA B CA  1 
ATOM   4858 C C   . ALA B 1 184 ? 13.999  -10.729 16.652  1.00 34.44  ? 213 ALA B C   1 
ATOM   4859 O O   . ALA B 1 184 ? 15.172  -10.865 16.995  1.00 33.35  ? 213 ALA B O   1 
ATOM   4860 C CB  . ALA B 1 184 ? 13.207  -8.349  16.495  1.00 33.83  ? 213 ALA B CB  1 
ATOM   4861 N N   . ALA B 1 185 ? 13.003  -11.511 17.094  1.00 36.62  ? 214 ALA B N   1 
ATOM   4862 C CA  . ALA B 1 185 ? 13.229  -12.636 17.992  1.00 37.93  ? 214 ALA B CA  1 
ATOM   4863 C C   . ALA B 1 185 ? 13.866  -13.790 17.229  1.00 35.80  ? 214 ALA B C   1 
ATOM   4864 O O   . ALA B 1 185 ? 14.788  -14.429 17.727  1.00 35.86  ? 214 ALA B O   1 
ATOM   4865 C CB  . ALA B 1 185 ? 11.931  -13.085 18.631  1.00 38.34  ? 214 ALA B CB  1 
ATOM   4866 N N   . LYS B 1 186 ? 13.347  -14.053 16.027  1.00 37.04  ? 215 LYS B N   1 
ATOM   4867 C CA  . LYS B 1 186 ? 13.826  -15.166 15.226  1.00 39.68  ? 215 LYS B CA  1 
ATOM   4868 C C   . LYS B 1 186 ? 15.320  -14.975 14.975  1.00 40.67  ? 215 LYS B C   1 
ATOM   4869 O O   . LYS B 1 186 ? 16.109  -15.896 15.186  1.00 38.29  ? 215 LYS B O   1 
ATOM   4870 C CB  . LYS B 1 186 ? 12.997  -15.282 13.942  1.00 42.32  ? 215 LYS B CB  1 
ATOM   4871 C CG  . LYS B 1 186 ? 13.052  -16.644 13.259  1.00 46.15  ? 215 LYS B CG  1 
ATOM   4872 C CD  . LYS B 1 186 ? 11.887  -17.576 13.579  1.00 49.80  ? 215 LYS B CD  1 
ATOM   4873 C CE  . LYS B 1 186 ? 12.330  -19.002 13.729  1.00 50.47  ? 215 LYS B CE  1 
ATOM   4874 N N   . ILE B 1 187 ? 15.685  -13.751 14.563  1.00 43.70  ? 216 ILE B N   1 
ATOM   4875 C CA  . ILE B 1 187 ? 17.069  -13.356 14.336  1.00 41.89  ? 216 ILE B CA  1 
ATOM   4876 C C   . ILE B 1 187 ? 17.882  -13.645 15.590  1.00 38.82  ? 216 ILE B C   1 
ATOM   4877 O O   . ILE B 1 187 ? 18.879  -14.356 15.532  1.00 38.06  ? 216 ILE B O   1 
ATOM   4878 C CB  . ILE B 1 187 ? 17.176  -11.866 13.955  1.00 38.60  ? 216 ILE B CB  1 
ATOM   4879 C CG1 . ILE B 1 187 ? 16.545  -11.567 12.589  1.00 38.35  ? 216 ILE B CG1 1 
ATOM   4880 C CG2 . ILE B 1 187 ? 18.633  -11.409 14.005  1.00 37.59  ? 216 ILE B CG2 1 
ATOM   4881 C CD1 . ILE B 1 187 ? 16.278  -10.090 12.335  1.00 39.14  ? 216 ILE B CD1 1 
ATOM   4882 N N   . TYR B 1 188 ? 17.426  -13.088 16.714  1.00 36.27  ? 217 TYR B N   1 
ATOM   4883 C CA  . TYR B 1 188 ? 18.115  -13.220 17.986  1.00 36.72  ? 217 TYR B CA  1 
ATOM   4884 C C   . TYR B 1 188 ? 18.292  -14.689 18.379  1.00 37.09  ? 217 TYR B C   1 
ATOM   4885 O O   . TYR B 1 188 ? 19.309  -15.049 18.966  1.00 34.33  ? 217 TYR B O   1 
ATOM   4886 C CB  . TYR B 1 188 ? 17.365  -12.460 19.085  1.00 34.44  ? 217 TYR B CB  1 
ATOM   4887 C CG  . TYR B 1 188 ? 18.080  -12.462 20.428  1.00 33.47  ? 217 TYR B CG  1 
ATOM   4888 C CD1 . TYR B 1 188 ? 19.120  -11.578 20.690  1.00 35.44  ? 217 TYR B CD1 1 
ATOM   4889 C CD2 . TYR B 1 188 ? 17.742  -13.372 21.424  1.00 34.37  ? 217 TYR B CD2 1 
ATOM   4890 C CE1 . TYR B 1 188 ? 19.786  -11.580 21.906  1.00 36.05  ? 217 TYR B CE1 1 
ATOM   4891 C CE2 . TYR B 1 188 ? 18.407  -13.393 22.640  1.00 34.01  ? 217 TYR B CE2 1 
ATOM   4892 C CZ  . TYR B 1 188 ? 19.427  -12.491 22.887  1.00 35.73  ? 217 TYR B CZ  1 
ATOM   4893 O OH  . TYR B 1 188 ? 20.079  -12.500 24.089  1.00 34.65  ? 217 TYR B OH  1 
ATOM   4894 N N   . ARG B 1 189 ? 17.292  -15.530 18.105  1.00 39.10  ? 218 ARG B N   1 
ATOM   4895 C CA  . ARG B 1 189 ? 17.344  -16.912 18.555  1.00 42.54  ? 218 ARG B CA  1 
ATOM   4896 C C   . ARG B 1 189 ? 18.217  -17.745 17.618  1.00 42.57  ? 218 ARG B C   1 
ATOM   4897 O O   . ARG B 1 189 ? 18.866  -18.691 18.059  1.00 41.64  ? 218 ARG B O   1 
ATOM   4898 C CB  . ARG B 1 189 ? 15.944  -17.521 18.677  1.00 47.56  ? 218 ARG B CB  1 
ATOM   4899 C CG  . ARG B 1 189 ? 15.099  -16.913 19.787  1.00 53.32  ? 218 ARG B CG  1 
ATOM   4900 C CD  . ARG B 1 189 ? 13.987  -17.852 20.227  1.00 59.05  ? 218 ARG B CD  1 
ATOM   4901 N NE  . ARG B 1 189 ? 14.465  -18.858 21.185  1.00 65.14  ? 218 ARG B NE  1 
ATOM   4902 C CZ  . ARG B 1 189 ? 13.898  -19.193 22.348  1.00 68.44  ? 218 ARG B CZ  1 
ATOM   4903 N NH1 . ARG B 1 189 ? 12.776  -18.625 22.765  1.00 68.33  ? 218 ARG B NH1 1 
ATOM   4904 N NH2 . ARG B 1 189 ? 14.464  -20.125 23.093  1.00 69.49  ? 218 ARG B NH2 1 
ATOM   4905 N N   . ASN B 1 190 ? 18.220  -17.395 16.325  1.00 43.46  ? 219 ASN B N   1 
ATOM   4906 C CA  . ASN B 1 190 ? 19.041  -18.085 15.346  1.00 43.68  ? 219 ASN B CA  1 
ATOM   4907 C C   . ASN B 1 190 ? 20.513  -17.774 15.598  1.00 45.96  ? 219 ASN B C   1 
ATOM   4908 O O   . ASN B 1 190 ? 21.357  -18.658 15.485  1.00 50.04  ? 219 ASN B O   1 
ATOM   4909 C CB  . ASN B 1 190 ? 18.622  -17.753 13.918  1.00 45.99  ? 219 ASN B CB  1 
ATOM   4910 C CG  . ASN B 1 190 ? 17.245  -18.282 13.590  1.00 49.13  ? 219 ASN B CG  1 
ATOM   4911 O OD1 . ASN B 1 190 ? 16.543  -18.783 14.474  1.00 48.06  ? 219 ASN B OD1 1 
ATOM   4912 N ND2 . ASN B 1 190 ? 16.833  -18.171 12.334  1.00 50.18  ? 219 ASN B ND2 1 
ATOM   4913 N N   . LEU B 1 191 ? 20.823  -16.522 15.948  1.00 44.42  ? 220 LEU B N   1 
ATOM   4914 C CA  . LEU B 1 191 ? 22.210  -16.110 16.088  1.00 44.98  ? 220 LEU B CA  1 
ATOM   4915 C C   . LEU B 1 191 ? 22.765  -16.540 17.444  1.00 46.47  ? 220 LEU B C   1 
ATOM   4916 O O   . LEU B 1 191 ? 23.964  -16.780 17.545  1.00 44.37  ? 220 LEU B O   1 
ATOM   4917 C CB  . LEU B 1 191 ? 22.392  -14.603 15.879  1.00 44.08  ? 220 LEU B CB  1 
ATOM   4918 C CG  . LEU B 1 191 ? 22.479  -14.114 14.428  1.00 43.59  ? 220 LEU B CG  1 
ATOM   4919 C CD1 . LEU B 1 191 ? 22.733  -12.614 14.372  1.00 42.50  ? 220 LEU B CD1 1 
ATOM   4920 C CD2 . LEU B 1 191 ? 23.556  -14.848 13.639  1.00 44.09  ? 220 LEU B CD2 1 
ATOM   4921 N N   . TYR B 1 192 ? 21.913  -16.606 18.479  1.00 47.90  ? 221 TYR B N   1 
ATOM   4922 C CA  . TYR B 1 192 ? 22.404  -16.671 19.849  1.00 51.52  ? 221 TYR B CA  1 
ATOM   4923 C C   . TYR B 1 192 ? 21.723  -17.766 20.678  1.00 55.25  ? 221 TYR B C   1 
ATOM   4924 O O   . TYR B 1 192 ? 21.985  -17.861 21.876  1.00 53.42  ? 221 TYR B O   1 
ATOM   4925 C CB  . TYR B 1 192 ? 22.198  -15.284 20.469  1.00 53.86  ? 221 TYR B CB  1 
ATOM   4926 C CG  . TYR B 1 192 ? 22.782  -14.136 19.653  1.00 59.67  ? 221 TYR B CG  1 
ATOM   4927 C CD1 . TYR B 1 192 ? 24.125  -14.113 19.292  1.00 59.06  ? 221 TYR B CD1 1 
ATOM   4928 C CD2 . TYR B 1 192 ? 21.978  -13.093 19.204  1.00 61.56  ? 221 TYR B CD2 1 
ATOM   4929 C CE1 . TYR B 1 192 ? 24.653  -13.079 18.537  1.00 61.16  ? 221 TYR B CE1 1 
ATOM   4930 C CE2 . TYR B 1 192 ? 22.494  -12.055 18.445  1.00 61.48  ? 221 TYR B CE2 1 
ATOM   4931 C CZ  . TYR B 1 192 ? 23.835  -12.047 18.108  1.00 61.65  ? 221 TYR B CZ  1 
ATOM   4932 O OH  . TYR B 1 192 ? 24.338  -11.015 17.367  1.00 60.19  ? 221 TYR B OH  1 
ATOM   4933 N N   . ARG B 1 193 ? 20.870  -18.602 20.069  1.00 60.10  ? 222 ARG B N   1 
ATOM   4934 C CA  . ARG B 1 193 ? 20.204  -19.665 20.811  1.00 64.18  ? 222 ARG B CA  1 
ATOM   4935 C C   . ARG B 1 193 ? 20.036  -20.915 19.947  1.00 66.79  ? 222 ARG B C   1 
ATOM   4936 O O   . ARG B 1 193 ? 18.997  -21.568 19.999  1.00 72.56  ? 222 ARG B O   1 
ATOM   4937 C CB  . ARG B 1 193 ? 18.850  -19.194 21.361  1.00 67.75  ? 222 ARG B CB  1 
ATOM   4938 C CG  . ARG B 1 193 ? 18.894  -18.213 22.525  1.00 72.37  ? 222 ARG B CG  1 
ATOM   4939 C CD  . ARG B 1 193 ? 17.544  -18.175 23.241  1.00 82.19  ? 222 ARG B CD  1 
ATOM   4940 N NE  . ARG B 1 193 ? 17.417  -17.145 24.282  1.00 92.42  ? 222 ARG B NE  1 
ATOM   4941 C CZ  . ARG B 1 193 ? 18.040  -17.113 25.460  1.00 94.58  ? 222 ARG B CZ  1 
ATOM   4942 N NH1 . ARG B 1 193 ? 18.885  -18.069 25.806  1.00 100.51 ? 222 ARG B NH1 1 
ATOM   4943 N NH2 . ARG B 1 193 ? 17.815  -16.109 26.293  1.00 93.17  ? 222 ARG B NH2 1 
ATOM   4944 N N   . GLU B 1 194 ? 21.061  -21.237 19.149  1.00 68.92  ? 223 GLU B N   1 
ATOM   4945 C CA  . GLU B 1 194 ? 21.136  -22.496 18.418  1.00 68.97  ? 223 GLU B CA  1 
ATOM   4946 C C   . GLU B 1 194 ? 19.873  -22.753 17.591  1.00 63.26  ? 223 GLU B C   1 
ATOM   4947 O O   . GLU B 1 194 ? 19.502  -23.908 17.374  1.00 67.90  ? 223 GLU B O   1 
ATOM   4948 C CB  . GLU B 1 194 ? 21.427  -23.641 19.393  1.00 71.14  ? 223 GLU B CB  1 
ATOM   4949 C CG  . GLU B 1 194 ? 22.798  -23.533 20.056  1.00 74.11  ? 223 GLU B CG  1 
ATOM   4950 C CD  . GLU B 1 194 ? 23.190  -24.698 20.955  1.00 79.64  ? 223 GLU B CD  1 
ATOM   4951 O OE1 . GLU B 1 194 ? 22.617  -24.836 22.059  1.00 77.63  ? 223 GLU B OE1 1 
ATOM   4952 O OE2 . GLU B 1 194 ? 24.082  -25.473 20.547  1.00 77.47  ? 223 GLU B OE2 1 
ATOM   4953 N N   . GLY B 1 195 ? 19.220  -21.682 17.118  1.00 56.23  ? 224 GLY B N   1 
ATOM   4954 C CA  . GLY B 1 195 ? 18.159  -21.801 16.127  1.00 53.02  ? 224 GLY B CA  1 
ATOM   4955 C C   . GLY B 1 195 ? 16.803  -22.199 16.708  1.00 52.07  ? 224 GLY B C   1 
ATOM   4956 O O   . GLY B 1 195 ? 15.861  -22.421 15.949  1.00 49.19  ? 224 GLY B O   1 
ATOM   4957 N N   . SER B 1 196 ? 16.681  -22.240 18.043  1.00 52.74  ? 225 SER B N   1 
ATOM   4958 C CA  . SER B 1 196 ? 15.468  -22.732 18.679  1.00 54.18  ? 225 SER B CA  1 
ATOM   4959 C C   . SER B 1 196 ? 14.274  -21.833 18.341  1.00 53.99  ? 225 SER B C   1 
ATOM   4960 O O   . SER B 1 196 ? 14.449  -20.727 17.839  1.00 52.39  ? 225 SER B O   1 
ATOM   4961 C CB  . SER B 1 196 ? 15.664  -22.876 20.166  1.00 55.87  ? 225 SER B CB  1 
ATOM   4962 O OG  . SER B 1 196 ? 16.115  -21.658 20.737  1.00 61.38  ? 225 SER B OG  1 
ATOM   4963 N N   . GLY B 1 197 ? 13.057  -22.321 18.625  1.00 54.16  ? 226 GLY B N   1 
ATOM   4964 C CA  . GLY B 1 197 ? 11.831  -21.685 18.168  1.00 53.73  ? 226 GLY B CA  1 
ATOM   4965 C C   . GLY B 1 197 ? 11.403  -20.536 19.077  1.00 54.24  ? 226 GLY B C   1 
ATOM   4966 O O   . GLY B 1 197 ? 11.770  -20.506 20.250  1.00 55.77  ? 226 GLY B O   1 
ATOM   4967 N N   . ILE B 1 198 ? 10.603  -19.614 18.517  1.00 55.38  ? 227 ILE B N   1 
ATOM   4968 C CA  . ILE B 1 198 ? 10.180  -18.397 19.200  1.00 58.36  ? 227 ILE B CA  1 
ATOM   4969 C C   . ILE B 1 198 ? 8.894   -18.640 19.991  1.00 57.33  ? 227 ILE B C   1 
ATOM   4970 O O   . ILE B 1 198 ? 8.533   -17.835 20.846  1.00 56.59  ? 227 ILE B O   1 
ATOM   4971 C CB  . ILE B 1 198 ? 10.001  -17.227 18.210  1.00 59.71  ? 227 ILE B CB  1 
ATOM   4972 C CG1 . ILE B 1 198 ? 8.953   -17.537 17.123  1.00 57.91  ? 227 ILE B CG1 1 
ATOM   4973 C CG2 . ILE B 1 198 ? 11.349  -16.819 17.609  1.00 60.74  ? 227 ILE B CG2 1 
ATOM   4974 C CD1 . ILE B 1 198 ? 8.433   -16.316 16.385  1.00 56.61  ? 227 ILE B CD1 1 
ATOM   4975 N N   . GLY B 1 199 ? 8.187   -19.727 19.675  1.00 61.49  ? 228 GLY B N   1 
ATOM   4976 C CA  . GLY B 1 199 ? 6.968   -20.083 20.382  1.00 62.89  ? 228 GLY B CA  1 
ATOM   4977 C C   . GLY B 1 199 ? 5.739   -19.447 19.737  1.00 62.65  ? 228 GLY B C   1 
ATOM   4978 O O   . GLY B 1 199 ? 5.695   -19.248 18.522  1.00 59.57  ? 228 GLY B O   1 
ATOM   4979 N N   . ALA B 1 200 ? 4.740   -19.144 20.573  1.00 61.09  ? 229 ALA B N   1 
ATOM   4980 C CA  . ALA B 1 200 ? 3.484   -18.576 20.112  1.00 61.54  ? 229 ALA B CA  1 
ATOM   4981 C C   . ALA B 1 200 ? 3.273   -17.217 20.770  1.00 55.99  ? 229 ALA B C   1 
ATOM   4982 O O   . ALA B 1 200 ? 3.806   -16.958 21.846  1.00 51.82  ? 229 ALA B O   1 
ATOM   4983 C CB  . ALA B 1 200 ? 2.345   -19.520 20.429  1.00 64.83  ? 229 ALA B CB  1 
ATOM   4984 N N   . ILE B 1 201 ? 2.496   -16.363 20.098  1.00 56.02  ? 230 ILE B N   1 
ATOM   4985 C CA  . ILE B 1 201 ? 2.049   -15.104 20.673  1.00 58.26  ? 230 ILE B CA  1 
ATOM   4986 C C   . ILE B 1 201 ? 0.940   -15.414 21.679  1.00 58.97  ? 230 ILE B C   1 
ATOM   4987 O O   . ILE B 1 201 ? 0.241   -16.416 21.547  1.00 59.41  ? 230 ILE B O   1 
ATOM   4988 C CB  . ILE B 1 201 ? 1.600   -14.124 19.569  1.00 57.03  ? 230 ILE B CB  1 
ATOM   4989 C CG1 . ILE B 1 201 ? 2.777   -13.682 18.689  1.00 58.97  ? 230 ILE B CG1 1 
ATOM   4990 C CG2 . ILE B 1 201 ? 0.861   -12.914 20.141  1.00 56.14  ? 230 ILE B CG2 1 
ATOM   4991 C CD1 . ILE B 1 201 ? 3.779   -12.774 19.384  1.00 58.91  ? 230 ILE B CD1 1 
ATOM   4992 N N   . ASP B 1 202 ? 0.820   -14.553 22.696  1.00 59.85  ? 231 ASP B N   1 
ATOM   4993 C CA  . ASP B 1 202 ? -0.236  -14.633 23.690  1.00 62.57  ? 231 ASP B CA  1 
ATOM   4994 C C   . ASP B 1 202 ? -1.093  -13.371 23.597  1.00 63.05  ? 231 ASP B C   1 
ATOM   4995 O O   . ASP B 1 202 ? -0.629  -12.274 23.898  1.00 55.58  ? 231 ASP B O   1 
ATOM   4996 C CB  . ASP B 1 202 ? 0.355   -14.841 25.077  1.00 63.66  ? 231 ASP B CB  1 
ATOM   4997 C CG  . ASP B 1 202 ? -0.634  -14.915 26.232  1.00 65.36  ? 231 ASP B CG  1 
ATOM   4998 O OD1 . ASP B 1 202 ? -1.859  -14.839 25.977  1.00 62.28  ? 231 ASP B OD1 1 
ATOM   4999 O OD2 . ASP B 1 202 ? -0.166  -15.053 27.383  1.00 66.98  ? 231 ASP B OD2 1 
ATOM   5000 N N   . SER B 1 203 ? -2.367  -13.555 23.234  1.00 69.24  ? 232 SER B N   1 
ATOM   5001 C CA  . SER B 1 203 ? -3.260  -12.462 22.881  1.00 67.45  ? 232 SER B CA  1 
ATOM   5002 C C   . SER B 1 203 ? -3.556  -11.535 24.063  1.00 63.98  ? 232 SER B C   1 
ATOM   5003 O O   . SER B 1 203 ? -4.033  -10.421 23.855  1.00 62.08  ? 232 SER B O   1 
ATOM   5004 C CB  . SER B 1 203 ? -4.538  -13.010 22.295  1.00 71.38  ? 232 SER B CB  1 
ATOM   5005 O OG  . SER B 1 203 ? -5.459  -11.964 22.015  1.00 77.47  ? 232 SER B OG  1 
ATOM   5006 N N   . ASN B 1 204 ? -3.290  -11.983 25.298  1.00 64.09  ? 233 ASN B N   1 
ATOM   5007 C CA  . ASN B 1 204 ? -3.596  -11.186 26.478  1.00 63.91  ? 233 ASN B CA  1 
ATOM   5008 C C   . ASN B 1 204 ? -2.320  -10.630 27.117  1.00 59.90  ? 233 ASN B C   1 
ATOM   5009 O O   . ASN B 1 204 ? -2.356  -10.192 28.266  1.00 55.92  ? 233 ASN B O   1 
ATOM   5010 C CB  . ASN B 1 204 ? -4.447  -11.976 27.471  1.00 68.86  ? 233 ASN B CB  1 
ATOM   5011 C CG  . ASN B 1 204 ? -5.806  -12.338 26.911  1.00 70.05  ? 233 ASN B CG  1 
ATOM   5012 O OD1 . ASN B 1 204 ? -6.550  -11.459 26.458  1.00 64.95  ? 233 ASN B OD1 1 
ATOM   5013 N ND2 . ASN B 1 204 ? -6.149  -13.620 26.924  1.00 69.72  ? 233 ASN B ND2 1 
ATOM   5014 N N   . LEU B 1 205 ? -1.201  -10.632 26.373  1.00 57.44  ? 234 LEU B N   1 
ATOM   5015 C CA  . LEU B 1 205 ? -0.003  -9.895  26.760  1.00 55.86  ? 234 LEU B CA  1 
ATOM   5016 C C   . LEU B 1 205 ? 0.115   -8.635  25.902  1.00 54.05  ? 234 LEU B C   1 
ATOM   5017 O O   . LEU B 1 205 ? -0.547  -8.506  24.874  1.00 55.74  ? 234 LEU B O   1 
ATOM   5018 C CB  . LEU B 1 205 ? 1.257   -10.746 26.602  1.00 57.24  ? 234 LEU B CB  1 
ATOM   5019 C CG  . LEU B 1 205 ? 1.379   -11.989 27.487  1.00 60.16  ? 234 LEU B CG  1 
ATOM   5020 C CD1 . LEU B 1 205 ? 2.647   -12.749 27.116  1.00 57.91  ? 234 LEU B CD1 1 
ATOM   5021 C CD2 . LEU B 1 205 ? 1.375   -11.640 28.967  1.00 62.23  ? 234 LEU B CD2 1 
ATOM   5022 N N   . ASP B 1 206 ? 0.990   -7.718  26.323  1.00 49.04  ? 235 ASP B N   1 
ATOM   5023 C CA  . ASP B 1 206 ? 1.322   -6.553  25.519  1.00 48.88  ? 235 ASP B CA  1 
ATOM   5024 C C   . ASP B 1 206 ? 2.444   -6.891  24.532  1.00 41.14  ? 235 ASP B C   1 
ATOM   5025 O O   . ASP B 1 206 ? 3.103   -7.922  24.636  1.00 40.45  ? 235 ASP B O   1 
ATOM   5026 C CB  . ASP B 1 206 ? 1.644   -5.355  26.399  1.00 51.57  ? 235 ASP B CB  1 
ATOM   5027 C CG  . ASP B 1 206 ? 2.756   -5.588  27.410  1.00 54.53  ? 235 ASP B CG  1 
ATOM   5028 O OD1 . ASP B 1 206 ? 2.613   -6.536  28.212  1.00 57.85  ? 235 ASP B OD1 1 
ATOM   5029 O OD2 . ASP B 1 206 ? 3.753   -4.827  27.386  1.00 53.92  ? 235 ASP B OD2 1 
ATOM   5030 N N   . TRP B 1 207 ? 2.636   -5.987  23.566  1.00 37.66  ? 236 TRP B N   1 
ATOM   5031 C CA  . TRP B 1 207 ? 3.650   -6.082  22.525  1.00 34.23  ? 236 TRP B CA  1 
ATOM   5032 C C   . TRP B 1 207 ? 5.032   -6.390  23.102  1.00 32.67  ? 236 TRP B C   1 
ATOM   5033 O O   . TRP B 1 207 ? 5.714   -7.307  22.644  1.00 30.35  ? 236 TRP B O   1 
ATOM   5034 C CB  . TRP B 1 207 ? 3.674   -4.746  21.774  1.00 34.53  ? 236 TRP B CB  1 
ATOM   5035 C CG  . TRP B 1 207 ? 4.357   -4.761  20.435  1.00 34.44  ? 236 TRP B CG  1 
ATOM   5036 C CD1 . TRP B 1 207 ? 4.122   -5.594  19.380  1.00 36.03  ? 236 TRP B CD1 1 
ATOM   5037 C CD2 . TRP B 1 207 ? 5.374   -3.840  20.002  1.00 35.10  ? 236 TRP B CD2 1 
ATOM   5038 N NE1 . TRP B 1 207 ? 4.926   -5.261  18.323  1.00 35.83  ? 236 TRP B NE1 1 
ATOM   5039 C CE2 . TRP B 1 207 ? 5.703   -4.189  18.675  1.00 36.38  ? 236 TRP B CE2 1 
ATOM   5040 C CE3 . TRP B 1 207 ? 6.028   -2.760  20.604  1.00 35.35  ? 236 TRP B CE3 1 
ATOM   5041 C CZ2 . TRP B 1 207 ? 6.662   -3.491  17.946  1.00 35.71  ? 236 TRP B CZ2 1 
ATOM   5042 C CZ3 . TRP B 1 207 ? 6.970   -2.070  19.876  1.00 33.83  ? 236 TRP B CZ3 1 
ATOM   5043 C CH2 . TRP B 1 207 ? 7.273   -2.428  18.567  1.00 33.63  ? 236 TRP B CH2 1 
ATOM   5044 N N   . SER B 1 208 ? 5.441   -5.583  24.089  1.00 32.11  ? 237 SER B N   1 
ATOM   5045 C CA  . SER B 1 208 ? 6.756   -5.675  24.703  1.00 33.49  ? 237 SER B CA  1 
ATOM   5046 C C   . SER B 1 208 ? 6.953   -6.998  25.438  1.00 36.10  ? 237 SER B C   1 
ATOM   5047 O O   . SER B 1 208 ? 8.063   -7.526  25.456  1.00 36.83  ? 237 SER B O   1 
ATOM   5048 C CB  . SER B 1 208 ? 6.988   -4.525  25.640  1.00 34.40  ? 237 SER B CB  1 
ATOM   5049 O OG  . SER B 1 208 ? 7.034   -3.295  24.932  1.00 39.25  ? 237 SER B OG  1 
ATOM   5050 N N   . HIS B 1 209 ? 5.897   -7.503  26.085  1.00 39.16  ? 238 HIS B N   1 
ATOM   5051 C CA  . HIS B 1 209 ? 6.000   -8.711  26.895  1.00 42.38  ? 238 HIS B CA  1 
ATOM   5052 C C   . HIS B 1 209 ? 6.138   -9.933  25.981  1.00 41.63  ? 238 HIS B C   1 
ATOM   5053 O O   . HIS B 1 209 ? 6.930   -10.835 26.251  1.00 41.13  ? 238 HIS B O   1 
ATOM   5054 C CB  . HIS B 1 209 ? 4.811   -8.795  27.860  1.00 46.12  ? 238 HIS B CB  1 
ATOM   5055 C CG  . HIS B 1 209 ? 5.001   -9.688  29.042  1.00 51.46  ? 238 HIS B CG  1 
ATOM   5056 N ND1 . HIS B 1 209 ? 4.163   -9.623  30.137  1.00 53.40  ? 238 HIS B ND1 1 
ATOM   5057 C CD2 . HIS B 1 209 ? 5.882   -10.665 29.308  1.00 53.12  ? 238 HIS B CD2 1 
ATOM   5058 C CE1 . HIS B 1 209 ? 4.541   -10.525 31.034  1.00 55.02  ? 238 HIS B CE1 1 
ATOM   5059 N NE2 . HIS B 1 209 ? 5.586   -11.167 30.553  1.00 53.46  ? 238 HIS B NE2 1 
ATOM   5060 N N   . ASN B 1 210 ? 5.367   -9.949  24.889  1.00 42.85  ? 239 ASN B N   1 
ATOM   5061 C CA  . ASN B 1 210 ? 5.486   -10.987 23.878  1.00 43.88  ? 239 ASN B CA  1 
ATOM   5062 C C   . ASN B 1 210 ? 6.904   -10.988 23.306  1.00 44.10  ? 239 ASN B C   1 
ATOM   5063 O O   . ASN B 1 210 ? 7.494   -12.047 23.100  1.00 47.36  ? 239 ASN B O   1 
ATOM   5064 C CB  . ASN B 1 210 ? 4.438   -10.830 22.779  1.00 44.73  ? 239 ASN B CB  1 
ATOM   5065 C CG  . ASN B 1 210 ? 3.133   -11.520 23.106  1.00 44.79  ? 239 ASN B CG  1 
ATOM   5066 O OD1 . ASN B 1 210 ? 3.117   -12.727 23.360  1.00 51.53  ? 239 ASN B OD1 1 
ATOM   5067 N ND2 . ASN B 1 210 ? 2.026   -10.795 23.087  1.00 44.32  ? 239 ASN B ND2 1 
ATOM   5068 N N   . PHE B 1 211 ? 7.437   -9.791  23.048  1.00 41.52  ? 240 PHE B N   1 
ATOM   5069 C CA  . PHE B 1 211 ? 8.776   -9.632  22.508  1.00 41.99  ? 240 PHE B CA  1 
ATOM   5070 C C   . PHE B 1 211 ? 9.779   -10.339 23.419  1.00 41.60  ? 240 PHE B C   1 
ATOM   5071 O O   . PHE B 1 211 ? 10.524  -11.200 22.961  1.00 36.97  ? 240 PHE B O   1 
ATOM   5072 C CB  . PHE B 1 211 ? 9.032   -8.129  22.337  1.00 41.20  ? 240 PHE B CB  1 
ATOM   5073 C CG  . PHE B 1 211 ? 10.318  -7.716  21.631  1.00 40.06  ? 240 PHE B CG  1 
ATOM   5074 C CD1 . PHE B 1 211 ? 11.112  -8.631  20.948  1.00 38.07  ? 240 PHE B CD1 1 
ATOM   5075 C CD2 . PHE B 1 211 ? 10.703  -6.381  21.614  1.00 39.00  ? 240 PHE B CD2 1 
ATOM   5076 C CE1 . PHE B 1 211 ? 12.274  -8.221  20.310  1.00 36.37  ? 240 PHE B CE1 1 
ATOM   5077 C CE2 . PHE B 1 211 ? 11.857  -5.982  20.962  1.00 39.32  ? 240 PHE B CE2 1 
ATOM   5078 C CZ  . PHE B 1 211 ? 12.636  -6.903  20.309  1.00 38.02  ? 240 PHE B CZ  1 
ATOM   5079 N N   . THR B 1 212 ? 9.789   -9.976  24.708  1.00 42.22  ? 241 THR B N   1 
ATOM   5080 C CA  . THR B 1 212 ? 10.743  -10.545 25.653  1.00 45.76  ? 241 THR B CA  1 
ATOM   5081 C C   . THR B 1 212 ? 10.482  -12.043 25.807  1.00 48.18  ? 241 THR B C   1 
ATOM   5082 O O   . THR B 1 212 ? 11.418  -12.802 26.054  1.00 51.53  ? 241 THR B O   1 
ATOM   5083 C CB  . THR B 1 212 ? 10.684  -9.844  27.012  1.00 44.37  ? 241 THR B CB  1 
ATOM   5084 O OG1 . THR B 1 212 ? 9.357   -10.050 27.485  1.00 44.35  ? 241 THR B OG1 1 
ATOM   5085 C CG2 . THR B 1 212 ? 11.027  -8.367  26.942  1.00 44.31  ? 241 THR B CG2 1 
ATOM   5086 N N   . ASN B 1 213 ? 9.210   -12.454 25.689  1.00 48.02  ? 242 ASN B N   1 
ATOM   5087 C CA  . ASN B 1 213 ? 8.851   -13.863 25.734  1.00 48.70  ? 242 ASN B CA  1 
ATOM   5088 C C   . ASN B 1 213 ? 9.511   -14.607 24.580  1.00 47.32  ? 242 ASN B C   1 
ATOM   5089 O O   . ASN B 1 213 ? 10.081  -15.674 24.785  1.00 47.65  ? 242 ASN B O   1 
ATOM   5090 C CB  . ASN B 1 213 ? 7.345   -14.104 25.691  1.00 49.69  ? 242 ASN B CB  1 
ATOM   5091 C CG  . ASN B 1 213 ? 6.707   -14.026 27.056  1.00 51.31  ? 242 ASN B CG  1 
ATOM   5092 O OD1 . ASN B 1 213 ? 7.240   -13.361 27.950  1.00 50.79  ? 242 ASN B OD1 1 
ATOM   5093 N ND2 . ASN B 1 213 ? 5.566   -14.680 27.231  1.00 51.77  ? 242 ASN B ND2 1 
ATOM   5094 N N   . MET B 1 214 ? 9.392   -14.047 23.370  1.00 48.76  ? 243 MET B N   1 
ATOM   5095 C CA  . MET B 1 214 ? 9.922   -14.670 22.168  1.00 45.50  ? 243 MET B CA  1 
ATOM   5096 C C   . MET B 1 214 ? 11.449  -14.660 22.195  1.00 43.62  ? 243 MET B C   1 
ATOM   5097 O O   . MET B 1 214 ? 12.083  -15.527 21.604  1.00 47.72  ? 243 MET B O   1 
ATOM   5098 C CB  . MET B 1 214 ? 9.411   -13.961 20.909  1.00 47.61  ? 243 MET B CB  1 
ATOM   5099 C CG  . MET B 1 214 ? 7.959   -14.263 20.597  1.00 50.15  ? 243 MET B CG  1 
ATOM   5100 S SD  . MET B 1 214 ? 7.405   -13.530 19.047  1.00 51.57  ? 243 MET B SD  1 
ATOM   5101 C CE  . MET B 1 214 ? 7.254   -11.816 19.570  1.00 50.63  ? 243 MET B CE  1 
ATOM   5102 N N   . LEU B 1 215 ? 12.039  -13.678 22.878  1.00 43.58  ? 244 LEU B N   1 
ATOM   5103 C CA  . LEU B 1 215 ? 13.488  -13.578 22.962  1.00 43.64  ? 244 LEU B CA  1 
ATOM   5104 C C   . LEU B 1 215 ? 14.026  -14.731 23.804  1.00 44.13  ? 244 LEU B C   1 
ATOM   5105 O O   . LEU B 1 215 ? 15.054  -15.315 23.459  1.00 43.95  ? 244 LEU B O   1 
ATOM   5106 C CB  . LEU B 1 215 ? 13.914  -12.215 23.511  1.00 39.83  ? 244 LEU B CB  1 
ATOM   5107 C CG  . LEU B 1 215 ? 13.808  -11.051 22.521  1.00 38.61  ? 244 LEU B CG  1 
ATOM   5108 C CD1 . LEU B 1 215 ? 13.957  -9.696  23.207  1.00 38.90  ? 244 LEU B CD1 1 
ATOM   5109 C CD2 . LEU B 1 215 ? 14.830  -11.214 21.404  1.00 36.55  ? 244 LEU B CD2 1 
ATOM   5110 N N   . GLY B 1 216 ? 13.295  -15.068 24.874  1.00 45.19  ? 245 GLY B N   1 
ATOM   5111 C CA  . GLY B 1 216 ? 13.669  -16.156 25.766  1.00 43.69  ? 245 GLY B CA  1 
ATOM   5112 C C   . GLY B 1 216 ? 13.840  -15.672 27.201  1.00 41.30  ? 245 GLY B C   1 
ATOM   5113 O O   . GLY B 1 216 ? 14.114  -16.465 28.097  1.00 43.12  ? 245 GLY B O   1 
ATOM   5114 N N   . TYR B 1 217 ? 13.674  -14.361 27.401  1.00 40.74  ? 246 TYR B N   1 
ATOM   5115 C CA  . TYR B 1 217 ? 13.789  -13.755 28.715  1.00 41.05  ? 246 TYR B CA  1 
ATOM   5116 C C   . TYR B 1 217 ? 12.469  -13.941 29.453  1.00 43.16  ? 246 TYR B C   1 
ATOM   5117 O O   . TYR B 1 217 ? 11.405  -14.005 28.833  1.00 42.64  ? 246 TYR B O   1 
ATOM   5118 C CB  . TYR B 1 217 ? 14.173  -12.276 28.586  1.00 39.36  ? 246 TYR B CB  1 
ATOM   5119 C CG  . TYR B 1 217 ? 15.563  -12.054 28.011  1.00 36.54  ? 246 TYR B CG  1 
ATOM   5120 C CD1 . TYR B 1 217 ? 15.808  -12.237 26.659  1.00 34.80  ? 246 TYR B CD1 1 
ATOM   5121 C CD2 . TYR B 1 217 ? 16.627  -11.670 28.817  1.00 37.14  ? 246 TYR B CD2 1 
ATOM   5122 C CE1 . TYR B 1 217 ? 17.070  -12.060 26.125  1.00 36.44  ? 246 TYR B CE1 1 
ATOM   5123 C CE2 . TYR B 1 217 ? 17.892  -11.474 28.293  1.00 36.62  ? 246 TYR B CE2 1 
ATOM   5124 C CZ  . TYR B 1 217 ? 18.114  -11.675 26.943  1.00 37.18  ? 246 TYR B CZ  1 
ATOM   5125 O OH  . TYR B 1 217 ? 19.350  -11.492 26.400  1.00 39.07  ? 246 TYR B OH  1 
ATOM   5126 N N   . THR B 1 218 ? 12.579  -14.040 30.783  1.00 45.34  ? 247 THR B N   1 
ATOM   5127 C CA  . THR B 1 218 ? 11.444  -14.170 31.682  1.00 45.34  ? 247 THR B CA  1 
ATOM   5128 C C   . THR B 1 218 ? 11.735  -13.350 32.932  1.00 44.71  ? 247 THR B C   1 
ATOM   5129 O O   . THR B 1 218 ? 11.695  -13.861 34.046  1.00 45.92  ? 247 THR B O   1 
ATOM   5130 C CB  . THR B 1 218 ? 11.238  -15.644 32.016  1.00 46.51  ? 247 THR B CB  1 
ATOM   5131 O OG1 . THR B 1 218 ? 12.404  -15.972 32.767  1.00 44.16  ? 247 THR B OG1 1 
ATOM   5132 C CG2 . THR B 1 218 ? 11.103  -16.507 30.774  1.00 46.65  ? 247 THR B CG2 1 
ATOM   5133 N N   . ASP B 1 219 ? 12.084  -12.082 32.723  1.00 47.16  ? 248 ASP B N   1 
ATOM   5134 C CA  . ASP B 1 219 ? 12.327  -11.167 33.823  1.00 46.84  ? 248 ASP B CA  1 
ATOM   5135 C C   . ASP B 1 219 ? 11.292  -10.052 33.724  1.00 43.82  ? 248 ASP B C   1 
ATOM   5136 O O   . ASP B 1 219 ? 11.004  -9.552  32.638  1.00 38.98  ? 248 ASP B O   1 
ATOM   5137 C CB  . ASP B 1 219 ? 13.782  -10.719 33.857  1.00 46.46  ? 248 ASP B CB  1 
ATOM   5138 C CG  . ASP B 1 219 ? 14.186  -9.965  35.111  1.00 49.95  ? 248 ASP B CG  1 
ATOM   5139 O OD1 . ASP B 1 219 ? 13.856  -8.768  35.217  1.00 58.09  ? 248 ASP B OD1 1 
ATOM   5140 O OD2 . ASP B 1 219 ? 14.789  -10.594 35.999  1.00 61.62  ? 248 ASP B OD2 1 
ATOM   5141 N N   . HIS B 1 220 ? 10.707  -9.707  34.872  1.00 42.46  ? 249 HIS B N   1 
ATOM   5142 C CA  . HIS B 1 220 ? 9.733   -8.636  34.946  1.00 40.49  ? 249 HIS B CA  1 
ATOM   5143 C C   . HIS B 1 220 ? 10.413  -7.298  34.658  1.00 39.68  ? 249 HIS B C   1 
ATOM   5144 O O   . HIS B 1 220 ? 9.950   -6.539  33.814  1.00 36.71  ? 249 HIS B O   1 
ATOM   5145 C CB  . HIS B 1 220 ? 9.042   -8.646  36.312  1.00 38.54  ? 249 HIS B CB  1 
ATOM   5146 C CG  . HIS B 1 220 ? 8.107   -7.504  36.474  1.00 37.74  ? 249 HIS B CG  1 
ATOM   5147 N ND1 . HIS B 1 220 ? 6.881   -7.468  35.846  1.00 35.95  ? 249 HIS B ND1 1 
ATOM   5148 C CD2 . HIS B 1 220 ? 8.231   -6.346  37.136  1.00 37.88  ? 249 HIS B CD2 1 
ATOM   5149 C CE1 . HIS B 1 220 ? 6.280   -6.322  36.149  1.00 38.02  ? 249 HIS B CE1 1 
ATOM   5150 N NE2 . HIS B 1 220 ? 7.079   -5.625  36.930  1.00 37.16  ? 249 HIS B NE2 1 
ATOM   5151 N N   . GLN B 1 221 ? 11.523  -7.032  35.358  1.00 42.19  ? 250 GLN B N   1 
ATOM   5152 C CA  . GLN B 1 221 ? 12.200  -5.746  35.308  1.00 45.31  ? 250 GLN B CA  1 
ATOM   5153 C C   . GLN B 1 221 ? 12.874  -5.534  33.951  1.00 43.24  ? 250 GLN B C   1 
ATOM   5154 O O   . GLN B 1 221 ? 13.153  -4.393  33.586  1.00 41.13  ? 250 GLN B O   1 
ATOM   5155 C CB  . GLN B 1 221 ? 13.214  -5.640  36.446  1.00 50.56  ? 250 GLN B CB  1 
ATOM   5156 C CG  . GLN B 1 221 ? 12.593  -5.646  37.841  1.00 59.01  ? 250 GLN B CG  1 
ATOM   5157 C CD  . GLN B 1 221 ? 11.989  -4.320  38.261  1.00 63.79  ? 250 GLN B CD  1 
ATOM   5158 O OE1 . GLN B 1 221 ? 12.456  -3.676  39.209  1.00 68.05  ? 250 GLN B OE1 1 
ATOM   5159 N NE2 . GLN B 1 221 ? 10.935  -3.897  37.576  1.00 63.01  ? 250 GLN B NE2 1 
ATOM   5160 N N   . PHE B 1 222 ? 13.151  -6.630  33.233  1.00 35.89  ? 251 PHE B N   1 
ATOM   5161 C CA  . PHE B 1 222 ? 13.659  -6.551  31.879  1.00 36.37  ? 251 PHE B CA  1 
ATOM   5162 C C   . PHE B 1 222 ? 12.552  -6.030  30.973  1.00 37.50  ? 251 PHE B C   1 
ATOM   5163 O O   . PHE B 1 222 ? 12.768  -5.158  30.135  1.00 34.33  ? 251 PHE B O   1 
ATOM   5164 C CB  . PHE B 1 222 ? 14.083  -7.921  31.341  1.00 35.97  ? 251 PHE B CB  1 
ATOM   5165 C CG  . PHE B 1 222 ? 14.617  -7.873  29.915  1.00 36.18  ? 251 PHE B CG  1 
ATOM   5166 C CD1 . PHE B 1 222 ? 15.654  -7.015  29.572  1.00 39.68  ? 251 PHE B CD1 1 
ATOM   5167 C CD2 . PHE B 1 222 ? 14.072  -8.672  28.920  1.00 37.38  ? 251 PHE B CD2 1 
ATOM   5168 C CE1 . PHE B 1 222 ? 16.148  -6.972  28.277  1.00 38.72  ? 251 PHE B CE1 1 
ATOM   5169 C CE2 . PHE B 1 222 ? 14.556  -8.613  27.624  1.00 37.92  ? 251 PHE B CE2 1 
ATOM   5170 C CZ  . PHE B 1 222 ? 15.592  -7.765  27.308  1.00 39.60  ? 251 PHE B CZ  1 
ATOM   5171 N N   . THR B 1 223 ? 11.365  -6.608  31.165  1.00 37.95  ? 252 THR B N   1 
ATOM   5172 C CA  . THR B 1 223 ? 10.197  -6.310  30.362  1.00 38.81  ? 252 THR B CA  1 
ATOM   5173 C C   . THR B 1 223 ? 9.766   -4.861  30.578  1.00 38.87  ? 252 THR B C   1 
ATOM   5174 O O   . THR B 1 223 ? 9.287   -4.208  29.649  1.00 36.75  ? 252 THR B O   1 
ATOM   5175 C CB  . THR B 1 223 ? 9.126   -7.326  30.746  1.00 39.00  ? 252 THR B CB  1 
ATOM   5176 O OG1 . THR B 1 223 ? 9.729   -8.546  30.324  1.00 40.82  ? 252 THR B OG1 1 
ATOM   5177 C CG2 . THR B 1 223 ? 7.811   -7.113  30.023  1.00 40.39  ? 252 THR B CG2 1 
ATOM   5178 N N   . GLU B 1 224 ? 9.935   -4.375  31.814  1.00 38.08  ? 253 GLU B N   1 
ATOM   5179 C CA  . GLU B 1 224 ? 9.726   -2.972  32.132  1.00 37.62  ? 253 GLU B CA  1 
ATOM   5180 C C   . GLU B 1 224 ? 10.750  -2.124  31.381  1.00 36.10  ? 253 GLU B C   1 
ATOM   5181 O O   . GLU B 1 224 ? 10.443  -1.021  30.929  1.00 33.50  ? 253 GLU B O   1 
ATOM   5182 C CB  . GLU B 1 224 ? 9.848   -2.736  33.638  1.00 38.45  ? 253 GLU B CB  1 
ATOM   5183 C CG  . GLU B 1 224 ? 8.712   -3.357  34.447  1.00 40.66  ? 253 GLU B CG  1 
ATOM   5184 C CD  . GLU B 1 224 ? 7.351   -2.738  34.165  1.00 43.48  ? 253 GLU B CD  1 
ATOM   5185 O OE1 . GLU B 1 224 ? 6.603   -3.361  33.379  1.00 41.73  ? 253 GLU B OE1 1 
ATOM   5186 O OE2 . GLU B 1 224 ? 7.032   -1.656  34.718  1.00 41.49  ? 253 GLU B OE2 1 
ATOM   5187 N N   . LEU B 1 225 ? 11.981  -2.639  31.277  1.00 34.11  ? 254 LEU B N   1 
ATOM   5188 C CA  . LEU B 1 225 ? 13.029  -1.903  30.599  1.00 35.38  ? 254 LEU B CA  1 
ATOM   5189 C C   . LEU B 1 225 ? 12.643  -1.787  29.130  1.00 34.62  ? 254 LEU B C   1 
ATOM   5190 O O   . LEU B 1 225 ? 12.545  -0.690  28.595  1.00 38.47  ? 254 LEU B O   1 
ATOM   5191 C CB  . LEU B 1 225 ? 14.399  -2.552  30.775  1.00 34.70  ? 254 LEU B CB  1 
ATOM   5192 C CG  . LEU B 1 225 ? 15.521  -1.935  29.936  1.00 35.80  ? 254 LEU B CG  1 
ATOM   5193 C CD1 . LEU B 1 225 ? 15.800  -0.507  30.366  1.00 34.93  ? 254 LEU B CD1 1 
ATOM   5194 C CD2 . LEU B 1 225 ? 16.780  -2.787  30.002  1.00 37.69  ? 254 LEU B CD2 1 
ATOM   5195 N N   . THR B 1 226 ? 12.409  -2.938  28.505  1.00 32.77  ? 255 THR B N   1 
ATOM   5196 C CA  . THR B 1 226 ? 11.974  -3.011  27.123  1.00 33.95  ? 255 THR B CA  1 
ATOM   5197 C C   . THR B 1 226 ? 10.855  -2.004  26.874  1.00 35.62  ? 255 THR B C   1 
ATOM   5198 O O   . THR B 1 226 ? 10.898  -1.252  25.905  1.00 36.07  ? 255 THR B O   1 
ATOM   5199 C CB  . THR B 1 226 ? 11.539  -4.447  26.850  1.00 32.51  ? 255 THR B CB  1 
ATOM   5200 O OG1 . THR B 1 226 ? 12.713  -5.215  27.106  1.00 32.26  ? 255 THR B OG1 1 
ATOM   5201 C CG2 . THR B 1 226 ? 11.079  -4.663  25.422  1.00 31.67  ? 255 THR B CG2 1 
ATOM   5202 N N   . ARG B 1 227 ? 9.855   -1.999  27.761  1.00 37.28  ? 256 ARG B N   1 
ATOM   5203 C CA  . ARG B 1 227 ? 8.729   -1.089  27.641  1.00 35.43  ? 256 ARG B CA  1 
ATOM   5204 C C   . ARG B 1 227 ? 9.230   0.345   27.499  1.00 34.58  ? 256 ARG B C   1 
ATOM   5205 O O   . ARG B 1 227 ? 8.875   1.034   26.543  1.00 36.09  ? 256 ARG B O   1 
ATOM   5206 C CB  . ARG B 1 227 ? 7.774   -1.256  28.827  1.00 36.53  ? 256 ARG B CB  1 
ATOM   5207 C CG  . ARG B 1 227 ? 6.825   -2.431  28.635  1.00 36.88  ? 256 ARG B CG  1 
ATOM   5208 C CD  . ARG B 1 227 ? 6.065   -2.747  29.908  1.00 36.13  ? 256 ARG B CD  1 
ATOM   5209 N NE  . ARG B 1 227 ? 5.227   -3.935  29.735  1.00 36.22  ? 256 ARG B NE  1 
ATOM   5210 C CZ  . ARG B 1 227 ? 4.988   -4.882  30.640  1.00 39.04  ? 256 ARG B CZ  1 
ATOM   5211 N NH1 . ARG B 1 227 ? 5.512   -4.822  31.852  1.00 39.86  ? 256 ARG B NH1 1 
ATOM   5212 N NH2 . ARG B 1 227 ? 4.196   -5.897  30.328  1.00 39.12  ? 256 ARG B NH2 1 
ATOM   5213 N N   . LEU B 1 228 ? 10.082  0.769   28.436  1.00 33.18  ? 257 LEU B N   1 
ATOM   5214 C CA  . LEU B 1 228 ? 10.616  2.119   28.429  1.00 32.81  ? 257 LEU B CA  1 
ATOM   5215 C C   . LEU B 1 228 ? 11.489  2.345   27.194  1.00 32.60  ? 257 LEU B C   1 
ATOM   5216 O O   . LEU B 1 228 ? 11.345  3.354   26.513  1.00 30.40  ? 257 LEU B O   1 
ATOM   5217 C CB  . LEU B 1 228 ? 11.401  2.338   29.718  1.00 33.49  ? 257 LEU B CB  1 
ATOM   5218 C CG  . LEU B 1 228 ? 12.066  3.711   29.882  1.00 34.77  ? 257 LEU B CG  1 
ATOM   5219 C CD1 . LEU B 1 228 ? 11.030  4.812   29.863  1.00 35.19  ? 257 LEU B CD1 1 
ATOM   5220 C CD2 . LEU B 1 228 ? 12.911  3.768   31.163  1.00 34.57  ? 257 LEU B CD2 1 
ATOM   5221 N N   . TYR B 1 229 ? 12.418  1.414   26.950  1.00 33.97  ? 258 TYR B N   1 
ATOM   5222 C CA  . TYR B 1 229 ? 13.364  1.501   25.852  1.00 34.99  ? 258 TYR B CA  1 
ATOM   5223 C C   . TYR B 1 229 ? 12.591  1.784   24.572  1.00 32.64  ? 258 TYR B C   1 
ATOM   5224 O O   . TYR B 1 229 ? 12.885  2.746   23.874  1.00 33.96  ? 258 TYR B O   1 
ATOM   5225 C CB  . TYR B 1 229 ? 14.177  0.204   25.754  1.00 36.48  ? 258 TYR B CB  1 
ATOM   5226 C CG  . TYR B 1 229 ? 15.167  0.129   24.598  1.00 37.66  ? 258 TYR B CG  1 
ATOM   5227 C CD1 . TYR B 1 229 ? 14.727  -0.070  23.296  1.00 39.72  ? 258 TYR B CD1 1 
ATOM   5228 C CD2 . TYR B 1 229 ? 16.538  0.219   24.809  1.00 40.73  ? 258 TYR B CD2 1 
ATOM   5229 C CE1 . TYR B 1 229 ? 15.615  -0.150  22.236  1.00 43.38  ? 258 TYR B CE1 1 
ATOM   5230 C CE2 . TYR B 1 229 ? 17.439  0.137   23.757  1.00 42.80  ? 258 TYR B CE2 1 
ATOM   5231 C CZ  . TYR B 1 229 ? 16.976  -0.050  22.465  1.00 46.63  ? 258 TYR B CZ  1 
ATOM   5232 O OH  . TYR B 1 229 ? 17.831  -0.139  21.400  1.00 48.40  ? 258 TYR B OH  1 
ATOM   5233 N N   . LEU B 1 230 ? 11.604  0.931   24.298  1.00 30.94  ? 259 LEU B N   1 
ATOM   5234 C CA  . LEU B 1 230 ? 10.817  1.007   23.084  1.00 30.11  ? 259 LEU B CA  1 
ATOM   5235 C C   . LEU B 1 230 ? 10.062  2.337   22.987  1.00 31.84  ? 259 LEU B C   1 
ATOM   5236 O O   . LEU B 1 230 ? 9.960   2.903   21.904  1.00 33.26  ? 259 LEU B O   1 
ATOM   5237 C CB  . LEU B 1 230 ? 9.880   -0.193  23.021  1.00 29.49  ? 259 LEU B CB  1 
ATOM   5238 C CG  . LEU B 1 230 ? 10.543  -1.558  22.800  1.00 30.18  ? 259 LEU B CG  1 
ATOM   5239 C CD1 . LEU B 1 230 ? 9.490   -2.640  22.635  1.00 31.07  ? 259 LEU B CD1 1 
ATOM   5240 C CD2 . LEU B 1 230 ? 11.462  -1.577  21.602  1.00 32.57  ? 259 LEU B CD2 1 
ATOM   5241 N N   . THR B 1 231 ? 9.564   2.863   24.107  1.00 31.03  ? 260 THR B N   1 
ATOM   5242 C CA  . THR B 1 231 ? 8.891   4.154   24.090  1.00 31.35  ? 260 THR B CA  1 
ATOM   5243 C C   . THR B 1 231 ? 9.874   5.263   23.712  1.00 33.15  ? 260 THR B C   1 
ATOM   5244 O O   . THR B 1 231 ? 9.638   5.981   22.744  1.00 37.71  ? 260 THR B O   1 
ATOM   5245 C CB  . THR B 1 231 ? 8.222   4.418   25.440  1.00 31.94  ? 260 THR B CB  1 
ATOM   5246 O OG1 . THR B 1 231 ? 7.150   3.487   25.525  1.00 30.61  ? 260 THR B OG1 1 
ATOM   5247 C CG2 . THR B 1 231 ? 7.616   5.807   25.559  1.00 31.48  ? 260 THR B CG2 1 
ATOM   5248 N N   . ILE B 1 232 ? 10.973  5.411   24.467  1.00 32.87  ? 261 ILE B N   1 
ATOM   5249 C CA  . ILE B 1 232 ? 11.810  6.602   24.367  1.00 33.41  ? 261 ILE B CA  1 
ATOM   5250 C C   . ILE B 1 232 ? 12.682  6.601   23.106  1.00 30.89  ? 261 ILE B C   1 
ATOM   5251 O O   . ILE B 1 232 ? 13.227  7.646   22.771  1.00 32.33  ? 261 ILE B O   1 
ATOM   5252 C CB  . ILE B 1 232 ? 12.665  6.814   25.637  1.00 34.40  ? 261 ILE B CB  1 
ATOM   5253 C CG1 . ILE B 1 232 ? 13.734  5.736   25.800  1.00 35.48  ? 261 ILE B CG1 1 
ATOM   5254 C CG2 . ILE B 1 232 ? 11.779  6.945   26.881  1.00 35.44  ? 261 ILE B CG2 1 
ATOM   5255 C CD1 . ILE B 1 232 ? 14.626  5.914   27.016  1.00 36.36  ? 261 ILE B CD1 1 
ATOM   5256 N N   . HIS B 1 233 ? 12.835  5.461   22.415  1.00 28.66  ? 262 HIS B N   1 
ATOM   5257 C CA  . HIS B 1 233 ? 13.616  5.408   21.181  1.00 29.61  ? 262 HIS B CA  1 
ATOM   5258 C C   . HIS B 1 233 ? 12.718  5.539   19.943  1.00 30.18  ? 262 HIS B C   1 
ATOM   5259 O O   . HIS B 1 233 ? 13.205  5.460   18.815  1.00 27.70  ? 262 HIS B O   1 
ATOM   5260 C CB  . HIS B 1 233 ? 14.374  4.075   21.064  1.00 31.02  ? 262 HIS B CB  1 
ATOM   5261 C CG  . HIS B 1 233 ? 15.571  3.916   21.942  1.00 32.33  ? 262 HIS B CG  1 
ATOM   5262 N ND1 . HIS B 1 233 ? 15.497  3.550   23.273  1.00 32.20  ? 262 HIS B ND1 1 
ATOM   5263 C CD2 . HIS B 1 233 ? 16.874  4.044   21.663  1.00 32.02  ? 262 HIS B CD2 1 
ATOM   5264 C CE1 . HIS B 1 233 ? 16.719  3.474   23.772  1.00 31.29  ? 262 HIS B CE1 1 
ATOM   5265 N NE2 . HIS B 1 233 ? 17.570  3.768   22.812  1.00 32.68  ? 262 HIS B NE2 1 
ATOM   5266 N N   . SER B 1 234 ? 11.407  5.743   20.155  1.00 30.20  ? 263 SER B N   1 
ATOM   5267 C CA  . SER B 1 234 ? 10.399  5.546   19.127  1.00 30.92  ? 263 SER B CA  1 
ATOM   5268 C C   . SER B 1 234 ? 10.507  6.579   18.009  1.00 32.98  ? 263 SER B C   1 
ATOM   5269 O O   . SER B 1 234 ? 10.194  6.269   16.860  1.00 31.63  ? 263 SER B O   1 
ATOM   5270 C CB  . SER B 1 234 ? 9.017   5.572   19.732  1.00 32.72  ? 263 SER B CB  1 
ATOM   5271 O OG  . SER B 1 234 ? 8.801   6.793   20.432  1.00 33.33  ? 263 SER B OG  1 
ATOM   5272 N N   . ASP B 1 235 ? 10.918  7.807   18.352  1.00 34.90  ? 264 ASP B N   1 
ATOM   5273 C CA  . ASP B 1 235 ? 10.822  8.918   17.421  1.00 37.02  ? 264 ASP B CA  1 
ATOM   5274 C C   . ASP B 1 235 ? 11.743  10.044  17.873  1.00 36.63  ? 264 ASP B C   1 
ATOM   5275 O O   . ASP B 1 235 ? 11.937  10.245  19.061  1.00 34.35  ? 264 ASP B O   1 
ATOM   5276 C CB  . ASP B 1 235 ? 9.386   9.403   17.294  1.00 40.41  ? 264 ASP B CB  1 
ATOM   5277 C CG  . ASP B 1 235 ? 9.041   10.090  15.979  1.00 42.68  ? 264 ASP B CG  1 
ATOM   5278 O OD1 . ASP B 1 235 ? 9.168   9.430   14.919  1.00 42.00  ? 264 ASP B OD1 1 
ATOM   5279 O OD2 . ASP B 1 235 ? 8.625   11.272  16.028  1.00 45.36  ? 264 ASP B OD2 1 
ATOM   5280 N N   . HIS B 1 236 ? 12.304  10.784  16.913  1.00 38.76  ? 265 HIS B N   1 
ATOM   5281 C CA  . HIS B 1 236 ? 13.221  11.860  17.246  1.00 40.20  ? 265 HIS B CA  1 
ATOM   5282 C C   . HIS B 1 236 ? 13.300  12.827  16.069  1.00 39.39  ? 265 HIS B C   1 
ATOM   5283 O O   . HIS B 1 236 ? 14.365  13.013  15.484  1.00 38.59  ? 265 HIS B O   1 
ATOM   5284 C CB  . HIS B 1 236 ? 14.571  11.272  17.669  1.00 42.50  ? 265 HIS B CB  1 
ATOM   5285 C CG  . HIS B 1 236 ? 15.343  12.125  18.614  1.00 43.52  ? 265 HIS B CG  1 
ATOM   5286 N ND1 . HIS B 1 236 ? 16.530  12.743  18.284  1.00 44.50  ? 265 HIS B ND1 1 
ATOM   5287 C CD2 . HIS B 1 236 ? 15.102  12.428  19.897  1.00 42.76  ? 265 HIS B CD2 1 
ATOM   5288 C CE1 . HIS B 1 236 ? 16.977  13.409  19.343  1.00 46.05  ? 265 HIS B CE1 1 
ATOM   5289 N NE2 . HIS B 1 236 ? 16.121  13.236  20.332  1.00 45.87  ? 265 HIS B NE2 1 
ATOM   5290 N N   . GLU B 1 237 ? 12.151  13.427  15.728  1.00 38.67  ? 266 GLU B N   1 
ATOM   5291 C CA  . GLU B 1 237 ? 12.051  14.372  14.623  1.00 39.30  ? 266 GLU B CA  1 
ATOM   5292 C C   . GLU B 1 237 ? 12.184  13.628  13.298  1.00 38.46  ? 266 GLU B C   1 
ATOM   5293 O O   . GLU B 1 237 ? 12.411  12.423  13.291  1.00 37.63  ? 266 GLU B O   1 
ATOM   5294 C CB  . GLU B 1 237 ? 13.119  15.467  14.673  1.00 40.85  ? 266 GLU B CB  1 
ATOM   5295 C CG  . GLU B 1 237 ? 12.703  16.689  15.475  1.00 45.09  ? 266 GLU B CG  1 
ATOM   5296 C CD  . GLU B 1 237 ? 13.524  17.922  15.145  1.00 47.61  ? 266 GLU B CD  1 
ATOM   5297 O OE1 . GLU B 1 237 ? 14.397  17.860  14.244  1.00 46.66  ? 266 GLU B OE1 1 
ATOM   5298 O OE2 . GLU B 1 237 ? 13.271  18.951  15.812  1.00 48.91  ? 266 GLU B OE2 1 
ATOM   5299 N N   . GLY B 1 238 ? 12.058  14.370  12.188  1.00 37.79  ? 267 GLY B N   1 
ATOM   5300 C CA  . GLY B 1 238 ? 12.158  13.807  10.853  1.00 37.78  ? 267 GLY B CA  1 
ATOM   5301 C C   . GLY B 1 238 ? 13.577  13.885  10.293  1.00 37.37  ? 267 GLY B C   1 
ATOM   5302 O O   . GLY B 1 238 ? 13.888  13.243  9.286   1.00 35.29  ? 267 GLY B O   1 
ATOM   5303 N N   . GLY B 1 239 ? 14.442  14.639  10.977  1.00 35.15  ? 268 GLY B N   1 
ATOM   5304 C CA  . GLY B 1 239 ? 15.729  15.012  10.422  1.00 33.93  ? 268 GLY B CA  1 
ATOM   5305 C C   . GLY B 1 239 ? 16.790  13.936  10.613  1.00 31.77  ? 268 GLY B C   1 
ATOM   5306 O O   . GLY B 1 239 ? 17.819  13.981  9.941   1.00 32.08  ? 268 GLY B O   1 
ATOM   5307 N N   . ASN B 1 240 ? 16.545  12.981  11.520  1.00 29.63  ? 269 ASN B N   1 
ATOM   5308 C CA  . ASN B 1 240 ? 17.523  11.938  11.788  1.00 28.01  ? 269 ASN B CA  1 
ATOM   5309 C C   . ASN B 1 240 ? 17.577  11.021  10.571  1.00 25.60  ? 269 ASN B C   1 
ATOM   5310 O O   . ASN B 1 240 ? 16.601  10.908  9.833   1.00 22.25  ? 269 ASN B O   1 
ATOM   5311 C CB  . ASN B 1 240 ? 17.288  11.219  13.117  1.00 27.76  ? 269 ASN B CB  1 
ATOM   5312 C CG  . ASN B 1 240 ? 16.078  10.313  13.138  1.00 28.41  ? 269 ASN B CG  1 
ATOM   5313 O OD1 . ASN B 1 240 ? 16.066  9.223   12.537  1.00 26.34  ? 269 ASN B OD1 1 
ATOM   5314 N ND2 . ASN B 1 240 ? 15.070  10.714  13.892  1.00 29.08  ? 269 ASN B ND2 1 
ATOM   5315 N N   . VAL B 1 241 ? 18.737  10.391  10.364  1.00 25.69  ? 270 VAL B N   1 
ATOM   5316 C CA  . VAL B 1 241 ? 18.968  9.628   9.147   1.00 26.30  ? 270 VAL B CA  1 
ATOM   5317 C C   . VAL B 1 241 ? 17.839  8.620   8.941   1.00 23.26  ? 270 VAL B C   1 
ATOM   5318 O O   . VAL B 1 241 ? 17.341  8.520   7.829   1.00 22.49  ? 270 VAL B O   1 
ATOM   5319 C CB  . VAL B 1 241 ? 20.357  8.967   9.068   1.00 27.73  ? 270 VAL B CB  1 
ATOM   5320 C CG1 . VAL B 1 241 ? 20.463  7.937   7.942   1.00 27.16  ? 270 VAL B CG1 1 
ATOM   5321 C CG2 . VAL B 1 241 ? 21.449  10.018  8.906   1.00 28.47  ? 270 VAL B CG2 1 
ATOM   5322 N N   . SER B 1 242 ? 17.409  7.910   9.994   1.00 24.15  ? 271 SER B N   1 
ATOM   5323 C CA  . SER B 1 242 ? 16.462  6.821   9.815   1.00 25.99  ? 271 SER B CA  1 
ATOM   5324 C C   . SER B 1 242 ? 15.055  7.353   9.534   1.00 25.25  ? 271 SER B C   1 
ATOM   5325 O O   . SER B 1 242 ? 14.332  6.745   8.750   1.00 22.59  ? 271 SER B O   1 
ATOM   5326 C CB  . SER B 1 242 ? 16.474  5.838   10.973  1.00 27.98  ? 271 SER B CB  1 
ATOM   5327 O OG  . SER B 1 242 ? 15.901  6.378   12.156  1.00 27.97  ? 271 SER B OG  1 
ATOM   5328 N N   . ALA B 1 243 ? 14.661  8.470   10.171  1.00 23.93  ? 272 ALA B N   1 
ATOM   5329 C CA  . ALA B 1 243 ? 13.364  9.082   9.910   1.00 22.75  ? 272 ALA B CA  1 
ATOM   5330 C C   . ALA B 1 243 ? 13.378  9.757   8.539   1.00 23.85  ? 272 ALA B C   1 
ATOM   5331 O O   . ALA B 1 243 ? 12.410  9.688   7.783   1.00 25.25  ? 272 ALA B O   1 
ATOM   5332 C CB  . ALA B 1 243 ? 12.991  10.079  11.001  1.00 22.81  ? 272 ALA B CB  1 
ATOM   5333 N N   . HIS B 1 244 ? 14.483  10.423  8.209   1.00 24.66  ? 273 HIS B N   1 
ATOM   5334 C CA  . HIS B 1 244 ? 14.560  11.098  6.929   1.00 24.21  ? 273 HIS B CA  1 
ATOM   5335 C C   . HIS B 1 244 ? 14.483  10.057  5.808   1.00 25.37  ? 273 HIS B C   1 
ATOM   5336 O O   . HIS B 1 244 ? 13.783  10.250  4.812   1.00 22.98  ? 273 HIS B O   1 
ATOM   5337 C CB  . HIS B 1 244 ? 15.783  12.010  6.895   1.00 23.85  ? 273 HIS B CB  1 
ATOM   5338 C CG  . HIS B 1 244 ? 15.817  12.872  5.679   1.00 25.33  ? 273 HIS B CG  1 
ATOM   5339 N ND1 . HIS B 1 244 ? 16.943  13.542  5.261   1.00 27.34  ? 273 HIS B ND1 1 
ATOM   5340 C CD2 . HIS B 1 244 ? 14.858  13.163  4.792   1.00 25.73  ? 273 HIS B CD2 1 
ATOM   5341 C CE1 . HIS B 1 244 ? 16.666  14.199  4.148   1.00 26.68  ? 273 HIS B CE1 1 
ATOM   5342 N NE2 . HIS B 1 244 ? 15.405  13.976  3.843   1.00 25.44  ? 273 HIS B NE2 1 
ATOM   5343 N N   . THR B 1 245 ? 15.206  8.943   5.984   1.00 26.78  ? 274 THR B N   1 
ATOM   5344 C CA  . THR B 1 245 ? 15.213  7.882   4.990   1.00 24.87  ? 274 THR B CA  1 
ATOM   5345 C C   . THR B 1 245 ? 13.794  7.357   4.789   1.00 25.15  ? 274 THR B C   1 
ATOM   5346 O O   . THR B 1 245 ? 13.359  7.296   3.644   1.00 24.95  ? 274 THR B O   1 
ATOM   5347 C CB  . THR B 1 245 ? 16.202  6.793   5.390   1.00 25.35  ? 274 THR B CB  1 
ATOM   5348 O OG1 . THR B 1 245 ? 17.436  7.503   5.501   1.00 25.96  ? 274 THR B OG1 1 
ATOM   5349 C CG2 . THR B 1 245 ? 16.299  5.682   4.359   1.00 24.64  ? 274 THR B CG2 1 
ATOM   5350 N N   . SER B 1 246 ? 13.052  7.043   5.874   1.00 25.76  ? 275 SER B N   1 
ATOM   5351 C CA  . SER B 1 246 ? 11.700  6.498   5.733   1.00 27.31  ? 275 SER B CA  1 
ATOM   5352 C C   . SER B 1 246 ? 10.804  7.481   4.996   1.00 27.06  ? 275 SER B C   1 
ATOM   5353 O O   . SER B 1 246 ? 9.962   7.090   4.188   1.00 26.23  ? 275 SER B O   1 
ATOM   5354 C CB  . SER B 1 246 ? 11.056  6.098   7.053   1.00 28.42  ? 275 SER B CB  1 
ATOM   5355 O OG  . SER B 1 246 ? 10.781  7.218   7.887   1.00 29.64  ? 275 SER B OG  1 
ATOM   5356 N N   . HIS B 1 247 ? 10.989  8.763   5.314   1.00 27.71  ? 276 HIS B N   1 
ATOM   5357 C CA  . HIS B 1 247 ? 10.217  9.836   4.723   1.00 30.53  ? 276 HIS B CA  1 
ATOM   5358 C C   . HIS B 1 247 ? 10.568  9.938   3.237   1.00 28.77  ? 276 HIS B C   1 
ATOM   5359 O O   . HIS B 1 247 ? 9.694   10.011  2.367   1.00 26.53  ? 276 HIS B O   1 
ATOM   5360 C CB  . HIS B 1 247 ? 10.502  11.123  5.504   1.00 34.92  ? 276 HIS B CB  1 
ATOM   5361 C CG  . HIS B 1 247 ? 9.618   12.268  5.158   1.00 41.99  ? 276 HIS B CG  1 
ATOM   5362 N ND1 . HIS B 1 247 ? 8.557   12.654  5.952   1.00 43.79  ? 276 HIS B ND1 1 
ATOM   5363 C CD2 . HIS B 1 247 ? 9.659   13.130  4.132   1.00 42.61  ? 276 HIS B CD2 1 
ATOM   5364 C CE1 . HIS B 1 247 ? 7.983   13.716  5.410   1.00 45.30  ? 276 HIS B CE1 1 
ATOM   5365 N NE2 . HIS B 1 247 ? 8.632   14.017  4.300   1.00 43.96  ? 276 HIS B NE2 1 
ATOM   5366 N N   . LEU B 1 248 ? 11.869  9.931   2.955   1.00 26.47  ? 277 LEU B N   1 
ATOM   5367 C CA  . LEU B 1 248 ? 12.348  10.067  1.588   1.00 26.41  ? 277 LEU B CA  1 
ATOM   5368 C C   . LEU B 1 248 ? 11.795  8.940   0.720   1.00 25.47  ? 277 LEU B C   1 
ATOM   5369 O O   . LEU B 1 248 ? 11.203  9.207   -0.322  1.00 25.81  ? 277 LEU B O   1 
ATOM   5370 C CB  . LEU B 1 248 ? 13.874  10.102  1.640   1.00 27.08  ? 277 LEU B CB  1 
ATOM   5371 C CG  . LEU B 1 248 ? 14.609  10.326  0.319   1.00 27.62  ? 277 LEU B CG  1 
ATOM   5372 C CD1 . LEU B 1 248 ? 13.996  11.440  -0.491  1.00 28.62  ? 277 LEU B CD1 1 
ATOM   5373 C CD2 . LEU B 1 248 ? 16.066  10.626  0.601   1.00 27.35  ? 277 LEU B CD2 1 
ATOM   5374 N N   . VAL B 1 249 ? 11.953  7.686   1.167   1.00 25.38  ? 278 VAL B N   1 
ATOM   5375 C CA  . VAL B 1 249 ? 11.563  6.529   0.368   1.00 26.36  ? 278 VAL B CA  1 
ATOM   5376 C C   . VAL B 1 249 ? 10.035  6.441   0.344   1.00 26.69  ? 278 VAL B C   1 
ATOM   5377 O O   . VAL B 1 249 ? 9.442   6.081   -0.669  1.00 24.19  ? 278 VAL B O   1 
ATOM   5378 C CB  . VAL B 1 249 ? 12.220  5.250   0.927   1.00 27.44  ? 278 VAL B CB  1 
ATOM   5379 C CG1 . VAL B 1 249 ? 11.727  3.980   0.246   1.00 29.06  ? 278 VAL B CG1 1 
ATOM   5380 C CG2 . VAL B 1 249 ? 13.743  5.314   0.855   1.00 27.94  ? 278 VAL B CG2 1 
ATOM   5381 N N   . GLY B 1 250 ? 9.395   6.802   1.467   1.00 26.39  ? 279 GLY B N   1 
ATOM   5382 C CA  . GLY B 1 250 ? 7.944   6.840   1.552   1.00 27.09  ? 279 GLY B CA  1 
ATOM   5383 C C   . GLY B 1 250 ? 7.332   7.808   0.541   1.00 28.45  ? 279 GLY B C   1 
ATOM   5384 O O   . GLY B 1 250 ? 6.281   7.524   -0.022  1.00 35.38  ? 279 GLY B O   1 
ATOM   5385 N N   . SER B 1 251 ? 8.010   8.933   0.302   1.00 28.66  ? 280 SER B N   1 
ATOM   5386 C CA  . SER B 1 251 ? 7.501   9.999   -0.547  1.00 30.19  ? 280 SER B CA  1 
ATOM   5387 C C   . SER B 1 251 ? 7.451   9.565   -2.010  1.00 32.78  ? 280 SER B C   1 
ATOM   5388 O O   . SER B 1 251 ? 6.734   10.174  -2.802  1.00 32.27  ? 280 SER B O   1 
ATOM   5389 C CB  . SER B 1 251 ? 8.300   11.273  -0.385  1.00 28.73  ? 280 SER B CB  1 
ATOM   5390 O OG  . SER B 1 251 ? 9.532   11.236  -1.094  1.00 28.61  ? 280 SER B OG  1 
ATOM   5391 N N   . ALA B 1 252 ? 8.193   8.502   -2.359  1.00 34.34  ? 281 ALA B N   1 
ATOM   5392 C CA  . ALA B 1 252 ? 8.111   7.912   -3.690  1.00 31.05  ? 281 ALA B CA  1 
ATOM   5393 C C   . ALA B 1 252 ? 6.946   6.931   -3.761  1.00 31.40  ? 281 ALA B C   1 
ATOM   5394 O O   . ALA B 1 252 ? 6.783   6.243   -4.766  1.00 32.83  ? 281 ALA B O   1 
ATOM   5395 C CB  . ALA B 1 252 ? 9.426   7.238   -4.037  1.00 29.61  ? 281 ALA B CB  1 
ATOM   5396 N N   . LEU B 1 253 ? 6.170   6.858   -2.670  1.00 33.36  ? 282 LEU B N   1 
ATOM   5397 C CA  . LEU B 1 253 ? 5.021   5.975   -2.535  1.00 33.63  ? 282 LEU B CA  1 
ATOM   5398 C C   . LEU B 1 253 ? 5.465   4.517   -2.459  1.00 32.71  ? 282 LEU B C   1 
ATOM   5399 O O   . LEU B 1 253 ? 4.703   3.629   -2.816  1.00 32.81  ? 282 LEU B O   1 
ATOM   5400 C CB  . LEU B 1 253 ? 3.987   6.172   -3.648  1.00 34.61  ? 282 LEU B CB  1 
ATOM   5401 C CG  . LEU B 1 253 ? 3.494   7.605   -3.872  1.00 32.37  ? 282 LEU B CG  1 
ATOM   5402 C CD1 . LEU B 1 253 ? 2.362   7.581   -4.877  1.00 33.26  ? 282 LEU B CD1 1 
ATOM   5403 C CD2 . LEU B 1 253 ? 3.048   8.288   -2.598  1.00 30.90  ? 282 LEU B CD2 1 
ATOM   5404 N N   . SER B 1 254 ? 6.683   4.266   -1.971  1.00 33.01  ? 283 SER B N   1 
ATOM   5405 C CA  . SER B 1 254 ? 7.047   2.927   -1.549  1.00 34.29  ? 283 SER B CA  1 
ATOM   5406 C C   . SER B 1 254 ? 6.271   2.575   -0.281  1.00 33.83  ? 283 SER B C   1 
ATOM   5407 O O   . SER B 1 254 ? 6.002   3.431   0.565   1.00 32.98  ? 283 SER B O   1 
ATOM   5408 C CB  . SER B 1 254 ? 8.541   2.782   -1.352  1.00 38.59  ? 283 SER B CB  1 
ATOM   5409 O OG  . SER B 1 254 ? 9.195   2.515   -2.585  1.00 37.37  ? 283 SER B OG  1 
ATOM   5410 N N   . ASP B 1 255 ? 5.911   1.293   -0.176  1.00 32.92  ? 284 ASP B N   1 
ATOM   5411 C CA  . ASP B 1 255 ? 5.081   0.788   0.903   1.00 33.96  ? 284 ASP B CA  1 
ATOM   5412 C C   . ASP B 1 255 ? 5.884   0.765   2.206   1.00 32.43  ? 284 ASP B C   1 
ATOM   5413 O O   . ASP B 1 255 ? 7.114   0.828   2.188   1.00 31.08  ? 284 ASP B O   1 
ATOM   5414 C CB  . ASP B 1 255 ? 4.538   -0.581  0.523   1.00 36.05  ? 284 ASP B CB  1 
ATOM   5415 C CG  . ASP B 1 255 ? 5.581   -1.687  0.443   1.00 37.40  ? 284 ASP B CG  1 
ATOM   5416 O OD1 . ASP B 1 255 ? 6.043   -2.131  1.524   1.00 34.59  ? 284 ASP B OD1 1 
ATOM   5417 O OD2 . ASP B 1 255 ? 5.939   -2.074  -0.696  1.00 36.29  ? 284 ASP B OD2 1 
ATOM   5418 N N   . PRO B 1 256 ? 5.219   0.672   3.380   1.00 32.83  ? 285 PRO B N   1 
ATOM   5419 C CA  . PRO B 1 256 ? 5.919   0.708   4.666   1.00 32.35  ? 285 PRO B CA  1 
ATOM   5420 C C   . PRO B 1 256 ? 7.086   -0.268  4.836   1.00 33.51  ? 285 PRO B C   1 
ATOM   5421 O O   . PRO B 1 256 ? 8.069   0.061   5.499   1.00 30.81  ? 285 PRO B O   1 
ATOM   5422 C CB  . PRO B 1 256 ? 4.766   0.419   5.657   1.00 34.29  ? 285 PRO B CB  1 
ATOM   5423 C CG  . PRO B 1 256 ? 3.555   0.994   4.971   1.00 33.57  ? 285 PRO B CG  1 
ATOM   5424 C CD  . PRO B 1 256 ? 3.754   0.560   3.530   1.00 32.94  ? 285 PRO B CD  1 
ATOM   5425 N N   . TYR B 1 257 ? 6.981   -1.466  4.238   1.00 33.93  ? 286 TYR B N   1 
ATOM   5426 C CA  . TYR B 1 257 ? 8.036   -2.462  4.356   1.00 32.93  ? 286 TYR B CA  1 
ATOM   5427 C C   . TYR B 1 257 ? 9.318   -1.908  3.729   1.00 29.55  ? 286 TYR B C   1 
ATOM   5428 O O   . TYR B 1 257 ? 10.365  -1.919  4.369   1.00 30.87  ? 286 TYR B O   1 
ATOM   5429 C CB  . TYR B 1 257 ? 7.594   -3.818  3.781   1.00 35.11  ? 286 TYR B CB  1 
ATOM   5430 C CG  . TYR B 1 257 ? 6.407   -4.442  4.505   1.00 37.93  ? 286 TYR B CG  1 
ATOM   5431 C CD1 . TYR B 1 257 ? 6.575   -5.109  5.713   1.00 37.78  ? 286 TYR B CD1 1 
ATOM   5432 C CD2 . TYR B 1 257 ? 5.115   -4.347  3.996   1.00 38.45  ? 286 TYR B CD2 1 
ATOM   5433 C CE1 . TYR B 1 257 ? 5.499   -5.654  6.393   1.00 37.37  ? 286 TYR B CE1 1 
ATOM   5434 C CE2 . TYR B 1 257 ? 4.031   -4.905  4.659   1.00 37.46  ? 286 TYR B CE2 1 
ATOM   5435 C CZ  . TYR B 1 257 ? 4.224   -5.558  5.863   1.00 37.84  ? 286 TYR B CZ  1 
ATOM   5436 O OH  . TYR B 1 257 ? 3.164   -6.106  6.532   1.00 39.04  ? 286 TYR B OH  1 
ATOM   5437 N N   . LEU B 1 258 ? 9.236   -1.403  2.491   1.00 28.27  ? 287 LEU B N   1 
ATOM   5438 C CA  . LEU B 1 258 ? 10.404  -0.876  1.795   1.00 27.77  ? 287 LEU B CA  1 
ATOM   5439 C C   . LEU B 1 258 ? 10.957  0.368   2.492   1.00 27.59  ? 287 LEU B C   1 
ATOM   5440 O O   . LEU B 1 258 ? 12.176  0.536   2.589   1.00 27.72  ? 287 LEU B O   1 
ATOM   5441 C CB  . LEU B 1 258 ? 10.074  -0.556  0.341   1.00 28.68  ? 287 LEU B CB  1 
ATOM   5442 C CG  . LEU B 1 258 ? 9.578   -1.722  -0.521  1.00 30.58  ? 287 LEU B CG  1 
ATOM   5443 C CD1 . LEU B 1 258 ? 9.524   -1.281  -1.977  1.00 30.65  ? 287 LEU B CD1 1 
ATOM   5444 C CD2 . LEU B 1 258 ? 10.427  -2.976  -0.358  1.00 30.47  ? 287 LEU B CD2 1 
ATOM   5445 N N   . SER B 1 259 ? 10.062  1.246   2.960   1.00 26.10  ? 288 SER B N   1 
ATOM   5446 C CA  . SER B 1 259 ? 10.469  2.484   3.603   1.00 25.86  ? 288 SER B CA  1 
ATOM   5447 C C   . SER B 1 259 ? 11.203  2.196   4.908   1.00 25.49  ? 288 SER B C   1 
ATOM   5448 O O   . SER B 1 259 ? 12.209  2.832   5.193   1.00 26.87  ? 288 SER B O   1 
ATOM   5449 C CB  . SER B 1 259 ? 9.288   3.392   3.847   1.00 26.08  ? 288 SER B CB  1 
ATOM   5450 O OG  . SER B 1 259 ? 8.582   3.598   2.634   1.00 30.80  ? 288 SER B OG  1 
ATOM   5451 N N   . PHE B 1 260 ? 10.650  1.280   5.716   1.00 27.34  ? 289 PHE B N   1 
ATOM   5452 C CA  . PHE B 1 260 ? 11.211  0.940   7.013   1.00 26.03  ? 289 PHE B CA  1 
ATOM   5453 C C   . PHE B 1 260 ? 12.536  0.210   6.813   1.00 26.49  ? 289 PHE B C   1 
ATOM   5454 O O   . PHE B 1 260 ? 13.490  0.443   7.543   1.00 23.39  ? 289 PHE B O   1 
ATOM   5455 C CB  . PHE B 1 260 ? 10.245  0.071   7.823   1.00 26.19  ? 289 PHE B CB  1 
ATOM   5456 C CG  . PHE B 1 260 ? 10.790  -0.268  9.200   1.00 26.18  ? 289 PHE B CG  1 
ATOM   5457 C CD1 . PHE B 1 260 ? 10.884  0.711   10.182  1.00 26.98  ? 289 PHE B CD1 1 
ATOM   5458 C CD2 . PHE B 1 260 ? 11.235  -1.548  9.498   1.00 25.56  ? 289 PHE B CD2 1 
ATOM   5459 C CE1 . PHE B 1 260 ? 11.413  0.408   11.422  1.00 26.67  ? 289 PHE B CE1 1 
ATOM   5460 C CE2 . PHE B 1 260 ? 11.770  -1.844  10.736  1.00 25.36  ? 289 PHE B CE2 1 
ATOM   5461 C CZ  . PHE B 1 260 ? 11.839  -0.871  11.701  1.00 27.07  ? 289 PHE B CZ  1 
ATOM   5462 N N   . ALA B 1 261 ? 12.574  -0.695  5.828   1.00 28.04  ? 290 ALA B N   1 
ATOM   5463 C CA  . ALA B 1 261 ? 13.789  -1.430  5.525   1.00 28.42  ? 290 ALA B CA  1 
ATOM   5464 C C   . ALA B 1 261 ? 14.910  -0.435  5.272   1.00 28.28  ? 290 ALA B C   1 
ATOM   5465 O O   . ALA B 1 261 ? 15.978  -0.532  5.877   1.00 29.89  ? 290 ALA B O   1 
ATOM   5466 C CB  . ALA B 1 261 ? 13.575  -2.337  4.327   1.00 29.06  ? 290 ALA B CB  1 
ATOM   5467 N N   . ALA B 1 262 ? 14.645  0.523   4.375   1.00 28.33  ? 291 ALA B N   1 
ATOM   5468 C CA  . ALA B 1 262 ? 15.635  1.533   4.024   1.00 27.56  ? 291 ALA B CA  1 
ATOM   5469 C C   . ALA B 1 262 ? 16.093  2.282   5.275   1.00 26.23  ? 291 ALA B C   1 
ATOM   5470 O O   . ALA B 1 262 ? 17.283  2.518   5.463   1.00 26.19  ? 291 ALA B O   1 
ATOM   5471 C CB  . ALA B 1 262 ? 15.065  2.476   2.990   1.00 26.95  ? 291 ALA B CB  1 
ATOM   5472 N N   . ALA B 1 263 ? 15.134  2.644   6.129   1.00 24.68  ? 292 ALA B N   1 
ATOM   5473 C CA  . ALA B 1 263 ? 15.422  3.364   7.359   1.00 25.88  ? 292 ALA B CA  1 
ATOM   5474 C C   . ALA B 1 263 ? 16.338  2.551   8.283   1.00 26.54  ? 292 ALA B C   1 
ATOM   5475 O O   . ALA B 1 263 ? 17.126  3.117   9.041   1.00 25.10  ? 292 ALA B O   1 
ATOM   5476 C CB  . ALA B 1 263 ? 14.113  3.712   8.037   1.00 24.55  ? 292 ALA B CB  1 
ATOM   5477 N N   . MET B 1 264 ? 16.236  1.217   8.214   1.00 26.98  ? 293 MET B N   1 
ATOM   5478 C CA  . MET B 1 264 ? 17.054  0.340   9.029   1.00 27.84  ? 293 MET B CA  1 
ATOM   5479 C C   . MET B 1 264 ? 18.486  0.342   8.511   1.00 27.26  ? 293 MET B C   1 
ATOM   5480 O O   . MET B 1 264 ? 19.424  0.379   9.307   1.00 25.10  ? 293 MET B O   1 
ATOM   5481 C CB  . MET B 1 264 ? 16.494  -1.086  9.061   1.00 29.68  ? 293 MET B CB  1 
ATOM   5482 C CG  . MET B 1 264 ? 15.227  -1.224  9.880   1.00 31.72  ? 293 MET B CG  1 
ATOM   5483 S SD  . MET B 1 264 ? 15.389  -0.517  11.530  1.00 33.22  ? 293 MET B SD  1 
ATOM   5484 C CE  . MET B 1 264 ? 14.752  1.153   11.337  1.00 36.01  ? 293 MET B CE  1 
ATOM   5485 N N   . ASN B 1 265 ? 18.635  0.341   7.182   1.00 28.38  ? 294 ASN B N   1 
ATOM   5486 C CA  . ASN B 1 265 ? 19.937  0.500   6.555   1.00 28.41  ? 294 ASN B CA  1 
ATOM   5487 C C   . ASN B 1 265 ? 20.569  1.818   6.982   1.00 29.83  ? 294 ASN B C   1 
ATOM   5488 O O   . ASN B 1 265 ? 21.783  1.883   7.157   1.00 30.05  ? 294 ASN B O   1 
ATOM   5489 C CB  . ASN B 1 265 ? 19.859  0.381   5.041   1.00 30.03  ? 294 ASN B CB  1 
ATOM   5490 C CG  . ASN B 1 265 ? 19.792  -1.061  4.603   1.00 30.97  ? 294 ASN B CG  1 
ATOM   5491 O OD1 . ASN B 1 265 ? 19.721  -1.969  5.436   1.00 30.84  ? 294 ASN B OD1 1 
ATOM   5492 N ND2 . ASN B 1 265 ? 19.817  -1.298  3.304   1.00 35.17  ? 294 ASN B ND2 1 
ATOM   5493 N N   . GLY B 1 266 ? 19.740  2.857   7.164   1.00 28.73  ? 295 GLY B N   1 
ATOM   5494 C CA  . GLY B 1 266 ? 20.227  4.118   7.701   1.00 27.31  ? 295 GLY B CA  1 
ATOM   5495 C C   . GLY B 1 266 ? 20.629  3.963   9.163   1.00 28.35  ? 295 GLY B C   1 
ATOM   5496 O O   . GLY B 1 266 ? 21.697  4.408   9.585   1.00 30.10  ? 295 GLY B O   1 
ATOM   5497 N N   . LEU B 1 267 ? 19.767  3.300   9.939   1.00 29.02  ? 296 LEU B N   1 
ATOM   5498 C CA  . LEU B 1 267 ? 20.007  3.136   11.362  1.00 30.13  ? 296 LEU B CA  1 
ATOM   5499 C C   . LEU B 1 267 ? 21.281  2.332   11.620  1.00 29.75  ? 296 LEU B C   1 
ATOM   5500 O O   . LEU B 1 267 ? 21.945  2.569   12.624  1.00 27.25  ? 296 LEU B O   1 
ATOM   5501 C CB  . LEU B 1 267 ? 18.800  2.485   12.029  1.00 30.07  ? 296 LEU B CB  1 
ATOM   5502 C CG  . LEU B 1 267 ? 18.768  2.580   13.554  1.00 30.37  ? 296 LEU B CG  1 
ATOM   5503 C CD1 . LEU B 1 267 ? 18.553  4.012   14.010  1.00 31.32  ? 296 LEU B CD1 1 
ATOM   5504 C CD2 . LEU B 1 267 ? 17.706  1.668   14.108  1.00 31.96  ? 296 LEU B CD2 1 
ATOM   5505 N N   . ALA B 1 268 ? 21.602  1.393   10.711  1.00 29.36  ? 297 ALA B N   1 
ATOM   5506 C CA  . ALA B 1 268 ? 22.747  0.497   10.833  1.00 29.11  ? 297 ALA B CA  1 
ATOM   5507 C C   . ALA B 1 268 ? 24.076  1.251   10.780  1.00 30.61  ? 297 ALA B C   1 
ATOM   5508 O O   . ALA B 1 268 ? 25.115  0.697   11.125  1.00 32.66  ? 297 ALA B O   1 
ATOM   5509 C CB  . ALA B 1 268 ? 22.696  -0.564  9.739   1.00 27.52  ? 297 ALA B CB  1 
ATOM   5510 N N   . GLY B 1 269 ? 24.067  2.495   10.295  1.00 32.80  ? 298 GLY B N   1 
ATOM   5511 C CA  . GLY B 1 269 ? 25.295  3.257   10.174  1.00 30.43  ? 298 GLY B CA  1 
ATOM   5512 C C   . GLY B 1 269 ? 25.901  3.586   11.537  1.00 30.39  ? 298 GLY B C   1 
ATOM   5513 O O   . GLY B 1 269 ? 25.188  3.984   12.459  1.00 31.82  ? 298 GLY B O   1 
ATOM   5514 N N   . PRO B 1 270 ? 27.241  3.478   11.685  1.00 29.26  ? 299 PRO B N   1 
ATOM   5515 C CA  . PRO B 1 270 ? 27.932  3.908   12.905  1.00 30.73  ? 299 PRO B CA  1 
ATOM   5516 C C   . PRO B 1 270 ? 27.542  5.243   13.543  1.00 31.18  ? 299 PRO B C   1 
ATOM   5517 O O   . PRO B 1 270 ? 27.513  5.359   14.762  1.00 36.45  ? 299 PRO B O   1 
ATOM   5518 C CB  . PRO B 1 270 ? 29.386  3.911   12.403  1.00 30.81  ? 299 PRO B CB  1 
ATOM   5519 C CG  . PRO B 1 270 ? 29.454  2.714   11.471  1.00 29.63  ? 299 PRO B CG  1 
ATOM   5520 C CD  . PRO B 1 270 ? 28.152  2.861   10.703  1.00 29.17  ? 299 PRO B CD  1 
ATOM   5521 N N   . LEU B 1 271 ? 27.266  6.259   12.728  1.00 31.39  ? 300 LEU B N   1 
ATOM   5522 C CA  . LEU B 1 271 ? 26.955  7.585   13.245  1.00 33.25  ? 300 LEU B CA  1 
ATOM   5523 C C   . LEU B 1 271 ? 25.474  7.719   13.593  1.00 35.24  ? 300 LEU B C   1 
ATOM   5524 O O   . LEU B 1 271 ? 25.049  8.791   14.008  1.00 40.16  ? 300 LEU B O   1 
ATOM   5525 C CB  . LEU B 1 271 ? 27.358  8.651   12.229  1.00 32.89  ? 300 LEU B CB  1 
ATOM   5526 C CG  . LEU B 1 271 ? 28.843  8.701   11.875  1.00 31.87  ? 300 LEU B CG  1 
ATOM   5527 C CD1 . LEU B 1 271 ? 29.072  9.882   10.961  1.00 32.21  ? 300 LEU B CD1 1 
ATOM   5528 C CD2 . LEU B 1 271 ? 29.721  8.770   13.124  1.00 32.18  ? 300 LEU B CD2 1 
ATOM   5529 N N   . HIS B 1 272 ? 24.697  6.648   13.406  1.00 37.86  ? 301 HIS B N   1 
ATOM   5530 C CA  . HIS B 1 272 ? 23.303  6.632   13.805  1.00 38.91  ? 301 HIS B CA  1 
ATOM   5531 C C   . HIS B 1 272 ? 23.135  5.585   14.907  1.00 41.71  ? 301 HIS B C   1 
ATOM   5532 O O   . HIS B 1 272 ? 23.577  5.802   16.032  1.00 42.17  ? 301 HIS B O   1 
ATOM   5533 C CB  . HIS B 1 272 ? 22.425  6.498   12.553  1.00 37.78  ? 301 HIS B CB  1 
ATOM   5534 C CG  . HIS B 1 272 ? 21.019  6.963   12.741  1.00 35.89  ? 301 HIS B CG  1 
ATOM   5535 N ND1 . HIS B 1 272 ? 20.674  7.887   13.704  1.00 35.00  ? 301 HIS B ND1 1 
ATOM   5536 C CD2 . HIS B 1 272 ? 19.881  6.669   12.086  1.00 34.78  ? 301 HIS B CD2 1 
ATOM   5537 C CE1 . HIS B 1 272 ? 19.366  8.123   13.630  1.00 34.51  ? 301 HIS B CE1 1 
ATOM   5538 N NE2 . HIS B 1 272 ? 18.866  7.393   12.656  1.00 31.95  ? 301 HIS B NE2 1 
ATOM   5539 N N   . GLY B 1 273 ? 22.563  4.423   14.568  1.00 48.02  ? 302 GLY B N   1 
ATOM   5540 C CA  . GLY B 1 273 ? 22.053  3.490   15.563  1.00 50.47  ? 302 GLY B CA  1 
ATOM   5541 C C   . GLY B 1 273 ? 23.140  2.623   16.193  1.00 50.64  ? 302 GLY B C   1 
ATOM   5542 O O   . GLY B 1 273 ? 22.927  2.080   17.274  1.00 50.41  ? 302 GLY B O   1 
ATOM   5543 N N   . LEU B 1 274 ? 24.299  2.521   15.526  1.00 52.61  ? 303 LEU B N   1 
ATOM   5544 C CA  . LEU B 1 274 ? 25.392  1.663   15.967  1.00 53.71  ? 303 LEU B CA  1 
ATOM   5545 C C   . LEU B 1 274 ? 26.212  2.292   17.095  1.00 55.56  ? 303 LEU B C   1 
ATOM   5546 O O   . LEU B 1 274 ? 27.173  1.676   17.551  1.00 57.40  ? 303 LEU B O   1 
ATOM   5547 C CB  . LEU B 1 274 ? 26.299  1.311   14.786  1.00 53.81  ? 303 LEU B CB  1 
ATOM   5548 C CG  . LEU B 1 274 ? 26.366  -0.170  14.402  1.00 55.10  ? 303 LEU B CG  1 
ATOM   5549 C CD1 . LEU B 1 274 ? 25.023  -0.731  13.948  1.00 54.15  ? 303 LEU B CD1 1 
ATOM   5550 C CD2 . LEU B 1 274 ? 27.435  -0.362  13.338  1.00 54.35  ? 303 LEU B CD2 1 
ATOM   5551 N N   . ALA B 1 275 ? 25.853  3.503   17.545  1.00 56.24  ? 304 ALA B N   1 
ATOM   5552 C CA  . ALA B 1 275 ? 26.549  4.146   18.652  1.00 55.64  ? 304 ALA B CA  1 
ATOM   5553 C C   . ALA B 1 275 ? 26.300  3.404   19.967  1.00 58.33  ? 304 ALA B C   1 
ATOM   5554 O O   . ALA B 1 275 ? 27.092  3.521   20.901  1.00 53.58  ? 304 ALA B O   1 
ATOM   5555 C CB  . ALA B 1 275 ? 26.130  5.596   18.753  1.00 54.54  ? 304 ALA B CB  1 
ATOM   5556 N N   . ASN B 1 276 ? 25.188  2.657   20.037  1.00 64.97  ? 305 ASN B N   1 
ATOM   5557 C CA  . ASN B 1 276 ? 24.813  1.908   21.226  1.00 68.15  ? 305 ASN B CA  1 
ATOM   5558 C C   . ASN B 1 276 ? 25.895  0.875   21.555  1.00 65.60  ? 305 ASN B C   1 
ATOM   5559 O O   . ASN B 1 276 ? 26.267  0.703   22.715  1.00 61.27  ? 305 ASN B O   1 
ATOM   5560 C CB  . ASN B 1 276 ? 23.424  1.299   21.045  1.00 75.09  ? 305 ASN B CB  1 
ATOM   5561 C CG  . ASN B 1 276 ? 22.839  0.760   22.330  1.00 82.39  ? 305 ASN B CG  1 
ATOM   5562 O OD1 . ASN B 1 276 ? 23.473  0.832   23.390  1.00 87.23  ? 305 ASN B OD1 1 
ATOM   5563 N ND2 . ASN B 1 276 ? 21.625  0.230   22.261  1.00 85.22  ? 305 ASN B ND2 1 
ATOM   5564 N N   . GLN B 1 277 ? 26.414  0.200   20.523  1.00 65.38  ? 306 GLN B N   1 
ATOM   5565 C CA  . GLN B 1 277 ? 27.475  -0.778  20.700  1.00 66.94  ? 306 GLN B CA  1 
ATOM   5566 C C   . GLN B 1 277 ? 28.767  -0.058  21.069  1.00 68.42  ? 306 GLN B C   1 
ATOM   5567 O O   . GLN B 1 277 ? 29.335  -0.307  22.132  1.00 70.21  ? 306 GLN B O   1 
ATOM   5568 C CB  . GLN B 1 277 ? 27.685  -1.616  19.440  1.00 68.72  ? 306 GLN B CB  1 
ATOM   5569 C CG  . GLN B 1 277 ? 26.489  -2.493  19.087  1.00 72.39  ? 306 GLN B CG  1 
ATOM   5570 C CD  . GLN B 1 277 ? 25.414  -1.769  18.304  1.00 74.47  ? 306 GLN B CD  1 
ATOM   5571 O OE1 . GLN B 1 277 ? 24.995  -0.658  18.657  1.00 71.42  ? 306 GLN B OE1 1 
ATOM   5572 N NE2 . GLN B 1 277 ? 24.958  -2.392  17.225  1.00 73.97  ? 306 GLN B NE2 1 
ATOM   5573 N N   . GLU B 1 278 ? 29.182  0.860   20.185  1.00 65.15  ? 307 GLU B N   1 
ATOM   5574 C CA  . GLU B 1 278 ? 30.429  1.600   20.311  1.00 64.68  ? 307 GLU B CA  1 
ATOM   5575 C C   . GLU B 1 278 ? 30.699  1.940   21.769  1.00 61.80  ? 307 GLU B C   1 
ATOM   5576 O O   . GLU B 1 278 ? 31.817  1.767   22.254  1.00 64.87  ? 307 GLU B O   1 
ATOM   5577 C CB  . GLU B 1 278 ? 30.380  2.904   19.513  1.00 69.46  ? 307 GLU B CB  1 
ATOM   5578 C CG  . GLU B 1 278 ? 30.423  2.697   18.002  1.00 73.63  ? 307 GLU B CG  1 
ATOM   5579 C CD  . GLU B 1 278 ? 29.986  3.916   17.206  1.00 82.05  ? 307 GLU B CD  1 
ATOM   5580 O OE1 . GLU B 1 278 ? 30.595  4.997   17.376  1.00 85.78  ? 307 GLU B OE1 1 
ATOM   5581 O OE2 . GLU B 1 278 ? 29.025  3.779   16.416  1.00 83.54  ? 307 GLU B OE2 1 
ATOM   5582 N N   . VAL B 1 279 ? 29.657  2.423   22.452  1.00 57.05  ? 308 VAL B N   1 
ATOM   5583 C CA  . VAL B 1 279 ? 29.792  2.854   23.830  1.00 54.85  ? 308 VAL B CA  1 
ATOM   5584 C C   . VAL B 1 279 ? 30.268  1.675   24.672  1.00 54.79  ? 308 VAL B C   1 
ATOM   5585 O O   . VAL B 1 279 ? 31.226  1.821   25.423  1.00 53.78  ? 308 VAL B O   1 
ATOM   5586 C CB  . VAL B 1 279 ? 28.489  3.478   24.369  1.00 51.07  ? 308 VAL B CB  1 
ATOM   5587 C CG1 . VAL B 1 279 ? 28.562  3.780   25.861  1.00 49.37  ? 308 VAL B CG1 1 
ATOM   5588 C CG2 . VAL B 1 279 ? 28.130  4.740   23.596  1.00 51.20  ? 308 VAL B CG2 1 
ATOM   5589 N N   . LEU B 1 280 ? 29.625  0.511   24.511  1.00 59.72  ? 309 LEU B N   1 
ATOM   5590 C CA  . LEU B 1 280 ? 29.830  -0.607  25.419  1.00 63.33  ? 309 LEU B CA  1 
ATOM   5591 C C   . LEU B 1 280 ? 31.193  -1.257  25.175  1.00 64.06  ? 309 LEU B C   1 
ATOM   5592 O O   . LEU B 1 280 ? 31.800  -1.782  26.106  1.00 60.94  ? 309 LEU B O   1 
ATOM   5593 C CB  . LEU B 1 280 ? 28.687  -1.613  25.291  1.00 65.48  ? 309 LEU B CB  1 
ATOM   5594 C CG  . LEU B 1 280 ? 28.499  -2.549  26.490  1.00 66.22  ? 309 LEU B CG  1 
ATOM   5595 C CD1 . LEU B 1 280 ? 28.206  -1.774  27.763  1.00 66.82  ? 309 LEU B CD1 1 
ATOM   5596 C CD2 . LEU B 1 280 ? 27.397  -3.547  26.222  1.00 66.88  ? 309 LEU B CD2 1 
ATOM   5597 N N   . VAL B 1 281 ? 31.665  -1.214  23.923  1.00 68.38  ? 310 VAL B N   1 
ATOM   5598 C CA  . VAL B 1 281 ? 33.020  -1.624  23.587  1.00 71.63  ? 310 VAL B CA  1 
ATOM   5599 C C   . VAL B 1 281 ? 34.005  -0.754  24.363  1.00 75.46  ? 310 VAL B C   1 
ATOM   5600 O O   . VAL B 1 281 ? 34.879  -1.266  25.062  1.00 76.34  ? 310 VAL B O   1 
ATOM   5601 C CB  . VAL B 1 281 ? 33.283  -1.514  22.073  1.00 73.03  ? 310 VAL B CB  1 
ATOM   5602 C CG1 . VAL B 1 281 ? 34.753  -1.732  21.730  1.00 73.40  ? 310 VAL B CG1 1 
ATOM   5603 C CG2 . VAL B 1 281 ? 32.395  -2.458  21.269  1.00 72.41  ? 310 VAL B CG2 1 
ATOM   5604 N N   . TRP B 1 282 ? 33.838  0.566   24.211  1.00 78.04  ? 311 TRP B N   1 
ATOM   5605 C CA  . TRP B 1 282 ? 34.724  1.561   24.791  1.00 77.61  ? 311 TRP B CA  1 
ATOM   5606 C C   . TRP B 1 282 ? 34.651  1.536   26.317  1.00 78.71  ? 311 TRP B C   1 
ATOM   5607 O O   . TRP B 1 282 ? 35.625  1.873   26.984  1.00 83.11  ? 311 TRP B O   1 
ATOM   5608 C CB  . TRP B 1 282 ? 34.370  2.945   24.230  1.00 79.71  ? 311 TRP B CB  1 
ATOM   5609 C CG  . TRP B 1 282 ? 35.187  4.078   24.789  1.00 83.56  ? 311 TRP B CG  1 
ATOM   5610 C CD1 . TRP B 1 282 ? 36.387  4.536   24.330  1.00 84.71  ? 311 TRP B CD1 1 
ATOM   5611 C CD2 . TRP B 1 282 ? 34.839  4.915   25.915  1.00 86.75  ? 311 TRP B CD2 1 
ATOM   5612 N NE1 . TRP B 1 282 ? 36.815  5.589   25.094  1.00 89.01  ? 311 TRP B NE1 1 
ATOM   5613 C CE2 . TRP B 1 282 ? 35.888  5.848   26.070  1.00 86.70  ? 311 TRP B CE2 1 
ATOM   5614 C CE3 . TRP B 1 282 ? 33.754  4.965   26.798  1.00 90.19  ? 311 TRP B CE3 1 
ATOM   5615 C CZ2 . TRP B 1 282 ? 35.876  6.815   27.074  1.00 85.98  ? 311 TRP B CZ2 1 
ATOM   5616 C CZ3 . TRP B 1 282 ? 33.745  5.924   27.789  1.00 90.72  ? 311 TRP B CZ3 1 
ATOM   5617 C CH2 . TRP B 1 282 ? 34.792  6.836   27.922  1.00 88.55  ? 311 TRP B CH2 1 
ATOM   5618 N N   . LEU B 1 283 ? 33.493  1.146   26.865  1.00 81.51  ? 312 LEU B N   1 
ATOM   5619 C CA  . LEU B 1 283 ? 33.326  1.024   28.306  1.00 82.43  ? 312 LEU B CA  1 
ATOM   5620 C C   . LEU B 1 283 ? 34.109  -0.182  28.815  1.00 85.80  ? 312 LEU B C   1 
ATOM   5621 O O   . LEU B 1 283 ? 34.787  -0.090  29.834  1.00 87.41  ? 312 LEU B O   1 
ATOM   5622 C CB  . LEU B 1 283 ? 31.851  0.910   28.684  1.00 79.36  ? 312 LEU B CB  1 
ATOM   5623 C CG  . LEU B 1 283 ? 31.050  2.214   28.674  1.00 79.55  ? 312 LEU B CG  1 
ATOM   5624 C CD1 . LEU B 1 283 ? 29.562  1.907   28.773  1.00 79.01  ? 312 LEU B CD1 1 
ATOM   5625 C CD2 . LEU B 1 283 ? 31.488  3.139   29.800  1.00 76.22  ? 312 LEU B CD2 1 
ATOM   5626 N N   . THR B 1 284 ? 33.994  -1.311  28.106  1.00 89.88  ? 313 THR B N   1 
ATOM   5627 C CA  . THR B 1 284 ? 34.607  -2.555  28.541  1.00 95.43  ? 313 THR B CA  1 
ATOM   5628 C C   . THR B 1 284 ? 36.123  -2.479  28.355  1.00 99.53  ? 313 THR B C   1 
ATOM   5629 O O   . THR B 1 284 ? 36.869  -2.868  29.251  1.00 97.11  ? 313 THR B O   1 
ATOM   5630 C CB  . THR B 1 284 ? 33.978  -3.726  27.787  1.00 93.90  ? 313 THR B CB  1 
ATOM   5631 O OG1 . THR B 1 284 ? 32.602  -3.684  28.150  1.00 90.02  ? 313 THR B OG1 1 
ATOM   5632 C CG2 . THR B 1 284 ? 34.559  -5.069  28.191  1.00 95.49  ? 313 THR B CG2 1 
ATOM   5633 N N   . GLN B 1 285 ? 36.569  -1.959  27.202  1.00 100.73 ? 314 GLN B N   1 
ATOM   5634 C CA  . GLN B 1 285 ? 37.991  -1.827  26.919  1.00 99.56  ? 314 GLN B CA  1 
ATOM   5635 C C   . GLN B 1 285 ? 38.619  -0.823  27.885  1.00 107.75 ? 314 GLN B C   1 
ATOM   5636 O O   . GLN B 1 285 ? 39.809  -0.915  28.172  1.00 114.41 ? 314 GLN B O   1 
ATOM   5637 C CB  . GLN B 1 285 ? 38.261  -1.446  25.461  1.00 96.03  ? 314 GLN B CB  1 
ATOM   5638 C CG  . GLN B 1 285 ? 38.139  0.046   25.156  1.00 92.54  ? 314 GLN B CG  1 
ATOM   5639 C CD  . GLN B 1 285 ? 38.343  0.406   23.697  1.00 86.42  ? 314 GLN B CD  1 
ATOM   5640 O OE1 . GLN B 1 285 ? 38.335  1.586   23.328  1.00 82.44  ? 314 GLN B OE1 1 
ATOM   5641 N NE2 . GLN B 1 285 ? 38.531  -0.592  22.844  1.00 83.55  ? 314 GLN B NE2 1 
ATOM   5642 N N   . LEU B 1 286 ? 37.819  0.140   28.367  1.00 113.04 ? 315 LEU B N   1 
ATOM   5643 C CA  . LEU B 1 286 ? 38.223  1.007   29.465  1.00 118.08 ? 315 LEU B CA  1 
ATOM   5644 C C   . LEU B 1 286 ? 38.461  0.148   30.704  1.00 121.91 ? 315 LEU B C   1 
ATOM   5645 O O   . LEU B 1 286 ? 39.506  0.264   31.338  1.00 128.27 ? 315 LEU B O   1 
ATOM   5646 C CB  . LEU B 1 286 ? 37.186  2.108   29.708  1.00 120.19 ? 315 LEU B CB  1 
ATOM   5647 C CG  . LEU B 1 286 ? 37.174  2.791   31.083  1.00 121.87 ? 315 LEU B CG  1 
ATOM   5648 C CD1 . LEU B 1 286 ? 38.506  3.367   31.534  1.00 121.40 ? 315 LEU B CD1 1 
ATOM   5649 C CD2 . LEU B 1 286 ? 36.135  3.900   31.053  1.00 124.21 ? 315 LEU B CD2 1 
ATOM   5650 N N   . GLN B 1 287 ? 37.509  -0.746  31.008  1.00 123.05 ? 316 GLN B N   1 
ATOM   5651 C CA  . GLN B 1 287 ? 37.619  -1.630  32.158  1.00 122.27 ? 316 GLN B CA  1 
ATOM   5652 C C   . GLN B 1 287 ? 38.651  -2.733  31.902  1.00 123.42 ? 316 GLN B C   1 
ATOM   5653 O O   . GLN B 1 287 ? 38.777  -3.653  32.709  1.00 119.42 ? 316 GLN B O   1 
ATOM   5654 C CB  . GLN B 1 287 ? 36.263  -2.229  32.540  1.00 118.35 ? 316 GLN B CB  1 
ATOM   5655 C CG  . GLN B 1 287 ? 35.192  -1.190  32.854  1.00 116.53 ? 316 GLN B CG  1 
ATOM   5656 C CD  . GLN B 1 287 ? 34.179  -1.660  33.875  1.00 113.56 ? 316 GLN B CD  1 
ATOM   5657 O OE1 . GLN B 1 287 ? 33.928  -0.993  34.885  1.00 110.84 ? 316 GLN B OE1 1 
ATOM   5658 N NE2 . GLN B 1 287 ? 33.585  -2.816  33.621  1.00 111.12 ? 316 GLN B NE2 1 
ATOM   5659 N N   . LYS B 1 288 ? 39.381  -2.630  30.780  1.00 123.29 ? 317 LYS B N   1 
ATOM   5660 C CA  . LYS B 1 288 ? 40.477  -3.530  30.450  1.00 120.04 ? 317 LYS B CA  1 
ATOM   5661 C C   . LYS B 1 288 ? 41.816  -2.823  30.664  1.00 116.58 ? 317 LYS B C   1 
ATOM   5662 O O   . LYS B 1 288 ? 42.749  -3.418  31.197  1.00 116.24 ? 317 LYS B O   1 
ATOM   5663 C CB  . LYS B 1 288 ? 40.350  -4.015  29.001  1.00 113.67 ? 317 LYS B CB  1 
ATOM   5664 N N   . GLU B 1 289 ? 41.909  -1.562  30.222  1.00 112.79 ? 318 GLU B N   1 
ATOM   5665 C CA  . GLU B 1 289 ? 43.094  -0.752  30.453  1.00 109.26 ? 318 GLU B CA  1 
ATOM   5666 C C   . GLU B 1 289 ? 43.265  -0.533  31.953  1.00 110.55 ? 318 GLU B C   1 
ATOM   5667 O O   . GLU B 1 289 ? 44.322  -0.827  32.507  1.00 112.51 ? 318 GLU B O   1 
ATOM   5668 C CB  . GLU B 1 289 ? 43.020  0.581   29.709  1.00 110.23 ? 318 GLU B CB  1 
ATOM   5669 C CG  . GLU B 1 289 ? 43.030  0.416   28.191  1.00 111.96 ? 318 GLU B CG  1 
ATOM   5670 C CD  . GLU B 1 289 ? 43.747  1.519   27.427  1.00 113.84 ? 318 GLU B CD  1 
ATOM   5671 O OE1 . GLU B 1 289 ? 44.017  1.303   26.226  1.00 113.90 ? 318 GLU B OE1 1 
ATOM   5672 O OE2 . GLU B 1 289 ? 44.030  2.587   28.016  1.00 111.26 ? 318 GLU B OE2 1 
ATOM   5673 N N   . VAL B 1 290 ? 42.211  -0.017  32.596  1.00 111.80 ? 319 VAL B N   1 
ATOM   5674 C CA  . VAL B 1 290 ? 42.157  0.069   34.047  1.00 110.25 ? 319 VAL B CA  1 
ATOM   5675 C C   . VAL B 1 290 ? 41.595  -1.257  34.558  1.00 106.35 ? 319 VAL B C   1 
ATOM   5676 O O   . VAL B 1 290 ? 41.486  -2.215  33.795  1.00 100.45 ? 319 VAL B O   1 
ATOM   5677 C CB  . VAL B 1 290 ? 41.338  1.286   34.534  1.00 112.58 ? 319 VAL B CB  1 
ATOM   5678 C CG1 . VAL B 1 290 ? 41.790  2.577   33.861  1.00 113.67 ? 319 VAL B CG1 1 
ATOM   5679 C CG2 . VAL B 1 290 ? 39.834  1.106   34.360  1.00 112.94 ? 319 VAL B CG2 1 
ATOM   5680 N N   . GLY B 1 291 ? 41.260  -1.314  35.852  1.00 105.75 ? 320 GLY B N   1 
ATOM   5681 C CA  . GLY B 1 291 ? 40.555  -2.457  36.409  1.00 104.91 ? 320 GLY B CA  1 
ATOM   5682 C C   . GLY B 1 291 ? 39.080  -2.454  36.010  1.00 105.67 ? 320 GLY B C   1 
ATOM   5683 O O   . GLY B 1 291 ? 38.716  -1.916  34.970  1.00 103.93 ? 320 GLY B O   1 
ATOM   5684 N N   . LYS B 1 292 ? 38.239  -3.079  36.841  1.00 109.07 ? 321 LYS B N   1 
ATOM   5685 C CA  . LYS B 1 292 ? 36.795  -2.995  36.682  1.00 108.42 ? 321 LYS B CA  1 
ATOM   5686 C C   . LYS B 1 292 ? 36.218  -2.032  37.719  1.00 113.05 ? 321 LYS B C   1 
ATOM   5687 O O   . LYS B 1 292 ? 34.999  -1.929  37.849  1.00 109.46 ? 321 LYS B O   1 
ATOM   5688 C CB  . LYS B 1 292 ? 36.146  -4.377  36.821  1.00 105.19 ? 321 LYS B CB  1 
ATOM   5689 N N   . ASP B 1 293 ? 37.103  -1.341  38.456  1.00 116.20 ? 322 ASP B N   1 
ATOM   5690 C CA  . ASP B 1 293 ? 36.696  -0.472  39.549  1.00 116.64 ? 322 ASP B CA  1 
ATOM   5691 C C   . ASP B 1 293 ? 37.646  0.724   39.609  1.00 114.38 ? 322 ASP B C   1 
ATOM   5692 O O   . ASP B 1 293 ? 38.450  0.846   40.532  1.00 114.84 ? 322 ASP B O   1 
ATOM   5693 C CB  . ASP B 1 293 ? 36.633  -1.229  40.869  1.00 118.90 ? 322 ASP B CB  1 
ATOM   5694 C CG  . ASP B 1 293 ? 36.397  -2.731  40.768  1.00 121.55 ? 322 ASP B CG  1 
ATOM   5695 O OD1 . ASP B 1 293 ? 37.314  -3.438  40.295  1.00 120.85 ? 322 ASP B OD1 1 
ATOM   5696 O OD2 . ASP B 1 293 ? 35.301  -3.183  41.159  1.00 125.96 ? 322 ASP B OD2 1 
ATOM   5697 N N   . VAL B 1 294 ? 37.540  1.599   38.604  1.00 111.90 ? 323 VAL B N   1 
ATOM   5698 C CA  . VAL B 1 294 ? 38.326  2.821   38.538  1.00 110.60 ? 323 VAL B CA  1 
ATOM   5699 C C   . VAL B 1 294 ? 37.631  3.903   39.365  1.00 111.33 ? 323 VAL B C   1 
ATOM   5700 O O   . VAL B 1 294 ? 36.403  3.957   39.420  1.00 106.70 ? 323 VAL B O   1 
ATOM   5701 C CB  . VAL B 1 294 ? 38.556  3.270   37.079  1.00 108.92 ? 323 VAL B CB  1 
ATOM   5702 C CG1 . VAL B 1 294 ? 37.275  3.260   36.249  1.00 109.62 ? 323 VAL B CG1 1 
ATOM   5703 C CG2 . VAL B 1 294 ? 39.230  4.635   36.999  1.00 106.57 ? 323 VAL B CG2 1 
ATOM   5704 N N   . SER B 1 295 ? 38.433  4.767   40.004  1.00 113.07 ? 324 SER B N   1 
ATOM   5705 C CA  . SER B 1 295 ? 37.913  5.854   40.818  1.00 110.96 ? 324 SER B CA  1 
ATOM   5706 C C   . SER B 1 295 ? 37.609  7.057   39.921  1.00 111.05 ? 324 SER B C   1 
ATOM   5707 O O   . SER B 1 295 ? 36.901  6.911   38.926  1.00 111.02 ? 324 SER B O   1 
ATOM   5708 C CB  . SER B 1 295 ? 38.865  6.184   41.948  1.00 108.10 ? 324 SER B CB  1 
ATOM   5709 O OG  . SER B 1 295 ? 40.040  6.825   41.470  1.00 106.89 ? 324 SER B OG  1 
ATOM   5710 N N   . ASP B 1 296 ? 38.128  8.240   40.288  1.00 109.16 ? 325 ASP B N   1 
ATOM   5711 C CA  . ASP B 1 296 ? 37.974  9.455   39.499  1.00 106.63 ? 325 ASP B CA  1 
ATOM   5712 C C   . ASP B 1 296 ? 39.319  9.884   38.907  1.00 105.59 ? 325 ASP B C   1 
ATOM   5713 O O   . ASP B 1 296 ? 39.360  10.438  37.807  1.00 100.22 ? 325 ASP B O   1 
ATOM   5714 C CB  . ASP B 1 296 ? 37.328  10.563  40.320  1.00 102.34 ? 325 ASP B CB  1 
ATOM   5715 C CG  . ASP B 1 296 ? 35.807  10.535  40.388  1.00 100.89 ? 325 ASP B CG  1 
ATOM   5716 O OD1 . ASP B 1 296 ? 35.249  9.450   40.654  1.00 100.26 ? 325 ASP B OD1 1 
ATOM   5717 O OD2 . ASP B 1 296 ? 35.193  11.603  40.184  1.00 99.65  ? 325 ASP B OD2 1 
ATOM   5718 N N   . GLU B 1 297 ? 40.411  9.633   39.648  1.00 101.50 ? 326 GLU B N   1 
ATOM   5719 C CA  . GLU B 1 297 ? 41.754  10.032  39.248  1.00 97.96  ? 326 GLU B CA  1 
ATOM   5720 C C   . GLU B 1 297 ? 42.114  9.409   37.901  1.00 91.45  ? 326 GLU B C   1 
ATOM   5721 O O   . GLU B 1 297 ? 42.237  10.111  36.898  1.00 84.69  ? 326 GLU B O   1 
ATOM   5722 C CB  . GLU B 1 297 ? 42.787  9.628   40.305  1.00 98.10  ? 326 GLU B CB  1 
ATOM   5723 C CG  . GLU B 1 297 ? 43.086  10.699  41.351  1.00 97.65  ? 326 GLU B CG  1 
ATOM   5724 C CD  . GLU B 1 297 ? 42.021  10.967  42.402  1.00 97.75  ? 326 GLU B CD  1 
ATOM   5725 O OE1 . GLU B 1 297 ? 40.839  11.165  42.042  1.00 95.95  ? 326 GLU B OE1 1 
ATOM   5726 O OE2 . GLU B 1 297 ? 42.391  11.014  43.596  1.00 96.14  ? 326 GLU B OE2 1 
ATOM   5727 N N   . LYS B 1 298 ? 42.288  8.083   37.899  1.00 88.58  ? 327 LYS B N   1 
ATOM   5728 C CA  . LYS B 1 298 ? 42.588  7.337   36.689  1.00 92.60  ? 327 LYS B CA  1 
ATOM   5729 C C   . LYS B 1 298 ? 41.536  7.641   35.628  1.00 94.52  ? 327 LYS B C   1 
ATOM   5730 O O   . LYS B 1 298 ? 41.852  7.734   34.444  1.00 90.56  ? 327 LYS B O   1 
ATOM   5731 C CB  . LYS B 1 298 ? 42.545  5.832   36.966  1.00 95.39  ? 327 LYS B CB  1 
ATOM   5732 C CG  . LYS B 1 298 ? 43.634  5.254   37.858  1.00 97.77  ? 327 LYS B CG  1 
ATOM   5733 C CD  . LYS B 1 298 ? 43.214  3.953   38.536  1.00 100.09 ? 327 LYS B CD  1 
ATOM   5734 C CE  . LYS B 1 298 ? 42.639  2.936   37.593  1.00 101.93 ? 327 LYS B CE  1 
ATOM   5735 N NZ  . LYS B 1 298 ? 41.938  1.868   38.308  1.00 103.02 ? 327 LYS B NZ  1 
ATOM   5736 N N   . LEU B 1 299 ? 40.285  7.776   36.086  1.00 97.21  ? 328 LEU B N   1 
ATOM   5737 C CA  . LEU B 1 299 ? 39.147  8.031   35.220  1.00 100.68 ? 328 LEU B CA  1 
ATOM   5738 C C   . LEU B 1 299 ? 39.346  9.340   34.456  1.00 100.20 ? 328 LEU B C   1 
ATOM   5739 O O   . LEU B 1 299 ? 39.076  9.399   33.257  1.00 103.07 ? 328 LEU B O   1 
ATOM   5740 C CB  . LEU B 1 299 ? 37.879  8.059   36.072  1.00 102.57 ? 328 LEU B CB  1 
ATOM   5741 C CG  . LEU B 1 299 ? 36.549  7.974   35.316  1.00 105.57 ? 328 LEU B CG  1 
ATOM   5742 C CD1 . LEU B 1 299 ? 36.293  6.577   34.776  1.00 107.03 ? 328 LEU B CD1 1 
ATOM   5743 C CD2 . LEU B 1 299 ? 35.405  8.411   36.209  1.00 105.91 ? 328 LEU B CD2 1 
ATOM   5744 N N   . ARG B 1 300 ? 39.823  10.379  35.157  1.00 93.94  ? 329 ARG B N   1 
ATOM   5745 C CA  . ARG B 1 300 ? 40.052  11.682  34.551  1.00 90.67  ? 329 ARG B CA  1 
ATOM   5746 C C   . ARG B 1 300 ? 41.159  11.584  33.500  1.00 90.26  ? 329 ARG B C   1 
ATOM   5747 O O   . ARG B 1 300 ? 41.174  12.358  32.544  1.00 91.30  ? 329 ARG B O   1 
ATOM   5748 C CB  . ARG B 1 300 ? 40.382  12.727  35.625  1.00 87.14  ? 329 ARG B CB  1 
ATOM   5749 N N   . ASP B 1 301 ? 42.076  10.623  33.685  1.00 90.79  ? 330 ASP B N   1 
ATOM   5750 C CA  . ASP B 1 301 ? 43.185  10.410  32.767  1.00 89.34  ? 330 ASP B CA  1 
ATOM   5751 C C   . ASP B 1 301 ? 42.693  9.729   31.489  1.00 91.62  ? 330 ASP B C   1 
ATOM   5752 O O   . ASP B 1 301 ? 42.964  10.215  30.393  1.00 90.38  ? 330 ASP B O   1 
ATOM   5753 C CB  . ASP B 1 301 ? 44.323  9.662   33.446  1.00 85.21  ? 330 ASP B CB  1 
ATOM   5754 C CG  . ASP B 1 301 ? 44.867  10.315  34.711  1.00 85.77  ? 330 ASP B CG  1 
ATOM   5755 O OD1 . ASP B 1 301 ? 44.248  11.292  35.186  1.00 81.20  ? 330 ASP B OD1 1 
ATOM   5756 O OD2 . ASP B 1 301 ? 45.913  9.850   35.211  1.00 83.82  ? 330 ASP B OD2 1 
ATOM   5757 N N   . TYR B 1 302 ? 41.964  8.613   31.632  1.00 95.55  ? 331 TYR B N   1 
ATOM   5758 C CA  . TYR B 1 302 ? 41.509  7.831   30.488  1.00 96.03  ? 331 TYR B CA  1 
ATOM   5759 C C   . TYR B 1 302 ? 40.648  8.697   29.572  1.00 91.95  ? 331 TYR B C   1 
ATOM   5760 O O   . TYR B 1 302 ? 40.708  8.554   28.353  1.00 88.87  ? 331 TYR B O   1 
ATOM   5761 C CB  . TYR B 1 302 ? 40.715  6.585   30.895  1.00 99.12  ? 331 TYR B CB  1 
ATOM   5762 C CG  . TYR B 1 302 ? 40.421  5.614   29.755  1.00 103.71 ? 331 TYR B CG  1 
ATOM   5763 C CD1 . TYR B 1 302 ? 39.351  5.817   28.886  1.00 103.76 ? 331 TYR B CD1 1 
ATOM   5764 C CD2 . TYR B 1 302 ? 41.205  4.482   29.555  1.00 103.03 ? 331 TYR B CD2 1 
ATOM   5765 C CE1 . TYR B 1 302 ? 39.081  4.935   27.851  1.00 101.72 ? 331 TYR B CE1 1 
ATOM   5766 C CE2 . TYR B 1 302 ? 40.943  3.592   28.525  1.00 101.19 ? 331 TYR B CE2 1 
ATOM   5767 C CZ  . TYR B 1 302 ? 39.878  3.819   27.670  1.00 100.58 ? 331 TYR B CZ  1 
ATOM   5768 O OH  . TYR B 1 302 ? 39.612  2.948   26.656  1.00 99.40  ? 331 TYR B OH  1 
ATOM   5769 N N   . ILE B 1 303 ? 39.834  9.571   30.175  1.00 93.52  ? 332 ILE B N   1 
ATOM   5770 C CA  . ILE B 1 303 ? 39.001  10.505  29.434  1.00 97.93  ? 332 ILE B CA  1 
ATOM   5771 C C   . ILE B 1 303 ? 39.893  11.451  28.630  1.00 99.38  ? 332 ILE B C   1 
ATOM   5772 O O   . ILE B 1 303 ? 39.669  11.645  27.436  1.00 96.17  ? 332 ILE B O   1 
ATOM   5773 C CB  . ILE B 1 303 ? 38.046  11.254  30.387  1.00 99.73  ? 332 ILE B CB  1 
ATOM   5774 C CG1 . ILE B 1 303 ? 36.884  10.364  30.839  1.00 98.68  ? 332 ILE B CG1 1 
ATOM   5775 C CG2 . ILE B 1 303 ? 37.530  12.552  29.771  1.00 101.04 ? 332 ILE B CG2 1 
ATOM   5776 C CD1 . ILE B 1 303 ? 35.995  9.877   29.706  1.00 100.10 ? 332 ILE B CD1 1 
ATOM   5777 N N   . TRP B 1 304 ? 40.909  12.022  29.292  1.00 97.21  ? 333 TRP B N   1 
ATOM   5778 C CA  . TRP B 1 304 ? 41.787  12.999  28.665  1.00 94.08  ? 333 TRP B CA  1 
ATOM   5779 C C   . TRP B 1 304 ? 42.682  12.344  27.613  1.00 90.38  ? 333 TRP B C   1 
ATOM   5780 O O   . TRP B 1 304 ? 42.961  12.952  26.581  1.00 85.41  ? 333 TRP B O   1 
ATOM   5781 C CB  . TRP B 1 304 ? 42.606  13.746  29.728  1.00 91.97  ? 333 TRP B CB  1 
ATOM   5782 C CG  . TRP B 1 304 ? 41.954  15.025  30.183  1.00 92.34  ? 333 TRP B CG  1 
ATOM   5783 C CD1 . TRP B 1 304 ? 41.567  15.353  31.449  1.00 91.92  ? 333 TRP B CD1 1 
ATOM   5784 C CD2 . TRP B 1 304 ? 41.633  16.165  29.355  1.00 92.26  ? 333 TRP B CD2 1 
ATOM   5785 N NE1 . TRP B 1 304 ? 41.012  16.604  31.464  1.00 93.46  ? 333 TRP B NE1 1 
ATOM   5786 C CE2 . TRP B 1 304 ? 41.042  17.130  30.198  1.00 92.87  ? 333 TRP B CE2 1 
ATOM   5787 C CE3 . TRP B 1 304 ? 41.781  16.460  27.995  1.00 95.11  ? 333 TRP B CE3 1 
ATOM   5788 C CZ2 . TRP B 1 304 ? 40.604  18.365  29.722  1.00 95.20  ? 333 TRP B CZ2 1 
ATOM   5789 C CZ3 . TRP B 1 304 ? 41.350  17.683  27.526  1.00 94.92  ? 333 TRP B CZ3 1 
ATOM   5790 C CH2 . TRP B 1 304 ? 40.769  18.621  28.380  1.00 93.08  ? 333 TRP B CH2 1 
ATOM   5791 N N   . ASN B 1 305 ? 43.109  11.102  27.870  1.00 90.05  ? 334 ASN B N   1 
ATOM   5792 C CA  . ASN B 1 305 ? 43.946  10.356  26.941  1.00 91.24  ? 334 ASN B CA  1 
ATOM   5793 C C   . ASN B 1 305 ? 43.175  10.036  25.659  1.00 91.87  ? 334 ASN B C   1 
ATOM   5794 O O   . ASN B 1 305 ? 43.758  9.984   24.577  1.00 95.47  ? 334 ASN B O   1 
ATOM   5795 C CB  . ASN B 1 305 ? 44.487  9.081   27.580  1.00 91.46  ? 334 ASN B CB  1 
ATOM   5796 C CG  . ASN B 1 305 ? 45.464  9.362   28.698  1.00 91.81  ? 334 ASN B CG  1 
ATOM   5797 O OD1 . ASN B 1 305 ? 45.782  10.525  28.973  1.00 89.46  ? 334 ASN B OD1 1 
ATOM   5798 N ND2 . ASN B 1 305 ? 45.952  8.317   29.349  1.00 89.81  ? 334 ASN B ND2 1 
ATOM   5799 N N   . THR B 1 306 ? 41.864  9.804   25.793  1.00 87.69  ? 335 THR B N   1 
ATOM   5800 C CA  . THR B 1 306 ? 40.987  9.592   24.653  1.00 80.50  ? 335 THR B CA  1 
ATOM   5801 C C   . THR B 1 306 ? 40.759  10.916  23.926  1.00 85.68  ? 335 THR B C   1 
ATOM   5802 O O   . THR B 1 306 ? 40.479  10.921  22.730  1.00 89.44  ? 335 THR B O   1 
ATOM   5803 C CB  . THR B 1 306 ? 39.679  8.972   25.144  1.00 74.77  ? 335 THR B CB  1 
ATOM   5804 O OG1 . THR B 1 306 ? 40.071  7.712   25.679  1.00 68.55  ? 335 THR B OG1 1 
ATOM   5805 C CG2 . THR B 1 306 ? 38.654  8.775   24.043  1.00 74.87  ? 335 THR B CG2 1 
ATOM   5806 N N   . LEU B 1 307 ? 40.891  12.033  24.656  1.00 92.86  ? 336 LEU B N   1 
ATOM   5807 C CA  . LEU B 1 307 ? 40.569  13.356  24.143  1.00 94.44  ? 336 LEU B CA  1 
ATOM   5808 C C   . LEU B 1 307 ? 41.830  14.181  23.877  1.00 93.52  ? 336 LEU B C   1 
ATOM   5809 O O   . LEU B 1 307 ? 41.746  15.399  23.717  1.00 92.48  ? 336 LEU B O   1 
ATOM   5810 C CB  . LEU B 1 307 ? 39.654  14.028  25.165  1.00 96.60  ? 336 LEU B CB  1 
ATOM   5811 C CG  . LEU B 1 307 ? 38.236  13.459  25.266  1.00 99.10  ? 336 LEU B CG  1 
ATOM   5812 C CD1 . LEU B 1 307 ? 37.551  13.998  26.508  1.00 103.80 ? 336 LEU B CD1 1 
ATOM   5813 C CD2 . LEU B 1 307 ? 37.423  13.772  24.019  1.00 98.11  ? 336 LEU B CD2 1 
ATOM   5814 N N   . ASN B 1 308 ? 42.993  13.518  23.831  1.00 90.44  ? 337 ASN B N   1 
ATOM   5815 C CA  . ASN B 1 308 ? 44.228  14.156  23.397  1.00 90.15  ? 337 ASN B CA  1 
ATOM   5816 C C   . ASN B 1 308 ? 44.800  13.425  22.184  1.00 88.26  ? 337 ASN B C   1 
ATOM   5817 O O   . ASN B 1 308 ? 45.336  14.060  21.278  1.00 91.20  ? 337 ASN B O   1 
ATOM   5818 C CB  . ASN B 1 308 ? 45.251  14.245  24.526  1.00 89.47  ? 337 ASN B CB  1 
ATOM   5819 C CG  . ASN B 1 308 ? 44.876  15.283  25.558  1.00 89.77  ? 337 ASN B CG  1 
ATOM   5820 O OD1 . ASN B 1 308 ? 44.683  16.456  25.219  1.00 85.47  ? 337 ASN B OD1 1 
ATOM   5821 N ND2 . ASN B 1 308 ? 44.771  14.880  26.816  1.00 92.59  ? 337 ASN B ND2 1 
ATOM   5822 N N   . SER B 1 309 ? 44.685  12.092  22.177  1.00 85.19  ? 338 SER B N   1 
ATOM   5823 C CA  . SER B 1 309 ? 45.216  11.264  21.105  1.00 82.81  ? 338 SER B CA  1 
ATOM   5824 C C   . SER B 1 309 ? 44.372  11.394  19.836  1.00 81.14  ? 338 SER B C   1 
ATOM   5825 O O   . SER B 1 309 ? 44.791  10.954  18.767  1.00 79.70  ? 338 SER B O   1 
ATOM   5826 C CB  . SER B 1 309 ? 45.310  9.829   21.548  1.00 83.96  ? 338 SER B CB  1 
ATOM   5827 O OG  . SER B 1 309 ? 46.036  9.722   22.765  1.00 83.20  ? 338 SER B OG  1 
ATOM   5828 N N   . GLY B 1 310 ? 43.174  11.975  19.967  1.00 79.97  ? 339 GLY B N   1 
ATOM   5829 C CA  . GLY B 1 310 ? 42.368  12.362  18.820  1.00 80.69  ? 339 GLY B CA  1 
ATOM   5830 C C   . GLY B 1 310 ? 41.183  11.423  18.626  1.00 79.75  ? 339 GLY B C   1 
ATOM   5831 O O   . GLY B 1 310 ? 40.992  10.886  17.538  1.00 82.89  ? 339 GLY B O   1 
ATOM   5832 N N   . ARG B 1 311 ? 40.393  11.250  19.693  1.00 79.31  ? 340 ARG B N   1 
ATOM   5833 C CA  . ARG B 1 311 ? 39.251  10.350  19.687  1.00 79.61  ? 340 ARG B CA  1 
ATOM   5834 C C   . ARG B 1 311 ? 38.081  11.020  20.401  1.00 83.12  ? 340 ARG B C   1 
ATOM   5835 O O   . ARG B 1 311 ? 38.228  12.115  20.948  1.00 80.49  ? 340 ARG B O   1 
ATOM   5836 C CB  . ARG B 1 311 ? 39.626  8.997   20.307  1.00 76.27  ? 340 ARG B CB  1 
ATOM   5837 C CG  . ARG B 1 311 ? 40.247  8.033   19.308  1.00 75.10  ? 340 ARG B CG  1 
ATOM   5838 C CD  . ARG B 1 311 ? 40.935  6.853   19.978  1.00 76.44  ? 340 ARG B CD  1 
ATOM   5839 N NE  . ARG B 1 311 ? 42.115  7.225   20.770  1.00 78.75  ? 340 ARG B NE  1 
ATOM   5840 C CZ  . ARG B 1 311 ? 42.277  7.064   22.082  1.00 85.06  ? 340 ARG B CZ  1 
ATOM   5841 N NH1 . ARG B 1 311 ? 43.465  7.265   22.629  1.00 82.21  ? 340 ARG B NH1 1 
ATOM   5842 N NH2 . ARG B 1 311 ? 41.274  6.662   22.845  1.00 91.82  ? 340 ARG B NH2 1 
ATOM   5843 N N   . VAL B 1 312 ? 36.928  10.336  20.376  1.00 80.32  ? 341 VAL B N   1 
ATOM   5844 C CA  . VAL B 1 312 ? 35.666  10.886  20.843  1.00 78.25  ? 341 VAL B CA  1 
ATOM   5845 C C   . VAL B 1 312 ? 35.186  10.075  22.048  1.00 73.09  ? 341 VAL B C   1 
ATOM   5846 O O   . VAL B 1 312 ? 35.370  8.860   22.091  1.00 70.61  ? 341 VAL B O   1 
ATOM   5847 C CB  . VAL B 1 312 ? 34.671  10.866  19.660  1.00 74.29  ? 341 VAL B CB  1 
ATOM   5848 C CG1 . VAL B 1 312 ? 33.885  9.561   19.559  1.00 69.82  ? 341 VAL B CG1 1 
ATOM   5849 C CG2 . VAL B 1 312 ? 33.733  12.066  19.685  1.00 74.33  ? 341 VAL B CG2 1 
ATOM   5850 N N   . VAL B 1 313 ? 34.599  10.756  23.041  1.00 71.82  ? 342 VAL B N   1 
ATOM   5851 C CA  . VAL B 1 313 ? 33.935  10.065  24.136  1.00 76.60  ? 342 VAL B CA  1 
ATOM   5852 C C   . VAL B 1 313 ? 32.593  9.595   23.585  1.00 78.52  ? 342 VAL B C   1 
ATOM   5853 O O   . VAL B 1 313 ? 31.755  10.425  23.236  1.00 76.84  ? 342 VAL B O   1 
ATOM   5854 C CB  . VAL B 1 313 ? 33.749  10.898  25.423  1.00 77.15  ? 342 VAL B CB  1 
ATOM   5855 C CG1 . VAL B 1 313 ? 33.115  10.083  26.546  1.00 77.42  ? 342 VAL B CG1 1 
ATOM   5856 C CG2 . VAL B 1 313 ? 35.060  11.499  25.912  1.00 75.66  ? 342 VAL B CG2 1 
ATOM   5857 N N   . PRO B 1 314 ? 32.361  8.264   23.464  1.00 80.80  ? 343 PRO B N   1 
ATOM   5858 C CA  . PRO B 1 314 ? 31.196  7.744   22.745  1.00 80.06  ? 343 PRO B CA  1 
ATOM   5859 C C   . PRO B 1 314 ? 29.900  7.922   23.527  1.00 76.36  ? 343 PRO B C   1 
ATOM   5860 O O   . PRO B 1 314 ? 29.908  7.923   24.759  1.00 82.17  ? 343 PRO B O   1 
ATOM   5861 C CB  . PRO B 1 314 ? 31.551  6.268   22.528  1.00 81.63  ? 343 PRO B CB  1 
ATOM   5862 C CG  . PRO B 1 314 ? 32.408  5.927   23.727  1.00 82.88  ? 343 PRO B CG  1 
ATOM   5863 C CD  . PRO B 1 314 ? 33.198  7.192   24.028  1.00 80.94  ? 343 PRO B CD  1 
ATOM   5864 N N   . GLY B 1 315 ? 28.795  8.077   22.787  1.00 69.85  ? 344 GLY B N   1 
ATOM   5865 C CA  . GLY B 1 315 ? 27.498  8.360   23.378  1.00 68.41  ? 344 GLY B CA  1 
ATOM   5866 C C   . GLY B 1 315 ? 27.425  9.756   24.000  1.00 67.32  ? 344 GLY B C   1 
ATOM   5867 O O   . GLY B 1 315 ? 26.525  10.033  24.787  1.00 69.61  ? 344 GLY B O   1 
ATOM   5868 N N   . TYR B 1 316 ? 28.370  10.632  23.645  1.00 64.86  ? 345 TYR B N   1 
ATOM   5869 C CA  . TYR B 1 316 ? 28.322  12.027  24.048  1.00 61.58  ? 345 TYR B CA  1 
ATOM   5870 C C   . TYR B 1 316 ? 28.292  12.868  22.773  1.00 59.66  ? 345 TYR B C   1 
ATOM   5871 O O   . TYR B 1 316 ? 28.991  12.556  21.815  1.00 60.09  ? 345 TYR B O   1 
ATOM   5872 C CB  . TYR B 1 316 ? 29.498  12.323  24.984  1.00 58.79  ? 345 TYR B CB  1 
ATOM   5873 C CG  . TYR B 1 316 ? 29.357  11.780  26.400  1.00 58.15  ? 345 TYR B CG  1 
ATOM   5874 C CD1 . TYR B 1 316 ? 29.642  10.451  26.700  1.00 59.52  ? 345 TYR B CD1 1 
ATOM   5875 C CD2 . TYR B 1 316 ? 28.956  12.607  27.442  1.00 57.87  ? 345 TYR B CD2 1 
ATOM   5876 C CE1 . TYR B 1 316 ? 29.518  9.959   27.990  1.00 60.18  ? 345 TYR B CE1 1 
ATOM   5877 C CE2 . TYR B 1 316 ? 28.831  12.130  28.736  1.00 59.69  ? 345 TYR B CE2 1 
ATOM   5878 C CZ  . TYR B 1 316 ? 29.109  10.803  29.010  1.00 60.62  ? 345 TYR B CZ  1 
ATOM   5879 O OH  . TYR B 1 316 ? 28.972  10.357  30.293  1.00 65.40  ? 345 TYR B OH  1 
ATOM   5880 N N   . GLY B 1 317 ? 27.436  13.896  22.749  1.00 59.40  ? 346 GLY B N   1 
ATOM   5881 C CA  . GLY B 1 317 ? 27.337  14.801  21.612  1.00 56.94  ? 346 GLY B CA  1 
ATOM   5882 C C   . GLY B 1 317 ? 26.092  14.536  20.767  1.00 56.34  ? 346 GLY B C   1 
ATOM   5883 O O   . GLY B 1 317 ? 25.513  13.453  20.825  1.00 55.83  ? 346 GLY B O   1 
ATOM   5884 N N   . HIS B 1 318 ? 25.694  15.546  19.980  1.00 54.26  ? 347 HIS B N   1 
ATOM   5885 C CA  . HIS B 1 318 ? 24.511  15.461  19.136  1.00 52.94  ? 347 HIS B CA  1 
ATOM   5886 C C   . HIS B 1 318 ? 24.580  16.521  18.042  1.00 54.68  ? 347 HIS B C   1 
ATOM   5887 O O   . HIS B 1 318 ? 25.349  17.473  18.146  1.00 59.11  ? 347 HIS B O   1 
ATOM   5888 C CB  . HIS B 1 318 ? 23.229  15.660  19.954  1.00 50.99  ? 347 HIS B CB  1 
ATOM   5889 C CG  . HIS B 1 318 ? 22.027  15.001  19.366  1.00 46.36  ? 347 HIS B CG  1 
ATOM   5890 N ND1 . HIS B 1 318 ? 21.714  13.695  19.675  1.00 46.22  ? 347 HIS B ND1 1 
ATOM   5891 C CD2 . HIS B 1 318 ? 21.081  15.413  18.517  1.00 43.79  ? 347 HIS B CD2 1 
ATOM   5892 C CE1 . HIS B 1 318 ? 20.616  13.345  19.023  1.00 44.33  ? 347 HIS B CE1 1 
ATOM   5893 N NE2 . HIS B 1 318 ? 20.210  14.376  18.321  1.00 44.40  ? 347 HIS B NE2 1 
ATOM   5894 N N   . ALA B 1 319 ? 23.743  16.350  17.011  1.00 54.96  ? 348 ALA B N   1 
ATOM   5895 C CA  . ALA B 1 319 ? 23.746  17.209  15.839  1.00 56.98  ? 348 ALA B CA  1 
ATOM   5896 C C   . ALA B 1 319 ? 22.870  18.447  16.043  1.00 59.21  ? 348 ALA B C   1 
ATOM   5897 O O   . ALA B 1 319 ? 22.983  19.408  15.281  1.00 54.67  ? 348 ALA B O   1 
ATOM   5898 C CB  . ALA B 1 319 ? 23.310  16.405  14.632  1.00 54.40  ? 348 ALA B CB  1 
ATOM   5899 N N   . VAL B 1 320 ? 21.993  18.423  17.057  1.00 61.93  ? 349 VAL B N   1 
ATOM   5900 C CA  . VAL B 1 320 ? 21.160  19.575  17.376  1.00 64.77  ? 349 VAL B CA  1 
ATOM   5901 C C   . VAL B 1 320 ? 20.994  19.731  18.888  1.00 63.03  ? 349 VAL B C   1 
ATOM   5902 O O   . VAL B 1 320 ? 20.979  20.859  19.371  1.00 65.24  ? 349 VAL B O   1 
ATOM   5903 C CB  . VAL B 1 320 ? 19.791  19.572  16.662  1.00 65.41  ? 349 VAL B CB  1 
ATOM   5904 C CG1 . VAL B 1 320 ? 19.230  18.171  16.485  1.00 66.05  ? 349 VAL B CG1 1 
ATOM   5905 C CG2 . VAL B 1 320 ? 18.775  20.491  17.341  1.00 66.03  ? 349 VAL B CG2 1 
ATOM   5906 N N   . LEU B 1 321 ? 20.816  18.631  19.630  1.00 60.48  ? 350 LEU B N   1 
ATOM   5907 C CA  . LEU B 1 321 ? 20.748  18.720  21.081  1.00 63.01  ? 350 LEU B CA  1 
ATOM   5908 C C   . LEU B 1 321 ? 22.055  19.301  21.617  1.00 65.76  ? 350 LEU B C   1 
ATOM   5909 O O   . LEU B 1 321 ? 23.135  18.851  21.242  1.00 68.38  ? 350 LEU B O   1 
ATOM   5910 C CB  . LEU B 1 321 ? 20.413  17.391  21.758  1.00 62.00  ? 350 LEU B CB  1 
ATOM   5911 C CG  . LEU B 1 321 ? 18.994  17.290  22.328  1.00 61.98  ? 350 LEU B CG  1 
ATOM   5912 C CD1 . LEU B 1 321 ? 18.671  15.883  22.782  1.00 60.88  ? 350 LEU B CD1 1 
ATOM   5913 C CD2 . LEU B 1 321 ? 18.821  18.271  23.479  1.00 64.59  ? 350 LEU B CD2 1 
ATOM   5914 N N   . ARG B 1 322 ? 21.922  20.312  22.486  1.00 67.01  ? 351 ARG B N   1 
ATOM   5915 C CA  . ARG B 1 322 ? 23.055  21.005  23.080  1.00 66.33  ? 351 ARG B CA  1 
ATOM   5916 C C   . ARG B 1 322 ? 23.049  20.883  24.604  1.00 60.42  ? 351 ARG B C   1 
ATOM   5917 O O   . ARG B 1 322 ? 23.909  21.465  25.256  1.00 55.71  ? 351 ARG B O   1 
ATOM   5918 C CB  . ARG B 1 322 ? 23.025  22.484  22.677  1.00 68.26  ? 351 ARG B CB  1 
ATOM   5919 C CG  . ARG B 1 322 ? 23.039  22.724  21.175  1.00 69.26  ? 351 ARG B CG  1 
ATOM   5920 C CD  . ARG B 1 322 ? 24.326  22.262  20.511  1.00 68.75  ? 351 ARG B CD  1 
ATOM   5921 N NE  . ARG B 1 322 ? 24.193  22.267  19.049  1.00 70.02  ? 351 ARG B NE  1 
ATOM   5922 C CZ  . ARG B 1 322 ? 24.542  21.282  18.222  1.00 73.78  ? 351 ARG B CZ  1 
ATOM   5923 N NH1 . ARG B 1 322 ? 24.270  21.381  16.931  1.00 74.48  ? 351 ARG B NH1 1 
ATOM   5924 N NH2 . ARG B 1 322 ? 25.140  20.193  18.676  1.00 74.58  ? 351 ARG B NH2 1 
ATOM   5925 N N   . LYS B 1 323 ? 22.093  20.128  25.162  1.00 60.37  ? 352 LYS B N   1 
ATOM   5926 C CA  . LYS B 1 323 ? 22.096  19.772  26.574  1.00 63.56  ? 352 LYS B CA  1 
ATOM   5927 C C   . LYS B 1 323 ? 22.028  18.250  26.687  1.00 58.09  ? 352 LYS B C   1 
ATOM   5928 O O   . LYS B 1 323 ? 21.797  17.568  25.694  1.00 54.64  ? 352 LYS B O   1 
ATOM   5929 C CB  . LYS B 1 323 ? 20.907  20.416  27.302  1.00 70.47  ? 352 LYS B CB  1 
ATOM   5930 C CG  . LYS B 1 323 ? 20.936  20.360  28.833  1.00 79.12  ? 352 LYS B CG  1 
ATOM   5931 C CD  . LYS B 1 323 ? 19.619  20.692  29.528  1.00 85.57  ? 352 LYS B CD  1 
ATOM   5932 C CE  . LYS B 1 323 ? 19.264  22.150  29.504  1.00 87.57  ? 352 LYS B CE  1 
ATOM   5933 N NZ  . LYS B 1 323 ? 17.923  22.369  30.053  1.00 87.98  ? 352 LYS B NZ  1 
ATOM   5934 N N   . THR B 1 324 ? 22.265  17.740  27.903  1.00 58.99  ? 353 THR B N   1 
ATOM   5935 C CA  . THR B 1 324 ? 21.937  16.375  28.287  1.00 56.98  ? 353 THR B CA  1 
ATOM   5936 C C   . THR B 1 324 ? 20.601  15.970  27.662  1.00 53.98  ? 353 THR B C   1 
ATOM   5937 O O   . THR B 1 324 ? 19.616  16.703  27.742  1.00 52.33  ? 353 THR B O   1 
ATOM   5938 C CB  . THR B 1 324 ? 21.888  16.262  29.813  1.00 57.70  ? 353 THR B CB  1 
ATOM   5939 O OG1 . THR B 1 324 ? 23.136  16.722  30.317  1.00 58.42  ? 353 THR B OG1 1 
ATOM   5940 C CG2 . THR B 1 324 ? 21.674  14.836  30.289  1.00 59.60  ? 353 THR B CG2 1 
ATOM   5941 N N   . ASP B 1 325 ? 20.596  14.782  27.047  1.00 48.49  ? 354 ASP B N   1 
ATOM   5942 C CA  . ASP B 1 325 ? 19.423  14.227  26.395  1.00 45.88  ? 354 ASP B CA  1 
ATOM   5943 C C   . ASP B 1 325 ? 18.446  13.760  27.476  1.00 43.71  ? 354 ASP B C   1 
ATOM   5944 O O   . ASP B 1 325 ? 18.845  13.076  28.412  1.00 49.65  ? 354 ASP B O   1 
ATOM   5945 C CB  . ASP B 1 325 ? 19.872  13.136  25.434  1.00 44.43  ? 354 ASP B CB  1 
ATOM   5946 C CG  . ASP B 1 325 ? 18.838  12.590  24.461  1.00 46.49  ? 354 ASP B CG  1 
ATOM   5947 O OD1 . ASP B 1 325 ? 17.646  12.938  24.603  1.00 44.28  ? 354 ASP B OD1 1 
ATOM   5948 O OD2 . ASP B 1 325 ? 19.245  11.815  23.562  1.00 50.45  ? 354 ASP B OD2 1 
ATOM   5949 N N   . PRO B 1 326 ? 17.142  14.127  27.427  1.00 41.04  ? 355 PRO B N   1 
ATOM   5950 C CA  . PRO B 1 326 ? 16.175  13.594  28.391  1.00 38.14  ? 355 PRO B CA  1 
ATOM   5951 C C   . PRO B 1 326 ? 16.025  12.075  28.312  1.00 37.46  ? 355 PRO B C   1 
ATOM   5952 O O   . PRO B 1 326 ? 15.560  11.442  29.254  1.00 38.47  ? 355 PRO B O   1 
ATOM   5953 C CB  . PRO B 1 326 ? 14.862  14.332  28.037  1.00 38.47  ? 355 PRO B CB  1 
ATOM   5954 C CG  . PRO B 1 326 ? 15.052  14.770  26.596  1.00 37.94  ? 355 PRO B CG  1 
ATOM   5955 C CD  . PRO B 1 326 ? 16.536  15.078  26.477  1.00 38.59  ? 355 PRO B CD  1 
ATOM   5956 N N   . ARG B 1 327 ? 16.415  11.494  27.174  1.00 39.12  ? 356 ARG B N   1 
ATOM   5957 C CA  . ARG B 1 327 ? 16.437  10.049  27.025  1.00 37.00  ? 356 ARG B CA  1 
ATOM   5958 C C   . ARG B 1 327 ? 17.551  9.449   27.880  1.00 35.13  ? 356 ARG B C   1 
ATOM   5959 O O   . ARG B 1 327 ? 17.371  8.384   28.458  1.00 36.65  ? 356 ARG B O   1 
ATOM   5960 C CB  . ARG B 1 327 ? 16.557  9.710   25.539  1.00 37.82  ? 356 ARG B CB  1 
ATOM   5961 C CG  . ARG B 1 327 ? 15.326  10.135  24.751  1.00 39.51  ? 356 ARG B CG  1 
ATOM   5962 C CD  . ARG B 1 327 ? 15.467  9.820   23.274  1.00 40.72  ? 356 ARG B CD  1 
ATOM   5963 N NE  . ARG B 1 327 ? 16.554  10.582  22.652  1.00 40.08  ? 356 ARG B NE  1 
ATOM   5964 C CZ  . ARG B 1 327 ? 17.073  10.326  21.458  1.00 42.38  ? 356 ARG B CZ  1 
ATOM   5965 N NH1 . ARG B 1 327 ? 16.587  9.355   20.697  1.00 42.13  ? 356 ARG B NH1 1 
ATOM   5966 N NH2 . ARG B 1 327 ? 18.087  11.052  21.023  1.00 43.73  ? 356 ARG B NH2 1 
ATOM   5967 N N   . TYR B 1 328 ? 18.695  10.133  27.975  1.00 37.64  ? 357 TYR B N   1 
ATOM   5968 C CA  . TYR B 1 328 ? 19.763  9.708   28.872  1.00 43.48  ? 357 TYR B CA  1 
ATOM   5969 C C   . TYR B 1 328 ? 19.273  9.779   30.315  1.00 42.63  ? 357 TYR B C   1 
ATOM   5970 O O   . TYR B 1 328 ? 19.328  8.788   31.041  1.00 43.85  ? 357 TYR B O   1 
ATOM   5971 C CB  . TYR B 1 328 ? 21.016  10.576  28.724  1.00 47.29  ? 357 TYR B CB  1 
ATOM   5972 C CG  . TYR B 1 328 ? 22.199  10.184  29.602  1.00 53.02  ? 357 TYR B CG  1 
ATOM   5973 C CD1 . TYR B 1 328 ? 22.268  10.559  30.942  1.00 55.05  ? 357 TYR B CD1 1 
ATOM   5974 C CD2 . TYR B 1 328 ? 23.267  9.460   29.079  1.00 55.65  ? 357 TYR B CD2 1 
ATOM   5975 C CE1 . TYR B 1 328 ? 23.357  10.219  31.732  1.00 56.08  ? 357 TYR B CE1 1 
ATOM   5976 C CE2 . TYR B 1 328 ? 24.366  9.123   29.855  1.00 55.37  ? 357 TYR B CE2 1 
ATOM   5977 C CZ  . TYR B 1 328 ? 24.413  9.507   31.184  1.00 57.74  ? 357 TYR B CZ  1 
ATOM   5978 O OH  . TYR B 1 328 ? 25.492  9.157   31.944  1.00 63.04  ? 357 TYR B OH  1 
ATOM   5979 N N   . THR B 1 329 ? 18.805  10.974  30.703  1.00 43.13  ? 358 THR B N   1 
ATOM   5980 C CA  . THR B 1 329 ? 18.285  11.250  32.032  1.00 43.45  ? 358 THR B CA  1 
ATOM   5981 C C   . THR B 1 329 ? 17.334  10.140  32.466  1.00 46.99  ? 358 THR B C   1 
ATOM   5982 O O   . THR B 1 329 ? 17.413  9.653   33.588  1.00 50.91  ? 358 THR B O   1 
ATOM   5983 C CB  . THR B 1 329 ? 17.592  12.609  31.984  1.00 43.57  ? 358 THR B CB  1 
ATOM   5984 O OG1 . THR B 1 329 ? 18.629  13.482  31.535  1.00 43.32  ? 358 THR B OG1 1 
ATOM   5985 C CG2 . THR B 1 329 ? 17.025  13.039  33.324  1.00 41.27  ? 358 THR B CG2 1 
ATOM   5986 N N   . CYS B 1 330 ? 16.442  9.748   31.553  1.00 49.29  ? 359 CYS B N   1 
ATOM   5987 C CA  . CYS B 1 330 ? 15.384  8.794   31.835  1.00 50.25  ? 359 CYS B CA  1 
ATOM   5988 C C   . CYS B 1 330 ? 15.952  7.396   32.107  1.00 48.42  ? 359 CYS B C   1 
ATOM   5989 O O   . CYS B 1 330 ? 15.494  6.695   33.008  1.00 43.84  ? 359 CYS B O   1 
ATOM   5990 C CB  . CYS B 1 330 ? 14.406  8.796   30.668  1.00 54.75  ? 359 CYS B CB  1 
ATOM   5991 S SG  . CYS B 1 330 ? 13.090  7.572   30.842  1.00 61.73  ? 359 CYS B SG  1 
ATOM   5992 N N   . GLN B 1 331 ? 16.942  6.986   31.308  1.00 48.97  ? 360 GLN B N   1 
ATOM   5993 C CA  . GLN B 1 331 ? 17.606  5.701   31.482  1.00 47.68  ? 360 GLN B CA  1 
ATOM   5994 C C   . GLN B 1 331 ? 18.448  5.697   32.758  1.00 47.87  ? 360 GLN B C   1 
ATOM   5995 O O   . GLN B 1 331 ? 18.534  4.677   33.440  1.00 44.55  ? 360 GLN B O   1 
ATOM   5996 C CB  . GLN B 1 331 ? 18.464  5.406   30.254  1.00 46.41  ? 360 GLN B CB  1 
ATOM   5997 C CG  . GLN B 1 331 ? 17.645  5.146   28.994  1.00 45.55  ? 360 GLN B CG  1 
ATOM   5998 C CD  . GLN B 1 331 ? 18.482  4.640   27.842  1.00 44.01  ? 360 GLN B CD  1 
ATOM   5999 O OE1 . GLN B 1 331 ? 18.430  3.460   27.481  1.00 45.49  ? 360 GLN B OE1 1 
ATOM   6000 N NE2 . GLN B 1 331 ? 19.293  5.521   27.276  1.00 44.64  ? 360 GLN B NE2 1 
ATOM   6001 N N   . ARG B 1 332 ? 19.061  6.844   33.076  1.00 48.39  ? 361 ARG B N   1 
ATOM   6002 C CA  . ARG B 1 332 ? 19.837  6.996   34.296  1.00 51.71  ? 361 ARG B CA  1 
ATOM   6003 C C   . ARG B 1 332 ? 18.946  6.832   35.525  1.00 53.95  ? 361 ARG B C   1 
ATOM   6004 O O   . ARG B 1 332 ? 19.314  6.137   36.466  1.00 56.24  ? 361 ARG B O   1 
ATOM   6005 C CB  . ARG B 1 332 ? 20.525  8.364   34.327  1.00 53.64  ? 361 ARG B CB  1 
ATOM   6006 C CG  . ARG B 1 332 ? 21.348  8.623   35.580  1.00 54.22  ? 361 ARG B CG  1 
ATOM   6007 C CD  . ARG B 1 332 ? 21.827  10.056  35.627  1.00 53.98  ? 361 ARG B CD  1 
ATOM   6008 N NE  . ARG B 1 332 ? 22.356  10.414  36.946  1.00 58.88  ? 361 ARG B NE  1 
ATOM   6009 C CZ  . ARG B 1 332 ? 23.505  10.006  37.482  1.00 57.24  ? 361 ARG B CZ  1 
ATOM   6010 N NH1 . ARG B 1 332 ? 24.297  9.157   36.845  1.00 59.98  ? 361 ARG B NH1 1 
ATOM   6011 N NH2 . ARG B 1 332 ? 23.862  10.470  38.665  1.00 56.73  ? 361 ARG B NH2 1 
ATOM   6012 N N   . GLU B 1 333 ? 17.786  7.496   35.513  1.00 55.89  ? 362 GLU B N   1 
ATOM   6013 C CA  . GLU B 1 333 ? 16.843  7.438   36.617  1.00 56.70  ? 362 GLU B CA  1 
ATOM   6014 C C   . GLU B 1 333 ? 16.399  5.994   36.839  1.00 53.34  ? 362 GLU B C   1 
ATOM   6015 O O   . GLU B 1 333 ? 16.240  5.563   37.978  1.00 58.25  ? 362 GLU B O   1 
ATOM   6016 C CB  . GLU B 1 333 ? 15.663  8.377   36.350  1.00 59.57  ? 362 GLU B CB  1 
ATOM   6017 C CG  . GLU B 1 333 ? 16.014  9.856   36.513  1.00 60.30  ? 362 GLU B CG  1 
ATOM   6018 C CD  . GLU B 1 333 ? 14.979  10.859  36.014  1.00 63.52  ? 362 GLU B CD  1 
ATOM   6019 O OE1 . GLU B 1 333 ? 13.932  10.439  35.470  1.00 66.66  ? 362 GLU B OE1 1 
ATOM   6020 O OE2 . GLU B 1 333 ? 15.220  12.078  36.177  1.00 61.40  ? 362 GLU B OE2 1 
ATOM   6021 N N   . PHE B 1 334 ? 16.209  5.250   35.746  1.00 49.80  ? 363 PHE B N   1 
ATOM   6022 C CA  . PHE B 1 334 ? 15.800  3.856   35.829  1.00 47.31  ? 363 PHE B CA  1 
ATOM   6023 C C   . PHE B 1 334 ? 16.869  3.046   36.569  1.00 48.68  ? 363 PHE B C   1 
ATOM   6024 O O   . PHE B 1 334 ? 16.538  2.155   37.350  1.00 45.00  ? 363 PHE B O   1 
ATOM   6025 C CB  . PHE B 1 334 ? 15.504  3.324   34.422  1.00 41.89  ? 363 PHE B CB  1 
ATOM   6026 C CG  . PHE B 1 334 ? 14.994  1.890   34.388  1.00 38.81  ? 363 PHE B CG  1 
ATOM   6027 C CD1 . PHE B 1 334 ? 13.648  1.607   34.581  1.00 39.86  ? 363 PHE B CD1 1 
ATOM   6028 C CD2 . PHE B 1 334 ? 15.859  0.827   34.153  1.00 38.38  ? 363 PHE B CD2 1 
ATOM   6029 C CE1 . PHE B 1 334 ? 13.185  0.302   34.551  1.00 38.81  ? 363 PHE B CE1 1 
ATOM   6030 C CE2 . PHE B 1 334 ? 15.394  -0.478  34.133  1.00 38.37  ? 363 PHE B CE2 1 
ATOM   6031 C CZ  . PHE B 1 334 ? 14.056  -0.737  34.331  1.00 39.64  ? 363 PHE B CZ  1 
ATOM   6032 N N   . ALA B 1 335 ? 18.148  3.363   36.313  1.00 52.06  ? 364 ALA B N   1 
ATOM   6033 C CA  . ALA B 1 335 ? 19.275  2.622   36.865  1.00 53.53  ? 364 ALA B CA  1 
ATOM   6034 C C   . ALA B 1 335 ? 19.430  2.903   38.356  1.00 55.58  ? 364 ALA B C   1 
ATOM   6035 O O   . ALA B 1 335 ? 19.694  1.988   39.136  1.00 56.13  ? 364 ALA B O   1 
ATOM   6036 C CB  . ALA B 1 335 ? 20.536  2.967   36.108  1.00 54.30  ? 364 ALA B CB  1 
ATOM   6037 N N   . LEU B 1 336 ? 19.243  4.171   38.740  1.00 55.98  ? 365 LEU B N   1 
ATOM   6038 C CA  . LEU B 1 336 ? 19.325  4.584   40.131  1.00 56.78  ? 365 LEU B CA  1 
ATOM   6039 C C   . LEU B 1 336 ? 18.369  3.769   41.002  1.00 58.74  ? 365 LEU B C   1 
ATOM   6040 O O   . LEU B 1 336 ? 18.621  3.619   42.197  1.00 64.05  ? 365 LEU B O   1 
ATOM   6041 C CB  . LEU B 1 336 ? 19.040  6.081   40.232  1.00 56.17  ? 365 LEU B CB  1 
ATOM   6042 C CG  . LEU B 1 336 ? 20.090  7.016   39.621  1.00 56.39  ? 365 LEU B CG  1 
ATOM   6043 C CD1 . LEU B 1 336 ? 19.616  8.453   39.738  1.00 55.57  ? 365 LEU B CD1 1 
ATOM   6044 C CD2 . LEU B 1 336 ? 21.475  6.860   40.252  1.00 56.37  ? 365 LEU B CD2 1 
ATOM   6045 N N   . LYS B 1 337 ? 17.287  3.243   40.409  1.00 57.50  ? 366 LYS B N   1 
ATOM   6046 C CA  . LYS B 1 337 ? 16.264  2.531   41.160  1.00 58.14  ? 366 LYS B CA  1 
ATOM   6047 C C   . LYS B 1 337 ? 16.523  1.025   41.186  1.00 57.97  ? 366 LYS B C   1 
ATOM   6048 O O   . LYS B 1 337 ? 16.349  0.396   42.224  1.00 62.20  ? 366 LYS B O   1 
ATOM   6049 C CB  . LYS B 1 337 ? 14.877  2.772   40.557  1.00 59.47  ? 366 LYS B CB  1 
ATOM   6050 C CG  . LYS B 1 337 ? 14.403  4.217   40.570  1.00 63.87  ? 366 LYS B CG  1 
ATOM   6051 C CD  . LYS B 1 337 ? 13.025  4.427   39.951  1.00 66.90  ? 366 LYS B CD  1 
ATOM   6052 C CE  . LYS B 1 337 ? 12.976  4.109   38.488  1.00 68.89  ? 366 LYS B CE  1 
ATOM   6053 N NZ  . LYS B 1 337 ? 11.620  4.248   37.953  1.00 72.41  ? 366 LYS B NZ  1 
ATOM   6054 N N   . HIS B 1 338 ? 16.923  0.449   40.047  1.00 58.20  ? 367 HIS B N   1 
ATOM   6055 C CA  . HIS B 1 338 ? 16.861  -0.993  39.857  1.00 56.84  ? 367 HIS B CA  1 
ATOM   6056 C C   . HIS B 1 338 ? 18.243  -1.647  39.899  1.00 53.91  ? 367 HIS B C   1 
ATOM   6057 O O   . HIS B 1 338 ? 18.361  -2.766  40.390  1.00 52.22  ? 367 HIS B O   1 
ATOM   6058 C CB  . HIS B 1 338 ? 16.109  -1.309  38.561  1.00 59.78  ? 367 HIS B CB  1 
ATOM   6059 C CG  . HIS B 1 338 ? 14.724  -0.761  38.561  1.00 64.36  ? 367 HIS B CG  1 
ATOM   6060 N ND1 . HIS B 1 338 ? 13.838  -0.954  39.599  1.00 70.40  ? 367 HIS B ND1 1 
ATOM   6061 C CD2 . HIS B 1 338 ? 14.076  -0.029  37.653  1.00 65.52  ? 367 HIS B CD2 1 
ATOM   6062 C CE1 . HIS B 1 338 ? 12.693  -0.350  39.312  1.00 69.22  ? 367 HIS B CE1 1 
ATOM   6063 N NE2 . HIS B 1 338 ? 12.819  0.223   38.134  1.00 67.46  ? 367 HIS B NE2 1 
ATOM   6064 N N   . LEU B 1 339 ? 19.278  -0.983  39.363  1.00 52.88  ? 368 LEU B N   1 
ATOM   6065 C CA  . LEU B 1 339 ? 20.623  -1.549  39.375  1.00 53.46  ? 368 LEU B CA  1 
ATOM   6066 C C   . LEU B 1 339 ? 21.650  -0.505  39.817  1.00 56.86  ? 368 LEU B C   1 
ATOM   6067 O O   . LEU B 1 339 ? 22.609  -0.231  39.092  1.00 56.77  ? 368 LEU B O   1 
ATOM   6068 C CB  . LEU B 1 339 ? 20.974  -2.133  38.006  1.00 56.51  ? 368 LEU B CB  1 
ATOM   6069 C CG  . LEU B 1 339 ? 20.606  -1.298  36.773  1.00 56.13  ? 368 LEU B CG  1 
ATOM   6070 C CD1 . LEU B 1 339 ? 21.742  -1.274  35.775  1.00 57.03  ? 368 LEU B CD1 1 
ATOM   6071 C CD2 . LEU B 1 339 ? 19.362  -1.853  36.104  1.00 56.13  ? 368 LEU B CD2 1 
ATOM   6072 N N   . PRO B 1 340 ? 21.506  0.095   41.025  1.00 59.20  ? 369 PRO B N   1 
ATOM   6073 C CA  . PRO B 1 340 ? 22.386  1.191   41.451  1.00 61.93  ? 369 PRO B CA  1 
ATOM   6074 C C   . PRO B 1 340 ? 23.852  0.879   41.772  1.00 62.82  ? 369 PRO B C   1 
ATOM   6075 O O   . PRO B 1 340 ? 24.671  1.798   41.807  1.00 65.39  ? 369 PRO B O   1 
ATOM   6076 C CB  . PRO B 1 340 ? 21.643  1.758   42.685  1.00 60.20  ? 369 PRO B CB  1 
ATOM   6077 C CG  . PRO B 1 340 ? 20.876  0.581   43.235  1.00 61.26  ? 369 PRO B CG  1 
ATOM   6078 C CD  . PRO B 1 340 ? 20.455  -0.207  42.010  1.00 61.13  ? 369 PRO B CD  1 
ATOM   6079 N N   . ASN B 1 341 ? 24.190  -0.399  41.992  1.00 59.96  ? 370 ASN B N   1 
ATOM   6080 C CA  . ASN B 1 341 ? 25.548  -0.768  42.361  1.00 62.45  ? 370 ASN B CA  1 
ATOM   6081 C C   . ASN B 1 341 ? 26.233  -1.560  41.246  1.00 66.08  ? 370 ASN B C   1 
ATOM   6082 O O   . ASN B 1 341 ? 27.260  -2.193  41.484  1.00 65.37  ? 370 ASN B O   1 
ATOM   6083 C CB  . ASN B 1 341 ? 25.571  -1.545  43.671  1.00 65.74  ? 370 ASN B CB  1 
ATOM   6084 C CG  . ASN B 1 341 ? 25.000  -0.742  44.815  1.00 68.04  ? 370 ASN B CG  1 
ATOM   6085 O OD1 . ASN B 1 341 ? 25.571  0.287   45.193  1.00 67.46  ? 370 ASN B OD1 1 
ATOM   6086 N ND2 . ASN B 1 341 ? 23.888  -1.192  45.379  1.00 70.28  ? 370 ASN B ND2 1 
ATOM   6087 N N   . ASP B 1 342 ? 25.690  -1.493  40.022  1.00 66.60  ? 371 ASP B N   1 
ATOM   6088 C CA  . ASP B 1 342 ? 26.255  -2.218  38.895  1.00 64.21  ? 371 ASP B CA  1 
ATOM   6089 C C   . ASP B 1 342 ? 27.599  -1.607  38.498  1.00 66.95  ? 371 ASP B C   1 
ATOM   6090 O O   . ASP B 1 342 ? 27.682  -0.406  38.256  1.00 71.17  ? 371 ASP B O   1 
ATOM   6091 C CB  . ASP B 1 342 ? 25.322  -2.230  37.696  1.00 61.40  ? 371 ASP B CB  1 
ATOM   6092 C CG  . ASP B 1 342 ? 25.922  -2.854  36.446  1.00 60.58  ? 371 ASP B CG  1 
ATOM   6093 O OD1 . ASP B 1 342 ? 25.984  -4.100  36.389  1.00 61.16  ? 371 ASP B OD1 1 
ATOM   6094 O OD2 . ASP B 1 342 ? 26.373  -2.086  35.569  1.00 57.68  ? 371 ASP B OD2 1 
ATOM   6095 N N   . PRO B 1 343 ? 28.688  -2.406  38.403  1.00 65.78  ? 372 PRO B N   1 
ATOM   6096 C CA  . PRO B 1 343 ? 29.994  -1.881  38.002  1.00 65.21  ? 372 PRO B CA  1 
ATOM   6097 C C   . PRO B 1 343 ? 29.977  -1.059  36.715  1.00 67.30  ? 372 PRO B C   1 
ATOM   6098 O O   . PRO B 1 343 ? 30.651  -0.036  36.623  1.00 69.23  ? 372 PRO B O   1 
ATOM   6099 C CB  . PRO B 1 343 ? 30.841  -3.155  37.849  1.00 64.86  ? 372 PRO B CB  1 
ATOM   6100 C CG  . PRO B 1 343 ? 30.216  -4.133  38.811  1.00 64.16  ? 372 PRO B CG  1 
ATOM   6101 C CD  . PRO B 1 343 ? 28.730  -3.843  38.722  1.00 65.10  ? 372 PRO B CD  1 
ATOM   6102 N N   . MET B 1 344 ? 29.215  -1.520  35.719  1.00 68.16  ? 373 MET B N   1 
ATOM   6103 C CA  . MET B 1 344 ? 29.188  -0.869  34.420  1.00 66.38  ? 373 MET B CA  1 
ATOM   6104 C C   . MET B 1 344 ? 28.402  0.435   34.506  1.00 64.10  ? 373 MET B C   1 
ATOM   6105 O O   . MET B 1 344 ? 28.762  1.415   33.855  1.00 63.73  ? 373 MET B O   1 
ATOM   6106 C CB  . MET B 1 344 ? 28.563  -1.775  33.353  1.00 74.95  ? 373 MET B CB  1 
ATOM   6107 C CG  . MET B 1 344 ? 29.323  -3.068  33.112  1.00 81.33  ? 373 MET B CG  1 
ATOM   6108 S SD  . MET B 1 344 ? 30.983  -2.804  32.454  1.00 96.65  ? 373 MET B SD  1 
ATOM   6109 C CE  . MET B 1 344 ? 30.667  -2.094  30.831  1.00 95.95  ? 373 MET B CE  1 
ATOM   6110 N N   . PHE B 1 345 ? 27.326  0.440   35.303  1.00 63.64  ? 374 PHE B N   1 
ATOM   6111 C CA  . PHE B 1 345 ? 26.498  1.627   35.450  1.00 65.93  ? 374 PHE B CA  1 
ATOM   6112 C C   . PHE B 1 345 ? 27.294  2.722   36.157  1.00 68.16  ? 374 PHE B C   1 
ATOM   6113 O O   . PHE B 1 345 ? 27.293  3.871   35.722  1.00 65.00  ? 374 PHE B O   1 
ATOM   6114 C CB  . PHE B 1 345 ? 25.198  1.403   36.231  1.00 62.04  ? 374 PHE B CB  1 
ATOM   6115 C CG  . PHE B 1 345 ? 24.537  2.709   36.662  1.00 61.55  ? 374 PHE B CG  1 
ATOM   6116 C CD1 . PHE B 1 345 ? 24.344  3.750   35.755  1.00 60.38  ? 374 PHE B CD1 1 
ATOM   6117 C CD2 . PHE B 1 345 ? 24.169  2.920   37.987  1.00 59.66  ? 374 PHE B CD2 1 
ATOM   6118 C CE1 . PHE B 1 345 ? 23.773  4.949   36.156  1.00 58.58  ? 374 PHE B CE1 1 
ATOM   6119 C CE2 . PHE B 1 345 ? 23.596  4.120   38.382  1.00 59.62  ? 374 PHE B CE2 1 
ATOM   6120 C CZ  . PHE B 1 345 ? 23.395  5.129   37.466  1.00 59.37  ? 374 PHE B CZ  1 
ATOM   6121 N N   . LYS B 1 346 ? 27.958  2.355   37.259  1.00 75.42  ? 375 LYS B N   1 
ATOM   6122 C CA  . LYS B 1 346 ? 28.657  3.325   38.086  1.00 80.97  ? 375 LYS B CA  1 
ATOM   6123 C C   . LYS B 1 346 ? 29.814  3.933   37.295  1.00 78.66  ? 375 LYS B C   1 
ATOM   6124 O O   . LYS B 1 346 ? 30.219  5.059   37.568  1.00 85.43  ? 375 LYS B O   1 
ATOM   6125 C CB  . LYS B 1 346 ? 29.132  2.713   39.409  1.00 84.19  ? 375 LYS B CB  1 
ATOM   6126 C CG  . LYS B 1 346 ? 28.051  1.975   40.187  1.00 87.23  ? 375 LYS B CG  1 
ATOM   6127 C CD  . LYS B 1 346 ? 28.314  1.842   41.681  1.00 89.87  ? 375 LYS B CD  1 
ATOM   6128 C CE  . LYS B 1 346 ? 27.898  3.059   42.443  1.00 90.07  ? 375 LYS B CE  1 
ATOM   6129 N NZ  . LYS B 1 346 ? 27.864  2.785   43.881  1.00 93.03  ? 375 LYS B NZ  1 
ATOM   6130 N N   . LEU B 1 347 ? 30.339  3.176   36.322  1.00 75.54  ? 376 LEU B N   1 
ATOM   6131 C CA  . LEU B 1 347 ? 31.312  3.697   35.378  1.00 76.62  ? 376 LEU B CA  1 
ATOM   6132 C C   . LEU B 1 347 ? 30.630  4.730   34.481  1.00 81.71  ? 376 LEU B C   1 
ATOM   6133 O O   . LEU B 1 347 ? 31.136  5.838   34.316  1.00 82.62  ? 376 LEU B O   1 
ATOM   6134 C CB  . LEU B 1 347 ? 31.909  2.547   34.568  1.00 74.83  ? 376 LEU B CB  1 
ATOM   6135 C CG  . LEU B 1 347 ? 32.961  2.928   33.522  1.00 76.78  ? 376 LEU B CG  1 
ATOM   6136 C CD1 . LEU B 1 347 ? 34.225  3.459   34.178  1.00 78.39  ? 376 LEU B CD1 1 
ATOM   6137 C CD2 . LEU B 1 347 ? 33.273  1.737   32.637  1.00 76.71  ? 376 LEU B CD2 1 
ATOM   6138 N N   . VAL B 1 348 ? 29.480  4.343   33.907  1.00 82.04  ? 377 VAL B N   1 
ATOM   6139 C CA  . VAL B 1 348 ? 28.635  5.246   33.139  1.00 77.91  ? 377 VAL B CA  1 
ATOM   6140 C C   . VAL B 1 348 ? 28.353  6.489   33.981  1.00 76.00  ? 377 VAL B C   1 
ATOM   6141 O O   . VAL B 1 348 ? 28.571  7.606   33.521  1.00 75.14  ? 377 VAL B O   1 
ATOM   6142 C CB  . VAL B 1 348 ? 27.330  4.555   32.682  1.00 72.90  ? 377 VAL B CB  1 
ATOM   6143 C CG1 . VAL B 1 348 ? 26.196  5.537   32.402  1.00 69.29  ? 377 VAL B CG1 1 
ATOM   6144 C CG2 . VAL B 1 348 ? 27.563  3.657   31.475  1.00 71.33  ? 377 VAL B CG2 1 
ATOM   6145 N N   . ALA B 1 349 ? 27.881  6.270   35.214  1.00 78.34  ? 378 ALA B N   1 
ATOM   6146 C CA  . ALA B 1 349 ? 27.525  7.348   36.122  1.00 85.26  ? 378 ALA B CA  1 
ATOM   6147 C C   . ALA B 1 349 ? 28.718  8.275   36.353  1.00 92.41  ? 378 ALA B C   1 
ATOM   6148 O O   . ALA B 1 349 ? 28.563  9.492   36.324  1.00 97.17  ? 378 ALA B O   1 
ATOM   6149 C CB  . ALA B 1 349 ? 27.014  6.775   37.425  1.00 83.90  ? 378 ALA B CB  1 
ATOM   6150 N N   . GLN B 1 350 ? 29.902  7.689   36.576  1.00 97.76  ? 379 GLN B N   1 
ATOM   6151 C CA  . GLN B 1 350 ? 31.099  8.452   36.898  1.00 104.90 ? 379 GLN B CA  1 
ATOM   6152 C C   . GLN B 1 350 ? 31.515  9.343   35.727  1.00 107.28 ? 379 GLN B C   1 
ATOM   6153 O O   . GLN B 1 350 ? 32.039  10.435  35.939  1.00 108.80 ? 379 GLN B O   1 
ATOM   6154 C CB  . GLN B 1 350 ? 32.261  7.538   37.290  1.00 109.04 ? 379 GLN B CB  1 
ATOM   6155 C CG  . GLN B 1 350 ? 32.267  7.108   38.753  1.00 111.18 ? 379 GLN B CG  1 
ATOM   6156 C CD  . GLN B 1 350 ? 33.384  6.136   39.071  1.00 115.17 ? 379 GLN B CD  1 
ATOM   6157 O OE1 . GLN B 1 350 ? 33.378  4.982   38.626  1.00 115.65 ? 379 GLN B OE1 1 
ATOM   6158 N NE2 . GLN B 1 350 ? 34.359  6.590   39.845  1.00 117.16 ? 379 GLN B NE2 1 
ATOM   6159 N N   . LEU B 1 351 ? 31.285  8.868   34.497  1.00 108.26 ? 380 LEU B N   1 
ATOM   6160 C CA  . LEU B 1 351 ? 31.605  9.629   33.297  1.00 105.97 ? 380 LEU B CA  1 
ATOM   6161 C C   . LEU B 1 351 ? 30.700  10.858  33.201  1.00 99.11  ? 380 LEU B C   1 
ATOM   6162 O O   . LEU B 1 351 ? 31.103  11.883  32.658  1.00 94.31  ? 380 LEU B O   1 
ATOM   6163 C CB  . LEU B 1 351 ? 31.467  8.740   32.061  1.00 107.56 ? 380 LEU B CB  1 
ATOM   6164 C CG  . LEU B 1 351 ? 32.342  7.482   32.020  1.00 108.60 ? 380 LEU B CG  1 
ATOM   6165 C CD1 . LEU B 1 351 ? 31.913  6.579   30.877  1.00 107.10 ? 380 LEU B CD1 1 
ATOM   6166 C CD2 . LEU B 1 351 ? 33.817  7.817   31.905  1.00 109.44 ? 380 LEU B CD2 1 
ATOM   6167 N N   . TYR B 1 352 ? 29.475  10.747  33.731  1.00 94.93  ? 381 TYR B N   1 
ATOM   6168 C CA  . TYR B 1 352 ? 28.521  11.847  33.727  1.00 94.32  ? 381 TYR B CA  1 
ATOM   6169 C C   . TYR B 1 352 ? 28.964  12.944  34.698  1.00 97.48  ? 381 TYR B C   1 
ATOM   6170 O O   . TYR B 1 352 ? 28.531  14.087  34.571  1.00 91.93  ? 381 TYR B O   1 
ATOM   6171 C CB  . TYR B 1 352 ? 27.136  11.281  34.059  1.00 88.96  ? 381 TYR B CB  1 
ATOM   6172 C CG  . TYR B 1 352 ? 25.966  12.250  33.940  1.00 87.58  ? 381 TYR B CG  1 
ATOM   6173 C CD1 . TYR B 1 352 ? 25.928  13.238  32.960  1.00 86.80  ? 381 TYR B CD1 1 
ATOM   6174 C CD2 . TYR B 1 352 ? 24.887  12.164  34.811  1.00 88.09  ? 381 TYR B CD2 1 
ATOM   6175 C CE1 . TYR B 1 352 ? 24.856  14.110  32.857  1.00 84.92  ? 381 TYR B CE1 1 
ATOM   6176 C CE2 . TYR B 1 352 ? 23.810  13.031  34.719  1.00 86.38  ? 381 TYR B CE2 1 
ATOM   6177 C CZ  . TYR B 1 352 ? 23.795  14.005  33.738  1.00 83.70  ? 381 TYR B CZ  1 
ATOM   6178 O OH  . TYR B 1 352 ? 22.732  14.855  33.652  1.00 85.66  ? 381 TYR B OH  1 
ATOM   6179 N N   . LYS B 1 353 ? 29.816  12.591  35.670  1.00 101.69 ? 382 LYS B N   1 
ATOM   6180 C CA  . LYS B 1 353 ? 30.369  13.555  36.609  1.00 102.81 ? 382 LYS B CA  1 
ATOM   6181 C C   . LYS B 1 353 ? 31.536  14.307  35.973  1.00 100.06 ? 382 LYS B C   1 
ATOM   6182 O O   . LYS B 1 353 ? 31.706  15.501  36.211  1.00 98.06  ? 382 LYS B O   1 
ATOM   6183 C CB  . LYS B 1 353 ? 30.909  12.888  37.880  1.00 104.84 ? 382 LYS B CB  1 
ATOM   6184 C CG  . LYS B 1 353 ? 29.975  11.911  38.582  1.00 107.77 ? 382 LYS B CG  1 
ATOM   6185 C CD  . LYS B 1 353 ? 30.481  11.418  39.934  1.00 106.65 ? 382 LYS B CD  1 
ATOM   6186 C CE  . LYS B 1 353 ? 31.886  10.897  39.901  1.00 104.18 ? 382 LYS B CE  1 
ATOM   6187 N NZ  . LYS B 1 353 ? 32.258  10.267  41.169  1.00 102.21 ? 382 LYS B NZ  1 
ATOM   6188 N N   . ILE B 1 354 ? 32.339  13.587  35.178  1.00 98.79  ? 383 ILE B N   1 
ATOM   6189 C CA  . ILE B 1 354 ? 33.650  14.057  34.757  1.00 99.82  ? 383 ILE B CA  1 
ATOM   6190 C C   . ILE B 1 354 ? 33.601  14.591  33.325  1.00 100.04 ? 383 ILE B C   1 
ATOM   6191 O O   . ILE B 1 354 ? 34.124  15.671  33.062  1.00 101.93 ? 383 ILE B O   1 
ATOM   6192 C CB  . ILE B 1 354 ? 34.695  12.936  34.929  1.00 98.90  ? 383 ILE B CB  1 
ATOM   6193 C CG1 . ILE B 1 354 ? 34.764  12.476  36.397  1.00 96.29  ? 383 ILE B CG1 1 
ATOM   6194 C CG2 . ILE B 1 354 ? 36.063  13.361  34.384  1.00 99.16  ? 383 ILE B CG2 1 
ATOM   6195 C CD1 . ILE B 1 354 ? 36.120  11.962  36.849  1.00 98.04  ? 383 ILE B CD1 1 
ATOM   6196 N N   . VAL B 1 355 ? 32.981  13.836  32.409  1.00 105.74 ? 384 VAL B N   1 
ATOM   6197 C CA  . VAL B 1 355 ? 33.057  14.118  30.981  1.00 108.74 ? 384 VAL B CA  1 
ATOM   6198 C C   . VAL B 1 355 ? 32.423  15.470  30.651  1.00 109.44 ? 384 VAL B C   1 
ATOM   6199 O O   . VAL B 1 355 ? 32.953  16.195  29.811  1.00 109.49 ? 384 VAL B O   1 
ATOM   6200 C CB  . VAL B 1 355 ? 32.431  13.004  30.119  1.00 108.11 ? 384 VAL B CB  1 
ATOM   6201 C CG1 . VAL B 1 355 ? 32.405  13.376  28.641  1.00 105.56 ? 384 VAL B CG1 1 
ATOM   6202 C CG2 . VAL B 1 355 ? 33.149  11.675  30.313  1.00 110.94 ? 384 VAL B CG2 1 
ATOM   6203 N N   . PRO B 1 356 ? 31.269  15.858  31.248  1.00 112.45 ? 385 PRO B N   1 
ATOM   6204 C CA  . PRO B 1 356 ? 30.677  17.167  30.951  1.00 116.90 ? 385 PRO B CA  1 
ATOM   6205 C C   . PRO B 1 356 ? 31.345  18.379  31.607  1.00 115.27 ? 385 PRO B C   1 
ATOM   6206 O O   . PRO B 1 356 ? 30.737  19.445  31.690  1.00 118.42 ? 385 PRO B O   1 
ATOM   6207 C CB  . PRO B 1 356 ? 29.222  16.983  31.418  1.00 117.49 ? 385 PRO B CB  1 
ATOM   6208 C CG  . PRO B 1 356 ? 29.311  15.991  32.550  1.00 116.10 ? 385 PRO B CG  1 
ATOM   6209 C CD  . PRO B 1 356 ? 30.457  15.062  32.185  1.00 112.08 ? 385 PRO B CD  1 
ATOM   6210 N N   . ASN B 1 357 ? 32.589  18.208  32.081  1.00 104.75 ? 386 ASN B N   1 
ATOM   6211 C CA  . ASN B 1 357 ? 33.426  19.322  32.501  1.00 91.84  ? 386 ASN B CA  1 
ATOM   6212 C C   . ASN B 1 357 ? 34.634  19.443  31.573  1.00 84.44  ? 386 ASN B C   1 
ATOM   6213 O O   . ASN B 1 357 ? 35.102  20.550  31.329  1.00 87.81  ? 386 ASN B O   1 
ATOM   6214 C CB  . ASN B 1 357 ? 33.854  19.201  33.961  1.00 90.51  ? 386 ASN B CB  1 
ATOM   6215 C CG  . ASN B 1 357 ? 32.678  19.199  34.913  1.00 87.45  ? 386 ASN B CG  1 
ATOM   6216 O OD1 . ASN B 1 357 ? 31.970  18.192  35.018  1.00 88.94  ? 386 ASN B OD1 1 
ATOM   6217 N ND2 . ASN B 1 357 ? 32.460  20.295  35.627  1.00 79.79  ? 386 ASN B ND2 1 
ATOM   6218 N N   . VAL B 1 358 ? 35.127  18.310  31.056  1.00 83.69  ? 387 VAL B N   1 
ATOM   6219 C CA  . VAL B 1 358 ? 36.370  18.269  30.298  1.00 83.28  ? 387 VAL B CA  1 
ATOM   6220 C C   . VAL B 1 358 ? 36.109  18.493  28.807  1.00 82.73  ? 387 VAL B C   1 
ATOM   6221 O O   . VAL B 1 358 ? 37.039  18.813  28.070  1.00 77.40  ? 387 VAL B O   1 
ATOM   6222 C CB  . VAL B 1 358 ? 37.134  16.948  30.513  1.00 83.54  ? 387 VAL B CB  1 
ATOM   6223 C CG1 . VAL B 1 358 ? 37.399  16.676  31.989  1.00 84.66  ? 387 VAL B CG1 1 
ATOM   6224 C CG2 . VAL B 1 358 ? 36.429  15.759  29.871  1.00 83.08  ? 387 VAL B CG2 1 
ATOM   6225 N N   . LEU B 1 359 ? 34.863  18.293  28.359  1.00 84.99  ? 388 LEU B N   1 
ATOM   6226 C CA  . LEU B 1 359 ? 34.518  18.456  26.954  1.00 92.14  ? 388 LEU B CA  1 
ATOM   6227 C C   . LEU B 1 359 ? 34.258  19.926  26.634  1.00 95.17  ? 388 LEU B C   1 
ATOM   6228 O O   . LEU B 1 359 ? 34.538  20.379  25.525  1.00 89.54  ? 388 LEU B O   1 
ATOM   6229 C CB  . LEU B 1 359 ? 33.312  17.592  26.589  1.00 93.08  ? 388 LEU B CB  1 
ATOM   6230 C CG  . LEU B 1 359 ? 33.622  16.142  26.205  1.00 95.93  ? 388 LEU B CG  1 
ATOM   6231 C CD1 . LEU B 1 359 ? 32.330  15.374  26.025  1.00 96.43  ? 388 LEU B CD1 1 
ATOM   6232 C CD2 . LEU B 1 359 ? 34.463  16.058  24.936  1.00 95.66  ? 388 LEU B CD2 1 
ATOM   6233 N N   . LEU B 1 360 ? 33.704  20.652  27.611  1.00 103.60 ? 389 LEU B N   1 
ATOM   6234 C CA  . LEU B 1 360 ? 33.465  22.081  27.483  1.00 107.80 ? 389 LEU B CA  1 
ATOM   6235 C C   . LEU B 1 360 ? 34.679  22.862  27.993  1.00 110.95 ? 389 LEU B C   1 
ATOM   6236 O O   . LEU B 1 360 ? 34.701  24.087  27.901  1.00 117.49 ? 389 LEU B O   1 
ATOM   6237 C CB  . LEU B 1 360 ? 32.163  22.474  28.187  1.00 107.35 ? 389 LEU B CB  1 
ATOM   6238 C CG  . LEU B 1 360 ? 31.888  21.850  29.560  1.00 111.19 ? 389 LEU B CG  1 
ATOM   6239 C CD1 . LEU B 1 360 ? 32.711  22.518  30.644  1.00 113.90 ? 389 LEU B CD1 1 
ATOM   6240 C CD2 . LEU B 1 360 ? 30.404  21.907  29.887  1.00 111.34 ? 389 LEU B CD2 1 
ATOM   6241 N N   . GLU B 1 361 ? 35.683  22.145  28.523  1.00 109.54 ? 390 GLU B N   1 
ATOM   6242 C CA  . GLU B 1 361 ? 36.997  22.705  28.810  1.00 107.75 ? 390 GLU B CA  1 
ATOM   6243 C C   . GLU B 1 361 ? 37.836  22.783  27.536  1.00 103.30 ? 390 GLU B C   1 
ATOM   6244 O O   . GLU B 1 361 ? 38.414  23.827  27.239  1.00 105.89 ? 390 GLU B O   1 
ATOM   6245 C CB  . GLU B 1 361 ? 37.792  21.860  29.809  1.00 112.19 ? 390 GLU B CB  1 
ATOM   6246 C CG  . GLU B 1 361 ? 37.704  22.342  31.255  1.00 114.94 ? 390 GLU B CG  1 
ATOM   6247 C CD  . GLU B 1 361 ? 38.529  21.501  32.214  1.00 117.32 ? 390 GLU B CD  1 
ATOM   6248 O OE1 . GLU B 1 361 ? 39.768  21.450  32.047  1.00 115.47 ? 390 GLU B OE1 1 
ATOM   6249 O OE2 . GLU B 1 361 ? 37.934  20.890  33.125  1.00 118.90 ? 390 GLU B OE2 1 
ATOM   6250 N N   . GLN B 1 362 ? 37.917  21.656  26.816  1.00 100.64 ? 391 GLN B N   1 
ATOM   6251 C CA  . GLN B 1 362 ? 38.814  21.500  25.678  1.00 96.20  ? 391 GLN B CA  1 
ATOM   6252 C C   . GLN B 1 362 ? 38.272  22.192  24.428  1.00 86.79  ? 391 GLN B C   1 
ATOM   6253 O O   . GLN B 1 362 ? 39.046  22.497  23.523  1.00 78.58  ? 391 GLN B O   1 
ATOM   6254 C CB  . GLN B 1 362 ? 39.047  20.025  25.349  1.00 96.86  ? 391 GLN B CB  1 
ATOM   6255 C CG  . GLN B 1 362 ? 37.782  19.258  24.979  1.00 100.10 ? 391 GLN B CG  1 
ATOM   6256 C CD  . GLN B 1 362 ? 37.993  17.762  24.949  1.00 103.21 ? 391 GLN B CD  1 
ATOM   6257 O OE1 . GLN B 1 362 ? 37.612  17.038  25.876  1.00 96.99  ? 391 GLN B OE1 1 
ATOM   6258 N NE2 . GLN B 1 362 ? 38.632  17.294  23.887  1.00 108.42 ? 391 GLN B NE2 1 
ATOM   6259 N N   . GLY B 1 363 ? 36.951  22.414  24.379  1.00 82.50  ? 392 GLY B N   1 
ATOM   6260 C CA  . GLY B 1 363 ? 36.303  22.944  23.191  1.00 84.69  ? 392 GLY B CA  1 
ATOM   6261 C C   . GLY B 1 363 ? 36.242  21.877  22.101  1.00 89.78  ? 392 GLY B C   1 
ATOM   6262 O O   . GLY B 1 363 ? 35.951  20.719  22.389  1.00 100.33 ? 392 GLY B O   1 
ATOM   6263 N N   . LYS B 1 364 ? 36.520  22.279  20.856  1.00 91.15  ? 393 LYS B N   1 
ATOM   6264 C CA  . LYS B 1 364 ? 36.546  21.365  19.725  1.00 95.52  ? 393 LYS B CA  1 
ATOM   6265 C C   . LYS B 1 364 ? 35.281  20.505  19.700  1.00 108.27 ? 393 LYS B C   1 
ATOM   6266 O O   . LYS B 1 364 ? 35.363  19.309  19.431  1.00 118.06 ? 393 LYS B O   1 
ATOM   6267 C CB  . LYS B 1 364 ? 37.804  20.491  19.799  1.00 91.47  ? 393 LYS B CB  1 
ATOM   6268 N N   . ALA B 1 365 ? 34.121  21.126  19.973  1.00 113.91 ? 394 ALA B N   1 
ATOM   6269 C CA  . ALA B 1 365 ? 32.841  20.431  20.058  1.00 112.51 ? 394 ALA B CA  1 
ATOM   6270 C C   . ALA B 1 365 ? 31.705  21.450  20.153  1.00 106.06 ? 394 ALA B C   1 
ATOM   6271 O O   . ALA B 1 365 ? 31.953  22.652  20.087  1.00 107.57 ? 394 ALA B O   1 
ATOM   6272 C CB  . ALA B 1 365 ? 32.836  19.488  21.247  1.00 114.68 ? 394 ALA B CB  1 
ATOM   6273 N N   . LYS B 1 366 ? 30.462  20.960  20.293  1.00 100.70 ? 395 LYS B N   1 
ATOM   6274 C CA  . LYS B 1 366 ? 29.311  21.821  20.538  1.00 98.93  ? 395 LYS B CA  1 
ATOM   6275 C C   . LYS B 1 366 ? 28.409  21.244  21.630  1.00 96.76  ? 395 LYS B C   1 
ATOM   6276 O O   . LYS B 1 366 ? 27.960  21.986  22.503  1.00 99.16  ? 395 LYS B O   1 
ATOM   6277 C CB  . LYS B 1 366 ? 28.532  22.110  19.249  1.00 99.09  ? 395 LYS B CB  1 
ATOM   6278 C CG  . LYS B 1 366 ? 28.914  23.430  18.584  1.00 102.21 ? 395 LYS B CG  1 
ATOM   6279 C CD  . LYS B 1 366 ? 28.414  24.663  19.333  1.00 102.22 ? 395 LYS B CD  1 
ATOM   6280 C CE  . LYS B 1 366 ? 29.247  25.894  19.126  1.00 101.09 ? 395 LYS B CE  1 
ATOM   6281 N NZ  . LYS B 1 366 ? 30.513  25.848  19.864  1.00 100.76 ? 395 LYS B NZ  1 
ATOM   6282 N N   . ASN B 1 367 ? 28.122  19.937  21.560  1.00 92.63  ? 396 ASN B N   1 
ATOM   6283 C CA  . ASN B 1 367 ? 27.352  19.250  22.587  1.00 87.44  ? 396 ASN B CA  1 
ATOM   6284 C C   . ASN B 1 367 ? 28.306  18.384  23.409  1.00 82.66  ? 396 ASN B C   1 
ATOM   6285 O O   . ASN B 1 367 ? 28.755  17.342  22.943  1.00 77.17  ? 396 ASN B O   1 
ATOM   6286 C CB  . ASN B 1 367 ? 26.190  18.481  21.960  1.00 86.35  ? 396 ASN B CB  1 
ATOM   6287 C CG  . ASN B 1 367 ? 25.334  17.731  22.959  1.00 82.81  ? 396 ASN B CG  1 
ATOM   6288 O OD1 . ASN B 1 367 ? 24.949  16.583  22.704  1.00 75.77  ? 396 ASN B OD1 1 
ATOM   6289 N ND2 . ASN B 1 367 ? 24.973  18.366  24.066  1.00 79.16  ? 396 ASN B ND2 1 
ATOM   6290 N N   . PRO B 1 368 ? 28.684  18.807  24.637  1.00 88.57  ? 397 PRO B N   1 
ATOM   6291 C CA  . PRO B 1 368 ? 29.526  17.989  25.516  1.00 88.15  ? 397 PRO B CA  1 
ATOM   6292 C C   . PRO B 1 368 ? 28.773  17.044  26.452  1.00 86.20  ? 397 PRO B C   1 
ATOM   6293 O O   . PRO B 1 368 ? 29.380  16.382  27.292  1.00 87.81  ? 397 PRO B O   1 
ATOM   6294 C CB  . PRO B 1 368 ? 30.243  19.105  26.290  1.00 92.18  ? 397 PRO B CB  1 
ATOM   6295 C CG  . PRO B 1 368 ? 29.155  20.131  26.522  1.00 91.27  ? 397 PRO B CG  1 
ATOM   6296 C CD  . PRO B 1 368 ? 28.362  20.120  25.225  1.00 90.60  ? 397 PRO B CD  1 
ATOM   6297 N N   . TRP B 1 369 ? 27.444  17.011  26.317  1.00 82.09  ? 398 TRP B N   1 
ATOM   6298 C CA  . TRP B 1 369 ? 26.600  16.222  27.194  1.00 79.19  ? 398 TRP B CA  1 
ATOM   6299 C C   . TRP B 1 369 ? 26.262  14.904  26.502  1.00 70.22  ? 398 TRP B C   1 
ATOM   6300 O O   . TRP B 1 369 ? 26.488  14.762  25.301  1.00 63.07  ? 398 TRP B O   1 
ATOM   6301 C CB  . TRP B 1 369 ? 25.361  17.043  27.572  1.00 84.92  ? 398 TRP B CB  1 
ATOM   6302 C CG  . TRP B 1 369 ? 25.719  18.361  28.209  1.00 96.89  ? 398 TRP B CG  1 
ATOM   6303 C CD1 . TRP B 1 369 ? 25.871  19.560  27.576  1.00 100.27 ? 398 TRP B CD1 1 
ATOM   6304 C CD2 . TRP B 1 369 ? 26.003  18.605  29.605  1.00 104.12 ? 398 TRP B CD2 1 
ATOM   6305 N NE1 . TRP B 1 369 ? 26.217  20.533  28.475  1.00 105.04 ? 398 TRP B NE1 1 
ATOM   6306 C CE2 . TRP B 1 369 ? 26.306  19.980  29.727  1.00 106.04 ? 398 TRP B CE2 1 
ATOM   6307 C CE3 . TRP B 1 369 ? 26.024  17.808  30.756  1.00 105.28 ? 398 TRP B CE3 1 
ATOM   6308 C CZ2 . TRP B 1 369 ? 26.626  20.565  30.951  1.00 106.70 ? 398 TRP B CZ2 1 
ATOM   6309 C CZ3 . TRP B 1 369 ? 26.334  18.389  31.967  1.00 104.84 ? 398 TRP B CZ3 1 
ATOM   6310 C CH2 . TRP B 1 369 ? 26.636  19.748  32.060  1.00 106.07 ? 398 TRP B CH2 1 
ATOM   6311 N N   . PRO B 1 370 ? 25.763  13.885  27.240  1.00 63.44  ? 399 PRO B N   1 
ATOM   6312 C CA  . PRO B 1 370 ? 25.484  12.577  26.642  1.00 60.73  ? 399 PRO B CA  1 
ATOM   6313 C C   . PRO B 1 370 ? 24.192  12.479  25.828  1.00 55.49  ? 399 PRO B C   1 
ATOM   6314 O O   . PRO B 1 370 ? 23.317  13.338  25.926  1.00 53.23  ? 399 PRO B O   1 
ATOM   6315 C CB  . PRO B 1 370 ? 25.458  11.680  27.887  1.00 62.05  ? 399 PRO B CB  1 
ATOM   6316 C CG  . PRO B 1 370 ? 24.875  12.566  28.963  1.00 63.42  ? 399 PRO B CG  1 
ATOM   6317 C CD  . PRO B 1 370 ? 25.477  13.929  28.683  1.00 64.09  ? 399 PRO B CD  1 
ATOM   6318 N N   . ASN B 1 371 ? 24.101  11.420  25.012  1.00 53.09  ? 400 ASN B N   1 
ATOM   6319 C CA  . ASN B 1 371 ? 22.887  11.084  24.285  1.00 50.91  ? 400 ASN B CA  1 
ATOM   6320 C C   . ASN B 1 371 ? 22.391  9.707   24.732  1.00 48.60  ? 400 ASN B C   1 
ATOM   6321 O O   . ASN B 1 371 ? 23.026  9.037   25.544  1.00 44.07  ? 400 ASN B O   1 
ATOM   6322 C CB  . ASN B 1 371 ? 23.085  11.189  22.776  1.00 50.41  ? 400 ASN B CB  1 
ATOM   6323 C CG  . ASN B 1 371 ? 24.171  10.274  22.263  1.00 54.47  ? 400 ASN B CG  1 
ATOM   6324 O OD1 . ASN B 1 371 ? 24.271  9.122   22.703  1.00 55.97  ? 400 ASN B OD1 1 
ATOM   6325 N ND2 . ASN B 1 371 ? 24.996  10.764  21.347  1.00 54.43  ? 400 ASN B ND2 1 
ATOM   6326 N N   . VAL B 1 372 ? 21.246  9.305   24.171  1.00 48.12  ? 401 VAL B N   1 
ATOM   6327 C CA  . VAL B 1 372 ? 20.506  8.119   24.576  1.00 48.31  ? 401 VAL B CA  1 
ATOM   6328 C C   . VAL B 1 372 ? 21.377  6.862   24.518  1.00 44.71  ? 401 VAL B C   1 
ATOM   6329 O O   . VAL B 1 372 ? 21.198  5.961   25.333  1.00 40.47  ? 401 VAL B O   1 
ATOM   6330 C CB  . VAL B 1 372 ? 19.250  7.978   23.688  1.00 49.49  ? 401 VAL B CB  1 
ATOM   6331 C CG1 . VAL B 1 372 ? 19.590  7.774   22.215  1.00 47.40  ? 401 VAL B CG1 1 
ATOM   6332 C CG2 . VAL B 1 372 ? 18.331  6.864   24.177  1.00 52.09  ? 401 VAL B CG2 1 
ATOM   6333 N N   . ASP B 1 373 ? 22.301  6.798   23.549  1.00 45.57  ? 402 ASP B N   1 
ATOM   6334 C CA  . ASP B 1 373 ? 23.091  5.600   23.300  1.00 45.77  ? 402 ASP B CA  1 
ATOM   6335 C C   . ASP B 1 373 ? 24.207  5.425   24.330  1.00 40.46  ? 402 ASP B C   1 
ATOM   6336 O O   . ASP B 1 373 ? 24.794  4.357   24.401  1.00 39.38  ? 402 ASP B O   1 
ATOM   6337 C CB  . ASP B 1 373 ? 23.674  5.598   21.897  1.00 48.34  ? 402 ASP B CB  1 
ATOM   6338 C CG  . ASP B 1 373 ? 22.649  5.664   20.775  1.00 52.72  ? 402 ASP B CG  1 
ATOM   6339 O OD1 . ASP B 1 373 ? 21.734  4.813   20.776  1.00 54.43  ? 402 ASP B OD1 1 
ATOM   6340 O OD2 . ASP B 1 373 ? 22.775  6.566   19.912  1.00 59.09  ? 402 ASP B OD2 1 
ATOM   6341 N N   . ALA B 1 374 ? 24.498  6.454   25.134  1.00 41.01  ? 403 ALA B N   1 
ATOM   6342 C CA  . ALA B 1 374 ? 25.527  6.346   26.162  1.00 43.34  ? 403 ALA B CA  1 
ATOM   6343 C C   . ALA B 1 374 ? 25.088  5.443   27.312  1.00 43.15  ? 403 ALA B C   1 
ATOM   6344 O O   . ALA B 1 374 ? 25.906  5.100   28.168  1.00 41.02  ? 403 ALA B O   1 
ATOM   6345 C CB  . ALA B 1 374 ? 25.888  7.716   26.704  1.00 43.10  ? 403 ALA B CB  1 
ATOM   6346 N N   . HIS B 1 375 ? 23.792  5.110   27.373  1.00 41.86  ? 404 HIS B N   1 
ATOM   6347 C CA  . HIS B 1 375 ? 23.246  4.548   28.597  1.00 43.42  ? 404 HIS B CA  1 
ATOM   6348 C C   . HIS B 1 375 ? 22.548  3.211   28.363  1.00 44.52  ? 404 HIS B C   1 
ATOM   6349 O O   . HIS B 1 375 ? 22.439  2.423   29.297  1.00 46.09  ? 404 HIS B O   1 
ATOM   6350 C CB  . HIS B 1 375 ? 22.295  5.549   29.260  1.00 41.96  ? 404 HIS B CB  1 
ATOM   6351 C CG  . HIS B 1 375 ? 22.390  5.541   30.748  1.00 39.61  ? 404 HIS B CG  1 
ATOM   6352 N ND1 . HIS B 1 375 ? 22.054  4.446   31.516  1.00 40.23  ? 404 HIS B ND1 1 
ATOM   6353 C CD2 . HIS B 1 375 ? 22.820  6.475   31.595  1.00 36.26  ? 404 HIS B CD2 1 
ATOM   6354 C CE1 . HIS B 1 375 ? 22.259  4.730   32.793  1.00 39.13  ? 404 HIS B CE1 1 
ATOM   6355 N NE2 . HIS B 1 375 ? 22.724  5.962   32.863  1.00 39.72  ? 404 HIS B NE2 1 
ATOM   6356 N N   . SER B 1 376 ? 22.059  2.962   27.142  1.00 44.02  ? 405 SER B N   1 
ATOM   6357 C CA  . SER B 1 376 ? 21.169  1.835   26.915  1.00 46.70  ? 405 SER B CA  1 
ATOM   6358 C C   . SER B 1 376 ? 21.924  0.522   27.111  1.00 46.52  ? 405 SER B C   1 
ATOM   6359 O O   . SER B 1 376 ? 21.382  -0.422  27.692  1.00 42.26  ? 405 SER B O   1 
ATOM   6360 C CB  . SER B 1 376 ? 20.511  1.909   25.554  1.00 49.38  ? 405 SER B CB  1 
ATOM   6361 O OG  . SER B 1 376 ? 21.466  2.051   24.512  1.00 50.96  ? 405 SER B OG  1 
ATOM   6362 N N   . GLY B 1 377 ? 23.190  0.509   26.669  1.00 47.96  ? 406 GLY B N   1 
ATOM   6363 C CA  . GLY B 1 377 ? 24.022  -0.682  26.665  1.00 46.59  ? 406 GLY B CA  1 
ATOM   6364 C C   . GLY B 1 377 ? 24.093  -1.348  28.034  1.00 45.05  ? 406 GLY B C   1 
ATOM   6365 O O   . GLY B 1 377 ? 23.918  -2.557  28.137  1.00 43.73  ? 406 GLY B O   1 
ATOM   6366 N N   . VAL B 1 378 ? 24.364  -0.557  29.077  1.00 47.61  ? 407 VAL B N   1 
ATOM   6367 C CA  . VAL B 1 378 ? 24.580  -1.111  30.405  1.00 52.86  ? 407 VAL B CA  1 
ATOM   6368 C C   . VAL B 1 378 ? 23.280  -1.708  30.941  1.00 50.89  ? 407 VAL B C   1 
ATOM   6369 O O   . VAL B 1 378 ? 23.319  -2.696  31.672  1.00 53.09  ? 407 VAL B O   1 
ATOM   6370 C CB  . VAL B 1 378 ? 25.177  -0.091  31.394  1.00 59.26  ? 407 VAL B CB  1 
ATOM   6371 C CG1 . VAL B 1 378 ? 26.598  0.294   30.999  1.00 63.27  ? 407 VAL B CG1 1 
ATOM   6372 C CG2 . VAL B 1 378 ? 24.306  1.150   31.555  1.00 59.43  ? 407 VAL B CG2 1 
ATOM   6373 N N   . LEU B 1 379 ? 22.134  -1.116  30.569  1.00 47.73  ? 408 LEU B N   1 
ATOM   6374 C CA  . LEU B 1 379 ? 20.836  -1.611  31.012  1.00 43.11  ? 408 LEU B CA  1 
ATOM   6375 C C   . LEU B 1 379 ? 20.597  -2.994  30.405  1.00 38.50  ? 408 LEU B C   1 
ATOM   6376 O O   . LEU B 1 379 ? 20.316  -3.947  31.120  1.00 39.03  ? 408 LEU B O   1 
ATOM   6377 C CB  . LEU B 1 379 ? 19.706  -0.636  30.674  1.00 40.09  ? 408 LEU B CB  1 
ATOM   6378 C CG  . LEU B 1 379 ? 19.886  0.806   31.164  1.00 41.09  ? 408 LEU B CG  1 
ATOM   6379 C CD1 . LEU B 1 379 ? 18.737  1.688   30.718  1.00 42.09  ? 408 LEU B CD1 1 
ATOM   6380 C CD2 . LEU B 1 379 ? 20.036  0.881   32.671  1.00 42.11  ? 408 LEU B CD2 1 
ATOM   6381 N N   . LEU B 1 380 ? 20.739  -3.108  29.084  1.00 35.30  ? 409 LEU B N   1 
ATOM   6382 C CA  . LEU B 1 380 ? 20.569  -4.385  28.403  1.00 35.66  ? 409 LEU B CA  1 
ATOM   6383 C C   . LEU B 1 380 ? 21.491  -5.440  29.005  1.00 37.51  ? 409 LEU B C   1 
ATOM   6384 O O   . LEU B 1 380 ? 21.046  -6.551  29.303  1.00 38.06  ? 409 LEU B O   1 
ATOM   6385 C CB  . LEU B 1 380 ? 20.836  -4.234  26.906  1.00 35.37  ? 409 LEU B CB  1 
ATOM   6386 C CG  . LEU B 1 380 ? 19.889  -3.311  26.132  1.00 34.89  ? 409 LEU B CG  1 
ATOM   6387 C CD1 . LEU B 1 380 ? 20.237  -3.343  24.656  1.00 34.61  ? 409 LEU B CD1 1 
ATOM   6388 C CD2 . LEU B 1 380 ? 18.422  -3.657  26.357  1.00 34.19  ? 409 LEU B CD2 1 
ATOM   6389 N N   . GLN B 1 381 ? 22.769  -5.065  29.184  1.00 41.21  ? 410 GLN B N   1 
ATOM   6390 C CA  . GLN B 1 381 ? 23.820  -5.976  29.613  1.00 41.66  ? 410 GLN B CA  1 
ATOM   6391 C C   . GLN B 1 381 ? 23.508  -6.517  31.010  1.00 40.59  ? 410 GLN B C   1 
ATOM   6392 O O   . GLN B 1 381 ? 23.731  -7.697  31.279  1.00 40.38  ? 410 GLN B O   1 
ATOM   6393 C CB  . GLN B 1 381 ? 25.187  -5.289  29.527  1.00 46.76  ? 410 GLN B CB  1 
ATOM   6394 C CG  . GLN B 1 381 ? 26.356  -6.181  29.936  1.00 50.87  ? 410 GLN B CG  1 
ATOM   6395 C CD  . GLN B 1 381 ? 27.718  -5.634  29.559  1.00 51.87  ? 410 GLN B CD  1 
ATOM   6396 O OE1 . GLN B 1 381 ? 28.154  -4.590  30.059  1.00 58.32  ? 410 GLN B OE1 1 
ATOM   6397 N NE2 . GLN B 1 381 ? 28.421  -6.350  28.692  1.00 50.13  ? 410 GLN B NE2 1 
ATOM   6398 N N   . TYR B 1 382 ? 22.954  -5.669  31.883  1.00 39.86  ? 411 TYR B N   1 
ATOM   6399 C CA  . TYR B 1 382 ? 22.637  -6.071  33.246  1.00 40.30  ? 411 TYR B CA  1 
ATOM   6400 C C   . TYR B 1 382 ? 21.692  -7.275  33.253  1.00 40.65  ? 411 TYR B C   1 
ATOM   6401 O O   . TYR B 1 382 ? 21.779  -8.109  34.156  1.00 40.18  ? 411 TYR B O   1 
ATOM   6402 C CB  . TYR B 1 382 ? 22.044  -4.881  34.006  1.00 42.12  ? 411 TYR B CB  1 
ATOM   6403 C CG  . TYR B 1 382 ? 21.591  -5.182  35.429  1.00 44.92  ? 411 TYR B CG  1 
ATOM   6404 C CD1 . TYR B 1 382 ? 22.483  -5.172  36.501  1.00 46.58  ? 411 TYR B CD1 1 
ATOM   6405 C CD2 . TYR B 1 382 ? 20.258  -5.461  35.704  1.00 47.21  ? 411 TYR B CD2 1 
ATOM   6406 C CE1 . TYR B 1 382 ? 22.062  -5.436  37.797  1.00 44.41  ? 411 TYR B CE1 1 
ATOM   6407 C CE2 . TYR B 1 382 ? 19.823  -5.723  36.993  1.00 46.79  ? 411 TYR B CE2 1 
ATOM   6408 C CZ  . TYR B 1 382 ? 20.727  -5.713  38.041  1.00 45.36  ? 411 TYR B CZ  1 
ATOM   6409 O OH  . TYR B 1 382 ? 20.257  -5.977  39.292  1.00 46.02  ? 411 TYR B OH  1 
ATOM   6410 N N   . TYR B 1 383 ? 20.818  -7.373  32.236  1.00 37.34  ? 412 TYR B N   1 
ATOM   6411 C CA  . TYR B 1 383 ? 19.726  -8.334  32.239  1.00 35.35  ? 412 TYR B CA  1 
ATOM   6412 C C   . TYR B 1 383 ? 20.027  -9.566  31.382  1.00 36.84  ? 412 TYR B C   1 
ATOM   6413 O O   . TYR B 1 383 ? 19.107  -10.322 31.076  1.00 37.09  ? 412 TYR B O   1 
ATOM   6414 C CB  . TYR B 1 383 ? 18.458  -7.617  31.760  1.00 33.57  ? 412 TYR B CB  1 
ATOM   6415 C CG  . TYR B 1 383 ? 17.933  -6.597  32.759  1.00 32.93  ? 412 TYR B CG  1 
ATOM   6416 C CD1 . TYR B 1 383 ? 17.271  -7.016  33.907  1.00 34.49  ? 412 TYR B CD1 1 
ATOM   6417 C CD2 . TYR B 1 383 ? 18.095  -5.228  32.567  1.00 32.77  ? 412 TYR B CD2 1 
ATOM   6418 C CE1 . TYR B 1 383 ? 16.787  -6.111  34.835  1.00 34.11  ? 412 TYR B CE1 1 
ATOM   6419 C CE2 . TYR B 1 383 ? 17.621  -4.308  33.495  1.00 33.00  ? 412 TYR B CE2 1 
ATOM   6420 C CZ  . TYR B 1 383 ? 16.963  -4.755  34.631  1.00 33.10  ? 412 TYR B CZ  1 
ATOM   6421 O OH  . TYR B 1 383 ? 16.458  -3.912  35.576  1.00 34.65  ? 412 TYR B OH  1 
ATOM   6422 N N   . GLY B 1 384 ? 21.286  -9.761  30.967  1.00 39.74  ? 413 GLY B N   1 
ATOM   6423 C CA  . GLY B 1 384 ? 21.678  -10.964 30.237  1.00 39.26  ? 413 GLY B CA  1 
ATOM   6424 C C   . GLY B 1 384 ? 21.715  -10.777 28.718  1.00 41.31  ? 413 GLY B C   1 
ATOM   6425 O O   . GLY B 1 384 ? 22.191  -11.661 28.007  1.00 38.83  ? 413 GLY B O   1 
ATOM   6426 N N   . MET B 1 385 ? 21.191  -9.644  28.223  1.00 44.56  ? 414 MET B N   1 
ATOM   6427 C CA  . MET B 1 385 ? 21.304  -9.266  26.820  1.00 47.32  ? 414 MET B CA  1 
ATOM   6428 C C   . MET B 1 385 ? 22.698  -8.685  26.597  1.00 45.30  ? 414 MET B C   1 
ATOM   6429 O O   . MET B 1 385 ? 22.912  -7.485  26.763  1.00 45.25  ? 414 MET B O   1 
ATOM   6430 C CB  . MET B 1 385 ? 20.221  -8.242  26.458  1.00 48.88  ? 414 MET B CB  1 
ATOM   6431 C CG  . MET B 1 385 ? 20.324  -7.641  25.067  1.00 49.98  ? 414 MET B CG  1 
ATOM   6432 S SD  . MET B 1 385 ? 19.345  -8.471  23.803  1.00 55.37  ? 414 MET B SD  1 
ATOM   6433 C CE  . MET B 1 385 ? 17.664  -8.309  24.411  1.00 50.27  ? 414 MET B CE  1 
ATOM   6434 N N   . THR B 1 386 ? 23.648  -9.562  26.259  1.00 43.52  ? 415 THR B N   1 
ATOM   6435 C CA  . THR B 1 386 ? 25.056  -9.198  26.226  1.00 45.46  ? 415 THR B CA  1 
ATOM   6436 C C   . THR B 1 386 ? 25.551  -9.094  24.784  1.00 42.78  ? 415 THR B C   1 
ATOM   6437 O O   . THR B 1 386 ? 26.680  -8.679  24.559  1.00 42.24  ? 415 THR B O   1 
ATOM   6438 C CB  . THR B 1 386 ? 25.866  -10.224 27.022  1.00 46.43  ? 415 THR B CB  1 
ATOM   6439 O OG1 . THR B 1 386 ? 25.510  -11.498 26.494  1.00 45.24  ? 415 THR B OG1 1 
ATOM   6440 C CG2 . THR B 1 386 ? 25.570  -10.177 28.510  1.00 48.33  ? 415 THR B CG2 1 
ATOM   6441 N N   . GLU B 1 387 ? 24.698  -9.451  23.819  1.00 44.54  ? 416 GLU B N   1 
ATOM   6442 C CA  . GLU B 1 387 ? 25.082  -9.513  22.416  1.00 47.50  ? 416 GLU B CA  1 
ATOM   6443 C C   . GLU B 1 387 ? 24.991  -8.113  21.800  1.00 44.82  ? 416 GLU B C   1 
ATOM   6444 O O   . GLU B 1 387 ? 24.013  -7.772  21.132  1.00 42.59  ? 416 GLU B O   1 
ATOM   6445 C CB  . GLU B 1 387 ? 24.212  -10.548 21.698  1.00 48.05  ? 416 GLU B CB  1 
ATOM   6446 C CG  . GLU B 1 387 ? 24.274  -11.944 22.319  1.00 49.40  ? 416 GLU B CG  1 
ATOM   6447 C CD  . GLU B 1 387 ? 23.365  -12.235 23.508  1.00 49.52  ? 416 GLU B CD  1 
ATOM   6448 O OE1 . GLU B 1 387 ? 23.440  -13.374 24.006  1.00 50.20  ? 416 GLU B OE1 1 
ATOM   6449 O OE2 . GLU B 1 387 ? 22.576  -11.368 23.938  1.00 50.68  ? 416 GLU B OE2 1 
ATOM   6450 N N   . MET B 1 388 ? 26.028  -7.309  22.050  1.00 40.60  ? 417 MET B N   1 
ATOM   6451 C CA  . MET B 1 388 ? 26.107  -5.933  21.586  1.00 43.42  ? 417 MET B CA  1 
ATOM   6452 C C   . MET B 1 388 ? 25.523  -5.777  20.182  1.00 41.65  ? 417 MET B C   1 
ATOM   6453 O O   . MET B 1 388 ? 24.703  -4.893  19.949  1.00 43.85  ? 417 MET B O   1 
ATOM   6454 C CB  . MET B 1 388 ? 27.566  -5.466  21.551  1.00 47.24  ? 417 MET B CB  1 
ATOM   6455 C CG  . MET B 1 388 ? 28.168  -5.284  22.919  1.00 54.53  ? 417 MET B CG  1 
ATOM   6456 S SD  . MET B 1 388 ? 29.956  -5.493  22.923  1.00 63.63  ? 417 MET B SD  1 
ATOM   6457 C CE  . MET B 1 388 ? 30.233  -5.584  24.699  1.00 63.06  ? 417 MET B CE  1 
ATOM   6458 N N   . ASN B 1 389 ? 25.947  -6.636  19.248  1.00 35.66  ? 418 ASN B N   1 
ATOM   6459 C CA  . ASN B 1 389 ? 25.646  -6.448  17.839  1.00 35.01  ? 418 ASN B CA  1 
ATOM   6460 C C   . ASN B 1 389 ? 24.147  -6.544  17.565  1.00 30.85  ? 418 ASN B C   1 
ATOM   6461 O O   . ASN B 1 389 ? 23.705  -6.210  16.472  1.00 30.98  ? 418 ASN B O   1 
ATOM   6462 C CB  . ASN B 1 389 ? 26.444  -7.412  16.967  1.00 39.51  ? 418 ASN B CB  1 
ATOM   6463 C CG  . ASN B 1 389 ? 27.894  -7.007  16.850  1.00 43.11  ? 418 ASN B CG  1 
ATOM   6464 O OD1 . ASN B 1 389 ? 28.336  -6.061  17.514  1.00 47.68  ? 418 ASN B OD1 1 
ATOM   6465 N ND2 . ASN B 1 389 ? 28.648  -7.711  16.019  1.00 46.33  ? 418 ASN B ND2 1 
ATOM   6466 N N   . TYR B 1 390 ? 23.366  -6.983  18.556  1.00 28.80  ? 419 TYR B N   1 
ATOM   6467 C CA  . TYR B 1 390 ? 21.927  -7.086  18.412  1.00 27.18  ? 419 TYR B CA  1 
ATOM   6468 C C   . TYR B 1 390 ? 21.227  -5.813  18.885  1.00 27.46  ? 419 TYR B C   1 
ATOM   6469 O O   . TYR B 1 390 ? 20.035  -5.651  18.653  1.00 27.13  ? 419 TYR B O   1 
ATOM   6470 C CB  . TYR B 1 390 ? 21.412  -8.280  19.218  1.00 25.94  ? 419 TYR B CB  1 
ATOM   6471 C CG  . TYR B 1 390 ? 19.919  -8.499  19.035  1.00 24.07  ? 419 TYR B CG  1 
ATOM   6472 C CD1 . TYR B 1 390 ? 19.427  -9.031  17.856  1.00 23.08  ? 419 TYR B CD1 1 
ATOM   6473 C CD2 . TYR B 1 390 ? 19.005  -8.150  20.025  1.00 23.63  ? 419 TYR B CD2 1 
ATOM   6474 C CE1 . TYR B 1 390 ? 18.070  -9.227  17.667  1.00 22.70  ? 419 TYR B CE1 1 
ATOM   6475 C CE2 . TYR B 1 390 ? 17.647  -8.338  19.844  1.00 21.57  ? 419 TYR B CE2 1 
ATOM   6476 C CZ  . TYR B 1 390 ? 17.182  -8.889  18.666  1.00 22.51  ? 419 TYR B CZ  1 
ATOM   6477 O OH  . TYR B 1 390 ? 15.847  -9.095  18.448  1.00 25.63  ? 419 TYR B OH  1 
ATOM   6478 N N   . TYR B 1 391 ? 21.955  -4.910  19.544  1.00 28.51  ? 420 TYR B N   1 
ATOM   6479 C CA  . TYR B 1 391 ? 21.312  -3.833  20.282  1.00 31.59  ? 420 TYR B CA  1 
ATOM   6480 C C   . TYR B 1 391 ? 20.561  -2.891  19.338  1.00 31.27  ? 420 TYR B C   1 
ATOM   6481 O O   . TYR B 1 391 ? 19.483  -2.414  19.671  1.00 31.38  ? 420 TYR B O   1 
ATOM   6482 C CB  . TYR B 1 391 ? 22.332  -3.093  21.157  1.00 33.37  ? 420 TYR B CB  1 
ATOM   6483 C CG  . TYR B 1 391 ? 22.881  -3.833  22.377  1.00 32.91  ? 420 TYR B CG  1 
ATOM   6484 C CD1 . TYR B 1 391 ? 22.439  -5.103  22.744  1.00 34.18  ? 420 TYR B CD1 1 
ATOM   6485 C CD2 . TYR B 1 391 ? 23.817  -3.223  23.204  1.00 34.05  ? 420 TYR B CD2 1 
ATOM   6486 C CE1 . TYR B 1 391 ? 22.942  -5.757  23.859  1.00 32.93  ? 420 TYR B CE1 1 
ATOM   6487 C CE2 . TYR B 1 391 ? 24.318  -3.859  24.330  1.00 33.35  ? 420 TYR B CE2 1 
ATOM   6488 C CZ  . TYR B 1 391 ? 23.885  -5.133  24.653  1.00 32.76  ? 420 TYR B CZ  1 
ATOM   6489 O OH  . TYR B 1 391 ? 24.384  -5.768  25.748  1.00 34.57  ? 420 TYR B OH  1 
ATOM   6490 N N   . THR B 1 392 ? 21.095  -2.642  18.142  1.00 33.51  ? 421 THR B N   1 
ATOM   6491 C CA  . THR B 1 392 ? 20.486  -1.650  17.267  1.00 35.43  ? 421 THR B CA  1 
ATOM   6492 C C   . THR B 1 392 ? 19.138  -2.168  16.772  1.00 35.06  ? 421 THR B C   1 
ATOM   6493 O O   . THR B 1 392 ? 18.254  -1.373  16.458  1.00 32.44  ? 421 THR B O   1 
ATOM   6494 C CB  . THR B 1 392 ? 21.414  -1.298  16.104  1.00 36.84  ? 421 THR B CB  1 
ATOM   6495 O OG1 . THR B 1 392 ? 22.659  -0.947  16.703  1.00 36.62  ? 421 THR B OG1 1 
ATOM   6496 C CG2 . THR B 1 392 ? 20.898  -0.130  15.280  1.00 36.15  ? 421 THR B CG2 1 
ATOM   6497 N N   . VAL B 1 393 ? 19.006  -3.499  16.680  1.00 34.22  ? 422 VAL B N   1 
ATOM   6498 C CA  . VAL B 1 393 ? 17.767  -4.137  16.262  1.00 34.50  ? 422 VAL B CA  1 
ATOM   6499 C C   . VAL B 1 393 ? 16.637  -3.713  17.199  1.00 33.63  ? 422 VAL B C   1 
ATOM   6500 O O   . VAL B 1 393 ? 15.517  -3.481  16.754  1.00 31.80  ? 422 VAL B O   1 
ATOM   6501 C CB  . VAL B 1 393 ? 17.920  -5.672  16.207  1.00 34.22  ? 422 VAL B CB  1 
ATOM   6502 C CG1 . VAL B 1 393 ? 16.583  -6.402  16.165  1.00 34.02  ? 422 VAL B CG1 1 
ATOM   6503 C CG2 . VAL B 1 393 ? 18.773  -6.090  15.020  1.00 35.88  ? 422 VAL B CG2 1 
ATOM   6504 N N   . LEU B 1 394 ? 16.939  -3.632  18.496  1.00 35.58  ? 423 LEU B N   1 
ATOM   6505 C CA  . LEU B 1 394 ? 15.967  -3.185  19.480  1.00 37.94  ? 423 LEU B CA  1 
ATOM   6506 C C   . LEU B 1 394 ? 15.578  -1.750  19.148  1.00 37.99  ? 423 LEU B C   1 
ATOM   6507 O O   . LEU B 1 394 ? 14.407  -1.383  19.234  1.00 40.77  ? 423 LEU B O   1 
ATOM   6508 C CB  . LEU B 1 394 ? 16.530  -3.270  20.898  1.00 38.95  ? 423 LEU B CB  1 
ATOM   6509 C CG  . LEU B 1 394 ? 17.040  -4.643  21.344  1.00 42.44  ? 423 LEU B CG  1 
ATOM   6510 C CD1 . LEU B 1 394 ? 17.809  -4.521  22.653  1.00 43.25  ? 423 LEU B CD1 1 
ATOM   6511 C CD2 . LEU B 1 394 ? 15.902  -5.635  21.478  1.00 42.38  ? 423 LEU B CD2 1 
ATOM   6512 N N   . PHE B 1 395 ? 16.594  -0.945  18.819  1.00 35.59  ? 424 PHE B N   1 
ATOM   6513 C CA  . PHE B 1 395 ? 16.389  0.403   18.324  1.00 32.90  ? 424 PHE B CA  1 
ATOM   6514 C C   . PHE B 1 395 ? 15.429  0.331   17.138  1.00 31.08  ? 424 PHE B C   1 
ATOM   6515 O O   . PHE B 1 395 ? 14.371  0.942   17.158  1.00 29.99  ? 424 PHE B O   1 
ATOM   6516 C CB  . PHE B 1 395 ? 17.761  1.004   18.008  1.00 33.07  ? 424 PHE B CB  1 
ATOM   6517 C CG  . PHE B 1 395 ? 17.865  2.523   18.066  1.00 33.63  ? 424 PHE B CG  1 
ATOM   6518 C CD1 . PHE B 1 395 ? 16.773  3.342   17.783  1.00 33.86  ? 424 PHE B CD1 1 
ATOM   6519 C CD2 . PHE B 1 395 ? 19.082  3.127   18.381  1.00 34.09  ? 424 PHE B CD2 1 
ATOM   6520 C CE1 . PHE B 1 395 ? 16.891  4.725   17.827  1.00 32.56  ? 424 PHE B CE1 1 
ATOM   6521 C CE2 . PHE B 1 395 ? 19.198  4.509   18.418  1.00 33.80  ? 424 PHE B CE2 1 
ATOM   6522 C CZ  . PHE B 1 395 ? 18.100  5.303   18.145  1.00 34.51  ? 424 PHE B CZ  1 
ATOM   6523 N N   . GLY B 1 396 ? 15.777  -0.474  16.135  1.00 29.62  ? 425 GLY B N   1 
ATOM   6524 C CA  . GLY B 1 396 ? 14.952  -0.624  14.950  1.00 29.31  ? 425 GLY B CA  1 
ATOM   6525 C C   . GLY B 1 396 ? 13.476  -0.821  15.293  1.00 28.59  ? 425 GLY B C   1 
ATOM   6526 O O   . GLY B 1 396 ? 12.615  -0.137  14.742  1.00 27.71  ? 425 GLY B O   1 
ATOM   6527 N N   . VAL B 1 397 ? 13.185  -1.760  16.204  1.00 27.89  ? 426 VAL B N   1 
ATOM   6528 C CA  . VAL B 1 397 ? 11.810  -2.140  16.482  1.00 25.06  ? 426 VAL B CA  1 
ATOM   6529 C C   . VAL B 1 397 ? 11.075  -0.940  17.085  1.00 24.46  ? 426 VAL B C   1 
ATOM   6530 O O   . VAL B 1 397 ? 9.896   -0.707  16.804  1.00 24.44  ? 426 VAL B O   1 
ATOM   6531 C CB  . VAL B 1 397 ? 11.762  -3.384  17.384  1.00 24.67  ? 426 VAL B CB  1 
ATOM   6532 C CG1 . VAL B 1 397 ? 10.360  -3.634  17.933  1.00 25.94  ? 426 VAL B CG1 1 
ATOM   6533 C CG2 . VAL B 1 397 ? 12.274  -4.623  16.652  1.00 24.03  ? 426 VAL B CG2 1 
ATOM   6534 N N   . SER B 1 398 ? 11.788  -0.158  17.891  1.00 23.17  ? 427 SER B N   1 
ATOM   6535 C CA  . SER B 1 398 ? 11.202  0.998   18.549  1.00 25.06  ? 427 SER B CA  1 
ATOM   6536 C C   . SER B 1 398 ? 10.873  2.095   17.535  1.00 26.72  ? 427 SER B C   1 
ATOM   6537 O O   . SER B 1 398 ? 9.767   2.641   17.529  1.00 26.68  ? 427 SER B O   1 
ATOM   6538 C CB  . SER B 1 398 ? 12.110  1.526   19.606  1.00 24.81  ? 427 SER B CB  1 
ATOM   6539 O OG  . SER B 1 398 ? 11.435  2.560   20.301  1.00 28.51  ? 427 SER B OG  1 
ATOM   6540 N N   . ARG B 1 399 ? 11.848  2.397   16.672  1.00 26.64  ? 428 ARG B N   1 
ATOM   6541 C CA  . ARG B 1 399 ? 11.775  3.537   15.777  1.00 27.55  ? 428 ARG B CA  1 
ATOM   6542 C C   . ARG B 1 399 ? 10.695  3.314   14.719  1.00 29.28  ? 428 ARG B C   1 
ATOM   6543 O O   . ARG B 1 399 ? 10.262  4.273   14.087  1.00 34.54  ? 428 ARG B O   1 
ATOM   6544 C CB  . ARG B 1 399 ? 13.180  3.794   15.225  1.00 26.81  ? 428 ARG B CB  1 
ATOM   6545 C CG  . ARG B 1 399 ? 13.358  4.962   14.268  1.00 26.79  ? 428 ARG B CG  1 
ATOM   6546 C CD  . ARG B 1 399 ? 13.042  6.327   14.854  1.00 27.10  ? 428 ARG B CD  1 
ATOM   6547 N NE  . ARG B 1 399 ? 13.671  6.602   16.154  1.00 26.36  ? 428 ARG B NE  1 
ATOM   6548 C CZ  . ARG B 1 399 ? 14.643  7.475   16.389  1.00 26.70  ? 428 ARG B CZ  1 
ATOM   6549 N NH1 . ARG B 1 399 ? 15.409  7.897   15.396  1.00 30.21  ? 428 ARG B NH1 1 
ATOM   6550 N NH2 . ARG B 1 399 ? 14.881  7.900   17.621  1.00 25.21  ? 428 ARG B NH2 1 
ATOM   6551 N N   . ALA B 1 400 ? 10.248  2.065   14.543  1.00 28.04  ? 429 ALA B N   1 
ATOM   6552 C CA  . ALA B 1 400 ? 9.135   1.755   13.658  1.00 29.90  ? 429 ALA B CA  1 
ATOM   6553 C C   . ALA B 1 400 ? 7.880   2.502   14.108  1.00 31.22  ? 429 ALA B C   1 
ATOM   6554 O O   . ALA B 1 400 ? 7.069   2.938   13.291  1.00 26.92  ? 429 ALA B O   1 
ATOM   6555 C CB  . ALA B 1 400 ? 8.880   0.262   13.644  1.00 28.40  ? 429 ALA B CB  1 
ATOM   6556 N N   . LEU B 1 401 ? 7.700   2.599   15.426  1.00 33.26  ? 430 LEU B N   1 
ATOM   6557 C CA  . LEU B 1 401 ? 6.524   3.257   15.968  1.00 34.23  ? 430 LEU B CA  1 
ATOM   6558 C C   . LEU B 1 401 ? 6.460   4.678   15.415  1.00 32.50  ? 430 LEU B C   1 
ATOM   6559 O O   . LEU B 1 401 ? 5.438   5.077   14.858  1.00 31.91  ? 430 LEU B O   1 
ATOM   6560 C CB  . LEU B 1 401 ? 6.544   3.232   17.497  1.00 32.89  ? 430 LEU B CB  1 
ATOM   6561 C CG  . LEU B 1 401 ? 6.477   1.845   18.142  1.00 33.01  ? 430 LEU B CG  1 
ATOM   6562 C CD1 . LEU B 1 401 ? 6.432   1.942   19.658  1.00 32.31  ? 430 LEU B CD1 1 
ATOM   6563 C CD2 . LEU B 1 401 ? 5.283   1.056   17.626  1.00 33.00  ? 430 LEU B CD2 1 
ATOM   6564 N N   . GLY B 1 402 ? 7.567   5.414   15.560  1.00 29.84  ? 431 GLY B N   1 
ATOM   6565 C CA  . GLY B 1 402 ? 7.623   6.818   15.186  1.00 32.03  ? 431 GLY B CA  1 
ATOM   6566 C C   . GLY B 1 402 ? 7.490   7.027   13.677  1.00 31.87  ? 431 GLY B C   1 
ATOM   6567 O O   . GLY B 1 402 ? 6.663   7.826   13.231  1.00 32.34  ? 431 GLY B O   1 
ATOM   6568 N N   . VAL B 1 403 ? 8.299   6.301   12.894  1.00 29.58  ? 432 VAL B N   1 
ATOM   6569 C CA  . VAL B 1 403 ? 8.413   6.589   11.476  1.00 30.83  ? 432 VAL B CA  1 
ATOM   6570 C C   . VAL B 1 403 ? 7.154   6.119   10.752  1.00 31.08  ? 432 VAL B C   1 
ATOM   6571 O O   . VAL B 1 403 ? 6.757   6.727   9.760   1.00 30.45  ? 432 VAL B O   1 
ATOM   6572 C CB  . VAL B 1 403 ? 9.683   6.021   10.817  1.00 32.32  ? 432 VAL B CB  1 
ATOM   6573 C CG1 . VAL B 1 403 ? 10.928  6.617   11.457  1.00 32.98  ? 432 VAL B CG1 1 
ATOM   6574 C CG2 . VAL B 1 403 ? 9.727   4.494   10.816  1.00 32.46  ? 432 VAL B CG2 1 
ATOM   6575 N N   . LEU B 1 404 ? 6.547   5.025   11.221  1.00 30.64  ? 433 LEU B N   1 
ATOM   6576 C CA  . LEU B 1 404 ? 5.315   4.543   10.617  1.00 29.11  ? 433 LEU B CA  1 
ATOM   6577 C C   . LEU B 1 404 ? 4.184   5.476   11.034  1.00 29.74  ? 433 LEU B C   1 
ATOM   6578 O O   . LEU B 1 404 ? 3.379   5.868   10.197  1.00 30.18  ? 433 LEU B O   1 
ATOM   6579 C CB  . LEU B 1 404 ? 5.044   3.081   10.973  1.00 28.89  ? 433 LEU B CB  1 
ATOM   6580 C CG  . LEU B 1 404 ? 6.096   2.078   10.482  1.00 28.97  ? 433 LEU B CG  1 
ATOM   6581 C CD1 . LEU B 1 404 ? 5.876   0.679   11.003  1.00 29.43  ? 433 LEU B CD1 1 
ATOM   6582 C CD2 . LEU B 1 404 ? 6.123   2.034   8.971   1.00 31.07  ? 433 LEU B CD2 1 
ATOM   6583 N N   . ALA B 1 405 ? 4.166   5.907   12.300  1.00 29.47  ? 434 ALA B N   1 
ATOM   6584 C CA  . ALA B 1 405 ? 3.195   6.912   12.705  1.00 31.95  ? 434 ALA B CA  1 
ATOM   6585 C C   . ALA B 1 405 ? 3.221   8.090   11.729  1.00 31.22  ? 434 ALA B C   1 
ATOM   6586 O O   . ALA B 1 405 ? 2.171   8.542   11.292  1.00 34.43  ? 434 ALA B O   1 
ATOM   6587 C CB  . ALA B 1 405 ? 3.428   7.355   14.134  1.00 33.35  ? 434 ALA B CB  1 
ATOM   6588 N N   . GLN B 1 406 ? 4.416   8.549   11.344  1.00 31.99  ? 435 GLN B N   1 
ATOM   6589 C CA  . GLN B 1 406 ? 4.557   9.692   10.449  1.00 33.32  ? 435 GLN B CA  1 
ATOM   6590 C C   . GLN B 1 406 ? 4.083   9.362   9.032   1.00 32.84  ? 435 GLN B C   1 
ATOM   6591 O O   . GLN B 1 406 ? 3.510   10.220  8.363   1.00 31.87  ? 435 GLN B O   1 
ATOM   6592 C CB  . GLN B 1 406 ? 6.008   10.165  10.359  1.00 36.45  ? 435 GLN B CB  1 
ATOM   6593 C CG  . GLN B 1 406 ? 6.245   11.338  9.408   1.00 38.73  ? 435 GLN B CG  1 
ATOM   6594 C CD  . GLN B 1 406 ? 5.513   12.604  9.804   1.00 40.65  ? 435 GLN B CD  1 
ATOM   6595 O OE1 . GLN B 1 406 ? 5.592   13.062  10.947  1.00 44.06  ? 435 GLN B OE1 1 
ATOM   6596 N NE2 . GLN B 1 406 ? 4.774   13.177  8.866   1.00 41.03  ? 435 GLN B NE2 1 
ATOM   6597 N N   . LEU B 1 407 ? 4.370   8.137   8.566   1.00 30.34  ? 436 LEU B N   1 
ATOM   6598 C CA  . LEU B 1 407 ? 4.160   7.778   7.173   1.00 28.26  ? 436 LEU B CA  1 
ATOM   6599 C C   . LEU B 1 407 ? 2.665   7.781   6.854   1.00 30.66  ? 436 LEU B C   1 
ATOM   6600 O O   . LEU B 1 407 ? 2.240   8.179   5.769   1.00 32.22  ? 436 LEU B O   1 
ATOM   6601 C CB  . LEU B 1 407 ? 4.794   6.408   6.955   1.00 26.33  ? 436 LEU B CB  1 
ATOM   6602 C CG  . LEU B 1 407 ? 4.822   5.896   5.513   1.00 25.40  ? 436 LEU B CG  1 
ATOM   6603 C CD1 . LEU B 1 407 ? 5.716   6.768   4.649   1.00 25.87  ? 436 LEU B CD1 1 
ATOM   6604 C CD2 . LEU B 1 407 ? 5.250   4.444   5.472   1.00 24.20  ? 436 LEU B CD2 1 
ATOM   6605 N N   . ILE B 1 408 ? 1.873   7.325   7.823   1.00 32.55  ? 437 ILE B N   1 
ATOM   6606 C CA  . ILE B 1 408 ? 0.423   7.355   7.735   1.00 35.60  ? 437 ILE B CA  1 
ATOM   6607 C C   . ILE B 1 408 ? -0.034  8.778   7.422   1.00 33.52  ? 437 ILE B C   1 
ATOM   6608 O O   . ILE B 1 408 ? -0.840  8.972   6.521   1.00 33.60  ? 437 ILE B O   1 
ATOM   6609 C CB  . ILE B 1 408 ? -0.201  6.812   9.037   1.00 35.87  ? 437 ILE B CB  1 
ATOM   6610 C CG1 . ILE B 1 408 ? 0.073   5.300   9.189   1.00 34.49  ? 437 ILE B CG1 1 
ATOM   6611 C CG2 . ILE B 1 408 ? -1.698  7.130   9.098   1.00 36.56  ? 437 ILE B CG2 1 
ATOM   6612 C CD1 . ILE B 1 408 ? -0.315  4.715   10.536  1.00 33.60  ? 437 ILE B CD1 1 
ATOM   6613 N N   . TRP B 1 409 ? 0.507   9.752   8.161   1.00 32.11  ? 438 TRP B N   1 
ATOM   6614 C CA  . TRP B 1 409 ? 0.149   11.152  8.013   1.00 34.36  ? 438 TRP B CA  1 
ATOM   6615 C C   . TRP B 1 409 ? 0.685   11.752  6.712   1.00 36.87  ? 438 TRP B C   1 
ATOM   6616 O O   . TRP B 1 409 ? 0.010   12.572  6.097   1.00 44.39  ? 438 TRP B O   1 
ATOM   6617 C CB  . TRP B 1 409 ? 0.643   11.951  9.225   1.00 36.54  ? 438 TRP B CB  1 
ATOM   6618 C CG  . TRP B 1 409 ? -0.279  11.861  10.412  1.00 43.70  ? 438 TRP B CG  1 
ATOM   6619 C CD1 . TRP B 1 409 ? -0.147  11.069  11.515  1.00 46.53  ? 438 TRP B CD1 1 
ATOM   6620 C CD2 . TRP B 1 409 ? -1.503  12.600  10.595  1.00 45.30  ? 438 TRP B CD2 1 
ATOM   6621 N NE1 . TRP B 1 409 ? -1.193  11.271  12.374  1.00 44.65  ? 438 TRP B NE1 1 
ATOM   6622 C CE2 . TRP B 1 409 ? -2.044  12.198  11.836  1.00 46.57  ? 438 TRP B CE2 1 
ATOM   6623 C CE3 . TRP B 1 409 ? -2.189  13.553  9.835   1.00 48.35  ? 438 TRP B CE3 1 
ATOM   6624 C CZ2 . TRP B 1 409 ? -3.241  12.718  12.329  1.00 47.20  ? 438 TRP B CZ2 1 
ATOM   6625 C CZ3 . TRP B 1 409 ? -3.371  14.066  10.323  1.00 49.39  ? 438 TRP B CZ3 1 
ATOM   6626 C CH2 . TRP B 1 409 ? -3.888  13.653  11.554  1.00 48.51  ? 438 TRP B CH2 1 
ATOM   6627 N N   . SER B 1 410 ? 1.892   11.360  6.285   1.00 33.01  ? 439 SER B N   1 
ATOM   6628 C CA  . SER B 1 410 ? 2.454   11.881  5.049   1.00 32.28  ? 439 SER B CA  1 
ATOM   6629 C C   . SER B 1 410 ? 1.537   11.558  3.865   1.00 33.82  ? 439 SER B C   1 
ATOM   6630 O O   . SER B 1 410 ? 1.343   12.394  2.984   1.00 32.80  ? 439 SER B O   1 
ATOM   6631 C CB  . SER B 1 410 ? 3.859   11.370  4.825   1.00 31.26  ? 439 SER B CB  1 
ATOM   6632 O OG  . SER B 1 410 ? 4.752   11.930  5.776   1.00 29.93  ? 439 SER B OG  1 
ATOM   6633 N N   . ARG B 1 411 ? 0.978   10.342  3.850   1.00 34.55  ? 440 ARG B N   1 
ATOM   6634 C CA  . ARG B 1 411 ? 0.145   9.883   2.748   1.00 36.35  ? 440 ARG B CA  1 
ATOM   6635 C C   . ARG B 1 411 ? -1.308  10.319  2.936   1.00 40.41  ? 440 ARG B C   1 
ATOM   6636 O O   . ARG B 1 411 ? -2.095  10.248  1.998   1.00 41.00  ? 440 ARG B O   1 
ATOM   6637 C CB  . ARG B 1 411 ? 0.219   8.360   2.617   1.00 35.60  ? 440 ARG B CB  1 
ATOM   6638 C CG  . ARG B 1 411 ? 1.597   7.807   2.274   1.00 35.99  ? 440 ARG B CG  1 
ATOM   6639 C CD  . ARG B 1 411 ? 2.116   8.152   0.883   1.00 34.38  ? 440 ARG B CD  1 
ATOM   6640 N NE  . ARG B 1 411 ? 2.684   9.500   0.778   1.00 36.05  ? 440 ARG B NE  1 
ATOM   6641 C CZ  . ARG B 1 411 ? 3.750   9.949   1.426   1.00 35.29  ? 440 ARG B CZ  1 
ATOM   6642 N NH1 . ARG B 1 411 ? 4.418   9.146   2.230   1.00 37.54  ? 440 ARG B NH1 1 
ATOM   6643 N NH2 . ARG B 1 411 ? 4.143   11.201  1.276   1.00 35.80  ? 440 ARG B NH2 1 
ATOM   6644 N N   . ALA B 1 412 ? -1.682  10.735  4.152   1.00 45.81  ? 441 ALA B N   1 
ATOM   6645 C CA  . ALA B 1 412 ? -2.994  11.329  4.374   1.00 45.82  ? 441 ALA B CA  1 
ATOM   6646 C C   . ALA B 1 412 ? -2.958  12.807  3.988   1.00 43.94  ? 441 ALA B C   1 
ATOM   6647 O O   . ALA B 1 412 ? -3.932  13.315  3.446   1.00 43.93  ? 441 ALA B O   1 
ATOM   6648 C CB  . ALA B 1 412 ? -3.440  11.135  5.808   1.00 45.45  ? 441 ALA B CB  1 
ATOM   6649 N N   . LEU B 1 413 ? -1.821  13.474  4.244   1.00 41.26  ? 442 LEU B N   1 
ATOM   6650 C CA  . LEU B 1 413 ? -1.661  14.892  3.966   1.00 39.31  ? 442 LEU B CA  1 
ATOM   6651 C C   . LEU B 1 413 ? -1.091  15.107  2.564   1.00 37.53  ? 442 LEU B C   1 
ATOM   6652 O O   . LEU B 1 413 ? -0.770  16.237  2.196   1.00 36.71  ? 442 LEU B O   1 
ATOM   6653 C CB  . LEU B 1 413 ? -0.763  15.510  5.038   1.00 39.97  ? 442 LEU B CB  1 
ATOM   6654 C CG  . LEU B 1 413 ? -1.250  15.379  6.486   1.00 41.93  ? 442 LEU B CG  1 
ATOM   6655 C CD1 . LEU B 1 413 ? -0.186  15.865  7.446   1.00 42.04  ? 442 LEU B CD1 1 
ATOM   6656 C CD2 . LEU B 1 413 ? -2.553  16.129  6.722   1.00 44.75  ? 442 LEU B CD2 1 
ATOM   6657 N N   . GLY B 1 414 ? -0.968  14.018  1.792   1.00 38.41  ? 443 GLY B N   1 
ATOM   6658 C CA  . GLY B 1 414 ? -0.461  14.058  0.428   1.00 36.93  ? 443 GLY B CA  1 
ATOM   6659 C C   . GLY B 1 414 ? 0.854   14.826  0.310   1.00 35.43  ? 443 GLY B C   1 
ATOM   6660 O O   . GLY B 1 414 ? 0.981   15.712  -0.530  1.00 40.07  ? 443 GLY B O   1 
ATOM   6661 N N   . PHE B 1 415 ? 1.836   14.503  1.155   1.00 34.79  ? 444 PHE B N   1 
ATOM   6662 C CA  . PHE B 1 415 ? 3.175   15.034  0.953   1.00 34.57  ? 444 PHE B CA  1 
ATOM   6663 C C   . PHE B 1 415 ? 3.706   14.456  -0.357  1.00 32.94  ? 444 PHE B C   1 
ATOM   6664 O O   . PHE B 1 415 ? 3.511   13.271  -0.636  1.00 27.15  ? 444 PHE B O   1 
ATOM   6665 C CB  . PHE B 1 415 ? 4.136   14.749  2.110   1.00 37.26  ? 444 PHE B CB  1 
ATOM   6666 C CG  . PHE B 1 415 ? 3.849   15.465  3.429   1.00 38.28  ? 444 PHE B CG  1 
ATOM   6667 C CD1 . PHE B 1 415 ? 2.841   16.422  3.540   1.00 39.01  ? 444 PHE B CD1 1 
ATOM   6668 C CD2 . PHE B 1 415 ? 4.619   15.190  4.553   1.00 36.40  ? 444 PHE B CD2 1 
ATOM   6669 C CE1 . PHE B 1 415 ? 2.599   17.058  4.748   1.00 40.29  ? 444 PHE B CE1 1 
ATOM   6670 C CE2 . PHE B 1 415 ? 4.366   15.824  5.759   1.00 39.06  ? 444 PHE B CE2 1 
ATOM   6671 C CZ  . PHE B 1 415 ? 3.361   16.758  5.852   1.00 39.71  ? 444 PHE B CZ  1 
ATOM   6672 N N   . PRO B 1 416 ? 4.343   15.281  -1.221  1.00 34.37  ? 445 PRO B N   1 
ATOM   6673 C CA  . PRO B 1 416 ? 4.842   14.800  -2.511  1.00 35.27  ? 445 PRO B CA  1 
ATOM   6674 C C   . PRO B 1 416 ? 6.303   14.369  -2.442  1.00 35.07  ? 445 PRO B C   1 
ATOM   6675 O O   . PRO B 1 416 ? 7.000   14.658  -1.475  1.00 33.20  ? 445 PRO B O   1 
ATOM   6676 C CB  . PRO B 1 416 ? 4.638   16.054  -3.367  1.00 35.01  ? 445 PRO B CB  1 
ATOM   6677 C CG  . PRO B 1 416 ? 4.996   17.194  -2.421  1.00 34.60  ? 445 PRO B CG  1 
ATOM   6678 C CD  . PRO B 1 416 ? 4.607   16.719  -1.025  1.00 32.95  ? 445 PRO B CD  1 
ATOM   6679 N N   . LEU B 1 417 ? 6.749   13.696  -3.505  1.00 35.88  ? 446 LEU B N   1 
ATOM   6680 C CA  . LEU B 1 417 ? 8.112   13.215  -3.639  1.00 32.66  ? 446 LEU B CA  1 
ATOM   6681 C C   . LEU B 1 417 ? 9.089   14.252  -3.104  1.00 33.57  ? 446 LEU B C   1 
ATOM   6682 O O   . LEU B 1 417 ? 9.074   15.398  -3.545  1.00 37.53  ? 446 LEU B O   1 
ATOM   6683 C CB  . LEU B 1 417 ? 8.343   12.950  -5.126  1.00 32.26  ? 446 LEU B CB  1 
ATOM   6684 C CG  . LEU B 1 417 ? 9.600   12.158  -5.496  1.00 31.29  ? 446 LEU B CG  1 
ATOM   6685 C CD1 . LEU B 1 417 ? 9.450   10.709  -5.138  1.00 30.84  ? 446 LEU B CD1 1 
ATOM   6686 C CD2 . LEU B 1 417 ? 9.897   12.300  -6.970  1.00 30.94  ? 446 LEU B CD2 1 
ATOM   6687 N N   . GLU B 1 418 ? 9.942   13.841  -2.158  1.00 34.36  ? 447 GLU B N   1 
ATOM   6688 C CA  . GLU B 1 418 ? 11.088  14.642  -1.764  1.00 32.21  ? 447 GLU B CA  1 
ATOM   6689 C C   . GLU B 1 418 ? 12.098  14.608  -2.909  1.00 33.13  ? 447 GLU B C   1 
ATOM   6690 O O   . GLU B 1 418 ? 12.500  13.536  -3.369  1.00 31.41  ? 447 GLU B O   1 
ATOM   6691 C CB  . GLU B 1 418 ? 11.688  14.151  -0.446  1.00 33.79  ? 447 GLU B CB  1 
ATOM   6692 C CG  . GLU B 1 418 ? 12.819  15.041  0.064   1.00 36.76  ? 447 GLU B CG  1 
ATOM   6693 C CD  . GLU B 1 418 ? 13.335  14.748  1.465   1.00 41.43  ? 447 GLU B CD  1 
ATOM   6694 O OE1 . GLU B 1 418 ? 14.578  14.756  1.649   1.00 42.75  ? 447 GLU B OE1 1 
ATOM   6695 O OE2 . GLU B 1 418 ? 12.509  14.504  2.377   1.00 41.36  ? 447 GLU B OE2 1 
ATOM   6696 N N   . ARG B 1 419 ? 12.484  15.792  -3.385  1.00 32.53  ? 448 ARG B N   1 
ATOM   6697 C CA  . ARG B 1 419 ? 13.310  15.884  -4.574  1.00 33.33  ? 448 ARG B CA  1 
ATOM   6698 C C   . ARG B 1 419 ? 13.998  17.243  -4.590  1.00 34.90  ? 448 ARG B C   1 
ATOM   6699 O O   . ARG B 1 419 ? 13.646  18.116  -5.379  1.00 34.67  ? 448 ARG B O   1 
ATOM   6700 C CB  . ARG B 1 419 ? 12.465  15.635  -5.826  1.00 34.23  ? 448 ARG B CB  1 
ATOM   6701 C CG  . ARG B 1 419 ? 13.268  15.050  -6.980  1.00 36.62  ? 448 ARG B CG  1 
ATOM   6702 C CD  . ARG B 1 419 ? 14.290  16.005  -7.587  1.00 36.27  ? 448 ARG B CD  1 
ATOM   6703 N NE  . ARG B 1 419 ? 14.934  15.424  -8.773  1.00 36.41  ? 448 ARG B NE  1 
ATOM   6704 C CZ  . ARG B 1 419 ? 16.216  15.541  -9.116  1.00 34.76  ? 448 ARG B CZ  1 
ATOM   6705 N NH1 . ARG B 1 419 ? 16.666  14.911  -10.184 1.00 34.57  ? 448 ARG B NH1 1 
ATOM   6706 N NH2 . ARG B 1 419 ? 17.050  16.274  -8.399  1.00 35.23  ? 448 ARG B NH2 1 
ATOM   6707 N N   . PRO B 1 420 ? 15.019  17.449  -3.729  1.00 36.67  ? 449 PRO B N   1 
ATOM   6708 C CA  . PRO B 1 420 ? 15.755  18.706  -3.707  1.00 38.24  ? 449 PRO B CA  1 
ATOM   6709 C C   . PRO B 1 420 ? 16.641  18.813  -4.944  1.00 37.66  ? 449 PRO B C   1 
ATOM   6710 O O   . PRO B 1 420 ? 16.675  17.902  -5.763  1.00 37.11  ? 449 PRO B O   1 
ATOM   6711 C CB  . PRO B 1 420 ? 16.555  18.649  -2.392  1.00 37.96  ? 449 PRO B CB  1 
ATOM   6712 C CG  . PRO B 1 420 ? 16.743  17.169  -2.135  1.00 40.05  ? 449 PRO B CG  1 
ATOM   6713 C CD  . PRO B 1 420 ? 15.519  16.479  -2.743  1.00 38.85  ? 449 PRO B CD  1 
ATOM   6714 N N   . LYS B 1 421 ? 17.314  19.959  -5.063  1.00 38.41  ? 450 LYS B N   1 
ATOM   6715 C CA  . LYS B 1 421 ? 18.287  20.225  -6.111  1.00 40.55  ? 450 LYS B CA  1 
ATOM   6716 C C   . LYS B 1 421 ? 19.692  20.052  -5.535  1.00 38.48  ? 450 LYS B C   1 
ATOM   6717 O O   . LYS B 1 421 ? 19.986  20.568  -4.454  1.00 38.09  ? 450 LYS B O   1 
ATOM   6718 C CB  . LYS B 1 421 ? 18.079  21.666  -6.601  1.00 43.56  ? 450 LYS B CB  1 
ATOM   6719 C CG  . LYS B 1 421 ? 19.006  22.151  -7.708  1.00 44.59  ? 450 LYS B CG  1 
ATOM   6720 C CD  . LYS B 1 421 ? 18.751  21.455  -9.037  1.00 47.71  ? 450 LYS B CD  1 
ATOM   6721 C CE  . LYS B 1 421 ? 19.664  21.918  -10.128 1.00 47.52  ? 450 LYS B CE  1 
ATOM   6722 N NZ  . LYS B 1 421 ? 19.175  21.428  -11.419 1.00 47.90  ? 450 LYS B NZ  1 
ATOM   6723 N N   . SER B 1 422 ? 20.554  19.338  -6.272  1.00 36.20  ? 451 SER B N   1 
ATOM   6724 C CA  . SER B 1 422 ? 21.943  19.166  -5.880  1.00 34.72  ? 451 SER B CA  1 
ATOM   6725 C C   . SER B 1 422 ? 22.838  20.086  -6.707  1.00 37.18  ? 451 SER B C   1 
ATOM   6726 O O   . SER B 1 422 ? 22.401  20.634  -7.717  1.00 35.47  ? 451 SER B O   1 
ATOM   6727 C CB  . SER B 1 422 ? 22.376  17.728  -6.018  1.00 32.42  ? 451 SER B CB  1 
ATOM   6728 O OG  . SER B 1 422 ? 22.560  17.377  -7.380  1.00 28.79  ? 451 SER B OG  1 
ATOM   6729 N N   . MET B 1 423 ? 24.103  20.213  -6.274  1.00 39.24  ? 452 MET B N   1 
ATOM   6730 C CA  . MET B 1 423 ? 25.105  21.011  -6.966  1.00 39.76  ? 452 MET B CA  1 
ATOM   6731 C C   . MET B 1 423 ? 26.467  20.334  -6.874  1.00 38.18  ? 452 MET B C   1 
ATOM   6732 O O   . MET B 1 423 ? 26.836  19.807  -5.828  1.00 39.43  ? 452 MET B O   1 
ATOM   6733 C CB  . MET B 1 423 ? 25.265  22.401  -6.337  1.00 43.82  ? 452 MET B CB  1 
ATOM   6734 C CG  . MET B 1 423 ? 24.028  23.275  -6.389  1.00 47.85  ? 452 MET B CG  1 
ATOM   6735 S SD  . MET B 1 423 ? 23.533  23.672  -8.076  1.00 59.14  ? 452 MET B SD  1 
ATOM   6736 C CE  . MET B 1 423 ? 24.829  24.828  -8.556  1.00 58.97  ? 452 MET B CE  1 
ATOM   6737 N N   . SER B 1 424 ? 27.232  20.380  -7.969  1.00 36.85  ? 453 SER B N   1 
ATOM   6738 C CA  . SER B 1 424 ? 28.660  20.113  -7.912  1.00 35.84  ? 453 SER B CA  1 
ATOM   6739 C C   . SER B 1 424 ? 29.376  21.323  -7.315  1.00 34.59  ? 453 SER B C   1 
ATOM   6740 O O   . SER B 1 424 ? 28.815  22.415  -7.236  1.00 31.80  ? 453 SER B O   1 
ATOM   6741 C CB  . SER B 1 424 ? 29.215  19.796  -9.273  1.00 37.99  ? 453 SER B CB  1 
ATOM   6742 O OG  . SER B 1 424 ? 29.332  20.978  -10.057 1.00 36.72  ? 453 SER B OG  1 
ATOM   6743 N N   . THR B 1 425 ? 30.625  21.116  -6.903  1.00 36.81  ? 454 THR B N   1 
ATOM   6744 C CA  . THR B 1 425 ? 31.460  22.212  -6.442  1.00 40.31  ? 454 THR B CA  1 
ATOM   6745 C C   . THR B 1 425 ? 31.712  23.144  -7.627  1.00 42.69  ? 454 THR B C   1 
ATOM   6746 O O   . THR B 1 425 ? 31.464  24.346  -7.540  1.00 42.78  ? 454 THR B O   1 
ATOM   6747 C CB  . THR B 1 425 ? 32.732  21.632  -5.825  1.00 41.60  ? 454 THR B CB  1 
ATOM   6748 O OG1 . THR B 1 425 ? 32.251  20.972  -4.657  1.00 38.57  ? 454 THR B OG1 1 
ATOM   6749 C CG2 . THR B 1 425 ? 33.759  22.680  -5.433  1.00 42.04  ? 454 THR B CG2 1 
ATOM   6750 N N   . GLU B 1 426 ? 32.140  22.554  -8.748  1.00 45.11  ? 455 GLU B N   1 
ATOM   6751 C CA  . GLU B 1 426 ? 32.309  23.264  -10.007 1.00 50.66  ? 455 GLU B CA  1 
ATOM   6752 C C   . GLU B 1 426 ? 31.111  24.176  -10.266 1.00 49.10  ? 455 GLU B C   1 
ATOM   6753 O O   . GLU B 1 426 ? 31.277  25.380  -10.458 1.00 51.07  ? 455 GLU B O   1 
ATOM   6754 C CB  . GLU B 1 426 ? 32.496  22.207  -11.099 1.00 57.16  ? 455 GLU B CB  1 
ATOM   6755 C CG  . GLU B 1 426 ? 32.765  22.760  -12.496 1.00 65.34  ? 455 GLU B CG  1 
ATOM   6756 C CD  . GLU B 1 426 ? 32.907  21.687  -13.572 1.00 75.39  ? 455 GLU B CD  1 
ATOM   6757 O OE1 . GLU B 1 426 ? 33.362  22.021  -14.691 1.00 78.41  ? 455 GLU B OE1 1 
ATOM   6758 O OE2 . GLU B 1 426 ? 32.550  20.513  -13.305 1.00 79.95  ? 455 GLU B OE2 1 
ATOM   6759 N N   . GLY B 1 427 ? 29.906  23.585  -10.268 1.00 46.77  ? 456 GLY B N   1 
ATOM   6760 C CA  . GLY B 1 427 ? 28.671  24.306  -10.536 1.00 42.81  ? 456 GLY B CA  1 
ATOM   6761 C C   . GLY B 1 427 ? 28.345  25.324  -9.443  1.00 44.03  ? 456 GLY B C   1 
ATOM   6762 O O   . GLY B 1 427 ? 27.791  26.385  -9.735  1.00 43.60  ? 456 GLY B O   1 
ATOM   6763 N N   . LEU B 1 428 ? 28.664  24.980  -8.185  1.00 43.01  ? 457 LEU B N   1 
ATOM   6764 C CA  . LEU B 1 428 ? 28.497  25.892  -7.063  1.00 44.77  ? 457 LEU B CA  1 
ATOM   6765 C C   . LEU B 1 428 ? 29.360  27.132  -7.272  1.00 48.08  ? 457 LEU B C   1 
ATOM   6766 O O   . LEU B 1 428 ? 28.944  28.236  -6.932  1.00 43.57  ? 457 LEU B O   1 
ATOM   6767 C CB  . LEU B 1 428 ? 28.844  25.249  -5.720  1.00 44.15  ? 457 LEU B CB  1 
ATOM   6768 C CG  . LEU B 1 428 ? 27.671  24.900  -4.802  1.00 45.70  ? 457 LEU B CG  1 
ATOM   6769 C CD1 . LEU B 1 428 ? 28.211  24.284  -3.520  1.00 44.41  ? 457 LEU B CD1 1 
ATOM   6770 C CD2 . LEU B 1 428 ? 26.799  26.114  -4.496  1.00 44.46  ? 457 LEU B CD2 1 
ATOM   6771 N N   . MET B 1 429 ? 30.577  26.924  -7.787  1.00 54.41  ? 458 MET B N   1 
ATOM   6772 C CA  . MET B 1 429 ? 31.538  28.003  -7.938  1.00 58.08  ? 458 MET B CA  1 
ATOM   6773 C C   . MET B 1 429 ? 31.002  29.033  -8.927  1.00 58.35  ? 458 MET B C   1 
ATOM   6774 O O   . MET B 1 429 ? 31.013  30.231  -8.636  1.00 56.47  ? 458 MET B O   1 
ATOM   6775 C CB  . MET B 1 429 ? 32.908  27.482  -8.389  1.00 59.21  ? 458 MET B CB  1 
ATOM   6776 C CG  . MET B 1 429 ? 33.755  26.945  -7.258  1.00 58.91  ? 458 MET B CG  1 
ATOM   6777 S SD  . MET B 1 429 ? 35.227  26.089  -7.851  1.00 66.44  ? 458 MET B SD  1 
ATOM   6778 C CE  . MET B 1 429 ? 36.080  25.785  -6.299  1.00 66.75  ? 458 MET B CE  1 
ATOM   6779 N N   . LYS B 1 430 ? 30.509  28.558  -10.076 1.00 55.09  ? 459 LYS B N   1 
ATOM   6780 C CA  . LYS B 1 430 ? 30.026  29.467  -11.101 1.00 59.81  ? 459 LYS B CA  1 
ATOM   6781 C C   . LYS B 1 430 ? 28.777  30.193  -10.606 1.00 59.57  ? 459 LYS B C   1 
ATOM   6782 O O   . LYS B 1 430 ? 28.557  31.343  -10.973 1.00 64.41  ? 459 LYS B O   1 
ATOM   6783 C CB  . LYS B 1 430 ? 29.768  28.783  -12.448 1.00 61.26  ? 459 LYS B CB  1 
ATOM   6784 C CG  . LYS B 1 430 ? 31.024  28.311  -13.171 1.00 63.02  ? 459 LYS B CG  1 
ATOM   6785 C CD  . LYS B 1 430 ? 30.898  28.281  -14.690 1.00 68.22  ? 459 LYS B CD  1 
ATOM   6786 C CE  . LYS B 1 430 ? 29.660  27.593  -15.176 1.00 73.34  ? 459 LYS B CE  1 
ATOM   6787 N NZ  . LYS B 1 430 ? 29.509  26.249  -14.607 1.00 76.49  ? 459 LYS B NZ  1 
ATOM   6788 N N   . PHE B 1 431 ? 27.970  29.523  -9.773  1.00 57.84  ? 460 PHE B N   1 
ATOM   6789 C CA  . PHE B 1 431 ? 26.723  30.100  -9.299  1.00 56.72  ? 460 PHE B CA  1 
ATOM   6790 C C   . PHE B 1 431 ? 27.021  31.341  -8.457  1.00 58.29  ? 460 PHE B C   1 
ATOM   6791 O O   . PHE B 1 431 ? 26.410  32.384  -8.677  1.00 56.76  ? 460 PHE B O   1 
ATOM   6792 C CB  . PHE B 1 431 ? 25.885  29.065  -8.538  1.00 57.97  ? 460 PHE B CB  1 
ATOM   6793 C CG  . PHE B 1 431 ? 24.595  29.626  -7.952  1.00 56.20  ? 460 PHE B CG  1 
ATOM   6794 C CD1 . PHE B 1 431 ? 23.512  29.925  -8.772  1.00 55.71  ? 460 PHE B CD1 1 
ATOM   6795 C CD2 . PHE B 1 431 ? 24.468  29.855  -6.587  1.00 56.35  ? 460 PHE B CD2 1 
ATOM   6796 C CE1 . PHE B 1 431 ? 22.342  30.446  -8.242  1.00 55.46  ? 460 PHE B CE1 1 
ATOM   6797 C CE2 . PHE B 1 431 ? 23.293  30.375  -6.062  1.00 58.29  ? 460 PHE B CE2 1 
ATOM   6798 C CZ  . PHE B 1 431 ? 22.234  30.670  -6.889  1.00 56.04  ? 460 PHE B CZ  1 
ATOM   6799 N N   . VAL B 1 432 ? 27.961  31.226  -7.504  1.00 61.65  ? 461 VAL B N   1 
ATOM   6800 C CA  . VAL B 1 432 ? 28.288  32.328  -6.606  1.00 61.86  ? 461 VAL B CA  1 
ATOM   6801 C C   . VAL B 1 432 ? 29.009  33.411  -7.408  1.00 62.73  ? 461 VAL B C   1 
ATOM   6802 O O   . VAL B 1 432 ? 28.851  34.594  -7.117  1.00 60.73  ? 461 VAL B O   1 
ATOM   6803 C CB  . VAL B 1 432 ? 29.101  31.928  -5.355  1.00 60.90  ? 461 VAL B CB  1 
ATOM   6804 C CG1 . VAL B 1 432 ? 28.425  30.810  -4.570  1.00 61.63  ? 461 VAL B CG1 1 
ATOM   6805 C CG2 . VAL B 1 432 ? 30.541  31.546  -5.677  1.00 62.60  ? 461 VAL B CG2 1 
ATOM   6806 N N   . ASP B 1 433 ? 29.771  32.991  -8.431  1.00 64.19  ? 462 ASP B N   1 
ATOM   6807 C CA  . ASP B 1 433 ? 30.382  33.894  -9.397  1.00 63.61  ? 462 ASP B CA  1 
ATOM   6808 C C   . ASP B 1 433 ? 29.341  34.353  -10.418 1.00 65.81  ? 462 ASP B C   1 
ATOM   6809 O O   . ASP B 1 433 ? 29.617  34.360  -11.618 1.00 66.60  ? 462 ASP B O   1 
ATOM   6810 C CB  . ASP B 1 433 ? 31.518  33.215  -10.151 1.00 65.28  ? 462 ASP B CB  1 
ATOM   6811 C CG  . ASP B 1 433 ? 32.746  32.818  -9.343  1.00 68.87  ? 462 ASP B CG  1 
ATOM   6812 O OD1 . ASP B 1 433 ? 32.801  33.142  -8.134  1.00 65.55  ? 462 ASP B OD1 1 
ATOM   6813 O OD2 . ASP B 1 433 ? 33.645  32.183  -9.940  1.00 74.57  ? 462 ASP B OD2 1 
ATOM   6814 N N   . SER B 1 434 ? 28.152  34.744  -9.938  1.00 66.34  ? 463 SER B N   1 
ATOM   6815 C CA  . SER B 1 434 ? 27.040  35.110  -10.800 1.00 68.52  ? 463 SER B CA  1 
ATOM   6816 C C   . SER B 1 434 ? 27.499  36.160  -11.824 1.00 71.19  ? 463 SER B C   1 
ATOM   6817 O O   . SER B 1 434 ? 27.447  35.845  -13.034 1.00 76.79  ? 463 SER B O   1 
ATOM   6818 C CB  . SER B 1 434 ? 25.874  35.630  -9.991  1.00 68.13  ? 463 SER B CB  1 
ATOM   6819 O OG  . SER B 1 434 ? 25.818  35.013  -8.712  1.00 71.12  ? 463 SER B OG  1 
HETATM 6820 N N1A . COA C 2 .   ? 0.279   15.165  -18.180 1.00 73.99  ? 501 COA A N1A 1 
HETATM 6821 C C2A . COA C 2 .   ? -0.668  15.872  -17.546 1.00 73.34  ? 501 COA A C2A 1 
HETATM 6822 N N3A . COA C 2 .   ? -0.550  16.715  -16.523 1.00 69.77  ? 501 COA A N3A 1 
HETATM 6823 C C4A . COA C 2 .   ? 0.731   16.810  -16.134 1.00 71.82  ? 501 COA A C4A 1 
HETATM 6824 C C5A . COA C 2 .   ? 1.813   16.151  -16.683 1.00 71.45  ? 501 COA A C5A 1 
HETATM 6825 C C6A . COA C 2 .   ? 1.563   15.287  -17.767 1.00 70.96  ? 501 COA A C6A 1 
HETATM 6826 N N6A . COA C 2 .   ? 2.506   14.589  -18.393 1.00 72.42  ? 501 COA A N6A 1 
HETATM 6827 N N7A . COA C 2 .   ? 2.977   16.506  -16.013 1.00 72.14  ? 501 COA A N7A 1 
HETATM 6828 C C8A . COA C 2 .   ? 2.582   17.352  -15.089 1.00 72.48  ? 501 COA A C8A 1 
HETATM 6829 N N9A . COA C 2 .   ? 1.228   17.578  -15.115 1.00 70.68  ? 501 COA A N9A 1 
HETATM 6830 C C1B . COA C 2 .   ? 0.450   18.446  -14.229 1.00 71.69  ? 501 COA A C1B 1 
HETATM 6831 C C2B . COA C 2 .   ? 0.504   18.052  -12.755 1.00 74.08  ? 501 COA A C2B 1 
HETATM 6832 O O2B . COA C 2 .   ? -0.430  17.057  -12.394 1.00 77.51  ? 501 COA A O2B 1 
HETATM 6833 C C3B . COA C 2 .   ? 0.167   19.377  -12.074 1.00 70.37  ? 501 COA A C3B 1 
HETATM 6834 O O3B . COA C 2 .   ? -1.243  19.543  -11.959 1.00 73.75  ? 501 COA A O3B 1 
HETATM 6835 P P3B . COA C 2 .   ? -1.655  20.347  -10.615 1.00 79.33  ? 501 COA A P3B 1 
HETATM 6836 O O7A . COA C 2 .   ? -1.770  19.310  -9.510  1.00 76.82  ? 501 COA A O7A 1 
HETATM 6837 O O8A . COA C 2 .   ? -2.992  21.006  -10.925 1.00 79.99  ? 501 COA A O8A 1 
HETATM 6838 O O9A . COA C 2 .   ? -0.567  21.372  -10.329 1.00 75.12  ? 501 COA A O9A 1 
HETATM 6839 C C4B . COA C 2 .   ? 0.768   20.417  -13.017 1.00 71.32  ? 501 COA A C4B 1 
HETATM 6840 O O4B . COA C 2 .   ? 0.994   19.742  -14.284 1.00 69.95  ? 501 COA A O4B 1 
HETATM 6841 C C5B . COA C 2 .   ? 2.062   21.025  -12.534 1.00 72.88  ? 501 COA A C5B 1 
HETATM 6842 O O5B . COA C 2 .   ? 2.926   19.975  -12.027 1.00 70.82  ? 501 COA A O5B 1 
HETATM 6843 P P1A . COA C 2 .   ? 4.441   19.917  -12.544 1.00 66.40  ? 501 COA A P1A 1 
HETATM 6844 O O1A . COA C 2 .   ? 4.961   21.304  -12.717 1.00 68.68  ? 501 COA A O1A 1 
HETATM 6845 O O2A . COA C 2 .   ? 4.540   18.981  -13.698 1.00 71.45  ? 501 COA A O2A 1 
HETATM 6846 O O3A . COA C 2 .   ? 5.160   19.262  -11.266 1.00 65.62  ? 501 COA A O3A 1 
HETATM 6847 P P2A . COA C 2 .   ? 5.383   17.817  -10.600 1.00 58.00  ? 501 COA A P2A 1 
HETATM 6848 O O4A . COA C 2 .   ? 6.800   17.745  -10.132 1.00 57.85  ? 501 COA A O4A 1 
HETATM 6849 O O5A . COA C 2 .   ? 4.273   17.550  -9.638  1.00 59.77  ? 501 COA A O5A 1 
HETATM 6850 O O6A . COA C 2 .   ? 5.219   16.805  -11.833 1.00 54.39  ? 501 COA A O6A 1 
HETATM 6851 C CBP . COA C 2 .   ? 5.787   14.535  -12.542 1.00 50.38  ? 501 COA A CBP 1 
HETATM 6852 C CCP . COA C 2 .   ? 6.326   15.912  -12.157 1.00 52.82  ? 501 COA A CCP 1 
HETATM 6853 C CDP . COA C 2 .   ? 6.950   13.694  -13.079 1.00 52.14  ? 501 COA A CDP 1 
HETATM 6854 C CEP . COA C 2 .   ? 5.210   13.847  -11.297 1.00 50.88  ? 501 COA A CEP 1 
HETATM 6855 C CAP . COA C 2 .   ? 4.703   14.684  -13.619 1.00 46.90  ? 501 COA A CAP 1 
HETATM 6856 O OAP . COA C 2 .   ? 5.279   15.390  -14.701 1.00 46.80  ? 501 COA A OAP 1 
HETATM 6857 C C9P . COA C 2 .   ? 4.100   13.381  -14.119 1.00 45.09  ? 501 COA A C9P 1 
HETATM 6858 O O9P . COA C 2 .   ? 3.182   12.864  -13.489 1.00 45.07  ? 501 COA A O9P 1 
HETATM 6859 N N8P . COA C 2 .   ? 4.587   12.864  -15.241 1.00 44.11  ? 501 COA A N8P 1 
HETATM 6860 C C7P . COA C 2 .   ? 4.195   11.555  -15.752 1.00 42.78  ? 501 COA A C7P 1 
HETATM 6861 C C6P . COA C 2 .   ? 4.860   10.417  -14.994 1.00 42.98  ? 501 COA A C6P 1 
HETATM 6862 C C5P . COA C 2 .   ? 6.305   10.190  -15.402 1.00 45.96  ? 501 COA A C5P 1 
HETATM 6863 O O5P . COA C 2 .   ? 6.600   10.002  -16.582 1.00 48.84  ? 501 COA A O5P 1 
HETATM 6864 N N4P . COA C 2 .   ? 7.236   10.204  -14.435 1.00 43.57  ? 501 COA A N4P 1 
HETATM 6865 C C3P . COA C 2 .   ? 8.647   9.912   -14.652 1.00 44.42  ? 501 COA A C3P 1 
HETATM 6866 C C2P . COA C 2 .   ? 9.573   10.978  -14.089 1.00 46.51  ? 501 COA A C2P 1 
HETATM 6867 S S1P . COA C 2 .   ? 9.687   11.029  -12.279 1.00 51.72  ? 501 COA A S1P 1 
HETATM 6868 C C1  . CIT D 3 .   ? 14.613  12.242  -11.074 1.00 42.23  ? 502 CIT A C1  1 
HETATM 6869 O O1  . CIT D 3 .   ? 14.317  12.911  -10.064 1.00 41.13  ? 502 CIT A O1  1 
HETATM 6870 O O2  . CIT D 3 .   ? 15.478  12.611  -11.903 1.00 44.11  ? 502 CIT A O2  1 
HETATM 6871 C C2  . CIT D 3 .   ? 13.856  10.935  -11.288 1.00 41.00  ? 502 CIT A C2  1 
HETATM 6872 C C3  . CIT D 3 .   ? 14.417  9.933   -12.314 1.00 43.01  ? 502 CIT A C3  1 
HETATM 6873 O O7  . CIT D 3 .   ? 13.743  8.696   -12.163 1.00 43.67  ? 502 CIT A O7  1 
HETATM 6874 C C4  . CIT D 3 .   ? 14.169  10.464  -13.730 1.00 43.79  ? 502 CIT A C4  1 
HETATM 6875 C C5  . CIT D 3 .   ? 13.250  9.639   -14.610 1.00 50.49  ? 502 CIT A C5  1 
HETATM 6876 O O3  . CIT D 3 .   ? 12.766  10.211  -15.596 1.00 54.12  ? 502 CIT A O3  1 
HETATM 6877 O O4  . CIT D 3 .   ? 13.026  8.440   -14.314 1.00 56.84  ? 502 CIT A O4  1 
HETATM 6878 C C6  . CIT D 3 .   ? 15.938  9.708   -12.105 1.00 38.76  ? 502 CIT A C6  1 
HETATM 6879 O O5  . CIT D 3 .   ? 16.631  9.550   -13.121 1.00 37.65  ? 502 CIT A O5  1 
HETATM 6880 O O6  . CIT D 3 .   ? 16.364  9.696   -10.944 1.00 36.33  ? 502 CIT A O6  1 
HETATM 6881 O O1  . OAA E 4 .   ? 19.620  12.754  14.347  1.00 68.28  ? 501 OAA B O1  1 
HETATM 6882 O O2  . OAA E 4 .   ? 20.733  10.985  15.020  1.00 72.22  ? 501 OAA B O2  1 
HETATM 6883 O O4  . OAA E 4 .   ? 18.036  8.647   17.841  1.00 65.98  ? 501 OAA B O4  1 
HETATM 6884 O O5  . OAA E 4 .   ? 17.498  9.461   15.930  1.00 54.49  ? 501 OAA B O5  1 
HETATM 6885 O O3  . OAA E 4 .   ? 19.892  10.301  18.004  1.00 54.20  ? 501 OAA B O3  1 
HETATM 6886 C C1  . OAA E 4 .   ? 19.846  11.848  15.168  1.00 67.77  ? 501 OAA B C1  1 
HETATM 6887 C C2  . OAA E 4 .   ? 18.971  11.781  16.416  1.00 65.13  ? 501 OAA B C2  1 
HETATM 6888 C C3  . OAA E 4 .   ? 19.032  10.455  17.149  1.00 61.59  ? 501 OAA B C3  1 
HETATM 6889 C C4  . OAA E 4 .   ? 18.148  9.505   16.973  1.00 60.17  ? 501 OAA B C4  1 
HETATM 6890 N N1A . ACO F 5 .   ? 34.217  14.248  22.305  1.00 125.81 ? 502 ACO B N1A 1 
HETATM 6891 C C2A . ACO F 5 .   ? 35.172  14.710  21.487  1.00 126.91 ? 502 ACO B C2A 1 
HETATM 6892 N N3A . ACO F 5 .   ? 35.050  15.375  20.341  1.00 129.17 ? 502 ACO B N3A 1 
HETATM 6893 C C4A . ACO F 5 .   ? 33.756  15.573  20.042  1.00 130.58 ? 502 ACO B C4A 1 
HETATM 6894 C C5A . ACO F 5 .   ? 32.665  15.164  20.779  1.00 130.55 ? 502 ACO B C5A 1 
HETATM 6895 C C6A . ACO F 5 .   ? 32.921  14.467  21.976  1.00 128.55 ? 502 ACO B C6A 1 
HETATM 6896 N N6A . ACO F 5 .   ? 31.968  14.012  22.784  1.00 132.22 ? 502 ACO B N6A 1 
HETATM 6897 N N7A . ACO F 5 .   ? 31.489  15.550  20.149  1.00 135.78 ? 502 ACO B N7A 1 
HETATM 6898 C C8A . ACO F 5 .   ? 31.882  16.175  19.062  1.00 137.84 ? 502 ACO B C8A 1 
HETATM 6899 N N9A . ACO F 5 .   ? 33.250  16.221  18.946  1.00 135.00 ? 502 ACO B N9A 1 
HETATM 6900 C C1B . ACO F 5 .   ? 34.036  16.827  17.869  1.00 130.59 ? 502 ACO B C1B 1 
HETATM 6901 C C2B . ACO F 5 .   ? 33.903  16.125  16.524  1.00 126.03 ? 502 ACO B C2B 1 
HETATM 6902 O O2B . ACO F 5 .   ? 34.689  14.953  16.479  1.00 117.81 ? 502 ACO B O2B 1 
HETATM 6903 C C3B . ACO F 5 .   ? 34.385  17.238  15.589  1.00 126.20 ? 502 ACO B C3B 1 
HETATM 6904 O O3B . ACO F 5 .   ? 35.812  17.285  15.556  1.00 131.43 ? 502 ACO B O3B 1 
HETATM 6905 P P3B . ACO F 5 .   ? 36.442  17.108  14.078  1.00 129.04 ? 502 ACO B P3B 1 
HETATM 6906 O O7A . ACO F 5 .   ? 35.975  15.762  13.560  1.00 134.01 ? 502 ACO B O7A 1 
HETATM 6907 O O8A . ACO F 5 .   ? 35.915  18.255  13.236  1.00 126.16 ? 502 ACO B O8A 1 
HETATM 6908 O O9A . ACO F 5 .   ? 37.951  17.162  14.250  1.00 123.62 ? 502 ACO B O9A 1 
HETATM 6909 C C4B . ACO F 5 .   ? 33.827  18.499  16.254  1.00 121.98 ? 502 ACO B C4B 1 
HETATM 6910 O O4B . ACO F 5 .   ? 33.573  18.137  17.637  1.00 128.53 ? 502 ACO B O4B 1 
HETATM 6911 C C5B . ACO F 5 .   ? 32.564  19.053  15.640  1.00 115.21 ? 502 ACO B C5B 1 
HETATM 6912 O O5B . ACO F 5 .   ? 31.413  18.406  16.245  1.00 110.28 ? 502 ACO B O5B 1 
HETATM 6913 P P1A . ACO F 5 .   ? 30.052  19.204  16.549  1.00 98.46  ? 502 ACO B P1A 1 
HETATM 6914 O O1A . ACO F 5 .   ? 30.286  20.675  16.459  1.00 100.52 ? 502 ACO B O1A 1 
HETATM 6915 O O2A . ACO F 5 .   ? 29.453  18.679  17.812  1.00 94.25  ? 502 ACO B O2A 1 
HETATM 6916 O O3A . ACO F 5 .   ? 29.154  18.738  15.300  1.00 86.93  ? 502 ACO B O3A 1 
HETATM 6917 P P2A . ACO F 5 .   ? 28.967  17.298  14.616  1.00 81.47  ? 502 ACO B P2A 1 
HETATM 6918 O O4A . ACO F 5 .   ? 27.658  17.231  13.896  1.00 70.61  ? 502 ACO B O4A 1 
HETATM 6919 O O5A . ACO F 5 .   ? 30.221  16.965  13.879  1.00 88.06  ? 502 ACO B O5A 1 
HETATM 6920 O O6A . ACO F 5 .   ? 28.875  16.372  15.925  1.00 87.48  ? 502 ACO B O6A 1 
HETATM 6921 C CBP . ACO F 5 .   ? 28.317  14.175  16.795  1.00 87.92  ? 502 ACO B CBP 1 
HETATM 6922 C CCP . ACO F 5 .   ? 29.242  14.958  15.863  1.00 90.32  ? 502 ACO B CCP 1 
HETATM 6923 C CDP . ACO F 5 .   ? 28.333  14.843  18.177  1.00 87.56  ? 502 ACO B CDP 1 
HETATM 6924 C CEP . ACO F 5 .   ? 26.893  14.245  16.225  1.00 90.70  ? 502 ACO B CEP 1 
HETATM 6925 C CAP . ACO F 5 .   ? 28.703  12.694  16.945  1.00 89.36  ? 502 ACO B CAP 1 
HETATM 6926 O OAP . ACO F 5 .   ? 28.989  12.158  15.662  1.00 83.70  ? 502 ACO B OAP 1 
HETATM 6927 C C9P . ACO F 5 .   ? 29.862  12.388  17.883  1.00 91.45  ? 502 ACO B C9P 1 
HETATM 6928 O O9P . ACO F 5 .   ? 31.013  12.658  17.546  1.00 90.43  ? 502 ACO B O9P 1 
HETATM 6929 N N8P . ACO F 5 .   ? 29.557  11.835  19.053  1.00 91.97  ? 502 ACO B N8P 1 
HETATM 6930 C C7P . ACO F 5 .   ? 30.527  11.142  19.892  1.00 91.16  ? 502 ACO B C7P 1 
HETATM 6931 C C6P . ACO F 5 .   ? 30.281  9.655   19.924  1.00 91.38  ? 502 ACO B C6P 1 
HETATM 6932 C C5P . ACO F 5 .   ? 29.834  9.141   18.571  1.00 94.20  ? 502 ACO B C5P 1 
HETATM 6933 O O5P . ACO F 5 .   ? 30.655  8.756   17.740  1.00 96.85  ? 502 ACO B O5P 1 
HETATM 6934 N N4P . ACO F 5 .   ? 28.518  9.145   18.328  1.00 88.70  ? 502 ACO B N4P 1 
HETATM 6935 C C3P . ACO F 5 .   ? 27.925  8.721   17.070  1.00 82.22  ? 502 ACO B C3P 1 
HETATM 6936 C C2P . ACO F 5 .   ? 26.580  9.362   16.839  1.00 83.08  ? 502 ACO B C2P 1 
HETATM 6937 S S1P . ACO F 5 .   ? 25.489  9.304   18.281  1.00 87.06  ? 502 ACO B S1P 1 
HETATM 6938 C C   . ACO F 5 .   ? 23.858  9.978   18.110  1.00 86.56  ? 502 ACO B C   1 
HETATM 6939 O O   . ACO F 5 .   ? 23.033  9.988   18.992  1.00 84.64  ? 502 ACO B O   1 
HETATM 6940 C CH3 . ACO F 5 .   ? 23.616  10.538  16.753  1.00 84.46  ? 502 ACO B CH3 1 
HETATM 6941 O O   . HOH G 6 .   ? 15.427  -16.885 0.448   1.00 40.39  ? 601 HOH A O   1 
HETATM 6942 O O   . HOH G 6 .   ? 33.910  8.503   12.023  1.00 32.29  ? 602 HOH A O   1 
HETATM 6943 O O   . HOH G 6 .   ? 15.398  13.236  -2.749  1.00 40.09  ? 603 HOH A O   1 
HETATM 6944 O O   . HOH G 6 .   ? 32.613  10.845  5.405   1.00 31.62  ? 604 HOH A O   1 
HETATM 6945 O O   . HOH G 6 .   ? 23.052  14.969  -21.627 1.00 38.13  ? 605 HOH A O   1 
HETATM 6946 O O   . HOH G 6 .   ? 7.982   20.394  -8.628  1.00 48.70  ? 606 HOH A O   1 
HETATM 6947 O O   . HOH G 6 .   ? 6.361   18.819  -15.489 1.00 38.93  ? 607 HOH A O   1 
HETATM 6948 O O   . HOH G 6 .   ? 29.949  -0.600  -27.974 1.00 36.33  ? 608 HOH A O   1 
HETATM 6949 O O   . HOH G 6 .   ? 33.197  3.286   -22.593 1.00 43.43  ? 609 HOH A O   1 
HETATM 6950 O O   . HOH G 6 .   ? 21.623  6.895   -29.521 1.00 37.31  ? 610 HOH A O   1 
HETATM 6951 O O   . HOH G 6 .   ? 20.124  8.638   -15.674 1.00 24.62  ? 611 HOH A O   1 
HETATM 6952 O O   . HOH G 6 .   ? 41.944  1.210   -16.179 1.00 77.01  ? 612 HOH A O   1 
HETATM 6953 O O   . HOH G 6 .   ? 12.263  19.982  -25.915 1.00 44.94  ? 613 HOH A O   1 
HETATM 6954 O O   . HOH G 6 .   ? 4.359   20.391  17.600  1.00 31.59  ? 614 HOH A O   1 
HETATM 6955 O O   . HOH G 6 .   ? 43.721  7.610   1.805   1.00 36.28  ? 615 HOH A O   1 
HETATM 6956 O O   . HOH G 6 .   ? 34.789  -12.880 -7.875  1.00 35.64  ? 616 HOH A O   1 
HETATM 6957 O O   . HOH G 6 .   ? 32.652  19.497  -9.042  1.00 39.08  ? 617 HOH A O   1 
HETATM 6958 O O   . HOH G 6 .   ? 32.207  12.528  -7.767  1.00 61.00  ? 618 HOH A O   1 
HETATM 6959 O O   . HOH G 6 .   ? 29.549  11.117  7.134   1.00 35.52  ? 619 HOH A O   1 
HETATM 6960 O O   . HOH G 6 .   ? 29.344  5.537   3.518   1.00 28.63  ? 620 HOH A O   1 
HETATM 6961 O O   . HOH G 6 .   ? 29.400  -2.869  -20.783 1.00 34.08  ? 621 HOH A O   1 
HETATM 6962 O O   . HOH G 6 .   ? 18.861  14.420  -18.260 1.00 35.95  ? 622 HOH A O   1 
HETATM 6963 O O   . HOH G 6 .   ? 44.552  1.082   -1.573  1.00 39.01  ? 623 HOH A O   1 
HETATM 6964 O O   . HOH G 6 .   ? 6.210   -6.099  -22.771 1.00 64.99  ? 624 HOH A O   1 
HETATM 6965 O O   . HOH G 6 .   ? 25.700  8.230   -3.157  1.00 28.05  ? 625 HOH A O   1 
HETATM 6966 O O   . HOH G 6 .   ? 31.199  -8.560  -13.425 1.00 34.25  ? 626 HOH A O   1 
HETATM 6967 O O   . HOH G 6 .   ? 39.364  6.932   -25.221 1.00 46.87  ? 627 HOH A O   1 
HETATM 6968 O O   . HOH G 6 .   ? 36.739  16.384  9.696   1.00 54.10  ? 628 HOH A O   1 
HETATM 6969 O O   . HOH G 6 .   ? -7.246  6.603   -37.763 1.00 73.36  ? 629 HOH A O   1 
HETATM 6970 O O   . HOH G 6 .   ? 37.507  -15.585 -18.011 1.00 44.00  ? 630 HOH A O   1 
HETATM 6971 O O   . HOH G 6 .   ? 27.538  12.143  2.629   1.00 28.05  ? 631 HOH A O   1 
HETATM 6972 O O   . HOH G 6 .   ? 43.705  21.180  -6.624  1.00 39.32  ? 632 HOH A O   1 
HETATM 6973 O O   . HOH G 6 .   ? 10.484  8.682   -30.865 1.00 34.10  ? 633 HOH A O   1 
HETATM 6974 O O   . HOH G 6 .   ? 38.356  9.061   3.284   1.00 49.08  ? 634 HOH A O   1 
HETATM 6975 O O   . HOH G 6 .   ? 33.892  -14.283 -9.954  1.00 54.54  ? 635 HOH A O   1 
HETATM 6976 O O   . HOH G 6 .   ? 27.007  9.854   -1.445  1.00 29.22  ? 636 HOH A O   1 
HETATM 6977 O O   . HOH G 6 .   ? 29.257  13.624  10.500  1.00 35.19  ? 637 HOH A O   1 
HETATM 6978 O O   . HOH G 6 .   ? -4.449  15.348  -16.275 1.00 46.52  ? 638 HOH A O   1 
HETATM 6979 O O   . HOH G 6 .   ? 44.952  16.159  -11.328 1.00 50.44  ? 639 HOH A O   1 
HETATM 6980 O O   . HOH G 6 .   ? 17.050  16.627  -25.935 1.00 42.71  ? 640 HOH A O   1 
HETATM 6981 O O   . HOH G 6 .   ? 5.231   8.676   -35.972 1.00 44.99  ? 641 HOH A O   1 
HETATM 6982 O O   . HOH G 6 .   ? 33.523  2.108   -32.081 1.00 39.37  ? 642 HOH A O   1 
HETATM 6983 O O   . HOH G 6 .   ? 7.653   29.637  -1.170  1.00 60.66  ? 643 HOH A O   1 
HETATM 6984 O O   . HOH G 6 .   ? 24.592  15.452  2.826   1.00 35.79  ? 644 HOH A O   1 
HETATM 6985 O O   . HOH G 6 .   ? 41.048  5.460   -26.581 1.00 56.70  ? 645 HOH A O   1 
HETATM 6986 O O   . HOH G 6 .   ? 10.513  26.111  -14.434 1.00 53.47  ? 646 HOH A O   1 
HETATM 6987 O O   . HOH G 6 .   ? 31.745  21.091  -23.622 1.00 55.57  ? 647 HOH A O   1 
HETATM 6988 O O   . HOH G 6 .   ? 41.434  -1.090  0.907   1.00 37.55  ? 648 HOH A O   1 
HETATM 6989 O O   . HOH G 6 .   ? 26.151  16.985  0.369   1.00 30.75  ? 649 HOH A O   1 
HETATM 6990 O O   . HOH G 6 .   ? 13.255  10.936  -7.892  1.00 44.07  ? 650 HOH A O   1 
HETATM 6991 O O   . HOH G 6 .   ? 36.118  3.097   -28.930 1.00 36.92  ? 651 HOH A O   1 
HETATM 6992 O O   . HOH G 6 .   ? 16.091  27.199  -7.337  1.00 41.43  ? 652 HOH A O   1 
HETATM 6993 O O   . HOH G 6 .   ? 32.846  8.535   14.058  1.00 44.33  ? 653 HOH A O   1 
HETATM 6994 O O   . HOH G 6 .   ? 41.062  17.362  -17.073 1.00 49.42  ? 654 HOH A O   1 
HETATM 6995 O O   . HOH G 6 .   ? 41.045  0.923   2.169   1.00 44.95  ? 655 HOH A O   1 
HETATM 6996 O O   . HOH G 6 .   ? -5.775  17.017  -38.242 1.00 59.80  ? 656 HOH A O   1 
HETATM 6997 O O   . HOH G 6 .   ? 27.852  -9.417  -28.987 1.00 46.80  ? 657 HOH A O   1 
HETATM 6998 O O   . HOH G 6 .   ? 8.013   14.947  -33.305 1.00 51.48  ? 658 HOH A O   1 
HETATM 6999 O O   . HOH G 6 .   ? 33.392  -19.016 -19.695 1.00 40.46  ? 659 HOH A O   1 
HETATM 7000 O O   . HOH G 6 .   ? 36.845  -17.012 -19.919 1.00 50.71  ? 660 HOH A O   1 
HETATM 7001 O O   . HOH G 6 .   ? 36.202  20.585  2.627   1.00 45.31  ? 661 HOH A O   1 
HETATM 7002 O O   . HOH G 6 .   ? 1.999   16.396  -36.976 1.00 64.22  ? 662 HOH A O   1 
HETATM 7003 O O   . HOH G 6 .   ? 7.794   28.169  17.848  1.00 62.63  ? 663 HOH A O   1 
HETATM 7004 O O   . HOH G 6 .   ? -0.127  6.709   -15.232 1.00 42.01  ? 664 HOH A O   1 
HETATM 7005 O O   . HOH G 6 .   ? 8.236   25.431  -5.690  1.00 56.92  ? 665 HOH A O   1 
HETATM 7006 O O   . HOH G 6 .   ? 6.586   24.889  -7.465  1.00 46.22  ? 666 HOH A O   1 
HETATM 7007 O O   . HOH G 6 .   ? 1.725   -3.655  -11.837 1.00 44.63  ? 667 HOH A O   1 
HETATM 7008 O O   . HOH G 6 .   ? 8.338   -23.597 -13.032 1.00 38.06  ? 668 HOH A O   1 
HETATM 7009 O O   . HOH H 6 .   ? 41.948  6.329   40.230  1.00 54.77  ? 601 HOH B O   1 
HETATM 7010 O O   . HOH H 6 .   ? 12.136  -10.317 18.984  1.00 55.98  ? 602 HOH B O   1 
HETATM 7011 O O   . HOH H 6 .   ? 23.103  -3.793  16.591  1.00 32.72  ? 603 HOH B O   1 
HETATM 7012 O O   . HOH H 6 .   ? 35.055  16.927  11.386  1.00 36.67  ? 604 HOH B O   1 
HETATM 7013 O O   . HOH H 6 .   ? 13.411  7.285   34.152  1.00 42.70  ? 605 HOH B O   1 
HETATM 7014 O O   . HOH H 6 .   ? -2.457  5.427   -7.462  1.00 47.25  ? 606 HOH B O   1 
HETATM 7015 O O   . HOH H 6 .   ? 6.736   9.593   2.902   1.00 32.87  ? 607 HOH B O   1 
HETATM 7016 O O   . HOH H 6 .   ? 14.174  -0.695  42.648  1.00 46.67  ? 608 HOH B O   1 
HETATM 7017 O O   . HOH H 6 .   ? 7.337   5.037   8.041   1.00 38.94  ? 609 HOH B O   1 
HETATM 7018 O O   . HOH H 6 .   ? 36.737  25.648  27.456  1.00 52.73  ? 610 HOH B O   1 
HETATM 7019 O O   . HOH H 6 .   ? 1.534   11.349  -0.468  1.00 45.16  ? 611 HOH B O   1 
HETATM 7020 O O   . HOH H 6 .   ? 18.796  12.971  7.842   1.00 30.02  ? 612 HOH B O   1 
HETATM 7021 O O   . HOH H 6 .   ? -9.697  -4.919  -6.951  1.00 45.98  ? 613 HOH B O   1 
HETATM 7022 O O   . HOH H 6 .   ? 17.245  -11.233 32.588  1.00 37.47  ? 614 HOH B O   1 
HETATM 7023 O O   . HOH H 6 .   ? 24.811  17.641  -8.627  1.00 36.86  ? 615 HOH B O   1 
HETATM 7024 O O   . HOH H 6 .   ? 3.872   -0.903  32.519  1.00 53.07  ? 616 HOH B O   1 
HETATM 7025 O O   . HOH H 6 .   ? 17.778  0.526   35.733  1.00 56.60  ? 617 HOH B O   1 
HETATM 7026 O O   . HOH H 6 .   ? -1.797  15.178  16.465  1.00 48.17  ? 618 HOH B O   1 
HETATM 7027 O O   . HOH H 6 .   ? 30.687  28.384  8.740   1.00 48.81  ? 619 HOH B O   1 
HETATM 7028 O O   . HOH H 6 .   ? -4.497  9.379   1.301   1.00 33.27  ? 620 HOH B O   1 
HETATM 7029 O O   . HOH H 6 .   ? -8.540  1.760   -10.484 1.00 33.16  ? 621 HOH B O   1 
HETATM 7030 O O   . HOH H 6 .   ? 15.842  14.024  23.012  1.00 42.25  ? 622 HOH B O   1 
HETATM 7031 O O   . HOH H 6 .   ? -12.101 13.912  14.697  1.00 44.25  ? 623 HOH B O   1 
HETATM 7032 O O   . HOH H 6 .   ? 21.458  -16.127 11.346  1.00 39.88  ? 624 HOH B O   1 
HETATM 7033 O O   . HOH H 6 .   ? -2.230  -17.305 25.060  1.00 48.18  ? 625 HOH B O   1 
HETATM 7034 O O   . HOH H 6 .   ? 9.238   17.887  13.615  1.00 36.30  ? 626 HOH B O   1 
HETATM 7035 O O   . HOH H 6 .   ? 20.633  11.051  12.114  1.00 34.33  ? 627 HOH B O   1 
HETATM 7036 O O   . HOH H 6 .   ? 16.789  -24.018 2.696   1.00 35.65  ? 628 HOH B O   1 
HETATM 7037 O O   . HOH H 6 .   ? 22.260  -13.993 26.320  1.00 41.86  ? 629 HOH B O   1 
HETATM 7038 O O   . HOH H 6 .   ? 4.434   -13.303 29.398  1.00 96.85  ? 630 HOH B O   1 
HETATM 7039 O O   . HOH H 6 .   ? 20.297  -15.295 25.656  1.00 37.08  ? 631 HOH B O   1 
HETATM 7040 O O   . HOH H 6 .   ? -17.473 11.209  11.089  1.00 52.28  ? 632 HOH B O   1 
HETATM 7041 O O   . HOH H 6 .   ? 7.848   4.817   41.040  1.00 46.35  ? 633 HOH B O   1 
HETATM 7042 O O   . HOH H 6 .   ? 12.331  9.849   14.378  1.00 21.13  ? 634 HOH B O   1 
HETATM 7043 O O   . HOH H 6 .   ? 27.982  7.860   30.590  1.00 42.26  ? 635 HOH B O   1 
HETATM 7044 O O   . HOH H 6 .   ? 16.577  -9.010  2.083   1.00 59.20  ? 636 HOH B O   1 
HETATM 7045 O O   . HOH H 6 .   ? 14.003  8.617   20.343  1.00 34.27  ? 637 HOH B O   1 
HETATM 7046 O O   . HOH H 6 .   ? 1.040   3.576   27.260  1.00 42.45  ? 638 HOH B O   1 
HETATM 7047 O O   . HOH H 6 .   ? 19.450  -24.104 5.301   1.00 45.75  ? 639 HOH B O   1 
HETATM 7048 O O   . HOH H 6 .   ? 17.214  -1.600  2.518   1.00 51.78  ? 640 HOH B O   1 
HETATM 7049 O O   . HOH H 6 .   ? 28.903  -8.999  28.187  1.00 65.85  ? 641 HOH B O   1 
HETATM 7050 O O   . HOH H 6 .   ? 30.974  -9.109  16.454  1.00 40.20  ? 642 HOH B O   1 
HETATM 7051 O O   . HOH H 6 .   ? 25.785  -14.798 23.813  1.00 35.82  ? 643 HOH B O   1 
HETATM 7052 O O   . HOH H 6 .   ? 12.564  10.978  32.335  1.00 43.68  ? 644 HOH B O   1 
HETATM 7053 O O   . HOH H 6 .   ? -0.658  -2.143  -12.756 1.00 48.11  ? 645 HOH B O   1 
HETATM 7054 O O   . HOH H 6 .   ? -9.956  10.741  6.566   1.00 46.86  ? 646 HOH B O   1 
HETATM 7055 O O   . HOH H 6 .   ? 21.002  23.162  17.735  1.00 56.64  ? 647 HOH B O   1 
HETATM 7056 O O   . HOH H 6 .   ? 10.484  1.375   36.851  1.00 45.26  ? 648 HOH B O   1 
HETATM 7057 O O   . HOH H 6 .   ? -5.124  13.619  25.000  1.00 49.82  ? 649 HOH B O   1 
HETATM 7058 O O   . HOH H 6 .   ? 10.024  15.912  2.145   1.00 42.14  ? 650 HOH B O   1 
HETATM 7059 O O   . HOH H 6 .   ? -8.764  -1.105  -8.561  1.00 44.26  ? 651 HOH B O   1 
HETATM 7060 O O   . HOH H 6 .   ? 28.732  29.122  7.240   1.00 48.05  ? 652 HOH B O   1 
HETATM 7061 O O   . HOH H 6 .   ? 4.836   13.666  -5.746  1.00 34.90  ? 653 HOH B O   1 
HETATM 7062 O O   . HOH H 6 .   ? 25.762  -4.079  32.639  1.00 42.59  ? 654 HOH B O   1 
HETATM 7063 O O   . HOH H 6 .   ? 10.204  -20.408 15.665  1.00 56.74  ? 655 HOH B O   1 
HETATM 7064 O O   . HOH H 6 .   ? -5.389  -7.617  -6.492  1.00 45.69  ? 656 HOH B O   1 
HETATM 7065 O O   . HOH H 6 .   ? -8.307  -2.060  10.761  1.00 45.63  ? 657 HOH B O   1 
HETATM 7066 O O   . HOH H 6 .   ? -3.301  28.851  8.929   1.00 45.67  ? 658 HOH B O   1 
HETATM 7067 O O   . HOH H 6 .   ? 8.072   8.734   7.895   1.00 30.89  ? 659 HOH B O   1 
HETATM 7068 O O   . HOH H 6 .   ? 37.460  7.105   31.906  1.00 63.52  ? 660 HOH B O   1 
HETATM 7069 O O   . HOH H 6 .   ? 24.092  -3.348  47.619  1.00 47.59  ? 661 HOH B O   1 
HETATM 7070 O O   . HOH H 6 .   ? -15.812 -0.911  20.450  1.00 40.39  ? 662 HOH B O   1 
HETATM 7071 O O   . HOH H 6 .   ? 28.037  -2.968  16.434  1.00 39.67  ? 663 HOH B O   1 
HETATM 7072 O O   . HOH H 6 .   ? -6.620  7.650   9.344   1.00 69.24  ? 664 HOH B O   1 
HETATM 7073 O O   . HOH H 6 .   ? 31.428  16.090  39.547  1.00 50.13  ? 665 HOH B O   1 
HETATM 7074 O O   . HOH H 6 .   ? 16.913  16.861  30.075  1.00 40.40  ? 666 HOH B O   1 
HETATM 7075 O O   . HOH H 6 .   ? 2.693   32.336  -7.129  1.00 47.67  ? 667 HOH B O   1 
HETATM 7076 O O   . HOH H 6 .   ? -0.751  19.486  -1.609  1.00 46.52  ? 668 HOH B O   1 
HETATM 7077 O O   . HOH H 6 .   ? 49.066  11.190  20.816  1.00 50.05  ? 669 HOH B O   1 
HETATM 7078 O O   . HOH H 6 .   ? -8.173  3.630   34.054  1.00 47.18  ? 670 HOH B O   1 
HETATM 7079 O O   . HOH H 6 .   ? 33.176  33.714  -13.632 1.00 54.81  ? 671 HOH B O   1 
HETATM 7080 O O   . HOH H 6 .   ? -12.560 18.566  17.427  1.00 52.00  ? 672 HOH B O   1 
HETATM 7081 O O   . HOH H 6 .   ? 38.842  17.802  9.720   1.00 42.92  ? 673 HOH B O   1 
HETATM 7082 O O   . HOH H 6 .   ? 37.709  -5.834  23.941  1.00 35.57  ? 674 HOH B O   1 
# 
