data_8ZVU
# 
_entry.id   8ZVU 
# 
_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   8ZVU         pdb_00008zvu 10.2210/pdb8zvu/pdb 
WWPDB D_1300048626 ?            ?                   
# 
_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                        8ZVU 
_pdbx_database_status.recvd_initial_deposition_date   2024-06-12 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              yl521gl@ustc.edu.cn 
_pdbx_contact_author.name_first         Lin 
_pdbx_contact_author.name_last          Yang 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-1550-6947 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Yang, L.Y.' 1 0000-0003-1550-6947 
'Fang, Y.J.' 2 0009-0009-0272-0830 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Human citrate synthase intermediate 4' 
_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 'CITRIC ACID'                     192.124   1   ?       ? ? ? 
3 non-polymer syn 'COENZYME A'                      767.534   1   ?       ? ? ? 
4 non-polymer syn 'OXALOACETATE ION'                131.064   1   ?       ? ? ? 
5 water       nat water                             18.015    345 ?       ? ? ? 
# 
_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 'CITRIC ACID'      CIT 
3 'COENZYME A'       COA 
4 'OXALOACETATE ION' OAA 
5 water              HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   THR n 
1 3   ASN n 
1 4   LEU n 
1 5   LYS n 
1 6   ASP n 
1 7   ILE n 
1 8   LEU n 
1 9   ALA n 
1 10  ASP n 
1 11  LEU n 
1 12  ILE n 
1 13  PRO n 
1 14  LYS n 
1 15  GLU n 
1 16  GLN n 
1 17  ALA n 
1 18  ARG n 
1 19  ILE n 
1 20  LYS n 
1 21  THR n 
1 22  PHE n 
1 23  ARG n 
1 24  GLN n 
1 25  GLN n 
1 26  HIS n 
1 27  GLY n 
1 28  LYS n 
1 29  THR n 
1 30  VAL n 
1 31  VAL n 
1 32  GLY n 
1 33  GLN n 
1 34  ILE n 
1 35  THR n 
1 36  VAL n 
1 37  ASP n 
1 38  MET n 
1 39  MET n 
1 40  TYR n 
1 41  GLY n 
1 42  GLY n 
1 43  MET n 
1 44  ARG n 
1 45  GLY n 
1 46  MET n 
1 47  LYS n 
1 48  GLY n 
1 49  LEU n 
1 50  VAL n 
1 51  TYR n 
1 52  GLU n 
1 53  THR n 
1 54  SER n 
1 55  VAL n 
1 56  LEU n 
1 57  ASP n 
1 58  PRO n 
1 59  ASP n 
1 60  GLU n 
1 61  GLY n 
1 62  ILE n 
1 63  ARG n 
1 64  PHE n 
1 65  ARG n 
1 66  GLY n 
1 67  PHE n 
1 68  SER n 
1 69  ILE n 
1 70  PRO n 
1 71  GLU n 
1 72  CYS n 
1 73  GLN n 
1 74  LYS n 
1 75  LEU n 
1 76  LEU n 
1 77  PRO n 
1 78  LYS n 
1 79  ALA n 
1 80  LYS n 
1 81  GLY n 
1 82  GLY n 
1 83  GLU n 
1 84  GLU n 
1 85  PRO n 
1 86  LEU n 
1 87  PRO n 
1 88  GLU n 
1 89  GLY n 
1 90  LEU n 
1 91  PHE n 
1 92  TRP n 
1 93  LEU n 
1 94  LEU n 
1 95  VAL n 
1 96  THR n 
1 97  GLY n 
1 98  HIS n 
1 99  ILE n 
1 100 PRO n 
1 101 THR n 
1 102 GLU n 
1 103 GLU n 
1 104 GLN n 
1 105 VAL n 
1 106 SER n 
1 107 TRP n 
1 108 LEU n 
1 109 SER n 
1 110 LYS n 
1 111 GLU n 
1 112 TRP n 
1 113 ALA n 
1 114 LYS n 
1 115 ARG n 
1 116 ALA n 
1 117 ALA n 
1 118 LEU n 
1 119 PRO n 
1 120 SER n 
1 121 HIS n 
1 122 VAL n 
1 123 VAL n 
1 124 THR n 
1 125 MET n 
1 126 LEU n 
1 127 ASP n 
1 128 ASN n 
1 129 PHE n 
1 130 PRO n 
1 131 THR n 
1 132 ASN n 
1 133 LEU n 
1 134 HIS n 
1 135 PRO n 
1 136 MET n 
1 137 SER n 
1 138 GLN n 
1 139 LEU n 
1 140 SER n 
1 141 ALA n 
1 142 ALA n 
1 143 VAL n 
1 144 THR n 
1 145 ALA n 
1 146 LEU n 
1 147 ASN n 
1 148 SER n 
1 149 GLU n 
1 150 SER n 
1 151 ASN n 
1 152 PHE n 
1 153 ALA n 
1 154 ARG n 
1 155 ALA n 
1 156 TYR n 
1 157 ALA n 
1 158 GLN n 
1 159 GLY n 
1 160 ILE n 
1 161 SER n 
1 162 ARG n 
1 163 THR n 
1 164 LYS n 
1 165 TYR n 
1 166 TRP n 
1 167 GLU n 
1 168 LEU n 
1 169 ILE n 
1 170 TYR n 
1 171 GLU n 
1 172 ASP n 
1 173 SER n 
1 174 MET n 
1 175 ASP n 
1 176 LEU n 
1 177 ILE n 
1 178 ALA n 
1 179 LYS n 
1 180 LEU n 
1 181 PRO n 
1 182 CYS n 
1 183 VAL n 
1 184 ALA n 
1 185 ALA n 
1 186 LYS n 
1 187 ILE n 
1 188 TYR n 
1 189 ARG n 
1 190 ASN n 
1 191 LEU n 
1 192 TYR n 
1 193 ARG n 
1 194 GLU n 
1 195 GLY n 
1 196 SER n 
1 197 GLY n 
1 198 ILE n 
1 199 GLY n 
1 200 ALA n 
1 201 ILE n 
1 202 ASP n 
1 203 SER n 
1 204 ASN n 
1 205 LEU n 
1 206 ASP n 
1 207 TRP n 
1 208 SER n 
1 209 HIS n 
1 210 ASN n 
1 211 PHE n 
1 212 THR n 
1 213 ASN n 
1 214 MET n 
1 215 LEU n 
1 216 GLY n 
1 217 TYR n 
1 218 THR n 
1 219 ASP n 
1 220 HIS n 
1 221 GLN n 
1 222 PHE n 
1 223 THR n 
1 224 GLU n 
1 225 LEU n 
1 226 THR n 
1 227 ARG n 
1 228 LEU n 
1 229 TYR n 
1 230 LEU n 
1 231 THR n 
1 232 ILE n 
1 233 HIS n 
1 234 SER n 
1 235 ASP n 
1 236 HIS n 
1 237 GLU n 
1 238 GLY n 
1 239 GLY n 
1 240 ASN n 
1 241 VAL n 
1 242 SER n 
1 243 ALA n 
1 244 HIS n 
1 245 THR n 
1 246 SER n 
1 247 HIS n 
1 248 LEU n 
1 249 VAL n 
1 250 GLY n 
1 251 SER n 
1 252 ALA n 
1 253 LEU n 
1 254 SER n 
1 255 ASP n 
1 256 PRO n 
1 257 TYR n 
1 258 LEU n 
1 259 SER n 
1 260 PHE n 
1 261 ALA n 
1 262 ALA n 
1 263 ALA n 
1 264 MET n 
1 265 ASN n 
1 266 GLY n 
1 267 LEU n 
1 268 ALA n 
1 269 GLY n 
1 270 PRO n 
1 271 LEU n 
1 272 HIS n 
1 273 GLY n 
1 274 LEU n 
1 275 ALA n 
1 276 ASN n 
1 277 GLN n 
1 278 GLU n 
1 279 VAL n 
1 280 LEU n 
1 281 VAL n 
1 282 TRP n 
1 283 LEU n 
1 284 THR n 
1 285 GLN n 
1 286 LEU n 
1 287 GLN n 
1 288 LYS n 
1 289 GLU n 
1 290 VAL n 
1 291 GLY n 
1 292 LYS n 
1 293 ASP n 
1 294 VAL n 
1 295 SER n 
1 296 ASP n 
1 297 GLU n 
1 298 LYS n 
1 299 LEU n 
1 300 ARG n 
1 301 ASP n 
1 302 TYR n 
1 303 ILE n 
1 304 TRP n 
1 305 ASN n 
1 306 THR n 
1 307 LEU n 
1 308 ASN n 
1 309 SER n 
1 310 GLY n 
1 311 ARG n 
1 312 VAL n 
1 313 VAL n 
1 314 PRO n 
1 315 GLY n 
1 316 TYR n 
1 317 GLY n 
1 318 HIS n 
1 319 ALA n 
1 320 VAL n 
1 321 LEU n 
1 322 ARG n 
1 323 LYS n 
1 324 THR n 
1 325 ASP n 
1 326 PRO n 
1 327 ARG n 
1 328 TYR n 
1 329 THR n 
1 330 CYS n 
1 331 GLN n 
1 332 ARG n 
1 333 GLU n 
1 334 PHE n 
1 335 ALA n 
1 336 LEU n 
1 337 LYS n 
1 338 HIS n 
1 339 LEU n 
1 340 PRO n 
1 341 ASN n 
1 342 ASP n 
1 343 PRO n 
1 344 MET n 
1 345 PHE n 
1 346 LYS n 
1 347 LEU n 
1 348 VAL n 
1 349 ALA n 
1 350 GLN n 
1 351 LEU n 
1 352 TYR n 
1 353 LYS n 
1 354 ILE n 
1 355 VAL n 
1 356 PRO n 
1 357 ASN n 
1 358 VAL n 
1 359 LEU n 
1 360 LEU n 
1 361 GLU n 
1 362 GLN n 
1 363 GLY n 
1 364 LYS n 
1 365 ALA n 
1 366 LYS n 
1 367 ASN n 
1 368 PRO n 
1 369 TRP n 
1 370 PRO n 
1 371 ASN n 
1 372 VAL n 
1 373 ASP n 
1 374 ALA n 
1 375 HIS n 
1 376 SER n 
1 377 GLY n 
1 378 VAL n 
1 379 LEU n 
1 380 LEU n 
1 381 GLN n 
1 382 TYR n 
1 383 TYR n 
1 384 GLY n 
1 385 MET n 
1 386 THR n 
1 387 GLU n 
1 388 MET n 
1 389 ASN n 
1 390 TYR n 
1 391 TYR n 
1 392 THR n 
1 393 VAL n 
1 394 LEU n 
1 395 PHE n 
1 396 GLY n 
1 397 VAL n 
1 398 SER n 
1 399 ARG n 
1 400 ALA n 
1 401 LEU n 
1 402 GLY n 
1 403 VAL n 
1 404 LEU n 
1 405 ALA n 
1 406 GLN n 
1 407 LEU n 
1 408 ILE n 
1 409 TRP n 
1 410 SER n 
1 411 ARG n 
1 412 ALA n 
1 413 LEU n 
1 414 GLY n 
1 415 PHE n 
1 416 PRO n 
1 417 LEU n 
1 418 GLU n 
1 419 ARG n 
1 420 PRO n 
1 421 LYS n 
1 422 SER n 
1 423 MET n 
1 424 SER n 
1 425 THR n 
1 426 GLU n 
1 427 GLY n 
1 428 LEU n 
1 429 MET n 
1 430 LYS n 
1 431 PHE n 
1 432 VAL n 
1 433 ASP n 
1 434 SER n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   434 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CS 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE            ? 'C3 H7 N O2'          89.093  
ARG 'L-peptide linking' y ARGININE           ? 'C6 H15 N4 O2 1'      175.209 
ASN 'L-peptide linking' y ASPARAGINE         ? 'C4 H8 N2 O3'         132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'    ? 'C4 H7 N O4'          133.103 
CIT non-polymer         . 'CITRIC ACID'      ? 'C6 H8 O7'            192.124 
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 CIT 1   501 501 CIT CIT A . 
D 3 COA 1   502 502 COA COA A . 
E 4 OAA 1   501 501 OAA OAA B . 
F 5 HOH 1   601 224 HOH HOH A . 
F 5 HOH 2   602 72  HOH HOH A . 
F 5 HOH 3   603 180 HOH HOH A . 
F 5 HOH 4   604 62  HOH HOH A . 
F 5 HOH 5   605 10  HOH HOH A . 
F 5 HOH 6   606 195 HOH HOH A . 
F 5 HOH 7   607 126 HOH HOH A . 
F 5 HOH 8   608 222 HOH HOH A . 
F 5 HOH 9   609 389 HOH HOH A . 
F 5 HOH 10  610 491 HOH HOH A . 
F 5 HOH 11  611 294 HOH HOH A . 
F 5 HOH 12  612 303 HOH HOH A . 
F 5 HOH 13  613 34  HOH HOH A . 
F 5 HOH 14  614 106 HOH HOH A . 
F 5 HOH 15  615 293 HOH HOH A . 
F 5 HOH 16  616 311 HOH HOH A . 
F 5 HOH 17  617 267 HOH HOH A . 
F 5 HOH 18  618 84  HOH HOH A . 
F 5 HOH 19  619 43  HOH HOH A . 
F 5 HOH 20  620 53  HOH HOH A . 
F 5 HOH 21  621 6   HOH HOH A . 
F 5 HOH 22  622 13  HOH HOH A . 
F 5 HOH 23  623 158 HOH HOH A . 
F 5 HOH 24  624 130 HOH HOH A . 
F 5 HOH 25  625 221 HOH HOH A . 
F 5 HOH 26  626 22  HOH HOH A . 
F 5 HOH 27  627 322 HOH HOH A . 
F 5 HOH 28  628 78  HOH HOH A . 
F 5 HOH 29  629 59  HOH HOH A . 
F 5 HOH 30  630 379 HOH HOH A . 
F 5 HOH 31  631 4   HOH HOH A . 
F 5 HOH 32  632 324 HOH HOH A . 
F 5 HOH 33  633 68  HOH HOH A . 
F 5 HOH 34  634 137 HOH HOH A . 
F 5 HOH 35  635 45  HOH HOH A . 
F 5 HOH 36  636 161 HOH HOH A . 
F 5 HOH 37  637 116 HOH HOH A . 
F 5 HOH 38  638 165 HOH HOH A . 
F 5 HOH 39  639 153 HOH HOH A . 
F 5 HOH 40  640 146 HOH HOH A . 
F 5 HOH 41  641 231 HOH HOH A . 
F 5 HOH 42  642 31  HOH HOH A . 
F 5 HOH 43  643 138 HOH HOH A . 
F 5 HOH 44  644 115 HOH HOH A . 
F 5 HOH 45  645 318 HOH HOH A . 
F 5 HOH 46  646 244 HOH HOH A . 
F 5 HOH 47  647 12  HOH HOH A . 
F 5 HOH 48  648 111 HOH HOH A . 
F 5 HOH 49  649 448 HOH HOH A . 
F 5 HOH 50  650 73  HOH HOH A . 
F 5 HOH 51  651 140 HOH HOH A . 
F 5 HOH 52  652 339 HOH HOH A . 
F 5 HOH 53  653 50  HOH HOH A . 
F 5 HOH 54  654 71  HOH HOH A . 
F 5 HOH 55  655 205 HOH HOH A . 
F 5 HOH 56  656 349 HOH HOH A . 
F 5 HOH 57  657 325 HOH HOH A . 
F 5 HOH 58  658 5   HOH HOH A . 
F 5 HOH 59  659 489 HOH HOH A . 
F 5 HOH 60  660 80  HOH HOH A . 
F 5 HOH 61  661 368 HOH HOH A . 
F 5 HOH 62  662 79  HOH HOH A . 
F 5 HOH 63  663 25  HOH HOH A . 
F 5 HOH 64  664 92  HOH HOH A . 
F 5 HOH 65  665 8   HOH HOH A . 
F 5 HOH 66  666 304 HOH HOH A . 
F 5 HOH 67  667 259 HOH HOH A . 
F 5 HOH 68  668 132 HOH HOH A . 
F 5 HOH 69  669 49  HOH HOH A . 
F 5 HOH 70  670 239 HOH HOH A . 
F 5 HOH 71  671 168 HOH HOH A . 
F 5 HOH 72  672 131 HOH HOH A . 
F 5 HOH 73  673 15  HOH HOH A . 
F 5 HOH 74  674 60  HOH HOH A . 
F 5 HOH 75  675 415 HOH HOH A . 
F 5 HOH 76  676 90  HOH HOH A . 
F 5 HOH 77  677 184 HOH HOH A . 
F 5 HOH 78  678 65  HOH HOH A . 
F 5 HOH 79  679 181 HOH HOH A . 
F 5 HOH 80  680 1   HOH HOH A . 
F 5 HOH 81  681 95  HOH HOH A . 
F 5 HOH 82  682 86  HOH HOH A . 
F 5 HOH 83  683 30  HOH HOH A . 
F 5 HOH 84  684 113 HOH HOH A . 
F 5 HOH 85  685 208 HOH HOH A . 
F 5 HOH 86  686 46  HOH HOH A . 
F 5 HOH 87  687 149 HOH HOH A . 
F 5 HOH 88  688 249 HOH HOH A . 
F 5 HOH 89  689 490 HOH HOH A . 
F 5 HOH 90  690 122 HOH HOH A . 
F 5 HOH 91  691 206 HOH HOH A . 
F 5 HOH 92  692 278 HOH HOH A . 
F 5 HOH 93  693 220 HOH HOH A . 
F 5 HOH 94  694 302 HOH HOH A . 
F 5 HOH 95  695 171 HOH HOH A . 
F 5 HOH 96  696 67  HOH HOH A . 
F 5 HOH 97  697 342 HOH HOH A . 
F 5 HOH 98  698 343 HOH HOH A . 
F 5 HOH 99  699 492 HOH HOH A . 
F 5 HOH 100 700 17  HOH HOH A . 
F 5 HOH 101 701 107 HOH HOH A . 
F 5 HOH 102 702 460 HOH HOH A . 
F 5 HOH 103 703 363 HOH HOH A . 
F 5 HOH 104 704 58  HOH HOH A . 
F 5 HOH 105 705 253 HOH HOH A . 
F 5 HOH 106 706 451 HOH HOH A . 
F 5 HOH 107 707 3   HOH HOH A . 
F 5 HOH 108 708 97  HOH HOH A . 
F 5 HOH 109 709 99  HOH HOH A . 
F 5 HOH 110 710 257 HOH HOH A . 
F 5 HOH 111 711 271 HOH HOH A . 
F 5 HOH 112 712 76  HOH HOH A . 
F 5 HOH 113 713 139 HOH HOH A . 
F 5 HOH 114 714 317 HOH HOH A . 
F 5 HOH 115 715 245 HOH HOH A . 
F 5 HOH 116 716 96  HOH HOH A . 
F 5 HOH 117 717 172 HOH HOH A . 
F 5 HOH 118 718 152 HOH HOH A . 
F 5 HOH 119 719 290 HOH HOH A . 
F 5 HOH 120 720 61  HOH HOH A . 
F 5 HOH 121 721 340 HOH HOH A . 
F 5 HOH 122 722 258 HOH HOH A . 
F 5 HOH 123 723 128 HOH HOH A . 
F 5 HOH 124 724 276 HOH HOH A . 
F 5 HOH 125 725 47  HOH HOH A . 
F 5 HOH 126 726 179 HOH HOH A . 
F 5 HOH 127 727 423 HOH HOH A . 
F 5 HOH 128 728 422 HOH HOH A . 
F 5 HOH 129 729 335 HOH HOH A . 
F 5 HOH 130 730 406 HOH HOH A . 
F 5 HOH 131 731 370 HOH HOH A . 
F 5 HOH 132 732 462 HOH HOH A . 
F 5 HOH 133 733 269 HOH HOH A . 
F 5 HOH 134 734 284 HOH HOH A . 
F 5 HOH 135 735 134 HOH HOH A . 
F 5 HOH 136 736 209 HOH HOH A . 
F 5 HOH 137 737 112 HOH HOH A . 
F 5 HOH 138 738 481 HOH HOH A . 
F 5 HOH 139 739 74  HOH HOH A . 
F 5 HOH 140 740 337 HOH HOH A . 
F 5 HOH 141 741 37  HOH HOH A . 
F 5 HOH 142 742 309 HOH HOH A . 
F 5 HOH 143 743 332 HOH HOH A . 
F 5 HOH 144 744 449 HOH HOH A . 
F 5 HOH 145 745 419 HOH HOH A . 
F 5 HOH 146 746 228 HOH HOH A . 
F 5 HOH 147 747 281 HOH HOH A . 
F 5 HOH 148 748 360 HOH HOH A . 
F 5 HOH 149 749 464 HOH HOH A . 
F 5 HOH 150 750 277 HOH HOH A . 
F 5 HOH 151 751 485 HOH HOH A . 
F 5 HOH 152 752 201 HOH HOH A . 
F 5 HOH 153 753 459 HOH HOH A . 
F 5 HOH 154 754 478 HOH HOH A . 
F 5 HOH 155 755 454 HOH HOH A . 
F 5 HOH 156 756 461 HOH HOH A . 
F 5 HOH 157 757 262 HOH HOH A . 
F 5 HOH 158 758 315 HOH HOH A . 
F 5 HOH 159 759 477 HOH HOH A . 
F 5 HOH 160 760 413 HOH HOH A . 
F 5 HOH 161 761 215 HOH HOH A . 
F 5 HOH 162 762 105 HOH HOH A . 
F 5 HOH 163 763 480 HOH HOH A . 
F 5 HOH 164 764 484 HOH HOH A . 
F 5 HOH 165 765 145 HOH HOH A . 
F 5 HOH 166 766 470 HOH HOH A . 
F 5 HOH 167 767 468 HOH HOH A . 
F 5 HOH 168 768 310 HOH HOH A . 
F 5 HOH 169 769 471 HOH HOH A . 
F 5 HOH 170 770 430 HOH HOH A . 
F 5 HOH 171 771 227 HOH HOH A . 
F 5 HOH 172 772 475 HOH HOH A . 
G 5 HOH 1   601 383 HOH HOH B . 
G 5 HOH 2   602 136 HOH HOH B . 
G 5 HOH 3   603 14  HOH HOH B . 
G 5 HOH 4   604 199 HOH HOH B . 
G 5 HOH 5   605 118 HOH HOH B . 
G 5 HOH 6   606 272 HOH HOH B . 
G 5 HOH 7   607 177 HOH HOH B . 
G 5 HOH 8   608 351 HOH HOH B . 
G 5 HOH 9   609 298 HOH HOH B . 
G 5 HOH 10  610 35  HOH HOH B . 
G 5 HOH 11  611 424 HOH HOH B . 
G 5 HOH 12  612 175 HOH HOH B . 
G 5 HOH 13  613 286 HOH HOH B . 
G 5 HOH 14  614 232 HOH HOH B . 
G 5 HOH 15  615 69  HOH HOH B . 
G 5 HOH 16  616 188 HOH HOH B . 
G 5 HOH 17  617 313 HOH HOH B . 
G 5 HOH 18  618 347 HOH HOH B . 
G 5 HOH 19  619 29  HOH HOH B . 
G 5 HOH 20  620 39  HOH HOH B . 
G 5 HOH 21  621 101 HOH HOH B . 
G 5 HOH 22  622 66  HOH HOH B . 
G 5 HOH 23  623 102 HOH HOH B . 
G 5 HOH 24  624 147 HOH HOH B . 
G 5 HOH 25  625 190 HOH HOH B . 
G 5 HOH 26  626 174 HOH HOH B . 
G 5 HOH 27  627 120 HOH HOH B . 
G 5 HOH 28  628 186 HOH HOH B . 
G 5 HOH 29  629 2   HOH HOH B . 
G 5 HOH 30  630 75  HOH HOH B . 
G 5 HOH 31  631 150 HOH HOH B . 
G 5 HOH 32  632 336 HOH HOH B . 
G 5 HOH 33  633 21  HOH HOH B . 
G 5 HOH 34  634 42  HOH HOH B . 
G 5 HOH 35  635 19  HOH HOH B . 
G 5 HOH 36  636 355 HOH HOH B . 
G 5 HOH 37  637 240 HOH HOH B . 
G 5 HOH 38  638 52  HOH HOH B . 
G 5 HOH 39  639 242 HOH HOH B . 
G 5 HOH 40  640 260 HOH HOH B . 
G 5 HOH 41  641 119 HOH HOH B . 
G 5 HOH 42  642 256 HOH HOH B . 
G 5 HOH 43  643 141 HOH HOH B . 
G 5 HOH 44  644 7   HOH HOH B . 
G 5 HOH 45  645 297 HOH HOH B . 
G 5 HOH 46  646 100 HOH HOH B . 
G 5 HOH 47  647 210 HOH HOH B . 
G 5 HOH 48  648 57  HOH HOH B . 
G 5 HOH 49  649 16  HOH HOH B . 
G 5 HOH 50  650 127 HOH HOH B . 
G 5 HOH 51  651 56  HOH HOH B . 
G 5 HOH 52  652 273 HOH HOH B . 
G 5 HOH 53  653 26  HOH HOH B . 
G 5 HOH 54  654 216 HOH HOH B . 
G 5 HOH 55  655 198 HOH HOH B . 
G 5 HOH 56  656 98  HOH HOH B . 
G 5 HOH 57  657 9   HOH HOH B . 
G 5 HOH 58  658 388 HOH HOH B . 
G 5 HOH 59  659 200 HOH HOH B . 
G 5 HOH 60  660 192 HOH HOH B . 
G 5 HOH 61  661 18  HOH HOH B . 
G 5 HOH 62  662 211 HOH HOH B . 
G 5 HOH 63  663 178 HOH HOH B . 
G 5 HOH 64  664 251 HOH HOH B . 
G 5 HOH 65  665 23  HOH HOH B . 
G 5 HOH 66  666 420 HOH HOH B . 
G 5 HOH 67  667 81  HOH HOH B . 
G 5 HOH 68  668 77  HOH HOH B . 
G 5 HOH 69  669 431 HOH HOH B . 
G 5 HOH 70  670 36  HOH HOH B . 
G 5 HOH 71  671 162 HOH HOH B . 
G 5 HOH 72  672 40  HOH HOH B . 
G 5 HOH 73  673 218 HOH HOH B . 
G 5 HOH 74  674 193 HOH HOH B . 
G 5 HOH 75  675 82  HOH HOH B . 
G 5 HOH 76  676 203 HOH HOH B . 
G 5 HOH 77  677 191 HOH HOH B . 
G 5 HOH 78  678 365 HOH HOH B . 
G 5 HOH 79  679 110 HOH HOH B . 
G 5 HOH 80  680 346 HOH HOH B . 
G 5 HOH 81  681 44  HOH HOH B . 
G 5 HOH 82  682 20  HOH HOH B . 
G 5 HOH 83  683 160 HOH HOH B . 
G 5 HOH 84  684 323 HOH HOH B . 
G 5 HOH 85  685 288 HOH HOH B . 
G 5 HOH 86  686 300 HOH HOH B . 
G 5 HOH 87  687 88  HOH HOH B . 
G 5 HOH 88  688 125 HOH HOH B . 
G 5 HOH 89  689 250 HOH HOH B . 
G 5 HOH 90  690 243 HOH HOH B . 
G 5 HOH 91  691 453 HOH HOH B . 
G 5 HOH 92  692 417 HOH HOH B . 
G 5 HOH 93  693 129 HOH HOH B . 
G 5 HOH 94  694 488 HOH HOH B . 
G 5 HOH 95  695 41  HOH HOH B . 
G 5 HOH 96  696 144 HOH HOH B . 
G 5 HOH 97  697 170 HOH HOH B . 
G 5 HOH 98  698 91  HOH HOH B . 
G 5 HOH 99  699 54  HOH HOH B . 
G 5 HOH 100 700 121 HOH HOH B . 
G 5 HOH 101 701 435 HOH HOH B . 
G 5 HOH 102 702 114 HOH HOH B . 
G 5 HOH 103 703 155 HOH HOH B . 
G 5 HOH 104 704 270 HOH HOH B . 
G 5 HOH 105 705 213 HOH HOH B . 
G 5 HOH 106 706 358 HOH HOH B . 
G 5 HOH 107 707 51  HOH HOH B . 
G 5 HOH 108 708 401 HOH HOH B . 
G 5 HOH 109 709 38  HOH HOH B . 
G 5 HOH 110 710 295 HOH HOH B . 
G 5 HOH 111 711 70  HOH HOH B . 
G 5 HOH 112 712 316 HOH HOH B . 
G 5 HOH 113 713 93  HOH HOH B . 
G 5 HOH 114 714 331 HOH HOH B . 
G 5 HOH 115 715 28  HOH HOH B . 
G 5 HOH 116 716 27  HOH HOH B . 
G 5 HOH 117 717 124 HOH HOH B . 
G 5 HOH 118 718 169 HOH HOH B . 
G 5 HOH 119 719 397 HOH HOH B . 
G 5 HOH 120 720 429 HOH HOH B . 
G 5 HOH 121 721 85  HOH HOH B . 
G 5 HOH 122 722 142 HOH HOH B . 
G 5 HOH 123 723 455 HOH HOH B . 
G 5 HOH 124 724 301 HOH HOH B . 
G 5 HOH 125 725 350 HOH HOH B . 
G 5 HOH 126 726 305 HOH HOH B . 
G 5 HOH 127 727 280 HOH HOH B . 
G 5 HOH 128 728 416 HOH HOH B . 
G 5 HOH 129 729 33  HOH HOH B . 
G 5 HOH 130 730 214 HOH HOH B . 
G 5 HOH 131 731 204 HOH HOH B . 
G 5 HOH 132 732 55  HOH HOH B . 
G 5 HOH 133 733 341 HOH HOH B . 
G 5 HOH 134 734 123 HOH HOH B . 
G 5 HOH 135 735 234 HOH HOH B . 
G 5 HOH 136 736 248 HOH HOH B . 
G 5 HOH 137 737 292 HOH HOH B . 
G 5 HOH 138 738 275 HOH HOH B . 
G 5 HOH 139 739 157 HOH HOH B . 
G 5 HOH 140 740 333 HOH HOH B . 
G 5 HOH 141 741 469 HOH HOH B . 
G 5 HOH 142 742 404 HOH HOH B . 
G 5 HOH 143 743 189 HOH HOH B . 
G 5 HOH 144 744 89  HOH HOH B . 
G 5 HOH 145 745 375 HOH HOH B . 
G 5 HOH 146 746 166 HOH HOH B . 
G 5 HOH 147 747 287 HOH HOH B . 
G 5 HOH 148 748 83  HOH HOH B . 
G 5 HOH 149 749 187 HOH HOH B . 
G 5 HOH 150 750 487 HOH HOH B . 
G 5 HOH 151 751 359 HOH HOH B . 
G 5 HOH 152 752 274 HOH HOH B . 
G 5 HOH 153 753 456 HOH HOH B . 
G 5 HOH 154 754 164 HOH HOH B . 
G 5 HOH 155 755 458 HOH HOH B . 
G 5 HOH 156 756 268 HOH HOH B . 
G 5 HOH 157 757 463 HOH HOH B . 
G 5 HOH 158 758 443 HOH HOH B . 
G 5 HOH 159 759 223 HOH HOH B . 
G 5 HOH 160 760 255 HOH HOH B . 
G 5 HOH 161 761 326 HOH HOH B . 
G 5 HOH 162 762 457 HOH HOH B . 
G 5 HOH 163 763 151 HOH HOH B . 
G 5 HOH 164 764 299 HOH HOH B . 
G 5 HOH 165 765 473 HOH HOH B . 
G 5 HOH 166 766 163 HOH HOH B . 
G 5 HOH 167 767 479 HOH HOH B . 
G 5 HOH 168 768 230 HOH HOH B . 
G 5 HOH 169 769 426 HOH HOH B . 
G 5 HOH 170 770 482 HOH HOH B . 
G 5 HOH 171 771 386 HOH HOH B . 
G 5 HOH 172 772 183 HOH HOH B . 
G 5 HOH 173 773 486 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 ? NZ  ? A LYS 186 NZ  
2  1 Y 1 A LYS 321 ? CG  ? A LYS 292 CG  
3  1 Y 1 A LYS 321 ? CD  ? A LYS 292 CD  
4  1 Y 1 A LYS 321 ? CE  ? A LYS 292 CE  
5  1 Y 1 A LYS 321 ? NZ  ? A LYS 292 NZ  
6  1 Y 1 A LYS 395 ? CG  ? A LYS 366 CG  
7  1 Y 1 A LYS 395 ? CD  ? A LYS 366 CD  
8  1 Y 1 A LYS 395 ? CE  ? A LYS 366 CE  
9  1 Y 1 A LYS 395 ? NZ  ? A LYS 366 NZ  
10 1 Y 1 B LYS 215 ? NZ  ? B LYS 186 NZ  
11 1 Y 1 B ARG 351 ? CG  ? B ARG 322 CG  
12 1 Y 1 B ARG 351 ? CD  ? B ARG 322 CD  
13 1 Y 1 B ARG 351 ? NE  ? B ARG 322 NE  
14 1 Y 1 B ARG 351 ? CZ  ? B ARG 322 CZ  
15 1 Y 1 B ARG 351 ? NH1 ? B ARG 322 NH1 
16 1 Y 1 B ARG 351 ? NH2 ? B ARG 322 NH2 
17 1 Y 1 B LYS 395 ? CG  ? B LYS 366 CG  
18 1 Y 1 B LYS 395 ? CD  ? B LYS 366 CD  
19 1 Y 1 B LYS 395 ? CE  ? B LYS 366 CE  
20 1 Y 1 B LYS 395 ? NZ  ? B LYS 366 NZ  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? 5.8.0419 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .        4 
# 
_cell.angle_alpha                  101.45 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   98.91 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  116.47 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8ZVU 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     57.912 
_cell.length_a_esd                 ? 
_cell.length_b                     59.689 
_cell.length_b_esd                 ? 
_cell.length_c                     73.434 
_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                         8ZVU 
_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                   8ZVU 
_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             2.20 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          44.09 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.2 M ammonium acetate pH=7.1, 20% w/v PEG3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            289.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-10-26 
_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                                       8ZVU 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.78 
_reflns.d_resolution_low                               50.98 
_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                                     71771 
_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                           90.3 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                2.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          6.8 
_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                                0.128 
_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                                   0.968 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.104 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.78 
_reflns_shell.d_res_low                                     1.88 
_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                             10449 
_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                               1.345 
_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                                  0.404 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.109 
_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]                            -0.89 
_refine.aniso_B[1][2]                            0.73 
_refine.aniso_B[1][3]                            -0.67 
_refine.aniso_B[2][2]                            0.40 
_refine.aniso_B[2][3]                            0.64 
_refine.aniso_B[3][3]                            -0.53 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               35.923 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.960 
_refine.correlation_coeff_Fo_to_Fc_free          0.938 
_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                                 8ZVU 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.78 
_refine.ls_d_res_low                             50.98 
_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                     66996 
_refine.ls_number_reflns_R_free                  3427 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    88.60 
_refine.ls_percent_reflns_R_free                 4.9 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.18573 
_refine.ls_R_factor_R_free                       0.23311 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.18326 
_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                       0.151 
_refine.pdbx_overall_ESU_R_Free                  0.145 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             4.109 
_refine.overall_SU_ML                            0.121 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.78 
_refine_hist.d_res_low                        50.98 
_refine_hist.number_atoms_solvent             345 
_refine_hist.number_atoms_total               7239 
_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        6824 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         70 
_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' ? 0.009  0.012  7080  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  6640  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.756  1.827  9628  ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.579  1.745  15297 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.497  5.000  872   ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 9.682  5.000  40    ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 15.157 10.000 1172  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.084  0.200  1060  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.008  0.020  8316  ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  1609  ? 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' ? 3.602  3.481  3479  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 3.602  3.481  3479  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 5.219  6.250  4348  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 5.219  6.251  4349  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 4.460  4.022  3601  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 4.455  4.022  3601  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 6.805  7.170  5279  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 9.029  36.07  8255  ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 9.034  35.96  8195  ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.780 
_refine_ls_shell.d_res_low                        1.826 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             245 
_refine_ls_shell.number_reflns_R_work             4764 
_refine_ls_shell.percent_reflns_obs               84.63 
_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                  0.267 
_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                  0.321 
# 
_struct.entry_id                     8ZVU 
_struct.title                        'Human citrate synthase intermediate 4' 
_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        8ZVU 
_struct_keywords.text            'citrate synthase, complex, reaction intermediate, 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 5 ? 
# 
_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 8ZVU A 1 ? 434 ? O75390 30 ? 463 ? 30 463 
2 1 8ZVU 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)' 10780 ? 
1 MORE         -57   ? 
1 'SSA (A^2)'  30550 ? 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASN A 3   ? GLY A 27  ? ASN A 32  GLY A 56  1 ? 25 
HELX_P HELX_P2  AA2 VAL A 36  ? GLY A 41  ? VAL A 65  GLY A 70  1 ? 6  
HELX_P HELX_P3  AA3 ILE A 69  ? LEU A 76  ? ILE A 98  LEU A 105 1 ? 8  
HELX_P HELX_P4  AA4 LEU A 86  ? GLY A 97  ? LEU A 115 GLY A 126 1 ? 12 
HELX_P HELX_P5  AA5 THR A 101 ? ARG A 115 ? THR A 130 ARG A 144 1 ? 15 
HELX_P HELX_P6  AA6 PRO A 119 ? PHE A 129 ? PRO A 148 PHE A 158 1 ? 11 
HELX_P HELX_P7  AA7 HIS A 134 ? LEU A 146 ? HIS A 163 LEU A 175 1 ? 13 
HELX_P HELX_P8  AA8 ASN A 147 ? GLU A 149 ? ASN A 176 GLU A 178 5 ? 3  
HELX_P HELX_P9  AA9 SER A 150 ? GLN A 158 ? SER A 179 GLN A 187 1 ? 9  
HELX_P HELX_P10 AB1 SER A 161 ? THR A 163 ? SER A 190 THR A 192 5 ? 3  
HELX_P HELX_P11 AB2 LYS A 164 ? ARG A 193 ? LYS A 193 ARG A 222 1 ? 30 
HELX_P HELX_P12 AB3 ASP A 206 ? GLY A 216 ? ASP A 235 GLY A 245 1 ? 11 
HELX_P HELX_P13 AB4 ASP A 219 ? HIS A 233 ? ASP A 248 HIS A 262 1 ? 15 
HELX_P HELX_P14 AB5 ASN A 240 ? ALA A 252 ? ASN A 269 ALA A 281 1 ? 13 
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   ? GLY B 27  ? ASN B 32  GLY B 56  1 ? 25 
HELX_P HELX_P26 AC8 VAL B 36  ? GLY B 41  ? VAL B 65  GLY B 70  1 ? 6  
HELX_P HELX_P27 AC9 ILE B 69  ? LEU B 76  ? ILE B 98  LEU B 105 1 ? 8  
HELX_P HELX_P28 AD1 LEU B 86  ? GLY B 97  ? LEU B 115 GLY B 126 1 ? 12 
HELX_P HELX_P29 AD2 THR B 101 ? ARG B 115 ? THR B 130 ARG B 144 1 ? 15 
HELX_P HELX_P30 AD3 PRO B 119 ? PHE B 129 ? PRO B 148 PHE B 158 1 ? 11 
HELX_P HELX_P31 AD4 HIS B 134 ? LEU B 146 ? HIS B 163 LEU B 175 1 ? 13 
HELX_P HELX_P32 AD5 ASN B 147 ? GLU B 149 ? ASN B 176 GLU B 178 5 ? 3  
HELX_P HELX_P33 AD6 SER B 150 ? GLN B 158 ? SER B 179 GLN B 187 1 ? 9  
HELX_P HELX_P34 AD7 SER B 161 ? THR B 163 ? SER B 190 THR B 192 5 ? 3  
HELX_P HELX_P35 AD8 LYS B 164 ? ARG B 193 ? LYS B 193 ARG B 222 1 ? 30 
HELX_P HELX_P36 AD9 ASP B 206 ? GLY B 216 ? ASP B 235 GLY B 245 1 ? 11 
HELX_P HELX_P37 AE1 ASP B 219 ? HIS B 233 ? ASP B 248 HIS B 262 1 ? 15 
HELX_P HELX_P38 AE2 ASN B 240 ? ALA B 252 ? ASN B 269 ALA B 281 1 ? 13 
HELX_P HELX_P39 AE3 ASP B 255 ? ALA B 268 ? ASP B 284 ALA B 297 1 ? 14 
HELX_P HELX_P40 AE4 GLY B 269 ? LEU B 274 ? GLY B 298 LEU B 303 1 ? 6  
HELX_P HELX_P41 AE5 LEU B 274 ? GLY B 291 ? LEU B 303 GLY B 320 1 ? 18 
HELX_P HELX_P42 AE6 SER B 295 ? ASN B 308 ? SER B 324 ASN B 337 1 ? 14 
HELX_P HELX_P43 AE7 ASP B 325 ? LEU B 339 ? ASP B 354 LEU B 368 1 ? 15 
HELX_P HELX_P44 AE8 ASP B 342 ? VAL B 355 ? ASP B 371 VAL B 384 1 ? 14 
HELX_P HELX_P45 AE9 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 ? SER B 434 ? SER B 453 SER B 463 1 ? 11 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 2 ? 
AA3 ? 3 ? 
AA4 ? 2 ? 
AA5 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA2 1 2 ? parallel      
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? parallel      
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
# 
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  
AA5 3 PHE B 67  ? SER B 68  ? PHE B 96  SER B 97  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N ILE A 34  ? N ILE A 63  O GLY B 32  ? O GLY B 61  
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  
AA5 2 3 N PHE B 64  ? N PHE B 93  O PHE B 67  ? O PHE B 96  
# 
_pdbx_entry_details.entry_id                   8ZVU 
_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_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O B PRO 385 ? ? N B VAL 387 ? ? 2.18 
2 1 O A HOH 738 ? ? O A HOH 751 ? ? 2.19 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 C B VAL 384 ? ? N B PRO 385 ? ? 1.468 1.338 0.130 0.019 Y 
2 1 C B LYS 393 ? ? N B ALA 394 ? ? 1.544 1.336 0.208 0.023 Y 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CG A MET 75  ? ? SD A MET 75  ? ? CE  A MET 75  ? ? 90.03  100.20 -10.17 1.60 N 
2 1 CG A MET 414 ? ? SD A MET 414 ? ? CE  A MET 414 ? ? 117.10 100.20 16.90  1.60 N 
3 1 CG A MET 417 ? ? SD A MET 417 ? ? CE  A MET 417 ? ? 89.51  100.20 -10.69 1.60 N 
4 1 CB A LEU 457 ? ? CG A LEU 457 ? ? CD2 A LEU 457 ? ? 122.63 111.00 11.63  1.70 N 
5 1 CB B LYS 109 ? ? CA B LYS 109 ? ? C   B LYS 109 ? ? 127.15 110.40 16.75  2.00 N 
6 1 CB B CYS 359 ? ? CA B CYS 359 ? ? C   B CYS 359 ? ? 122.63 111.50 11.13  1.20 N 
7 1 C  B VAL 384 ? ? N  B PRO 385 ? ? CA  B PRO 385 ? ? 105.59 119.30 -13.71 1.50 Y 
8 1 CG B MET 414 ? ? SD B MET 414 ? ? CE  B MET 414 ? ? 117.35 100.20 17.15  1.60 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 ASP A 88  ? ? -102.58 -62.70  
2  1 ARG A 222 ? ? -142.61 36.82   
3  1 HIS A 265 ? ? -150.77 57.49   
4  1 GLU A 266 ? ? 72.45   -175.95 
5  1 VAL A 349 ? ? -137.03 -41.05  
6  1 LEU A 368 ? ? -146.47 47.61   
7  1 GLN A 391 ? ? -71.14  -71.48  
8  1 ALA A 394 ? ? -107.11 -76.28  
9  1 LYS A 395 ? ? 92.71   -39.04  
10 1 ARG A 448 ? ? -152.38 76.26   
11 1 HIS B 55  ? ? -143.69 15.25   
12 1 GLU B 266 ? ? 70.53   -178.08 
13 1 ASP B 322 ? ? -86.46  35.52   
14 1 ARG B 351 ? ? -168.24 5.61    
15 1 ASN B 386 ? ? 0.29    57.58   
16 1 VAL B 387 ? ? 48.23   107.41  
17 1 GLN B 391 ? ? -103.45 -66.16  
18 1 ALA B 394 ? ? -130.85 -84.09  
19 1 LYS B 395 ? ? 143.49  -14.68  
20 1 ARG B 448 ? ? -159.32 77.19   
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG A 144 ? ? 0.072 'SIDE CHAIN' 
2 1 ARG A 329 ? ? 0.093 'SIDE CHAIN' 
3 1 ARG B 52  ? ? 0.106 'SIDE CHAIN' 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      B 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       773 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.06 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CIT C1   C N N 74  
CIT O1   O N N 75  
CIT O2   O N N 76  
CIT C2   C N N 77  
CIT C3   C N N 78  
CIT O7   O N N 79  
CIT C4   C N N 80  
CIT C5   C N N 81  
CIT O3   O N N 82  
CIT O4   O N N 83  
CIT C6   C N N 84  
CIT O5   O N N 85  
CIT O6   O N N 86  
CIT HO2  H N N 87  
CIT H21  H N N 88  
CIT H22  H N N 89  
CIT HO7  H N N 90  
CIT H41  H N N 91  
CIT H42  H N N 92  
CIT HO4  H N N 93  
CIT HO6  H N N 94  
COA N1A  N Y N 95  
COA C2A  C Y N 96  
COA N3A  N Y N 97  
COA C4A  C Y N 98  
COA C5A  C Y N 99  
COA C6A  C Y N 100 
COA N6A  N N N 101 
COA N7A  N Y N 102 
COA C8A  C Y N 103 
COA N9A  N Y N 104 
COA C1B  C N R 105 
COA C2B  C N R 106 
COA O2B  O N N 107 
COA C3B  C N S 108 
COA O3B  O N N 109 
COA P3B  P N N 110 
COA O7A  O N N 111 
COA O8A  O N N 112 
COA O9A  O N N 113 
COA C4B  C N R 114 
COA O4B  O N N 115 
COA C5B  C N N 116 
COA O5B  O N N 117 
COA P1A  P N S 118 
COA O1A  O N N 119 
COA O2A  O N N 120 
COA O3A  O N N 121 
COA P2A  P N S 122 
COA O4A  O N N 123 
COA O5A  O N N 124 
COA O6A  O N N 125 
COA CBP  C N N 126 
COA CCP  C N N 127 
COA CDP  C N N 128 
COA CEP  C N N 129 
COA CAP  C N R 130 
COA OAP  O N N 131 
COA C9P  C N N 132 
COA O9P  O N N 133 
COA N8P  N N N 134 
COA C7P  C N N 135 
COA C6P  C N N 136 
COA C5P  C N N 137 
COA O5P  O N N 138 
COA N4P  N N N 139 
COA C3P  C N N 140 
COA C2P  C N N 141 
COA S1P  S N N 142 
COA H2A  H N N 143 
COA H61A H N N 144 
COA H62A H N N 145 
COA H8A  H N N 146 
COA H1B  H N N 147 
COA H2B  H N N 148 
COA HO2A H N N 149 
COA H3B  H N N 150 
COA HOA8 H N N 151 
COA HOA9 H N N 152 
COA H4B  H N N 153 
COA H51A H N N 154 
COA H52A H N N 155 
COA HOA2 H N N 156 
COA HOA5 H N N 157 
COA H121 H N N 158 
COA H122 H N N 159 
COA H131 H N N 160 
COA H132 H N N 161 
COA H133 H N N 162 
COA H141 H N N 163 
COA H142 H N N 164 
COA H143 H N N 165 
COA H10  H N N 166 
COA HO1  H N N 167 
COA HN8  H N N 168 
COA H71  H N N 169 
COA H72  H N N 170 
COA H61  H N N 171 
COA H62  H N N 172 
COA HN4  H N N 173 
COA H31  H N N 174 
COA H32  H N N 175 
COA H21  H N N 176 
COA H22  H N N 177 
COA HS1  H N N 178 
CYS N    N N N 179 
CYS CA   C N R 180 
CYS C    C N N 181 
CYS O    O N N 182 
CYS CB   C N N 183 
CYS SG   S N N 184 
CYS OXT  O N N 185 
CYS H    H N N 186 
CYS H2   H N N 187 
CYS HA   H N N 188 
CYS HB2  H N N 189 
CYS HB3  H N N 190 
CYS HG   H N N 191 
CYS HXT  H N N 192 
GLN N    N N N 193 
GLN CA   C N S 194 
GLN C    C N N 195 
GLN O    O N N 196 
GLN CB   C N N 197 
GLN CG   C N N 198 
GLN CD   C N N 199 
GLN OE1  O N N 200 
GLN NE2  N N N 201 
GLN OXT  O N N 202 
GLN H    H N N 203 
GLN H2   H N N 204 
GLN HA   H N N 205 
GLN HB2  H N N 206 
GLN HB3  H N N 207 
GLN HG2  H N N 208 
GLN HG3  H N N 209 
GLN HE21 H N N 210 
GLN HE22 H N N 211 
GLN HXT  H N N 212 
GLU N    N N N 213 
GLU CA   C N S 214 
GLU C    C N N 215 
GLU O    O N N 216 
GLU CB   C N N 217 
GLU CG   C N N 218 
GLU CD   C N N 219 
GLU OE1  O N N 220 
GLU OE2  O N N 221 
GLU OXT  O N N 222 
GLU H    H N N 223 
GLU H2   H N N 224 
GLU HA   H N N 225 
GLU HB2  H N N 226 
GLU HB3  H N N 227 
GLU HG2  H N N 228 
GLU HG3  H N N 229 
GLU HE2  H N N 230 
GLU HXT  H N N 231 
GLY N    N N N 232 
GLY CA   C N N 233 
GLY C    C N N 234 
GLY O    O N N 235 
GLY OXT  O N N 236 
GLY H    H N N 237 
GLY H2   H N N 238 
GLY HA2  H N N 239 
GLY HA3  H N N 240 
GLY HXT  H N N 241 
HIS N    N N N 242 
HIS CA   C N S 243 
HIS C    C N N 244 
HIS O    O N N 245 
HIS CB   C N N 246 
HIS CG   C Y N 247 
HIS ND1  N Y N 248 
HIS CD2  C Y N 249 
HIS CE1  C Y N 250 
HIS NE2  N Y N 251 
HIS OXT  O N N 252 
HIS H    H N N 253 
HIS H2   H N N 254 
HIS HA   H N N 255 
HIS HB2  H N N 256 
HIS HB3  H N N 257 
HIS HD1  H N N 258 
HIS HD2  H N N 259 
HIS HE1  H N N 260 
HIS HE2  H N N 261 
HIS HXT  H N N 262 
HOH O    O N N 263 
HOH H1   H N N 264 
HOH H2   H N N 265 
ILE N    N N N 266 
ILE CA   C N S 267 
ILE C    C N N 268 
ILE O    O N N 269 
ILE CB   C N S 270 
ILE CG1  C N N 271 
ILE CG2  C N N 272 
ILE CD1  C N N 273 
ILE OXT  O N N 274 
ILE H    H N N 275 
ILE H2   H N N 276 
ILE HA   H N N 277 
ILE HB   H N N 278 
ILE HG12 H N N 279 
ILE HG13 H N N 280 
ILE HG21 H N N 281 
ILE HG22 H N N 282 
ILE HG23 H N N 283 
ILE HD11 H N N 284 
ILE HD12 H N N 285 
ILE HD13 H N N 286 
ILE HXT  H N N 287 
LEU N    N N N 288 
LEU CA   C N S 289 
LEU C    C N N 290 
LEU O    O N N 291 
LEU CB   C N N 292 
LEU CG   C N N 293 
LEU CD1  C N N 294 
LEU CD2  C N N 295 
LEU OXT  O N N 296 
LEU H    H N N 297 
LEU H2   H N N 298 
LEU HA   H N N 299 
LEU HB2  H N N 300 
LEU HB3  H N N 301 
LEU HG   H N N 302 
LEU HD11 H N N 303 
LEU HD12 H N N 304 
LEU HD13 H N N 305 
LEU HD21 H N N 306 
LEU HD22 H N N 307 
LEU HD23 H N N 308 
LEU HXT  H N N 309 
LYS N    N N N 310 
LYS CA   C N S 311 
LYS C    C N N 312 
LYS O    O N N 313 
LYS CB   C N N 314 
LYS CG   C N N 315 
LYS CD   C N N 316 
LYS CE   C N N 317 
LYS NZ   N N N 318 
LYS OXT  O N N 319 
LYS H    H N N 320 
LYS H2   H N N 321 
LYS HA   H N N 322 
LYS HB2  H N N 323 
LYS HB3  H N N 324 
LYS HG2  H N N 325 
LYS HG3  H N N 326 
LYS HD2  H N N 327 
LYS HD3  H N N 328 
LYS HE2  H N N 329 
LYS HE3  H N N 330 
LYS HZ1  H N N 331 
LYS HZ2  H N N 332 
LYS HZ3  H N N 333 
LYS HXT  H N N 334 
MET N    N N N 335 
MET CA   C N S 336 
MET C    C N N 337 
MET O    O N N 338 
MET CB   C N N 339 
MET CG   C N N 340 
MET SD   S N N 341 
MET CE   C N N 342 
MET OXT  O N N 343 
MET H    H N N 344 
MET H2   H N N 345 
MET HA   H N N 346 
MET HB2  H N N 347 
MET HB3  H N N 348 
MET HG2  H N N 349 
MET HG3  H N N 350 
MET HE1  H N N 351 
MET HE2  H N N 352 
MET HE3  H N N 353 
MET HXT  H N N 354 
OAA O1   O N N 355 
OAA O2   O N N 356 
OAA O4   O N N 357 
OAA O5   O N N 358 
OAA O3   O N N 359 
OAA C1   C N N 360 
OAA C2   C N N 361 
OAA C3   C N N 362 
OAA C4   C N N 363 
OAA HO5  H N N 364 
OAA H21  H N N 365 
OAA H22  H N N 366 
PHE N    N N N 367 
PHE CA   C N S 368 
PHE C    C N N 369 
PHE O    O N N 370 
PHE CB   C N N 371 
PHE CG   C Y N 372 
PHE CD1  C Y N 373 
PHE CD2  C Y N 374 
PHE CE1  C Y N 375 
PHE CE2  C Y N 376 
PHE CZ   C Y N 377 
PHE OXT  O N N 378 
PHE H    H N N 379 
PHE H2   H N N 380 
PHE HA   H N N 381 
PHE HB2  H N N 382 
PHE HB3  H N N 383 
PHE HD1  H N N 384 
PHE HD2  H N N 385 
PHE HE1  H N N 386 
PHE HE2  H N N 387 
PHE HZ   H N N 388 
PHE HXT  H N N 389 
PRO N    N N N 390 
PRO CA   C N S 391 
PRO C    C N N 392 
PRO O    O N N 393 
PRO CB   C N N 394 
PRO CG   C N N 395 
PRO CD   C N N 396 
PRO OXT  O N N 397 
PRO H    H N N 398 
PRO HA   H N N 399 
PRO HB2  H N N 400 
PRO HB3  H N N 401 
PRO HG2  H N N 402 
PRO HG3  H N N 403 
PRO HD2  H N N 404 
PRO HD3  H N N 405 
PRO HXT  H N N 406 
SER N    N N N 407 
SER CA   C N S 408 
SER C    C N N 409 
SER O    O N N 410 
SER CB   C N N 411 
SER OG   O N N 412 
SER OXT  O N N 413 
SER H    H N N 414 
SER H2   H N N 415 
SER HA   H N N 416 
SER HB2  H N N 417 
SER HB3  H N N 418 
SER HG   H N N 419 
SER HXT  H N N 420 
THR N    N N N 421 
THR CA   C N S 422 
THR C    C N N 423 
THR O    O N N 424 
THR CB   C N R 425 
THR OG1  O N N 426 
THR CG2  C N N 427 
THR OXT  O N N 428 
THR H    H N N 429 
THR H2   H N N 430 
THR HA   H N N 431 
THR HB   H N N 432 
THR HG1  H N N 433 
THR HG21 H N N 434 
THR HG22 H N N 435 
THR HG23 H N N 436 
THR HXT  H N N 437 
TRP N    N N N 438 
TRP CA   C N S 439 
TRP C    C N N 440 
TRP O    O N N 441 
TRP CB   C N N 442 
TRP CG   C Y N 443 
TRP CD1  C Y N 444 
TRP CD2  C Y N 445 
TRP NE1  N Y N 446 
TRP CE2  C Y N 447 
TRP CE3  C Y N 448 
TRP CZ2  C Y N 449 
TRP CZ3  C Y N 450 
TRP CH2  C Y N 451 
TRP OXT  O N N 452 
TRP H    H N N 453 
TRP H2   H N N 454 
TRP HA   H N N 455 
TRP HB2  H N N 456 
TRP HB3  H N N 457 
TRP HD1  H N N 458 
TRP HE1  H N N 459 
TRP HE3  H N N 460 
TRP HZ2  H N N 461 
TRP HZ3  H N N 462 
TRP HH2  H N N 463 
TRP HXT  H N N 464 
TYR N    N N N 465 
TYR CA   C N S 466 
TYR C    C N N 467 
TYR O    O N N 468 
TYR CB   C N N 469 
TYR CG   C Y N 470 
TYR CD1  C Y N 471 
TYR CD2  C Y N 472 
TYR CE1  C Y N 473 
TYR CE2  C Y N 474 
TYR CZ   C Y N 475 
TYR OH   O N N 476 
TYR OXT  O N N 477 
TYR H    H N N 478 
TYR H2   H N N 479 
TYR HA   H N N 480 
TYR HB2  H N N 481 
TYR HB3  H N N 482 
TYR HD1  H N N 483 
TYR HD2  H N N 484 
TYR HE1  H N N 485 
TYR HE2  H N N 486 
TYR HH   H N N 487 
TYR HXT  H N N 488 
VAL N    N N N 489 
VAL CA   C N S 490 
VAL C    C N N 491 
VAL O    O N N 492 
VAL CB   C N N 493 
VAL CG1  C N N 494 
VAL CG2  C N N 495 
VAL OXT  O N N 496 
VAL H    H N N 497 
VAL H2   H N N 498 
VAL HA   H N N 499 
VAL HB   H N N 500 
VAL HG11 H N N 501 
VAL HG12 H N N 502 
VAL HG13 H N N 503 
VAL HG21 H N N 504 
VAL HG22 H N N 505 
VAL HG23 H N N 506 
VAL HXT  H N N 507 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CIT C1  O1   doub N N 70  
CIT C1  O2   sing N N 71  
CIT C1  C2   sing N N 72  
CIT O2  HO2  sing N N 73  
CIT C2  C3   sing N N 74  
CIT C2  H21  sing N N 75  
CIT C2  H22  sing N N 76  
CIT C3  O7   sing N N 77  
CIT C3  C4   sing N N 78  
CIT C3  C6   sing N N 79  
CIT O7  HO7  sing N N 80  
CIT C4  C5   sing N N 81  
CIT C4  H41  sing N N 82  
CIT C4  H42  sing N N 83  
CIT C5  O3   doub N N 84  
CIT C5  O4   sing N N 85  
CIT O4  HO4  sing N N 86  
CIT C6  O5   doub N N 87  
CIT C6  O6   sing N N 88  
CIT O6  HO6  sing N N 89  
COA N1A C2A  sing Y N 90  
COA N1A C6A  doub Y N 91  
COA C2A N3A  doub Y N 92  
COA C2A H2A  sing N N 93  
COA N3A C4A  sing Y N 94  
COA C4A C5A  doub Y N 95  
COA C4A N9A  sing Y N 96  
COA C5A C6A  sing Y N 97  
COA C5A N7A  sing Y N 98  
COA C6A N6A  sing N N 99  
COA N6A H61A sing N N 100 
COA N6A H62A sing N N 101 
COA N7A C8A  doub Y N 102 
COA C8A N9A  sing Y N 103 
COA C8A H8A  sing N N 104 
COA N9A C1B  sing N N 105 
COA C1B C2B  sing N N 106 
COA C1B O4B  sing N N 107 
COA C1B H1B  sing N N 108 
COA C2B O2B  sing N N 109 
COA C2B C3B  sing N N 110 
COA C2B H2B  sing N N 111 
COA O2B HO2A sing N N 112 
COA C3B O3B  sing N N 113 
COA C3B C4B  sing N N 114 
COA C3B H3B  sing N N 115 
COA O3B P3B  sing N N 116 
COA P3B O7A  doub N N 117 
COA P3B O8A  sing N N 118 
COA P3B O9A  sing N N 119 
COA O8A HOA8 sing N N 120 
COA O9A HOA9 sing N N 121 
COA C4B O4B  sing N N 122 
COA C4B C5B  sing N N 123 
COA C4B H4B  sing N N 124 
COA C5B O5B  sing N N 125 
COA C5B H51A sing N N 126 
COA C5B H52A sing N N 127 
COA O5B P1A  sing N N 128 
COA P1A O1A  doub N N 129 
COA P1A O2A  sing N N 130 
COA P1A O3A  sing N N 131 
COA O2A HOA2 sing N N 132 
COA O3A P2A  sing N N 133 
COA P2A O4A  doub N N 134 
COA P2A O5A  sing N N 135 
COA P2A O6A  sing N N 136 
COA O5A HOA5 sing N N 137 
COA O6A CCP  sing N N 138 
COA CBP CCP  sing N N 139 
COA CBP CDP  sing N N 140 
COA CBP CEP  sing N N 141 
COA CBP CAP  sing N N 142 
COA CCP H121 sing N N 143 
COA CCP H122 sing N N 144 
COA CDP H131 sing N N 145 
COA CDP H132 sing N N 146 
COA CDP H133 sing N N 147 
COA CEP H141 sing N N 148 
COA CEP H142 sing N N 149 
COA CEP H143 sing N N 150 
COA CAP OAP  sing N N 151 
COA CAP C9P  sing N N 152 
COA CAP H10  sing N N 153 
COA OAP HO1  sing N N 154 
COA C9P O9P  doub N N 155 
COA C9P N8P  sing N N 156 
COA N8P C7P  sing N N 157 
COA N8P HN8  sing N N 158 
COA C7P C6P  sing N N 159 
COA C7P H71  sing N N 160 
COA C7P H72  sing N N 161 
COA C6P C5P  sing N N 162 
COA C6P H61  sing N N 163 
COA C6P H62  sing N N 164 
COA C5P O5P  doub N N 165 
COA C5P N4P  sing N N 166 
COA N4P C3P  sing N N 167 
COA N4P HN4  sing N N 168 
COA C3P C2P  sing N N 169 
COA C3P H31  sing N N 170 
COA C3P H32  sing N N 171 
COA C2P S1P  sing N N 172 
COA C2P H21  sing N N 173 
COA C2P H22  sing N N 174 
COA S1P HS1  sing N N 175 
CYS N   CA   sing N N 176 
CYS N   H    sing N N 177 
CYS N   H2   sing N N 178 
CYS CA  C    sing N N 179 
CYS CA  CB   sing N N 180 
CYS CA  HA   sing N N 181 
CYS C   O    doub N N 182 
CYS C   OXT  sing N N 183 
CYS CB  SG   sing N N 184 
CYS CB  HB2  sing N N 185 
CYS CB  HB3  sing N N 186 
CYS SG  HG   sing N N 187 
CYS OXT HXT  sing N N 188 
GLN N   CA   sing N N 189 
GLN N   H    sing N N 190 
GLN N   H2   sing N N 191 
GLN CA  C    sing N N 192 
GLN CA  CB   sing N N 193 
GLN CA  HA   sing N N 194 
GLN C   O    doub N N 195 
GLN C   OXT  sing N N 196 
GLN CB  CG   sing N N 197 
GLN CB  HB2  sing N N 198 
GLN CB  HB3  sing N N 199 
GLN CG  CD   sing N N 200 
GLN CG  HG2  sing N N 201 
GLN CG  HG3  sing N N 202 
GLN CD  OE1  doub N N 203 
GLN CD  NE2  sing N N 204 
GLN NE2 HE21 sing N N 205 
GLN NE2 HE22 sing N N 206 
GLN OXT HXT  sing N N 207 
GLU N   CA   sing N N 208 
GLU N   H    sing N N 209 
GLU N   H2   sing N N 210 
GLU CA  C    sing N N 211 
GLU CA  CB   sing N N 212 
GLU CA  HA   sing N N 213 
GLU C   O    doub N N 214 
GLU C   OXT  sing N N 215 
GLU CB  CG   sing N N 216 
GLU CB  HB2  sing N N 217 
GLU CB  HB3  sing N N 218 
GLU CG  CD   sing N N 219 
GLU CG  HG2  sing N N 220 
GLU CG  HG3  sing N N 221 
GLU CD  OE1  doub N N 222 
GLU CD  OE2  sing N N 223 
GLU OE2 HE2  sing N N 224 
GLU OXT HXT  sing N N 225 
GLY N   CA   sing N N 226 
GLY N   H    sing N N 227 
GLY N   H2   sing N N 228 
GLY CA  C    sing N N 229 
GLY CA  HA2  sing N N 230 
GLY CA  HA3  sing N N 231 
GLY C   O    doub N N 232 
GLY C   OXT  sing N N 233 
GLY OXT HXT  sing N N 234 
HIS N   CA   sing N N 235 
HIS N   H    sing N N 236 
HIS N   H2   sing N N 237 
HIS CA  C    sing N N 238 
HIS CA  CB   sing N N 239 
HIS CA  HA   sing N N 240 
HIS C   O    doub N N 241 
HIS C   OXT  sing N N 242 
HIS CB  CG   sing N N 243 
HIS CB  HB2  sing N N 244 
HIS CB  HB3  sing N N 245 
HIS CG  ND1  sing Y N 246 
HIS CG  CD2  doub Y N 247 
HIS ND1 CE1  doub Y N 248 
HIS ND1 HD1  sing N N 249 
HIS CD2 NE2  sing Y N 250 
HIS CD2 HD2  sing N N 251 
HIS CE1 NE2  sing Y N 252 
HIS CE1 HE1  sing N N 253 
HIS NE2 HE2  sing N N 254 
HIS OXT HXT  sing N N 255 
HOH O   H1   sing N N 256 
HOH O   H2   sing N N 257 
ILE N   CA   sing N N 258 
ILE N   H    sing N N 259 
ILE N   H2   sing N N 260 
ILE CA  C    sing N N 261 
ILE CA  CB   sing N N 262 
ILE CA  HA   sing N N 263 
ILE C   O    doub N N 264 
ILE C   OXT  sing N N 265 
ILE CB  CG1  sing N N 266 
ILE CB  CG2  sing N N 267 
ILE CB  HB   sing N N 268 
ILE CG1 CD1  sing N N 269 
ILE CG1 HG12 sing N N 270 
ILE CG1 HG13 sing N N 271 
ILE CG2 HG21 sing N N 272 
ILE CG2 HG22 sing N N 273 
ILE CG2 HG23 sing N N 274 
ILE CD1 HD11 sing N N 275 
ILE CD1 HD12 sing N N 276 
ILE CD1 HD13 sing N N 277 
ILE OXT HXT  sing N N 278 
LEU N   CA   sing N N 279 
LEU N   H    sing N N 280 
LEU N   H2   sing N N 281 
LEU CA  C    sing N N 282 
LEU CA  CB   sing N N 283 
LEU CA  HA   sing N N 284 
LEU C   O    doub N N 285 
LEU C   OXT  sing N N 286 
LEU CB  CG   sing N N 287 
LEU CB  HB2  sing N N 288 
LEU CB  HB3  sing N N 289 
LEU CG  CD1  sing N N 290 
LEU CG  CD2  sing N N 291 
LEU CG  HG   sing N N 292 
LEU CD1 HD11 sing N N 293 
LEU CD1 HD12 sing N N 294 
LEU CD1 HD13 sing N N 295 
LEU CD2 HD21 sing N N 296 
LEU CD2 HD22 sing N N 297 
LEU CD2 HD23 sing N N 298 
LEU OXT HXT  sing N N 299 
LYS N   CA   sing N N 300 
LYS N   H    sing N N 301 
LYS N   H2   sing N N 302 
LYS CA  C    sing N N 303 
LYS CA  CB   sing N N 304 
LYS CA  HA   sing N N 305 
LYS C   O    doub N N 306 
LYS C   OXT  sing N N 307 
LYS CB  CG   sing N N 308 
LYS CB  HB2  sing N N 309 
LYS CB  HB3  sing N N 310 
LYS CG  CD   sing N N 311 
LYS CG  HG2  sing N N 312 
LYS CG  HG3  sing N N 313 
LYS CD  CE   sing N N 314 
LYS CD  HD2  sing N N 315 
LYS CD  HD3  sing N N 316 
LYS CE  NZ   sing N N 317 
LYS CE  HE2  sing N N 318 
LYS CE  HE3  sing N N 319 
LYS NZ  HZ1  sing N N 320 
LYS NZ  HZ2  sing N N 321 
LYS NZ  HZ3  sing N N 322 
LYS OXT HXT  sing N N 323 
MET N   CA   sing N N 324 
MET N   H    sing N N 325 
MET N   H2   sing N N 326 
MET CA  C    sing N N 327 
MET CA  CB   sing N N 328 
MET CA  HA   sing N N 329 
MET C   O    doub N N 330 
MET C   OXT  sing N N 331 
MET CB  CG   sing N N 332 
MET CB  HB2  sing N N 333 
MET CB  HB3  sing N N 334 
MET CG  SD   sing N N 335 
MET CG  HG2  sing N N 336 
MET CG  HG3  sing N N 337 
MET SD  CE   sing N N 338 
MET CE  HE1  sing N N 339 
MET CE  HE2  sing N N 340 
MET CE  HE3  sing N N 341 
MET OXT HXT  sing N N 342 
OAA O1  C1   doub N N 343 
OAA O2  C1   sing N N 344 
OAA O4  C4   doub N N 345 
OAA O5  C4   sing N N 346 
OAA O5  HO5  sing N N 347 
OAA O3  C3   doub N N 348 
OAA C1  C2   sing N N 349 
OAA C2  C3   sing N N 350 
OAA C2  H21  sing N N 351 
OAA C2  H22  sing N N 352 
OAA C3  C4   sing N N 353 
PHE N   CA   sing N N 354 
PHE N   H    sing N N 355 
PHE N   H2   sing N N 356 
PHE CA  C    sing N N 357 
PHE CA  CB   sing N N 358 
PHE CA  HA   sing N N 359 
PHE C   O    doub N N 360 
PHE C   OXT  sing N N 361 
PHE CB  CG   sing N N 362 
PHE CB  HB2  sing N N 363 
PHE CB  HB3  sing N N 364 
PHE CG  CD1  doub Y N 365 
PHE CG  CD2  sing Y N 366 
PHE CD1 CE1  sing Y N 367 
PHE CD1 HD1  sing N N 368 
PHE CD2 CE2  doub Y N 369 
PHE CD2 HD2  sing N N 370 
PHE CE1 CZ   doub Y N 371 
PHE CE1 HE1  sing N N 372 
PHE CE2 CZ   sing Y N 373 
PHE CE2 HE2  sing N N 374 
PHE CZ  HZ   sing N N 375 
PHE OXT HXT  sing N N 376 
PRO N   CA   sing N N 377 
PRO N   CD   sing N N 378 
PRO N   H    sing N N 379 
PRO CA  C    sing N N 380 
PRO CA  CB   sing N N 381 
PRO CA  HA   sing N N 382 
PRO C   O    doub N N 383 
PRO C   OXT  sing N N 384 
PRO CB  CG   sing N N 385 
PRO CB  HB2  sing N N 386 
PRO CB  HB3  sing N N 387 
PRO CG  CD   sing N N 388 
PRO CG  HG2  sing N N 389 
PRO CG  HG3  sing N N 390 
PRO CD  HD2  sing N N 391 
PRO CD  HD3  sing N N 392 
PRO OXT HXT  sing N N 393 
SER N   CA   sing N N 394 
SER N   H    sing N N 395 
SER N   H2   sing N N 396 
SER CA  C    sing N N 397 
SER CA  CB   sing N N 398 
SER CA  HA   sing N N 399 
SER C   O    doub N N 400 
SER C   OXT  sing N N 401 
SER CB  OG   sing N N 402 
SER CB  HB2  sing N N 403 
SER CB  HB3  sing N N 404 
SER OG  HG   sing N N 405 
SER OXT HXT  sing N N 406 
THR N   CA   sing N N 407 
THR N   H    sing N N 408 
THR N   H2   sing N N 409 
THR CA  C    sing N N 410 
THR CA  CB   sing N N 411 
THR CA  HA   sing N N 412 
THR C   O    doub N N 413 
THR C   OXT  sing N N 414 
THR CB  OG1  sing N N 415 
THR CB  CG2  sing N N 416 
THR CB  HB   sing N N 417 
THR OG1 HG1  sing N N 418 
THR CG2 HG21 sing N N 419 
THR CG2 HG22 sing N N 420 
THR CG2 HG23 sing N N 421 
THR OXT HXT  sing N N 422 
TRP N   CA   sing N N 423 
TRP N   H    sing N N 424 
TRP N   H2   sing N N 425 
TRP CA  C    sing N N 426 
TRP CA  CB   sing N N 427 
TRP CA  HA   sing N N 428 
TRP C   O    doub N N 429 
TRP C   OXT  sing N N 430 
TRP CB  CG   sing N N 431 
TRP CB  HB2  sing N N 432 
TRP CB  HB3  sing N N 433 
TRP CG  CD1  doub Y N 434 
TRP CG  CD2  sing Y N 435 
TRP CD1 NE1  sing Y N 436 
TRP CD1 HD1  sing N N 437 
TRP CD2 CE2  doub Y N 438 
TRP CD2 CE3  sing Y N 439 
TRP NE1 CE2  sing Y N 440 
TRP NE1 HE1  sing N N 441 
TRP CE2 CZ2  sing Y N 442 
TRP CE3 CZ3  doub Y N 443 
TRP CE3 HE3  sing N N 444 
TRP CZ2 CH2  doub Y N 445 
TRP CZ2 HZ2  sing N N 446 
TRP CZ3 CH2  sing Y N 447 
TRP CZ3 HZ3  sing N N 448 
TRP CH2 HH2  sing N N 449 
TRP OXT HXT  sing N N 450 
TYR N   CA   sing N N 451 
TYR N   H    sing N N 452 
TYR N   H2   sing N N 453 
TYR CA  C    sing N N 454 
TYR CA  CB   sing N N 455 
TYR CA  HA   sing N N 456 
TYR C   O    doub N N 457 
TYR C   OXT  sing N N 458 
TYR CB  CG   sing N N 459 
TYR CB  HB2  sing N N 460 
TYR CB  HB3  sing N N 461 
TYR CG  CD1  doub Y N 462 
TYR CG  CD2  sing Y N 463 
TYR CD1 CE1  sing Y N 464 
TYR CD1 HD1  sing N N 465 
TYR CD2 CE2  doub Y N 466 
TYR CD2 HD2  sing N N 467 
TYR CE1 CZ   doub Y N 468 
TYR CE1 HE1  sing N N 469 
TYR CE2 CZ   sing Y N 470 
TYR CE2 HE2  sing N N 471 
TYR CZ  OH   sing N N 472 
TYR OH  HH   sing N N 473 
TYR OXT HXT  sing N N 474 
VAL N   CA   sing N N 475 
VAL N   H    sing N N 476 
VAL N   H2   sing N N 477 
VAL CA  C    sing N N 478 
VAL CA  CB   sing N N 479 
VAL CA  HA   sing N N 480 
VAL C   O    doub N N 481 
VAL C   OXT  sing N N 482 
VAL CB  CG1  sing N N 483 
VAL CB  CG2  sing N N 484 
VAL CB  HB   sing N N 485 
VAL CG1 HG11 sing N N 486 
VAL CG1 HG12 sing N N 487 
VAL CG1 HG13 sing N N 488 
VAL CG2 HG21 sing N N 489 
VAL CG2 HG22 sing N N 490 
VAL CG2 HG23 sing N N 491 
VAL OXT HXT  sing N N 492 
# 
_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                    8ZVU 
_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]   0.017268 
_atom_sites.fract_transf_matrix[1][2]   0.008598 
_atom_sites.fract_transf_matrix[1][3]   0.005571 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.018715 
_atom_sites.fract_transf_matrix[2][3]   0.005942 
_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]   0.014462 
_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   ? 48.300  4.249   -12.802 1.00 59.95  ? 30  SER A N   1 
ATOM   2    C CA  . SER A 1 1   ? 48.521  3.150   -13.786 1.00 64.93  ? 30  SER A CA  1 
ATOM   3    C C   . SER A 1 1   ? 47.195  2.710   -14.423 1.00 79.38  ? 30  SER A C   1 
ATOM   4    O O   . SER A 1 1   ? 46.535  3.455   -15.166 1.00 71.08  ? 30  SER A O   1 
ATOM   5    C CB  . SER A 1 1   ? 49.233  1.981   -13.120 1.00 69.02  ? 30  SER A CB  1 
ATOM   6    O OG  . SER A 1 1   ? 48.380  1.266   -12.230 1.00 64.09  ? 30  SER A OG  1 
ATOM   7    N N   . THR A 1 2   ? 46.835  1.447   -14.171 1.00 70.59  ? 31  THR A N   1 
ATOM   8    C CA  . THR A 1 2   ? 45.486  0.968   -14.410 1.00 67.63  ? 31  THR A CA  1 
ATOM   9    C C   . THR A 1 2   ? 44.773  0.766   -13.069 1.00 52.18  ? 31  THR A C   1 
ATOM   10   O O   . THR A 1 2   ? 43.577  0.499   -13.085 1.00 48.61  ? 31  THR A O   1 
ATOM   11   C CB  . THR A 1 2   ? 45.515  -0.327  -15.229 1.00 67.97  ? 31  THR A CB  1 
ATOM   12   O OG1 . THR A 1 2   ? 46.560  -1.045  -14.573 1.00 63.54  ? 31  THR A OG1 1 
ATOM   13   C CG2 . THR A 1 2   ? 45.739  -0.107  -16.719 1.00 59.80  ? 31  THR A CG2 1 
ATOM   14   N N   . ASN A 1 3   ? 45.485  0.860   -11.924 1.00 40.78  ? 32  ASN A N   1 
ATOM   15   C CA  . ASN A 1 3   ? 44.832  0.604   -10.650 1.00 32.11  ? 32  ASN A CA  1 
ATOM   16   C C   . ASN A 1 3   ? 44.040  1.834   -10.228 1.00 27.85  ? 32  ASN A C   1 
ATOM   17   O O   . ASN A 1 3   ? 44.593  2.831   -9.792  1.00 27.33  ? 32  ASN A O   1 
ATOM   18   C CB  . ASN A 1 3   ? 45.754  0.184   -9.518  1.00 36.24  ? 32  ASN A CB  1 
ATOM   19   C CG  . ASN A 1 3   ? 44.962  -0.468  -8.407  1.00 37.21  ? 32  ASN A CG  1 
ATOM   20   O OD1 . ASN A 1 3   ? 43.806  -0.092  -8.122  1.00 31.35  ? 32  ASN A OD1 1 
ATOM   21   N ND2 . ASN A 1 3   ? 45.536  -1.508  -7.827  1.00 41.44  ? 32  ASN A ND2 1 
ATOM   22   N N   . LEU A 1 4   ? 42.715  1.733   -10.374 1.00 27.30  ? 33  LEU A N   1 
ATOM   23   C CA  . LEU A 1 4   ? 41.800  2.818   -10.089 1.00 22.49  ? 33  LEU A CA  1 
ATOM   24   C C   . LEU A 1 4   ? 41.991  3.301   -8.658  1.00 20.23  ? 33  LEU A C   1 
ATOM   25   O O   . LEU A 1 4   ? 41.902  4.495   -8.370  1.00 24.38  ? 33  LEU A O   1 
ATOM   26   C CB  . LEU A 1 4   ? 40.412  2.264   -10.360 1.00 22.92  ? 33  LEU A CB  1 
ATOM   27   C CG  . LEU A 1 4   ? 39.235  3.174   -10.008 1.00 24.31  ? 33  LEU A CG  1 
ATOM   28   C CD1 . LEU A 1 4   ? 39.287  4.425   -10.817 1.00 23.44  ? 33  LEU A CD1 1 
ATOM   29   C CD2 . LEU A 1 4   ? 37.922  2.417   -10.255 1.00 25.17  ? 33  LEU A CD2 1 
ATOM   30   N N   . LYS A 1 5   ? 42.268  2.385   -7.748  1.00 20.37  ? 34  LYS A N   1 
ATOM   31   C CA  . LYS A 1 5   ? 42.446  2.751   -6.354  1.00 21.25  ? 34  LYS A CA  1 
ATOM   32   C C   . LYS A 1 5   ? 43.625  3.710   -6.122  1.00 23.07  ? 34  LYS A C   1 
ATOM   33   O O   . LYS A 1 5   ? 43.514  4.668   -5.365  1.00 22.67  ? 34  LYS A O   1 
ATOM   34   C CB  . LYS A 1 5   ? 42.571  1.487   -5.495  1.00 23.68  ? 34  LYS A CB  1 
ATOM   35   C CG  . LYS A 1 5   ? 42.353  1.788   -4.021  1.00 26.94  ? 34  LYS A CG  1 
ATOM   36   C CD  . LYS A 1 5   ? 42.443  0.557   -3.122  1.00 29.93  ? 34  LYS A CD  1 
ATOM   37   C CE  . LYS A 1 5   ? 41.938  0.823   -1.737  1.00 31.42  ? 34  LYS A CE  1 
ATOM   38   N NZ  . LYS A 1 5   ? 42.205  -0.395  -0.958  1.00 34.64  ? 34  LYS A NZ  1 
ATOM   39   N N   . ASP A 1 6   ? 44.757  3.521   -6.808  1.00 26.82  ? 35  ASP A N   1 
ATOM   40   C CA  . ASP A 1 6   ? 45.874  4.457   -6.686  1.00 26.86  ? 35  ASP A CA  1 
ATOM   41   C C   . ASP A 1 6   ? 45.588  5.792   -7.381  1.00 23.67  ? 35  ASP A C   1 
ATOM   42   O O   . ASP A 1 6   ? 46.012  6.856   -6.907  1.00 20.97  ? 35  ASP A O   1 
ATOM   43   C CB  . ASP A 1 6   ? 47.153  3.813   -7.177  1.00 28.64  ? 35  ASP A CB  1 
ATOM   44   C CG  . ASP A 1 6   ? 47.545  2.602   -6.346  1.00 32.03  ? 35  ASP A CG  1 
ATOM   45   O OD1 . ASP A 1 6   ? 47.737  2.790   -5.138  1.00 35.48  ? 35  ASP A OD1 1 
ATOM   46   O OD2 . ASP A 1 6   ? 47.593  1.489   -6.909  1.00 41.95  ? 35  ASP A OD2 1 
ATOM   47   N N   . ILE A 1 7   ? 44.887  5.735   -8.514  1.00 24.53  ? 36  ILE A N   1 
ATOM   48   C CA  . ILE A 1 7   ? 44.516  6.947   -9.223  1.00 27.40  ? 36  ILE A CA  1 
ATOM   49   C C   . ILE A 1 7   ? 43.600  7.787   -8.334  1.00 28.74  ? 36  ILE A C   1 
ATOM   50   O O   . ILE A 1 7   ? 43.712  9.007   -8.248  1.00 25.15  ? 36  ILE A O   1 
ATOM   51   C CB  . ILE A 1 7   ? 43.882  6.559   -10.569 1.00 31.81  ? 36  ILE A CB  1 
ATOM   52   C CG1 . ILE A 1 7   ? 44.954  5.945   -11.487 1.00 33.45  ? 36  ILE A CG1 1 
ATOM   53   C CG2 . ILE A 1 7   ? 43.194  7.743   -11.228 1.00 31.36  ? 36  ILE A CG2 1 
ATOM   54   C CD1 . ILE A 1 7   ? 44.411  4.893   -12.449 1.00 37.16  ? 36  ILE A CD1 1 
ATOM   55   N N   . LEU A 1 8   ? 42.677  7.112   -7.657  1.00 27.70  ? 37  LEU A N   1 
ATOM   56   C CA  . LEU A 1 8   ? 41.728  7.820   -6.823  1.00 26.83  ? 37  LEU A CA  1 
ATOM   57   C C   . LEU A 1 8   ? 42.437  8.416   -5.617  1.00 23.21  ? 37  LEU A C   1 
ATOM   58   O O   . LEU A 1 8   ? 42.193  9.562   -5.246  1.00 22.84  ? 37  LEU A O   1 
ATOM   59   C CB  . LEU A 1 8   ? 40.630  6.791   -6.569  1.00 27.47  ? 37  LEU A CB  1 
ATOM   60   C CG  . LEU A 1 8   ? 39.500  7.165   -5.627  1.00 30.03  ? 37  LEU A CG  1 
ATOM   61   C CD1 . LEU A 1 8   ? 38.731  8.437   -6.012  1.00 31.18  ? 37  LEU A CD1 1 
ATOM   62   C CD2 . LEU A 1 8   ? 38.603  5.930   -5.623  1.00 30.21  ? 37  LEU A CD2 1 
ATOM   63   N N   . ALA A 1 9   ? 43.372  7.673   -5.024  1.00 21.89  ? 38  ALA A N   1 
ATOM   64   C CA  . ALA A 1 9   ? 44.148  8.149   -3.898  1.00 21.22  ? 38  ALA A CA  1 
ATOM   65   C C   . ALA A 1 9   ? 44.861  9.458   -4.219  1.00 24.19  ? 38  ALA A C   1 
ATOM   66   O O   . ALA A 1 9   ? 44.981  10.290  -3.342  1.00 22.96  ? 38  ALA A O   1 
ATOM   67   C CB  . ALA A 1 9   ? 45.144  7.090   -3.428  1.00 21.54  ? 38  ALA A CB  1 
ATOM   68   N N   . ASP A 1 10  ? 45.284  9.652   -5.473  1.00 23.52  ? 39  ASP A N   1 
ATOM   69   C CA  . ASP A 1 10  ? 46.004  10.853  -5.883  1.00 28.05  ? 39  ASP A CA  1 
ATOM   70   C C   . ASP A 1 10  ? 45.066  12.045  -6.087  1.00 27.28  ? 39  ASP A C   1 
ATOM   71   O O   . ASP A 1 10  ? 45.440  13.165  -5.752  1.00 29.89  ? 39  ASP A O   1 
ATOM   72   C CB  . ASP A 1 10  ? 46.904  10.573  -7.080  1.00 29.43  ? 39  ASP A CB  1 
ATOM   73   C CG  . ASP A 1 10  ? 48.103  9.667   -6.801  1.00 35.73  ? 39  ASP A CG  1 
ATOM   74   O OD1 . ASP A 1 10  ? 48.555  9.582   -5.629  1.00 39.19  ? 39  ASP A OD1 1 
ATOM   75   O OD2 . ASP A 1 10  ? 48.543  9.019   -7.757  1.00 40.67  ? 39  ASP A OD2 1 
ATOM   76   N N   . LEU A 1 11  ? 43.819  11.788  -6.528  1.00 24.68  ? 40  LEU A N   1 
ATOM   77   C CA  . LEU A 1 11  ? 42.821  12.818  -6.783  1.00 24.39  ? 40  LEU A CA  1 
ATOM   78   C C   . LEU A 1 11  ? 42.249  13.395  -5.494  1.00 23.62  ? 40  LEU A C   1 
ATOM   79   O O   . LEU A 1 11  ? 41.937  14.571  -5.433  1.00 29.01  ? 40  LEU A O   1 
ATOM   80   C CB  . LEU A 1 11  ? 41.682  12.264  -7.624  1.00 25.09  ? 40  LEU A CB  1 
ATOM   81   C CG  . LEU A 1 11  ? 42.030  11.820  -9.042  1.00 30.41  ? 40  LEU A CG  1 
ATOM   82   C CD1 . LEU A 1 11  ? 40.848  11.029  -9.605  1.00 28.15  ? 40  LEU A CD1 1 
ATOM   83   C CD2 . LEU A 1 11  ? 42.365  12.995  -9.934  1.00 33.10  ? 40  LEU A CD2 1 
ATOM   84   N N   . ILE A 1 12  ? 42.083  12.572  -4.463  1.00 22.64  ? 41  ILE A N   1 
ATOM   85   C CA  . ILE A 1 12  ? 41.328  12.949  -3.291  1.00 22.48  ? 41  ILE A CA  1 
ATOM   86   C C   . ILE A 1 12  ? 41.930  14.166  -2.595  1.00 26.17  ? 41  ILE A C   1 
ATOM   87   O O   . ILE A 1 12  ? 41.199  15.113  -2.281  1.00 26.52  ? 41  ILE A O   1 
ATOM   88   C CB  . ILE A 1 12  ? 41.163  11.746  -2.354  1.00 21.36  ? 41  ILE A CB  1 
ATOM   89   C CG1 . ILE A 1 12  ? 40.126  10.768  -2.912  1.00 19.41  ? 41  ILE A CG1 1 
ATOM   90   C CG2 . ILE A 1 12  ? 40.802  12.200  -0.937  1.00 23.12  ? 41  ILE A CG2 1 
ATOM   91   C CD1 . ILE A 1 12  ? 40.208  9.368   -2.348  1.00 18.83  ? 41  ILE A CD1 1 
ATOM   92   N N   . PRO A 1 13  ? 43.252  14.239  -2.310  1.00 27.77  ? 42  PRO A N   1 
ATOM   93   C CA  . PRO A 1 13  ? 43.781  15.413  -1.605  1.00 28.08  ? 42  PRO A CA  1 
ATOM   94   C C   . PRO A 1 13  ? 43.527  16.736  -2.305  1.00 28.84  ? 42  PRO A C   1 
ATOM   95   O O   . PRO A 1 13  ? 43.286  17.773  -1.665  1.00 26.06  ? 42  PRO A O   1 
ATOM   96   C CB  . PRO A 1 13  ? 45.323  15.126  -1.411  1.00 28.36  ? 42  PRO A CB  1 
ATOM   97   C CG  . PRO A 1 13  ? 45.510  13.693  -1.853  1.00 27.68  ? 42  PRO A CG  1 
ATOM   98   C CD  . PRO A 1 13  ? 44.249  13.166  -2.492  1.00 25.68  ? 42  PRO A CD  1 
ATOM   99   N N   . LYS A 1 14  ? 43.609  16.688  -3.636  1.00 31.90  ? 43  LYS A N   1 
ATOM   100  C CA  . LYS A 1 14  ? 43.375  17.854  -4.466  1.00 36.52  ? 43  LYS A CA  1 
ATOM   101  C C   . LYS A 1 14  ? 41.980  18.406  -4.174  1.00 32.39  ? 43  LYS A C   1 
ATOM   102  O O   . LYS A 1 14  ? 41.816  19.584  -3.957  1.00 29.96  ? 43  LYS A O   1 
ATOM   103  C CB  . LYS A 1 14  ? 43.407  17.442  -5.944  1.00 41.03  ? 43  LYS A CB  1 
ATOM   104  C CG  . LYS A 1 14  ? 44.772  17.057  -6.560  1.00 54.07  ? 43  LYS A CG  1 
ATOM   105  C CD  . LYS A 1 14  ? 44.612  16.638  -8.021  1.00 60.17  ? 43  LYS A CD  1 
ATOM   106  C CE  . LYS A 1 14  ? 45.836  16.624  -8.887  1.00 72.33  ? 43  LYS A CE  1 
ATOM   107  N NZ  . LYS A 1 14  ? 46.793  15.584  -8.499  1.00 79.49  ? 43  LYS A NZ  1 
ATOM   108  N N   . GLU A 1 15  ? 40.989  17.517  -4.174  1.00 29.75  ? 44  GLU A N   1 
ATOM   109  C CA  . GLU A 1 15  ? 39.591  17.906  -4.083  1.00 31.59  ? 44  GLU A CA  1 
ATOM   110  C C   . GLU A 1 15  ? 39.258  18.324  -2.653  1.00 27.02  ? 44  GLU A C   1 
ATOM   111  O O   . GLU A 1 15  ? 38.529  19.289  -2.458  1.00 29.21  ? 44  GLU A O   1 
ATOM   112  C CB  . GLU A 1 15  ? 38.748  16.726  -4.539  1.00 31.87  ? 44  GLU A CB  1 
ATOM   113  C CG  . GLU A 1 15  ? 37.322  17.100  -4.896  1.00 42.05  ? 44  GLU A CG  1 
ATOM   114  C CD  . GLU A 1 15  ? 37.224  18.079  -6.048  1.00 47.11  ? 44  GLU A CD  1 
ATOM   115  O OE1 . GLU A 1 15  ? 38.018  17.944  -7.010  1.00 48.19  ? 44  GLU A OE1 1 
ATOM   116  O OE2 . GLU A 1 15  ? 36.344  18.971  -5.950  1.00 55.74  ? 44  GLU A OE2 1 
ATOM   117  N N   . GLN A 1 16  ? 39.799  17.609  -1.677  1.00 24.54  ? 45  GLN A N   1 
ATOM   118  C CA  . GLN A 1 16  ? 39.699  18.007  -0.278  1.00 28.56  ? 45  GLN A CA  1 
ATOM   119  C C   . GLN A 1 16  ? 40.117  19.479  -0.097  1.00 28.41  ? 45  GLN A C   1 
ATOM   120  O O   . GLN A 1 16  ? 39.410  20.254  0.550   1.00 25.92  ? 45  GLN A O   1 
ATOM   121  C CB  . GLN A 1 16  ? 40.542  17.134  0.655   1.00 25.16  ? 45  GLN A CB  1 
ATOM   122  C CG  . GLN A 1 16  ? 40.033  15.705  0.809   1.00 29.12  ? 45  GLN A CG  1 
ATOM   123  C CD  . GLN A 1 16  ? 40.966  14.821  1.604   1.00 30.24  ? 45  GLN A CD  1 
ATOM   124  O OE1 . GLN A 1 16  ? 42.171  15.073  1.672   1.00 32.00  ? 45  GLN A OE1 1 
ATOM   125  N NE2 . GLN A 1 16  ? 40.446  13.730  2.149   1.00 28.63  ? 45  GLN A NE2 1 
ATOM   126  N N   . ALA A 1 17  ? 41.263  19.870  -0.680  1.00 31.18  ? 46  ALA A N   1 
ATOM   127  C CA  . ALA A 1 17  ? 41.829  21.187  -0.413  1.00 33.47  ? 46  ALA A CA  1 
ATOM   128  C C   . ALA A 1 17  ? 41.002  22.255  -1.126  1.00 34.24  ? 46  ALA A C   1 
ATOM   129  O O   . ALA A 1 17  ? 40.756  23.311  -0.548  1.00 29.86  ? 46  ALA A O   1 
ATOM   130  C CB  . ALA A 1 17  ? 43.302  21.243  -0.797  1.00 32.99  ? 46  ALA A CB  1 
ATOM   131  N N   . ARG A 1 18  ? 40.534  21.925  -2.336  1.00 31.71  ? 47  ARG A N   1 
ATOM   132  C CA  . ARG A 1 18  ? 39.665  22.773  -3.126  1.00 35.88  ? 47  ARG A CA  1 
ATOM   133  C C   . ARG A 1 18  ? 38.322  23.009  -2.428  1.00 35.00  ? 47  ARG A C   1 
ATOM   134  O O   . ARG A 1 18  ? 37.821  24.123  -2.432  1.00 30.05  ? 47  ARG A O   1 
ATOM   135  C CB  . ARG A 1 18  ? 39.499  22.138  -4.510  1.00 37.55  ? 47  ARG A CB  1 
ATOM   136  C CG  . ARG A 1 18  ? 38.351  22.637  -5.365  1.00 43.70  ? 47  ARG A CG  1 
ATOM   137  C CD  . ARG A 1 18  ? 38.478  22.078  -6.789  1.00 57.09  ? 47  ARG A CD  1 
ATOM   138  N NE  . ARG A 1 18  ? 37.216  22.153  -7.533  1.00 62.10  ? 47  ARG A NE  1 
ATOM   139  C CZ  . ARG A 1 18  ? 37.004  21.683  -8.761  1.00 78.36  ? 47  ARG A CZ  1 
ATOM   140  N NH1 . ARG A 1 18  ? 38.001  21.160  -9.462  1.00 82.00  ? 47  ARG A NH1 1 
ATOM   141  N NH2 . ARG A 1 18  ? 35.789  21.747  -9.292  1.00 75.83  ? 47  ARG A NH2 1 
ATOM   142  N N   . ILE A 1 19  ? 37.739  21.973  -1.817  1.00 27.45  ? 48  ILE A N   1 
ATOM   143  C CA  . ILE A 1 19  ? 36.532  22.161  -1.046  1.00 28.15  ? 48  ILE A CA  1 
ATOM   144  C C   . ILE A 1 19  ? 36.823  22.952  0.228   1.00 31.37  ? 48  ILE A C   1 
ATOM   145  O O   . ILE A 1 19  ? 35.974  23.728  0.678   1.00 31.46  ? 48  ILE A O   1 
ATOM   146  C CB  . ILE A 1 19  ? 35.841  20.808  -0.786  1.00 27.53  ? 48  ILE A CB  1 
ATOM   147  C CG1 . ILE A 1 19  ? 35.196  20.317  -2.045  1.00 28.08  ? 48  ILE A CG1 1 
ATOM   148  C CG2 . ILE A 1 19  ? 34.821  20.902  0.350   1.00 25.32  ? 48  ILE A CG2 1 
ATOM   149  C CD1 . ILE A 1 19  ? 34.831  18.834  -2.023  1.00 31.91  ? 48  ILE A CD1 1 
ATOM   150  N N   . LYS A 1 20  ? 37.989  22.753  0.848   1.00 29.48  ? 49  LYS A N   1 
ATOM   151  C CA  . LYS A 1 20  ? 38.229  23.332  2.164   1.00 31.11  ? 49  LYS A CA  1 
ATOM   152  C C   . LYS A 1 20  ? 38.287  24.850  2.005   1.00 37.09  ? 49  LYS A C   1 
ATOM   153  O O   . LYS A 1 20  ? 37.740  25.581  2.832   1.00 33.85  ? 49  LYS A O   1 
ATOM   154  C CB  . LYS A 1 20  ? 39.519  22.793  2.780   1.00 33.44  ? 49  LYS A CB  1 
ATOM   155  C CG  . LYS A 1 20  ? 39.878  23.254  4.176   1.00 37.58  ? 49  LYS A CG  1 
ATOM   156  C CD  . LYS A 1 20  ? 41.347  22.932  4.461   1.00 41.42  ? 49  LYS A CD  1 
ATOM   157  C CE  . LYS A 1 20  ? 41.921  23.433  5.754   1.00 46.10  ? 49  LYS A CE  1 
ATOM   158  N NZ  . LYS A 1 20  ? 41.138  23.003  6.913   1.00 48.55  ? 49  LYS A NZ  1 
ATOM   159  N N   . THR A 1 21  ? 38.924  25.285  0.912   1.00 34.24  ? 50  THR A N   1 
ATOM   160  C CA  . THR A 1 21  ? 39.118  26.702  0.622   1.00 40.70  ? 50  THR A CA  1 
ATOM   161  C C   . THR A 1 21  ? 37.796  27.356  0.238   1.00 40.40  ? 50  THR A C   1 
ATOM   162  O O   . THR A 1 21  ? 37.514  28.475  0.663   1.00 39.29  ? 50  THR A O   1 
ATOM   163  C CB  . THR A 1 21  ? 40.136  26.853  -0.510  1.00 39.16  ? 50  THR A CB  1 
ATOM   164  O OG1 . THR A 1 21  ? 41.367  26.338  -0.008  1.00 39.90  ? 50  THR A OG1 1 
ATOM   165  C CG2 . THR A 1 21  ? 40.352  28.299  -0.906  1.00 42.86  ? 50  THR A CG2 1 
ATOM   166  N N   . PHE A 1 22  ? 37.038  26.674  -0.636  1.00 36.15  ? 51  PHE A N   1 
ATOM   167  C CA  . PHE A 1 22  ? 35.715  27.116  -1.040  1.00 32.45  ? 51  PHE A CA  1 
ATOM   168  C C   . PHE A 1 22  ? 34.813  27.312  0.179   1.00 29.94  ? 51  PHE A C   1 
ATOM   169  O O   . PHE A 1 22  ? 34.093  28.294  0.267   1.00 35.21  ? 51  PHE A O   1 
ATOM   170  C CB  . PHE A 1 22  ? 35.169  26.136  -2.071  1.00 31.40  ? 51  PHE A CB  1 
ATOM   171  C CG  . PHE A 1 22  ? 33.763  26.460  -2.547  1.00 34.22  ? 51  PHE A CG  1 
ATOM   172  C CD1 . PHE A 1 22  ? 33.473  27.709  -3.086  1.00 35.88  ? 51  PHE A CD1 1 
ATOM   173  C CD2 . PHE A 1 22  ? 32.732  25.523  -2.424  1.00 31.25  ? 51  PHE A CD2 1 
ATOM   174  C CE1 . PHE A 1 22  ? 32.178  28.019  -3.493  1.00 35.97  ? 51  PHE A CE1 1 
ATOM   175  C CE2 . PHE A 1 22  ? 31.445  25.839  -2.814  1.00 33.16  ? 51  PHE A CE2 1 
ATOM   176  C CZ  . PHE A 1 22  ? 31.162  27.100  -3.324  1.00 38.47  ? 51  PHE A CZ  1 
ATOM   177  N N   . ARG A 1 23  ? 34.827  26.395  1.126   1.00 32.65  ? 52  ARG A N   1 
ATOM   178  C CA  . ARG A 1 23  ? 33.995  26.528  2.316   1.00 32.53  ? 52  ARG A CA  1 
ATOM   179  C C   . ARG A 1 23  ? 34.518  27.655  3.215   1.00 39.12  ? 52  ARG A C   1 
ATOM   180  O O   . ARG A 1 23  ? 33.731  28.396  3.809   1.00 30.84  ? 52  ARG A O   1 
ATOM   181  C CB  . ARG A 1 23  ? 33.914  25.224  3.110   1.00 35.09  ? 52  ARG A CB  1 
ATOM   182  C CG  . ARG A 1 23  ? 33.201  24.128  2.321   1.00 36.78  ? 52  ARG A CG  1 
ATOM   183  C CD  . ARG A 1 23  ? 33.033  22.875  3.119   1.00 34.85  ? 52  ARG A CD  1 
ATOM   184  N NE  . ARG A 1 23  ? 32.201  23.160  4.289   1.00 40.38  ? 52  ARG A NE  1 
ATOM   185  C CZ  . ARG A 1 23  ? 31.856  22.292  5.208   1.00 43.36  ? 52  ARG A CZ  1 
ATOM   186  N NH1 . ARG A 1 23  ? 32.366  21.082  5.158   1.00 41.65  ? 52  ARG A NH1 1 
ATOM   187  N NH2 . ARG A 1 23  ? 30.982  22.633  6.159   1.00 42.94  ? 52  ARG A NH2 1 
ATOM   188  N N   . GLN A 1 24  ? 35.847  27.805  3.300   1.00 36.74  ? 53  GLN A N   1 
ATOM   189  C CA  . GLN A 1 24  ? 36.428  28.907  4.058   1.00 40.13  ? 53  GLN A CA  1 
ATOM   190  C C   . GLN A 1 24  ? 35.970  30.245  3.485   1.00 38.79  ? 53  GLN A C   1 
ATOM   191  O O   . GLN A 1 24  ? 35.545  31.118  4.235   1.00 41.89  ? 53  GLN A O   1 
ATOM   192  C CB  . GLN A 1 24  ? 37.957  28.885  4.074   1.00 36.26  ? 53  GLN A CB  1 
ATOM   193  C CG  . GLN A 1 24  ? 38.522  27.846  5.035   1.00 40.03  ? 53  GLN A CG  1 
ATOM   194  C CD  . GLN A 1 24  ? 40.021  27.725  4.886   1.00 41.59  ? 53  GLN A CD  1 
ATOM   195  O OE1 . GLN A 1 24  ? 40.601  28.102  3.856   1.00 47.11  ? 53  GLN A OE1 1 
ATOM   196  N NE2 . GLN A 1 24  ? 40.658  27.236  5.933   1.00 47.09  ? 53  GLN A NE2 1 
ATOM   197  N N   . GLN A 1 25  ? 36.053  30.384  2.162   1.00 42.28  ? 54  GLN A N   1 
ATOM   198  C CA  . GLN A 1 25  ? 35.727  31.628  1.499   1.00 43.25  ? 54  GLN A CA  1 
ATOM   199  C C   . GLN A 1 25  ? 34.223  31.876  1.361   1.00 48.03  ? 54  GLN A C   1 
ATOM   200  O O   . GLN A 1 25  ? 33.818  33.037  1.325   1.00 47.83  ? 54  GLN A O   1 
ATOM   201  C CB  . GLN A 1 25  ? 36.359  31.604  0.115   1.00 54.50  ? 54  GLN A CB  1 
ATOM   202  C CG  . GLN A 1 25  ? 37.850  31.912  0.103   1.00 57.91  ? 54  GLN A CG  1 
ATOM   203  C CD  . GLN A 1 25  ? 38.378  31.933  -1.314  1.00 68.76  ? 54  GLN A CD  1 
ATOM   204  O OE1 . GLN A 1 25  ? 39.427  31.359  -1.619  1.00 67.89  ? 54  GLN A OE1 1 
ATOM   205  N NE2 . GLN A 1 25  ? 37.648  32.601  -2.200  1.00 78.32  ? 54  GLN A NE2 1 
ATOM   206  N N   . HIS A 1 26  ? 33.397  30.821  1.231   1.00 40.46  ? 55  HIS A N   1 
ATOM   207  C CA  . HIS A 1 26  ? 31.993  31.007  0.886   1.00 38.79  ? 55  HIS A CA  1 
ATOM   208  C C   . HIS A 1 26  ? 31.014  30.113  1.635   1.00 37.30  ? 55  HIS A C   1 
ATOM   209  O O   . HIS A 1 26  ? 29.861  30.023  1.219   1.00 40.84  ? 55  HIS A O   1 
ATOM   210  C CB  . HIS A 1 26  ? 31.746  30.765  -0.604  1.00 40.73  ? 55  HIS A CB  1 
ATOM   211  C CG  . HIS A 1 26  ? 32.661  31.517  -1.500  1.00 50.40  ? 55  HIS A CG  1 
ATOM   212  N ND1 . HIS A 1 26  ? 32.489  32.861  -1.756  1.00 62.45  ? 55  HIS A ND1 1 
ATOM   213  C CD2 . HIS A 1 26  ? 33.716  31.136  -2.231  1.00 56.74  ? 55  HIS A CD2 1 
ATOM   214  C CE1 . HIS A 1 26  ? 33.432  33.265  -2.600  1.00 63.22  ? 55  HIS A CE1 1 
ATOM   215  N NE2 . HIS A 1 26  ? 34.188  32.230  -2.907  1.00 62.10  ? 55  HIS A NE2 1 
ATOM   216  N N   . GLY A 1 27  ? 31.416  29.537  2.764   1.00 34.56  ? 56  GLY A N   1 
ATOM   217  C CA  . GLY A 1 27  ? 30.535  28.678  3.539   1.00 39.55  ? 56  GLY A CA  1 
ATOM   218  C C   . GLY A 1 27  ? 29.245  29.370  4.003   1.00 43.46  ? 56  GLY A C   1 
ATOM   219  O O   . GLY A 1 27  ? 28.210  28.707  4.169   1.00 35.49  ? 56  GLY A O   1 
ATOM   220  N N   . LYS A 1 28  ? 29.316  30.686  4.288   1.00 41.54  ? 57  LYS A N   1 
ATOM   221  C CA  . LYS A 1 28  ? 28.157  31.413  4.806   1.00 42.13  ? 57  LYS A CA  1 
ATOM   222  C C   . LYS A 1 28  ? 27.266  31.997  3.703   1.00 34.84  ? 57  LYS A C   1 
ATOM   223  O O   . LYS A 1 28  ? 26.238  32.567  4.009   1.00 39.80  ? 57  LYS A O   1 
ATOM   224  C CB  . LYS A 1 28  ? 28.621  32.477  5.810   1.00 47.12  ? 57  LYS A CB  1 
ATOM   225  C CG  . LYS A 1 28  ? 29.475  31.876  6.906   1.00 54.49  ? 57  LYS A CG  1 
ATOM   226  C CD  . LYS A 1 28  ? 29.609  32.677  8.188   1.00 62.54  ? 57  LYS A CD  1 
ATOM   227  C CE  . LYS A 1 28  ? 30.266  31.855  9.249   1.00 65.11  ? 57  LYS A CE  1 
ATOM   228  N NZ  . LYS A 1 28  ? 30.320  32.617  10.502  1.00 76.99  ? 57  LYS A NZ  1 
ATOM   229  N N   . THR A 1 29  ? 27.647  31.870  2.431   1.00 34.19  ? 58  THR A N   1 
ATOM   230  C CA  . THR A 1 29  ? 26.889  32.395  1.302   1.00 34.05  ? 58  THR A CA  1 
ATOM   231  C C   . THR A 1 29  ? 25.547  31.673  1.159   1.00 36.68  ? 58  THR A C   1 
ATOM   232  O O   . THR A 1 29  ? 25.492  30.438  1.142   1.00 31.16  ? 58  THR A O   1 
ATOM   233  C CB  . THR A 1 29  ? 27.716  32.182  0.039   1.00 34.86  ? 58  THR A CB  1 
ATOM   234  O OG1 . THR A 1 29  ? 28.922  32.830  0.408   1.00 39.73  ? 58  THR A OG1 1 
ATOM   235  C CG2 . THR A 1 29  ? 27.105  32.751  -1.225  1.00 34.74  ? 58  THR A CG2 1 
ATOM   236  N N   . VAL A 1 30  ? 24.491  32.447  0.913   1.00 34.06  ? 59  VAL A N   1 
ATOM   237  C CA  . VAL A 1 30  ? 23.157  31.895  0.858   1.00 32.38  ? 59  VAL A CA  1 
ATOM   238  C C   . VAL A 1 30  ? 22.873  31.474  -0.570  1.00 36.99  ? 59  VAL A C   1 
ATOM   239  O O   . VAL A 1 30  ? 23.041  32.254  -1.509  1.00 34.92  ? 59  VAL A O   1 
ATOM   240  C CB  . VAL A 1 30  ? 22.143  32.934  1.371   1.00 32.55  ? 59  VAL A CB  1 
ATOM   241  C CG1 . VAL A 1 30  ? 20.688  32.505  1.164   1.00 32.81  ? 59  VAL A CG1 1 
ATOM   242  C CG2 . VAL A 1 30  ? 22.388  33.243  2.831   1.00 31.94  ? 59  VAL A CG2 1 
ATOM   243  N N   . VAL A 1 31  ? 22.409  30.236  -0.732  1.00 33.59  ? 60  VAL A N   1 
ATOM   244  C CA  . VAL A 1 31  ? 22.164  29.750  -2.071  1.00 33.61  ? 60  VAL A CA  1 
ATOM   245  C C   . VAL A 1 31  ? 20.674  29.532  -2.302  1.00 30.22  ? 60  VAL A C   1 
ATOM   246  O O   . VAL A 1 31  ? 20.289  29.208  -3.412  1.00 31.13  ? 60  VAL A O   1 
ATOM   247  C CB  . VAL A 1 31  ? 22.945  28.462  -2.331  1.00 33.30  ? 60  VAL A CB  1 
ATOM   248  C CG1 . VAL A 1 31  ? 24.442  28.726  -2.244  1.00 37.46  ? 60  VAL A CG1 1 
ATOM   249  C CG2 . VAL A 1 31  ? 22.480  27.336  -1.414  1.00 36.62  ? 60  VAL A CG2 1 
ATOM   250  N N   . GLY A 1 32  ? 19.848  29.698  -1.266  1.00 29.46  ? 61  GLY A N   1 
ATOM   251  C CA  . GLY A 1 32  ? 18.415  29.522  -1.446  1.00 27.81  ? 61  GLY A CA  1 
ATOM   252  C C   . GLY A 1 32  ? 17.678  29.755  -0.143  1.00 26.99  ? 61  GLY A C   1 
ATOM   253  O O   . GLY A 1 32  ? 18.297  29.933  0.899   1.00 29.56  ? 61  GLY A O   1 
ATOM   254  N N   . GLN A 1 33  ? 16.351  29.775  -0.219  1.00 26.67  ? 62  GLN A N   1 
ATOM   255  C CA  . GLN A 1 33  ? 15.530  30.054  0.941   1.00 31.81  ? 62  GLN A CA  1 
ATOM   256  C C   . GLN A 1 33  ? 14.645  28.833  1.146   1.00 30.92  ? 62  GLN A C   1 
ATOM   257  O O   . GLN A 1 33  ? 14.288  28.182  0.161   1.00 31.89  ? 62  GLN A O   1 
ATOM   258  C CB  . GLN A 1 33  ? 14.611  31.268  0.799   1.00 37.67  ? 62  GLN A CB  1 
ATOM   259  C CG  . GLN A 1 33  ? 15.181  32.437  -0.006  1.00 47.37  ? 62  GLN A CG  1 
ATOM   260  C CD  . GLN A 1 33  ? 16.032  33.375  0.815   1.00 56.75  ? 62  GLN A CD  1 
ATOM   261  O OE1 . GLN A 1 33  ? 17.242  33.501  0.591   1.00 57.63  ? 62  GLN A OE1 1 
ATOM   262  N NE2 . GLN A 1 33  ? 15.403  34.045  1.769   1.00 56.29  ? 62  GLN A NE2 1 
ATOM   263  N N   . ILE A 1 34  ? 14.304  28.543  2.414   1.00 24.72  ? 63  ILE A N   1 
ATOM   264  C CA  . ILE A 1 34  ? 13.298  27.532  2.717   1.00 25.29  ? 63  ILE A CA  1 
ATOM   265  C C   . ILE A 1 34  ? 11.971  28.214  3.040   1.00 23.65  ? 63  ILE A C   1 
ATOM   266  O O   . ILE A 1 34  ? 11.917  29.034  3.928   1.00 28.82  ? 63  ILE A O   1 
ATOM   267  C CB  . ILE A 1 34  ? 13.737  26.658  3.901   1.00 24.74  ? 63  ILE A CB  1 
ATOM   268  C CG1 . ILE A 1 34  ? 15.134  26.059  3.667   1.00 28.54  ? 63  ILE A CG1 1 
ATOM   269  C CG2 . ILE A 1 34  ? 12.708  25.563  4.172   1.00 24.02  ? 63  ILE A CG2 1 
ATOM   270  C CD1 . ILE A 1 34  ? 15.812  25.593  4.936   1.00 31.63  ? 63  ILE A CD1 1 
ATOM   271  N N   . THR A 1 35  ? 10.901  27.791  2.367   1.00 23.77  ? 64  THR A N   1 
ATOM   272  C CA  . THR A 1 35  ? 9.537   28.221  2.639   1.00 24.06  ? 64  THR A CA  1 
ATOM   273  C C   . THR A 1 35  ? 8.734   27.105  3.300   1.00 24.92  ? 64  THR A C   1 
ATOM   274  O O   . THR A 1 35  ? 9.068   25.911  3.188   1.00 22.80  ? 64  THR A O   1 
ATOM   275  C CB  . THR A 1 35  ? 8.821   28.623  1.344   1.00 22.14  ? 64  THR A CB  1 
ATOM   276  O OG1 . THR A 1 35  ? 8.662   27.455  0.538   1.00 24.13  ? 64  THR A OG1 1 
ATOM   277  C CG2 . THR A 1 35  ? 9.551   29.673  0.548   1.00 23.37  ? 64  THR A CG2 1 
ATOM   278  N N   . VAL A 1 36  ? 7.618   27.490  3.932   1.00 23.64  ? 65  VAL A N   1 
ATOM   279  C CA  . VAL A 1 36  ? 6.684   26.507  4.479   1.00 24.64  ? 65  VAL A CA  1 
ATOM   280  C C   . VAL A 1 36  ? 6.269   25.461  3.422   1.00 25.49  ? 65  VAL A C   1 
ATOM   281  O O   . VAL A 1 36  ? 6.291   24.255  3.685   1.00 24.25  ? 65  VAL A O   1 
ATOM   282  C CB  . VAL A 1 36  ? 5.490   27.254  5.103   1.00 24.16  ? 65  VAL A CB  1 
ATOM   283  C CG1 . VAL A 1 36  ? 4.298   26.367  5.402   1.00 25.66  ? 65  VAL A CG1 1 
ATOM   284  C CG2 . VAL A 1 36  ? 5.942   28.006  6.348   1.00 24.35  ? 65  VAL A CG2 1 
ATOM   285  N N   . ASP A 1 37  ? 5.900   25.906  2.220   1.00 23.05  ? 66  ASP A N   1 
ATOM   286  C CA  . ASP A 1 37  ? 5.491   25.013  1.156   1.00 24.27  ? 66  ASP A CA  1 
ATOM   287  C C   . ASP A 1 37  ? 6.576   23.974  0.827   1.00 24.95  ? 66  ASP A C   1 
ATOM   288  O O   . ASP A 1 37  ? 6.224   22.856  0.491   1.00 22.76  ? 66  ASP A O   1 
ATOM   289  C CB  . ASP A 1 37  ? 5.037   25.768  -0.084  1.00 27.93  ? 66  ASP A CB  1 
ATOM   290  C CG  . ASP A 1 37  ? 3.551   26.144  -0.077  1.00 29.44  ? 66  ASP A CG  1 
ATOM   291  O OD1 . ASP A 1 37  ? 2.784   25.519  0.679   1.00 33.71  ? 66  ASP A OD1 1 
ATOM   292  O OD2 . ASP A 1 37  ? 3.164   27.063  -0.809  1.00 33.81  ? 66  ASP A OD2 1 
ATOM   293  N N   . MET A 1 38  ? 7.865   24.353  0.865   1.00 23.94  ? 67  MET A N   1 
ATOM   294  C CA  . MET A 1 38  ? 8.937   23.429  0.534   1.00 26.69  ? 67  MET A CA  1 
ATOM   295  C C   . MET A 1 38  ? 9.004   22.298  1.565   1.00 25.60  ? 67  MET A C   1 
ATOM   296  O O   . MET A 1 38  ? 9.281   21.146  1.197   1.00 28.65  ? 67  MET A O   1 
ATOM   297  C CB  . MET A 1 38  ? 10.295  24.132  0.448   1.00 25.88  ? 67  MET A CB  1 
ATOM   298  C CG  . MET A 1 38  ? 10.450  25.090  -0.723  1.00 28.61  ? 67  MET A CG  1 
ATOM   299  S SD  . MET A 1 38  ? 12.026  25.988  -0.562  1.00 33.99  ? 67  MET A SD  1 
ATOM   300  C CE  . MET A 1 38  ? 11.758  27.234  -1.843  1.00 35.32  ? 67  MET A CE  1 
ATOM   301  N N   . MET A 1 39  ? 8.766   22.652  2.838   1.00 23.00  ? 68  MET A N   1 
ATOM   302  C CA  . MET A 1 39  ? 8.731   21.704  3.927   1.00 22.72  ? 68  MET A CA  1 
ATOM   303  C C   . MET A 1 39  ? 7.601   20.702  3.724   1.00 23.23  ? 68  MET A C   1 
ATOM   304  O O   . MET A 1 39  ? 7.830   19.490  3.902   1.00 24.22  ? 68  MET A O   1 
ATOM   305  C CB  . MET A 1 39  ? 8.625   22.422  5.267   1.00 25.05  ? 68  MET A CB  1 
ATOM   306  C CG  . MET A 1 39  ? 9.847   23.187  5.579   1.00 26.18  ? 68  MET A CG  1 
ATOM   307  S SD  . MET A 1 39  ? 9.817   23.969  7.190   1.00 31.31  ? 68  MET A SD  1 
ATOM   308  C CE  . MET A 1 39  ? 9.898   22.592  8.339   1.00 29.45  ? 68  MET A CE  1 
ATOM   309  N N   . TYR A 1 40  ? 6.399   21.190  3.361   1.00 20.47  ? 69  TYR A N   1 
ATOM   310  C CA  . TYR A 1 40  ? 5.275   20.316  3.139   1.00 22.99  ? 69  TYR A CA  1 
ATOM   311  C C   . TYR A 1 40  ? 5.387   19.571  1.810   1.00 25.77  ? 69  TYR A C   1 
ATOM   312  O O   . TYR A 1 40  ? 4.764   18.506  1.683   1.00 28.63  ? 69  TYR A O   1 
ATOM   313  C CB  . TYR A 1 40  ? 3.919   21.029  3.162   1.00 24.81  ? 69  TYR A CB  1 
ATOM   314  C CG  . TYR A 1 40  ? 3.497   21.359  4.576   1.00 25.08  ? 69  TYR A CG  1 
ATOM   315  C CD1 . TYR A 1 40  ? 2.943   20.381  5.381   1.00 23.59  ? 69  TYR A CD1 1 
ATOM   316  C CD2 . TYR A 1 40  ? 3.648   22.642  5.093   1.00 24.15  ? 69  TYR A CD2 1 
ATOM   317  C CE1 . TYR A 1 40  ? 2.590   20.637  6.685   1.00 23.32  ? 69  TYR A CE1 1 
ATOM   318  C CE2 . TYR A 1 40  ? 3.317   22.906  6.412   1.00 26.06  ? 69  TYR A CE2 1 
ATOM   319  C CZ  . TYR A 1 40  ? 2.784   21.900  7.198   1.00 25.71  ? 69  TYR A CZ  1 
ATOM   320  O OH  . TYR A 1 40  ? 2.393   22.159  8.468   1.00 27.28  ? 69  TYR A OH  1 
ATOM   321  N N   . GLY A 1 41  ? 6.156   20.121  0.857   1.00 22.11  ? 70  GLY A N   1 
ATOM   322  C CA  . GLY A 1 41  ? 6.220   19.635  -0.506  1.00 22.76  ? 70  GLY A CA  1 
ATOM   323  C C   . GLY A 1 41  ? 7.474   18.793  -0.814  1.00 22.93  ? 70  GLY A C   1 
ATOM   324  O O   . GLY A 1 41  ? 7.944   18.750  -1.962  1.00 22.31  ? 70  GLY A O   1 
ATOM   325  N N   . GLY A 1 42  ? 8.035   18.137  0.201   1.00 23.74  ? 71  GLY A N   1 
ATOM   326  C CA  . GLY A 1 42  ? 9.124   17.188  -0.025  1.00 24.58  ? 71  GLY A CA  1 
ATOM   327  C C   . GLY A 1 42  ? 10.422  17.857  -0.479  1.00 22.06  ? 71  GLY A C   1 
ATOM   328  O O   . GLY A 1 42  ? 11.150  17.315  -1.301  1.00 23.70  ? 71  GLY A O   1 
ATOM   329  N N   . MET A 1 43  ? 10.717  19.035  0.049   1.00 20.43  ? 72  MET A N   1 
ATOM   330  C CA  . MET A 1 43  ? 11.969  19.718  -0.208  1.00 22.40  ? 72  MET A CA  1 
ATOM   331  C C   . MET A 1 43  ? 12.080  20.124  -1.683  1.00 22.50  ? 72  MET A C   1 
ATOM   332  O O   . MET A 1 43  ? 13.170  20.446  -2.126  1.00 21.98  ? 72  MET A O   1 
ATOM   333  C CB  . MET A 1 43  ? 13.156  18.836  0.160   1.00 23.54  ? 72  MET A CB  1 
ATOM   334  C CG  . MET A 1 43  ? 13.198  18.354  1.629   1.00 27.51  ? 72  MET A CG  1 
ATOM   335  S SD  . MET A 1 43  ? 14.745  17.448  1.891   1.00 32.84  ? 72  MET A SD  1 
ATOM   336  C CE  . MET A 1 43  ? 14.751  17.128  3.662   1.00 32.65  ? 72  MET A CE  1 
ATOM   337  N N   . ARG A 1 44  ? 10.972  20.122  -2.419  1.00 26.79  ? 73  ARG A N   1 
ATOM   338  C CA  . ARG A 1 44  ? 10.959  20.469  -3.832  1.00 34.78  ? 73  ARG A CA  1 
ATOM   339  C C   . ARG A 1 44  ? 11.587  21.842  -4.082  1.00 32.90  ? 73  ARG A C   1 
ATOM   340  O O   . ARG A 1 44  ? 11.164  22.835  -3.502  1.00 33.55  ? 73  ARG A O   1 
ATOM   341  C CB  . ARG A 1 44  ? 9.529   20.480  -4.390  1.00 39.94  ? 73  ARG A CB  1 
ATOM   342  C CG  . ARG A 1 44  ? 9.453   20.474  -5.913  1.00 50.17  ? 73  ARG A CG  1 
ATOM   343  C CD  . ARG A 1 44  ? 8.015   20.745  -6.401  1.00 57.17  ? 73  ARG A CD  1 
ATOM   344  N NE  . ARG A 1 44  ? 7.087   19.852  -5.695  1.00 72.41  ? 73  ARG A NE  1 
ATOM   345  C CZ  . ARG A 1 44  ? 6.424   20.120  -4.555  1.00 74.70  ? 73  ARG A CZ  1 
ATOM   346  N NH1 . ARG A 1 44  ? 6.354   21.356  -4.074  1.00 83.89  ? 73  ARG A NH1 1 
ATOM   347  N NH2 . ARG A 1 44  ? 5.819   19.143  -3.900  1.00 60.82  ? 73  ARG A NH2 1 
ATOM   348  N N   . GLY A 1 45  ? 12.587  21.877  -4.974  1.00 37.34  ? 74  GLY A N   1 
ATOM   349  C CA  . GLY A 1 45  ? 13.345  23.085  -5.267  1.00 38.93  ? 74  GLY A CA  1 
ATOM   350  C C   . GLY A 1 45  ? 14.277  23.522  -4.136  1.00 38.19  ? 74  GLY A C   1 
ATOM   351  O O   . GLY A 1 45  ? 14.715  24.660  -4.093  1.00 45.24  ? 74  GLY A O   1 
ATOM   352  N N   . MET A 1 46  ? 14.565  22.663  -3.167  1.00 31.05  ? 75  MET A N   1 
ATOM   353  C CA  . MET A 1 46  ? 15.419  23.089  -2.072  1.00 31.98  ? 75  MET A CA  1 
ATOM   354  C C   . MET A 1 46  ? 16.816  22.542  -2.342  1.00 30.96  ? 75  MET A C   1 
ATOM   355  O O   . MET A 1 46  ? 16.961  21.330  -2.510  1.00 31.31  ? 75  MET A O   1 
ATOM   356  C CB  . MET A 1 46  ? 14.836  22.535  -0.766  1.00 34.41  ? 75  MET A CB  1 
ATOM   357  C CG  . MET A 1 46  ? 15.445  23.044  0.490   1.00 33.98  ? 75  MET A CG  1 
ATOM   358  S SD  . MET A 1 46  ? 14.863  22.156  1.965   1.00 40.38  ? 75  MET A SD  1 
ATOM   359  C CE  . MET A 1 46  ? 13.201  22.745  1.665   1.00 36.52  ? 75  MET A CE  1 
ATOM   360  N N   . LYS A 1 47  ? 17.835  23.419  -2.338  1.00 30.08  ? 76  LYS A N   1 
ATOM   361  C CA  . LYS A 1 47  ? 19.224  22.977  -2.481  1.00 31.25  ? 76  LYS A CA  1 
ATOM   362  C C   . LYS A 1 47  ? 19.643  22.303  -1.172  1.00 33.46  ? 76  LYS A C   1 
ATOM   363  O O   . LYS A 1 47  ? 19.709  22.949  -0.120  1.00 34.01  ? 76  LYS A O   1 
ATOM   364  C CB  . LYS A 1 47  ? 20.135  24.135  -2.906  1.00 34.72  ? 76  LYS A CB  1 
ATOM   365  C CG  . LYS A 1 47  ? 20.066  24.446  -4.412  1.00 40.15  ? 76  LYS A CG  1 
ATOM   366  C CD  . LYS A 1 47  ? 20.782  25.746  -4.756  1.00 47.88  ? 76  LYS A CD  1 
ATOM   367  C CE  . LYS A 1 47  ? 20.712  26.112  -6.221  1.00 50.65  ? 76  LYS A CE  1 
ATOM   368  N NZ  . LYS A 1 47  ? 19.363  26.539  -6.633  1.00 55.25  ? 76  LYS A NZ  1 
ATOM   369  N N   . GLY A 1 48  ? 19.807  20.978  -1.218  1.00 26.15  ? 77  GLY A N   1 
ATOM   370  C CA  . GLY A 1 48  ? 19.878  20.191  0.011   1.00 25.93  ? 77  GLY A CA  1 
ATOM   371  C C   . GLY A 1 48  ? 21.218  19.474  0.241   1.00 23.92  ? 77  GLY A C   1 
ATOM   372  O O   . GLY A 1 48  ? 21.582  19.206  1.378   1.00 24.30  ? 77  GLY A O   1 
ATOM   373  N N   . LEU A 1 49  ? 21.924  19.099  -0.834  1.00 22.39  ? 78  LEU A N   1 
ATOM   374  C CA  . LEU A 1 49  ? 23.083  18.242  -0.685  1.00 23.97  ? 78  LEU A CA  1 
ATOM   375  C C   . LEU A 1 49  ? 24.063  18.424  -1.837  1.00 19.23  ? 78  LEU A C   1 
ATOM   376  O O   . LEU A 1 49  ? 23.717  18.911  -2.903  1.00 19.27  ? 78  LEU A O   1 
ATOM   377  C CB  . LEU A 1 49  ? 22.580  16.812  -0.549  1.00 29.19  ? 78  LEU A CB  1 
ATOM   378  C CG  . LEU A 1 49  ? 22.046  16.150  -1.817  1.00 29.54  ? 78  LEU A CG  1 
ATOM   379  C CD1 . LEU A 1 49  ? 22.132  14.649  -1.555  1.00 32.12  ? 78  LEU A CD1 1 
ATOM   380  C CD2 . LEU A 1 49  ? 20.631  16.472  -2.141  1.00 33.70  ? 78  LEU A CD2 1 
ATOM   381  N N   . VAL A 1 50  ? 25.314  18.135  -1.520  1.00 21.21  ? 79  VAL A N   1 
ATOM   382  C CA  . VAL A 1 50  ? 26.380  18.104  -2.499  1.00 20.82  ? 79  VAL A CA  1 
ATOM   383  C C   . VAL A 1 50  ? 26.551  16.668  -2.997  1.00 19.75  ? 79  VAL A C   1 
ATOM   384  O O   . VAL A 1 50  ? 26.666  15.718  -2.223  1.00 19.20  ? 79  VAL A O   1 
ATOM   385  C CB  . VAL A 1 50  ? 27.684  18.605  -1.866  1.00 20.12  ? 79  VAL A CB  1 
ATOM   386  C CG1 . VAL A 1 50  ? 28.825  18.461  -2.859  1.00 20.42  ? 79  VAL A CG1 1 
ATOM   387  C CG2 . VAL A 1 50  ? 27.525  20.041  -1.380  1.00 23.45  ? 79  VAL A CG2 1 
ATOM   388  N N   . TYR A 1 51  ? 26.543  16.532  -4.307  1.00 21.16  ? 80  TYR A N   1 
ATOM   389  C CA  . TYR A 1 51  ? 26.639  15.226  -4.940  1.00 22.67  ? 80  TYR A CA  1 
ATOM   390  C C   . TYR A 1 51  ? 27.428  15.441  -6.229  1.00 22.38  ? 80  TYR A C   1 
ATOM   391  O O   . TYR A 1 51  ? 27.047  16.277  -7.034  1.00 22.81  ? 80  TYR A O   1 
ATOM   392  C CB  . TYR A 1 51  ? 25.201  14.734  -5.108  1.00 22.79  ? 80  TYR A CB  1 
ATOM   393  C CG  . TYR A 1 51  ? 25.042  13.293  -5.537  1.00 21.65  ? 80  TYR A CG  1 
ATOM   394  C CD1 . TYR A 1 51  ? 25.077  12.970  -6.878  1.00 24.15  ? 80  TYR A CD1 1 
ATOM   395  C CD2 . TYR A 1 51  ? 24.788  12.289  -4.623  1.00 21.96  ? 80  TYR A CD2 1 
ATOM   396  C CE1 . TYR A 1 51  ? 24.902  11.670  -7.300  1.00 25.10  ? 80  TYR A CE1 1 
ATOM   397  C CE2 . TYR A 1 51  ? 24.653  10.967  -5.022  1.00 23.48  ? 80  TYR A CE2 1 
ATOM   398  C CZ  . TYR A 1 51  ? 24.710  10.663  -6.376  1.00 23.59  ? 80  TYR A CZ  1 
ATOM   399  O OH  . TYR A 1 51  ? 24.567  9.381   -6.847  1.00 25.20  ? 80  TYR A OH  1 
ATOM   400  N N   . GLU A 1 52  ? 28.569  14.759  -6.350  1.00 23.40  ? 81  GLU A N   1 
ATOM   401  C CA  . GLU A 1 52  ? 29.642  15.191  -7.235  1.00 24.77  ? 81  GLU A CA  1 
ATOM   402  C C   . GLU A 1 52  ? 29.608  14.499  -8.585  1.00 24.65  ? 81  GLU A C   1 
ATOM   403  O O   . GLU A 1 52  ? 30.149  15.030  -9.579  1.00 24.00  ? 81  GLU A O   1 
ATOM   404  C CB  . GLU A 1 52  ? 31.008  14.862  -6.635  1.00 27.52  ? 81  GLU A CB  1 
ATOM   405  C CG  . GLU A 1 52  ? 31.240  15.502  -5.268  1.00 32.06  ? 81  GLU A CG  1 
ATOM   406  C CD  . GLU A 1 52  ? 31.500  16.984  -5.360  1.00 33.88  ? 81  GLU A CD  1 
ATOM   407  O OE1 . GLU A 1 52  ? 31.104  17.569  -6.363  1.00 30.40  ? 81  GLU A OE1 1 
ATOM   408  O OE2 . GLU A 1 52  ? 32.172  17.508  -4.466  1.00 34.07  ? 81  GLU A OE2 1 
ATOM   409  N N   . THR A 1 53  ? 28.945  13.337  -8.636  1.00 23.60  ? 82  THR A N   1 
ATOM   410  C CA  . THR A 1 53  ? 29.112  12.462  -9.785  1.00 25.64  ? 82  THR A CA  1 
ATOM   411  C C   . THR A 1 53  ? 28.315  12.935  -10.999 1.00 23.20  ? 82  THR A C   1 
ATOM   412  O O   . THR A 1 53  ? 28.722  12.713  -12.135 1.00 23.44  ? 82  THR A O   1 
ATOM   413  C CB  . THR A 1 53  ? 28.844  11.016  -9.367  1.00 27.79  ? 82  THR A CB  1 
ATOM   414  O OG1 . THR A 1 53  ? 27.605  10.870  -8.669  1.00 26.14  ? 82  THR A OG1 1 
ATOM   415  C CG2 . THR A 1 53  ? 29.991  10.508  -8.509  1.00 27.25  ? 82  THR A CG2 1 
ATOM   416  N N   . SER A 1 54  ? 27.164  13.570  -10.794 1.00 22.44  ? 83  SER A N   1 
ATOM   417  C CA  . SER A 1 54  ? 26.342  13.958  -11.921 1.00 25.66  ? 83  SER A CA  1 
ATOM   418  C C   . SER A 1 54  ? 25.468  15.142  -11.536 1.00 23.26  ? 83  SER A C   1 
ATOM   419  O O   . SER A 1 54  ? 25.193  15.362  -10.355 1.00 22.31  ? 83  SER A O   1 
ATOM   420  C CB  . SER A 1 54  ? 25.498  12.769  -12.421 1.00 25.44  ? 83  SER A CB  1 
ATOM   421  O OG  . SER A 1 54  ? 24.473  12.461  -11.476 1.00 22.47  ? 83  SER A OG  1 
ATOM   422  N N   . VAL A 1 55  ? 25.125  15.922  -12.564 1.00 27.95  ? 84  VAL A N   1 
ATOM   423  C CA  . VAL A 1 55  ? 24.381  17.163  -12.447 1.00 28.19  ? 84  VAL A CA  1 
ATOM   424  C C   . VAL A 1 55  ? 23.375  17.211  -13.592 1.00 25.04  ? 84  VAL A C   1 
ATOM   425  O O   . VAL A 1 55  ? 23.685  16.946  -14.733 1.00 27.13  ? 84  VAL A O   1 
ATOM   426  C CB  . VAL A 1 55  ? 25.352  18.369  -12.438 1.00 31.34  ? 84  VAL A CB  1 
ATOM   427  C CG1 . VAL A 1 55  ? 24.638  19.714  -12.492 1.00 35.12  ? 84  VAL A CG1 1 
ATOM   428  C CG2 . VAL A 1 55  ? 26.288  18.336  -11.228 1.00 31.30  ? 84  VAL A CG2 1 
ATOM   429  N N   . LEU A 1 56  ? 22.133  17.485  -13.249 1.00 35.59  ? 85  LEU A N   1 
ATOM   430  C CA  . LEU A 1 56  ? 21.059  17.574  -14.219 1.00 42.27  ? 85  LEU A CA  1 
ATOM   431  C C   . LEU A 1 56  ? 20.822  19.043  -14.504 1.00 47.93  ? 85  LEU A C   1 
ATOM   432  O O   . LEU A 1 56  ? 20.406  19.768  -13.600 1.00 55.89  ? 85  LEU A O   1 
ATOM   433  C CB  . LEU A 1 56  ? 19.808  16.934  -13.614 1.00 45.08  ? 85  LEU A CB  1 
ATOM   434  C CG  . LEU A 1 56  ? 18.539  17.006  -14.463 1.00 53.66  ? 85  LEU A CG  1 
ATOM   435  C CD1 . LEU A 1 56  ? 18.733  16.205  -15.724 1.00 54.62  ? 85  LEU A CD1 1 
ATOM   436  C CD2 . LEU A 1 56  ? 17.372  16.476  -13.649 1.00 62.59  ? 85  LEU A CD2 1 
ATOM   437  N N   . ASP A 1 57  ? 21.131  19.466  -15.730 1.00 55.01  ? 86  ASP A N   1 
ATOM   438  C CA  . ASP A 1 57  ? 20.513  20.661  -16.277 1.00 74.02  ? 86  ASP A CA  1 
ATOM   439  C C   . ASP A 1 57  ? 19.037  20.318  -16.500 1.00 74.42  ? 86  ASP A C   1 
ATOM   440  O O   . ASP A 1 57  ? 18.743  19.293  -17.127 1.00 66.15  ? 86  ASP A O   1 
ATOM   441  C CB  . ASP A 1 57  ? 21.151  21.135  -17.577 1.00 73.32  ? 86  ASP A CB  1 
ATOM   442  C CG  . ASP A 1 57  ? 22.569  20.667  -17.860 1.00 80.58  ? 86  ASP A CG  1 
ATOM   443  O OD1 . ASP A 1 57  ? 22.988  19.674  -17.239 1.00 85.93  ? 86  ASP A OD1 1 
ATOM   444  O OD2 . ASP A 1 57  ? 23.242  21.306  -18.700 1.00 92.53  ? 86  ASP A OD2 1 
ATOM   445  N N   . PRO A 1 58  ? 18.068  21.122  -15.979 1.00 77.84  ? 87  PRO A N   1 
ATOM   446  C CA  . PRO A 1 58  ? 16.662  20.990  -16.393 1.00 73.69  ? 87  PRO A CA  1 
ATOM   447  C C   . PRO A 1 58  ? 16.485  21.011  -17.917 1.00 70.09  ? 87  PRO A C   1 
ATOM   448  O O   . PRO A 1 58  ? 15.478  20.545  -18.441 1.00 71.51  ? 87  PRO A O   1 
ATOM   449  C CB  . PRO A 1 58  ? 15.967  22.180  -15.675 1.00 74.33  ? 87  PRO A CB  1 
ATOM   450  C CG  . PRO A 1 58  ? 16.843  22.458  -14.454 1.00 73.20  ? 87  PRO A CG  1 
ATOM   451  C CD  . PRO A 1 58  ? 18.263  22.149  -14.934 1.00 70.87  ? 87  PRO A CD  1 
ATOM   452  N N   . ASP A 1 59  ? 17.538  21.454  -18.616 1.00 81.35  ? 88  ASP A N   1 
ATOM   453  C CA  . ASP A 1 59  ? 17.504  21.867  -20.011 1.00 80.59  ? 88  ASP A CA  1 
ATOM   454  C C   . ASP A 1 59  ? 18.083  20.785  -20.932 1.00 69.47  ? 88  ASP A C   1 
ATOM   455  O O   . ASP A 1 59  ? 17.365  20.283  -21.790 1.00 61.98  ? 88  ASP A O   1 
ATOM   456  C CB  . ASP A 1 59  ? 18.213  23.208  -20.140 1.00 89.58  ? 88  ASP A CB  1 
ATOM   457  C CG  . ASP A 1 59  ? 19.406  23.391  -19.205 1.00 96.49  ? 88  ASP A CG  1 
ATOM   458  O OD1 . ASP A 1 59  ? 19.243  23.169  -17.980 1.00 80.15  ? 88  ASP A OD1 1 
ATOM   459  O OD2 . ASP A 1 59  ? 20.500  23.728  -19.702 1.00 112.42 ? 88  ASP A OD2 1 
ATOM   460  N N   . GLU A 1 60  ? 19.379  20.452  -20.771 1.00 71.46  ? 89  GLU A N   1 
ATOM   461  C CA  . GLU A 1 60  ? 20.104  19.562  -21.684 1.00 71.20  ? 89  GLU A CA  1 
ATOM   462  C C   . GLU A 1 60  ? 20.234  18.135  -21.130 1.00 59.21  ? 89  GLU A C   1 
ATOM   463  O O   . GLU A 1 60  ? 20.717  17.229  -21.817 1.00 51.76  ? 89  GLU A O   1 
ATOM   464  C CB  . GLU A 1 60  ? 21.458  20.188  -22.017 1.00 78.11  ? 89  GLU A CB  1 
ATOM   465  C CG  . GLU A 1 60  ? 21.300  21.577  -22.637 1.00 92.83  ? 89  GLU A CG  1 
ATOM   466  C CD  . GLU A 1 60  ? 22.581  22.341  -22.936 1.00 100.78 ? 89  GLU A CD  1 
ATOM   467  O OE1 . GLU A 1 60  ? 22.806  23.393  -22.293 1.00 96.49  ? 89  GLU A OE1 1 
ATOM   468  O OE2 . GLU A 1 60  ? 23.344  21.899  -23.825 1.00 102.12 ? 89  GLU A OE2 1 
ATOM   469  N N   . GLY A 1 61  ? 19.752  17.924  -19.903 1.00 48.07  ? 90  GLY A N   1 
ATOM   470  C CA  . GLY A 1 61  ? 19.649  16.590  -19.343 1.00 47.16  ? 90  GLY A CA  1 
ATOM   471  C C   . GLY A 1 61  ? 20.890  16.268  -18.521 1.00 37.54  ? 90  GLY A C   1 
ATOM   472  O O   . GLY A 1 61  ? 21.650  17.168  -18.183 1.00 30.75  ? 90  GLY A O   1 
ATOM   473  N N   . ILE A 1 62  ? 21.041  14.992  -18.159 1.00 31.56  ? 91  ILE A N   1 
ATOM   474  C CA  . ILE A 1 62  ? 22.015  14.619  -17.137 1.00 26.83  ? 91  ILE A CA  1 
ATOM   475  C C   . ILE A 1 62  ? 23.418  14.791  -17.697 1.00 28.24  ? 91  ILE A C   1 
ATOM   476  O O   . ILE A 1 62  ? 23.643  14.549  -18.892 1.00 29.35  ? 91  ILE A O   1 
ATOM   477  C CB  . ILE A 1 62  ? 21.759  13.197  -16.630 1.00 28.05  ? 91  ILE A CB  1 
ATOM   478  C CG1 . ILE A 1 62  ? 22.555  12.916  -15.332 1.00 29.95  ? 91  ILE A CG1 1 
ATOM   479  C CG2 . ILE A 1 62  ? 22.002  12.132  -17.708 1.00 30.82  ? 91  ILE A CG2 1 
ATOM   480  C CD1 . ILE A 1 62  ? 22.098  13.735  -14.143 1.00 29.08  ? 91  ILE A CD1 1 
ATOM   481  N N   . ARG A 1 63  ? 24.336  15.264  -16.851 1.00 25.66  ? 92  ARG A N   1 
ATOM   482  C CA  . ARG A 1 63  ? 25.745  15.237  -17.226 1.00 28.31  ? 92  ARG A CA  1 
ATOM   483  C C   . ARG A 1 63  ? 26.532  14.410  -16.212 1.00 26.58  ? 92  ARG A C   1 
ATOM   484  O O   . ARG A 1 63  ? 26.432  14.662  -15.011 1.00 26.57  ? 92  ARG A O   1 
ATOM   485  C CB  . ARG A 1 63  ? 26.345  16.644  -17.304 1.00 28.50  ? 92  ARG A CB  1 
ATOM   486  C CG  . ARG A 1 63  ? 25.802  17.429  -18.493 1.00 39.99  ? 92  ARG A CG  1 
ATOM   487  C CD  . ARG A 1 63  ? 26.628  18.665  -18.818 1.00 42.12  ? 92  ARG A CD  1 
ATOM   488  N NE  . ARG A 1 63  ? 26.069  19.305  -20.017 1.00 61.58  ? 92  ARG A NE  1 
ATOM   489  C CZ  . ARG A 1 63  ? 26.671  19.481  -21.198 1.00 69.03  ? 92  ARG A CZ  1 
ATOM   490  N NH1 . ARG A 1 63  ? 27.896  19.019  -21.445 1.00 63.58  ? 92  ARG A NH1 1 
ATOM   491  N NH2 . ARG A 1 63  ? 26.021  20.127  -22.152 1.00 72.66  ? 92  ARG A NH2 1 
ATOM   492  N N   . PHE A 1 64  ? 27.361  13.497  -16.736 1.00 25.48  ? 93  PHE A N   1 
ATOM   493  C CA  . PHE A 1 64  ? 28.234  12.656  -15.930 1.00 22.81  ? 93  PHE A CA  1 
ATOM   494  C C   . PHE A 1 64  ? 29.613  13.295  -15.855 1.00 25.09  ? 93  PHE A C   1 
ATOM   495  O O   . PHE A 1 64  ? 30.300  13.351  -16.881 1.00 28.67  ? 93  PHE A O   1 
ATOM   496  C CB  . PHE A 1 64  ? 28.295  11.274  -16.567 1.00 23.83  ? 93  PHE A CB  1 
ATOM   497  C CG  . PHE A 1 64  ? 26.965  10.553  -16.706 1.00 24.41  ? 93  PHE A CG  1 
ATOM   498  C CD1 . PHE A 1 64  ? 26.080  10.463  -15.641 1.00 25.44  ? 93  PHE A CD1 1 
ATOM   499  C CD2 . PHE A 1 64  ? 26.641  9.890   -17.881 1.00 25.93  ? 93  PHE A CD2 1 
ATOM   500  C CE1 . PHE A 1 64  ? 24.889  9.765   -15.760 1.00 26.09  ? 93  PHE A CE1 1 
ATOM   501  C CE2 . PHE A 1 64  ? 25.462  9.161   -17.980 1.00 28.52  ? 93  PHE A CE2 1 
ATOM   502  C CZ  . PHE A 1 64  ? 24.567  9.139   -16.932 1.00 26.15  ? 93  PHE A CZ  1 
ATOM   503  N N   . ARG A 1 65  ? 29.945  13.884  -14.684 1.00 22.50  ? 94  ARG A N   1 
ATOM   504  C CA  . ARG A 1 65  ? 31.202  14.598  -14.502 1.00 22.45  ? 94  ARG A CA  1 
ATOM   505  C C   . ARG A 1 65  ? 31.435  15.562  -15.663 1.00 28.01  ? 94  ARG A C   1 
ATOM   506  O O   . ARG A 1 65  ? 32.534  15.663  -16.195 1.00 27.94  ? 94  ARG A O   1 
ATOM   507  C CB  . ARG A 1 65  ? 32.391  13.665  -14.320 1.00 21.64  ? 94  ARG A CB  1 
ATOM   508  C CG  . ARG A 1 65  ? 32.309  12.908  -12.992 1.00 20.69  ? 94  ARG A CG  1 
ATOM   509  C CD  . ARG A 1 65  ? 32.614  13.746  -11.799 1.00 21.86  ? 94  ARG A CD  1 
ATOM   510  N NE  . ARG A 1 65  ? 32.978  12.858  -10.694 1.00 23.36  ? 94  ARG A NE  1 
ATOM   511  C CZ  . ARG A 1 65  ? 33.407  13.198  -9.488  1.00 25.10  ? 94  ARG A CZ  1 
ATOM   512  N NH1 . ARG A 1 65  ? 33.647  14.455  -9.169  1.00 26.39  ? 94  ARG A NH1 1 
ATOM   513  N NH2 . ARG A 1 65  ? 33.680  12.261  -8.620  1.00 24.85  ? 94  ARG A NH2 1 
ATOM   514  N N   . GLY A 1 66  ? 30.367  16.273  -16.037 1.00 29.02  ? 95  GLY A N   1 
ATOM   515  C CA  . GLY A 1 66  ? 30.465  17.331  -17.035 1.00 30.19  ? 95  GLY A CA  1 
ATOM   516  C C   . GLY A 1 66  ? 30.221  16.834  -18.461 1.00 27.42  ? 95  GLY A C   1 
ATOM   517  O O   . GLY A 1 66  ? 30.159  17.648  -19.372 1.00 28.25  ? 95  GLY A O   1 
ATOM   518  N N   . PHE A 1 67  ? 30.003  15.533  -18.670 1.00 26.60  ? 96  PHE A N   1 
ATOM   519  C CA  . PHE A 1 67  ? 29.815  14.999  -20.016 1.00 28.19  ? 96  PHE A CA  1 
ATOM   520  C C   . PHE A 1 67  ? 28.361  14.598  -20.243 1.00 32.03  ? 96  PHE A C   1 
ATOM   521  O O   . PHE A 1 67  ? 27.803  13.850  -19.448 1.00 29.13  ? 96  PHE A O   1 
ATOM   522  C CB  . PHE A 1 67  ? 30.753  13.804  -20.194 1.00 27.29  ? 96  PHE A CB  1 
ATOM   523  C CG  . PHE A 1 67  ? 32.256  14.083  -20.240 1.00 26.25  ? 96  PHE A CG  1 
ATOM   524  C CD1 . PHE A 1 67  ? 32.894  14.385  -21.442 1.00 25.74  ? 96  PHE A CD1 1 
ATOM   525  C CD2 . PHE A 1 67  ? 33.037  14.034  -19.089 1.00 24.05  ? 96  PHE A CD2 1 
ATOM   526  C CE1 . PHE A 1 67  ? 34.274  14.592  -21.488 1.00 27.12  ? 96  PHE A CE1 1 
ATOM   527  C CE2 . PHE A 1 67  ? 34.402  14.272  -19.129 1.00 25.40  ? 96  PHE A CE2 1 
ATOM   528  C CZ  . PHE A 1 67  ? 35.025  14.571  -20.331 1.00 28.66  ? 96  PHE A CZ  1 
ATOM   529  N N   . SER A 1 68  ? 27.749  15.041  -21.353 1.00 25.84  ? 97  SER A N   1 
ATOM   530  C CA  . SER A 1 68  ? 26.404  14.575  -21.675 1.00 26.25  ? 97  SER A CA  1 
ATOM   531  C C   . SER A 1 68  ? 26.457  13.104  -22.103 1.00 24.02  ? 97  SER A C   1 
ATOM   532  O O   . SER A 1 68  ? 27.516  12.552  -22.360 1.00 23.55  ? 97  SER A O   1 
ATOM   533  C CB  . SER A 1 68  ? 25.755  15.437  -22.758 1.00 29.52  ? 97  SER A CB  1 
ATOM   534  O OG  . SER A 1 68  ? 26.441  15.174  -23.978 1.00 28.66  ? 97  SER A OG  1 
ATOM   535  N N   . ILE A 1 69  ? 25.285  12.497  -22.249 1.00 23.14  ? 98  ILE A N   1 
ATOM   536  C CA  . ILE A 1 69  ? 25.136  11.147  -22.723 1.00 27.14  ? 98  ILE A CA  1 
ATOM   537  C C   . ILE A 1 69  ? 25.657  11.018  -24.149 1.00 30.41  ? 98  ILE A C   1 
ATOM   538  O O   . ILE A 1 69  ? 26.361  10.052  -24.450 1.00 28.19  ? 98  ILE A O   1 
ATOM   539  C CB  . ILE A 1 69  ? 23.677  10.687  -22.642 1.00 28.75  ? 98  ILE A CB  1 
ATOM   540  C CG1 . ILE A 1 69  ? 23.212  10.573  -21.231 1.00 33.68  ? 98  ILE A CG1 1 
ATOM   541  C CG2 . ILE A 1 69  ? 23.466  9.370   -23.372 1.00 29.19  ? 98  ILE A CG2 1 
ATOM   542  C CD1 . ILE A 1 69  ? 24.152  9.792   -20.391 1.00 40.66  ? 98  ILE A CD1 1 
ATOM   543  N N   . PRO A 1 70  ? 25.248  11.895  -25.087 1.00 31.72  ? 99  PRO A N   1 
ATOM   544  C CA  . PRO A 1 70  ? 25.856  11.895  -26.420 1.00 34.35  ? 99  PRO A CA  1 
ATOM   545  C C   . PRO A 1 70  ? 27.388  11.938  -26.396 1.00 27.86  ? 99  PRO A C   1 
ATOM   546  O O   . PRO A 1 70  ? 28.041  11.166  -27.075 1.00 29.03  ? 99  PRO A O   1 
ATOM   547  C CB  . PRO A 1 70  ? 25.241  13.178  -27.052 1.00 36.99  ? 99  PRO A CB  1 
ATOM   548  C CG  . PRO A 1 70  ? 23.878  13.305  -26.390 1.00 33.89  ? 99  PRO A CG  1 
ATOM   549  C CD  . PRO A 1 70  ? 24.122  12.850  -24.950 1.00 34.55  ? 99  PRO A CD  1 
ATOM   550  N N   . GLU A 1 71  ? 27.964  12.831  -25.579 1.00 31.85  ? 100 GLU A N   1 
ATOM   551  C CA  . GLU A 1 71  ? 29.408  12.905  -25.440 1.00 31.10  ? 100 GLU A CA  1 
ATOM   552  C C   . GLU A 1 71  ? 29.960  11.574  -24.924 1.00 30.60  ? 100 GLU A C   1 
ATOM   553  O O   . GLU A 1 71  ? 30.988  11.122  -25.444 1.00 33.84  ? 100 GLU A O   1 
ATOM   554  C CB  . GLU A 1 71  ? 29.844  14.086  -24.588 1.00 35.85  ? 100 GLU A CB  1 
ATOM   555  C CG  . GLU A 1 71  ? 29.581  15.448  -25.222 1.00 35.36  ? 100 GLU A CG  1 
ATOM   556  C CD  . GLU A 1 71  ? 29.990  16.550  -24.256 1.00 38.21  ? 100 GLU A CD  1 
ATOM   557  O OE1 . GLU A 1 71  ? 30.928  17.322  -24.574 1.00 37.87  ? 100 GLU A OE1 1 
ATOM   558  O OE2 . GLU A 1 71  ? 29.411  16.620  -23.142 1.00 38.03  ? 100 GLU A OE2 1 
ATOM   559  N N   . CYS A 1 72  ? 29.281  10.900  -23.952 1.00 31.60  ? 101 CYS A N   1 
ATOM   560  C CA  . CYS A 1 72  ? 29.782  9.635   -23.402 1.00 26.45  ? 101 CYS A CA  1 
ATOM   561  C C   . CYS A 1 72  ? 29.676  8.468   -24.396 1.00 28.16  ? 101 CYS A C   1 
ATOM   562  O O   . CYS A 1 72  ? 30.530  7.577   -24.421 1.00 24.41  ? 101 CYS A O   1 
ATOM   563  C CB  . CYS A 1 72  ? 29.084  9.219   -22.100 1.00 28.70  ? 101 CYS A CB  1 
ATOM   564  S SG  . CYS A 1 72  ? 29.382  10.367  -20.729 1.00 30.78  ? 101 CYS A SG  1 
ATOM   565  N N   . GLN A 1 73  ? 28.585  8.423   -25.161 1.00 27.38  ? 102 GLN A N   1 
ATOM   566  C CA  . GLN A 1 73  ? 28.406  7.445   -26.221 1.00 31.06  ? 102 GLN A CA  1 
ATOM   567  C C   . GLN A 1 73  ? 29.583  7.462   -27.205 1.00 28.79  ? 102 GLN A C   1 
ATOM   568  O O   . GLN A 1 73  ? 30.009  6.408   -27.650 1.00 34.95  ? 102 GLN A O   1 
ATOM   569  C CB  . GLN A 1 73  ? 27.121  7.676   -27.022 1.00 35.50  ? 102 GLN A CB  1 
ATOM   570  C CG  . GLN A 1 73  ? 25.854  7.256   -26.287 1.00 38.94  ? 102 GLN A CG  1 
ATOM   571  C CD  . GLN A 1 73  ? 24.582  7.660   -27.007 1.00 38.61  ? 102 GLN A CD  1 
ATOM   572  O OE1 . GLN A 1 73  ? 24.046  8.747   -26.810 1.00 44.38  ? 102 GLN A OE1 1 
ATOM   573  N NE2 . GLN A 1 73  ? 24.044  6.758   -27.810 1.00 41.06  ? 102 GLN A NE2 1 
ATOM   574  N N   . LYS A 1 74  ? 30.098  8.628   -27.548 1.00 31.81  ? 103 LYS A N   1 
ATOM   575  C CA  . LYS A 1 74  ? 31.275  8.732   -28.401 1.00 36.38  ? 103 LYS A CA  1 
ATOM   576  C C   . LYS A 1 74  ? 32.586  8.418   -27.672 1.00 35.78  ? 103 LYS A C   1 
ATOM   577  O O   . LYS A 1 74  ? 33.434  7.731   -28.226 1.00 38.36  ? 103 LYS A O   1 
ATOM   578  C CB  . LYS A 1 74  ? 31.335  10.139  -29.000 1.00 38.46  ? 103 LYS A CB  1 
ATOM   579  C CG  . LYS A 1 74  ? 30.274  10.298  -30.061 1.00 44.29  ? 103 LYS A CG  1 
ATOM   580  C CD  . LYS A 1 74  ? 30.383  11.551  -30.917 1.00 44.34  ? 103 LYS A CD  1 
ATOM   581  C CE  . LYS A 1 74  ? 29.517  11.481  -32.133 1.00 44.65  ? 103 LYS A CE  1 
ATOM   582  N NZ  . LYS A 1 74  ? 28.137  11.135  -31.796 1.00 47.86  ? 103 LYS A NZ  1 
ATOM   583  N N   . LEU A 1 75  ? 32.778  8.906   -26.439 1.00 31.71  ? 104 LEU A N   1 
ATOM   584  C CA  . LEU A 1 75  ? 34.106  8.880   -25.822 1.00 30.95  ? 104 LEU A CA  1 
ATOM   585  C C   . LEU A 1 75  ? 34.416  7.595   -25.055 1.00 30.78  ? 104 LEU A C   1 
ATOM   586  O O   . LEU A 1 75  ? 35.590  7.233   -24.928 1.00 27.18  ? 104 LEU A O   1 
ATOM   587  C CB  . LEU A 1 75  ? 34.231  10.060  -24.877 1.00 36.72  ? 104 LEU A CB  1 
ATOM   588  C CG  . LEU A 1 75  ? 34.331  11.427  -25.551 1.00 37.85  ? 104 LEU A CG  1 
ATOM   589  C CD1 . LEU A 1 75  ? 34.174  12.466  -24.501 1.00 31.64  ? 104 LEU A CD1 1 
ATOM   590  C CD2 . LEU A 1 75  ? 35.680  11.565  -26.267 1.00 40.37  ? 104 LEU A CD2 1 
ATOM   591  N N   . LEU A 1 76  ? 33.396  6.978   -24.445 1.00 30.33  ? 105 LEU A N   1 
ATOM   592  C CA  . LEU A 1 76  ? 33.590  5.805   -23.608 1.00 29.73  ? 105 LEU A CA  1 
ATOM   593  C C   . LEU A 1 76  ? 33.952  4.567   -24.434 1.00 32.96  ? 105 LEU A C   1 
ATOM   594  O O   . LEU A 1 76  ? 33.334  4.301   -25.483 1.00 28.54  ? 105 LEU A O   1 
ATOM   595  C CB  . LEU A 1 76  ? 32.310  5.544   -22.814 1.00 27.19  ? 105 LEU A CB  1 
ATOM   596  C CG  . LEU A 1 76  ? 32.031  6.503   -21.658 1.00 27.01  ? 105 LEU A CG  1 
ATOM   597  C CD1 . LEU A 1 76  ? 30.815  5.955   -20.889 1.00 26.61  ? 105 LEU A CD1 1 
ATOM   598  C CD2 . LEU A 1 76  ? 33.235  6.653   -20.741 1.00 27.29  ? 105 LEU A CD2 1 
ATOM   599  N N   . PRO A 1 77  ? 34.925  3.741   -23.952 1.00 30.68  ? 106 PRO A N   1 
ATOM   600  C CA  . PRO A 1 77  ? 35.193  2.446   -24.572 1.00 29.03  ? 106 PRO A CA  1 
ATOM   601  C C   . PRO A 1 77  ? 33.976  1.577   -24.822 1.00 33.53  ? 106 PRO A C   1 
ATOM   602  O O   . PRO A 1 77  ? 33.054  1.502   -24.006 1.00 29.81  ? 106 PRO A O   1 
ATOM   603  C CB  . PRO A 1 77  ? 36.148  1.808   -23.589 1.00 31.94  ? 106 PRO A CB  1 
ATOM   604  C CG  . PRO A 1 77  ? 36.973  3.009   -23.130 1.00 30.48  ? 106 PRO A CG  1 
ATOM   605  C CD  . PRO A 1 77  ? 35.924  4.090   -22.926 1.00 27.03  ? 106 PRO A CD  1 
ATOM   606  N N   . LYS A 1 78  ? 34.058  0.861   -25.950 1.00 29.39  ? 107 LYS A N   1 
ATOM   607  C CA  . LYS A 1 78  ? 33.065  -0.097  -26.386 1.00 31.76  ? 107 LYS A CA  1 
ATOM   608  C C   . LYS A 1 78  ? 33.620  -1.509  -26.223 1.00 26.66  ? 107 LYS A C   1 
ATOM   609  O O   . LYS A 1 78  ? 34.816  -1.702  -26.096 1.00 29.13  ? 107 LYS A O   1 
ATOM   610  C CB  . LYS A 1 78  ? 32.783  0.282   -27.854 1.00 36.01  ? 107 LYS A CB  1 
ATOM   611  C CG  . LYS A 1 78  ? 32.187  1.669   -27.968 1.00 41.23  ? 107 LYS A CG  1 
ATOM   612  C CD  . LYS A 1 78  ? 32.124  2.308   -29.343 1.00 52.41  ? 107 LYS A CD  1 
ATOM   613  C CE  . LYS A 1 78  ? 31.243  3.532   -29.253 1.00 61.34  ? 107 LYS A CE  1 
ATOM   614  N NZ  . LYS A 1 78  ? 31.513  4.366   -28.066 1.00 58.39  ? 107 LYS A NZ  1 
ATOM   615  N N   . ALA A 1 79  ? 32.767  -2.521  -26.295 1.00 28.11  ? 108 ALA A N   1 
ATOM   616  C CA  . ALA A 1 79  ? 33.276  -3.861  -26.515 1.00 30.26  ? 108 ALA A CA  1 
ATOM   617  C C   . ALA A 1 79  ? 33.855  -3.967  -27.930 1.00 39.20  ? 108 ALA A C   1 
ATOM   618  O O   . ALA A 1 79  ? 33.302  -3.388  -28.867 1.00 32.49  ? 108 ALA A O   1 
ATOM   619  C CB  . ALA A 1 79  ? 32.185  -4.858  -26.332 1.00 30.16  ? 108 ALA A CB  1 
ATOM   620  N N   . LYS A 1 80  ? 34.937  -4.742  -28.068 1.00 41.95  ? 109 LYS A N   1 
ATOM   621  C CA  . LYS A 1 80  ? 35.395  -5.192  -29.371 1.00 50.39  ? 109 LYS A CA  1 
ATOM   622  C C   . LYS A 1 80  ? 34.182  -5.691  -30.158 1.00 45.63  ? 109 LYS A C   1 
ATOM   623  O O   . LYS A 1 80  ? 33.424  -6.505  -29.647 1.00 41.10  ? 109 LYS A O   1 
ATOM   624  C CB  . LYS A 1 80  ? 36.500  -6.229  -29.128 1.00 55.85  ? 109 LYS A CB  1 
ATOM   625  C CG  . LYS A 1 80  ? 36.968  -7.039  -30.336 1.00 62.03  ? 109 LYS A CG  1 
ATOM   626  C CD  . LYS A 1 80  ? 38.208  -7.883  -30.041 1.00 71.62  ? 109 LYS A CD  1 
ATOM   627  C CE  . LYS A 1 80  ? 38.381  -9.056  -30.967 1.00 72.09  ? 109 LYS A CE  1 
ATOM   628  N NZ  . LYS A 1 80  ? 38.218  -8.652  -32.368 1.00 67.86  ? 109 LYS A NZ  1 
ATOM   629  N N   . GLY A 1 81  ? 33.963  -5.121  -31.357 1.00 50.13  ? 110 GLY A N   1 
ATOM   630  C CA  . GLY A 1 81  ? 32.864  -5.498  -32.237 1.00 51.65  ? 110 GLY A CA  1 
ATOM   631  C C   . GLY A 1 81  ? 31.507  -4.923  -31.808 1.00 55.44  ? 110 GLY A C   1 
ATOM   632  O O   . GLY A 1 81  ? 30.466  -5.362  -32.304 1.00 47.88  ? 110 GLY A O   1 
ATOM   633  N N   . GLY A 1 82  ? 31.514  -3.926  -30.902 1.00 53.16  ? 111 GLY A N   1 
ATOM   634  C CA  . GLY A 1 82  ? 30.285  -3.330  -30.388 1.00 43.17  ? 111 GLY A CA  1 
ATOM   635  C C   . GLY A 1 82  ? 30.273  -1.821  -30.591 1.00 39.36  ? 111 GLY A C   1 
ATOM   636  O O   . GLY A 1 82  ? 31.286  -1.253  -30.950 1.00 40.11  ? 111 GLY A O   1 
ATOM   637  N N   . GLU A 1 83  ? 29.122  -1.185  -30.342 1.00 39.38  ? 112 GLU A N   1 
ATOM   638  C CA  . GLU A 1 83  ? 28.958  0.243   -30.557 1.00 43.43  ? 112 GLU A CA  1 
ATOM   639  C C   . GLU A 1 83  ? 28.490  0.965   -29.289 1.00 37.11  ? 112 GLU A C   1 
ATOM   640  O O   . GLU A 1 83  ? 28.538  2.179   -29.242 1.00 35.26  ? 112 GLU A O   1 
ATOM   641  C CB  . GLU A 1 83  ? 27.901  0.591   -31.610 1.00 45.58  ? 112 GLU A CB  1 
ATOM   642  C CG  . GLU A 1 83  ? 28.101  -0.045  -32.983 1.00 59.23  ? 112 GLU A CG  1 
ATOM   643  C CD  . GLU A 1 83  ? 26.984  0.314   -33.977 1.00 66.83  ? 112 GLU A CD  1 
ATOM   644  O OE1 . GLU A 1 83  ? 26.842  1.519   -34.297 1.00 64.23  ? 112 GLU A OE1 1 
ATOM   645  O OE2 . GLU A 1 83  ? 26.237  -0.589  -34.431 1.00 71.33  ? 112 GLU A OE2 1 
ATOM   646  N N   . GLU A 1 84  ? 28.013  0.255   -28.270 1.00 36.65  ? 113 GLU A N   1 
ATOM   647  C CA  . GLU A 1 84  ? 27.449  0.925   -27.102 1.00 33.31  ? 113 GLU A CA  1 
ATOM   648  C C   . GLU A 1 84  ? 28.499  1.078   -25.994 1.00 28.78  ? 113 GLU A C   1 
ATOM   649  O O   . GLU A 1 84  ? 29.347  0.222   -25.785 1.00 29.33  ? 113 GLU A O   1 
ATOM   650  C CB  . GLU A 1 84  ? 26.245  0.141   -26.581 1.00 30.96  ? 113 GLU A CB  1 
ATOM   651  C CG  . GLU A 1 84  ? 25.121  -0.001  -27.600 1.00 34.46  ? 113 GLU A CG  1 
ATOM   652  C CD  . GLU A 1 84  ? 24.561  1.323   -28.097 1.00 36.89  ? 113 GLU A CD  1 
ATOM   653  O OE1 . GLU A 1 84  ? 24.738  2.328   -27.383 1.00 31.56  ? 113 GLU A OE1 1 
ATOM   654  O OE2 . GLU A 1 84  ? 24.011  1.351   -29.241 1.00 39.62  ? 113 GLU A OE2 1 
ATOM   655  N N   . PRO A 1 85  ? 28.461  2.172   -25.207 1.00 30.63  ? 114 PRO A N   1 
ATOM   656  C CA  . PRO A 1 85  ? 29.441  2.395   -24.139 1.00 28.47  ? 114 PRO A CA  1 
ATOM   657  C C   . PRO A 1 85  ? 29.369  1.320   -23.060 1.00 27.61  ? 114 PRO A C   1 
ATOM   658  O O   . PRO A 1 85  ? 28.305  0.822   -22.744 1.00 26.19  ? 114 PRO A O   1 
ATOM   659  C CB  . PRO A 1 85  ? 29.053  3.794   -23.628 1.00 28.05  ? 114 PRO A CB  1 
ATOM   660  C CG  . PRO A 1 85  ? 27.558  3.855   -23.854 1.00 27.53  ? 114 PRO A CG  1 
ATOM   661  C CD  . PRO A 1 85  ? 27.440  3.233   -25.253 1.00 31.56  ? 114 PRO A CD  1 
ATOM   662  N N   . LEU A 1 86  ? 30.538  0.926   -22.544 1.00 27.81  ? 115 LEU A N   1 
ATOM   663  C CA  . LEU A 1 86  ? 30.607  -0.082  -21.509 1.00 27.84  ? 115 LEU A CA  1 
ATOM   664  C C   . LEU A 1 86  ? 30.378  0.618   -20.173 1.00 26.00  ? 115 LEU A C   1 
ATOM   665  O O   . LEU A 1 86  ? 31.012  1.617   -19.891 1.00 25.44  ? 115 LEU A O   1 
ATOM   666  C CB  . LEU A 1 86  ? 31.920  -0.859  -21.497 1.00 29.42  ? 115 LEU A CB  1 
ATOM   667  C CG  . LEU A 1 86  ? 32.181  -1.769  -22.704 1.00 31.39  ? 115 LEU A CG  1 
ATOM   668  C CD1 . LEU A 1 86  ? 33.436  -2.580  -22.464 1.00 33.01  ? 115 LEU A CD1 1 
ATOM   669  C CD2 . LEU A 1 86  ? 31.036  -2.679  -23.040 1.00 31.09  ? 115 LEU A CD2 1 
ATOM   670  N N   . PRO A 1 87  ? 29.484  0.077   -19.326 1.00 23.54  ? 116 PRO A N   1 
ATOM   671  C CA  . PRO A 1 87  ? 29.290  0.592   -17.977 1.00 24.54  ? 116 PRO A CA  1 
ATOM   672  C C   . PRO A 1 87  ? 30.530  0.778   -17.113 1.00 22.70  ? 116 PRO A C   1 
ATOM   673  O O   . PRO A 1 87  ? 30.556  1.671   -16.273 1.00 23.12  ? 116 PRO A O   1 
ATOM   674  C CB  . PRO A 1 87  ? 28.339  -0.430  -17.346 1.00 26.95  ? 116 PRO A CB  1 
ATOM   675  C CG  . PRO A 1 87  ? 27.629  -1.061  -18.477 1.00 27.23  ? 116 PRO A CG  1 
ATOM   676  C CD  . PRO A 1 87  ? 28.570  -1.015  -19.652 1.00 25.02  ? 116 PRO A CD  1 
ATOM   677  N N   . GLU A 1 88  ? 31.532  -0.054  -17.340 1.00 21.65  ? 117 GLU A N   1 
ATOM   678  C CA  . GLU A 1 88  ? 32.799  0.019   -16.665 1.00 21.78  ? 117 GLU A CA  1 
ATOM   679  C C   . GLU A 1 88  ? 33.362  1.400   -16.869 1.00 22.87  ? 117 GLU A C   1 
ATOM   680  O O   . GLU A 1 88  ? 33.872  1.983   -15.918 1.00 21.01  ? 117 GLU A O   1 
ATOM   681  C CB  . GLU A 1 88  ? 33.803  -1.019  -17.167 1.00 27.00  ? 117 GLU A CB  1 
ATOM   682  C CG  . GLU A 1 88  ? 33.491  -2.461  -16.784 1.00 27.84  ? 117 GLU A CG  1 
ATOM   683  C CD  . GLU A 1 88  ? 32.635  -3.253  -17.750 1.00 26.67  ? 117 GLU A CD  1 
ATOM   684  O OE1 . GLU A 1 88  ? 31.629  -2.686  -18.250 1.00 26.24  ? 117 GLU A OE1 1 
ATOM   685  O OE2 . GLU A 1 88  ? 32.929  -4.478  -17.925 1.00 24.78  ? 117 GLU A OE2 1 
ATOM   686  N N   . GLY A 1 89  ? 33.340  1.884   -18.133 1.00 21.51  ? 118 GLY A N   1 
ATOM   687  C CA  . GLY A 1 89  ? 33.935  3.176   -18.408 1.00 21.90  ? 118 GLY A CA  1 
ATOM   688  C C   . GLY A 1 89  ? 33.167  4.315   -17.738 1.00 20.67  ? 118 GLY A C   1 
ATOM   689  O O   . GLY A 1 89  ? 33.747  5.343   -17.388 1.00 20.77  ? 118 GLY A O   1 
ATOM   690  N N   . LEU A 1 90  ? 31.844  4.160   -17.649 1.00 23.17  ? 119 LEU A N   1 
ATOM   691  C CA  . LEU A 1 90  ? 30.994  5.140   -17.006 1.00 22.21  ? 119 LEU A CA  1 
ATOM   692  C C   . LEU A 1 90  ? 31.417  5.218   -15.550 1.00 19.92  ? 119 LEU A C   1 
ATOM   693  O O   . LEU A 1 90  ? 31.596  6.312   -15.034 1.00 20.98  ? 119 LEU A O   1 
ATOM   694  C CB  . LEU A 1 90  ? 29.517  4.764   -17.209 1.00 21.77  ? 119 LEU A CB  1 
ATOM   695  C CG  . LEU A 1 90  ? 28.453  5.622   -16.519 1.00 23.45  ? 119 LEU A CG  1 
ATOM   696  C CD1 . LEU A 1 90  ? 28.432  5.238   -15.021 1.00 24.14  ? 119 LEU A CD1 1 
ATOM   697  C CD2 . LEU A 1 90  ? 28.698  7.080   -16.685 1.00 22.63  ? 119 LEU A CD2 1 
ATOM   698  N N   . PHE A 1 91  ? 31.595  4.063   -14.901 1.00 19.63  ? 120 PHE A N   1 
ATOM   699  C CA  . PHE A 1 91  ? 31.971  4.076   -13.481 1.00 19.74  ? 120 PHE A CA  1 
ATOM   700  C C   . PHE A 1 91  ? 33.327  4.734   -13.300 1.00 20.06  ? 120 PHE A C   1 
ATOM   701  O O   . PHE A 1 91  ? 33.518  5.587   -12.434 1.00 20.00  ? 120 PHE A O   1 
ATOM   702  C CB  . PHE A 1 91  ? 31.974  2.645   -12.950 1.00 20.39  ? 120 PHE A CB  1 
ATOM   703  C CG  . PHE A 1 91  ? 32.341  2.536   -11.481 1.00 18.97  ? 120 PHE A CG  1 
ATOM   704  C CD1 . PHE A 1 91  ? 31.416  2.897   -10.530 1.00 19.89  ? 120 PHE A CD1 1 
ATOM   705  C CD2 . PHE A 1 91  ? 33.602  2.108   -11.063 1.00 19.32  ? 120 PHE A CD2 1 
ATOM   706  C CE1 . PHE A 1 91  ? 31.721  2.750   -9.177  1.00 19.63  ? 120 PHE A CE1 1 
ATOM   707  C CE2 . PHE A 1 91  ? 33.891  1.940   -9.716  1.00 19.14  ? 120 PHE A CE2 1 
ATOM   708  C CZ  . PHE A 1 91  ? 32.974  2.352   -8.783  1.00 18.97  ? 120 PHE A CZ  1 
ATOM   709  N N   . TRP A 1 92  ? 34.265  4.392   -14.181 1.00 20.01  ? 121 TRP A N   1 
ATOM   710  C CA  . TRP A 1 92  ? 35.589  4.998   -14.109 1.00 19.76  ? 121 TRP A CA  1 
ATOM   711  C C   . TRP A 1 92  ? 35.436  6.516   -14.194 1.00 19.62  ? 121 TRP A C   1 
ATOM   712  O O   . TRP A 1 92  ? 36.041  7.271   -13.434 1.00 20.88  ? 121 TRP A O   1 
ATOM   713  C CB  . TRP A 1 92  ? 36.451  4.452   -15.241 1.00 22.37  ? 121 TRP A CB  1 
ATOM   714  C CG  . TRP A 1 92  ? 37.889  4.883   -15.130 1.00 23.44  ? 121 TRP A CG  1 
ATOM   715  C CD1 . TRP A 1 92  ? 38.413  6.105   -15.405 1.00 24.64  ? 121 TRP A CD1 1 
ATOM   716  C CD2 . TRP A 1 92  ? 38.976  4.057   -14.703 1.00 21.75  ? 121 TRP A CD2 1 
ATOM   717  N NE1 . TRP A 1 92  ? 39.766  6.096   -15.176 1.00 24.70  ? 121 TRP A NE1 1 
ATOM   718  C CE2 . TRP A 1 92  ? 40.138  4.845   -14.759 1.00 25.33  ? 121 TRP A CE2 1 
ATOM   719  C CE3 . TRP A 1 92  ? 39.077  2.715   -14.328 1.00 23.38  ? 121 TRP A CE3 1 
ATOM   720  C CZ2 . TRP A 1 92  ? 41.400  4.350   -14.422 1.00 23.03  ? 121 TRP A CZ2 1 
ATOM   721  C CZ3 . TRP A 1 92  ? 40.329  2.219   -14.035 1.00 25.05  ? 121 TRP A CZ3 1 
ATOM   722  C CH2 . TRP A 1 92  ? 41.466  3.031   -14.064 1.00 23.87  ? 121 TRP A CH2 1 
ATOM   723  N N   . LEU A 1 93  ? 34.637  6.978   -15.170 1.00 23.12  ? 122 LEU A N   1 
ATOM   724  C CA  . LEU A 1 93  ? 34.387  8.421   -15.322 1.00 23.04  ? 122 LEU A CA  1 
ATOM   725  C C   . LEU A 1 93  ? 33.832  9.014   -14.026 1.00 20.96  ? 122 LEU A C   1 
ATOM   726  O O   . LEU A 1 93  ? 34.242  10.076  -13.575 1.00 20.12  ? 122 LEU A O   1 
ATOM   727  C CB  . LEU A 1 93  ? 33.477  8.710   -16.527 1.00 21.83  ? 122 LEU A CB  1 
ATOM   728  C CG  . LEU A 1 93  ? 32.954  10.147  -16.654 1.00 24.27  ? 122 LEU A CG  1 
ATOM   729  C CD1 . LEU A 1 93  ? 34.083  11.128  -16.842 1.00 24.18  ? 122 LEU A CD1 1 
ATOM   730  C CD2 . LEU A 1 93  ? 31.940  10.223  -17.814 1.00 24.69  ? 122 LEU A CD2 1 
ATOM   731  N N   . LEU A 1 94  ? 32.791  8.388   -13.479 1.00 23.11  ? 123 LEU A N   1 
ATOM   732  C CA  . LEU A 1 94  ? 32.147  8.952   -12.304 1.00 20.95  ? 123 LEU A CA  1 
ATOM   733  C C   . LEU A 1 94  ? 33.147  9.028   -11.148 1.00 20.25  ? 123 LEU A C   1 
ATOM   734  O O   . LEU A 1 94  ? 33.141  9.988   -10.389 1.00 21.24  ? 123 LEU A O   1 
ATOM   735  C CB  . LEU A 1 94  ? 30.937  8.079   -11.955 1.00 20.47  ? 123 LEU A CB  1 
ATOM   736  C CG  . LEU A 1 94  ? 29.765  8.105   -12.933 1.00 23.03  ? 123 LEU A CG  1 
ATOM   737  C CD1 . LEU A 1 94  ? 28.499  7.490   -12.302 1.00 25.77  ? 123 LEU A CD1 1 
ATOM   738  C CD2 . LEU A 1 94  ? 29.418  9.502   -13.402 1.00 23.81  ? 123 LEU A CD2 1 
ATOM   739  N N   . VAL A 1 95  ? 34.024  8.034   -11.018 1.00 23.21  ? 124 VAL A N   1 
ATOM   740  C CA  . VAL A 1 95  ? 34.953  7.958   -9.892  1.00 26.45  ? 124 VAL A CA  1 
ATOM   741  C C   . VAL A 1 95  ? 36.089  8.969   -10.040 1.00 26.32  ? 124 VAL A C   1 
ATOM   742  O O   . VAL A 1 95  ? 36.535  9.520   -9.026  1.00 22.84  ? 124 VAL A O   1 
ATOM   743  C CB  . VAL A 1 95  ? 35.537  6.542   -9.728  1.00 27.73  ? 124 VAL A CB  1 
ATOM   744  C CG1 . VAL A 1 95  ? 36.728  6.505   -8.778  1.00 32.45  ? 124 VAL A CG1 1 
ATOM   745  C CG2 . VAL A 1 95  ? 34.459  5.607   -9.234  1.00 27.55  ? 124 VAL A CG2 1 
ATOM   746  N N   . THR A 1 96  ? 36.606  9.141   -11.271 1.00 24.57  ? 125 THR A N   1 
ATOM   747  C CA  . THR A 1 96  ? 37.855  9.870   -11.463 1.00 25.64  ? 125 THR A CA  1 
ATOM   748  C C   . THR A 1 96  ? 37.592  11.236  -12.063 1.00 27.33  ? 125 THR A C   1 
ATOM   749  O O   . THR A 1 96  ? 38.459  12.113  -11.967 1.00 26.19  ? 125 THR A O   1 
ATOM   750  C CB  . THR A 1 96  ? 38.844  9.117   -12.352 1.00 25.12  ? 125 THR A CB  1 
ATOM   751  O OG1 . THR A 1 96  ? 38.291  9.056   -13.674 1.00 23.94  ? 125 THR A OG1 1 
ATOM   752  C CG2 . THR A 1 96  ? 39.184  7.762   -11.766 1.00 26.75  ? 125 THR A CG2 1 
ATOM   753  N N   . GLY A 1 97  ? 36.441  11.379  -12.733 1.00 24.90  ? 126 GLY A N   1 
ATOM   754  C CA  . GLY A 1 97  ? 36.209  12.590  -13.496 1.00 28.46  ? 126 GLY A CA  1 
ATOM   755  C C   . GLY A 1 97  ? 36.949  12.581  -14.830 1.00 26.92  ? 126 GLY A C   1 
ATOM   756  O O   . GLY A 1 97  ? 36.892  13.582  -15.539 1.00 26.06  ? 126 GLY A O   1 
ATOM   757  N N   . HIS A 1 98  ? 37.559  11.446  -15.185 1.00 25.86  ? 127 HIS A N   1 
ATOM   758  C CA  . HIS A 1 98  ? 38.299  11.338  -16.437 1.00 29.27  ? 127 HIS A CA  1 
ATOM   759  C C   . HIS A 1 98  ? 37.709  10.241  -17.294 1.00 27.94  ? 127 HIS A C   1 
ATOM   760  O O   . HIS A 1 98  ? 37.269  9.209   -16.804 1.00 27.09  ? 127 HIS A O   1 
ATOM   761  C CB  . HIS A 1 98  ? 39.797  11.064  -16.181 1.00 31.30  ? 127 HIS A CB  1 
ATOM   762  C CG  . HIS A 1 98  ? 40.425  12.084  -15.277 1.00 39.15  ? 127 HIS A CG  1 
ATOM   763  N ND1 . HIS A 1 98  ? 40.169  13.428  -15.385 1.00 51.04  ? 127 HIS A ND1 1 
ATOM   764  C CD2 . HIS A 1 98  ? 41.312  11.964  -14.264 1.00 45.90  ? 127 HIS A CD2 1 
ATOM   765  C CE1 . HIS A 1 98  ? 40.880  14.089  -14.473 1.00 51.22  ? 127 HIS A CE1 1 
ATOM   766  N NE2 . HIS A 1 98  ? 41.579  13.225  -13.783 1.00 50.08  ? 127 HIS A NE2 1 
ATOM   767  N N   . ILE A 1 99  ? 37.741  10.445  -18.620 1.00 28.18  ? 128 ILE A N   1 
ATOM   768  C CA  . ILE A 1 99  ? 37.381  9.383   -19.534 1.00 26.84  ? 128 ILE A CA  1 
ATOM   769  C C   . ILE A 1 99  ? 38.443  8.283   -19.460 1.00 25.71  ? 128 ILE A C   1 
ATOM   770  O O   . ILE A 1 99  ? 39.604  8.597   -19.555 1.00 28.68  ? 128 ILE A O   1 
ATOM   771  C CB  . ILE A 1 99  ? 37.260  9.953   -20.963 1.00 29.40  ? 128 ILE A CB  1 
ATOM   772  C CG1 . ILE A 1 99  ? 36.147  11.022  -21.048 1.00 31.28  ? 128 ILE A CG1 1 
ATOM   773  C CG2 . ILE A 1 99  ? 37.045  8.807   -21.954 1.00 26.75  ? 128 ILE A CG2 1 
ATOM   774  C CD1 . ILE A 1 99  ? 34.719  10.475  -20.983 1.00 28.83  ? 128 ILE A CD1 1 
ATOM   775  N N   . PRO A 1 100 ? 38.112  6.983   -19.273 1.00 25.74  ? 129 PRO A N   1 
ATOM   776  C CA  . PRO A 1 100 ? 39.116  5.912   -19.255 1.00 26.25  ? 129 PRO A CA  1 
ATOM   777  C C   . PRO A 1 100 ? 39.653  5.598   -20.646 1.00 26.77  ? 129 PRO A C   1 
ATOM   778  O O   . PRO A 1 100 ? 38.906  5.715   -21.603 1.00 24.58  ? 129 PRO A O   1 
ATOM   779  C CB  . PRO A 1 100 ? 38.310  4.701   -18.756 1.00 23.28  ? 129 PRO A CB  1 
ATOM   780  C CG  . PRO A 1 100 ? 36.937  4.985   -19.221 1.00 26.36  ? 129 PRO A CG  1 
ATOM   781  C CD  . PRO A 1 100 ? 36.754  6.471   -19.036 1.00 26.49  ? 129 PRO A CD  1 
ATOM   782  N N   . THR A 1 101 ? 40.900  5.121   -20.697 1.00 28.15  ? 130 THR A N   1 
ATOM   783  C CA  . THR A 1 101 ? 41.432  4.400   -21.835 1.00 31.34  ? 130 THR A CA  1 
ATOM   784  C C   . THR A 1 101 ? 40.740  3.043   -21.952 1.00 32.89  ? 130 THR A C   1 
ATOM   785  O O   . THR A 1 101 ? 40.093  2.570   -21.012 1.00 29.19  ? 130 THR A O   1 
ATOM   786  C CB  . THR A 1 101 ? 42.948  4.210   -21.670 1.00 31.80  ? 130 THR A CB  1 
ATOM   787  O OG1 . THR A 1 101 ? 43.146  3.287   -20.594 1.00 30.93  ? 130 THR A OG1 1 
ATOM   788  C CG2 . THR A 1 101 ? 43.690  5.521   -21.458 1.00 31.95  ? 130 THR A CG2 1 
ATOM   789  N N   . GLU A 1 102 ? 40.922  2.419   -23.126 1.00 32.69  ? 131 GLU A N   1 
ATOM   790  C CA  . GLU A 1 102 ? 40.562  1.038   -23.381 1.00 36.26  ? 131 GLU A CA  1 
ATOM   791  C C   . GLU A 1 102 ? 41.167  0.129   -22.313 1.00 31.16  ? 131 GLU A C   1 
ATOM   792  O O   . GLU A 1 102 ? 40.520  -0.776  -21.839 1.00 31.23  ? 131 GLU A O   1 
ATOM   793  C CB  . GLU A 1 102 ? 41.115  0.568   -24.735 1.00 41.05  ? 131 GLU A CB  1 
ATOM   794  C CG  . GLU A 1 102 ? 40.361  1.102   -25.952 1.00 48.03  ? 131 GLU A CG  1 
ATOM   795  C CD  . GLU A 1 102 ? 39.022  0.435   -26.242 1.00 59.42  ? 131 GLU A CD  1 
ATOM   796  O OE1 . GLU A 1 102 ? 38.718  -0.603  -25.603 1.00 60.12  ? 131 GLU A OE1 1 
ATOM   797  O OE2 . GLU A 1 102 ? 38.263  0.966   -27.092 1.00 61.81  ? 131 GLU A OE2 1 
ATOM   798  N N   . GLU A 1 103 ? 42.440  0.358   -21.988 1.00 34.99  ? 132 GLU A N   1 
ATOM   799  C CA  . GLU A 1 103 ? 43.179  -0.496  -21.078 1.00 35.76  ? 132 GLU A CA  1 
ATOM   800  C C   . GLU A 1 103 ? 42.570  -0.423  -19.669 1.00 29.04  ? 132 GLU A C   1 
ATOM   801  O O   . GLU A 1 103 ? 42.446  -1.433  -19.001 1.00 29.02  ? 132 GLU A O   1 
ATOM   802  C CB  . GLU A 1 103 ? 44.658  -0.089  -21.125 1.00 42.76  ? 132 GLU A CB  1 
ATOM   803  C CG  . GLU A 1 103 ? 45.348  -0.418  -22.451 1.00 52.02  ? 132 GLU A CG  1 
ATOM   804  C CD  . GLU A 1 103 ? 45.134  0.486   -23.675 1.00 59.05  ? 132 GLU A CD  1 
ATOM   805  O OE1 . GLU A 1 103 ? 44.469  1.549   -23.663 1.00 46.05  ? 132 GLU A OE1 1 
ATOM   806  O OE2 . GLU A 1 103 ? 45.688  0.075   -24.713 1.00 69.07  ? 132 GLU A OE2 1 
ATOM   807  N N   . GLN A 1 104 ? 42.228  0.783   -19.217 1.00 24.13  ? 133 GLN A N   1 
ATOM   808  C CA  . GLN A 1 104 ? 41.630  0.964   -17.910 1.00 26.80  ? 133 GLN A CA  1 
ATOM   809  C C   . GLN A 1 104 ? 40.271  0.268   -17.846 1.00 25.67  ? 133 GLN A C   1 
ATOM   810  O O   . GLN A 1 104 ? 39.921  -0.380  -16.865 1.00 29.00  ? 133 GLN A O   1 
ATOM   811  C CB  . GLN A 1 104 ? 41.545  2.452   -17.629 1.00 25.78  ? 133 GLN A CB  1 
ATOM   812  C CG  . GLN A 1 104 ? 42.914  3.079   -17.417 1.00 25.75  ? 133 GLN A CG  1 
ATOM   813  C CD  . GLN A 1 104 ? 42.890  4.585   -17.342 1.00 27.16  ? 133 GLN A CD  1 
ATOM   814  O OE1 . GLN A 1 104 ? 42.020  5.271   -17.899 1.00 29.37  ? 133 GLN A OE1 1 
ATOM   815  N NE2 . GLN A 1 104 ? 43.869  5.102   -16.629 1.00 28.51  ? 133 GLN A NE2 1 
ATOM   816  N N   . VAL A 1 105 ? 39.522  0.320   -18.935 1.00 29.82  ? 134 VAL A N   1 
ATOM   817  C CA  . VAL A 1 105 ? 38.233  -0.339  -18.952 1.00 27.98  ? 134 VAL A CA  1 
ATOM   818  C C   . VAL A 1 105 ? 38.481  -1.842  -18.881 1.00 29.13  ? 134 VAL A C   1 
ATOM   819  O O   . VAL A 1 105 ? 37.798  -2.534  -18.128 1.00 27.24  ? 134 VAL A O   1 
ATOM   820  C CB  . VAL A 1 105 ? 37.366  0.088   -20.156 1.00 28.04  ? 134 VAL A CB  1 
ATOM   821  C CG1 . VAL A 1 105 ? 36.250  -0.892  -20.439 1.00 27.82  ? 134 VAL A CG1 1 
ATOM   822  C CG2 . VAL A 1 105 ? 36.805  1.494   -19.947 1.00 28.80  ? 134 VAL A CG2 1 
ATOM   823  N N   . SER A 1 106 ? 39.457  -2.348  -19.665 1.00 29.29  ? 135 SER A N   1 
ATOM   824  C CA  A SER A 1 106 ? 39.799  -3.765  -19.657 0.50 29.23  ? 135 SER A CA  1 
ATOM   825  C CA  B SER A 1 106 ? 39.797  -3.769  -19.657 0.50 29.02  ? 135 SER A CA  1 
ATOM   826  C C   . SER A 1 106 ? 40.195  -4.234  -18.251 1.00 26.45  ? 135 SER A C   1 
ATOM   827  O O   . SER A 1 106 ? 39.739  -5.288  -17.798 1.00 27.43  ? 135 SER A O   1 
ATOM   828  C CB  A SER A 1 106 ? 40.885  -4.064  -20.647 0.50 30.33  ? 135 SER A CB  1 
ATOM   829  C CB  B SER A 1 106 ? 40.877  -4.085  -20.656 0.50 29.86  ? 135 SER A CB  1 
ATOM   830  O OG  A SER A 1 106 ? 40.983  -5.464  -20.836 0.50 31.61  ? 135 SER A OG  1 
ATOM   831  O OG  B SER A 1 106 ? 40.405  -3.852  -21.974 0.50 30.58  ? 135 SER A OG  1 
ATOM   832  N N   . TRP A 1 107 ? 41.017  -3.440  -17.555 1.00 25.23  ? 136 TRP A N   1 
ATOM   833  C CA  . TRP A 1 107 ? 41.428  -3.787  -16.194 1.00 27.47  ? 136 TRP A CA  1 
ATOM   834  C C   . TRP A 1 107 ? 40.216  -3.869  -15.243 1.00 27.14  ? 136 TRP A C   1 
ATOM   835  O O   . TRP A 1 107 ? 40.098  -4.748  -14.390 1.00 28.16  ? 136 TRP A O   1 
ATOM   836  C CB  . TRP A 1 107 ? 42.443  -2.750  -15.708 1.00 29.76  ? 136 TRP A CB  1 
ATOM   837  C CG  . TRP A 1 107 ? 42.831  -2.910  -14.261 1.00 30.72  ? 136 TRP A CG  1 
ATOM   838  C CD1 . TRP A 1 107 ? 43.889  -3.611  -13.756 1.00 33.99  ? 136 TRP A CD1 1 
ATOM   839  C CD2 . TRP A 1 107 ? 42.155  -2.326  -13.128 1.00 30.61  ? 136 TRP A CD2 1 
ATOM   840  N NE1 . TRP A 1 107 ? 43.919  -3.499  -12.388 1.00 34.72  ? 136 TRP A NE1 1 
ATOM   841  C CE2 . TRP A 1 107 ? 42.858  -2.731  -11.973 1.00 35.18  ? 136 TRP A CE2 1 
ATOM   842  C CE3 . TRP A 1 107 ? 41.017  -1.534  -12.971 1.00 30.45  ? 136 TRP A CE3 1 
ATOM   843  C CZ2 . TRP A 1 107 ? 42.460  -2.361  -10.687 1.00 34.94  ? 136 TRP A CZ2 1 
ATOM   844  C CZ3 . TRP A 1 107 ? 40.628  -1.173  -11.704 1.00 28.44  ? 136 TRP A CZ3 1 
ATOM   845  C CH2 . TRP A 1 107 ? 41.335  -1.581  -10.580 1.00 32.39  ? 136 TRP A CH2 1 
ATOM   846  N N   . LEU A 1 108 ? 39.280  -2.940  -15.390 1.00 29.08  ? 137 LEU A N   1 
ATOM   847  C CA  . LEU A 1 108 ? 38.121  -2.906  -14.524 1.00 26.84  ? 137 LEU A CA  1 
ATOM   848  C C   . LEU A 1 108 ? 37.167  -4.063  -14.801 1.00 24.63  ? 137 LEU A C   1 
ATOM   849  O O   . LEU A 1 108 ? 36.610  -4.613  -13.861 1.00 23.80  ? 137 LEU A O   1 
ATOM   850  C CB  . LEU A 1 108 ? 37.471  -1.531  -14.649 1.00 27.90  ? 137 LEU A CB  1 
ATOM   851  C CG  . LEU A 1 108 ? 36.279  -1.261  -13.744 1.00 27.95  ? 137 LEU A CG  1 
ATOM   852  C CD1 . LEU A 1 108 ? 36.646  -1.482  -12.286 1.00 28.35  ? 137 LEU A CD1 1 
ATOM   853  C CD2 . LEU A 1 108 ? 35.796  0.141   -13.965 1.00 24.58  ? 137 LEU A CD2 1 
ATOM   854  N N   . SER A 1 109 ? 36.960  -4.468  -16.067 1.00 23.61  ? 138 SER A N   1 
ATOM   855  C CA  . SER A 1 109 ? 36.177  -5.661  -16.347 1.00 25.37  ? 138 SER A CA  1 
ATOM   856  C C   . SER A 1 109 ? 36.731  -6.871  -15.612 1.00 27.26  ? 138 SER A C   1 
ATOM   857  O O   . SER A 1 109 ? 35.968  -7.738  -15.137 1.00 27.20  ? 138 SER A O   1 
ATOM   858  C CB  . SER A 1 109 ? 36.113  -6.013  -17.817 1.00 25.95  ? 138 SER A CB  1 
ATOM   859  O OG  . SER A 1 109 ? 35.471  -5.001  -18.585 1.00 26.76  ? 138 SER A OG  1 
ATOM   860  N N   . LYS A 1 110 ? 38.071  -6.984  -15.610 1.00 24.66  ? 139 LYS A N   1 
ATOM   861  C CA  . LYS A 1 110 ? 38.691  -8.165  -15.035 1.00 28.41  ? 139 LYS A CA  1 
ATOM   862  C C   . LYS A 1 110 ? 38.581  -8.101  -13.507 1.00 25.28  ? 139 LYS A C   1 
ATOM   863  O O   . LYS A 1 110 ? 38.351  -9.120  -12.896 1.00 26.88  ? 139 LYS A O   1 
ATOM   864  C CB  . LYS A 1 110 ? 40.151  -8.262  -15.493 1.00 34.19  ? 139 LYS A CB  1 
ATOM   865  C CG  . LYS A 1 110 ? 40.317  -8.643  -16.959 1.00 38.74  ? 139 LYS A CG  1 
ATOM   866  C CD  . LYS A 1 110 ? 41.766  -8.566  -17.441 1.00 46.23  ? 139 LYS A CD  1 
ATOM   867  C CE  . LYS A 1 110 ? 41.871  -8.783  -18.931 1.00 53.95  ? 139 LYS A CE  1 
ATOM   868  N NZ  . LYS A 1 110 ? 42.975  -8.016  -19.526 1.00 62.76  ? 139 LYS A NZ  1 
ATOM   869  N N   . GLU A 1 111 ? 38.715  -6.915  -12.901 1.00 25.00  ? 140 GLU A N   1 
ATOM   870  C CA  . GLU A 1 111 ? 38.547  -6.782  -11.459 1.00 29.36  ? 140 GLU A CA  1 
ATOM   871  C C   . GLU A 1 111 ? 37.153  -7.234  -11.012 1.00 28.39  ? 140 GLU A C   1 
ATOM   872  O O   . GLU A 1 111 ? 37.017  -7.858  -9.968  1.00 25.47  ? 140 GLU A O   1 
ATOM   873  C CB  . GLU A 1 111 ? 38.714  -5.359  -10.967 1.00 34.16  ? 140 GLU A CB  1 
ATOM   874  C CG  . GLU A 1 111 ? 40.155  -4.920  -10.783 1.00 43.58  ? 140 GLU A CG  1 
ATOM   875  C CD  . GLU A 1 111 ? 40.784  -5.650  -9.606  1.00 41.95  ? 140 GLU A CD  1 
ATOM   876  O OE1 . GLU A 1 111 ? 40.423  -5.465  -8.420  1.00 45.66  ? 140 GLU A OE1 1 
ATOM   877  O OE2 . GLU A 1 111 ? 41.588  -6.496  -9.941  1.00 41.86  ? 140 GLU A OE2 1 
ATOM   878  N N   . TRP A 1 112 ? 36.114  -6.862  -11.759 1.00 26.24  ? 141 TRP A N   1 
ATOM   879  C CA  . TRP A 1 112 ? 34.747  -7.230  -11.428 1.00 24.71  ? 141 TRP A CA  1 
ATOM   880  C C   . TRP A 1 112 ? 34.503  -8.722  -11.654 1.00 28.47  ? 141 TRP A C   1 
ATOM   881  O O   . TRP A 1 112 ? 33.938  -9.396  -10.795 1.00 28.34  ? 141 TRP A O   1 
ATOM   882  C CB  . TRP A 1 112 ? 33.749  -6.341  -12.190 1.00 24.76  ? 141 TRP A CB  1 
ATOM   883  C CG  . TRP A 1 112 ? 33.694  -4.928  -11.650 1.00 22.32  ? 141 TRP A CG  1 
ATOM   884  C CD1 . TRP A 1 112 ? 34.271  -4.457  -10.512 1.00 23.28  ? 141 TRP A CD1 1 
ATOM   885  C CD2 . TRP A 1 112 ? 33.003  -3.808  -12.230 1.00 23.01  ? 141 TRP A CD2 1 
ATOM   886  N NE1 . TRP A 1 112 ? 34.043  -3.118  -10.381 1.00 25.31  ? 141 TRP A NE1 1 
ATOM   887  C CE2 . TRP A 1 112 ? 33.255  -2.694  -11.413 1.00 24.99  ? 141 TRP A CE2 1 
ATOM   888  C CE3 . TRP A 1 112 ? 32.245  -3.630  -13.386 1.00 25.47  ? 141 TRP A CE3 1 
ATOM   889  C CZ2 . TRP A 1 112 ? 32.742  -1.433  -11.686 1.00 25.58  ? 141 TRP A CZ2 1 
ATOM   890  C CZ3 . TRP A 1 112 ? 31.724  -2.385  -13.661 1.00 26.46  ? 141 TRP A CZ3 1 
ATOM   891  C CH2 . TRP A 1 112 ? 32.004  -1.295  -12.842 1.00 25.62  ? 141 TRP A CH2 1 
ATOM   892  N N   . ALA A 1 113 ? 35.025  -9.284  -12.751 1.00 28.59  ? 142 ALA A N   1 
ATOM   893  C CA  . ALA A 1 113 ? 35.007  -10.735 -12.945 1.00 29.83  ? 142 ALA A CA  1 
ATOM   894  C C   . ALA A 1 113 ? 35.540  -11.487 -11.715 1.00 29.21  ? 142 ALA A C   1 
ATOM   895  O O   . ALA A 1 113 ? 34.856  -12.361 -11.190 1.00 29.90  ? 142 ALA A O   1 
ATOM   896  C CB  . ALA A 1 113 ? 35.793  -11.086 -14.177 1.00 30.68  ? 142 ALA A CB  1 
ATOM   897  N N   . LYS A 1 114 ? 36.672  -11.039 -11.169 1.00 28.69  ? 143 LYS A N   1 
ATOM   898  C CA  . LYS A 1 114 ? 37.377  -11.741 -10.103 1.00 32.47  ? 143 LYS A CA  1 
ATOM   899  C C   . LYS A 1 114 ? 36.644  -11.613 -8.771  1.00 30.67  ? 143 LYS A C   1 
ATOM   900  O O   . LYS A 1 114 ? 36.802  -12.490 -7.934  1.00 27.87  ? 143 LYS A O   1 
ATOM   901  C CB  . LYS A 1 114 ? 38.762  -11.175 -9.756  1.00 38.04  ? 143 LYS A CB  1 
ATOM   902  C CG  . LYS A 1 114 ? 39.861  -11.229 -10.787 1.00 51.18  ? 143 LYS A CG  1 
ATOM   903  C CD  . LYS A 1 114 ? 41.110  -10.530 -10.251 1.00 53.88  ? 143 LYS A CD  1 
ATOM   904  C CE  . LYS A 1 114 ? 42.262  -10.510 -11.218 1.00 58.46  ? 143 LYS A CE  1 
ATOM   905  N NZ  . LYS A 1 114 ? 43.339  -9.647  -10.719 1.00 55.07  ? 143 LYS A NZ  1 
ATOM   906  N N   . ARG A 1 115 ? 35.850  -10.525 -8.557  1.00 25.98  ? 144 ARG A N   1 
ATOM   907  C CA  . ARG A 1 115 ? 35.201  -10.300 -7.267  1.00 24.31  ? 144 ARG A CA  1 
ATOM   908  C C   . ARG A 1 115 ? 33.767  -10.842 -7.218  1.00 24.47  ? 144 ARG A C   1 
ATOM   909  O O   . ARG A 1 115 ? 33.061  -10.585 -6.251  1.00 27.71  ? 144 ARG A O   1 
ATOM   910  C CB  . ARG A 1 115 ? 35.190  -8.792  -6.985  1.00 23.65  ? 144 ARG A CB  1 
ATOM   911  C CG  . ARG A 1 115 ? 36.539  -8.150  -6.728  1.00 25.95  ? 144 ARG A CG  1 
ATOM   912  C CD  . ARG A 1 115 ? 36.480  -6.666  -6.871  1.00 25.53  ? 144 ARG A CD  1 
ATOM   913  N NE  . ARG A 1 115 ? 37.808  -6.120  -6.558  1.00 27.72  ? 144 ARG A NE  1 
ATOM   914  C CZ  . ARG A 1 115 ? 38.124  -5.389  -5.508  1.00 26.79  ? 144 ARG A CZ  1 
ATOM   915  N NH1 . ARG A 1 115 ? 37.351  -5.411  -4.452  1.00 25.13  ? 144 ARG A NH1 1 
ATOM   916  N NH2 . ARG A 1 115 ? 39.285  -4.746  -5.485  1.00 27.66  ? 144 ARG A NH2 1 
ATOM   917  N N   . ALA A 1 116 ? 33.344  -11.603 -8.234  1.00 28.50  ? 145 ALA A N   1 
ATOM   918  C CA  . ALA A 1 116 ? 31.940  -11.917 -8.480  1.00 31.30  ? 145 ALA A CA  1 
ATOM   919  C C   . ALA A 1 116 ? 31.333  -13.038 -7.623  1.00 32.49  ? 145 ALA A C   1 
ATOM   920  O O   . ALA A 1 116 ? 30.114  -13.246 -7.695  1.00 41.25  ? 145 ALA A O   1 
ATOM   921  C CB  . ALA A 1 116 ? 31.738  -12.248 -9.936  1.00 31.99  ? 145 ALA A CB  1 
ATOM   922  N N   . ALA A 1 117 ? 32.101  -13.718 -6.780  1.00 30.64  ? 146 ALA A N   1 
ATOM   923  C CA  . ALA A 1 117 ? 31.571  -14.857 -6.037  1.00 34.15  ? 146 ALA A CA  1 
ATOM   924  C C   . ALA A 1 117 ? 30.534  -14.455 -4.984  1.00 30.81  ? 146 ALA A C   1 
ATOM   925  O O   . ALA A 1 117 ? 30.779  -13.538 -4.206  1.00 32.56  ? 146 ALA A O   1 
ATOM   926  C CB  . ALA A 1 117 ? 32.695  -15.615 -5.373  1.00 37.00  ? 146 ALA A CB  1 
ATOM   927  N N   . LEU A 1 118 ? 29.454  -15.246 -4.884  1.00 28.17  ? 147 LEU A N   1 
ATOM   928  C CA  . LEU A 1 118 ? 28.490  -15.144 -3.800  1.00 27.35  ? 147 LEU A CA  1 
ATOM   929  C C   . LEU A 1 118 ? 28.822  -16.119 -2.662  1.00 28.75  ? 147 LEU A C   1 
ATOM   930  O O   . LEU A 1 118 ? 29.102  -17.292 -2.875  1.00 27.32  ? 147 LEU A O   1 
ATOM   931  C CB  . LEU A 1 118 ? 27.065  -15.377 -4.303  1.00 24.97  ? 147 LEU A CB  1 
ATOM   932  C CG  . LEU A 1 118 ? 26.548  -14.442 -5.394  1.00 27.35  ? 147 LEU A CG  1 
ATOM   933  C CD1 . LEU A 1 118 ? 25.085  -14.683 -5.660  1.00 28.51  ? 147 LEU A CD1 1 
ATOM   934  C CD2 . LEU A 1 118 ? 26.761  -13.007 -4.990  1.00 26.33  ? 147 LEU A CD2 1 
ATOM   935  N N   . PRO A 1 119 ? 28.695  -15.710 -1.388  1.00 28.88  ? 148 PRO A N   1 
ATOM   936  C CA  . PRO A 1 119 ? 28.782  -16.674 -0.288  1.00 27.57  ? 148 PRO A CA  1 
ATOM   937  C C   . PRO A 1 119 ? 27.571  -17.604 -0.258  1.00 25.21  ? 148 PRO A C   1 
ATOM   938  O O   . PRO A 1 119 ? 26.466  -17.229 -0.647  1.00 24.27  ? 148 PRO A O   1 
ATOM   939  C CB  . PRO A 1 119 ? 28.883  -15.771 0.959   1.00 26.54  ? 148 PRO A CB  1 
ATOM   940  C CG  . PRO A 1 119 ? 28.192  -14.502 0.569   1.00 29.84  ? 148 PRO A CG  1 
ATOM   941  C CD  . PRO A 1 119 ? 28.350  -14.338 -0.955  1.00 30.18  ? 148 PRO A CD  1 
ATOM   942  N N   . SER A 1 120 ? 27.741  -18.808 0.290   1.00 24.62  ? 149 SER A N   1 
ATOM   943  C CA  . SER A 1 120 ? 26.744  -19.864 0.148   1.00 23.05  ? 149 SER A CA  1 
ATOM   944  C C   . SER A 1 120 ? 25.400  -19.425 0.767   1.00 23.22  ? 149 SER A C   1 
ATOM   945  O O   . SER A 1 120 ? 24.306  -19.732 0.261   1.00 22.42  ? 149 SER A O   1 
ATOM   946  C CB  . SER A 1 120 ? 27.320  -21.116 0.747   1.00 28.71  ? 149 SER A CB  1 
ATOM   947  O OG  . SER A 1 120 ? 27.181  -20.997 2.154   1.00 50.39  ? 149 SER A OG  1 
ATOM   948  N N   . HIS A 1 121 ? 25.442  -18.612 1.828   1.00 20.79  ? 150 HIS A N   1 
ATOM   949  C CA  . HIS A 1 121 ? 24.198  -18.262 2.508   1.00 21.67  ? 150 HIS A CA  1 
ATOM   950  C C   . HIS A 1 121 ? 23.307  -17.393 1.627   1.00 21.83  ? 150 HIS A C   1 
ATOM   951  O O   . HIS A 1 121 ? 22.082  -17.464 1.744   1.00 21.25  ? 150 HIS A O   1 
ATOM   952  C CB  . HIS A 1 121 ? 24.426  -17.677 3.896   1.00 21.73  ? 150 HIS A CB  1 
ATOM   953  C CG  . HIS A 1 121 ? 24.886  -16.276 3.932   1.00 22.91  ? 150 HIS A CG  1 
ATOM   954  N ND1 . HIS A 1 121 ? 26.197  -15.890 3.790   1.00 25.38  ? 150 HIS A ND1 1 
ATOM   955  C CD2 . HIS A 1 121 ? 24.179  -15.159 4.103   1.00 22.90  ? 150 HIS A CD2 1 
ATOM   956  C CE1 . HIS A 1 121 ? 26.255  -14.578 3.897   1.00 26.84  ? 150 HIS A CE1 1 
ATOM   957  N NE2 . HIS A 1 121 ? 25.055  -14.125 4.095   1.00 23.49  ? 150 HIS A NE2 1 
ATOM   958  N N   . VAL A 1 122 ? 23.917  -16.624 0.720   1.00 21.65  ? 151 VAL A N   1 
ATOM   959  C CA  . VAL A 1 122 ? 23.159  -15.761 -0.155  1.00 22.69  ? 151 VAL A CA  1 
ATOM   960  C C   . VAL A 1 122 ? 22.617  -16.572 -1.324  1.00 23.69  ? 151 VAL A C   1 
ATOM   961  O O   . VAL A 1 122 ? 21.475  -16.441 -1.683  1.00 22.63  ? 151 VAL A O   1 
ATOM   962  C CB  . VAL A 1 122 ? 23.977  -14.537 -0.567  1.00 22.05  ? 151 VAL A CB  1 
ATOM   963  C CG1 . VAL A 1 122 ? 23.263  -13.695 -1.622  1.00 21.55  ? 151 VAL A CG1 1 
ATOM   964  C CG2 . VAL A 1 122 ? 24.342  -13.720 0.669   1.00 23.50  ? 151 VAL A CG2 1 
ATOM   965  N N   . VAL A 1 123 ? 23.392  -17.495 -1.865  1.00 27.06  ? 152 VAL A N   1 
ATOM   966  C CA  . VAL A 1 123 ? 22.856  -18.412 -2.868  1.00 24.44  ? 152 VAL A CA  1 
ATOM   967  C C   . VAL A 1 123 ? 21.628  -19.157 -2.334  1.00 23.14  ? 152 VAL A C   1 
ATOM   968  O O   . VAL A 1 123 ? 20.595  -19.233 -3.002  1.00 23.40  ? 152 VAL A O   1 
ATOM   969  C CB  . VAL A 1 123 ? 23.954  -19.380 -3.325  1.00 23.84  ? 152 VAL A CB  1 
ATOM   970  C CG1 . VAL A 1 123 ? 23.444  -20.254 -4.455  1.00 30.40  ? 152 VAL A CG1 1 
ATOM   971  C CG2 . VAL A 1 123 ? 25.194  -18.616 -3.816  1.00 25.42  ? 152 VAL A CG2 1 
ATOM   972  N N   . THR A 1 124 ? 21.714  -19.636 -1.088  1.00 20.45  ? 153 THR A N   1 
ATOM   973  C CA  . THR A 1 124 ? 20.668  -20.407 -0.462  1.00 22.77  ? 153 THR A CA  1 
ATOM   974  C C   . THR A 1 124 ? 19.403  -19.579 -0.261  1.00 23.14  ? 153 THR A C   1 
ATOM   975  O O   . THR A 1 124 ? 18.269  -20.061 -0.411  1.00 24.24  ? 153 THR A O   1 
ATOM   976  C CB  . THR A 1 124 ? 21.175  -20.904 0.891   1.00 24.34  ? 153 THR A CB  1 
ATOM   977  O OG1 . THR A 1 124 ? 22.261  -21.762 0.581   1.00 26.16  ? 153 THR A OG1 1 
ATOM   978  C CG2 . THR A 1 124 ? 20.112  -21.618 1.692   1.00 26.39  ? 153 THR A CG2 1 
ATOM   979  N N   . MET A 1 125 ? 19.602  -18.341 0.203   1.00 22.63  ? 154 MET A N   1 
ATOM   980  C CA  . MET A 1 125 ? 18.465  -17.485 0.509   1.00 23.62  ? 154 MET A CA  1 
ATOM   981  C C   . MET A 1 125 ? 17.691  -17.208 -0.776  1.00 21.98  ? 154 MET A C   1 
ATOM   982  O O   . MET A 1 125 ? 16.473  -17.279 -0.789  1.00 23.43  ? 154 MET A O   1 
ATOM   983  C CB  . MET A 1 125 ? 19.016  -16.218 1.156   1.00 26.69  ? 154 MET A CB  1 
ATOM   984  C CG  . MET A 1 125 ? 18.046  -15.145 1.478   1.00 36.44  ? 154 MET A CG  1 
ATOM   985  S SD  . MET A 1 125 ? 19.085  -13.686 1.704   1.00 41.46  ? 154 MET A SD  1 
ATOM   986  C CE  . MET A 1 125 ? 17.773  -12.533 2.042   1.00 42.84  ? 154 MET A CE  1 
ATOM   987  N N   . LEU A 1 126 ? 18.404  -16.894 -1.857  1.00 24.69  ? 155 LEU A N   1 
ATOM   988  C CA  . LEU A 1 126 ? 17.769  -16.651 -3.143  1.00 26.68  ? 155 LEU A CA  1 
ATOM   989  C C   . LEU A 1 126 ? 17.039  -17.888 -3.653  1.00 30.01  ? 155 LEU A C   1 
ATOM   990  O O   . LEU A 1 126 ? 15.922  -17.747 -4.152  1.00 28.81  ? 155 LEU A O   1 
ATOM   991  C CB  . LEU A 1 126 ? 18.777  -16.181 -4.183  1.00 27.23  ? 155 LEU A CB  1 
ATOM   992  C CG  . LEU A 1 126 ? 19.320  -14.763 -3.980  1.00 26.74  ? 155 LEU A CG  1 
ATOM   993  C CD1 . LEU A 1 126 ? 20.547  -14.506 -4.802  1.00 27.75  ? 155 LEU A CD1 1 
ATOM   994  C CD2 . LEU A 1 126 ? 18.206  -13.796 -4.320  1.00 31.76  ? 155 LEU A CD2 1 
ATOM   995  N N   . ASP A 1 127 ? 17.656  -19.081 -3.550  1.00 25.71  ? 156 ASP A N   1 
ATOM   996  C CA  . ASP A 1 127 ? 16.987  -20.303 -3.993  1.00 29.73  ? 156 ASP A CA  1 
ATOM   997  C C   . ASP A 1 127 ? 15.755  -20.643 -3.154  1.00 28.18  ? 156 ASP A C   1 
ATOM   998  O O   . ASP A 1 127 ? 14.865  -21.354 -3.622  1.00 30.95  ? 156 ASP A O   1 
ATOM   999  C CB  . ASP A 1 127 ? 17.958  -21.481 -4.109  1.00 30.56  ? 156 ASP A CB  1 
ATOM   1000 C CG  . ASP A 1 127 ? 19.107  -21.289 -5.096  1.00 30.10  ? 156 ASP A CG  1 
ATOM   1001 O OD1 . ASP A 1 127 ? 18.985  -20.471 -6.024  1.00 30.39  ? 156 ASP A OD1 1 
ATOM   1002 O OD2 . ASP A 1 127 ? 20.139  -21.944 -4.915  1.00 34.11  ? 156 ASP A OD2 1 
ATOM   1003 N N   . ASN A 1 128 ? 15.664  -20.140 -1.929  1.00 30.06  ? 157 ASN A N   1 
ATOM   1004 C CA  . ASN A 1 128 ? 14.546  -20.469 -1.062  1.00 31.33  ? 157 ASN A CA  1 
ATOM   1005 C C   . ASN A 1 128 ? 13.416  -19.434 -1.181  1.00 33.55  ? 157 ASN A C   1 
ATOM   1006 O O   . ASN A 1 128 ? 12.301  -19.686 -0.731  1.00 34.59  ? 157 ASN A O   1 
ATOM   1007 C CB  . ASN A 1 128 ? 14.997  -20.659 0.386   1.00 32.53  ? 157 ASN A CB  1 
ATOM   1008 C CG  . ASN A 1 128 ? 15.720  -21.976 0.635   1.00 36.22  ? 157 ASN A CG  1 
ATOM   1009 O OD1 . ASN A 1 128 ? 15.448  -22.975 -0.021  1.00 38.19  ? 157 ASN A OD1 1 
ATOM   1010 N ND2 . ASN A 1 128 ? 16.692  -22.000 1.536   1.00 38.85  ? 157 ASN A ND2 1 
ATOM   1011 N N   . PHE A 1 129 ? 13.676  -18.256 -1.743  1.00 29.79  ? 158 PHE A N   1 
ATOM   1012 C CA  . PHE A 1 129 ? 12.624  -17.251 -1.821  1.00 30.20  ? 158 PHE A CA  1 
ATOM   1013 C C   . PHE A 1 129 ? 11.437  -17.785 -2.641  1.00 32.06  ? 158 PHE A C   1 
ATOM   1014 O O   . PHE A 1 129 ? 11.619  -18.251 -3.771  1.00 31.84  ? 158 PHE A O   1 
ATOM   1015 C CB  . PHE A 1 129 ? 13.144  -15.976 -2.473  1.00 29.53  ? 158 PHE A CB  1 
ATOM   1016 C CG  . PHE A 1 129 ? 13.944  -15.025 -1.591  1.00 26.28  ? 158 PHE A CG  1 
ATOM   1017 C CD1 . PHE A 1 129 ? 13.709  -14.944 -0.233  1.00 26.20  ? 158 PHE A CD1 1 
ATOM   1018 C CD2 . PHE A 1 129 ? 14.908  -14.209 -2.156  1.00 28.23  ? 158 PHE A CD2 1 
ATOM   1019 C CE1 . PHE A 1 129 ? 14.411  -14.045 0.538   1.00 28.88  ? 158 PHE A CE1 1 
ATOM   1020 C CE2 . PHE A 1 129 ? 15.638  -13.334 -1.374  1.00 27.80  ? 158 PHE A CE2 1 
ATOM   1021 C CZ  . PHE A 1 129 ? 15.369  -13.260 -0.037  1.00 27.25  ? 158 PHE A CZ  1 
ATOM   1022 N N   . PRO A 1 130 ? 10.184  -17.595 -2.171  1.00 31.65  ? 159 PRO A N   1 
ATOM   1023 C CA  . PRO A 1 130 ? 9.000   -18.021 -2.920  1.00 30.02  ? 159 PRO A CA  1 
ATOM   1024 C C   . PRO A 1 130 ? 8.712   -17.127 -4.130  1.00 33.87  ? 159 PRO A C   1 
ATOM   1025 O O   . PRO A 1 130 ? 9.305   -16.058 -4.281  1.00 27.97  ? 159 PRO A O   1 
ATOM   1026 C CB  . PRO A 1 130 ? 7.917   -17.922 -1.836  1.00 29.86  ? 159 PRO A CB  1 
ATOM   1027 C CG  . PRO A 1 130 ? 8.319   -16.710 -1.014  1.00 29.46  ? 159 PRO A CG  1 
ATOM   1028 C CD  . PRO A 1 130 ? 9.838   -16.849 -0.943  1.00 32.16  ? 159 PRO A CD  1 
ATOM   1029 N N   . THR A 1 131 ? 7.807   -17.565 -5.031  1.00 32.67  ? 160 THR A N   1 
ATOM   1030 C CA  . THR A 1 131 ? 7.648   -16.888 -6.307  1.00 33.36  ? 160 THR A CA  1 
ATOM   1031 C C   . THR A 1 131 ? 6.783   -15.631 -6.149  1.00 29.72  ? 160 THR A C   1 
ATOM   1032 O O   . THR A 1 131 ? 6.708   -14.794 -7.042  1.00 33.14  ? 160 THR A O   1 
ATOM   1033 C CB  . THR A 1 131 ? 7.101   -17.867 -7.359  1.00 37.82  ? 160 THR A CB  1 
ATOM   1034 O OG1 . THR A 1 131 ? 5.807   -18.184 -6.879  1.00 39.56  ? 160 THR A OG1 1 
ATOM   1035 C CG2 . THR A 1 131 ? 7.941   -19.124 -7.523  1.00 41.36  ? 160 THR A CG2 1 
ATOM   1036 N N   . ASN A 1 132 ? 6.138   -15.451 -4.996  1.00 31.86  ? 161 ASN A N   1 
ATOM   1037 C CA  . ASN A 1 132 ? 5.306   -14.280 -4.771  1.00 34.96  ? 161 ASN A CA  1 
ATOM   1038 C C   . ASN A 1 132 ? 6.091   -13.183 -4.043  1.00 36.36  ? 161 ASN A C   1 
ATOM   1039 O O   . ASN A 1 132 ? 5.491   -12.214 -3.594  1.00 38.48  ? 161 ASN A O   1 
ATOM   1040 C CB  . ASN A 1 132 ? 4.066   -14.657 -3.965  1.00 38.49  ? 161 ASN A CB  1 
ATOM   1041 C CG  . ASN A 1 132 ? 4.423   -15.074 -2.561  1.00 38.74  ? 161 ASN A CG  1 
ATOM   1042 O OD1 . ASN A 1 132 ? 5.455   -15.719 -2.349  1.00 40.65  ? 161 ASN A OD1 1 
ATOM   1043 N ND2 . ASN A 1 132 ? 3.621   -14.685 -1.586  1.00 40.29  ? 161 ASN A ND2 1 
ATOM   1044 N N   . LEU A 1 133 ? 7.413   -13.360 -3.844  1.00 30.03  ? 162 LEU A N   1 
ATOM   1045 C CA  . LEU A 1 133 ? 8.219   -12.254 -3.337  1.00 27.88  ? 162 LEU A CA  1 
ATOM   1046 C C   . LEU A 1 133 ? 8.812   -11.516 -4.537  1.00 25.53  ? 162 LEU A C   1 
ATOM   1047 O O   . LEU A 1 133 ? 9.550   -12.069 -5.337  1.00 25.96  ? 162 LEU A O   1 
ATOM   1048 C CB  . LEU A 1 133 ? 9.268   -12.775 -2.370  1.00 26.34  ? 162 LEU A CB  1 
ATOM   1049 C CG  . LEU A 1 133 ? 10.190  -11.757 -1.714  1.00 27.79  ? 162 LEU A CG  1 
ATOM   1050 C CD1 . LEU A 1 133 ? 9.453   -10.800 -0.851  1.00 25.24  ? 162 LEU A CD1 1 
ATOM   1051 C CD2 . LEU A 1 133 ? 11.270  -12.471 -0.902  1.00 27.38  ? 162 LEU A CD2 1 
ATOM   1052 N N   . HIS A 1 134 ? 8.489   -10.238 -4.627  1.00 26.10  ? 163 HIS A N   1 
ATOM   1053 C CA  . HIS A 1 134 ? 8.829   -9.402  -5.761  1.00 27.25  ? 163 HIS A CA  1 
ATOM   1054 C C   . HIS A 1 134 ? 10.345  -9.395  -5.987  1.00 24.04  ? 163 HIS A C   1 
ATOM   1055 O O   . HIS A 1 134 ? 11.114  -9.449  -5.030  1.00 22.25  ? 163 HIS A O   1 
ATOM   1056 C CB  . HIS A 1 134 ? 8.272   -8.009  -5.445  1.00 28.61  ? 163 HIS A CB  1 
ATOM   1057 C CG  . HIS A 1 134 ? 8.336   -7.025  -6.551  1.00 32.49  ? 163 HIS A CG  1 
ATOM   1058 N ND1 . HIS A 1 134 ? 9.528   -6.479  -7.008  1.00 33.58  ? 163 HIS A ND1 1 
ATOM   1059 C CD2 . HIS A 1 134 ? 7.349   -6.503  -7.328  1.00 37.97  ? 163 HIS A CD2 1 
ATOM   1060 C CE1 . HIS A 1 134 ? 9.280   -5.654  -8.011  1.00 33.41  ? 163 HIS A CE1 1 
ATOM   1061 N NE2 . HIS A 1 134 ? 7.955   -5.624  -8.204  1.00 36.03  ? 163 HIS A NE2 1 
ATOM   1062 N N   . PRO A 1 135 ? 10.822  -9.352  -7.256  1.00 23.62  ? 164 PRO A N   1 
ATOM   1063 C CA  . PRO A 1 135 ? 12.252  -9.328  -7.555  1.00 22.93  ? 164 PRO A CA  1 
ATOM   1064 C C   . PRO A 1 135 ? 13.028  -8.254  -6.785  1.00 22.43  ? 164 PRO A C   1 
ATOM   1065 O O   . PRO A 1 135 ? 14.142  -8.504  -6.371  1.00 21.03  ? 164 PRO A O   1 
ATOM   1066 C CB  . PRO A 1 135 ? 12.266  -8.987  -9.058  1.00 24.32  ? 164 PRO A CB  1 
ATOM   1067 C CG  . PRO A 1 135 ? 10.954  -9.445  -9.584  1.00 25.52  ? 164 PRO A CG  1 
ATOM   1068 C CD  . PRO A 1 135 ? 9.982   -9.330  -8.480  1.00 25.78  ? 164 PRO A CD  1 
ATOM   1069 N N   . MET A 1 136 ? 12.466  -7.028  -6.693  1.00 22.12  ? 165 MET A N   1 
ATOM   1070 C CA  . MET A 1 136 ? 13.129  -5.929  -6.007  1.00 23.86  ? 165 MET A CA  1 
ATOM   1071 C C   . MET A 1 136 ? 13.305  -6.223  -4.509  1.00 19.37  ? 165 MET A C   1 
ATOM   1072 O O   . MET A 1 136 ? 14.337  -5.852  -3.950  1.00 20.71  ? 165 MET A O   1 
ATOM   1073 C CB  . MET A 1 136 ? 12.383  -4.609  -6.204  1.00 21.46  ? 165 MET A CB  1 
ATOM   1074 C CG  . MET A 1 136 ? 12.641  -4.005  -7.573  1.00 22.09  ? 165 MET A CG  1 
ATOM   1075 S SD  . MET A 1 136 ? 14.358  -3.525  -7.868  1.00 23.85  ? 165 MET A SD  1 
ATOM   1076 C CE  . MET A 1 136 ? 14.494  -2.203  -6.665  1.00 23.81  ? 165 MET A CE  1 
ATOM   1077 N N   . SER A 1 137 ? 12.342  -6.902  -3.894  1.00 17.10  ? 166 SER A N   1 
ATOM   1078 C CA  . SER A 1 137 ? 12.483  -7.332  -2.506  1.00 20.17  ? 166 SER A CA  1 
ATOM   1079 C C   . SER A 1 137 ? 13.568  -8.385  -2.355  1.00 20.31  ? 166 SER A C   1 
ATOM   1080 O O   . SER A 1 137 ? 14.338  -8.380  -1.370  1.00 20.25  ? 166 SER A O   1 
ATOM   1081 C CB  . SER A 1 137 ? 11.190  -7.840  -1.925  1.00 20.13  ? 166 SER A CB  1 
ATOM   1082 O OG  . SER A 1 137 ? 10.124  -6.918  -2.060  1.00 24.61  ? 166 SER A OG  1 
ATOM   1083 N N   . GLN A 1 138 ? 13.617  -9.330  -3.323  1.00 20.10  ? 167 GLN A N   1 
ATOM   1084 C CA  . GLN A 1 138 ? 14.665  -10.328 -3.301  1.00 19.65  ? 167 GLN A CA  1 
ATOM   1085 C C   . GLN A 1 138 ? 16.022  -9.642  -3.397  1.00 19.60  ? 167 GLN A C   1 
ATOM   1086 O O   . GLN A 1 138 ? 16.954  -10.003 -2.696  1.00 19.01  ? 167 GLN A O   1 
ATOM   1087 C CB  . GLN A 1 138 ? 14.496  -11.356 -4.417  1.00 19.95  ? 167 GLN A CB  1 
ATOM   1088 C CG  . GLN A 1 138 ? 13.171  -12.100 -4.313  1.00 23.08  ? 167 GLN A CG  1 
ATOM   1089 C CD  . GLN A 1 138 ? 13.168  -13.326 -5.186  1.00 25.87  ? 167 GLN A CD  1 
ATOM   1090 O OE1 . GLN A 1 138 ? 14.245  -13.828 -5.539  1.00 23.38  ? 167 GLN A OE1 1 
ATOM   1091 N NE2 . GLN A 1 138 ? 11.970  -13.846 -5.459  1.00 27.05  ? 167 GLN A NE2 1 
ATOM   1092 N N   . LEU A 1 139 ? 16.105  -8.639  -4.259  1.00 20.60  ? 168 LEU A N   1 
ATOM   1093 C CA  . LEU A 1 139 ? 17.373  -7.983  -4.550  1.00 21.02  ? 168 LEU A CA  1 
ATOM   1094 C C   . LEU A 1 139 ? 17.882  -7.270  -3.297  1.00 21.11  ? 168 LEU A C   1 
ATOM   1095 O O   . LEU A 1 139 ? 19.030  -7.468  -2.921  1.00 19.70  ? 168 LEU A O   1 
ATOM   1096 C CB  . LEU A 1 139 ? 17.220  -7.003  -5.701  1.00 21.45  ? 168 LEU A CB  1 
ATOM   1097 C CG  . LEU A 1 139 ? 18.417  -6.083  -5.943  1.00 21.85  ? 168 LEU A CG  1 
ATOM   1098 C CD1 . LEU A 1 139 ? 19.653  -6.823  -6.383  1.00 23.15  ? 168 LEU A CD1 1 
ATOM   1099 C CD2 . LEU A 1 139 ? 18.037  -4.991  -6.895  1.00 24.10  ? 168 LEU A CD2 1 
ATOM   1100 N N   . SER A 1 140 ? 16.985  -6.550  -2.621  1.00 20.24  ? 169 SER A N   1 
ATOM   1101 C CA  . SER A 1 140 ? 17.304  -5.778  -1.437  1.00 20.10  ? 169 SER A CA  1 
ATOM   1102 C C   . SER A 1 140 ? 17.695  -6.688  -0.272  1.00 18.59  ? 169 SER A C   1 
ATOM   1103 O O   . SER A 1 140 ? 18.722  -6.485  0.396   1.00 18.63  ? 169 SER A O   1 
ATOM   1104 C CB  . SER A 1 140 ? 16.165  -4.843  -1.030  1.00 21.40  ? 169 SER A CB  1 
ATOM   1105 O OG  . SER A 1 140 ? 16.551  -4.162  0.167   1.00 25.55  ? 169 SER A OG  1 
ATOM   1106 N N   . ALA A 1 141 ? 16.889  -7.724  -0.036  1.00 19.34  ? 170 ALA A N   1 
ATOM   1107 C CA  . ALA A 1 141 ? 17.183  -8.692  1.012   1.00 19.68  ? 170 ALA A CA  1 
ATOM   1108 C C   . ALA A 1 141 ? 18.535  -9.377  0.804   1.00 20.66  ? 170 ALA A C   1 
ATOM   1109 O O   . ALA A 1 141 ? 19.279  -9.549  1.765   1.00 18.75  ? 170 ALA A O   1 
ATOM   1110 C CB  . ALA A 1 141 ? 16.069  -9.682  1.148   1.00 18.90  ? 170 ALA A CB  1 
ATOM   1111 N N   . ALA A 1 142 ? 18.840  -9.768  -0.438  1.00 19.00  ? 171 ALA A N   1 
ATOM   1112 C CA  . ALA A 1 142 ? 20.079  -10.423 -0.783  1.00 21.34  ? 171 ALA A CA  1 
ATOM   1113 C C   . ALA A 1 142 ? 21.271  -9.509  -0.544  1.00 22.86  ? 171 ALA A C   1 
ATOM   1114 O O   . ALA A 1 142 ? 22.303  -9.945  -0.025  1.00 21.77  ? 171 ALA A O   1 
ATOM   1115 C CB  . ALA A 1 142 ? 20.022  -10.890 -2.229  1.00 24.36  ? 171 ALA A CB  1 
ATOM   1116 N N   . VAL A 1 143 ? 21.125  -8.227  -0.923  1.00 21.08  ? 172 VAL A N   1 
ATOM   1117 C CA  . VAL A 1 143 ? 22.209  -7.293  -0.811  1.00 20.22  ? 172 VAL A CA  1 
ATOM   1118 C C   . VAL A 1 143 ? 22.450  -7.036  0.671   1.00 18.77  ? 172 VAL A C   1 
ATOM   1119 O O   . VAL A 1 143 ? 23.594  -6.988  1.107   1.00 21.22  ? 172 VAL A O   1 
ATOM   1120 C CB  . VAL A 1 143 ? 21.980  -5.999  -1.603  1.00 22.22  ? 172 VAL A CB  1 
ATOM   1121 C CG1 . VAL A 1 143 ? 23.031  -4.933  -1.292  1.00 22.33  ? 172 VAL A CG1 1 
ATOM   1122 C CG2 . VAL A 1 143 ? 21.996  -6.309  -3.094  1.00 23.10  ? 172 VAL A CG2 1 
ATOM   1123 N N   . THR A 1 144 ? 21.380  -6.877  1.445   1.00 19.91  ? 173 THR A N   1 
ATOM   1124 C CA  . THR A 1 144 ? 21.497  -6.740  2.902   1.00 19.46  ? 173 THR A CA  1 
ATOM   1125 C C   . THR A 1 144 ? 22.272  -7.913  3.494   1.00 19.90  ? 173 THR A C   1 
ATOM   1126 O O   . THR A 1 144 ? 23.250  -7.695  4.208   1.00 19.37  ? 173 THR A O   1 
ATOM   1127 C CB  . THR A 1 144 ? 20.119  -6.588  3.551   1.00 21.12  ? 173 THR A CB  1 
ATOM   1128 O OG1 . THR A 1 144 ? 19.568  -5.340  3.120   1.00 20.96  ? 173 THR A OG1 1 
ATOM   1129 C CG2 . THR A 1 144 ? 20.264  -6.505  5.059   1.00 18.41  ? 173 THR A CG2 1 
ATOM   1130 N N   . ALA A 1 145 ? 21.914  -9.151  3.107   1.00 18.74  ? 174 ALA A N   1 
ATOM   1131 C CA  . ALA A 1 145 ? 22.604  -10.353 3.572   1.00 21.96  ? 174 ALA A CA  1 
ATOM   1132 C C   . ALA A 1 145 ? 24.077  -10.434 3.155   1.00 21.77  ? 174 ALA A C   1 
ATOM   1133 O O   . ALA A 1 145 ? 24.886  -11.106 3.804   1.00 24.48  ? 174 ALA A O   1 
ATOM   1134 C CB  . ALA A 1 145 ? 21.862  -11.592 3.090   1.00 21.85  ? 174 ALA A CB  1 
ATOM   1135 N N   . LEU A 1 146 ? 24.440  -9.836  2.031   1.00 19.21  ? 175 LEU A N   1 
ATOM   1136 C CA  . LEU A 1 146 ? 25.829  -9.813  1.616   1.00 19.62  ? 175 LEU A CA  1 
ATOM   1137 C C   . LEU A 1 146 ? 26.694  -8.986  2.563   1.00 21.69  ? 175 LEU A C   1 
ATOM   1138 O O   . LEU A 1 146 ? 27.919  -8.997  2.471   1.00 23.24  ? 175 LEU A O   1 
ATOM   1139 C CB  . LEU A 1 146 ? 25.903  -9.269  0.189   1.00 20.05  ? 175 LEU A CB  1 
ATOM   1140 C CG  . LEU A 1 146 ? 25.622  -10.270 -0.927  1.00 20.30  ? 175 LEU A CG  1 
ATOM   1141 C CD1 . LEU A 1 146 ? 25.400  -9.574  -2.258  1.00 22.73  ? 175 LEU A CD1 1 
ATOM   1142 C CD2 . LEU A 1 146 ? 26.798  -11.211 -1.012  1.00 21.52  ? 175 LEU A CD2 1 
ATOM   1143 N N   . ASN A 1 147 ? 26.084  -8.244  3.496   1.00 21.94  ? 176 ASN A N   1 
ATOM   1144 C CA  . ASN A 1 147 ? 26.887  -7.337  4.295   1.00 23.20  ? 176 ASN A CA  1 
ATOM   1145 C C   . ASN A 1 147 ? 27.754  -8.088  5.318   1.00 22.70  ? 176 ASN A C   1 
ATOM   1146 O O   . ASN A 1 147 ? 28.643  -7.502  5.912   1.00 19.17  ? 176 ASN A O   1 
ATOM   1147 C CB  . ASN A 1 147 ? 26.064  -6.224  4.933   1.00 23.61  ? 176 ASN A CB  1 
ATOM   1148 C CG  . ASN A 1 147 ? 26.029  -6.341  6.421   1.00 27.39  ? 176 ASN A CG  1 
ATOM   1149 O OD1 . ASN A 1 147 ? 25.621  -7.392  6.914   1.00 31.03  ? 176 ASN A OD1 1 
ATOM   1150 N ND2 . ASN A 1 147 ? 26.431  -5.279  7.123   1.00 24.39  ? 176 ASN A ND2 1 
ATOM   1151 N N   . SER A 1 148 ? 27.531  -9.400  5.456   1.00 23.79  ? 177 SER A N   1 
ATOM   1152 C CA  . SER A 1 148 ? 28.429  -10.333 6.093   1.00 21.96  ? 177 SER A CA  1 
ATOM   1153 C C   . SER A 1 148 ? 29.808  -10.251 5.456   1.00 23.99  ? 177 SER A C   1 
ATOM   1154 O O   . SER A 1 148 ? 30.787  -10.545 6.114   1.00 26.82  ? 177 SER A O   1 
ATOM   1155 C CB  . SER A 1 148 ? 27.839  -11.737 5.970   1.00 22.47  ? 177 SER A CB  1 
ATOM   1156 O OG  . SER A 1 148 ? 27.827  -12.186 4.622   1.00 26.08  ? 177 SER A OG  1 
ATOM   1157 N N   . GLU A 1 149 ? 29.894  -9.835  4.185   1.00 23.65  ? 178 GLU A N   1 
ATOM   1158 C CA  . GLU A 1 149 ? 31.195  -9.718  3.523   1.00 26.89  ? 178 GLU A CA  1 
ATOM   1159 C C   . GLU A 1 149 ? 31.823  -8.325  3.626   1.00 23.78  ? 178 GLU A C   1 
ATOM   1160 O O   . GLU A 1 149 ? 32.839  -8.083  2.984   1.00 26.15  ? 178 GLU A O   1 
ATOM   1161 C CB  . GLU A 1 149 ? 31.013  -10.024 2.035   1.00 33.16  ? 178 GLU A CB  1 
ATOM   1162 C CG  . GLU A 1 149 ? 30.158  -11.270 1.801   1.00 39.01  ? 178 GLU A CG  1 
ATOM   1163 C CD  . GLU A 1 149 ? 30.742  -12.550 2.384   1.00 48.58  ? 178 GLU A CD  1 
ATOM   1164 O OE1 . GLU A 1 149 ? 31.685  -13.012 1.691   1.00 51.27  ? 178 GLU A OE1 1 
ATOM   1165 O OE2 . GLU A 1 149 ? 30.257  -13.105 3.439   1.00 48.16  ? 178 GLU A OE2 1 
ATOM   1166 N N   . SER A 1 150 ? 31.245  -7.404  4.406   1.00 24.22  ? 179 SER A N   1 
ATOM   1167 C CA  . SER A 1 150 ? 31.682  -6.014  4.422   1.00 22.70  ? 179 SER A CA  1 
ATOM   1168 C C   . SER A 1 150 ? 33.032  -5.886  5.120   1.00 25.78  ? 179 SER A C   1 
ATOM   1169 O O   . SER A 1 150 ? 33.119  -6.167  6.311   1.00 25.04  ? 179 SER A O   1 
ATOM   1170 C CB  . SER A 1 150 ? 30.733  -5.062  5.073   1.00 20.57  ? 179 SER A CB  1 
ATOM   1171 O OG  . SER A 1 150 ? 31.275  -3.750  5.001   1.00 20.45  ? 179 SER A OG  1 
ATOM   1172 N N   . ASN A 1 151 ? 34.028  -5.413  4.363   1.00 25.34  ? 180 ASN A N   1 
ATOM   1173 C CA  . ASN A 1 151 ? 35.341  -5.041  4.870   1.00 29.29  ? 180 ASN A CA  1 
ATOM   1174 C C   . ASN A 1 151 ? 35.212  -3.785  5.725   1.00 28.72  ? 180 ASN A C   1 
ATOM   1175 O O   . ASN A 1 151 ? 35.880  -3.634  6.749   1.00 26.05  ? 180 ASN A O   1 
ATOM   1176 C CB  . ASN A 1 151 ? 36.350  -4.772  3.745   1.00 34.83  ? 180 ASN A CB  1 
ATOM   1177 C CG  . ASN A 1 151 ? 36.424  -5.881  2.714   1.00 40.62  ? 180 ASN A CG  1 
ATOM   1178 O OD1 . ASN A 1 151 ? 36.148  -5.662  1.513   1.00 49.87  ? 180 ASN A OD1 1 
ATOM   1179 N ND2 . ASN A 1 151 ? 36.759  -7.078  3.162   1.00 36.81  ? 180 ASN A ND2 1 
ATOM   1180 N N   . PHE A 1 152 ? 34.340  -2.870  5.278   1.00 25.61  ? 181 PHE A N   1 
ATOM   1181 C CA  . PHE A 1 152 ? 34.186  -1.577  5.935   1.00 23.93  ? 181 PHE A CA  1 
ATOM   1182 C C   . PHE A 1 152 ? 33.619  -1.797  7.337   1.00 24.29  ? 181 PHE A C   1 
ATOM   1183 O O   . PHE A 1 152 ? 34.125  -1.257  8.298   1.00 20.98  ? 181 PHE A O   1 
ATOM   1184 C CB  . PHE A 1 152 ? 33.295  -0.605  5.190   1.00 23.11  ? 181 PHE A CB  1 
ATOM   1185 C CG  . PHE A 1 152 ? 33.196  0.718   5.939   1.00 22.65  ? 181 PHE A CG  1 
ATOM   1186 C CD1 . PHE A 1 152 ? 34.218  1.645   5.895   1.00 26.38  ? 181 PHE A CD1 1 
ATOM   1187 C CD2 . PHE A 1 152 ? 32.093  1.011   6.717   1.00 26.06  ? 181 PHE A CD2 1 
ATOM   1188 C CE1 . PHE A 1 152 ? 34.118  2.863   6.546   1.00 24.70  ? 181 PHE A CE1 1 
ATOM   1189 C CE2 . PHE A 1 152 ? 32.008  2.216   7.379   1.00 29.35  ? 181 PHE A CE2 1 
ATOM   1190 C CZ  . PHE A 1 152 ? 33.031  3.127   7.310   1.00 27.61  ? 181 PHE A CZ  1 
ATOM   1191 N N   . ALA A 1 153 ? 32.589  -2.621  7.449   1.00 25.14  ? 182 ALA A N   1 
ATOM   1192 C CA  . ALA A 1 153 ? 31.958  -2.817  8.740   1.00 26.61  ? 182 ALA A CA  1 
ATOM   1193 C C   . ALA A 1 153 ? 32.985  -3.346  9.754   1.00 29.87  ? 182 ALA A C   1 
ATOM   1194 O O   . ALA A 1 153 ? 33.025  -2.905  10.893  1.00 27.67  ? 182 ALA A O   1 
ATOM   1195 C CB  . ALA A 1 153 ? 30.763  -3.737  8.550   1.00 25.18  ? 182 ALA A CB  1 
ATOM   1196 N N   . ARG A 1 154 ? 33.823  -4.295  9.338   1.00 31.70  ? 183 ARG A N   1 
ATOM   1197 C CA  . ARG A 1 154 ? 34.784  -4.924  10.231  1.00 34.73  ? 183 ARG A CA  1 
ATOM   1198 C C   . ARG A 1 154 ? 35.896  -3.934  10.568  1.00 32.05  ? 183 ARG A C   1 
ATOM   1199 O O   . ARG A 1 154 ? 36.278  -3.805  11.729  1.00 30.40  ? 183 ARG A O   1 
ATOM   1200 C CB  . ARG A 1 154 ? 35.328  -6.203  9.576   1.00 43.62  ? 183 ARG A CB  1 
ATOM   1201 C CG  . ARG A 1 154 ? 34.309  -7.339  9.592   1.00 55.27  ? 183 ARG A CG  1 
ATOM   1202 C CD  . ARG A 1 154 ? 34.891  -8.747  9.392   1.00 63.74  ? 183 ARG A CD  1 
ATOM   1203 N NE  . ARG A 1 154 ? 35.221  -9.081  7.999   1.00 71.18  ? 183 ARG A NE  1 
ATOM   1204 C CZ  . ARG A 1 154 ? 34.326  -9.358  7.043   1.00 86.08  ? 183 ARG A CZ  1 
ATOM   1205 N NH1 . ARG A 1 154 ? 34.717  -9.660  5.813   1.00 79.06  ? 183 ARG A NH1 1 
ATOM   1206 N NH2 . ARG A 1 154 ? 33.032  -9.329  7.315   1.00 92.83  ? 183 ARG A NH2 1 
ATOM   1207 N N   . ALA A 1 155 ? 36.377  -3.164  9.580   1.00 28.93  ? 184 ALA A N   1 
ATOM   1208 C CA  . ALA A 1 155 ? 37.441  -2.195  9.860   1.00 27.12  ? 184 ALA A CA  1 
ATOM   1209 C C   . ALA A 1 155 ? 36.942  -1.140  10.844  1.00 29.41  ? 184 ALA A C   1 
ATOM   1210 O O   . ALA A 1 155 ? 37.680  -0.663  11.726  1.00 28.86  ? 184 ALA A O   1 
ATOM   1211 C CB  . ALA A 1 155 ? 37.928  -1.549  8.588   1.00 25.36  ? 184 ALA A CB  1 
ATOM   1212 N N   . TYR A 1 156 ? 35.669  -0.741  10.689  1.00 27.67  ? 185 TYR A N   1 
ATOM   1213 C CA  . TYR A 1 156 ? 35.171  0.344   11.512  1.00 28.74  ? 185 TYR A CA  1 
ATOM   1214 C C   . TYR A 1 156 ? 35.179  -0.105  12.972  1.00 29.83  ? 185 TYR A C   1 
ATOM   1215 O O   . TYR A 1 156 ? 35.582  0.617   13.880  1.00 30.35  ? 185 TYR A O   1 
ATOM   1216 C CB  . TYR A 1 156 ? 33.779  0.835   11.068  1.00 26.74  ? 185 TYR A CB  1 
ATOM   1217 C CG  . TYR A 1 156 ? 33.328  2.031   11.883  1.00 26.94  ? 185 TYR A CG  1 
ATOM   1218 C CD1 . TYR A 1 156 ? 32.685  1.858   13.108  1.00 28.83  ? 185 TYR A CD1 1 
ATOM   1219 C CD2 . TYR A 1 156 ? 33.570  3.334   11.449  1.00 32.29  ? 185 TYR A CD2 1 
ATOM   1220 C CE1 . TYR A 1 156 ? 32.320  2.944   13.883  1.00 29.61  ? 185 TYR A CE1 1 
ATOM   1221 C CE2 . TYR A 1 156 ? 33.199  4.420   12.218  1.00 29.66  ? 185 TYR A CE2 1 
ATOM   1222 C CZ  . TYR A 1 156 ? 32.570  4.217   13.428  1.00 29.54  ? 185 TYR A CZ  1 
ATOM   1223 O OH  . TYR A 1 156 ? 32.158  5.268   14.195  1.00 40.04  ? 185 TYR A OH  1 
ATOM   1224 N N   . ALA A 1 157 ? 34.706  -1.318  13.196  1.00 32.83  ? 186 ALA A N   1 
ATOM   1225 C CA  . ALA A 1 157 ? 34.626  -1.863  14.535  1.00 35.76  ? 186 ALA A CA  1 
ATOM   1226 C C   . ALA A 1 157 ? 36.024  -1.989  15.162  1.00 39.85  ? 186 ALA A C   1 
ATOM   1227 O O   . ALA A 1 157 ? 36.157  -1.947  16.377  1.00 37.12  ? 186 ALA A O   1 
ATOM   1228 C CB  . ALA A 1 157 ? 33.908  -3.199  14.474  1.00 37.73  ? 186 ALA A CB  1 
ATOM   1229 N N   . GLN A 1 158 ? 37.074  -2.163  14.348  1.00 36.56  ? 187 GLN A N   1 
ATOM   1230 C CA  . GLN A 1 158 ? 38.437  -2.202  14.859  1.00 37.84  ? 187 GLN A CA  1 
ATOM   1231 C C   . GLN A 1 158 ? 39.078  -0.821  15.048  1.00 38.20  ? 187 GLN A C   1 
ATOM   1232 O O   . GLN A 1 158 ? 40.234  -0.750  15.455  1.00 39.49  ? 187 GLN A O   1 
ATOM   1233 C CB  . GLN A 1 158 ? 39.335  -2.968  13.894  1.00 42.08  ? 187 GLN A CB  1 
ATOM   1234 C CG  . GLN A 1 158 ? 38.993  -4.448  13.772  1.00 39.71  ? 187 GLN A CG  1 
ATOM   1235 C CD  . GLN A 1 158 ? 39.761  -5.116  12.655  1.00 45.82  ? 187 GLN A CD  1 
ATOM   1236 O OE1 . GLN A 1 158 ? 39.888  -4.596  11.539  1.00 55.35  ? 187 GLN A OE1 1 
ATOM   1237 N NE2 . GLN A 1 158 ? 40.292  -6.290  12.940  1.00 52.41  ? 187 GLN A NE2 1 
ATOM   1238 N N   . GLY A 1 159 ? 38.409  0.277   14.682  1.00 31.86  ? 188 GLY A N   1 
ATOM   1239 C CA  . GLY A 1 159 ? 38.890  1.618   14.999  1.00 31.69  ? 188 GLY A CA  1 
ATOM   1240 C C   . GLY A 1 159 ? 39.790  2.237   13.919  1.00 34.23  ? 188 GLY A C   1 
ATOM   1241 O O   . GLY A 1 159 ? 40.649  3.092   14.205  1.00 39.64  ? 188 GLY A O   1 
ATOM   1242 N N   . ILE A 1 160 ? 39.541  1.899   12.661  1.00 26.46  ? 189 ILE A N   1 
ATOM   1243 C CA  . ILE A 1 160 ? 40.309  2.482   11.573  1.00 29.79  ? 189 ILE A CA  1 
ATOM   1244 C C   . ILE A 1 160 ? 40.217  4.018   11.536  1.00 28.27  ? 189 ILE A C   1 
ATOM   1245 O O   . ILE A 1 160 ? 39.184  4.614   11.848  1.00 29.79  ? 189 ILE A O   1 
ATOM   1246 C CB  . ILE A 1 160 ? 39.864  1.816   10.264  1.00 30.82  ? 189 ILE A CB  1 
ATOM   1247 C CG1 . ILE A 1 160 ? 40.882  2.022   9.141   1.00 38.64  ? 189 ILE A CG1 1 
ATOM   1248 C CG2 . ILE A 1 160 ? 38.448  2.240   9.868   1.00 30.98  ? 189 ILE A CG2 1 
ATOM   1249 C CD1 . ILE A 1 160 ? 41.625  0.762   8.742   1.00 41.51  ? 189 ILE A CD1 1 
ATOM   1250 N N   . SER A 1 161 ? 41.313  4.676   11.102  1.00 26.59  ? 190 SER A N   1 
ATOM   1251 C CA  . SER A 1 161 ? 41.319  6.114   10.913  1.00 24.93  ? 190 SER A CA  1 
ATOM   1252 C C   . SER A 1 161 ? 40.270  6.536   9.881   1.00 24.40  ? 190 SER A C   1 
ATOM   1253 O O   . SER A 1 161 ? 40.175  5.938   8.814   1.00 23.36  ? 190 SER A O   1 
ATOM   1254 C CB  . SER A 1 161 ? 42.676  6.601   10.482  1.00 25.63  ? 190 SER A CB  1 
ATOM   1255 O OG  . SER A 1 161 ? 42.646  7.950   9.989   1.00 23.73  ? 190 SER A OG  1 
ATOM   1256 N N   . ARG A 1 162 ? 39.606  7.656   10.141  1.00 26.16  ? 191 ARG A N   1 
ATOM   1257 C CA  . ARG A 1 162 ? 38.656  8.245   9.198   1.00 31.47  ? 191 ARG A CA  1 
ATOM   1258 C C   . ARG A 1 162 ? 39.322  8.533   7.843   1.00 30.31  ? 191 ARG A C   1 
ATOM   1259 O O   . ARG A 1 162 ? 38.636  8.551   6.828   1.00 26.60  ? 191 ARG A O   1 
ATOM   1260 C CB  . ARG A 1 162 ? 38.183  9.616   9.687   1.00 36.72  ? 191 ARG A CB  1 
ATOM   1261 C CG  . ARG A 1 162 ? 37.324  9.718   10.933  1.00 51.79  ? 191 ARG A CG  1 
ATOM   1262 C CD  . ARG A 1 162 ? 37.448  11.135  11.489  1.00 58.93  ? 191 ARG A CD  1 
ATOM   1263 N NE  . ARG A 1 162 ? 36.257  11.593  12.206  1.00 70.97  ? 191 ARG A NE  1 
ATOM   1264 C CZ  . ARG A 1 162 ? 36.191  12.702  12.940  1.00 86.06  ? 191 ARG A CZ  1 
ATOM   1265 N NH1 . ARG A 1 162 ? 37.287  13.405  13.184  1.00 91.99  ? 191 ARG A NH1 1 
ATOM   1266 N NH2 . ARG A 1 162 ? 35.032  13.096  13.447  1.00 86.62  ? 191 ARG A NH2 1 
ATOM   1267 N N   . THR A 1 163 ? 40.647  8.805   7.843   1.00 27.45  ? 192 THR A N   1 
ATOM   1268 C CA  . THR A 1 163 ? 41.378  9.089   6.618   1.00 26.74  ? 192 THR A CA  1 
ATOM   1269 C C   . THR A 1 163 ? 41.310  7.888   5.678   1.00 26.71  ? 192 THR A C   1 
ATOM   1270 O O   . THR A 1 163 ? 41.628  7.996   4.492   1.00 27.29  ? 192 THR A O   1 
ATOM   1271 C CB  . THR A 1 163 ? 42.851  9.437   6.883   1.00 26.00  ? 192 THR A CB  1 
ATOM   1272 O OG1 . THR A 1 163 ? 43.492  8.282   7.395   1.00 22.96  ? 192 THR A OG1 1 
ATOM   1273 C CG2 . THR A 1 163 ? 42.994  10.621  7.810   1.00 28.89  ? 192 THR A CG2 1 
ATOM   1274 N N   . LYS A 1 164 ? 40.953  6.734   6.216   1.00 22.48  ? 193 LYS A N   1 
ATOM   1275 C CA  . LYS A 1 164 ? 40.994  5.512   5.435   1.00 26.75  ? 193 LYS A CA  1 
ATOM   1276 C C   . LYS A 1 164 ? 39.605  4.981   5.080   1.00 21.08  ? 193 LYS A C   1 
ATOM   1277 O O   . LYS A 1 164 ? 39.506  4.016   4.346   1.00 22.99  ? 193 LYS A O   1 
ATOM   1278 C CB  . LYS A 1 164 ? 41.752  4.451   6.236   1.00 34.55  ? 193 LYS A CB  1 
ATOM   1279 C CG  . LYS A 1 164 ? 43.210  4.851   6.435   1.00 43.57  ? 193 LYS A CG  1 
ATOM   1280 C CD  . LYS A 1 164 ? 44.194  4.063   5.588   1.00 54.22  ? 193 LYS A CD  1 
ATOM   1281 C CE  . LYS A 1 164 ? 44.229  2.607   5.974   1.00 57.93  ? 193 LYS A CE  1 
ATOM   1282 N NZ  . LYS A 1 164 ? 45.309  1.966   5.221   1.00 66.14  ? 193 LYS A NZ  1 
ATOM   1283 N N   . TYR A 1 165 ? 38.549  5.613   5.570   1.00 19.15  ? 194 TYR A N   1 
ATOM   1284 C CA  . TYR A 1 165 ? 37.206  5.140   5.286   1.00 21.68  ? 194 TYR A CA  1 
ATOM   1285 C C   . TYR A 1 165 ? 36.989  4.907   3.797   1.00 20.11  ? 194 TYR A C   1 
ATOM   1286 O O   . TYR A 1 165 ? 36.462  3.870   3.407   1.00 24.74  ? 194 TYR A O   1 
ATOM   1287 C CB  . TYR A 1 165 ? 36.152  6.120   5.797   1.00 22.06  ? 194 TYR A CB  1 
ATOM   1288 C CG  . TYR A 1 165 ? 35.954  6.227   7.290   1.00 21.05  ? 194 TYR A CG  1 
ATOM   1289 C CD1 . TYR A 1 165 ? 36.569  5.365   8.178   1.00 25.75  ? 194 TYR A CD1 1 
ATOM   1290 C CD2 . TYR A 1 165 ? 35.126  7.213   7.804   1.00 25.53  ? 194 TYR A CD2 1 
ATOM   1291 C CE1 . TYR A 1 165 ? 36.367  5.464   9.537   1.00 24.83  ? 194 TYR A CE1 1 
ATOM   1292 C CE2 . TYR A 1 165 ? 34.957  7.352   9.169   1.00 25.80  ? 194 TYR A CE2 1 
ATOM   1293 C CZ  . TYR A 1 165 ? 35.566  6.469   10.026  1.00 27.35  ? 194 TYR A CZ  1 
ATOM   1294 O OH  . TYR A 1 165 ? 35.392  6.616   11.362  1.00 31.31  ? 194 TYR A OH  1 
ATOM   1295 N N   . TRP A 1 166 ? 37.424  5.815   2.940   1.00 17.97  ? 195 TRP A N   1 
ATOM   1296 C CA  . TRP A 1 166 ? 37.128  5.699   1.516   1.00 18.82  ? 195 TRP A CA  1 
ATOM   1297 C C   . TRP A 1 166 ? 37.688  4.429   0.899   1.00 21.13  ? 195 TRP A C   1 
ATOM   1298 O O   . TRP A 1 166 ? 37.105  3.926   -0.070  1.00 19.99  ? 195 TRP A O   1 
ATOM   1299 C CB  . TRP A 1 166 ? 37.574  6.938   0.732   1.00 18.67  ? 195 TRP A CB  1 
ATOM   1300 C CG  . TRP A 1 166 ? 39.066  7.053   0.520   1.00 21.22  ? 195 TRP A CG  1 
ATOM   1301 C CD1 . TRP A 1 166 ? 39.975  7.754   1.257   1.00 24.16  ? 195 TRP A CD1 1 
ATOM   1302 C CD2 . TRP A 1 166 ? 39.814  6.440   -0.564  1.00 22.93  ? 195 TRP A CD2 1 
ATOM   1303 N NE1 . TRP A 1 166 ? 41.240  7.564   0.760   1.00 23.93  ? 195 TRP A NE1 1 
ATOM   1304 C CE2 . TRP A 1 166 ? 41.174  6.786   -0.366  1.00 22.86  ? 195 TRP A CE2 1 
ATOM   1305 C CE3 . TRP A 1 166 ? 39.463  5.642   -1.657  1.00 21.11  ? 195 TRP A CE3 1 
ATOM   1306 C CZ2 . TRP A 1 166 ? 42.171  6.380   -1.248  1.00 25.10  ? 195 TRP A CZ2 1 
ATOM   1307 C CZ3 . TRP A 1 166 ? 40.448  5.242   -2.525  1.00 24.63  ? 195 TRP A CZ3 1 
ATOM   1308 C CH2 . TRP A 1 166 ? 41.797  5.583   -2.304  1.00 23.97  ? 195 TRP A CH2 1 
ATOM   1309 N N   . GLU A 1 167 ? 38.848  3.949   1.417   1.00 19.96  ? 196 GLU A N   1 
ATOM   1310 C CA  . GLU A 1 167 ? 39.492  2.741   0.903   1.00 21.82  ? 196 GLU A CA  1 
ATOM   1311 C C   . GLU A 1 167 ? 38.600  1.513   1.046   1.00 22.66  ? 196 GLU A C   1 
ATOM   1312 O O   . GLU A 1 167 ? 38.472  0.713   0.132   1.00 21.98  ? 196 GLU A O   1 
ATOM   1313 C CB  . GLU A 1 167 ? 40.883  2.503   1.517   1.00 23.50  ? 196 GLU A CB  1 
ATOM   1314 C CG  . GLU A 1 167 ? 41.819  3.679   1.305   1.00 29.06  ? 196 GLU A CG  1 
ATOM   1315 C CD  . GLU A 1 167 ? 43.271  3.441   1.717   1.00 36.69  ? 196 GLU A CD  1 
ATOM   1316 O OE1 . GLU A 1 167 ? 44.053  4.354   1.566   1.00 44.02  ? 196 GLU A OE1 1 
ATOM   1317 O OE2 . GLU A 1 167 ? 43.622  2.373   2.219   1.00 47.72  ? 196 GLU A OE2 1 
ATOM   1318 N N   . LEU A 1 168 ? 37.987  1.344   2.206   1.00 22.04  ? 197 LEU A N   1 
ATOM   1319 C CA  . LEU A 1 168 ? 37.209  0.158   2.485   1.00 23.15  ? 197 LEU A CA  1 
ATOM   1320 C C   . LEU A 1 168 ? 35.855  0.261   1.785   1.00 19.47  ? 197 LEU A C   1 
ATOM   1321 O O   . LEU A 1 168 ? 35.305  -0.729  1.360   1.00 19.84  ? 197 LEU A O   1 
ATOM   1322 C CB  . LEU A 1 168 ? 37.024  0.047   4.000   1.00 24.38  ? 197 LEU A CB  1 
ATOM   1323 C CG  . LEU A 1 168 ? 38.230  -0.352  4.855   1.00 31.73  ? 197 LEU A CG  1 
ATOM   1324 C CD1 . LEU A 1 168 ? 38.766  -1.657  4.443   1.00 35.59  ? 197 LEU A CD1 1 
ATOM   1325 C CD2 . LEU A 1 168 ? 39.353  0.661   4.876   1.00 41.52  ? 197 LEU A CD2 1 
ATOM   1326 N N   . ILE A 1 169 ? 35.324  1.471   1.685   1.00 20.81  ? 198 ILE A N   1 
ATOM   1327 C CA  . ILE A 1 169 ? 34.103  1.749   0.927   1.00 22.08  ? 198 ILE A CA  1 
ATOM   1328 C C   . ILE A 1 169 ? 34.335  1.415   -0.543  1.00 18.40  ? 198 ILE A C   1 
ATOM   1329 O O   . ILE A 1 169 ? 33.493  0.800   -1.161  1.00 17.97  ? 198 ILE A O   1 
ATOM   1330 C CB  . ILE A 1 169 ? 33.676  3.217   1.125   1.00 22.88  ? 198 ILE A CB  1 
ATOM   1331 C CG1 . ILE A 1 169 ? 33.360  3.533   2.589   1.00 24.03  ? 198 ILE A CG1 1 
ATOM   1332 C CG2 . ILE A 1 169 ? 32.554  3.653   0.197   1.00 24.62  ? 198 ILE A CG2 1 
ATOM   1333 C CD1 . ILE A 1 169 ? 32.094  2.896   3.150   1.00 21.09  ? 198 ILE A CD1 1 
ATOM   1334 N N   . TYR A 1 170 ? 35.527  1.719   -1.050  1.00 19.10  ? 199 TYR A N   1 
ATOM   1335 C CA  . TYR A 1 170 ? 35.878  1.447   -2.436  1.00 18.96  ? 199 TYR A CA  1 
ATOM   1336 C C   . TYR A 1 170 ? 35.878  -0.066  -2.637  1.00 21.44  ? 199 TYR A C   1 
ATOM   1337 O O   . TYR A 1 170 ? 35.312  -0.551  -3.623  1.00 18.90  ? 199 TYR A O   1 
ATOM   1338 C CB  . TYR A 1 170 ? 37.227  2.082   -2.815  1.00 19.28  ? 199 TYR A CB  1 
ATOM   1339 C CG  . TYR A 1 170 ? 37.891  1.510   -4.072  1.00 18.94  ? 199 TYR A CG  1 
ATOM   1340 C CD1 . TYR A 1 170 ? 38.740  0.407   -3.983  1.00 22.71  ? 199 TYR A CD1 1 
ATOM   1341 C CD2 . TYR A 1 170 ? 37.675  2.046   -5.336  1.00 21.80  ? 199 TYR A CD2 1 
ATOM   1342 C CE1 . TYR A 1 170 ? 39.308  -0.165  -5.115  1.00 22.75  ? 199 TYR A CE1 1 
ATOM   1343 C CE2 . TYR A 1 170 ? 38.289  1.532   -6.469  1.00 22.00  ? 199 TYR A CE2 1 
ATOM   1344 C CZ  . TYR A 1 170 ? 39.074  0.393   -6.363  1.00 23.43  ? 199 TYR A CZ  1 
ATOM   1345 O OH  . TYR A 1 170 ? 39.683  -0.160  -7.457  1.00 22.91  ? 199 TYR A OH  1 
ATOM   1346 N N   . GLU A 1 171 ? 36.565  -0.778  -1.730  1.00 20.45  ? 200 GLU A N   1 
ATOM   1347 C CA  . GLU A 1 171 ? 36.713  -2.234  -1.815  1.00 20.20  ? 200 GLU A CA  1 
ATOM   1348 C C   . GLU A 1 171 ? 35.341  -2.898  -1.767  1.00 18.93  ? 200 GLU A C   1 
ATOM   1349 O O   . GLU A 1 171 ? 35.033  -3.733  -2.603  1.00 19.94  ? 200 GLU A O   1 
ATOM   1350 C CB  . GLU A 1 171 ? 37.592  -2.822  -0.718  1.00 20.25  ? 200 GLU A CB  1 
ATOM   1351 C CG  . GLU A 1 171 ? 39.073  -2.499  -0.949  1.00 22.53  ? 200 GLU A CG  1 
ATOM   1352 C CD  . GLU A 1 171 ? 39.720  -3.022  -2.231  1.00 25.67  ? 200 GLU A CD  1 
ATOM   1353 O OE1 . GLU A 1 171 ? 40.768  -2.454  -2.616  1.00 25.39  ? 200 GLU A OE1 1 
ATOM   1354 O OE2 . GLU A 1 171 ? 39.230  -3.988  -2.866  1.00 29.17  ? 200 GLU A OE2 1 
ATOM   1355 N N   . ASP A 1 172 ? 34.516  -2.506  -0.805  1.00 17.97  ? 201 ASP A N   1 
ATOM   1356 C CA  . ASP A 1 172 ? 33.175  -3.068  -0.686  1.00 19.27  ? 201 ASP A CA  1 
ATOM   1357 C C   . ASP A 1 172 ? 32.314  -2.698  -1.887  1.00 19.76  ? 201 ASP A C   1 
ATOM   1358 O O   . ASP A 1 172 ? 31.462  -3.485  -2.297  1.00 20.83  ? 201 ASP A O   1 
ATOM   1359 C CB  . ASP A 1 172 ? 32.442  -2.603  0.566   1.00 19.19  ? 201 ASP A CB  1 
ATOM   1360 C CG  . ASP A 1 172 ? 32.860  -3.258  1.878   1.00 23.40  ? 201 ASP A CG  1 
ATOM   1361 O OD1 . ASP A 1 172 ? 33.600  -4.294  1.901   1.00 22.47  ? 201 ASP A OD1 1 
ATOM   1362 O OD2 . ASP A 1 172 ? 32.430  -2.736  2.902   1.00 21.69  ? 201 ASP A OD2 1 
ATOM   1363 N N   . SER A 1 173 ? 32.467  -1.499  -2.419  1.00 21.35  ? 202 SER A N   1 
ATOM   1364 C CA  . SER A 1 173 ? 31.636  -1.101  -3.559  1.00 20.65  ? 202 SER A CA  1 
ATOM   1365 C C   . SER A 1 173 ? 32.017  -1.947  -4.757  1.00 20.75  ? 202 SER A C   1 
ATOM   1366 O O   . SER A 1 173 ? 31.183  -2.290  -5.566  1.00 17.80  ? 202 SER A O   1 
ATOM   1367 C CB  . SER A 1 173 ? 31.786  0.372   -3.889  1.00 19.68  ? 202 SER A CB  1 
ATOM   1368 O OG  . SER A 1 173 ? 31.337  1.187   -2.821  1.00 20.88  ? 202 SER A OG  1 
ATOM   1369 N N   . MET A 1 174 ? 33.332  -2.167  -4.948  1.00 19.85  ? 203 MET A N   1 
ATOM   1370 C CA  . MET A 1 174 ? 33.792  -2.932  -6.102  1.00 21.13  ? 203 MET A CA  1 
ATOM   1371 C C   . MET A 1 174 ? 33.295  -4.365  -5.991  1.00 21.23  ? 203 MET A C   1 
ATOM   1372 O O   . MET A 1 174 ? 32.862  -4.957  -7.005  1.00 20.55  ? 203 MET A O   1 
ATOM   1373 C CB  . MET A 1 174 ? 35.318  -2.917  -6.183  1.00 20.03  ? 203 MET A CB  1 
ATOM   1374 C CG  . MET A 1 174 ? 35.887  -1.535  -6.501  1.00 18.36  ? 203 MET A CG  1 
ATOM   1375 S SD  . MET A 1 174 ? 35.878  -1.170  -8.269  1.00 23.75  ? 203 MET A SD  1 
ATOM   1376 C CE  . MET A 1 174 ? 37.257  -2.234  -8.730  1.00 24.75  ? 203 MET A CE  1 
ATOM   1377 N N   . ASP A 1 175 ? 33.270  -4.896  -4.745  1.00 19.05  ? 204 ASP A N   1 
ATOM   1378 C CA  . ASP A 1 175 ? 32.785  -6.243  -4.542  1.00 19.25  ? 204 ASP A CA  1 
ATOM   1379 C C   . ASP A 1 175 ? 31.280  -6.317  -4.826  1.00 19.47  ? 204 ASP A C   1 
ATOM   1380 O O   . ASP A 1 175 ? 30.789  -7.317  -5.368  1.00 21.86  ? 204 ASP A O   1 
ATOM   1381 C CB  . ASP A 1 175 ? 33.036  -6.728  -3.122  1.00 23.27  ? 204 ASP A CB  1 
ATOM   1382 C CG  . ASP A 1 175 ? 34.487  -7.046  -2.765  1.00 26.65  ? 204 ASP A CG  1 
ATOM   1383 O OD1 . ASP A 1 175 ? 35.307  -7.141  -3.676  1.00 29.12  ? 204 ASP A OD1 1 
ATOM   1384 O OD2 . ASP A 1 175 ? 34.818  -7.080  -1.562  1.00 26.62  ? 204 ASP A OD2 1 
ATOM   1385 N N   . LEU A 1 176 ? 30.538  -5.299  -4.379  1.00 17.46  ? 205 LEU A N   1 
ATOM   1386 C CA  . LEU A 1 176 ? 29.093  -5.294  -4.571  1.00 18.96  ? 205 LEU A CA  1 
ATOM   1387 C C   . LEU A 1 176 ? 28.763  -5.217  -6.053  1.00 17.82  ? 205 LEU A C   1 
ATOM   1388 O O   . LEU A 1 176 ? 27.902  -5.944  -6.517  1.00 18.53  ? 205 LEU A O   1 
ATOM   1389 C CB  . LEU A 1 176 ? 28.451  -4.123  -3.823  1.00 20.14  ? 205 LEU A CB  1 
ATOM   1390 C CG  . LEU A 1 176 ? 26.921  -3.987  -3.967  1.00 22.19  ? 205 LEU A CG  1 
ATOM   1391 C CD1 . LEU A 1 176 ? 26.152  -5.283  -3.813  1.00 23.08  ? 205 LEU A CD1 1 
ATOM   1392 C CD2 . LEU A 1 176 ? 26.408  -2.980  -2.942  1.00 23.71  ? 205 LEU A CD2 1 
ATOM   1393 N N   . ILE A 1 177 ? 29.382  -4.265  -6.768  1.00 18.32  ? 206 ILE A N   1 
ATOM   1394 C CA  . ILE A 1 177 ? 29.120  -4.123  -8.207  1.00 17.94  ? 206 ILE A CA  1 
ATOM   1395 C C   . ILE A 1 177 ? 29.402  -5.436  -8.933  1.00 18.75  ? 206 ILE A C   1 
ATOM   1396 O O   . ILE A 1 177 ? 28.608  -5.907  -9.769  1.00 21.23  ? 206 ILE A O   1 
ATOM   1397 C CB  . ILE A 1 177 ? 29.929  -2.963  -8.773  1.00 20.77  ? 206 ILE A CB  1 
ATOM   1398 C CG1 . ILE A 1 177 ? 29.380  -1.620  -8.281  1.00 21.80  ? 206 ILE A CG1 1 
ATOM   1399 C CG2 . ILE A 1 177 ? 29.915  -3.041  -10.312 1.00 24.89  ? 206 ILE A CG2 1 
ATOM   1400 C CD1 . ILE A 1 177 ? 30.395  -0.494  -8.367  1.00 22.32  ? 206 ILE A CD1 1 
ATOM   1401 N N   . ALA A 1 178 ? 30.541  -6.051  -8.611  1.00 19.00  ? 207 ALA A N   1 
ATOM   1402 C CA  . ALA A 1 178 ? 30.887  -7.360  -9.179  1.00 19.61  ? 207 ALA A CA  1 
ATOM   1403 C C   . ALA A 1 178 ? 29.817  -8.429  -8.924  1.00 21.39  ? 207 ALA A C   1 
ATOM   1404 O O   . ALA A 1 178 ? 29.538  -9.220  -9.803  1.00 20.91  ? 207 ALA A O   1 
ATOM   1405 C CB  . ALA A 1 178 ? 32.195  -7.826  -8.680  1.00 19.89  ? 207 ALA A CB  1 
ATOM   1406 N N   . LYS A 1 179 ? 29.195  -8.448  -7.732  1.00 22.39  ? 208 LYS A N   1 
ATOM   1407 C CA  . LYS A 1 179 ? 28.265  -9.496  -7.350  1.00 19.90  ? 208 LYS A CA  1 
ATOM   1408 C C   . LYS A 1 179 ? 26.859  -9.242  -7.869  1.00 21.06  ? 208 LYS A C   1 
ATOM   1409 O O   . LYS A 1 179 ? 26.086  -10.170 -8.043  1.00 20.05  ? 208 LYS A O   1 
ATOM   1410 C CB  . LYS A 1 179 ? 28.230  -9.586  -5.826  1.00 22.40  ? 208 LYS A CB  1 
ATOM   1411 C CG  . LYS A 1 179 ? 29.539  -10.108 -5.267  1.00 22.62  ? 208 LYS A CG  1 
ATOM   1412 C CD  . LYS A 1 179 ? 29.681  -10.049 -3.751  1.00 24.23  ? 208 LYS A CD  1 
ATOM   1413 C CE  . LYS A 1 179 ? 31.157  -10.233 -3.413  1.00 27.71  ? 208 LYS A CE  1 
ATOM   1414 N NZ  . LYS A 1 179 ? 31.408  -9.855  -2.034  1.00 35.17  ? 208 LYS A NZ  1 
ATOM   1415 N N   . LEU A 1 180 ? 26.508  -7.978  -8.083  1.00 19.96  ? 209 LEU A N   1 
ATOM   1416 C CA  . LEU A 1 180 ? 25.132  -7.661  -8.383  1.00 20.51  ? 209 LEU A CA  1 
ATOM   1417 C C   . LEU A 1 180 ? 24.603  -8.445  -9.588  1.00 21.01  ? 209 LEU A C   1 
ATOM   1418 O O   . LEU A 1 180 ? 23.481  -8.861  -9.532  1.00 19.41  ? 209 LEU A O   1 
ATOM   1419 C CB  . LEU A 1 180 ? 25.006  -6.143  -8.565  1.00 22.46  ? 209 LEU A CB  1 
ATOM   1420 C CG  . LEU A 1 180 ? 24.731  -5.366  -7.289  1.00 22.35  ? 209 LEU A CG  1 
ATOM   1421 C CD1 . LEU A 1 180 ? 24.909  -3.909  -7.617  1.00 25.34  ? 209 LEU A CD1 1 
ATOM   1422 C CD2 . LEU A 1 180 ? 23.336  -5.621  -6.733  1.00 20.97  ? 209 LEU A CD2 1 
ATOM   1423 N N   . PRO A 1 181 ? 25.273  -8.560  -10.760 1.00 21.57  ? 210 PRO A N   1 
ATOM   1424 C CA  . PRO A 1 181 ? 24.725  -9.355  -11.853 1.00 25.86  ? 210 PRO A CA  1 
ATOM   1425 C C   . PRO A 1 181 ? 24.407  -10.803 -11.481 1.00 26.35  ? 210 PRO A C   1 
ATOM   1426 O O   . PRO A 1 181 ? 23.426  -11.353 -11.982 1.00 27.04  ? 210 PRO A O   1 
ATOM   1427 C CB  . PRO A 1 181 ? 25.820  -9.272  -12.943 1.00 24.47  ? 210 PRO A CB  1 
ATOM   1428 C CG  . PRO A 1 181 ? 26.551  -8.008  -12.617 1.00 25.90  ? 210 PRO A CG  1 
ATOM   1429 C CD  . PRO A 1 181 ? 26.553  -7.935  -11.091 1.00 23.40  ? 210 PRO A CD  1 
ATOM   1430 N N   . CYS A 1 182 ? 25.213  -11.372 -10.567 1.00 25.28  ? 211 CYS A N   1 
ATOM   1431 C CA  . CYS A 1 182 ? 25.030  -12.726 -10.076 1.00 27.92  ? 211 CYS A CA  1 
ATOM   1432 C C   . CYS A 1 182 ? 23.745  -12.828 -9.264  1.00 25.39  ? 211 CYS A C   1 
ATOM   1433 O O   . CYS A 1 182 ? 22.920  -13.682 -9.510  1.00 25.30  ? 211 CYS A O   1 
ATOM   1434 C CB  . CYS A 1 182 ? 26.195  -13.196 -9.211  1.00 29.98  ? 211 CYS A CB  1 
ATOM   1435 S SG  . CYS A 1 182 ? 27.735  -13.270 -10.148 1.00 39.09  ? 211 CYS A SG  1 
ATOM   1436 N N   . VAL A 1 183 ? 23.568  -11.892 -8.340  1.00 20.69  ? 212 VAL A N   1 
ATOM   1437 C CA  . VAL A 1 183 ? 22.336  -11.805 -7.587  1.00 21.99  ? 212 VAL A CA  1 
ATOM   1438 C C   . VAL A 1 183 ? 21.156  -11.607 -8.540  1.00 21.12  ? 212 VAL A C   1 
ATOM   1439 O O   . VAL A 1 183 ? 20.138  -12.298 -8.409  1.00 20.11  ? 212 VAL A O   1 
ATOM   1440 C CB  . VAL A 1 183 ? 22.418  -10.692 -6.527  1.00 20.06  ? 212 VAL A CB  1 
ATOM   1441 C CG1 . VAL A 1 183 ? 21.115  -10.547 -5.778  1.00 20.03  ? 212 VAL A CG1 1 
ATOM   1442 C CG2 . VAL A 1 183 ? 23.515  -10.965 -5.531  1.00 22.63  ? 212 VAL A CG2 1 
ATOM   1443 N N   . ALA A 1 184 ? 21.265  -10.605 -9.423  1.00 21.13  ? 213 ALA A N   1 
ATOM   1444 C CA  . ALA A 1 184 ? 20.164  -10.257 -10.306 1.00 25.03  ? 213 ALA A CA  1 
ATOM   1445 C C   . ALA A 1 184 ? 19.793  -11.442 -11.188 1.00 23.54  ? 213 ALA A C   1 
ATOM   1446 O O   . ALA A 1 184 ? 18.596  -11.702 -11.350 1.00 24.42  ? 213 ALA A O   1 
ATOM   1447 C CB  . ALA A 1 184 ? 20.484  -9.058  -11.134 1.00 24.45  ? 213 ALA A CB  1 
ATOM   1448 N N   . ALA A 1 185 ? 20.793  -12.126 -11.746 1.00 23.92  ? 214 ALA A N   1 
ATOM   1449 C CA  . ALA A 1 185 ? 20.542  -13.252 -12.651 1.00 23.12  ? 214 ALA A CA  1 
ATOM   1450 C C   . ALA A 1 185 ? 19.956  -14.450 -11.903 1.00 24.46  ? 214 ALA A C   1 
ATOM   1451 O O   . ALA A 1 185 ? 19.048  -15.101 -12.429 1.00 26.04  ? 214 ALA A O   1 
ATOM   1452 C CB  . ALA A 1 185 ? 21.774  -13.600 -13.388 1.00 22.60  ? 214 ALA A CB  1 
ATOM   1453 N N   . LYS A 1 186 ? 20.392  -14.705 -10.660 1.00 25.16  ? 215 LYS A N   1 
ATOM   1454 C CA  . LYS A 1 186 ? 19.798  -15.752 -9.840  1.00 26.81  ? 215 LYS A CA  1 
ATOM   1455 C C   . LYS A 1 186 ? 18.310  -15.491 -9.636  1.00 25.17  ? 215 LYS A C   1 
ATOM   1456 O O   . LYS A 1 186 ? 17.471  -16.395 -9.741  1.00 23.31  ? 215 LYS A O   1 
ATOM   1457 C CB  . LYS A 1 186 ? 20.479  -15.866 -8.473  1.00 32.51  ? 215 LYS A CB  1 
ATOM   1458 C CG  . LYS A 1 186 ? 20.374  -17.209 -7.763  1.00 42.73  ? 215 LYS A CG  1 
ATOM   1459 C CD  . LYS A 1 186 ? 21.630  -18.081 -7.706  1.00 42.34  ? 215 LYS A CD  1 
ATOM   1460 C CE  . LYS A 1 186 ? 21.308  -19.552 -7.941  1.00 36.87  ? 215 LYS A CE  1 
ATOM   1461 N N   . ILE A 1 187 ? 17.969  -14.231 -9.302  1.00 23.20  ? 216 ILE A N   1 
ATOM   1462 C CA  . ILE A 1 187 ? 16.573  -13.867 -9.133  1.00 22.24  ? 216 ILE A CA  1 
ATOM   1463 C C   . ILE A 1 187 ? 15.803  -14.163 -10.434 1.00 23.38  ? 216 ILE A C   1 
ATOM   1464 O O   . ILE A 1 187 ? 14.725  -14.761 -10.439 1.00 22.62  ? 216 ILE A O   1 
ATOM   1465 C CB  . ILE A 1 187 ? 16.455  -12.386 -8.728  1.00 22.77  ? 216 ILE A CB  1 
ATOM   1466 C CG1 . ILE A 1 187 ? 16.954  -12.161 -7.301  1.00 25.43  ? 216 ILE A CG1 1 
ATOM   1467 C CG2 . ILE A 1 187 ? 15.025  -11.883 -8.862  1.00 22.88  ? 216 ILE A CG2 1 
ATOM   1468 C CD1 . ILE A 1 187 ? 17.186  -10.698 -6.957  1.00 28.39  ? 216 ILE A CD1 1 
ATOM   1469 N N   . TYR A 1 188 ? 16.323  -13.667 -11.542 1.00 22.69  ? 217 TYR A N   1 
ATOM   1470 C CA  . TYR A 1 188 ? 15.630  -13.829 -12.808 1.00 24.30  ? 217 TYR A CA  1 
ATOM   1471 C C   . TYR A 1 188 ? 15.348  -15.307 -13.090 1.00 26.80  ? 217 TYR A C   1 
ATOM   1472 O O   . TYR A 1 188 ? 14.225  -15.682 -13.454 1.00 29.85  ? 217 TYR A O   1 
ATOM   1473 C CB  . TYR A 1 188 ? 16.444  -13.233 -13.957 1.00 25.31  ? 217 TYR A CB  1 
ATOM   1474 C CG  . TYR A 1 188 ? 15.664  -13.231 -15.269 1.00 26.73  ? 217 TYR A CG  1 
ATOM   1475 C CD1 . TYR A 1 188 ? 14.690  -12.277 -15.513 1.00 26.69  ? 217 TYR A CD1 1 
ATOM   1476 C CD2 . TYR A 1 188 ? 15.954  -14.150 -16.282 1.00 30.05  ? 217 TYR A CD2 1 
ATOM   1477 C CE1 . TYR A 1 188 ? 13.953  -12.291 -16.689 1.00 30.79  ? 217 TYR A CE1 1 
ATOM   1478 C CE2 . TYR A 1 188 ? 15.238  -14.160 -17.474 1.00 32.04  ? 217 TYR A CE2 1 
ATOM   1479 C CZ  . TYR A 1 188 ? 14.242  -13.217 -17.688 1.00 32.83  ? 217 TYR A CZ  1 
ATOM   1480 O OH  . TYR A 1 188 ? 13.553  -13.191 -18.891 1.00 29.54  ? 217 TYR A OH  1 
ATOM   1481 N N   . ARG A 1 189 ? 16.371  -16.144 -12.944 1.00 25.59  ? 218 ARG A N   1 
ATOM   1482 C CA  . ARG A 1 189 ? 16.246  -17.551 -13.323 1.00 28.17  ? 218 ARG A CA  1 
ATOM   1483 C C   . ARG A 1 189 ? 15.384  -18.333 -12.330 1.00 31.82  ? 218 ARG A C   1 
ATOM   1484 O O   . ARG A 1 189 ? 14.657  -19.260 -12.714 1.00 30.46  ? 218 ARG A O   1 
ATOM   1485 C CB  . ARG A 1 189 ? 17.601  -18.230 -13.475 1.00 28.37  ? 218 ARG A CB  1 
ATOM   1486 C CG  . ARG A 1 189 ? 18.509  -17.582 -14.494 1.00 34.01  ? 218 ARG A CG  1 
ATOM   1487 C CD  . ARG A 1 189 ? 19.612  -18.528 -14.947 1.00 43.53  ? 218 ARG A CD  1 
ATOM   1488 N NE  . ARG A 1 189 ? 19.028  -19.416 -15.956 1.00 51.36  ? 218 ARG A NE  1 
ATOM   1489 C CZ  . ARG A 1 189 ? 19.507  -19.636 -17.168 1.00 54.62  ? 218 ARG A CZ  1 
ATOM   1490 N NH1 . ARG A 1 189 ? 20.712  -19.195 -17.506 1.00 50.07  ? 218 ARG A NH1 1 
ATOM   1491 N NH2 . ARG A 1 189 ? 18.765  -20.326 -18.014 1.00 53.35  ? 218 ARG A NH2 1 
ATOM   1492 N N   . ASN A 1 190 ? 15.482  -17.989 -11.039 1.00 30.02  ? 219 ASN A N   1 
ATOM   1493 C CA  . ASN A 1 190 ? 14.668  -18.649 -10.030 1.00 29.59  ? 219 ASN A CA  1 
ATOM   1494 C C   . ASN A 1 190 ? 13.203  -18.342 -10.288 1.00 29.96  ? 219 ASN A C   1 
ATOM   1495 O O   . ASN A 1 190 ? 12.346  -19.205 -10.134 1.00 29.51  ? 219 ASN A O   1 
ATOM   1496 C CB  . ASN A 1 190 ? 15.043  -18.272 -8.594  1.00 28.81  ? 219 ASN A CB  1 
ATOM   1497 C CG  . ASN A 1 190 ? 16.368  -18.859 -8.173  1.00 35.93  ? 219 ASN A CG  1 
ATOM   1498 O OD1 . ASN A 1 190 ? 16.951  -19.636 -8.942  1.00 35.44  ? 219 ASN A OD1 1 
ATOM   1499 N ND2 . ASN A 1 190 ? 16.882  -18.473 -7.005  1.00 30.15  ? 219 ASN A ND2 1 
ATOM   1500 N N   . LEU A 1 191 ? 12.905  -17.109 -10.687 1.00 29.06  ? 220 LEU A N   1 
ATOM   1501 C CA  . LEU A 1 191 ? 11.516  -16.719 -10.842 1.00 32.56  ? 220 LEU A CA  1 
ATOM   1502 C C   . LEU A 1 191 ? 10.965  -17.137 -12.204 1.00 32.63  ? 220 LEU A C   1 
ATOM   1503 O O   . LEU A 1 191 ? 9.795   -17.501 -12.267 1.00 29.65  ? 220 LEU A O   1 
ATOM   1504 C CB  . LEU A 1 191 ? 11.366  -15.220 -10.650 1.00 30.47  ? 220 LEU A CB  1 
ATOM   1505 C CG  . LEU A 1 191 ? 11.387  -14.738 -9.193  1.00 31.93  ? 220 LEU A CG  1 
ATOM   1506 C CD1 . LEU A 1 191 ? 11.445  -13.228 -9.170  1.00 29.33  ? 220 LEU A CD1 1 
ATOM   1507 C CD2 . LEU A 1 191 ? 10.187  -15.261 -8.416  1.00 32.48  ? 220 LEU A CD2 1 
ATOM   1508 N N   . TYR A 1 192 ? 11.759  -16.944 -13.269 1.00 33.35  ? 221 TYR A N   1 
ATOM   1509 C CA  . TYR A 1 192 ? 11.233  -16.927 -14.628 1.00 35.03  ? 221 TYR A CA  1 
ATOM   1510 C C   . TYR A 1 192 ? 11.842  -18.033 -15.491 1.00 39.92  ? 221 TYR A C   1 
ATOM   1511 O O   . TYR A 1 192 ? 11.517  -18.112 -16.660 1.00 37.29  ? 221 TYR A O   1 
ATOM   1512 C CB  . TYR A 1 192 ? 11.456  -15.579 -15.304 1.00 37.31  ? 221 TYR A CB  1 
ATOM   1513 C CG  . TYR A 1 192 ? 10.923  -14.435 -14.448 1.00 35.18  ? 221 TYR A CG  1 
ATOM   1514 C CD1 . TYR A 1 192 ? 9.597   -14.404 -14.017 1.00 32.11  ? 221 TYR A CD1 1 
ATOM   1515 C CD2 . TYR A 1 192 ? 11.778  -13.425 -14.023 1.00 34.20  ? 221 TYR A CD2 1 
ATOM   1516 C CE1 . TYR A 1 192 ? 9.124   -13.379 -13.216 1.00 34.72  ? 221 TYR A CE1 1 
ATOM   1517 C CE2 . TYR A 1 192 ? 11.311  -12.392 -13.230 1.00 31.71  ? 221 TYR A CE2 1 
ATOM   1518 C CZ  . TYR A 1 192 ? 10.007  -12.392 -12.788 1.00 32.93  ? 221 TYR A CZ  1 
ATOM   1519 O OH  . TYR A 1 192 ? 9.630   -11.334 -12.017 1.00 35.14  ? 221 TYR A OH  1 
ATOM   1520 N N   . ARG A 1 193 ? 12.702  -18.891 -14.928 1.00 41.25  ? 222 ARG A N   1 
ATOM   1521 C CA  . ARG A 1 193 ? 13.274  -20.005 -15.678 1.00 39.75  ? 222 ARG A CA  1 
ATOM   1522 C C   . ARG A 1 193 ? 13.411  -21.250 -14.802 1.00 32.09  ? 222 ARG A C   1 
ATOM   1523 O O   . ARG A 1 193 ? 14.412  -21.947 -14.924 1.00 35.87  ? 222 ARG A O   1 
ATOM   1524 C CB  . ARG A 1 193 ? 14.646  -19.594 -16.214 1.00 40.46  ? 222 ARG A CB  1 
ATOM   1525 C CG  . ARG A 1 193 ? 14.617  -18.564 -17.325 1.00 46.54  ? 222 ARG A CG  1 
ATOM   1526 C CD  . ARG A 1 193 ? 15.895  -18.754 -18.124 1.00 66.64  ? 222 ARG A CD  1 
ATOM   1527 N NE  . ARG A 1 193 ? 16.224  -17.801 -19.193 1.00 73.64  ? 222 ARG A NE  1 
ATOM   1528 C CZ  . ARG A 1 193 ? 15.387  -17.221 -20.047 1.00 70.36  ? 222 ARG A CZ  1 
ATOM   1529 N NH1 . ARG A 1 193 ? 14.081  -17.188 -19.800 1.00 55.92  ? 222 ARG A NH1 1 
ATOM   1530 N NH2 . ARG A 1 193 ? 15.900  -16.602 -21.104 1.00 77.51  ? 222 ARG A NH2 1 
ATOM   1531 N N   . GLU A 1 194 ? 12.433  -21.468 -13.905 1.00 33.15  ? 223 GLU A N   1 
ATOM   1532 C CA  . GLU A 1 194 ? 12.309  -22.660 -13.073 1.00 44.40  ? 223 GLU A CA  1 
ATOM   1533 C C   . GLU A 1 194 ? 13.591  -23.048 -12.336 1.00 43.92  ? 223 GLU A C   1 
ATOM   1534 O O   . GLU A 1 194 ? 13.870  -24.236 -12.186 1.00 41.41  ? 223 GLU A O   1 
ATOM   1535 C CB  . GLU A 1 194 ? 11.941  -23.884 -13.920 1.00 50.47  ? 223 GLU A CB  1 
ATOM   1536 C CG  . GLU A 1 194 ? 10.664  -23.740 -14.742 1.00 54.29  ? 223 GLU A CG  1 
ATOM   1537 C CD  . GLU A 1 194 ? 10.421  -25.004 -15.563 1.00 66.96  ? 223 GLU A CD  1 
ATOM   1538 O OE1 . GLU A 1 194 ? 11.315  -25.371 -16.358 1.00 60.80  ? 223 GLU A OE1 1 
ATOM   1539 O OE2 . GLU A 1 194 ? 9.354   -25.643 -15.400 1.00 71.53  ? 223 GLU A OE2 1 
ATOM   1540 N N   . GLY A 1 195 ? 14.386  -22.071 -11.876 1.00 41.59  ? 224 GLY A N   1 
ATOM   1541 C CA  . GLY A 1 195 ? 15.466  -22.363 -10.945 1.00 36.28  ? 224 GLY A CA  1 
ATOM   1542 C C   . GLY A 1 195 ? 16.728  -22.900 -11.608 1.00 38.00  ? 224 GLY A C   1 
ATOM   1543 O O   . GLY A 1 195 ? 17.621  -23.373 -10.907 1.00 41.49  ? 224 GLY A O   1 
ATOM   1544 N N   . SER A 1 196 ? 16.828  -22.790 -12.938 1.00 38.43  ? 225 SER A N   1 
ATOM   1545 C CA  . SER A 1 196 ? 17.996  -23.264 -13.652 1.00 42.89  ? 225 SER A CA  1 
ATOM   1546 C C   . SER A 1 196 ? 19.198  -22.401 -13.282 1.00 44.86  ? 225 SER A C   1 
ATOM   1547 O O   . SER A 1 196 ? 19.040  -21.235 -12.912 1.00 40.41  ? 225 SER A O   1 
ATOM   1548 C CB  . SER A 1 196 ? 17.761  -23.281 -15.136 1.00 45.83  ? 225 SER A CB  1 
ATOM   1549 O OG  . SER A 1 196 ? 17.467  -21.984 -15.642 1.00 50.34  ? 225 SER A OG  1 
ATOM   1550 N N   . GLY A 1 197 ? 20.395  -22.982 -13.422 1.00 37.77  ? 226 GLY A N   1 
ATOM   1551 C CA  . GLY A 1 197 ? 21.613  -22.396 -12.900 1.00 38.10  ? 226 GLY A CA  1 
ATOM   1552 C C   . GLY A 1 197 ? 22.094  -21.214 -13.740 1.00 38.19  ? 226 GLY A C   1 
ATOM   1553 O O   . GLY A 1 197 ? 21.774  -21.116 -14.932 1.00 39.11  ? 226 GLY A O   1 
ATOM   1554 N N   . ILE A 1 198 ? 22.862  -20.318 -13.103 1.00 35.25  ? 227 ILE A N   1 
ATOM   1555 C CA  . ILE A 1 198 ? 23.319  -19.106 -13.773 1.00 38.14  ? 227 ILE A CA  1 
ATOM   1556 C C   . ILE A 1 198 ? 24.585  -19.360 -14.594 1.00 39.09  ? 227 ILE A C   1 
ATOM   1557 O O   . ILE A 1 198 ? 24.964  -18.523 -15.430 1.00 39.95  ? 227 ILE A O   1 
ATOM   1558 C CB  . ILE A 1 198 ? 23.511  -17.910 -12.821 1.00 35.44  ? 227 ILE A CB  1 
ATOM   1559 C CG1 . ILE A 1 198 ? 24.244  -18.265 -11.532 1.00 34.88  ? 227 ILE A CG1 1 
ATOM   1560 C CG2 . ILE A 1 198 ? 22.167  -17.231 -12.555 1.00 39.23  ? 227 ILE A CG2 1 
ATOM   1561 C CD1 . ILE A 1 198 ? 24.731  -17.039 -10.765 1.00 34.80  ? 227 ILE A CD1 1 
ATOM   1562 N N   . GLY A 1 199 ? 25.212  -20.512 -14.360 1.00 38.80  ? 228 GLY A N   1 
ATOM   1563 C CA  . GLY A 1 199 ? 26.470  -20.861 -14.984 1.00 37.22  ? 228 GLY A CA  1 
ATOM   1564 C C   . GLY A 1 199 ? 27.608  -20.092 -14.327 1.00 39.66  ? 228 GLY A C   1 
ATOM   1565 O O   . GLY A 1 199 ? 27.510  -19.690 -13.171 1.00 48.98  ? 228 GLY A O   1 
ATOM   1566 N N   . ALA A 1 200 ? 28.640  -19.808 -15.117 1.00 44.93  ? 229 ALA A N   1 
ATOM   1567 C CA  . ALA A 1 200 ? 29.907  -19.350 -14.587 1.00 44.45  ? 229 ALA A CA  1 
ATOM   1568 C C   . ALA A 1 200 ? 30.202  -17.977 -15.171 1.00 44.01  ? 229 ALA A C   1 
ATOM   1569 O O   . ALA A 1 200 ? 29.597  -17.578 -16.170 1.00 43.74  ? 229 ALA A O   1 
ATOM   1570 C CB  . ALA A 1 200 ? 30.989  -20.356 -14.921 1.00 46.82  ? 229 ALA A CB  1 
ATOM   1571 N N   . ILE A 1 201 ? 31.105  -17.276 -14.476 1.00 41.95  ? 230 ILE A N   1 
ATOM   1572 C CA  . ILE A 1 201 ? 31.676  -16.015 -14.898 1.00 41.94  ? 230 ILE A CA  1 
ATOM   1573 C C   . ILE A 1 201 ? 32.831  -16.325 -15.841 1.00 45.14  ? 230 ILE A C   1 
ATOM   1574 O O   . ILE A 1 201 ? 33.652  -17.188 -15.535 1.00 49.39  ? 230 ILE A O   1 
ATOM   1575 C CB  . ILE A 1 201 ? 32.160  -15.222 -13.664 1.00 42.40  ? 230 ILE A CB  1 
ATOM   1576 C CG1 . ILE A 1 201 ? 31.004  -14.775 -12.783 1.00 44.03  ? 230 ILE A CG1 1 
ATOM   1577 C CG2 . ILE A 1 201 ? 33.033  -14.032 -14.055 1.00 43.71  ? 230 ILE A CG2 1 
ATOM   1578 C CD1 . ILE A 1 201 ? 30.167  -13.639 -13.359 1.00 41.54  ? 230 ILE A CD1 1 
ATOM   1579 N N   . ASP A 1 202 ? 32.866  -15.637 -16.984 1.00 39.91  ? 231 ASP A N   1 
ATOM   1580 C CA  . ASP A 1 202 ? 34.019  -15.653 -17.864 1.00 41.61  ? 231 ASP A CA  1 
ATOM   1581 C C   . ASP A 1 202 ? 34.883  -14.444 -17.511 1.00 42.19  ? 231 ASP A C   1 
ATOM   1582 O O   . ASP A 1 202 ? 34.417  -13.313 -17.485 1.00 42.74  ? 231 ASP A O   1 
ATOM   1583 C CB  . ASP A 1 202 ? 33.635  -15.749 -19.335 1.00 43.10  ? 231 ASP A CB  1 
ATOM   1584 C CG  . ASP A 1 202 ? 34.795  -15.831 -20.330 1.00 46.59  ? 231 ASP A CG  1 
ATOM   1585 O OD1 . ASP A 1 202 ? 35.926  -15.396 -19.989 1.00 39.56  ? 231 ASP A OD1 1 
ATOM   1586 O OD2 . ASP A 1 202 ? 34.566  -16.357 -21.446 1.00 49.80  ? 231 ASP A OD2 1 
ATOM   1587 N N   . SER A 1 203 ? 36.153  -14.735 -17.255 1.00 37.53  ? 232 SER A N   1 
ATOM   1588 C CA  . SER A 1 203 ? 37.135  -13.804 -16.741 1.00 44.01  ? 232 SER A CA  1 
ATOM   1589 C C   . SER A 1 203 ? 37.490  -12.707 -17.737 1.00 37.36  ? 232 SER A C   1 
ATOM   1590 O O   . SER A 1 203 ? 38.039  -11.677 -17.350 1.00 40.99  ? 232 SER A O   1 
ATOM   1591 C CB  . SER A 1 203 ? 38.374  -14.590 -16.384 1.00 45.93  ? 232 SER A CB  1 
ATOM   1592 O OG  . SER A 1 203 ? 39.288  -13.765 -15.695 1.00 53.88  ? 232 SER A OG  1 
ATOM   1593 N N   . ASN A 1 204 ? 37.296  -12.970 -19.032 1.00 39.09  ? 233 ASN A N   1 
ATOM   1594 C CA  . ASN A 1 204 ? 37.689  -12.023 -20.057 1.00 36.11  ? 233 ASN A CA  1 
ATOM   1595 C C   . ASN A 1 204 ? 36.473  -11.360 -20.704 1.00 34.67  ? 233 ASN A C   1 
ATOM   1596 O O   . ASN A 1 204 ? 36.616  -10.736 -21.740 1.00 36.58  ? 233 ASN A O   1 
ATOM   1597 C CB  . ASN A 1 204 ? 38.498  -12.725 -21.148 1.00 51.94  ? 233 ASN A CB  1 
ATOM   1598 C CG  . ASN A 1 204 ? 39.849  -13.171 -20.644 1.00 57.89  ? 233 ASN A CG  1 
ATOM   1599 O OD1 . ASN A 1 204 ? 40.627  -12.359 -20.124 1.00 54.40  ? 233 ASN A OD1 1 
ATOM   1600 N ND2 . ASN A 1 204 ? 40.120  -14.463 -20.757 1.00 63.44  ? 233 ASN A ND2 1 
ATOM   1601 N N   . LEU A 1 205 ? 35.264  -11.533 -20.170 1.00 34.32  ? 234 LEU A N   1 
ATOM   1602 C CA  . LEU A 1 205 ? 34.138  -10.766 -20.706 1.00 35.24  ? 234 LEU A CA  1 
ATOM   1603 C C   . LEU A 1 205 ? 33.935  -9.507  -19.866 1.00 34.17  ? 234 LEU A C   1 
ATOM   1604 O O   . LEU A 1 205 ? 34.336  -9.445  -18.694 1.00 30.83  ? 234 LEU A O   1 
ATOM   1605 C CB  . LEU A 1 205 ? 32.854  -11.585 -20.823 1.00 34.33  ? 234 LEU A CB  1 
ATOM   1606 C CG  . LEU A 1 205 ? 32.939  -12.857 -21.682 1.00 34.74  ? 234 LEU A CG  1 
ATOM   1607 C CD1 . LEU A 1 205 ? 31.593  -13.561 -21.682 1.00 36.15  ? 234 LEU A CD1 1 
ATOM   1608 C CD2 . LEU A 1 205 ? 33.403  -12.577 -23.098 1.00 35.78  ? 234 LEU A CD2 1 
ATOM   1609 N N   . ASP A 1 206 ? 33.289  -8.507  -20.475 1.00 32.43  ? 235 ASP A N   1 
ATOM   1610 C CA  . ASP A 1 206 ? 32.803  -7.353  -19.718 1.00 34.84  ? 235 ASP A CA  1 
ATOM   1611 C C   . ASP A 1 206 ? 31.611  -7.760  -18.842 1.00 27.67  ? 235 ASP A C   1 
ATOM   1612 O O   . ASP A 1 206 ? 30.971  -8.798  -19.035 1.00 27.74  ? 235 ASP A O   1 
ATOM   1613 C CB  . ASP A 1 206 ? 32.477  -6.154  -20.606 1.00 30.98  ? 235 ASP A CB  1 
ATOM   1614 C CG  . ASP A 1 206 ? 31.396  -6.417  -21.642 1.00 35.89  ? 235 ASP A CG  1 
ATOM   1615 O OD1 . ASP A 1 206 ? 31.678  -7.237  -22.538 1.00 44.14  ? 235 ASP A OD1 1 
ATOM   1616 O OD2 . ASP A 1 206 ? 30.269  -5.852  -21.515 1.00 32.10  ? 235 ASP A OD2 1 
ATOM   1617 N N   . TRP A 1 207 ? 31.352  -6.908  -17.854 1.00 24.51  ? 236 TRP A N   1 
ATOM   1618 C CA  . TRP A 1 207 ? 30.325  -7.053  -16.835 1.00 22.78  ? 236 TRP A CA  1 
ATOM   1619 C C   . TRP A 1 207 ? 28.941  -7.330  -17.433 1.00 23.92  ? 236 TRP A C   1 
ATOM   1620 O O   . TRP A 1 207 ? 28.255  -8.246  -17.010 1.00 22.03  ? 236 TRP A O   1 
ATOM   1621 C CB  . TRP A 1 207 ? 30.347  -5.725  -16.046 1.00 22.72  ? 236 TRP A CB  1 
ATOM   1622 C CG  . TRP A 1 207 ? 29.572  -5.670  -14.759 1.00 21.15  ? 236 TRP A CG  1 
ATOM   1623 C CD1 . TRP A 1 207 ? 29.779  -6.362  -13.607 1.00 23.81  ? 236 TRP A CD1 1 
ATOM   1624 C CD2 . TRP A 1 207 ? 28.552  -4.689  -14.460 1.00 24.49  ? 236 TRP A CD2 1 
ATOM   1625 N NE1 . TRP A 1 207 ? 28.939  -5.914  -12.621 1.00 22.93  ? 236 TRP A NE1 1 
ATOM   1626 C CE2 . TRP A 1 207 ? 28.177  -4.885  -13.117 1.00 24.09  ? 236 TRP A CE2 1 
ATOM   1627 C CE3 . TRP A 1 207 ? 27.921  -3.686  -15.203 1.00 22.77  ? 236 TRP A CE3 1 
ATOM   1628 C CZ2 . TRP A 1 207 ? 27.191  -4.110  -12.522 1.00 26.27  ? 236 TRP A CZ2 1 
ATOM   1629 C CZ3 . TRP A 1 207 ? 26.934  -2.935  -14.608 1.00 25.17  ? 236 TRP A CZ3 1 
ATOM   1630 C CH2 . TRP A 1 207 ? 26.609  -3.114  -13.265 1.00 24.13  ? 236 TRP A CH2 1 
ATOM   1631 N N   . SER A 1 208 ? 28.560  -6.511  -18.434 1.00 23.92  ? 237 SER A N   1 
ATOM   1632 C CA  . SER A 1 208 ? 27.275  -6.576  -19.094 1.00 24.19  ? 237 SER A CA  1 
ATOM   1633 C C   . SER A 1 208 ? 27.108  -7.917  -19.808 1.00 24.22  ? 237 SER A C   1 
ATOM   1634 O O   . SER A 1 208 ? 26.034  -8.480  -19.797 1.00 24.31  ? 237 SER A O   1 
ATOM   1635 C CB  . SER A 1 208 ? 27.106  -5.464  -20.103 1.00 25.17  ? 237 SER A CB  1 
ATOM   1636 O OG  . SER A 1 208 ? 26.992  -4.186  -19.508 1.00 24.65  ? 237 SER A OG  1 
ATOM   1637 N N   . HIS A 1 209 ? 28.171  -8.420  -20.408 1.00 25.46  ? 238 HIS A N   1 
ATOM   1638 C CA  . HIS A 1 209 ? 28.100  -9.681  -21.150 1.00 29.58  ? 238 HIS A CA  1 
ATOM   1639 C C   . HIS A 1 209 ? 27.985  -10.861 -20.190 1.00 27.34  ? 238 HIS A C   1 
ATOM   1640 O O   . HIS A 1 209 ? 27.175  -11.780 -20.364 1.00 29.37  ? 238 HIS A O   1 
ATOM   1641 C CB  . HIS A 1 209 ? 29.279  -9.747  -22.132 1.00 33.72  ? 238 HIS A CB  1 
ATOM   1642 C CG  . HIS A 1 209 ? 29.170  -10.763 -23.200 1.00 40.25  ? 238 HIS A CG  1 
ATOM   1643 N ND1 . HIS A 1 209 ? 30.146  -10.850 -24.176 1.00 40.22  ? 238 HIS A ND1 1 
ATOM   1644 C CD2 . HIS A 1 209 ? 28.290  -11.762 -23.442 1.00 41.24  ? 238 HIS A CD2 1 
ATOM   1645 C CE1 . HIS A 1 209 ? 29.834  -11.844 -24.993 1.00 38.18  ? 238 HIS A CE1 1 
ATOM   1646 N NE2 . HIS A 1 209 ? 28.703  -12.382 -24.596 1.00 36.19  ? 238 HIS A NE2 1 
ATOM   1647 N N   . ASN A 1 210 ? 28.760  -10.830 -19.104 1.00 27.99  ? 239 ASN A N   1 
ATOM   1648 C CA  . ASN A 1 210 ? 28.627  -11.867 -18.096 1.00 26.39  ? 239 ASN A CA  1 
ATOM   1649 C C   . ASN A 1 210 ? 27.195  -11.899 -17.609 1.00 25.03  ? 239 ASN A C   1 
ATOM   1650 O O   . ASN A 1 210 ? 26.587  -12.968 -17.474 1.00 28.83  ? 239 ASN A O   1 
ATOM   1651 C CB  . ASN A 1 210 ? 29.628  -11.714 -16.950 1.00 28.73  ? 239 ASN A CB  1 
ATOM   1652 C CG  . ASN A 1 210 ? 30.968  -12.356 -17.264 1.00 31.32  ? 239 ASN A CG  1 
ATOM   1653 O OD1 . ASN A 1 210 ? 31.015  -13.454 -17.842 1.00 31.76  ? 239 ASN A OD1 1 
ATOM   1654 N ND2 . ASN A 1 210 ? 32.057  -11.693 -16.905 1.00 31.51  ? 239 ASN A ND2 1 
ATOM   1655 N N   . PHE A 1 211 ? 26.652  -10.703 -17.383 1.00 25.14  ? 240 PHE A N   1 
ATOM   1656 C CA  . PHE A 1 211 ? 25.288  -10.569 -16.927 1.00 24.94  ? 240 PHE A CA  1 
ATOM   1657 C C   . PHE A 1 211 ? 24.295  -11.227 -17.887 1.00 22.32  ? 240 PHE A C   1 
ATOM   1658 O O   . PHE A 1 211 ? 23.459  -12.005 -17.460 1.00 25.47  ? 240 PHE A O   1 
ATOM   1659 C CB  . PHE A 1 211 ? 24.990  -9.066  -16.691 1.00 24.32  ? 240 PHE A CB  1 
ATOM   1660 C CG  . PHE A 1 211 ? 23.672  -8.764  -15.999 1.00 24.58  ? 240 PHE A CG  1 
ATOM   1661 C CD1 . PHE A 1 211 ? 23.064  -9.695  -15.175 1.00 23.66  ? 240 PHE A CD1 1 
ATOM   1662 C CD2 . PHE A 1 211 ? 23.050  -7.545  -16.173 1.00 26.72  ? 240 PHE A CD2 1 
ATOM   1663 C CE1 . PHE A 1 211 ? 21.876  -9.436  -14.528 1.00 23.67  ? 240 PHE A CE1 1 
ATOM   1664 C CE2 . PHE A 1 211 ? 21.842  -7.287  -15.525 1.00 27.77  ? 240 PHE A CE2 1 
ATOM   1665 C CZ  . PHE A 1 211 ? 21.288  -8.223  -14.679 1.00 26.77  ? 240 PHE A CZ  1 
ATOM   1666 N N   . THR A 1 212 ? 24.307  -10.851 -19.169 1.00 25.13  ? 241 THR A N   1 
ATOM   1667 C CA  . THR A 1 212 ? 23.300  -11.353 -20.086 1.00 27.14  ? 241 THR A CA  1 
ATOM   1668 C C   . THR A 1 212 ? 23.497  -12.866 -20.266 1.00 27.92  ? 241 THR A C   1 
ATOM   1669 O O   . THR A 1 212 ? 22.499  -13.586 -20.374 1.00 29.12  ? 241 THR A O   1 
ATOM   1670 C CB  . THR A 1 212 ? 23.334  -10.613 -21.433 1.00 26.71  ? 241 THR A CB  1 
ATOM   1671 O OG1 . THR A 1 212 ? 24.641  -10.686 -21.996 1.00 24.27  ? 241 THR A OG1 1 
ATOM   1672 C CG2 . THR A 1 212 ? 23.032  -9.132  -21.311 1.00 27.74  ? 241 THR A CG2 1 
ATOM   1673 N N   . ASN A 1 213 ? 24.754  -13.345 -20.196 1.00 27.96  ? 242 ASN A N   1 
ATOM   1674 C CA  . ASN A 1 213 ? 25.018  -14.778 -20.206 1.00 30.84  ? 242 ASN A CA  1 
ATOM   1675 C C   . ASN A 1 213 ? 24.306  -15.462 -19.043 1.00 30.02  ? 242 ASN A C   1 
ATOM   1676 O O   . ASN A 1 213 ? 23.645  -16.473 -19.229 1.00 31.21  ? 242 ASN A O   1 
ATOM   1677 C CB  . ASN A 1 213 ? 26.502  -15.141 -20.150 1.00 33.58  ? 242 ASN A CB  1 
ATOM   1678 C CG  . ASN A 1 213 ? 27.217  -14.997 -21.470 1.00 34.78  ? 242 ASN A CG  1 
ATOM   1679 O OD1 . ASN A 1 213 ? 26.591  -14.719 -22.493 1.00 34.07  ? 242 ASN A OD1 1 
ATOM   1680 N ND2 . ASN A 1 213 ? 28.524  -15.204 -21.460 1.00 39.59  ? 242 ASN A ND2 1 
ATOM   1681 N N   . MET A 1 214 ? 24.475  -14.920 -17.833 1.00 28.53  ? 243 MET A N   1 
ATOM   1682 C CA  . MET A 1 214 ? 23.885  -15.493 -16.641 1.00 26.13  ? 243 MET A CA  1 
ATOM   1683 C C   . MET A 1 214 ? 22.364  -15.376 -16.651 1.00 28.35  ? 243 MET A C   1 
ATOM   1684 O O   . MET A 1 214 ? 21.722  -16.221 -16.052 1.00 30.11  ? 243 MET A O   1 
ATOM   1685 C CB  . MET A 1 214 ? 24.421  -14.816 -15.372 1.00 28.25  ? 243 MET A CB  1 
ATOM   1686 C CG  . MET A 1 214 ? 25.875  -15.115 -15.115 1.00 30.42  ? 243 MET A CG  1 
ATOM   1687 S SD  . MET A 1 214 ? 26.390  -14.506 -13.499 1.00 34.51  ? 243 MET A SD  1 
ATOM   1688 C CE  . MET A 1 214 ? 26.480  -12.727 -13.676 1.00 33.43  ? 243 MET A CE  1 
ATOM   1689 N N   . LEU A 1 215 ? 21.802  -14.338 -17.298 1.00 29.52  ? 244 LEU A N   1 
ATOM   1690 C CA  . LEU A 1 215 ? 20.355  -14.248 -17.490 1.00 30.77  ? 244 LEU A CA  1 
ATOM   1691 C C   . LEU A 1 215 ? 19.834  -15.269 -18.509 1.00 34.12  ? 244 LEU A C   1 
ATOM   1692 O O   . LEU A 1 215 ? 18.644  -15.567 -18.526 1.00 33.45  ? 244 LEU A O   1 
ATOM   1693 C CB  . LEU A 1 215 ? 19.987  -12.859 -17.961 1.00 29.17  ? 244 LEU A CB  1 
ATOM   1694 C CG  . LEU A 1 215 ? 20.084  -11.715 -16.950 1.00 28.76  ? 244 LEU A CG  1 
ATOM   1695 C CD1 . LEU A 1 215 ? 19.883  -10.431 -17.745 1.00 25.94  ? 244 LEU A CD1 1 
ATOM   1696 C CD2 . LEU A 1 215 ? 19.039  -11.899 -15.850 1.00 31.75  ? 244 LEU A CD2 1 
ATOM   1697 N N   . GLY A 1 216 ? 20.703  -15.757 -19.394 1.00 37.44  ? 245 GLY A N   1 
ATOM   1698 C CA  . GLY A 1 216 ? 20.291  -16.739 -20.384 1.00 40.44  ? 245 GLY A CA  1 
ATOM   1699 C C   . GLY A 1 216 ? 20.009  -16.089 -21.737 1.00 43.00  ? 245 GLY A C   1 
ATOM   1700 O O   . GLY A 1 216 ? 19.362  -16.685 -22.589 1.00 49.39  ? 245 GLY A O   1 
ATOM   1701 N N   . TYR A 1 217 ? 20.515  -14.876 -21.952 1.00 38.67  ? 246 TYR A N   1 
ATOM   1702 C CA  . TYR A 1 217 ? 20.400  -14.259 -23.259 1.00 44.41  ? 246 TYR A CA  1 
ATOM   1703 C C   . TYR A 1 217 ? 21.733  -14.400 -24.004 1.00 51.35  ? 246 TYR A C   1 
ATOM   1704 O O   . TYR A 1 217 ? 22.805  -14.260 -23.424 1.00 68.27  ? 246 TYR A O   1 
ATOM   1705 C CB  . TYR A 1 217 ? 19.895  -12.830 -23.059 1.00 39.99  ? 246 TYR A CB  1 
ATOM   1706 C CG  . TYR A 1 217 ? 18.458  -12.732 -22.570 1.00 38.39  ? 246 TYR A CG  1 
ATOM   1707 C CD1 . TYR A 1 217 ? 18.117  -13.049 -21.267 1.00 35.48  ? 246 TYR A CD1 1 
ATOM   1708 C CD2 . TYR A 1 217 ? 17.455  -12.248 -23.396 1.00 37.58  ? 246 TYR A CD2 1 
ATOM   1709 C CE1 . TYR A 1 217 ? 16.816  -12.944 -20.819 1.00 38.19  ? 246 TYR A CE1 1 
ATOM   1710 C CE2 . TYR A 1 217 ? 16.158  -12.108 -22.955 1.00 36.82  ? 246 TYR A CE2 1 
ATOM   1711 C CZ  . TYR A 1 217 ? 15.841  -12.462 -21.663 1.00 35.32  ? 246 TYR A CZ  1 
ATOM   1712 O OH  . TYR A 1 217 ? 14.565  -12.344 -21.257 1.00 34.50  ? 246 TYR A OH  1 
ATOM   1713 N N   . THR A 1 218 ? 21.667  -14.738 -25.291 1.00 52.16  ? 247 THR A N   1 
ATOM   1714 C CA  . THR A 1 218 ? 22.873  -14.957 -26.071 1.00 54.61  ? 247 THR A CA  1 
ATOM   1715 C C   . THR A 1 218 ? 22.872  -14.051 -27.296 1.00 53.41  ? 247 THR A C   1 
ATOM   1716 O O   . THR A 1 218 ? 23.725  -14.177 -28.165 1.00 60.54  ? 247 THR A O   1 
ATOM   1717 C CB  . THR A 1 218 ? 22.916  -16.438 -26.439 1.00 56.20  ? 247 THR A CB  1 
ATOM   1718 O OG1 . THR A 1 218 ? 21.578  -16.764 -26.814 1.00 58.30  ? 247 THR A OG1 1 
ATOM   1719 C CG2 . THR A 1 218 ? 23.318  -17.308 -25.263 1.00 55.74  ? 247 THR A CG2 1 
ATOM   1720 N N   . ASP A 1 219 ? 21.916  -13.133 -27.346 1.00 45.18  ? 248 ASP A N   1 
ATOM   1721 C CA  . ASP A 1 219 ? 21.738  -12.240 -28.471 1.00 44.36  ? 248 ASP A CA  1 
ATOM   1722 C C   . ASP A 1 219 ? 22.679  -11.044 -28.299 1.00 44.09  ? 248 ASP A C   1 
ATOM   1723 O O   . ASP A 1 219 ? 22.550  -10.284 -27.330 1.00 39.77  ? 248 ASP A O   1 
ATOM   1724 C CB  . ASP A 1 219 ? 20.256  -11.896 -28.539 1.00 51.66  ? 248 ASP A CB  1 
ATOM   1725 C CG  . ASP A 1 219 ? 19.766  -11.266 -29.828 1.00 58.52  ? 248 ASP A CG  1 
ATOM   1726 O OD1 . ASP A 1 219 ? 20.272  -10.173 -30.167 1.00 61.72  ? 248 ASP A OD1 1 
ATOM   1727 O OD2 . ASP A 1 219 ? 18.886  -11.888 -30.472 1.00 67.27  ? 248 ASP A OD2 1 
ATOM   1728 N N   . HIS A 1 220 ? 23.615  -10.863 -29.250 1.00 36.51  ? 249 HIS A N   1 
ATOM   1729 C CA  . HIS A 1 220 ? 24.584  -9.773  -29.234 1.00 34.90  ? 249 HIS A CA  1 
ATOM   1730 C C   . HIS A 1 220 ? 23.912  -8.389  -29.128 1.00 36.78  ? 249 HIS A C   1 
ATOM   1731 O O   . HIS A 1 220 ? 24.504  -7.455  -28.593 1.00 35.80  ? 249 HIS A O   1 
ATOM   1732 C CB  . HIS A 1 220 ? 25.499  -9.825  -30.474 1.00 43.33  ? 249 HIS A CB  1 
ATOM   1733 C CG  . HIS A 1 220 ? 26.331  -8.585  -30.713 1.00 44.34  ? 249 HIS A CG  1 
ATOM   1734 N ND1 . HIS A 1 220 ? 27.517  -8.322  -30.047 1.00 44.82  ? 249 HIS A ND1 1 
ATOM   1735 C CD2 . HIS A 1 220 ? 26.101  -7.516  -31.490 1.00 42.21  ? 249 HIS A CD2 1 
ATOM   1736 C CE1 . HIS A 1 220 ? 27.987  -7.147  -30.430 1.00 45.18  ? 249 HIS A CE1 1 
ATOM   1737 N NE2 . HIS A 1 220 ? 27.137  -6.631  -31.306 1.00 45.69  ? 249 HIS A NE2 1 
ATOM   1738 N N   . GLN A 1 221 ? 22.699  -8.218  -29.680 1.00 33.75  ? 250 GLN A N   1 
ATOM   1739 C CA  . GLN A 1 221 ? 22.072  -6.909  -29.666 1.00 38.90  ? 250 GLN A CA  1 
ATOM   1740 C C   . GLN A 1 221 ? 21.531  -6.620  -28.264 1.00 33.60  ? 250 GLN A C   1 
ATOM   1741 O O   . GLN A 1 221 ? 21.516  -5.463  -27.852 1.00 30.84  ? 250 GLN A O   1 
ATOM   1742 C CB  . GLN A 1 221 ? 21.008  -6.690  -30.752 1.00 46.44  ? 250 GLN A CB  1 
ATOM   1743 C CG  . GLN A 1 221 ? 21.585  -6.406  -32.142 1.00 56.24  ? 250 GLN A CG  1 
ATOM   1744 C CD  . GLN A 1 221 ? 22.788  -5.471  -32.182 1.00 63.66  ? 250 GLN A CD  1 
ATOM   1745 O OE1 . GLN A 1 221 ? 22.892  -4.475  -31.452 1.00 61.15  ? 250 GLN A OE1 1 
ATOM   1746 N NE2 . GLN A 1 221 ? 23.727  -5.778  -33.066 1.00 70.87  ? 250 GLN A NE2 1 
ATOM   1747 N N   . PHE A 1 222 ? 21.083  -7.674  -27.590 1.00 28.91  ? 251 PHE A N   1 
ATOM   1748 C CA  . PHE A 1 222 ? 20.535  -7.571  -26.249 1.00 31.76  ? 251 PHE A CA  1 
ATOM   1749 C C   . PHE A 1 222 ? 21.642  -7.247  -25.249 1.00 29.53  ? 251 PHE A C   1 
ATOM   1750 O O   . PHE A 1 222 ? 21.424  -6.435  -24.361 1.00 28.25  ? 251 PHE A O   1 
ATOM   1751 C CB  . PHE A 1 222 ? 19.797  -8.815  -25.782 1.00 28.32  ? 251 PHE A CB  1 
ATOM   1752 C CG  . PHE A 1 222 ? 19.195  -8.610  -24.393 1.00 32.73  ? 251 PHE A CG  1 
ATOM   1753 C CD1 . PHE A 1 222 ? 18.096  -7.781  -24.208 1.00 31.13  ? 251 PHE A CD1 1 
ATOM   1754 C CD2 . PHE A 1 222 ? 19.744  -9.230  -23.276 1.00 34.39  ? 251 PHE A CD2 1 
ATOM   1755 C CE1 . PHE A 1 222 ? 17.567  -7.581  -22.948 1.00 34.85  ? 251 PHE A CE1 1 
ATOM   1756 C CE2 . PHE A 1 222 ? 19.191  -9.043  -22.014 1.00 33.36  ? 251 PHE A CE2 1 
ATOM   1757 C CZ  . PHE A 1 222 ? 18.112  -8.217  -21.854 1.00 32.36  ? 251 PHE A CZ  1 
ATOM   1758 N N   . THR A 1 223 ? 22.834  -7.818  -25.426 1.00 26.74  ? 252 THR A N   1 
ATOM   1759 C CA  . THR A 1 223 ? 24.007  -7.375  -24.683 1.00 30.00  ? 252 THR A CA  1 
ATOM   1760 C C   . THR A 1 223 ? 24.333  -5.909  -24.958 1.00 28.10  ? 252 THR A C   1 
ATOM   1761 O O   . THR A 1 223 ? 24.674  -5.183  -24.039 1.00 24.99  ? 252 THR A O   1 
ATOM   1762 C CB  . THR A 1 223 ? 25.228  -8.257  -24.966 1.00 27.87  ? 252 THR A CB  1 
ATOM   1763 O OG1 . THR A 1 223 ? 24.699  -9.533  -24.650 1.00 26.85  ? 252 THR A OG1 1 
ATOM   1764 C CG2 . THR A 1 223 ? 26.409  -7.904  -24.083 1.00 28.44  ? 252 THR A CG2 1 
ATOM   1765 N N   . GLU A 1 224 ? 24.310  -5.476  -26.218 1.00 27.60  ? 253 GLU A N   1 
ATOM   1766 C CA  . GLU A 1 224 ? 24.557  -4.076  -26.548 1.00 26.86  ? 253 GLU A CA  1 
ATOM   1767 C C   . GLU A 1 224 ? 23.516  -3.160  -25.891 1.00 24.65  ? 253 GLU A C   1 
ATOM   1768 O O   . GLU A 1 224 ? 23.876  -2.103  -25.385 1.00 28.09  ? 253 GLU A O   1 
ATOM   1769 C CB  . GLU A 1 224 ? 24.559  -3.848  -28.071 1.00 27.24  ? 253 GLU A CB  1 
ATOM   1770 C CG  . GLU A 1 224 ? 25.826  -4.374  -28.722 1.00 31.93  ? 253 GLU A CG  1 
ATOM   1771 C CD  . GLU A 1 224 ? 26.989  -3.426  -28.528 1.00 33.96  ? 253 GLU A CD  1 
ATOM   1772 O OE1 . GLU A 1 224 ? 27.799  -3.611  -27.589 1.00 33.20  ? 253 GLU A OE1 1 
ATOM   1773 O OE2 . GLU A 1 224 ? 27.052  -2.465  -29.309 1.00 41.13  ? 253 GLU A OE2 1 
ATOM   1774 N N   . LEU A 1 225 ? 22.243  -3.567  -25.902 1.00 24.85  ? 254 LEU A N   1 
ATOM   1775 C CA  . LEU A 1 225 ? 21.165  -2.852  -25.256 1.00 24.45  ? 254 LEU A CA  1 
ATOM   1776 C C   . LEU A 1 225 ? 21.467  -2.767  -23.752 1.00 27.92  ? 254 LEU A C   1 
ATOM   1777 O O   . LEU A 1 225 ? 21.242  -1.723  -23.155 1.00 26.04  ? 254 LEU A O   1 
ATOM   1778 C CB  . LEU A 1 225 ? 19.804  -3.519  -25.421 1.00 26.02  ? 254 LEU A CB  1 
ATOM   1779 C CG  . LEU A 1 225 ? 18.652  -2.818  -24.683 1.00 29.37  ? 254 LEU A CG  1 
ATOM   1780 C CD1 . LEU A 1 225 ? 18.542  -1.352  -25.100 1.00 30.23  ? 254 LEU A CD1 1 
ATOM   1781 C CD2 . LEU A 1 225 ? 17.332  -3.492  -24.863 1.00 28.43  ? 254 LEU A CD2 1 
ATOM   1782 N N   . THR A 1 226 ? 21.915  -3.882  -23.164 1.00 26.63  ? 255 THR A N   1 
ATOM   1783 C CA  . THR A 1 226 ? 22.179  -3.932  -21.726 1.00 28.71  ? 255 THR A CA  1 
ATOM   1784 C C   . THR A 1 226 ? 23.335  -2.995  -21.376 1.00 27.75  ? 255 THR A C   1 
ATOM   1785 O O   . THR A 1 226 ? 23.270  -2.224  -20.412 1.00 31.11  ? 255 THR A O   1 
ATOM   1786 C CB  . THR A 1 226 ? 22.479  -5.377  -21.330 1.00 30.81  ? 255 THR A CB  1 
ATOM   1787 O OG1 . THR A 1 226 ? 21.274  -6.093  -21.570 1.00 26.03  ? 255 THR A OG1 1 
ATOM   1788 C CG2 . THR A 1 226 ? 22.902  -5.516  -19.875 1.00 29.83  ? 255 THR A CG2 1 
ATOM   1789 N N   . ARG A 1 227 ? 24.393  -3.042  -22.185 1.00 24.21  ? 256 ARG A N   1 
ATOM   1790 C CA  . ARG A 1 227 ? 25.512  -2.124  -22.013 1.00 28.02  ? 256 ARG A CA  1 
ATOM   1791 C C   . ARG A 1 227 ? 25.053  -0.659  -21.979 1.00 29.79  ? 256 ARG A C   1 
ATOM   1792 O O   . ARG A 1 227 ? 25.483  0.144   -21.127 1.00 27.13  ? 256 ARG A O   1 
ATOM   1793 C CB  . ARG A 1 227 ? 26.534  -2.337  -23.130 1.00 26.43  ? 256 ARG A CB  1 
ATOM   1794 C CG  . ARG A 1 227 ? 27.272  -3.656  -23.023 1.00 26.82  ? 256 ARG A CG  1 
ATOM   1795 C CD  . ARG A 1 227 ? 28.126  -3.880  -24.248 1.00 27.89  ? 256 ARG A CD  1 
ATOM   1796 N NE  . ARG A 1 227 ? 28.961  -5.057  -24.047 1.00 27.29  ? 256 ARG A NE  1 
ATOM   1797 C CZ  . ARG A 1 227 ? 29.175  -6.001  -24.970 1.00 33.83  ? 256 ARG A CZ  1 
ATOM   1798 N NH1 . ARG A 1 227 ? 28.660  -5.921  -26.186 1.00 33.29  ? 256 ARG A NH1 1 
ATOM   1799 N NH2 . ARG A 1 227 ? 29.924  -7.019  -24.668 1.00 28.20  ? 256 ARG A NH2 1 
ATOM   1800 N N   . LEU A 1 228 ? 24.218  -0.290  -22.955 1.00 26.68  ? 257 LEU A N   1 
ATOM   1801 C CA  . LEU A 1 228 ? 23.694  1.067   -23.029 1.00 27.99  ? 257 LEU A CA  1 
ATOM   1802 C C   . LEU A 1 228 ? 22.781  1.351   -21.826 1.00 27.01  ? 257 LEU A C   1 
ATOM   1803 O O   . LEU A 1 228 ? 22.869  2.435   -21.258 1.00 27.39  ? 257 LEU A O   1 
ATOM   1804 C CB  . LEU A 1 228 ? 22.959  1.316   -24.361 1.00 30.13  ? 257 LEU A CB  1 
ATOM   1805 C CG  . LEU A 1 228 ? 22.320  2.704   -24.512 1.00 31.09  ? 257 LEU A CG  1 
ATOM   1806 C CD1 . LEU A 1 228 ? 23.397  3.782   -24.600 1.00 33.29  ? 257 LEU A CD1 1 
ATOM   1807 C CD2 . LEU A 1 228 ? 21.395  2.800   -25.731 1.00 34.01  ? 257 LEU A CD2 1 
ATOM   1808 N N   . TYR A 1 229 ? 21.844  0.434   -21.523 1.00 22.37  ? 258 TYR A N   1 
ATOM   1809 C CA  . TYR A 1 229 ? 20.854  0.601   -20.475 1.00 22.64  ? 258 TYR A CA  1 
ATOM   1810 C C   . TYR A 1 229 ? 21.565  0.853   -19.132 1.00 23.35  ? 258 TYR A C   1 
ATOM   1811 O O   . TYR A 1 229 ? 21.191  1.750   -18.408 1.00 21.70  ? 258 TYR A O   1 
ATOM   1812 C CB  . TYR A 1 229 ? 19.927  -0.619  -20.458 1.00 25.65  ? 258 TYR A CB  1 
ATOM   1813 C CG  . TYR A 1 229 ? 18.845  -0.578  -19.393 1.00 28.62  ? 258 TYR A CG  1 
ATOM   1814 C CD1 . TYR A 1 229 ? 19.200  -0.728  -18.065 1.00 28.19  ? 258 TYR A CD1 1 
ATOM   1815 C CD2 . TYR A 1 229 ? 17.497  -0.347  -19.681 1.00 34.25  ? 258 TYR A CD2 1 
ATOM   1816 C CE1 . TYR A 1 229 ? 18.285  -0.631  -17.053 1.00 30.01  ? 258 TYR A CE1 1 
ATOM   1817 C CE2 . TYR A 1 229 ? 16.548  -0.336  -18.661 1.00 36.02  ? 258 TYR A CE2 1 
ATOM   1818 C CZ  . TYR A 1 229 ? 16.953  -0.464  -17.341 1.00 33.69  ? 258 TYR A CZ  1 
ATOM   1819 O OH  . TYR A 1 229 ? 16.142  -0.444  -16.220 1.00 37.40  ? 258 TYR A OH  1 
ATOM   1820 N N   . LEU A 1 230 ? 22.570  0.037   -18.797 1.00 27.38  ? 259 LEU A N   1 
ATOM   1821 C CA  . LEU A 1 230 ? 23.270  0.102   -17.523 1.00 24.06  ? 259 LEU A CA  1 
ATOM   1822 C C   . LEU A 1 230 ? 24.130  1.362   -17.454 1.00 25.45  ? 259 LEU A C   1 
ATOM   1823 O O   . LEU A 1 230 ? 24.329  1.927   -16.394 1.00 22.18  ? 259 LEU A O   1 
ATOM   1824 C CB  . LEU A 1 230 ? 24.111  -1.160  -17.365 1.00 23.34  ? 259 LEU A CB  1 
ATOM   1825 C CG  . LEU A 1 230 ? 23.349  -2.481  -17.221 1.00 23.93  ? 259 LEU A CG  1 
ATOM   1826 C CD1 . LEU A 1 230 ? 24.319  -3.619  -17.118 1.00 25.11  ? 259 LEU A CD1 1 
ATOM   1827 C CD2 . LEU A 1 230 ? 22.353  -2.509  -16.059 1.00 24.08  ? 259 LEU A CD2 1 
ATOM   1828 N N   . THR A 1 231 ? 24.642  1.838   -18.596 1.00 22.64  ? 260 THR A N   1 
ATOM   1829 C CA  . THR A 1 231 ? 25.348  3.107   -18.634 1.00 22.27  ? 260 THR A CA  1 
ATOM   1830 C C   . THR A 1 231 ? 24.393  4.261   -18.339 1.00 23.82  ? 260 THR A C   1 
ATOM   1831 O O   . THR A 1 231 ? 24.712  5.172   -17.564 1.00 21.97  ? 260 THR A O   1 
ATOM   1832 C CB  . THR A 1 231 ? 26.061  3.311   -19.977 1.00 23.93  ? 260 THR A CB  1 
ATOM   1833 O OG1 . THR A 1 231 ? 27.042  2.279   -20.062 1.00 24.75  ? 260 THR A OG1 1 
ATOM   1834 C CG2 . THR A 1 231 ? 26.760  4.664   -20.077 1.00 23.45  ? 260 THR A CG2 1 
ATOM   1835 N N   . ILE A 1 232 ? 23.221  4.275   -18.967 1.00 24.72  ? 261 ILE A N   1 
ATOM   1836 C CA  . ILE A 1 232 ? 22.427  5.510   -18.952 1.00 24.27  ? 261 ILE A CA  1 
ATOM   1837 C C   . ILE A 1 232 ? 21.548  5.655   -17.702 1.00 23.75  ? 261 ILE A C   1 
ATOM   1838 O O   . ILE A 1 232 ? 21.121  6.761   -17.405 1.00 22.32  ? 261 ILE A O   1 
ATOM   1839 C CB  . ILE A 1 232 ? 21.572  5.712   -20.207 1.00 24.89  ? 261 ILE A CB  1 
ATOM   1840 C CG1 . ILE A 1 232 ? 20.493  4.658   -20.368 1.00 27.48  ? 261 ILE A CG1 1 
ATOM   1841 C CG2 . ILE A 1 232 ? 22.463  5.877   -21.446 1.00 25.92  ? 261 ILE A CG2 1 
ATOM   1842 C CD1 . ILE A 1 232 ? 19.522  4.976   -21.498 1.00 30.01  ? 261 ILE A CD1 1 
ATOM   1843 N N   . HIS A 1 233 ? 21.252  4.563   -17.008 1.00 25.78  ? 262 HIS A N   1 
ATOM   1844 C CA  . HIS A 1 233 ? 20.469  4.624   -15.777 1.00 23.86  ? 262 HIS A CA  1 
ATOM   1845 C C   . HIS A 1 233 ? 21.381  4.775   -14.558 1.00 22.42  ? 262 HIS A C   1 
ATOM   1846 O O   . HIS A 1 233 ? 20.910  4.734   -13.427 1.00 22.75  ? 262 HIS A O   1 
ATOM   1847 C CB  . HIS A 1 233 ? 19.634  3.360   -15.622 1.00 24.56  ? 262 HIS A CB  1 
ATOM   1848 C CG  . HIS A 1 233 ? 18.470  3.295   -16.523 1.00 28.84  ? 262 HIS A CG  1 
ATOM   1849 N ND1 . HIS A 1 233 ? 18.611  3.040   -17.872 1.00 29.40  ? 262 HIS A ND1 1 
ATOM   1850 C CD2 . HIS A 1 233 ? 17.162  3.462   -16.287 1.00 33.12  ? 262 HIS A CD2 1 
ATOM   1851 C CE1 . HIS A 1 233 ? 17.402  3.069   -18.430 1.00 35.14  ? 262 HIS A CE1 1 
ATOM   1852 N NE2 . HIS A 1 233 ? 16.510  3.326   -17.482 1.00 36.65  ? 262 HIS A NE2 1 
ATOM   1853 N N   . SER A 1 234 ? 22.678  4.949   -14.790 1.00 21.87  ? 263 SER A N   1 
ATOM   1854 C CA  . SER A 1 234 ? 23.706  4.805   -13.761 1.00 19.47  ? 263 SER A CA  1 
ATOM   1855 C C   . SER A 1 234 ? 23.561  5.831   -12.647 1.00 21.85  ? 263 SER A C   1 
ATOM   1856 O O   . SER A 1 234 ? 23.847  5.529   -11.483 1.00 19.15  ? 263 SER A O   1 
ATOM   1857 C CB  . SER A 1 234 ? 25.081  4.902   -14.357 1.00 20.36  ? 263 SER A CB  1 
ATOM   1858 O OG  . SER A 1 234 ? 25.275  6.164   -15.012 1.00 24.05  ? 263 SER A OG  1 
ATOM   1859 N N   . ASP A 1 235 ? 23.181  7.074   -13.000 1.00 20.30  ? 264 ASP A N   1 
ATOM   1860 C CA  . ASP A 1 235 ? 23.191  8.170   -12.045 1.00 20.35  ? 264 ASP A CA  1 
ATOM   1861 C C   . ASP A 1 235 ? 22.274  9.268   -12.565 1.00 23.25  ? 264 ASP A C   1 
ATOM   1862 O O   . ASP A 1 235 ? 22.165  9.451   -13.776 1.00 22.61  ? 264 ASP A O   1 
ATOM   1863 C CB  . ASP A 1 235 ? 24.608  8.679   -11.837 1.00 22.63  ? 264 ASP A CB  1 
ATOM   1864 C CG  . ASP A 1 235 ? 24.909  9.287   -10.475 1.00 26.61  ? 264 ASP A CG  1 
ATOM   1865 O OD1 . ASP A 1 235 ? 24.386  8.753   -9.465  1.00 22.97  ? 264 ASP A OD1 1 
ATOM   1866 O OD2 . ASP A 1 235 ? 25.741  10.228  -10.437 1.00 29.88  ? 264 ASP A OD2 1 
ATOM   1867 N N   . HIS A 1 236 ? 21.600  9.969   -11.646 1.00 21.44  ? 265 HIS A N   1 
ATOM   1868 C CA  . HIS A 1 236 ? 20.762  11.093  -12.008 1.00 23.06  ? 265 HIS A CA  1 
ATOM   1869 C C   . HIS A 1 236 ? 20.688  12.124  -10.885 1.00 21.50  ? 265 HIS A C   1 
ATOM   1870 O O   . HIS A 1 236 ? 19.594  12.454  -10.428 1.00 20.36  ? 265 HIS A O   1 
ATOM   1871 C CB  . HIS A 1 236 ? 19.370  10.611  -12.399 1.00 25.35  ? 265 HIS A CB  1 
ATOM   1872 C CG  . HIS A 1 236 ? 18.787  11.444  -13.477 1.00 31.71  ? 265 HIS A CG  1 
ATOM   1873 N ND1 . HIS A 1 236 ? 17.747  12.337  -13.309 1.00 40.04  ? 265 HIS A ND1 1 
ATOM   1874 C CD2 . HIS A 1 236 ? 19.097  11.457  -14.785 1.00 33.75  ? 265 HIS A CD2 1 
ATOM   1875 C CE1 . HIS A 1 236 ? 17.456  12.880  -14.484 1.00 41.33  ? 265 HIS A CE1 1 
ATOM   1876 N NE2 . HIS A 1 236 ? 18.274  12.361  -15.401 1.00 34.33  ? 265 HIS A NE2 1 
ATOM   1877 N N   . GLU A 1 237 ? 21.869  12.599  -10.513 1.00 22.48  ? 266 GLU A N   1 
ATOM   1878 C CA  . GLU A 1 237 ? 21.997  13.584  -9.415  1.00 24.65  ? 266 GLU A CA  1 
ATOM   1879 C C   . GLU A 1 237 ? 21.740  12.912  -8.056  1.00 23.00  ? 266 GLU A C   1 
ATOM   1880 O O   . GLU A 1 237 ? 21.497  11.700  -8.009  1.00 21.27  ? 266 GLU A O   1 
ATOM   1881 C CB  . GLU A 1 237 ? 21.127  14.835  -9.532  1.00 28.88  ? 266 GLU A CB  1 
ATOM   1882 C CG  . GLU A 1 237 ? 21.646  15.883  -10.501 1.00 38.15  ? 266 GLU A CG  1 
ATOM   1883 C CD  . GLU A 1 237 ? 20.816  17.145  -10.378 1.00 41.26  ? 266 GLU A CD  1 
ATOM   1884 O OE1 . GLU A 1 237 ? 19.704  17.076  -9.818  1.00 44.14  ? 266 GLU A OE1 1 
ATOM   1885 O OE2 . GLU A 1 237 ? 21.285  18.194  -10.848 1.00 37.94  ? 266 GLU A OE2 1 
ATOM   1886 N N   . GLY A 1 238 ? 21.745  13.710  -7.008  1.00 19.30  ? 267 GLY A N   1 
ATOM   1887 C CA  . GLY A 1 238 ? 21.666  13.201  -5.651  1.00 19.16  ? 267 GLY A CA  1 
ATOM   1888 C C   . GLY A 1 238 ? 20.267  13.263  -5.045  1.00 18.25  ? 267 GLY A C   1 
ATOM   1889 O O   . GLY A 1 238 ? 20.006  12.629  -4.001  1.00 20.37  ? 267 GLY A O   1 
ATOM   1890 N N   . GLY A 1 239 ? 19.367  13.986  -5.682  1.00 18.99  ? 268 GLY A N   1 
ATOM   1891 C CA  . GLY A 1 239 ? 18.054  14.274  -5.107  1.00 19.91  ? 268 GLY A CA  1 
ATOM   1892 C C   . GLY A 1 239 ? 17.008  13.196  -5.382  1.00 19.93  ? 268 GLY A C   1 
ATOM   1893 O O   . GLY A 1 239 ? 15.962  13.154  -4.738  1.00 22.84  ? 268 GLY A O   1 
ATOM   1894 N N   . ASN A 1 240 ? 17.250  12.302  -6.343  1.00 21.57  ? 269 ASN A N   1 
ATOM   1895 C CA  . ASN A 1 240 ? 16.300  11.238  -6.612  1.00 20.79  ? 269 ASN A CA  1 
ATOM   1896 C C   . ASN A 1 240 ? 16.329  10.295  -5.394  1.00 20.28  ? 269 ASN A C   1 
ATOM   1897 O O   . ASN A 1 240 ? 17.329  10.217  -4.681  1.00 16.03  ? 269 ASN A O   1 
ATOM   1898 C CB  . ASN A 1 240 ? 16.576  10.517  -7.931  1.00 23.69  ? 269 ASN A CB  1 
ATOM   1899 C CG  . ASN A 1 240 ? 17.829  9.669   -7.903  1.00 23.33  ? 269 ASN A CG  1 
ATOM   1900 O OD1 . ASN A 1 240 ? 17.885  8.588   -7.297  1.00 21.81  ? 269 ASN A OD1 1 
ATOM   1901 N ND2 . ASN A 1 240 ? 18.887  10.175  -8.503  1.00 24.25  ? 269 ASN A ND2 1 
ATOM   1902 N N   . VAL A 1 241 ? 15.225  9.582   -5.142  1.00 18.08  ? 270 VAL A N   1 
ATOM   1903 C CA  . VAL A 1 241 ? 15.087  8.859   -3.868  1.00 20.28  ? 270 VAL A CA  1 
ATOM   1904 C C   . VAL A 1 241 ? 16.141  7.770   -3.665  1.00 20.16  ? 270 VAL A C   1 
ATOM   1905 O O   . VAL A 1 241 ? 16.628  7.573   -2.566  1.00 18.21  ? 270 VAL A O   1 
ATOM   1906 C CB  . VAL A 1 241 ? 13.665  8.295   -3.766  1.00 21.23  ? 270 VAL A CB  1 
ATOM   1907 C CG1 . VAL A 1 241 ? 13.476  7.376   -2.554  1.00 22.41  ? 270 VAL A CG1 1 
ATOM   1908 C CG2 . VAL A 1 241 ? 12.711  9.466   -3.688  1.00 29.04  ? 270 VAL A CG2 1 
ATOM   1909 N N   . SER A 1 242 ? 16.524  7.070   -4.717  1.00 19.01  ? 271 SER A N   1 
ATOM   1910 C CA  . SER A 1 242 ? 17.498  6.008   -4.567  1.00 20.68  ? 271 SER A CA  1 
ATOM   1911 C C   . SER A 1 242 ? 18.870  6.558   -4.191  1.00 19.66  ? 271 SER A C   1 
ATOM   1912 O O   . SER A 1 242 ? 19.455  6.088   -3.210  1.00 17.12  ? 271 SER A O   1 
ATOM   1913 C CB  . SER A 1 242 ? 17.512  5.044   -5.754  1.00 21.30  ? 271 SER A CB  1 
ATOM   1914 O OG  . SER A 1 242 ? 17.765  5.636   -7.012  1.00 21.96  ? 271 SER A OG  1 
ATOM   1915 N N   . ALA A 1 243 ? 19.321  7.588   -4.902  1.00 21.87  ? 272 ALA A N   1 
ATOM   1916 C CA  . ALA A 1 243 ? 20.604  8.215   -4.635  1.00 19.35  ? 272 ALA A CA  1 
ATOM   1917 C C   . ALA A 1 243 ? 20.577  8.894   -3.279  1.00 17.82  ? 272 ALA A C   1 
ATOM   1918 O O   . ALA A 1 243 ? 21.504  8.714   -2.492  1.00 18.01  ? 272 ALA A O   1 
ATOM   1919 C CB  . ALA A 1 243 ? 20.991  9.195   -5.686  1.00 21.51  ? 272 ALA A CB  1 
ATOM   1920 N N   . HIS A 1 244 ? 19.492  9.600   -2.990  1.00 16.52  ? 273 HIS A N   1 
ATOM   1921 C CA  . HIS A 1 244 ? 19.392  10.263  -1.704  1.00 17.88  ? 273 HIS A CA  1 
ATOM   1922 C C   . HIS A 1 244 ? 19.355  9.231   -0.560  1.00 17.93  ? 273 HIS A C   1 
ATOM   1923 O O   . HIS A 1 244 ? 19.923  9.499   0.494   1.00 18.07  ? 273 HIS A O   1 
ATOM   1924 C CB  . HIS A 1 244 ? 18.218  11.206  -1.683  1.00 17.95  ? 273 HIS A CB  1 
ATOM   1925 C CG  . HIS A 1 244 ? 18.063  12.043  -0.457  1.00 18.87  ? 273 HIS A CG  1 
ATOM   1926 N ND1 . HIS A 1 244 ? 16.891  12.704  -0.165  1.00 20.22  ? 273 HIS A ND1 1 
ATOM   1927 C CD2 . HIS A 1 244 ? 18.959  12.472  0.462   1.00 20.31  ? 273 HIS A CD2 1 
ATOM   1928 C CE1 . HIS A 1 244 ? 17.058  13.385  0.971   1.00 20.15  ? 273 HIS A CE1 1 
ATOM   1929 N NE2 . HIS A 1 244 ? 18.308  13.284  1.337   1.00 19.06  ? 273 HIS A NE2 1 
ATOM   1930 N N   . THR A 1 245 ? 18.593  8.112   -0.722  1.00 16.26  ? 274 THR A N   1 
ATOM   1931 C CA  . THR A 1 245 ? 18.500  7.133   0.355   1.00 16.49  ? 274 THR A CA  1 
ATOM   1932 C C   . THR A 1 245 ? 19.910  6.579   0.617   1.00 16.50  ? 274 THR A C   1 
ATOM   1933 O O   . THR A 1 245 ? 20.358  6.460   1.740   1.00 16.22  ? 274 THR A O   1 
ATOM   1934 C CB  . THR A 1 245 ? 17.480  6.057   -0.028  1.00 15.80  ? 274 THR A CB  1 
ATOM   1935 O OG1 . THR A 1 245 ? 16.193  6.651   -0.198  1.00 13.96  ? 274 THR A OG1 1 
ATOM   1936 C CG2 . THR A 1 245 ? 17.385  4.928   0.992   1.00 18.43  ? 274 THR A CG2 1 
ATOM   1937 N N   . SER A 1 246 ? 20.642  6.296   -0.457  1.00 17.81  ? 275 SER A N   1 
ATOM   1938 C CA  . SER A 1 246 ? 21.980  5.735   -0.355  1.00 19.04  ? 275 SER A CA  1 
ATOM   1939 C C   . SER A 1 246 ? 22.911  6.701   0.374   1.00 18.14  ? 275 SER A C   1 
ATOM   1940 O O   . SER A 1 246 ? 23.667  6.258   1.251   1.00 18.07  ? 275 SER A O   1 
ATOM   1941 C CB  . SER A 1 246 ? 22.540  5.293   -1.721  1.00 20.90  ? 275 SER A CB  1 
ATOM   1942 O OG  . SER A 1 246 ? 23.107  6.340   -2.491  1.00 27.46  ? 275 SER A OG  1 
ATOM   1943 N N   . HIS A 1 247 ? 22.767  7.994   0.057   1.00 18.52  ? 276 HIS A N   1 
ATOM   1944 C CA  . HIS A 1 247 ? 23.568  9.069   0.632   1.00 18.80  ? 276 HIS A CA  1 
ATOM   1945 C C   . HIS A 1 247 ? 23.288  9.215   2.122   1.00 18.67  ? 276 HIS A C   1 
ATOM   1946 O O   . HIS A 1 247 ? 24.190  9.414   2.958   1.00 17.99  ? 276 HIS A O   1 
ATOM   1947 C CB  . HIS A 1 247 ? 23.186  10.364  -0.078  1.00 23.87  ? 276 HIS A CB  1 
ATOM   1948 C CG  . HIS A 1 247 ? 24.032  11.540  0.217   1.00 26.18  ? 276 HIS A CG  1 
ATOM   1949 N ND1 . HIS A 1 247 ? 25.326  11.637  -0.266  1.00 25.15  ? 276 HIS A ND1 1 
ATOM   1950 C CD2 . HIS A 1 247 ? 23.786  12.667  0.917   1.00 23.85  ? 276 HIS A CD2 1 
ATOM   1951 C CE1 . HIS A 1 247 ? 25.829  12.795  0.134   1.00 28.72  ? 276 HIS A CE1 1 
ATOM   1952 N NE2 . HIS A 1 247 ? 24.931  13.436  0.860   1.00 24.84  ? 276 HIS A NE2 1 
ATOM   1953 N N   . LEU A 1 248 ? 21.993  9.230   2.438   1.00 16.74  ? 277 LEU A N   1 
ATOM   1954 C CA  . LEU A 1 248 ? 21.530  9.396   3.802   1.00 17.11  ? 277 LEU A CA  1 
ATOM   1955 C C   . LEU A 1 248 ? 21.960  8.227   4.693   1.00 17.24  ? 277 LEU A C   1 
ATOM   1956 O O   . LEU A 1 248 ? 22.531  8.420   5.767   1.00 17.66  ? 277 LEU A O   1 
ATOM   1957 C CB  . LEU A 1 248 ? 20.005  9.514   3.733   1.00 16.95  ? 277 LEU A CB  1 
ATOM   1958 C CG  . LEU A 1 248 ? 19.271  9.358   5.059   1.00 19.32  ? 277 LEU A CG  1 
ATOM   1959 C CD1 . LEU A 1 248 ? 19.718  10.462  6.054   1.00 20.89  ? 277 LEU A CD1 1 
ATOM   1960 C CD2 . LEU A 1 248 ? 17.781  9.455   4.813   1.00 20.87  ? 277 LEU A CD2 1 
ATOM   1961 N N   . VAL A 1 249 ? 21.694  6.992   4.254   1.00 16.48  ? 278 VAL A N   1 
ATOM   1962 C CA  . VAL A 1 249 ? 22.085  5.815   5.022   1.00 16.58  ? 278 VAL A CA  1 
ATOM   1963 C C   . VAL A 1 249 ? 23.611  5.700   5.100   1.00 17.80  ? 278 VAL A C   1 
ATOM   1964 O O   . VAL A 1 249 ? 24.162  5.470   6.176   1.00 17.09  ? 278 VAL A O   1 
ATOM   1965 C CB  . VAL A 1 249 ? 21.418  4.556   4.426   1.00 16.27  ? 278 VAL A CB  1 
ATOM   1966 C CG1 . VAL A 1 249 ? 22.024  3.237   4.953   1.00 17.12  ? 278 VAL A CG1 1 
ATOM   1967 C CG2 . VAL A 1 249 ? 19.907  4.604   4.680   1.00 17.42  ? 278 VAL A CG2 1 
ATOM   1968 N N   . GLY A 1 250 ? 24.286  5.891   3.983   1.00 15.53  ? 279 GLY A N   1 
ATOM   1969 C CA  . GLY A 1 250 ? 25.750  5.993   3.975   1.00 18.30  ? 279 GLY A CA  1 
ATOM   1970 C C   . GLY A 1 250 ? 26.346  6.996   4.966   1.00 16.93  ? 279 GLY A C   1 
ATOM   1971 O O   . GLY A 1 250 ? 27.431  6.766   5.523   1.00 16.67  ? 279 GLY A O   1 
ATOM   1972 N N   . SER A 1 251 ? 25.671  8.132   5.162   1.00 17.71  ? 280 SER A N   1 
ATOM   1973 C CA  . SER A 1 251 ? 26.177  9.219   5.989   1.00 18.37  ? 280 SER A CA  1 
ATOM   1974 C C   . SER A 1 251 ? 26.244  8.786   7.466   1.00 19.57  ? 280 SER A C   1 
ATOM   1975 O O   . SER A 1 251 ? 27.023  9.354   8.247   1.00 19.08  ? 280 SER A O   1 
ATOM   1976 C CB  . SER A 1 251 ? 25.322  10.491  5.858   1.00 17.83  ? 280 SER A CB  1 
ATOM   1977 O OG  . SER A 1 251 ? 24.104  10.365  6.603   1.00 18.17  ? 280 SER A OG  1 
ATOM   1978 N N   . ALA A 1 252 ? 25.478  7.772   7.850   1.00 18.11  ? 281 ALA A N   1 
ATOM   1979 C CA  . ALA A 1 252 ? 25.627  7.168   9.196   1.00 20.58  ? 281 ALA A CA  1 
ATOM   1980 C C   . ALA A 1 252 ? 26.716  6.086   9.290   1.00 18.90  ? 281 ALA A C   1 
ATOM   1981 O O   . ALA A 1 252 ? 26.879  5.436   10.329  1.00 17.41  ? 281 ALA A O   1 
ATOM   1982 C CB  . ALA A 1 252 ? 24.306  6.593   9.630   1.00 21.75  ? 281 ALA A CB  1 
ATOM   1983 N N   . LEU A 1 253 ? 27.487  5.916   8.210   1.00 20.19  ? 282 LEU A N   1 
ATOM   1984 C CA  . LEU A 1 253 ? 28.648  5.042   8.095   1.00 19.10  ? 282 LEU A CA  1 
ATOM   1985 C C   . LEU A 1 253 ? 28.211  3.592   7.947   1.00 19.67  ? 282 LEU A C   1 
ATOM   1986 O O   . LEU A 1 253 ? 28.979  2.660   8.124   1.00 19.83  ? 282 LEU A O   1 
ATOM   1987 C CB  . LEU A 1 253 ? 29.701  5.253   9.177   1.00 21.65  ? 282 LEU A CB  1 
ATOM   1988 C CG  . LEU A 1 253 ? 30.268  6.662   9.257   1.00 23.55  ? 282 LEU A CG  1 
ATOM   1989 C CD1 . LEU A 1 253 ? 31.399  6.677   10.281  1.00 25.38  ? 282 LEU A CD1 1 
ATOM   1990 C CD2 . LEU A 1 253 ? 30.714  7.136   7.894   1.00 26.20  ? 282 LEU A CD2 1 
ATOM   1991 N N   . SER A 1 254 ? 26.957  3.397   7.566   1.00 22.83  ? 283 SER A N   1 
ATOM   1992 C CA  . SER A 1 254 ? 26.550  2.094   7.080   1.00 20.17  ? 283 SER A CA  1 
ATOM   1993 C C   . SER A 1 254 ? 27.354  1.750   5.837   1.00 22.46  ? 283 SER A C   1 
ATOM   1994 O O   . SER A 1 254 ? 27.527  2.578   4.964   1.00 22.87  ? 283 SER A O   1 
ATOM   1995 C CB  . SER A 1 254 ? 25.072  2.106   6.773   1.00 23.53  ? 283 SER A CB  1 
ATOM   1996 O OG  . SER A 1 254 ? 24.315  2.223   7.970   1.00 23.32  ? 283 SER A OG  1 
ATOM   1997 N N   . ASP A 1 255 ? 27.710  0.468   5.710   1.00 22.51  ? 284 ASP A N   1 
ATOM   1998 C CA  . ASP A 1 255 ? 28.524  -0.000  4.621   1.00 22.12  ? 284 ASP A CA  1 
ATOM   1999 C C   . ASP A 1 255 ? 27.766  0.051   3.296   1.00 18.16  ? 284 ASP A C   1 
ATOM   2000 O O   . ASP A 1 255 ? 26.548  0.263   3.224   1.00 18.84  ? 284 ASP A O   1 
ATOM   2001 C CB  . ASP A 1 255 ? 29.082  -1.355  5.001   1.00 24.12  ? 284 ASP A CB  1 
ATOM   2002 C CG  . ASP A 1 255 ? 28.048  -2.454  5.037   1.00 26.33  ? 284 ASP A CG  1 
ATOM   2003 O OD1 . ASP A 1 255 ? 27.462  -2.709  3.954   1.00 27.45  ? 284 ASP A OD1 1 
ATOM   2004 O OD2 . ASP A 1 255 ? 27.828  -3.008  6.136   1.00 25.92  ? 284 ASP A OD2 1 
ATOM   2005 N N   . PRO A 1 256 ? 28.487  -0.063  2.156   1.00 18.45  ? 285 PRO A N   1 
ATOM   2006 C CA  . PRO A 1 256 ? 27.833  -0.017  0.837   1.00 17.20  ? 285 PRO A CA  1 
ATOM   2007 C C   . PRO A 1 256 ? 26.697  -1.014  0.596   1.00 16.56  ? 285 PRO A C   1 
ATOM   2008 O O   . PRO A 1 256 ? 25.715  -0.720  -0.086  1.00 16.90  ? 285 PRO A O   1 
ATOM   2009 C CB  . PRO A 1 256 ? 28.955  -0.280  -0.153  1.00 17.13  ? 285 PRO A CB  1 
ATOM   2010 C CG  . PRO A 1 256 ? 30.184  0.123   0.620   1.00 19.07  ? 285 PRO A CG  1 
ATOM   2011 C CD  . PRO A 1 256 ? 29.947  -0.236  2.088   1.00 17.31  ? 285 PRO A CD  1 
ATOM   2012 N N   . TYR A 1 257 ? 26.807  -2.207  1.174   1.00 17.09  ? 286 TYR A N   1 
ATOM   2013 C CA  . TYR A 1 257 ? 25.740  -3.192  1.058   1.00 18.60  ? 286 TYR A CA  1 
ATOM   2014 C C   . TYR A 1 257 ? 24.447  -2.657  1.712   1.00 17.26  ? 286 TYR A C   1 
ATOM   2015 O O   . TYR A 1 257 ? 23.396  -2.635  1.086   1.00 16.86  ? 286 TYR A O   1 
ATOM   2016 C CB  . TYR A 1 257 ? 26.136  -4.542  1.668   1.00 18.22  ? 286 TYR A CB  1 
ATOM   2017 C CG  . TYR A 1 257 ? 27.341  -5.192  1.018   1.00 21.39  ? 286 TYR A CG  1 
ATOM   2018 C CD1 . TYR A 1 257 ? 27.173  -6.018  -0.093  1.00 22.67  ? 286 TYR A CD1 1 
ATOM   2019 C CD2 . TYR A 1 257 ? 28.647  -4.970  1.471   1.00 23.83  ? 286 TYR A CD2 1 
ATOM   2020 C CE1 . TYR A 1 257 ? 28.253  -6.579  -0.761  1.00 21.17  ? 286 TYR A CE1 1 
ATOM   2021 C CE2 . TYR A 1 257 ? 29.734  -5.540  0.811   1.00 23.11  ? 286 TYR A CE2 1 
ATOM   2022 C CZ  . TYR A 1 257 ? 29.526  -6.369  -0.284  1.00 20.60  ? 286 TYR A CZ  1 
ATOM   2023 O OH  . TYR A 1 257 ? 30.538  -7.020  -0.920  1.00 20.09  ? 286 TYR A OH  1 
ATOM   2024 N N   . LEU A 1 258 ? 24.504  -2.180  2.966   1.00 17.54  ? 287 LEU A N   1 
ATOM   2025 C CA  . LEU A 1 258 ? 23.323  -1.618  3.606   1.00 18.92  ? 287 LEU A CA  1 
ATOM   2026 C C   . LEU A 1 258 ? 22.787  -0.356  2.901   1.00 18.16  ? 287 LEU A C   1 
ATOM   2027 O O   . LEU A 1 258 ? 21.575  -0.132  2.800   1.00 17.71  ? 287 LEU A O   1 
ATOM   2028 C CB  . LEU A 1 258 ? 23.691  -1.286  5.064   1.00 18.80  ? 287 LEU A CB  1 
ATOM   2029 C CG  . LEU A 1 258 ? 24.086  -2.508  5.899   1.00 20.82  ? 287 LEU A CG  1 
ATOM   2030 C CD1 . LEU A 1 258 ? 24.356  -2.075  7.328   1.00 21.42  ? 287 LEU A CD1 1 
ATOM   2031 C CD2 . LEU A 1 258 ? 23.078  -3.590  5.829   1.00 21.43  ? 287 LEU A CD2 1 
ATOM   2032 N N   . SER A 1 259 ? 23.696  0.504   2.471   1.00 17.36  ? 288 SER A N   1 
ATOM   2033 C CA  . SER A 1 259 ? 23.335  1.754   1.828   1.00 20.71  ? 288 SER A CA  1 
ATOM   2034 C C   . SER A 1 259 ? 22.593  1.437   0.531   1.00 18.34  ? 288 SER A C   1 
ATOM   2035 O O   . SER A 1 259 ? 21.579  2.066   0.207   1.00 18.17  ? 288 SER A O   1 
ATOM   2036 C CB  . SER A 1 259 ? 24.580  2.635   1.616   1.00 23.91  ? 288 SER A CB  1 
ATOM   2037 O OG  . SER A 1 259 ? 25.166  2.964   2.884   1.00 27.78  ? 288 SER A OG  1 
ATOM   2038 N N   . PHE A 1 260 ? 23.140  0.508   -0.239  1.00 18.88  ? 289 PHE A N   1 
ATOM   2039 C CA  . PHE A 1 260 ? 22.584  0.159   -1.534  1.00 18.05  ? 289 PHE A CA  1 
ATOM   2040 C C   . PHE A 1 260 ? 21.227  -0.532  -1.350  1.00 17.51  ? 289 PHE A C   1 
ATOM   2041 O O   . PHE A 1 260 ? 20.281  -0.233  -2.079  1.00 16.73  ? 289 PHE A O   1 
ATOM   2042 C CB  . PHE A 1 260 ? 23.541  -0.662  -2.388  1.00 18.71  ? 289 PHE A CB  1 
ATOM   2043 C CG  . PHE A 1 260 ? 22.989  -0.959  -3.771  1.00 20.15  ? 289 PHE A CG  1 
ATOM   2044 C CD1 . PHE A 1 260 ? 22.963  0.026   -4.750  1.00 24.61  ? 289 PHE A CD1 1 
ATOM   2045 C CD2 . PHE A 1 260 ? 22.545  -2.216  -4.107  1.00 20.32  ? 289 PHE A CD2 1 
ATOM   2046 C CE1 . PHE A 1 260 ? 22.428  -0.232  -5.995  1.00 23.96  ? 289 PHE A CE1 1 
ATOM   2047 C CE2 . PHE A 1 260 ? 21.983  -2.452  -5.340  1.00 21.38  ? 289 PHE A CE2 1 
ATOM   2048 C CZ  . PHE A 1 260 ? 21.982  -1.483  -6.295  1.00 21.25  ? 289 PHE A CZ  1 
ATOM   2049 N N   . ALA A 1 261 ? 21.106  -1.410  -0.345  1.00 17.09  ? 290 ALA A N   1 
ATOM   2050 C CA  . ALA A 1 261 ? 19.853  -2.157  -0.183  1.00 18.54  ? 290 ALA A CA  1 
ATOM   2051 C C   . ALA A 1 261 ? 18.760  -1.204  0.221   1.00 18.73  ? 290 ALA A C   1 
ATOM   2052 O O   . ALA A 1 261 ? 17.620  -1.360  -0.209  1.00 20.20  ? 290 ALA A O   1 
ATOM   2053 C CB  . ALA A 1 261 ? 19.994  -3.267  0.823   1.00 20.58  ? 290 ALA A CB  1 
ATOM   2054 N N   . ALA A 1 262 ? 19.093  -0.218  1.068   1.00 18.50  ? 291 ALA A N   1 
ATOM   2055 C CA  . ALA A 1 262 ? 18.130  0.818   1.437   1.00 18.93  ? 291 ALA A CA  1 
ATOM   2056 C C   . ALA A 1 262 ? 17.696  1.578   0.186   1.00 18.60  ? 291 ALA A C   1 
ATOM   2057 O O   . ALA A 1 262 ? 16.522  1.814   -0.008  1.00 17.74  ? 291 ALA A O   1 
ATOM   2058 C CB  . ALA A 1 262 ? 18.719  1.765   2.476   1.00 19.42  ? 291 ALA A CB  1 
ATOM   2059 N N   . ALA A 1 263 ? 18.664  1.933   -0.661  1.00 18.11  ? 292 ALA A N   1 
ATOM   2060 C CA  . ALA A 1 263 ? 18.393  2.620   -1.912  1.00 17.17  ? 292 ALA A CA  1 
ATOM   2061 C C   . ALA A 1 263 ? 17.419  1.836   -2.776  1.00 18.28  ? 292 ALA A C   1 
ATOM   2062 O O   . ALA A 1 263 ? 16.578  2.429   -3.437  1.00 18.90  ? 292 ALA A O   1 
ATOM   2063 C CB  . ALA A 1 263 ? 19.668  2.898   -2.670  1.00 16.71  ? 292 ALA A CB  1 
ATOM   2064 N N   . MET A 1 264 ? 17.588  0.512   -2.808  1.00 18.22  ? 293 MET A N   1 
ATOM   2065 C CA  . MET A 1 264 ? 16.707  -0.326  -3.617  1.00 19.25  ? 293 MET A CA  1 
ATOM   2066 C C   . MET A 1 264 ? 15.293  -0.292  -3.075  1.00 18.67  ? 293 MET A C   1 
ATOM   2067 O O   . MET A 1 264 ? 14.305  -0.328  -3.834  1.00 20.46  ? 293 MET A O   1 
ATOM   2068 C CB  . MET A 1 264 ? 17.207  -1.778  -3.742  1.00 18.92  ? 293 MET A CB  1 
ATOM   2069 C CG  . MET A 1 264 ? 18.512  -1.897  -4.529  1.00 20.25  ? 293 MET A CG  1 
ATOM   2070 S SD  . MET A 1 264 ? 18.486  -1.255  -6.232  1.00 22.85  ? 293 MET A SD  1 
ATOM   2071 C CE  . MET A 1 264 ? 18.858  0.478   -6.008  1.00 21.52  ? 293 MET A CE  1 
ATOM   2072 N N   . ASN A 1 265 ? 15.159  -0.284  -1.750  1.00 17.82  ? 294 ASN A N   1 
ATOM   2073 C CA  . ASN A 1 265 ? 13.799  -0.187  -1.201  1.00 18.65  ? 294 ASN A CA  1 
ATOM   2074 C C   . ASN A 1 265 ? 13.135  1.125   -1.625  1.00 19.80  ? 294 ASN A C   1 
ATOM   2075 O O   . ASN A 1 265 ? 11.920  1.197   -1.734  1.00 19.74  ? 294 ASN A O   1 
ATOM   2076 C CB  . ASN A 1 265 ? 13.828  -0.373  0.311   1.00 20.00  ? 294 ASN A CB  1 
ATOM   2077 C CG  . ASN A 1 265 ? 13.961  -1.843  0.671   1.00 21.69  ? 294 ASN A CG  1 
ATOM   2078 O OD1 . ASN A 1 265 ? 14.297  -2.658  -0.175  1.00 27.68  ? 294 ASN A OD1 1 
ATOM   2079 N ND2 . ASN A 1 265 ? 13.784  -2.203  1.917   1.00 23.05  ? 294 ASN A ND2 1 
ATOM   2080 N N   . GLY A 1 266 ? 13.924  2.211   -1.745  1.00 19.19  ? 295 GLY A N   1 
ATOM   2081 C CA  . GLY A 1 266 ? 13.442  3.451   -2.312  1.00 17.10  ? 295 GLY A CA  1 
ATOM   2082 C C   . GLY A 1 266 ? 13.098  3.317   -3.798  1.00 20.23  ? 295 GLY A C   1 
ATOM   2083 O O   . GLY A 1 266 ? 12.012  3.709   -4.239  1.00 18.85  ? 295 GLY A O   1 
ATOM   2084 N N   . LEU A 1 267 ? 13.981  2.669   -4.563  1.00 19.74  ? 296 LEU A N   1 
ATOM   2085 C CA  . LEU A 1 267 ? 13.766  2.500   -5.989  1.00 20.52  ? 296 LEU A CA  1 
ATOM   2086 C C   . LEU A 1 267 ? 12.490  1.707   -6.231  1.00 22.18  ? 296 LEU A C   1 
ATOM   2087 O O   . LEU A 1 267 ? 11.813  1.962   -7.213  1.00 23.58  ? 296 LEU A O   1 
ATOM   2088 C CB  . LEU A 1 267 ? 14.954  1.834   -6.676  1.00 23.39  ? 296 LEU A CB  1 
ATOM   2089 C CG  . LEU A 1 267 ? 14.938  1.842   -8.211  1.00 23.93  ? 296 LEU A CG  1 
ATOM   2090 C CD1 . LEU A 1 267 ? 14.951  3.276   -8.775  1.00 26.18  ? 296 LEU A CD1 1 
ATOM   2091 C CD2 . LEU A 1 267 ? 16.113  1.046   -8.731  1.00 23.82  ? 296 LEU A CD2 1 
ATOM   2092 N N   . ALA A 1 268 ? 12.168  0.783   -5.330  1.00 24.17  ? 297 ALA A N   1 
ATOM   2093 C CA  . ALA A 1 268 ? 11.027  -0.118  -5.477  1.00 21.16  ? 297 ALA A CA  1 
ATOM   2094 C C   . ALA A 1 268 ? 9.708   0.646   -5.339  1.00 22.89  ? 297 ALA A C   1 
ATOM   2095 O O   . ALA A 1 268 ? 8.673   0.130   -5.707  1.00 24.85  ? 297 ALA A O   1 
ATOM   2096 C CB  . ALA A 1 268 ? 11.109  -1.209  -4.435  1.00 20.93  ? 297 ALA A CB  1 
ATOM   2097 N N   . GLY A 1 269 ? 9.742   1.873   -4.814  1.00 22.30  ? 298 GLY A N   1 
ATOM   2098 C CA  . GLY A 1 269 ? 8.540   2.670   -4.673  1.00 23.38  ? 298 GLY A CA  1 
ATOM   2099 C C   . GLY A 1 269 ? 7.922   2.937   -6.044  1.00 23.37  ? 298 GLY A C   1 
ATOM   2100 O O   . GLY A 1 269 ? 8.635   3.238   -7.001  1.00 24.09  ? 298 GLY A O   1 
ATOM   2101 N N   . PRO A 1 270 ? 6.591   2.855   -6.180  1.00 23.94  ? 299 PRO A N   1 
ATOM   2102 C CA  . PRO A 1 270 ? 5.910   3.222   -7.419  1.00 28.38  ? 299 PRO A CA  1 
ATOM   2103 C C   . PRO A 1 270 ? 6.204   4.595   -8.031  1.00 29.45  ? 299 PRO A C   1 
ATOM   2104 O O   . PRO A 1 270 ? 6.345   4.702   -9.242  1.00 30.27  ? 299 PRO A O   1 
ATOM   2105 C CB  . PRO A 1 270 ? 4.394   3.099   -7.088  1.00 31.97  ? 299 PRO A CB  1 
ATOM   2106 C CG  . PRO A 1 270 ? 4.302   2.253   -5.848  1.00 28.63  ? 299 PRO A CG  1 
ATOM   2107 C CD  . PRO A 1 270 ? 5.664   2.347   -5.164  1.00 28.04  ? 299 PRO A CD  1 
ATOM   2108 N N   . LEU A 1 271 ? 6.354   5.629   -7.205  1.00 28.58  ? 300 LEU A N   1 
ATOM   2109 C CA  . LEU A 1 271 ? 6.747   6.951   -7.691  1.00 30.52  ? 300 LEU A CA  1 
ATOM   2110 C C   . LEU A 1 271 ? 8.224   7.089   -8.097  1.00 33.26  ? 300 LEU A C   1 
ATOM   2111 O O   . LEU A 1 271 ? 8.636   8.204   -8.392  1.00 36.75  ? 300 LEU A O   1 
ATOM   2112 C CB  . LEU A 1 271 ? 6.424   7.979   -6.611  1.00 26.17  ? 300 LEU A CB  1 
ATOM   2113 C CG  . LEU A 1 271 ? 4.969   8.066   -6.173  1.00 25.18  ? 300 LEU A CG  1 
ATOM   2114 C CD1 . LEU A 1 271 ? 4.800   9.243   -5.212  1.00 29.59  ? 300 LEU A CD1 1 
ATOM   2115 C CD2 . LEU A 1 271 ? 4.078   8.218   -7.415  1.00 30.99  ? 300 LEU A CD2 1 
ATOM   2116 N N   . HIS A 1 272 ? 9.047   6.039   -8.024  1.00 34.79  ? 301 HIS A N   1 
ATOM   2117 C CA  . HIS A 1 272 ? 10.475  6.188   -8.337  1.00 36.10  ? 301 HIS A CA  1 
ATOM   2118 C C   . HIS A 1 272 ? 10.923  5.221   -9.439  1.00 37.50  ? 301 HIS A C   1 
ATOM   2119 O O   . HIS A 1 272 ? 11.622  5.644   -10.362 1.00 43.06  ? 301 HIS A O   1 
ATOM   2120 C CB  . HIS A 1 272 ? 11.393  6.043   -7.102  1.00 37.43  ? 301 HIS A CB  1 
ATOM   2121 C CG  . HIS A 1 272 ? 12.850  6.311   -7.397  1.00 35.04  ? 301 HIS A CG  1 
ATOM   2122 N ND1 . HIS A 1 272 ? 13.226  6.925   -8.566  1.00 31.73  ? 301 HIS A ND1 1 
ATOM   2123 C CD2 . HIS A 1 272 ? 14.018  6.031   -6.754  1.00 34.57  ? 301 HIS A CD2 1 
ATOM   2124 C CE1 . HIS A 1 272 ? 14.571  7.069   -8.596  1.00 38.35  ? 301 HIS A CE1 1 
ATOM   2125 N NE2 . HIS A 1 272 ? 15.087  6.519   -7.532  1.00 31.30  ? 301 HIS A NE2 1 
ATOM   2126 N N   . GLY A 1 273 ? 10.559  3.932   -9.340  1.00 37.60  ? 302 GLY A N   1 
ATOM   2127 C CA  . GLY A 1 273 ? 11.154  2.938   -10.215 1.00 36.82  ? 302 GLY A CA  1 
ATOM   2128 C C   . GLY A 1 273 ? 10.157  2.020   -10.914 1.00 36.97  ? 302 GLY A C   1 
ATOM   2129 O O   . GLY A 1 273 ? 10.600  1.040   -11.492 1.00 44.49  ? 302 GLY A O   1 
ATOM   2130 N N   . LEU A 1 274 ? 8.843   2.302   -10.885 1.00 39.55  ? 303 LEU A N   1 
ATOM   2131 C CA  . LEU A 1 274 ? 7.853   1.450   -11.539 1.00 40.32  ? 303 LEU A CA  1 
ATOM   2132 C C   . LEU A 1 274 ? 7.259   2.098   -12.798 1.00 43.04  ? 303 LEU A C   1 
ATOM   2133 O O   . LEU A 1 274 ? 6.312   1.562   -13.367 1.00 41.49  ? 303 LEU A O   1 
ATOM   2134 C CB  . LEU A 1 274 ? 6.732   1.063   -10.582 1.00 48.93  ? 303 LEU A CB  1 
ATOM   2135 C CG  . LEU A 1 274 ? 6.955   -0.236  -9.795  1.00 56.02  ? 303 LEU A CG  1 
ATOM   2136 C CD1 . LEU A 1 274 ? 8.280   -0.259  -9.027  1.00 52.96  ? 303 LEU A CD1 1 
ATOM   2137 C CD2 . LEU A 1 274 ? 5.793   -0.478  -8.856  1.00 57.54  ? 303 LEU A CD2 1 
ATOM   2138 N N   . ALA A 1 275 ? 7.843   3.205   -13.273 1.00 38.40  ? 304 ALA A N   1 
ATOM   2139 C CA  . ALA A 1 275 ? 7.283   3.944   -14.395 1.00 37.64  ? 304 ALA A CA  1 
ATOM   2140 C C   . ALA A 1 275 ? 7.360   3.129   -15.696 1.00 38.98  ? 304 ALA A C   1 
ATOM   2141 O O   . ALA A 1 275 ? 6.407   3.107   -16.465 1.00 41.72  ? 304 ALA A O   1 
ATOM   2142 C CB  . ALA A 1 275 ? 8.009   5.264   -14.524 1.00 38.07  ? 304 ALA A CB  1 
ATOM   2143 N N   . ASN A 1 276 ? 8.525   2.518   -15.959 1.00 34.22  ? 305 ASN A N   1 
ATOM   2144 C CA  . ASN A 1 276 ? 8.748   1.603   -17.072 1.00 36.58  ? 305 ASN A CA  1 
ATOM   2145 C C   . ASN A 1 276 ? 7.551   0.673   -17.307 1.00 33.09  ? 305 ASN A C   1 
ATOM   2146 O O   . ASN A 1 276 ? 6.988   0.608   -18.396 1.00 35.77  ? 305 ASN A O   1 
ATOM   2147 C CB  . ASN A 1 276 ? 10.017  0.794   -16.815 1.00 37.92  ? 305 ASN A CB  1 
ATOM   2148 C CG  . ASN A 1 276 ? 10.365  -0.118  -17.966 1.00 43.34  ? 305 ASN A CG  1 
ATOM   2149 O OD1 . ASN A 1 276 ? 9.506   -0.446  -18.810 1.00 40.19  ? 305 ASN A OD1 1 
ATOM   2150 N ND2 . ASN A 1 276 ? 11.630  -0.518  -18.009 1.00 36.42  ? 305 ASN A ND2 1 
ATOM   2151 N N   . GLN A 1 277 ? 7.175   -0.055  -16.263 1.00 32.96  ? 306 GLN A N   1 
ATOM   2152 C CA  . GLN A 1 277 ? 6.071   -0.997  -16.260 1.00 35.99  ? 306 GLN A CA  1 
ATOM   2153 C C   . GLN A 1 277 ? 4.756   -0.276  -16.539 1.00 36.61  ? 306 GLN A C   1 
ATOM   2154 O O   . GLN A 1 277 ? 3.939   -0.773  -17.302 1.00 34.75  ? 306 GLN A O   1 
ATOM   2155 C CB  . GLN A 1 277 ? 5.949   -1.678  -14.883 1.00 38.18  ? 306 GLN A CB  1 
ATOM   2156 C CG  . GLN A 1 277 ? 7.107   -2.613  -14.549 1.00 44.02  ? 306 GLN A CG  1 
ATOM   2157 C CD  . GLN A 1 277 ? 8.270   -1.933  -13.836 1.00 47.75  ? 306 GLN A CD  1 
ATOM   2158 O OE1 . GLN A 1 277 ? 8.568   -0.755  -14.058 1.00 36.96  ? 306 GLN A OE1 1 
ATOM   2159 N NE2 . GLN A 1 277 ? 8.932   -2.667  -12.943 1.00 45.86  ? 306 GLN A NE2 1 
ATOM   2160 N N   . GLU A 1 278 ? 4.537   0.870   -15.873 1.00 40.55  ? 307 GLU A N   1 
ATOM   2161 C CA  . GLU A 1 278 ? 3.298   1.625   -16.017 1.00 45.09  ? 307 GLU A CA  1 
ATOM   2162 C C   . GLU A 1 278 ? 3.137   2.079   -17.468 1.00 39.55  ? 307 GLU A C   1 
ATOM   2163 O O   . GLU A 1 278 ? 2.025   2.069   -17.997 1.00 40.17  ? 307 GLU A O   1 
ATOM   2164 C CB  . GLU A 1 278 ? 3.231   2.854   -15.103 1.00 49.90  ? 307 GLU A CB  1 
ATOM   2165 C CG  . GLU A 1 278 ? 2.837   2.502   -13.672 1.00 61.58  ? 307 GLU A CG  1 
ATOM   2166 C CD  . GLU A 1 278 ? 2.328   3.633   -12.788 1.00 72.31  ? 307 GLU A CD  1 
ATOM   2167 O OE1 . GLU A 1 278 ? 1.446   4.424   -13.219 1.00 76.88  ? 307 GLU A OE1 1 
ATOM   2168 O OE2 . GLU A 1 278 ? 2.796   3.680   -11.626 1.00 69.48  ? 307 GLU A OE2 1 
ATOM   2169 N N   . VAL A 1 279 ? 4.240   2.521   -18.073 1.00 29.48  ? 308 VAL A N   1 
ATOM   2170 C CA  . VAL A 1 279 ? 4.252   2.871   -19.490 1.00 33.36  ? 308 VAL A CA  1 
ATOM   2171 C C   . VAL A 1 279 ? 3.816   1.663   -20.313 1.00 31.72  ? 308 VAL A C   1 
ATOM   2172 O O   . VAL A 1 279 ? 2.836   1.715   -21.025 1.00 34.42  ? 308 VAL A O   1 
ATOM   2173 C CB  . VAL A 1 279 ? 5.607   3.406   -19.990 1.00 30.23  ? 308 VAL A CB  1 
ATOM   2174 C CG1 . VAL A 1 279 ? 5.644   3.555   -21.514 1.00 30.12  ? 308 VAL A CG1 1 
ATOM   2175 C CG2 . VAL A 1 279 ? 5.908   4.763   -19.388 1.00 33.77  ? 308 VAL A CG2 1 
ATOM   2176 N N   . LEU A 1 280 ? 4.547   0.557   -20.171 1.00 34.12  ? 309 LEU A N   1 
ATOM   2177 C CA  . LEU A 1 280 ? 4.332   -0.611  -21.004 1.00 38.02  ? 309 LEU A CA  1 
ATOM   2178 C C   . LEU A 1 280 ? 2.911   -1.170  -20.841 1.00 37.50  ? 309 LEU A C   1 
ATOM   2179 O O   . LEU A 1 280 ? 2.301   -1.609  -21.808 1.00 39.55  ? 309 LEU A O   1 
ATOM   2180 C CB  . LEU A 1 280 ? 5.426   -1.633  -20.698 1.00 35.94  ? 309 LEU A CB  1 
ATOM   2181 C CG  . LEU A 1 280 ? 5.470   -2.866  -21.604 1.00 44.01  ? 309 LEU A CG  1 
ATOM   2182 C CD1 . LEU A 1 280 ? 5.548   -2.464  -23.083 1.00 40.18  ? 309 LEU A CD1 1 
ATOM   2183 C CD2 . LEU A 1 280 ? 6.630   -3.785  -21.210 1.00 45.09  ? 309 LEU A CD2 1 
ATOM   2184 N N   . VAL A 1 281 ? 2.338   -1.109  -19.645 1.00 35.37  ? 310 VAL A N   1 
ATOM   2185 C CA  . VAL A 1 281 ? 0.973   -1.585  -19.457 1.00 40.44  ? 310 VAL A CA  1 
ATOM   2186 C C   . VAL A 1 281 ? -0.006  -0.660  -20.194 1.00 43.19  ? 310 VAL A C   1 
ATOM   2187 O O   . VAL A 1 281 ? -0.991  -1.112  -20.796 1.00 45.75  ? 310 VAL A O   1 
ATOM   2188 C CB  . VAL A 1 281 ? 0.616   -1.719  -17.961 1.00 41.11  ? 310 VAL A CB  1 
ATOM   2189 C CG1 . VAL A 1 281 ? -0.830  -2.149  -17.770 1.00 42.52  ? 310 VAL A CG1 1 
ATOM   2190 C CG2 . VAL A 1 281 ? 1.533   -2.684  -17.222 1.00 38.25  ? 310 VAL A CG2 1 
ATOM   2191 N N   . TRP A 1 282 ? 0.281   0.644   -20.179 1.00 37.32  ? 311 TRP A N   1 
ATOM   2192 C CA  . TRP A 1 282 ? -0.577  1.618   -20.846 1.00 39.45  ? 311 TRP A CA  1 
ATOM   2193 C C   . TRP A 1 282 ? -0.528  1.457   -22.379 1.00 43.82  ? 311 TRP A C   1 
ATOM   2194 O O   . TRP A 1 282 ? -1.562  1.464   -23.055 1.00 40.99  ? 311 TRP A O   1 
ATOM   2195 C CB  . TRP A 1 282 ? -0.150  3.019   -20.387 1.00 42.09  ? 311 TRP A CB  1 
ATOM   2196 C CG  . TRP A 1 282 ? -0.957  4.153   -20.951 1.00 47.99  ? 311 TRP A CG  1 
ATOM   2197 C CD1 . TRP A 1 282 ? -2.145  4.644   -20.489 1.00 48.47  ? 311 TRP A CD1 1 
ATOM   2198 C CD2 . TRP A 1 282 ? -0.607  4.953   -22.096 1.00 48.92  ? 311 TRP A CD2 1 
ATOM   2199 N NE1 . TRP A 1 282 ? -2.543  5.704   -21.261 1.00 44.34  ? 311 TRP A NE1 1 
ATOM   2200 C CE2 . TRP A 1 282 ? -1.629  5.912   -22.254 1.00 52.72  ? 311 TRP A CE2 1 
ATOM   2201 C CE3 . TRP A 1 282 ? 0.462   4.959   -22.990 1.00 52.62  ? 311 TRP A CE3 1 
ATOM   2202 C CZ2 . TRP A 1 282 ? -1.612  6.858   -23.273 1.00 57.89  ? 311 TRP A CZ2 1 
ATOM   2203 C CZ3 . TRP A 1 282 ? 0.472   5.886   -24.004 1.00 52.86  ? 311 TRP A CZ3 1 
ATOM   2204 C CH2 . TRP A 1 282 ? -0.541  6.832   -24.133 1.00 56.79  ? 311 TRP A CH2 1 
ATOM   2205 N N   . LEU A 1 283 ? 0.685   1.317   -22.930 1.00 41.55  ? 312 LEU A N   1 
ATOM   2206 C CA  . LEU A 1 283 ? 0.890   1.129   -24.359 1.00 43.69  ? 312 LEU A CA  1 
ATOM   2207 C C   . LEU A 1 283 ? 0.150   -0.117  -24.846 1.00 53.83  ? 312 LEU A C   1 
ATOM   2208 O O   . LEU A 1 283 ? -0.465  -0.108  -25.913 1.00 45.77  ? 312 LEU A O   1 
ATOM   2209 C CB  . LEU A 1 283 ? 2.377   0.988   -24.681 1.00 42.50  ? 312 LEU A CB  1 
ATOM   2210 C CG  . LEU A 1 283 ? 3.259   2.224   -24.445 1.00 42.70  ? 312 LEU A CG  1 
ATOM   2211 C CD1 . LEU A 1 283 ? 4.720   1.830   -24.654 1.00 39.04  ? 312 LEU A CD1 1 
ATOM   2212 C CD2 . LEU A 1 283 ? 2.886   3.392   -25.334 1.00 41.53  ? 312 LEU A CD2 1 
ATOM   2213 N N   . THR A 1 284 ? 0.294   -1.220  -24.100 1.00 55.86  ? 313 THR A N   1 
ATOM   2214 C CA  . THR A 1 284 ? -0.306  -2.477  -24.498 1.00 48.01  ? 313 THR A CA  1 
ATOM   2215 C C   . THR A 1 284 ? -1.816  -2.255  -24.562 1.00 53.37  ? 313 THR A C   1 
ATOM   2216 O O   . THR A 1 284 ? -2.432  -2.544  -25.581 1.00 60.64  ? 313 THR A O   1 
ATOM   2217 C CB  . THR A 1 284 ? 0.117   -3.592  -23.537 1.00 49.04  ? 313 THR A CB  1 
ATOM   2218 O OG1 . THR A 1 284 ? 1.542   -3.544  -23.410 1.00 43.14  ? 313 THR A OG1 1 
ATOM   2219 C CG2 . THR A 1 284 ? -0.267  -4.972  -24.046 1.00 47.73  ? 313 THR A CG2 1 
ATOM   2220 N N   . GLN A 1 285 ? -2.388  -1.689  -23.489 1.00 56.40  ? 314 GLN A N   1 
ATOM   2221 C CA  . GLN A 1 285 ? -3.812  -1.392  -23.429 1.00 64.05  ? 314 GLN A CA  1 
ATOM   2222 C C   . GLN A 1 285 ? -4.208  -0.573  -24.656 1.00 65.31  ? 314 GLN A C   1 
ATOM   2223 O O   . GLN A 1 285 ? -5.131  -0.947  -25.376 1.00 67.51  ? 314 GLN A O   1 
ATOM   2224 C CB  . GLN A 1 285 ? -4.144  -0.668  -22.124 1.00 63.49  ? 314 GLN A CB  1 
ATOM   2225 C CG  . GLN A 1 285 ? -5.569  -0.127  -22.033 1.00 72.65  ? 314 GLN A CG  1 
ATOM   2226 C CD  . GLN A 1 285 ? -6.608  -1.193  -21.740 1.00 85.58  ? 314 GLN A CD  1 
ATOM   2227 O OE1 . GLN A 1 285 ? -7.230  -1.202  -20.671 1.00 86.14  ? 314 GLN A OE1 1 
ATOM   2228 N NE2 . GLN A 1 285 ? -6.813  -2.105  -22.682 1.00 84.29  ? 314 GLN A NE2 1 
ATOM   2229 N N   . LEU A 1 286 ? -3.477  0.526   -24.891 1.00 63.61  ? 315 LEU A N   1 
ATOM   2230 C CA  . LEU A 1 286 ? -3.702  1.412   -26.025 1.00 58.76  ? 315 LEU A CA  1 
ATOM   2231 C C   . LEU A 1 286 ? -3.762  0.620   -27.332 1.00 59.06  ? 315 LEU A C   1 
ATOM   2232 O O   . LEU A 1 286 ? -4.648  0.842   -28.165 1.00 50.53  ? 315 LEU A O   1 
ATOM   2233 C CB  . LEU A 1 286 ? -2.611  2.485   -26.066 1.00 52.28  ? 315 LEU A CB  1 
ATOM   2234 C CG  . LEU A 1 286 ? -2.624  3.424   -27.277 1.00 53.12  ? 315 LEU A CG  1 
ATOM   2235 C CD1 . LEU A 1 286 ? -4.014  3.949   -27.588 1.00 58.71  ? 315 LEU A CD1 1 
ATOM   2236 C CD2 . LEU A 1 286 ? -1.687  4.594   -27.054 1.00 51.71  ? 315 LEU A CD2 1 
ATOM   2237 N N   . GLN A 1 287 ? -2.808  -0.295  -27.523 1.00 58.30  ? 316 GLN A N   1 
ATOM   2238 C CA  . GLN A 1 287 ? -2.671  -0.940  -28.815 1.00 59.89  ? 316 GLN A CA  1 
ATOM   2239 C C   . GLN A 1 287 ? -3.719  -2.042  -28.983 1.00 64.71  ? 316 GLN A C   1 
ATOM   2240 O O   . GLN A 1 287 ? -3.894  -2.526  -30.102 1.00 55.16  ? 316 GLN A O   1 
ATOM   2241 C CB  . GLN A 1 287 ? -1.260  -1.446  -29.100 1.00 60.45  ? 316 GLN A CB  1 
ATOM   2242 C CG  . GLN A 1 287 ? -0.870  -1.220  -30.557 1.00 64.65  ? 316 GLN A CG  1 
ATOM   2243 C CD  . GLN A 1 287 ? 0.459   -1.809  -30.964 1.00 67.17  ? 316 GLN A CD  1 
ATOM   2244 O OE1 . GLN A 1 287 ? 1.050   -1.412  -31.978 1.00 72.42  ? 316 GLN A OE1 1 
ATOM   2245 N NE2 . GLN A 1 287 ? 0.937   -2.762  -30.180 1.00 66.59  ? 316 GLN A NE2 1 
ATOM   2246 N N   . LYS A 1 288 ? -4.405  -2.432  -27.896 1.00 63.51  ? 317 LYS A N   1 
ATOM   2247 C CA  . LYS A 1 288 ? -5.612  -3.238  -28.022 1.00 72.20  ? 317 LYS A CA  1 
ATOM   2248 C C   . LYS A 1 288 ? -6.748  -2.357  -28.537 1.00 71.29  ? 317 LYS A C   1 
ATOM   2249 O O   . LYS A 1 288 ? -7.317  -2.640  -29.588 1.00 73.58  ? 317 LYS A O   1 
ATOM   2250 C CB  . LYS A 1 288 ? -6.091  -3.930  -26.737 1.00 79.05  ? 317 LYS A CB  1 
ATOM   2251 C CG  . LYS A 1 288 ? -5.564  -5.346  -26.492 1.00 85.41  ? 317 LYS A CG  1 
ATOM   2252 C CD  . LYS A 1 288 ? -4.406  -5.471  -25.504 1.00 97.17  ? 317 LYS A CD  1 
ATOM   2253 C CE  . LYS A 1 288 ? -4.834  -5.223  -24.081 1.00 107.32 ? 317 LYS A CE  1 
ATOM   2254 N NZ  . LYS A 1 288 ? -3.722  -5.199  -23.124 1.00 103.75 ? 317 LYS A NZ  1 
ATOM   2255 N N   . GLU A 1 289 ? -7.051  -1.287  -27.788 1.00 72.88  ? 318 GLU A N   1 
ATOM   2256 C CA  . GLU A 1 289 ? -8.233  -0.464  -28.008 1.00 75.32  ? 318 GLU A CA  1 
ATOM   2257 C C   . GLU A 1 289 ? -8.247  0.168   -29.401 1.00 80.71  ? 318 GLU A C   1 
ATOM   2258 O O   . GLU A 1 289 ? -9.279  0.134   -30.064 1.00 80.44  ? 318 GLU A O   1 
ATOM   2259 C CB  . GLU A 1 289 ? -8.340  0.656   -26.975 1.00 72.78  ? 318 GLU A CB  1 
ATOM   2260 C CG  . GLU A 1 289 ? -8.473  0.133   -25.549 1.00 72.03  ? 318 GLU A CG  1 
ATOM   2261 C CD  . GLU A 1 289 ? -8.800  1.203   -24.528 1.00 74.78  ? 318 GLU A CD  1 
ATOM   2262 O OE1 . GLU A 1 289 ? -9.360  2.245   -24.927 1.00 75.62  ? 318 GLU A OE1 1 
ATOM   2263 O OE2 . GLU A 1 289 ? -8.457  1.004   -23.343 1.00 79.11  ? 318 GLU A OE2 1 
ATOM   2264 N N   . VAL A 1 290 ? -7.120  0.755   -29.833 1.00 83.90  ? 319 VAL A N   1 
ATOM   2265 C CA  . VAL A 1 290 ? -7.069  1.503   -31.085 1.00 80.40  ? 319 VAL A CA  1 
ATOM   2266 C C   . VAL A 1 290 ? -6.424  0.679   -32.203 1.00 85.21  ? 319 VAL A C   1 
ATOM   2267 O O   . VAL A 1 290 ? -6.257  1.199   -33.305 1.00 88.27  ? 319 VAL A O   1 
ATOM   2268 C CB  . VAL A 1 290 ? -6.339  2.855   -30.963 1.00 76.84  ? 319 VAL A CB  1 
ATOM   2269 C CG1 . VAL A 1 290 ? -6.860  3.685   -29.795 1.00 76.18  ? 319 VAL A CG1 1 
ATOM   2270 C CG2 . VAL A 1 290 ? -4.823  2.687   -30.881 1.00 83.24  ? 319 VAL A CG2 1 
ATOM   2271 N N   . GLY A 1 291 ? -6.025  -0.573  -31.929 1.00 94.10  ? 320 GLY A N   1 
ATOM   2272 C CA  . GLY A 1 291 ? -5.506  -1.462  -32.968 1.00 95.45  ? 320 GLY A CA  1 
ATOM   2273 C C   . GLY A 1 291 ? -4.016  -1.247  -33.248 1.00 96.31  ? 320 GLY A C   1 
ATOM   2274 O O   . GLY A 1 291 ? -3.382  -0.413  -32.606 1.00 101.82 ? 320 GLY A O   1 
ATOM   2275 N N   . LYS A 1 292 ? -3.472  -1.990  -34.231 1.00 98.29  ? 321 LYS A N   1 
ATOM   2276 C CA  . LYS A 1 292 ? -2.029  -2.109  -34.446 1.00 95.59  ? 321 LYS A CA  1 
ATOM   2277 C C   . LYS A 1 292 ? -1.465  -0.917  -35.223 1.00 93.30  ? 321 LYS A C   1 
ATOM   2278 O O   . LYS A 1 292 ? -0.634  -0.176  -34.702 1.00 101.28 ? 321 LYS A O   1 
ATOM   2279 C CB  . LYS A 1 292 ? -1.659  -3.401  -35.189 1.00 91.78  ? 321 LYS A CB  1 
ATOM   2280 N N   . ASP A 1 293 ? -1.876  -0.773  -36.489 1.00 96.89  ? 322 ASP A N   1 
ATOM   2281 C CA  . ASP A 1 293 ? -1.442  0.331   -37.334 1.00 99.41  ? 322 ASP A CA  1 
ATOM   2282 C C   . ASP A 1 293 ? -2.474  1.456   -37.242 1.00 91.49  ? 322 ASP A C   1 
ATOM   2283 O O   . ASP A 1 293 ? -3.287  1.632   -38.145 1.00 92.85  ? 322 ASP A O   1 
ATOM   2284 C CB  . ASP A 1 293 ? -1.226  -0.123  -38.774 1.00 106.75 ? 322 ASP A CB  1 
ATOM   2285 C CG  . ASP A 1 293 ? -0.470  -1.435  -38.973 1.00 110.33 ? 322 ASP A CG  1 
ATOM   2286 O OD1 . ASP A 1 293 ? -1.004  -2.495  -38.571 1.00 106.51 ? 322 ASP A OD1 1 
ATOM   2287 O OD2 . ASP A 1 293 ? 0.643   -1.396  -39.545 1.00 108.89 ? 322 ASP A OD2 1 
ATOM   2288 N N   . VAL A 1 294 ? -2.446  2.192   -36.124 1.00 84.69  ? 323 VAL A N   1 
ATOM   2289 C CA  . VAL A 1 294 ? -3.333  3.323   -35.890 1.00 79.55  ? 323 VAL A CA  1 
ATOM   2290 C C   . VAL A 1 294 ? -2.826  4.496   -36.726 1.00 76.24  ? 323 VAL A C   1 
ATOM   2291 O O   . VAL A 1 294 ? -1.661  4.510   -37.116 1.00 80.11  ? 323 VAL A O   1 
ATOM   2292 C CB  . VAL A 1 294 ? -3.403  3.663   -34.380 1.00 76.51  ? 323 VAL A CB  1 
ATOM   2293 C CG1 . VAL A 1 294 ? -2.055  4.098   -33.796 1.00 71.71  ? 323 VAL A CG1 1 
ATOM   2294 C CG2 . VAL A 1 294 ? -4.472  4.703   -34.060 1.00 70.39  ? 323 VAL A CG2 1 
ATOM   2295 N N   . SER A 1 295 ? -3.709  5.462   -37.009 1.00 77.53  ? 324 SER A N   1 
ATOM   2296 C CA  . SER A 1 295 ? -3.341  6.684   -37.712 1.00 74.81  ? 324 SER A CA  1 
ATOM   2297 C C   . SER A 1 295 ? -3.097  7.796   -36.694 1.00 68.61  ? 324 SER A C   1 
ATOM   2298 O O   . SER A 1 295 ? -3.624  7.749   -35.584 1.00 69.58  ? 324 SER A O   1 
ATOM   2299 C CB  . SER A 1 295 ? -4.404  7.083   -38.721 1.00 76.48  ? 324 SER A CB  1 
ATOM   2300 O OG  . SER A 1 295 ? -5.544  7.649   -38.085 1.00 74.78  ? 324 SER A OG  1 
ATOM   2301 N N   . ASP A 1 296 ? -2.322  8.813   -37.085 1.00 66.66  ? 325 ASP A N   1 
ATOM   2302 C CA  . ASP A 1 296 ? -2.006  9.924   -36.193 1.00 68.97  ? 325 ASP A CA  1 
ATOM   2303 C C   . ASP A 1 296 ? -3.291  10.522  -35.624 1.00 70.64  ? 325 ASP A C   1 
ATOM   2304 O O   . ASP A 1 296 ? -3.367  10.861  -34.442 1.00 63.49  ? 325 ASP A O   1 
ATOM   2305 C CB  . ASP A 1 296 ? -1.167  10.979  -36.897 1.00 72.76  ? 325 ASP A CB  1 
ATOM   2306 C CG  . ASP A 1 296 ? 0.321   10.672  -36.981 1.00 80.43  ? 325 ASP A CG  1 
ATOM   2307 O OD1 . ASP A 1 296 ? 0.940   10.509  -35.910 1.00 89.25  ? 325 ASP A OD1 1 
ATOM   2308 O OD2 . ASP A 1 296 ? 0.848   10.603  -38.110 1.00 79.19  ? 325 ASP A OD2 1 
ATOM   2309 N N   . GLU A 1 297 ? -4.290  10.646  -36.506 1.00 73.99  ? 326 GLU A N   1 
ATOM   2310 C CA  . GLU A 1 297 ? -5.587  11.224  -36.197 1.00 69.39  ? 326 GLU A CA  1 
ATOM   2311 C C   . GLU A 1 297 ? -6.212  10.484  -35.015 1.00 61.34  ? 326 GLU A C   1 
ATOM   2312 O O   . GLU A 1 297 ? -6.512  11.076  -33.975 1.00 52.55  ? 326 GLU A O   1 
ATOM   2313 C CB  . GLU A 1 297 ? -6.384  11.143  -37.505 1.00 75.25  ? 326 GLU A CB  1 
ATOM   2314 C CG  . GLU A 1 297 ? -7.723  11.879  -37.504 1.00 79.11  ? 326 GLU A CG  1 
ATOM   2315 C CD  . GLU A 1 297 ? -8.395  11.920  -38.872 1.00 85.61  ? 326 GLU A CD  1 
ATOM   2316 O OE1 . GLU A 1 297 ? -9.432  12.611  -39.006 1.00 78.87  ? 326 GLU A OE1 1 
ATOM   2317 O OE2 . GLU A 1 297 ? -7.885  11.266  -39.814 1.00 86.28  ? 326 GLU A OE2 1 
ATOM   2318 N N   . LYS A 1 298 ? -6.379  9.169   -35.185 1.00 63.93  ? 327 LYS A N   1 
ATOM   2319 C CA  . LYS A 1 298 ? -7.033  8.344   -34.185 1.00 66.48  ? 327 LYS A CA  1 
ATOM   2320 C C   . LYS A 1 298 ? -6.199  8.312   -32.904 1.00 68.83  ? 327 LYS A C   1 
ATOM   2321 O O   . LYS A 1 298 ? -6.757  8.247   -31.807 1.00 63.98  ? 327 LYS A O   1 
ATOM   2322 C CB  . LYS A 1 298 ? -7.224  6.915   -34.700 1.00 75.55  ? 327 LYS A CB  1 
ATOM   2323 C CG  . LYS A 1 298 ? -7.892  6.753   -36.066 1.00 85.67  ? 327 LYS A CG  1 
ATOM   2324 C CD  . LYS A 1 298 ? -7.684  5.376   -36.691 1.00 85.00  ? 327 LYS A CD  1 
ATOM   2325 C CE  . LYS A 1 298 ? -8.132  4.272   -35.777 1.00 87.81  ? 327 LYS A CE  1 
ATOM   2326 N NZ  . LYS A 1 298 ? -7.795  2.956   -36.317 1.00 85.44  ? 327 LYS A NZ  1 
ATOM   2327 N N   . LEU A 1 299 ? -4.864  8.352   -33.049 1.00 63.24  ? 328 LEU A N   1 
ATOM   2328 C CA  . LEU A 1 299 ? -3.975  8.376   -31.895 1.00 58.74  ? 328 LEU A CA  1 
ATOM   2329 C C   . LEU A 1 299 ? -4.213  9.653   -31.098 1.00 47.07  ? 328 LEU A C   1 
ATOM   2330 O O   . LEU A 1 299 ? -4.345  9.606   -29.879 1.00 44.26  ? 328 LEU A O   1 
ATOM   2331 C CB  . LEU A 1 299 ? -2.503  8.250   -32.290 1.00 64.68  ? 328 LEU A CB  1 
ATOM   2332 C CG  . LEU A 1 299 ? -1.530  7.995   -31.132 1.00 67.11  ? 328 LEU A CG  1 
ATOM   2333 C CD1 . LEU A 1 299 ? -1.731  6.610   -30.576 1.00 65.98  ? 328 LEU A CD1 1 
ATOM   2334 C CD2 . LEU A 1 299 ? -0.087  8.178   -31.546 1.00 73.58  ? 328 LEU A CD2 1 
ATOM   2335 N N   . ARG A 1 300 ? -4.249  10.802  -31.780 1.00 51.05  ? 329 ARG A N   1 
ATOM   2336 C CA  . ARG A 1 300 ? -4.417  12.067  -31.071 1.00 60.18  ? 329 ARG A CA  1 
ATOM   2337 C C   . ARG A 1 300 ? -5.773  12.064  -30.367 1.00 57.81  ? 329 ARG A C   1 
ATOM   2338 O O   . ARG A 1 300 ? -5.921  12.697  -29.330 1.00 54.28  ? 329 ARG A O   1 
ATOM   2339 C CB  . ARG A 1 300 ? -4.288  13.310  -31.966 1.00 62.62  ? 329 ARG A CB  1 
ATOM   2340 C CG  . ARG A 1 300 ? -4.421  14.639  -31.229 1.00 63.99  ? 329 ARG A CG  1 
ATOM   2341 C CD  . ARG A 1 300 ? -4.498  15.845  -32.157 1.00 67.07  ? 329 ARG A CD  1 
ATOM   2342 N NE  . ARG A 1 300 ? -3.296  15.847  -32.991 1.00 72.37  ? 329 ARG A NE  1 
ATOM   2343 C CZ  . ARG A 1 300 ? -3.235  15.564  -34.286 1.00 77.55  ? 329 ARG A CZ  1 
ATOM   2344 N NH1 . ARG A 1 300 ? -4.316  15.669  -35.048 1.00 78.67  ? 329 ARG A NH1 1 
ATOM   2345 N NH2 . ARG A 1 300 ? -2.065  15.236  -34.821 1.00 73.24  ? 329 ARG A NH2 1 
ATOM   2346 N N   . ASP A 1 301 ? -6.746  11.343  -30.944 1.00 58.57  ? 330 ASP A N   1 
ATOM   2347 C CA  . ASP A 1 301 ? -8.054  11.179  -30.335 1.00 60.04  ? 330 ASP A CA  1 
ATOM   2348 C C   . ASP A 1 301 ? -7.907  10.594  -28.933 1.00 60.87  ? 330 ASP A C   1 
ATOM   2349 O O   . ASP A 1 301 ? -8.330  11.219  -27.961 1.00 63.41  ? 330 ASP A O   1 
ATOM   2350 C CB  . ASP A 1 301 ? -8.978  10.375  -31.242 1.00 71.36  ? 330 ASP A CB  1 
ATOM   2351 C CG  . ASP A 1 301 ? -9.922  11.204  -32.105 1.00 80.11  ? 330 ASP A CG  1 
ATOM   2352 O OD1 . ASP A 1 301 ? -10.745 11.935  -31.514 1.00 90.07  ? 330 ASP A OD1 1 
ATOM   2353 O OD2 . ASP A 1 301 ? -9.835  11.122  -33.353 1.00 68.38  ? 330 ASP A OD2 1 
ATOM   2354 N N   . TYR A 1 302 ? -7.283  9.406   -28.839 1.00 60.73  ? 331 TYR A N   1 
ATOM   2355 C CA  . TYR A 1 302 ? -7.088  8.710   -27.574 1.00 54.60  ? 331 TYR A CA  1 
ATOM   2356 C C   . TYR A 1 302 ? -6.362  9.597   -26.559 1.00 62.19  ? 331 TYR A C   1 
ATOM   2357 O O   . TYR A 1 302 ? -6.720  9.579   -25.379 1.00 64.29  ? 331 TYR A O   1 
ATOM   2358 C CB  . TYR A 1 302 ? -6.322  7.406   -27.813 1.00 61.00  ? 331 TYR A CB  1 
ATOM   2359 C CG  . TYR A 1 302 ? -6.206  6.479   -26.603 1.00 64.13  ? 331 TYR A CG  1 
ATOM   2360 C CD1 . TYR A 1 302 ? -5.212  6.662   -25.638 1.00 59.08  ? 331 TYR A CD1 1 
ATOM   2361 C CD2 . TYR A 1 302 ? -7.072  5.398   -26.439 1.00 65.77  ? 331 TYR A CD2 1 
ATOM   2362 C CE1 . TYR A 1 302 ? -5.102  5.825   -24.537 1.00 59.02  ? 331 TYR A CE1 1 
ATOM   2363 C CE2 . TYR A 1 302 ? -6.970  4.553   -25.342 1.00 68.62  ? 331 TYR A CE2 1 
ATOM   2364 C CZ  . TYR A 1 302 ? -5.986  4.769   -24.387 1.00 67.76  ? 331 TYR A CZ  1 
ATOM   2365 O OH  . TYR A 1 302 ? -5.874  3.923   -23.318 1.00 68.38  ? 331 TYR A OH  1 
ATOM   2366 N N   . ILE A 1 303 ? -5.355  10.375  -27.013 1.00 63.20  ? 332 ILE A N   1 
ATOM   2367 C CA  . ILE A 1 303 ? -4.551  11.189  -26.111 1.00 55.99  ? 332 ILE A CA  1 
ATOM   2368 C C   . ILE A 1 303 ? -5.409  12.316  -25.556 1.00 53.69  ? 332 ILE A C   1 
ATOM   2369 O O   . ILE A 1 303 ? -5.395  12.553  -24.357 1.00 47.11  ? 332 ILE A O   1 
ATOM   2370 C CB  . ILE A 1 303 ? -3.275  11.751  -26.764 1.00 58.66  ? 332 ILE A CB  1 
ATOM   2371 C CG1 . ILE A 1 303 ? -2.449  10.675  -27.468 1.00 63.08  ? 332 ILE A CG1 1 
ATOM   2372 C CG2 . ILE A 1 303 ? -2.445  12.498  -25.718 1.00 59.27  ? 332 ILE A CG2 1 
ATOM   2373 C CD1 . ILE A 1 303 ? -2.017  9.539   -26.560 1.00 59.83  ? 332 ILE A CD1 1 
ATOM   2374 N N   . TRP A 1 304 ? -6.150  13.006  -26.435 1.00 57.58  ? 333 TRP A N   1 
ATOM   2375 C CA  . TRP A 1 304 ? -7.127  13.985  -25.972 1.00 60.38  ? 333 TRP A CA  1 
ATOM   2376 C C   . TRP A 1 304 ? -8.081  13.330  -24.973 1.00 58.67  ? 333 TRP A C   1 
ATOM   2377 O O   . TRP A 1 304 ? -8.246  13.844  -23.862 1.00 55.56  ? 333 TRP A O   1 
ATOM   2378 C CB  . TRP A 1 304 ? -7.865  14.668  -27.141 1.00 57.43  ? 333 TRP A CB  1 
ATOM   2379 C CG  . TRP A 1 304 ? -7.154  15.907  -27.641 1.00 60.49  ? 333 TRP A CG  1 
ATOM   2380 C CD1 . TRP A 1 304 ? -6.753  16.183  -28.921 1.00 58.95  ? 333 TRP A CD1 1 
ATOM   2381 C CD2 . TRP A 1 304 ? -6.748  17.049  -26.842 1.00 53.77  ? 333 TRP A CD2 1 
ATOM   2382 N NE1 . TRP A 1 304 ? -6.117  17.400  -28.970 1.00 60.21  ? 333 TRP A NE1 1 
ATOM   2383 C CE2 . TRP A 1 304 ? -6.099  17.955  -27.715 1.00 57.51  ? 333 TRP A CE2 1 
ATOM   2384 C CE3 . TRP A 1 304 ? -6.861  17.385  -25.486 1.00 55.63  ? 333 TRP A CE3 1 
ATOM   2385 C CZ2 . TRP A 1 304 ? -5.576  19.171  -27.268 1.00 55.89  ? 333 TRP A CZ2 1 
ATOM   2386 C CZ3 . TRP A 1 304 ? -6.365  18.595  -25.051 1.00 57.92  ? 333 TRP A CZ3 1 
ATOM   2387 C CH2 . TRP A 1 304 ? -5.733  19.475  -25.934 1.00 56.77  ? 333 TRP A CH2 1 
ATOM   2388 N N   . ASN A 1 305 ? -8.641  12.164  -25.328 1.00 56.52  ? 334 ASN A N   1 
ATOM   2389 C CA  . ASN A 1 305 ? -9.642  11.523  -24.476 1.00 61.16  ? 334 ASN A CA  1 
ATOM   2390 C C   . ASN A 1 305 ? -9.043  11.193  -23.106 1.00 61.20  ? 334 ASN A C   1 
ATOM   2391 O O   . ASN A 1 305 ? -9.718  11.332  -22.090 1.00 57.61  ? 334 ASN A O   1 
ATOM   2392 C CB  . ASN A 1 305 ? -10.282 10.320  -25.166 1.00 64.00  ? 334 ASN A CB  1 
ATOM   2393 C CG  . ASN A 1 305 ? -11.179 10.720  -26.318 1.00 66.81  ? 334 ASN A CG  1 
ATOM   2394 O OD1 . ASN A 1 305 ? -11.716 11.835  -26.333 1.00 63.17  ? 334 ASN A OD1 1 
ATOM   2395 N ND2 . ASN A 1 305 ? -11.380 9.824   -27.276 1.00 65.18  ? 334 ASN A ND2 1 
ATOM   2396 N N   . THR A 1 306 ? -7.767  10.786  -23.090 1.00 63.98  ? 335 THR A N   1 
ATOM   2397 C CA  . THR A 1 306 ? -7.037  10.482  -21.864 1.00 65.16  ? 335 THR A CA  1 
ATOM   2398 C C   . THR A 1 306 ? -6.962  11.704  -20.948 1.00 61.94  ? 335 THR A C   1 
ATOM   2399 O O   . THR A 1 306 ? -7.139  11.575  -19.738 1.00 58.18  ? 335 THR A O   1 
ATOM   2400 C CB  . THR A 1 306 ? -5.627  10.007  -22.230 1.00 68.92  ? 335 THR A CB  1 
ATOM   2401 O OG1 . THR A 1 306 ? -5.775  8.731   -22.851 1.00 65.75  ? 335 THR A OG1 1 
ATOM   2402 C CG2 . THR A 1 306 ? -4.701  9.910   -21.028 1.00 66.60  ? 335 THR A CG2 1 
ATOM   2403 N N   . LEU A 1 307 ? -6.606  12.862  -21.521 1.00 60.75  ? 336 LEU A N   1 
ATOM   2404 C CA  . LEU A 1 307 ? -6.447  14.097  -20.760 1.00 68.07  ? 336 LEU A CA  1 
ATOM   2405 C C   . LEU A 1 307 ? -7.806  14.593  -20.259 1.00 64.45  ? 336 LEU A C   1 
ATOM   2406 O O   . LEU A 1 307 ? -7.930  15.041  -19.115 1.00 58.57  ? 336 LEU A O   1 
ATOM   2407 C CB  . LEU A 1 307 ? -5.747  15.133  -21.646 1.00 63.48  ? 336 LEU A CB  1 
ATOM   2408 C CG  . LEU A 1 307 ? -4.321  14.774  -22.101 1.00 60.99  ? 336 LEU A CG  1 
ATOM   2409 C CD1 . LEU A 1 307 ? -3.696  15.893  -22.935 1.00 56.21  ? 336 LEU A CD1 1 
ATOM   2410 C CD2 . LEU A 1 307 ? -3.429  14.434  -20.916 1.00 57.32  ? 336 LEU A CD2 1 
ATOM   2411 N N   . ASN A 1 308 ? -8.812  14.493  -21.138 1.00 69.79  ? 337 ASN A N   1 
ATOM   2412 C CA  . ASN A 1 308 ? -10.172 14.940  -20.871 1.00 76.54  ? 337 ASN A CA  1 
ATOM   2413 C C   . ASN A 1 308 ? -10.734 14.257  -19.624 1.00 80.33  ? 337 ASN A C   1 
ATOM   2414 O O   . ASN A 1 308 ? -11.331 14.917  -18.773 1.00 77.69  ? 337 ASN A O   1 
ATOM   2415 C CB  . ASN A 1 308 ? -11.056 14.705  -22.092 1.00 77.14  ? 337 ASN A CB  1 
ATOM   2416 C CG  . ASN A 1 308 ? -10.706 15.638  -23.229 1.00 76.05  ? 337 ASN A CG  1 
ATOM   2417 O OD1 . ASN A 1 308 ? -9.997  16.629  -23.017 1.00 68.87  ? 337 ASN A OD1 1 
ATOM   2418 N ND2 . ASN A 1 308 ? -11.197 15.356  -24.430 1.00 75.75  ? 337 ASN A ND2 1 
ATOM   2419 N N   . SER A 1 309 ? -10.515 12.938  -19.522 1.00 81.35  ? 338 SER A N   1 
ATOM   2420 C CA  . SER A 1 309 ? -10.994 12.134  -18.408 1.00 75.35  ? 338 SER A CA  1 
ATOM   2421 C C   . SER A 1 309 ? -10.127 12.319  -17.159 1.00 70.94  ? 338 SER A C   1 
ATOM   2422 O O   . SER A 1 309 ? -10.291 11.592  -16.182 1.00 83.58  ? 338 SER A O   1 
ATOM   2423 C CB  . SER A 1 309 ? -11.076 10.683  -18.824 1.00 78.52  ? 338 SER A CB  1 
ATOM   2424 O OG  . SER A 1 309 ? -9.904  10.284  -19.521 1.00 78.71  ? 338 SER A OG  1 
ATOM   2425 N N   . GLY A 1 310 ? -9.205  13.288  -17.181 1.00 62.33  ? 339 GLY A N   1 
ATOM   2426 C CA  . GLY A 1 310 ? -8.345  13.565  -16.041 1.00 62.17  ? 339 GLY A CA  1 
ATOM   2427 C C   . GLY A 1 310 ? -7.234  12.528  -15.889 1.00 65.51  ? 339 GLY A C   1 
ATOM   2428 O O   . GLY A 1 310 ? -6.620  12.452  -14.825 1.00 58.09  ? 339 GLY A O   1 
ATOM   2429 N N   . ARG A 1 311 ? -6.987  11.749  -16.960 1.00 68.29  ? 340 ARG A N   1 
ATOM   2430 C CA  . ARG A 1 311 ? -6.055  10.625  -16.949 1.00 77.78  ? 340 ARG A CA  1 
ATOM   2431 C C   . ARG A 1 311 ? -4.684  11.080  -17.463 1.00 82.58  ? 340 ARG A C   1 
ATOM   2432 O O   . ARG A 1 311 ? -4.588  12.004  -18.271 1.00 83.08  ? 340 ARG A O   1 
ATOM   2433 C CB  . ARG A 1 311 ? -6.628  9.472   -17.792 1.00 83.97  ? 340 ARG A CB  1 
ATOM   2434 C CG  . ARG A 1 311 ? -7.572  8.471   -17.130 1.00 86.18  ? 340 ARG A CG  1 
ATOM   2435 C CD  . ARG A 1 311 ? -7.020  7.039   -17.074 1.00 84.30  ? 340 ARG A CD  1 
ATOM   2436 N NE  . ARG A 1 311 ? -6.991  6.399   -18.397 1.00 83.34  ? 340 ARG A NE  1 
ATOM   2437 C CZ  . ARG A 1 311 ? -5.922  6.224   -19.193 1.00 97.97  ? 340 ARG A CZ  1 
ATOM   2438 N NH1 . ARG A 1 311 ? -6.063  5.635   -20.375 1.00 98.17  ? 340 ARG A NH1 1 
ATOM   2439 N NH2 . ARG A 1 311 ? -4.715  6.642   -18.828 1.00 96.49  ? 340 ARG A NH2 1 
ATOM   2440 N N   . VAL A 1 312 ? -3.627  10.400  -17.001 1.00 85.55  ? 341 VAL A N   1 
ATOM   2441 C CA  . VAL A 1 312 ? -2.246  10.797  -17.250 1.00 80.48  ? 341 VAL A CA  1 
ATOM   2442 C C   . VAL A 1 312 ? -1.648  9.965   -18.387 1.00 68.88  ? 341 VAL A C   1 
ATOM   2443 O O   . VAL A 1 312 ? -1.954  8.775   -18.546 1.00 55.97  ? 341 VAL A O   1 
ATOM   2444 C CB  . VAL A 1 312 ? -1.440  10.648  -15.942 1.00 81.41  ? 341 VAL A CB  1 
ATOM   2445 C CG1 . VAL A 1 312 ? 0.067   10.670  -16.170 1.00 86.82  ? 341 VAL A CG1 1 
ATOM   2446 C CG2 . VAL A 1 312 ? -1.840  11.698  -14.913 1.00 80.42  ? 341 VAL A CG2 1 
ATOM   2447 N N   . VAL A 1 313 ? -0.784  10.608  -19.181 1.00 61.07  ? 342 VAL A N   1 
ATOM   2448 C CA  . VAL A 1 313 ? 0.005   9.894   -20.176 1.00 59.61  ? 342 VAL A CA  1 
ATOM   2449 C C   . VAL A 1 313 ? 1.334   9.521   -19.518 1.00 53.34  ? 342 VAL A C   1 
ATOM   2450 O O   . VAL A 1 313 ? 2.184   10.384  -19.317 1.00 58.89  ? 342 VAL A O   1 
ATOM   2451 C CB  . VAL A 1 313 ? 0.208   10.696  -21.481 1.00 62.08  ? 342 VAL A CB  1 
ATOM   2452 C CG1 . VAL A 1 313 ? 1.107   9.977   -22.479 1.00 63.85  ? 342 VAL A CG1 1 
ATOM   2453 C CG2 . VAL A 1 313 ? -1.120  11.028  -22.148 1.00 64.72  ? 342 VAL A CG2 1 
ATOM   2454 N N   . PRO A 1 314 ? 1.549   8.236   -19.147 1.00 47.96  ? 343 PRO A N   1 
ATOM   2455 C CA  . PRO A 1 314 ? 2.760   7.831   -18.442 1.00 44.40  ? 343 PRO A CA  1 
ATOM   2456 C C   . PRO A 1 314 ? 3.964   8.024   -19.349 1.00 39.59  ? 343 PRO A C   1 
ATOM   2457 O O   . PRO A 1 314 ? 3.868   7.888   -20.562 1.00 42.58  ? 343 PRO A O   1 
ATOM   2458 C CB  . PRO A 1 314 ? 2.538   6.351   -18.074 1.00 45.52  ? 343 PRO A CB  1 
ATOM   2459 C CG  . PRO A 1 314 ? 1.514   5.871   -19.083 1.00 48.65  ? 343 PRO A CG  1 
ATOM   2460 C CD  . PRO A 1 314 ? 0.659   7.091   -19.423 1.00 51.64  ? 343 PRO A CD  1 
ATOM   2461 N N   . GLY A 1 315 ? 5.094   8.386   -18.759 1.00 42.23  ? 344 GLY A N   1 
ATOM   2462 C CA  . GLY A 1 315 ? 6.326   8.470   -19.522 1.00 41.60  ? 344 GLY A CA  1 
ATOM   2463 C C   . GLY A 1 315 ? 6.668   9.892   -19.955 1.00 45.74  ? 344 GLY A C   1 
ATOM   2464 O O   . GLY A 1 315 ? 7.768   10.113  -20.470 1.00 48.35  ? 344 GLY A O   1 
ATOM   2465 N N   . TYR A 1 316 ? 5.727   10.829  -19.753 1.00 48.39  ? 345 TYR A N   1 
ATOM   2466 C CA  . TYR A 1 316 ? 5.901   12.242  -20.077 1.00 49.02  ? 345 TYR A CA  1 
ATOM   2467 C C   . TYR A 1 316 ? 5.943   13.021  -18.754 1.00 50.99  ? 345 TYR A C   1 
ATOM   2468 O O   . TYR A 1 316 ? 5.153   12.732  -17.858 1.00 54.33  ? 345 TYR A O   1 
ATOM   2469 C CB  . TYR A 1 316 ? 4.799   12.588  -21.100 1.00 45.72  ? 345 TYR A CB  1 
ATOM   2470 C CG  . TYR A 1 316 ? 5.087   12.093  -22.516 1.00 43.84  ? 345 TYR A CG  1 
ATOM   2471 C CD1 . TYR A 1 316 ? 4.853   10.772  -22.871 1.00 43.47  ? 345 TYR A CD1 1 
ATOM   2472 C CD2 . TYR A 1 316 ? 5.648   12.929  -23.481 1.00 45.71  ? 345 TYR A CD2 1 
ATOM   2473 C CE1 . TYR A 1 316 ? 5.169   10.285  -24.127 1.00 39.43  ? 345 TYR A CE1 1 
ATOM   2474 C CE2 . TYR A 1 316 ? 5.943   12.462  -24.757 1.00 42.40  ? 345 TYR A CE2 1 
ATOM   2475 C CZ  . TYR A 1 316 ? 5.713   11.135  -25.077 1.00 41.50  ? 345 TYR A CZ  1 
ATOM   2476 O OH  . TYR A 1 316 ? 6.043   10.623  -26.309 1.00 45.05  ? 345 TYR A OH  1 
ATOM   2477 N N   . GLY A 1 317 ? 6.920   13.939  -18.599 1.00 49.24  ? 346 GLY A N   1 
ATOM   2478 C CA  . GLY A 1 317 ? 7.049   14.818  -17.434 1.00 42.87  ? 346 GLY A CA  1 
ATOM   2479 C C   . GLY A 1 317 ? 8.223   14.441  -16.516 1.00 44.71  ? 346 GLY A C   1 
ATOM   2480 O O   . GLY A 1 317 ? 8.816   13.377  -16.667 1.00 47.32  ? 346 GLY A O   1 
ATOM   2481 N N   . HIS A 1 318 ? 8.542   15.299  -15.536 1.00 42.64  ? 347 HIS A N   1 
ATOM   2482 C CA  . HIS A 1 318 ? 9.596   15.013  -14.567 1.00 52.22  ? 347 HIS A CA  1 
ATOM   2483 C C   . HIS A 1 318 ? 9.575   16.050  -13.439 1.00 51.46  ? 347 HIS A C   1 
ATOM   2484 O O   . HIS A 1 318 ? 9.065   17.149  -13.616 1.00 55.35  ? 347 HIS A O   1 
ATOM   2485 C CB  . HIS A 1 318 ? 10.991  14.999  -15.223 1.00 56.41  ? 347 HIS A CB  1 
ATOM   2486 C CG  . HIS A 1 318 ? 12.061  14.258  -14.450 1.00 61.63  ? 347 HIS A CG  1 
ATOM   2487 N ND1 . HIS A 1 318 ? 12.167  12.887  -14.518 1.00 71.67  ? 347 HIS A ND1 1 
ATOM   2488 C CD2 . HIS A 1 318 ? 13.050  14.642  -13.614 1.00 67.91  ? 347 HIS A CD2 1 
ATOM   2489 C CE1 . HIS A 1 318 ? 13.175  12.476  -13.754 1.00 71.39  ? 347 HIS A CE1 1 
ATOM   2490 N NE2 . HIS A 1 318 ? 13.726  13.521  -13.192 1.00 64.17  ? 347 HIS A NE2 1 
ATOM   2491 N N   . ALA A 1 319 ? 10.207  15.710  -12.313 1.00 50.77  ? 348 ALA A N   1 
ATOM   2492 C CA  . ALA A 1 319 ? 10.342  16.611  -11.174 1.00 61.36  ? 348 ALA A CA  1 
ATOM   2493 C C   . ALA A 1 319 ? 11.334  17.764  -11.402 1.00 65.82  ? 348 ALA A C   1 
ATOM   2494 O O   . ALA A 1 319 ? 11.321  18.711  -10.609 1.00 63.46  ? 348 ALA A O   1 
ATOM   2495 C CB  . ALA A 1 319 ? 10.735  15.815  -9.944  1.00 58.84  ? 348 ALA A CB  1 
ATOM   2496 N N   . VAL A 1 320 ? 12.362  17.525  -12.390 1.00 66.05  ? 349 VAL A N   1 
ATOM   2497 C CA  . VAL A 1 320 ? 13.172  18.753  -12.667 1.00 62.51  ? 349 VAL A CA  1 
ATOM   2498 C C   . VAL A 1 320 ? 13.397  18.880  -14.184 1.00 62.37  ? 349 VAL A C   1 
ATOM   2499 O O   . VAL A 1 320 ? 13.163  19.989  -14.713 1.00 63.92  ? 349 VAL A O   1 
ATOM   2500 C CB  . VAL A 1 320 ? 14.485  18.800  -11.857 1.00 62.60  ? 349 VAL A CB  1 
ATOM   2501 C CG1 . VAL A 1 320 ? 15.009  17.413  -11.501 1.00 62.40  ? 349 VAL A CG1 1 
ATOM   2502 C CG2 . VAL A 1 320 ? 15.550  19.678  -12.503 1.00 64.15  ? 349 VAL A CG2 1 
ATOM   2503 N N   . LEU A 1 321 ? 13.668  17.843  -14.896 1.00 62.30  ? 350 LEU A N   1 
ATOM   2504 C CA  . LEU A 1 321 ? 13.817  17.951  -16.347 1.00 64.36  ? 350 LEU A CA  1 
ATOM   2505 C C   . LEU A 1 321 ? 12.662  18.781  -16.912 1.00 67.96  ? 350 LEU A C   1 
ATOM   2506 O O   . LEU A 1 321 ? 11.524  18.649  -16.452 1.00 70.37  ? 350 LEU A O   1 
ATOM   2507 C CB  . LEU A 1 321 ? 13.866  16.585  -17.042 1.00 65.98  ? 350 LEU A CB  1 
ATOM   2508 C CG  . LEU A 1 321 ? 15.233  15.897  -17.172 1.00 59.13  ? 350 LEU A CG  1 
ATOM   2509 C CD1 . LEU A 1 321 ? 15.045  14.401  -17.056 1.00 65.15  ? 350 LEU A CD1 1 
ATOM   2510 C CD2 . LEU A 1 321 ? 15.946  16.217  -18.488 1.00 56.46  ? 350 LEU A CD2 1 
ATOM   2511 N N   . ARG A 1 322 ? 12.968  19.592  -17.938 1.00 65.51  ? 351 ARG A N   1 
ATOM   2512 C CA  . ARG A 1 322 ? 11.975  20.388  -18.645 1.00 66.13  ? 351 ARG A CA  1 
ATOM   2513 C C   . ARG A 1 322 ? 12.237  20.343  -20.149 1.00 65.40  ? 351 ARG A C   1 
ATOM   2514 O O   . ARG A 1 322 ? 11.976  21.319  -20.840 1.00 74.00  ? 351 ARG A O   1 
ATOM   2515 C CB  . ARG A 1 322 ? 11.992  21.861  -18.198 1.00 70.24  ? 351 ARG A CB  1 
ATOM   2516 C CG  . ARG A 1 322 ? 11.769  22.138  -16.717 1.00 65.13  ? 351 ARG A CG  1 
ATOM   2517 C CD  . ARG A 1 322 ? 10.336  21.861  -16.282 1.00 68.97  ? 351 ARG A CD  1 
ATOM   2518 N NE  . ARG A 1 322 ? 10.175  21.837  -14.821 1.00 69.06  ? 351 ARG A NE  1 
ATOM   2519 C CZ  . ARG A 1 322 ? 9.929   20.748  -14.091 1.00 72.04  ? 351 ARG A CZ  1 
ATOM   2520 N NH1 . ARG A 1 322 ? 9.753   20.859  -12.787 1.00 71.69  ? 351 ARG A NH1 1 
ATOM   2521 N NH2 . ARG A 1 322 ? 9.865   19.551  -14.656 1.00 69.73  ? 351 ARG A NH2 1 
ATOM   2522 N N   . LYS A 1 323 ? 12.754  19.219  -20.657 1.00 67.65  ? 352 LYS A N   1 
ATOM   2523 C CA  . LYS A 1 323 ? 12.912  19.019  -22.093 1.00 59.78  ? 352 LYS A CA  1 
ATOM   2524 C C   . LYS A 1 323 ? 13.038  17.519  -22.354 1.00 50.97  ? 352 LYS A C   1 
ATOM   2525 O O   . LYS A 1 323 ? 12.946  16.734  -21.414 1.00 57.83  ? 352 LYS A O   1 
ATOM   2526 C CB  . LYS A 1 323 ? 14.106  19.804  -22.655 1.00 67.16  ? 352 LYS A CB  1 
ATOM   2527 C CG  . LYS A 1 323 ? 13.826  20.423  -24.027 1.00 77.14  ? 352 LYS A CG  1 
ATOM   2528 C CD  . LYS A 1 323 ? 15.037  20.865  -24.844 1.00 84.85  ? 352 LYS A CD  1 
ATOM   2529 C CE  . LYS A 1 323 ? 15.657  22.153  -24.379 1.00 89.20  ? 352 LYS A CE  1 
ATOM   2530 N NZ  . LYS A 1 323 ? 16.735  22.567  -25.282 1.00 85.66  ? 352 LYS A NZ  1 
ATOM   2531 N N   . THR A 1 324 ? 13.222  17.109  -23.621 1.00 44.80  ? 353 THR A N   1 
ATOM   2532 C CA  . THR A 1 324 ? 13.297  15.692  -23.924 1.00 45.51  ? 353 THR A CA  1 
ATOM   2533 C C   . THR A 1 324 ? 14.482  15.084  -23.156 1.00 45.35  ? 353 THR A C   1 
ATOM   2534 O O   . THR A 1 324 ? 15.574  15.647  -23.095 1.00 38.00  ? 353 THR A O   1 
ATOM   2535 C CB  . THR A 1 324 ? 13.375  15.422  -25.421 1.00 44.94  ? 353 THR A CB  1 
ATOM   2536 O OG1 . THR A 1 324 ? 12.116  15.789  -25.973 1.00 47.30  ? 353 THR A OG1 1 
ATOM   2537 C CG2 . THR A 1 324 ? 13.538  13.946  -25.732 1.00 42.20  ? 353 THR A CG2 1 
ATOM   2538 N N   . ASP A 1 325 ? 14.238  13.916  -22.552 1.00 41.64  ? 354 ASP A N   1 
ATOM   2539 C CA  . ASP A 1 325 ? 15.235  13.273  -21.710 1.00 37.04  ? 354 ASP A CA  1 
ATOM   2540 C C   . ASP A 1 325 ? 16.309  12.707  -22.623 1.00 35.30  ? 354 ASP A C   1 
ATOM   2541 O O   . ASP A 1 325 ? 16.010  11.986  -23.575 1.00 35.85  ? 354 ASP A O   1 
ATOM   2542 C CB  . ASP A 1 325 ? 14.583  12.239  -20.813 1.00 35.33  ? 354 ASP A CB  1 
ATOM   2543 C CG  . ASP A 1 325 ? 15.491  11.547  -19.799 1.00 37.63  ? 354 ASP A CG  1 
ATOM   2544 O OD1 . ASP A 1 325 ? 16.759  11.709  -19.889 1.00 32.41  ? 354 ASP A OD1 1 
ATOM   2545 O OD2 . ASP A 1 325 ? 14.914  10.859  -18.920 1.00 33.07  ? 354 ASP A OD2 1 
ATOM   2546 N N   . PRO A 1 326 ? 17.599  13.056  -22.438 1.00 33.20  ? 355 PRO A N   1 
ATOM   2547 C CA  . PRO A 1 326 ? 18.606  12.477  -23.324 1.00 33.66  ? 355 PRO A CA  1 
ATOM   2548 C C   . PRO A 1 326 ? 18.633  10.951  -23.227 1.00 32.45  ? 355 PRO A C   1 
ATOM   2549 O O   . PRO A 1 326 ? 19.049  10.268  -24.151 1.00 29.39  ? 355 PRO A O   1 
ATOM   2550 C CB  . PRO A 1 326 ? 19.908  13.184  -22.877 1.00 35.23  ? 355 PRO A CB  1 
ATOM   2551 C CG  . PRO A 1 326 ? 19.607  13.749  -21.512 1.00 35.93  ? 355 PRO A CG  1 
ATOM   2552 C CD  . PRO A 1 326 ? 18.120  14.085  -21.522 1.00 32.61  ? 355 PRO A CD  1 
ATOM   2553 N N   . ARG A 1 327 ? 18.151  10.405  -22.091 1.00 32.87  ? 356 ARG A N   1 
ATOM   2554 C CA  . ARG A 1 327 ? 18.103  8.969   -21.873 1.00 29.74  ? 356 ARG A CA  1 
ATOM   2555 C C   . ARG A 1 327 ? 17.023  8.333   -22.746 1.00 32.95  ? 356 ARG A C   1 
ATOM   2556 O O   . ARG A 1 327 ? 17.193  7.198   -23.190 1.00 33.16  ? 356 ARG A O   1 
ATOM   2557 C CB  . ARG A 1 327 ? 17.885  8.660   -20.386 1.00 30.98  ? 356 ARG A CB  1 
ATOM   2558 C CG  . ARG A 1 327 ? 19.045  9.082   -19.477 1.00 29.82  ? 356 ARG A CG  1 
ATOM   2559 C CD  . ARG A 1 327 ? 18.769  8.879   -17.987 1.00 30.82  ? 356 ARG A CD  1 
ATOM   2560 N NE  . ARG A 1 327 ? 17.570  9.586   -17.532 1.00 29.78  ? 356 ARG A NE  1 
ATOM   2561 C CZ  . ARG A 1 327 ? 16.904  9.459   -16.388 1.00 33.73  ? 356 ARG A CZ  1 
ATOM   2562 N NH1 . ARG A 1 327 ? 17.335  8.707   -15.378 1.00 30.89  ? 356 ARG A NH1 1 
ATOM   2563 N NH2 . ARG A 1 327 ? 15.748  10.101  -16.262 1.00 34.82  ? 356 ARG A NH2 1 
ATOM   2564 N N   . TYR A 1 328 ? 15.923  9.068   -23.002 1.00 34.10  ? 357 TYR A N   1 
ATOM   2565 C CA  . TYR A 1 328 ? 14.953  8.699   -24.042 1.00 30.68  ? 357 TYR A CA  1 
ATOM   2566 C C   . TYR A 1 328 ? 15.535  8.705   -25.460 1.00 28.80  ? 357 TYR A C   1 
ATOM   2567 O O   . TYR A 1 328 ? 15.441  7.718   -26.180 1.00 29.79  ? 357 TYR A O   1 
ATOM   2568 C CB  . TYR A 1 328 ? 13.757  9.643   -24.014 1.00 34.65  ? 357 TYR A CB  1 
ATOM   2569 C CG  . TYR A 1 328 ? 12.632  9.293   -24.978 1.00 34.43  ? 357 TYR A CG  1 
ATOM   2570 C CD1 . TYR A 1 328 ? 12.613  9.810   -26.275 1.00 35.73  ? 357 TYR A CD1 1 
ATOM   2571 C CD2 . TYR A 1 328 ? 11.557  8.506   -24.582 1.00 33.75  ? 357 TYR A CD2 1 
ATOM   2572 C CE1 . TYR A 1 328 ? 11.574  9.527   -27.150 1.00 29.11  ? 357 TYR A CE1 1 
ATOM   2573 C CE2 . TYR A 1 328 ? 10.505  8.230   -25.449 1.00 35.59  ? 357 TYR A CE2 1 
ATOM   2574 C CZ  . TYR A 1 328 ? 10.513  8.735   -26.746 1.00 38.26  ? 357 TYR A CZ  1 
ATOM   2575 O OH  . TYR A 1 328 ? 9.486   8.425   -27.631 1.00 35.66  ? 357 TYR A OH  1 
ATOM   2576 N N   . THR A 1 329 ? 16.143  9.811   -25.870 1.00 32.36  ? 358 THR A N   1 
ATOM   2577 C CA  . THR A 1 329 ? 16.708  9.962   -27.211 1.00 34.50  ? 358 THR A CA  1 
ATOM   2578 C C   . THR A 1 329 ? 17.656  8.801   -27.511 1.00 37.83  ? 358 THR A C   1 
ATOM   2579 O O   . THR A 1 329 ? 17.620  8.187   -28.579 1.00 37.71  ? 358 THR A O   1 
ATOM   2580 C CB  . THR A 1 329 ? 17.427  11.309  -27.264 1.00 34.84  ? 358 THR A CB  1 
ATOM   2581 O OG1 . THR A 1 329 ? 16.485  12.304  -26.884 1.00 33.42  ? 358 THR A OG1 1 
ATOM   2582 C CG2 . THR A 1 329 ? 17.974  11.696  -28.626 1.00 40.11  ? 358 THR A CG2 1 
ATOM   2583 N N   . CYS A 1 330 ? 18.508  8.488   -26.528 1.00 36.95  ? 359 CYS A N   1 
ATOM   2584 C CA  . CYS A 1 330 ? 19.419  7.360   -26.592 1.00 36.34  ? 359 CYS A CA  1 
ATOM   2585 C C   . CYS A 1 330 ? 18.726  6.061   -26.989 1.00 30.77  ? 359 CYS A C   1 
ATOM   2586 O O   . CYS A 1 330 ? 19.225  5.280   -27.808 1.00 30.05  ? 359 CYS A O   1 
ATOM   2587 C CB  . CYS A 1 330 ? 19.945  7.101   -25.178 1.00 50.22  ? 359 CYS A CB  1 
ATOM   2588 S SG  . CYS A 1 330 ? 21.715  6.865   -25.171 1.00 75.77  ? 359 CYS A SG  1 
ATOM   2589 N N   . GLN A 1 331 ? 17.619  5.769   -26.293 1.00 29.48  ? 360 GLN A N   1 
ATOM   2590 C CA  . GLN A 1 331 ? 16.866  4.564   -26.517 1.00 31.95  ? 360 GLN A CA  1 
ATOM   2591 C C   . GLN A 1 331 ? 16.168  4.639   -27.869 1.00 34.44  ? 360 GLN A C   1 
ATOM   2592 O O   . GLN A 1 331 ? 16.065  3.625   -28.545 1.00 32.80  ? 360 GLN A O   1 
ATOM   2593 C CB  . GLN A 1 331 ? 15.904  4.343   -25.358 1.00 38.27  ? 360 GLN A CB  1 
ATOM   2594 C CG  . GLN A 1 331 ? 16.630  3.951   -24.076 1.00 39.44  ? 360 GLN A CG  1 
ATOM   2595 C CD  . GLN A 1 331 ? 15.680  3.669   -22.942 1.00 40.78  ? 360 GLN A CD  1 
ATOM   2596 O OE1 . GLN A 1 331 ? 15.445  2.510   -22.590 1.00 47.33  ? 360 GLN A OE1 1 
ATOM   2597 N NE2 . GLN A 1 331 ? 15.102  4.726   -22.390 1.00 44.36  ? 360 GLN A NE2 1 
ATOM   2598 N N   . ARG A 1 332 ? 15.725  5.836   -28.257 1.00 35.13  ? 361 ARG A N   1 
ATOM   2599 C CA  . ARG A 1 332 ? 15.159  6.039   -29.589 1.00 36.41  ? 361 ARG A CA  1 
ATOM   2600 C C   . ARG A 1 332 ? 16.204  5.690   -30.656 1.00 36.49  ? 361 ARG A C   1 
ATOM   2601 O O   . ARG A 1 332 ? 15.931  4.823   -31.488 1.00 38.64  ? 361 ARG A O   1 
ATOM   2602 C CB  . ARG A 1 332 ? 14.561  7.443   -29.706 1.00 39.52  ? 361 ARG A CB  1 
ATOM   2603 C CG  . ARG A 1 332 ? 14.003  7.753   -31.089 1.00 46.57  ? 361 ARG A CG  1 
ATOM   2604 C CD  . ARG A 1 332 ? 13.364  9.126   -31.016 1.00 48.44  ? 361 ARG A CD  1 
ATOM   2605 N NE  . ARG A 1 332 ? 13.037  9.643   -32.348 1.00 50.72  ? 361 ARG A NE  1 
ATOM   2606 C CZ  . ARG A 1 332 ? 12.081  9.207   -33.163 1.00 55.69  ? 361 ARG A CZ  1 
ATOM   2607 N NH1 . ARG A 1 332 ? 11.249  8.246   -32.803 1.00 47.75  ? 361 ARG A NH1 1 
ATOM   2608 N NH2 . ARG A 1 332 ? 11.955  9.766   -34.357 1.00 62.48  ? 361 ARG A NH2 1 
ATOM   2609 N N   . GLU A 1 333 ? 17.401  6.307   -30.596 1.00 33.64  ? 362 GLU A N   1 
ATOM   2610 C CA  . GLU A 1 333 ? 18.465  6.058   -31.575 1.00 39.18  ? 362 GLU A CA  1 
ATOM   2611 C C   . GLU A 1 333 ? 18.709  4.552   -31.717 1.00 37.36  ? 362 GLU A C   1 
ATOM   2612 O O   . GLU A 1 333 ? 18.837  4.040   -32.825 1.00 38.64  ? 362 GLU A O   1 
ATOM   2613 C CB  . GLU A 1 333 ? 19.833  6.693   -31.265 1.00 40.26  ? 362 GLU A CB  1 
ATOM   2614 C CG  . GLU A 1 333 ? 19.892  8.215   -31.434 1.00 43.98  ? 362 GLU A CG  1 
ATOM   2615 C CD  . GLU A 1 333 ? 21.088  8.966   -30.840 1.00 45.14  ? 362 GLU A CD  1 
ATOM   2616 O OE1 . GLU A 1 333 ? 21.929  8.412   -30.110 1.00 47.03  ? 362 GLU A OE1 1 
ATOM   2617 O OE2 . GLU A 1 333 ? 21.147  10.184  -31.059 1.00 40.56  ? 362 GLU A OE2 1 
ATOM   2618 N N   . PHE A 1 334 ? 18.789  3.834   -30.579 1.00 33.48  ? 363 PHE A N   1 
ATOM   2619 C CA  . PHE A 1 334 ? 18.982  2.394   -30.587 1.00 32.29  ? 363 PHE A CA  1 
ATOM   2620 C C   . PHE A 1 334 ? 17.820  1.676   -31.266 1.00 33.55  ? 363 PHE A C   1 
ATOM   2621 O O   . PHE A 1 334 ? 18.023  0.657   -31.918 1.00 36.38  ? 363 PHE A O   1 
ATOM   2622 C CB  . PHE A 1 334 ? 19.072  1.857   -29.156 1.00 34.59  ? 363 PHE A CB  1 
ATOM   2623 C CG  . PHE A 1 334 ? 19.499  0.411   -29.072 1.00 30.82  ? 363 PHE A CG  1 
ATOM   2624 C CD1 . PHE A 1 334 ? 18.555  -0.610  -29.120 1.00 34.76  ? 363 PHE A CD1 1 
ATOM   2625 C CD2 . PHE A 1 334 ? 20.837  0.072   -28.973 1.00 28.92  ? 363 PHE A CD2 1 
ATOM   2626 C CE1 . PHE A 1 334 ? 18.947  -1.935  -29.041 1.00 33.24  ? 363 PHE A CE1 1 
ATOM   2627 C CE2 . PHE A 1 334 ? 21.222  -1.257  -28.912 1.00 31.91  ? 363 PHE A CE2 1 
ATOM   2628 C CZ  . PHE A 1 334 ? 20.272  -2.253  -28.945 1.00 33.02  ? 363 PHE A CZ  1 
ATOM   2629 N N   . ALA A 1 335 ? 16.591  2.137   -31.028 1.00 33.84  ? 364 ALA A N   1 
ATOM   2630 C CA  . ALA A 1 335 ? 15.436  1.525   -31.657 1.00 35.79  ? 364 ALA A CA  1 
ATOM   2631 C C   . ALA A 1 335 ? 15.454  1.788   -33.169 1.00 37.90  ? 364 ALA A C   1 
ATOM   2632 O O   . ALA A 1 335 ? 15.178  0.876   -33.920 1.00 36.02  ? 364 ALA A O   1 
ATOM   2633 C CB  . ALA A 1 335 ? 14.176  2.047   -31.032 1.00 35.03  ? 364 ALA A CB  1 
ATOM   2634 N N   . LEU A 1 336 ? 15.728  3.028   -33.602 1.00 36.47  ? 365 LEU A N   1 
ATOM   2635 C CA  . LEU A 1 336 ? 15.765  3.359   -35.028 1.00 40.48  ? 365 LEU A CA  1 
ATOM   2636 C C   . LEU A 1 336 ? 16.826  2.514   -35.748 1.00 41.53  ? 365 LEU A C   1 
ATOM   2637 O O   . LEU A 1 336 ? 16.684  2.214   -36.928 1.00 39.27  ? 365 LEU A O   1 
ATOM   2638 C CB  . LEU A 1 336 ? 16.029  4.856   -35.237 1.00 42.52  ? 365 LEU A CB  1 
ATOM   2639 C CG  . LEU A 1 336 ? 14.903  5.820   -34.827 1.00 43.80  ? 365 LEU A CG  1 
ATOM   2640 C CD1 . LEU A 1 336 ? 15.426  7.252   -34.695 1.00 46.83  ? 365 LEU A CD1 1 
ATOM   2641 C CD2 . LEU A 1 336 ? 13.708  5.780   -35.791 1.00 43.50  ? 365 LEU A CD2 1 
ATOM   2642 N N   . LYS A 1 337 ? 17.891  2.096   -35.045 1.00 43.06  ? 366 LYS A N   1 
ATOM   2643 C CA  . LYS A 1 337 ? 18.932  1.257   -35.637 1.00 45.45  ? 366 LYS A CA  1 
ATOM   2644 C C   . LYS A 1 337 ? 18.506  -0.206  -35.742 1.00 48.03  ? 366 LYS A C   1 
ATOM   2645 O O   . LYS A 1 337 ? 18.756  -0.847  -36.756 1.00 50.87  ? 366 LYS A O   1 
ATOM   2646 C CB  . LYS A 1 337 ? 20.207  1.135   -34.796 1.00 54.23  ? 366 LYS A CB  1 
ATOM   2647 C CG  . LYS A 1 337 ? 21.203  2.251   -34.827 1.00 57.33  ? 366 LYS A CG  1 
ATOM   2648 C CD  . LYS A 1 337 ? 22.321  2.017   -33.816 1.00 66.88  ? 366 LYS A CD  1 
ATOM   2649 C CE  . LYS A 1 337 ? 23.214  3.206   -33.598 1.00 77.32  ? 366 LYS A CE  1 
ATOM   2650 N NZ  . LYS A 1 337 ? 24.144  3.062   -32.468 1.00 79.89  ? 366 LYS A NZ  1 
ATOM   2651 N N   . HIS A 1 338 ? 17.909  -0.757  -34.674 1.00 42.19  ? 367 HIS A N   1 
ATOM   2652 C CA  . HIS A 1 338 ? 17.900  -2.196  -34.484 1.00 42.12  ? 367 HIS A CA  1 
ATOM   2653 C C   . HIS A 1 338 ? 16.517  -2.813  -34.626 1.00 41.54  ? 367 HIS A C   1 
ATOM   2654 O O   . HIS A 1 338 ? 16.443  -3.998  -34.911 1.00 46.74  ? 367 HIS A O   1 
ATOM   2655 C CB  . HIS A 1 338 ? 18.495  -2.577  -33.122 1.00 43.26  ? 367 HIS A CB  1 
ATOM   2656 C CG  . HIS A 1 338 ? 19.951  -2.233  -33.000 1.00 41.83  ? 367 HIS A CG  1 
ATOM   2657 N ND1 . HIS A 1 338 ? 20.902  -2.891  -33.745 1.00 39.79  ? 367 HIS A ND1 1 
ATOM   2658 C CD2 . HIS A 1 338 ? 20.618  -1.310  -32.292 1.00 46.60  ? 367 HIS A CD2 1 
ATOM   2659 C CE1 . HIS A 1 338 ? 22.100  -2.386  -33.494 1.00 41.27  ? 367 HIS A CE1 1 
ATOM   2660 N NE2 . HIS A 1 338 ? 21.962  -1.444  -32.592 1.00 45.15  ? 367 HIS A NE2 1 
ATOM   2661 N N   . LEU A 1 339 ? 15.444  -2.057  -34.374 1.00 47.35  ? 368 LEU A N   1 
ATOM   2662 C CA  . LEU A 1 339 ? 14.105  -2.628  -34.397 1.00 43.63  ? 368 LEU A CA  1 
ATOM   2663 C C   . LEU A 1 339 ? 13.077  -1.609  -34.901 1.00 45.11  ? 368 LEU A C   1 
ATOM   2664 O O   . LEU A 1 339 ? 11.997  -1.484  -34.318 1.00 40.62  ? 368 LEU A O   1 
ATOM   2665 C CB  . LEU A 1 339 ? 13.755  -3.127  -32.996 1.00 44.49  ? 368 LEU A CB  1 
ATOM   2666 C CG  . LEU A 1 339 ? 13.769  -2.084  -31.869 1.00 44.85  ? 368 LEU A CG  1 
ATOM   2667 C CD1 . LEU A 1 339 ? 12.443  -2.042  -31.109 1.00 40.79  ? 368 LEU A CD1 1 
ATOM   2668 C CD2 . LEU A 1 339 ? 14.908  -2.382  -30.897 1.00 40.97  ? 368 LEU A CD2 1 
ATOM   2669 N N   . PRO A 1 340 ? 13.340  -0.899  -36.027 1.00 40.34  ? 369 PRO A N   1 
ATOM   2670 C CA  . PRO A 1 340 ? 12.407  0.106   -36.543 1.00 45.70  ? 369 PRO A CA  1 
ATOM   2671 C C   . PRO A 1 340 ? 10.990  -0.373  -36.865 1.00 41.11  ? 369 PRO A C   1 
ATOM   2672 O O   . PRO A 1 340 ? 10.046  0.405   -36.777 1.00 44.33  ? 369 PRO A O   1 
ATOM   2673 C CB  . PRO A 1 340 ? 13.113  0.655   -37.805 1.00 46.59  ? 369 PRO A CB  1 
ATOM   2674 C CG  . PRO A 1 340 ? 14.146  -0.375  -38.173 1.00 43.37  ? 369 PRO A CG  1 
ATOM   2675 C CD  . PRO A 1 340 ? 14.553  -1.013  -36.854 1.00 43.90  ? 369 PRO A CD  1 
ATOM   2676 N N   . ASN A 1 341 ? 10.846  -1.646  -37.234 1.00 47.39  ? 370 ASN A N   1 
ATOM   2677 C CA  . ASN A 1 341 ? 9.569   -2.150  -37.719 1.00 53.00  ? 370 ASN A CA  1 
ATOM   2678 C C   . ASN A 1 341 ? 8.750   -2.748  -36.584 1.00 55.44  ? 370 ASN A C   1 
ATOM   2679 O O   . ASN A 1 341 ? 7.581   -3.082  -36.783 1.00 50.52  ? 370 ASN A O   1 
ATOM   2680 C CB  . ASN A 1 341 ? 9.794   -3.118  -38.872 1.00 57.65  ? 370 ASN A CB  1 
ATOM   2681 C CG  . ASN A 1 341 ? 10.505  -2.407  -40.000 1.00 57.95  ? 370 ASN A CG  1 
ATOM   2682 O OD1 . ASN A 1 341 ? 10.156  -1.263  -40.322 1.00 57.30  ? 370 ASN A OD1 1 
ATOM   2683 N ND2 . ASN A 1 341 ? 11.536  -3.024  -40.561 1.00 58.45  ? 370 ASN A ND2 1 
ATOM   2684 N N   . ASP A 1 342 ? 9.353   -2.848  -35.387 1.00 48.06  ? 371 ASP A N   1 
ATOM   2685 C CA  . ASP A 1 342 ? 8.627   -3.347  -34.239 1.00 47.93  ? 371 ASP A CA  1 
ATOM   2686 C C   . ASP A 1 342 ? 7.406   -2.465  -34.024 1.00 45.27  ? 371 ASP A C   1 
ATOM   2687 O O   . ASP A 1 342 ? 7.538   -1.240  -33.999 1.00 43.45  ? 371 ASP A O   1 
ATOM   2688 C CB  . ASP A 1 342 ? 9.511   -3.410  -33.004 1.00 52.30  ? 371 ASP A CB  1 
ATOM   2689 C CG  . ASP A 1 342 ? 8.751   -3.831  -31.759 1.00 50.71  ? 371 ASP A CG  1 
ATOM   2690 O OD1 . ASP A 1 342 ? 8.308   -5.000  -31.724 1.00 51.93  ? 371 ASP A OD1 1 
ATOM   2691 O OD2 . ASP A 1 342 ? 8.556   -2.966  -30.880 1.00 48.78  ? 371 ASP A OD2 1 
ATOM   2692 N N   . PRO A 1 343 ? 6.182   -3.045  -33.970 1.00 51.24  ? 372 PRO A N   1 
ATOM   2693 C CA  . PRO A 1 343 ? 4.946   -2.263  -33.833 1.00 52.81  ? 372 PRO A CA  1 
ATOM   2694 C C   . PRO A 1 343 ? 4.857   -1.416  -32.571 1.00 47.75  ? 372 PRO A C   1 
ATOM   2695 O O   . PRO A 1 343 ? 4.346   -0.293  -32.591 1.00 46.41  ? 372 PRO A O   1 
ATOM   2696 C CB  . PRO A 1 343 ? 3.833   -3.337  -33.844 1.00 52.33  ? 372 PRO A CB  1 
ATOM   2697 C CG  . PRO A 1 343 ? 4.462   -4.512  -34.553 1.00 48.89  ? 372 PRO A CG  1 
ATOM   2698 C CD  . PRO A 1 343 ? 5.913   -4.485  -34.151 1.00 50.00  ? 372 PRO A CD  1 
ATOM   2699 N N   . MET A 1 344 ? 5.331   -1.983  -31.457 1.00 45.98  ? 373 MET A N   1 
ATOM   2700 C CA  . MET A 1 344 ? 5.230   -1.290  -30.189 1.00 46.74  ? 373 MET A CA  1 
ATOM   2701 C C   . MET A 1 344 ? 6.155   -0.078  -30.220 1.00 40.51  ? 373 MET A C   1 
ATOM   2702 O O   . MET A 1 344 ? 5.762   0.994   -29.776 1.00 42.65  ? 373 MET A O   1 
ATOM   2703 C CB  . MET A 1 344 ? 5.524   -2.226  -29.013 1.00 56.24  ? 373 MET A CB  1 
ATOM   2704 C CG  . MET A 1 344 ? 4.395   -3.205  -28.703 1.00 62.02  ? 373 MET A CG  1 
ATOM   2705 S SD  . MET A 1 344 ? 2.970   -2.511  -27.837 1.00 61.63  ? 373 MET A SD  1 
ATOM   2706 C CE  . MET A 1 344 ? 3.737   -1.917  -26.320 1.00 64.64  ? 373 MET A CE  1 
ATOM   2707 N N   . PHE A 1 345 ? 7.330   -0.211  -30.858 1.00 43.91  ? 374 PHE A N   1 
ATOM   2708 C CA  . PHE A 1 345 ? 8.221   0.927   -31.016 1.00 39.69  ? 374 PHE A CA  1 
ATOM   2709 C C   . PHE A 1 345 ? 7.564   2.006   -31.882 1.00 40.10  ? 374 PHE A C   1 
ATOM   2710 O O   . PHE A 1 345 ? 7.567   3.185   -31.524 1.00 38.90  ? 374 PHE A O   1 
ATOM   2711 C CB  . PHE A 1 345 ? 9.579   0.510   -31.581 1.00 41.25  ? 374 PHE A CB  1 
ATOM   2712 C CG  . PHE A 1 345 ? 10.359  1.731   -32.037 1.00 40.55  ? 374 PHE A CG  1 
ATOM   2713 C CD1 . PHE A 1 345 ? 10.666  2.741   -31.136 1.00 38.03  ? 374 PHE A CD1 1 
ATOM   2714 C CD2 . PHE A 1 345 ? 10.699  1.905   -33.371 1.00 37.74  ? 374 PHE A CD2 1 
ATOM   2715 C CE1 . PHE A 1 345 ? 11.346  3.870   -31.544 1.00 39.78  ? 374 PHE A CE1 1 
ATOM   2716 C CE2 . PHE A 1 345 ? 11.357  3.050   -33.789 1.00 39.04  ? 374 PHE A CE2 1 
ATOM   2717 C CZ  . PHE A 1 345 ? 11.691  4.023   -32.876 1.00 43.03  ? 374 PHE A CZ  1 
ATOM   2718 N N   . LYS A 1 346 ? 6.994   1.613   -33.033 1.00 48.12  ? 375 LYS A N   1 
ATOM   2719 C CA  . LYS A 1 346 ? 6.356   2.566   -33.938 1.00 47.36  ? 375 LYS A CA  1 
ATOM   2720 C C   . LYS A 1 346 ? 5.343   3.437   -33.188 1.00 46.72  ? 375 LYS A C   1 
ATOM   2721 O O   . LYS A 1 346 ? 5.266   4.645   -33.426 1.00 49.04  ? 375 LYS A O   1 
ATOM   2722 C CB  . LYS A 1 346 ? 5.647   1.840   -35.086 1.00 54.42  ? 375 LYS A CB  1 
ATOM   2723 C CG  . LYS A 1 346 ? 6.552   1.245   -36.152 1.00 62.82  ? 375 LYS A CG  1 
ATOM   2724 C CD  . LYS A 1 346 ? 5.750   0.637   -37.298 1.00 74.67  ? 375 LYS A CD  1 
ATOM   2725 C CE  . LYS A 1 346 ? 6.589   -0.021  -38.341 1.00 83.45  ? 375 LYS A CE  1 
ATOM   2726 N NZ  . LYS A 1 346 ? 5.802   -0.517  -39.478 1.00 81.71  ? 375 LYS A NZ  1 
ATOM   2727 N N   . LEU A 1 347 ? 4.591   2.814   -32.264 1.00 42.37  ? 376 LEU A N   1 
ATOM   2728 C CA  . LEU A 1 347 ? 3.654   3.504   -31.387 1.00 40.15  ? 376 LEU A CA  1 
ATOM   2729 C C   . LEU A 1 347 ? 4.357   4.521   -30.490 1.00 43.89  ? 376 LEU A C   1 
ATOM   2730 O O   . LEU A 1 347 ? 3.938   5.683   -30.412 1.00 40.27  ? 376 LEU A O   1 
ATOM   2731 C CB  . LEU A 1 347 ? 2.910   2.447   -30.583 1.00 42.20  ? 376 LEU A CB  1 
ATOM   2732 C CG  . LEU A 1 347 ? 1.713   2.942   -29.776 1.00 46.15  ? 376 LEU A CG  1 
ATOM   2733 C CD1 . LEU A 1 347 ? 0.696   3.655   -30.669 1.00 48.20  ? 376 LEU A CD1 1 
ATOM   2734 C CD2 . LEU A 1 347 ? 1.096   1.749   -29.066 1.00 49.05  ? 376 LEU A CD2 1 
ATOM   2735 N N   . VAL A 1 348 ? 5.408   4.069   -29.779 1.00 45.74  ? 377 VAL A N   1 
ATOM   2736 C CA  . VAL A 1 348 ? 6.199   4.951   -28.935 1.00 41.35  ? 377 VAL A CA  1 
ATOM   2737 C C   . VAL A 1 348 ? 6.622   6.174   -29.742 1.00 37.98  ? 377 VAL A C   1 
ATOM   2738 O O   . VAL A 1 348 ? 6.464   7.291   -29.267 1.00 35.94  ? 377 VAL A O   1 
ATOM   2739 C CB  . VAL A 1 348 ? 7.416   4.210   -28.328 1.00 43.48  ? 377 VAL A CB  1 
ATOM   2740 C CG1 . VAL A 1 348 ? 8.518   5.160   -27.859 1.00 33.49  ? 377 VAL A CG1 1 
ATOM   2741 C CG2 . VAL A 1 348 ? 6.974   3.282   -27.200 1.00 47.61  ? 377 VAL A CG2 1 
ATOM   2742 N N   . ALA A 1 349 ? 7.152   5.950   -30.965 1.00 41.33  ? 378 ALA A N   1 
ATOM   2743 C CA  . ALA A 1 349 ? 7.653   7.021   -31.826 1.00 42.77  ? 378 ALA A CA  1 
ATOM   2744 C C   . ALA A 1 349 ? 6.508   7.908   -32.293 1.00 50.30  ? 378 ALA A C   1 
ATOM   2745 O O   . ALA A 1 349 ? 6.641   9.140   -32.289 1.00 47.61  ? 378 ALA A O   1 
ATOM   2746 C CB  . ALA A 1 349 ? 8.384   6.455   -33.028 1.00 40.91  ? 378 ALA A CB  1 
ATOM   2747 N N   . GLN A 1 350 ? 5.418   7.248   -32.728 1.00 46.91  ? 379 GLN A N   1 
ATOM   2748 C CA  . GLN A 1 350 ? 4.172   7.933   -33.050 1.00 51.74  ? 379 GLN A CA  1 
ATOM   2749 C C   . GLN A 1 350 ? 3.780   8.852   -31.896 1.00 47.18  ? 379 GLN A C   1 
ATOM   2750 O O   . GLN A 1 350 ? 3.448   10.017  -32.133 1.00 44.55  ? 379 GLN A O   1 
ATOM   2751 C CB  . GLN A 1 350 ? 3.050   6.936   -33.361 1.00 53.97  ? 379 GLN A CB  1 
ATOM   2752 C CG  . GLN A 1 350 ? 1.964   7.488   -34.277 1.00 64.42  ? 379 GLN A CG  1 
ATOM   2753 C CD  . GLN A 1 350 ? 1.056   6.419   -34.855 1.00 73.24  ? 379 GLN A CD  1 
ATOM   2754 O OE1 . GLN A 1 350 ? 0.968   5.282   -34.362 1.00 69.68  ? 379 GLN A OE1 1 
ATOM   2755 N NE2 . GLN A 1 350 ? 0.371   6.789   -35.930 1.00 71.73  ? 379 GLN A NE2 1 
ATOM   2756 N N   . LEU A 1 351 ? 3.864   8.339   -30.646 1.00 45.13  ? 380 LEU A N   1 
ATOM   2757 C CA  . LEU A 1 351 ? 3.405   9.096   -29.486 1.00 48.34  ? 380 LEU A CA  1 
ATOM   2758 C C   . LEU A 1 351 ? 4.300   10.307  -29.232 1.00 45.91  ? 380 LEU A C   1 
ATOM   2759 O O   . LEU A 1 351 ? 3.814   11.344  -28.758 1.00 41.45  ? 380 LEU A O   1 
ATOM   2760 C CB  . LEU A 1 351 ? 3.274   8.243   -28.226 1.00 48.94  ? 380 LEU A CB  1 
ATOM   2761 C CG  . LEU A 1 351 ? 2.116   7.239   -28.230 1.00 51.00  ? 380 LEU A CG  1 
ATOM   2762 C CD1 . LEU A 1 351 ? 2.346   6.116   -27.227 1.00 49.15  ? 380 LEU A CD1 1 
ATOM   2763 C CD2 . LEU A 1 351 ? 0.807   7.937   -27.945 1.00 50.87  ? 380 LEU A CD2 1 
ATOM   2764 N N   . TYR A 1 352 ? 5.599   10.178  -29.544 1.00 49.19  ? 381 TYR A N   1 
ATOM   2765 C CA  . TYR A 1 352 ? 6.528   11.294  -29.409 1.00 47.67  ? 381 TYR A CA  1 
ATOM   2766 C C   . TYR A 1 352 ? 6.123   12.429  -30.355 1.00 48.78  ? 381 TYR A C   1 
ATOM   2767 O O   . TYR A 1 352 ? 6.271   13.599  -29.998 1.00 44.74  ? 381 TYR A O   1 
ATOM   2768 C CB  . TYR A 1 352 ? 7.955   10.784  -29.656 1.00 49.93  ? 381 TYR A CB  1 
ATOM   2769 C CG  . TYR A 1 352 ? 9.070   11.787  -29.395 1.00 46.51  ? 381 TYR A CG  1 
ATOM   2770 C CD1 . TYR A 1 352 ? 9.027   12.631  -28.292 1.00 51.89  ? 381 TYR A CD1 1 
ATOM   2771 C CD2 . TYR A 1 352 ? 10.165  11.895  -30.253 1.00 51.33  ? 381 TYR A CD2 1 
ATOM   2772 C CE1 . TYR A 1 352 ? 10.035  13.547  -28.047 1.00 49.06  ? 381 TYR A CE1 1 
ATOM   2773 C CE2 . TYR A 1 352 ? 11.178  12.816  -30.020 1.00 49.73  ? 381 TYR A CE2 1 
ATOM   2774 C CZ  . TYR A 1 352 ? 11.109  13.641  -28.912 1.00 46.01  ? 381 TYR A CZ  1 
ATOM   2775 O OH  . TYR A 1 352 ? 12.054  14.579  -28.613 1.00 51.50  ? 381 TYR A OH  1 
ATOM   2776 N N   . LYS A 1 353 ? 5.628   12.073  -31.557 1.00 57.95  ? 382 LYS A N   1 
ATOM   2777 C CA  . LYS A 1 353 ? 5.132   13.028  -32.553 1.00 58.64  ? 382 LYS A CA  1 
ATOM   2778 C C   . LYS A 1 353 ? 3.887   13.781  -32.075 1.00 54.11  ? 382 LYS A C   1 
ATOM   2779 O O   . LYS A 1 353 ? 3.731   14.964  -32.378 1.00 54.17  ? 382 LYS A O   1 
ATOM   2780 C CB  . LYS A 1 353 ? 4.713   12.369  -33.877 1.00 62.36  ? 382 LYS A CB  1 
ATOM   2781 C CG  . LYS A 1 353 ? 5.768   11.602  -34.669 1.00 67.44  ? 382 LYS A CG  1 
ATOM   2782 C CD  . LYS A 1 353 ? 5.203   10.639  -35.715 1.00 67.93  ? 382 LYS A CD  1 
ATOM   2783 C CE  . LYS A 1 353 ? 4.105   11.231  -36.557 1.00 72.86  ? 382 LYS A CE  1 
ATOM   2784 N NZ  . LYS A 1 353 ? 3.573   10.294  -37.555 1.00 69.00  ? 382 LYS A NZ  1 
ATOM   2785 N N   . ILE A 1 354 ? 3.001   13.085  -31.344 1.00 58.72  ? 383 ILE A N   1 
ATOM   2786 C CA  . ILE A 1 354 ? 1.671   13.573  -30.979 1.00 53.34  ? 383 ILE A CA  1 
ATOM   2787 C C   . ILE A 1 354 ? 1.682   14.148  -29.566 1.00 47.97  ? 383 ILE A C   1 
ATOM   2788 O O   . ILE A 1 354 ? 1.319   15.299  -29.361 1.00 48.68  ? 383 ILE A O   1 
ATOM   2789 C CB  . ILE A 1 354 ? 0.637   12.431  -31.081 1.00 61.26  ? 383 ILE A CB  1 
ATOM   2790 C CG1 . ILE A 1 354 ? 0.559   11.836  -32.500 1.00 69.31  ? 383 ILE A CG1 1 
ATOM   2791 C CG2 . ILE A 1 354 ? -0.733  12.857  -30.558 1.00 61.14  ? 383 ILE A CG2 1 
ATOM   2792 C CD1 . ILE A 1 354 ? 0.434   12.860  -33.615 1.00 75.40  ? 383 ILE A CD1 1 
ATOM   2793 N N   . VAL A 1 355 ? 2.054   13.323  -28.579 1.00 43.69  ? 384 VAL A N   1 
ATOM   2794 C CA  . VAL A 1 355 ? 1.793   13.628  -27.178 1.00 40.22  ? 384 VAL A CA  1 
ATOM   2795 C C   . VAL A 1 355 ? 2.351   15.002  -26.814 1.00 46.62  ? 384 VAL A C   1 
ATOM   2796 O O   . VAL A 1 355 ? 1.658   15.761  -26.135 1.00 52.32  ? 384 VAL A O   1 
ATOM   2797 C CB  . VAL A 1 355 ? 2.290   12.536  -26.200 1.00 42.22  ? 384 VAL A CB  1 
ATOM   2798 C CG1 . VAL A 1 355 ? 2.163   12.964  -24.746 1.00 37.55  ? 384 VAL A CG1 1 
ATOM   2799 C CG2 . VAL A 1 355 ? 1.573   11.206  -26.429 1.00 43.78  ? 384 VAL A CG2 1 
ATOM   2800 N N   . PRO A 1 356 ? 3.595   15.395  -27.192 1.00 47.76  ? 385 PRO A N   1 
ATOM   2801 C CA  . PRO A 1 356 ? 4.107   16.711  -26.796 1.00 50.05  ? 385 PRO A CA  1 
ATOM   2802 C C   . PRO A 1 356 ? 3.270   17.878  -27.333 1.00 50.64  ? 385 PRO A C   1 
ATOM   2803 O O   . PRO A 1 356 ? 3.112   18.888  -26.650 1.00 54.59  ? 385 PRO A O   1 
ATOM   2804 C CB  . PRO A 1 356 ? 5.554   16.721  -27.341 1.00 55.64  ? 385 PRO A CB  1 
ATOM   2805 C CG  . PRO A 1 356 ? 5.896   15.260  -27.537 1.00 50.36  ? 385 PRO A CG  1 
ATOM   2806 C CD  . PRO A 1 356 ? 4.587   14.611  -27.945 1.00 49.29  ? 385 PRO A CD  1 
ATOM   2807 N N   . ASN A 1 357 ? 2.728   17.731  -28.551 1.00 57.50  ? 386 ASN A N   1 
ATOM   2808 C CA  . ASN A 1 357 ? 1.874   18.749  -29.155 1.00 68.43  ? 386 ASN A CA  1 
ATOM   2809 C C   . ASN A 1 357 ? 0.660   19.014  -28.265 1.00 64.92  ? 386 ASN A C   1 
ATOM   2810 O O   . ASN A 1 357 ? 0.476   20.133  -27.795 1.00 82.06  ? 386 ASN A O   1 
ATOM   2811 C CB  . ASN A 1 357 ? 1.455   18.364  -30.573 1.00 74.21  ? 386 ASN A CB  1 
ATOM   2812 C CG  . ASN A 1 357 ? 0.703   19.465  -31.286 1.00 74.24  ? 386 ASN A CG  1 
ATOM   2813 O OD1 . ASN A 1 357 ? -0.449  19.266  -31.686 1.00 66.62  ? 386 ASN A OD1 1 
ATOM   2814 N ND2 . ASN A 1 357 ? 1.329   20.621  -31.458 1.00 75.24  ? 386 ASN A ND2 1 
ATOM   2815 N N   . VAL A 1 358 ? -0.119  17.964  -27.984 1.00 65.40  ? 387 VAL A N   1 
ATOM   2816 C CA  . VAL A 1 358 ? -1.410  18.110  -27.325 1.00 66.35  ? 387 VAL A CA  1 
ATOM   2817 C C   . VAL A 1 358 ? -1.173  18.523  -25.873 1.00 64.34  ? 387 VAL A C   1 
ATOM   2818 O O   . VAL A 1 358 ? -1.977  19.264  -25.315 1.00 62.78  ? 387 VAL A O   1 
ATOM   2819 C CB  . VAL A 1 358 ? -2.352  16.884  -27.425 1.00 63.20  ? 387 VAL A CB  1 
ATOM   2820 C CG1 . VAL A 1 358 ? -1.963  15.932  -28.555 1.00 58.25  ? 387 VAL A CG1 1 
ATOM   2821 C CG2 . VAL A 1 358 ? -2.496  16.127  -26.109 1.00 62.49  ? 387 VAL A CG2 1 
ATOM   2822 N N   . LEU A 1 359 ? -0.066  18.067  -25.268 1.00 71.83  ? 388 LEU A N   1 
ATOM   2823 C CA  . LEU A 1 359 ? 0.218   18.344  -23.861 1.00 74.68  ? 388 LEU A CA  1 
ATOM   2824 C C   . LEU A 1 359 ? 0.398   19.846  -23.612 1.00 64.42  ? 388 LEU A C   1 
ATOM   2825 O O   . LEU A 1 359 ? 0.113   20.325  -22.511 1.00 63.20  ? 388 LEU A O   1 
ATOM   2826 C CB  . LEU A 1 359 ? 1.432   17.563  -23.343 1.00 77.69  ? 388 LEU A CB  1 
ATOM   2827 C CG  . LEU A 1 359 ? 1.174   16.176  -22.738 1.00 74.41  ? 388 LEU A CG  1 
ATOM   2828 C CD1 . LEU A 1 359 ? 2.389   15.755  -21.915 1.00 71.42  ? 388 LEU A CD1 1 
ATOM   2829 C CD2 . LEU A 1 359 ? -0.080  16.086  -21.877 1.00 76.06  ? 388 LEU A CD2 1 
ATOM   2830 N N   . LEU A 1 360 ? 0.890   20.588  -24.610 1.00 66.60  ? 389 LEU A N   1 
ATOM   2831 C CA  . LEU A 1 360 ? 1.021   22.029  -24.435 1.00 84.65  ? 389 LEU A CA  1 
ATOM   2832 C C   . LEU A 1 360 ? -0.289  22.694  -24.864 1.00 78.07  ? 389 LEU A C   1 
ATOM   2833 O O   . LEU A 1 360 ? -0.805  23.531  -24.117 1.00 66.60  ? 389 LEU A O   1 
ATOM   2834 C CB  . LEU A 1 360 ? 2.262   22.706  -25.034 1.00 91.04  ? 389 LEU A CB  1 
ATOM   2835 C CG  . LEU A 1 360 ? 2.943   22.069  -26.251 1.00 96.37  ? 389 LEU A CG  1 
ATOM   2836 C CD1 . LEU A 1 360 ? 2.450   22.637  -27.578 1.00 98.72  ? 389 LEU A CD1 1 
ATOM   2837 C CD2 . LEU A 1 360 ? 4.455   22.225  -26.121 1.00 86.93  ? 389 LEU A CD2 1 
ATOM   2838 N N   . GLU A 1 361 ? -0.856  22.259  -26.004 1.00 71.78  ? 390 GLU A N   1 
ATOM   2839 C CA  . GLU A 1 361 ? -2.187  22.688  -26.428 1.00 71.54  ? 390 GLU A CA  1 
ATOM   2840 C C   . GLU A 1 361 ? -3.153  22.706  -25.239 1.00 73.71  ? 390 GLU A C   1 
ATOM   2841 O O   . GLU A 1 361 ? -4.053  23.537  -25.202 1.00 85.06  ? 390 GLU A O   1 
ATOM   2842 C CB  . GLU A 1 361 ? -2.806  21.765  -27.476 1.00 75.90  ? 390 GLU A CB  1 
ATOM   2843 C CG  . GLU A 1 361 ? -3.635  22.490  -28.534 1.00 81.39  ? 390 GLU A CG  1 
ATOM   2844 C CD  . GLU A 1 361 ? -2.898  22.720  -29.843 1.00 81.92  ? 390 GLU A CD  1 
ATOM   2845 O OE1 . GLU A 1 361 ? -3.064  23.787  -30.479 1.00 72.24  ? 390 GLU A OE1 1 
ATOM   2846 O OE2 . GLU A 1 361 ? -2.155  21.791  -30.236 1.00 85.88  ? 390 GLU A OE2 1 
ATOM   2847 N N   . GLN A 1 362 ? -2.995  21.759  -24.298 1.00 74.79  ? 391 GLN A N   1 
ATOM   2848 C CA  . GLN A 1 362 ? -3.698  21.790  -23.021 1.00 77.60  ? 391 GLN A CA  1 
ATOM   2849 C C   . GLN A 1 362 ? -3.105  22.921  -22.179 1.00 85.07  ? 391 GLN A C   1 
ATOM   2850 O O   . GLN A 1 362 ? -3.746  23.955  -21.999 1.00 86.03  ? 391 GLN A O   1 
ATOM   2851 C CB  . GLN A 1 362 ? -3.633  20.424  -22.324 1.00 76.56  ? 391 GLN A CB  1 
ATOM   2852 C CG  . GLN A 1 362 ? -4.534  20.283  -21.097 1.00 73.68  ? 391 GLN A CG  1 
ATOM   2853 C CD  . GLN A 1 362 ? -4.117  19.208  -20.114 1.00 78.44  ? 391 GLN A CD  1 
ATOM   2854 O OE1 . GLN A 1 362 ? -4.723  19.058  -19.047 1.00 86.00  ? 391 GLN A OE1 1 
ATOM   2855 N NE2 . GLN A 1 362 ? -3.064  18.463  -20.418 1.00 81.36  ? 391 GLN A NE2 1 
ATOM   2856 N N   . GLY A 1 363 ? -1.868  22.726  -21.693 1.00 85.82  ? 392 GLY A N   1 
ATOM   2857 C CA  . GLY A 1 363 ? -1.144  23.752  -20.957 1.00 78.07  ? 392 GLY A CA  1 
ATOM   2858 C C   . GLY A 1 363 ? -1.025  23.459  -19.460 1.00 77.99  ? 392 GLY A C   1 
ATOM   2859 O O   . GLY A 1 363 ? -0.647  24.347  -18.703 1.00 70.82  ? 392 GLY A O   1 
ATOM   2860 N N   . LYS A 1 364 ? -1.322  22.222  -19.035 1.00 90.99  ? 393 LYS A N   1 
ATOM   2861 C CA  . LYS A 1 364 ? -1.225  21.839  -17.631 1.00 101.66 ? 393 LYS A CA  1 
ATOM   2862 C C   . LYS A 1 364 ? -0.094  20.821  -17.475 1.00 105.01 ? 393 LYS A C   1 
ATOM   2863 O O   . LYS A 1 364 ? -0.253  19.813  -16.788 1.00 107.21 ? 393 LYS A O   1 
ATOM   2864 C CB  . LYS A 1 364 ? -2.584  21.305  -17.149 1.00 107.84 ? 393 LYS A CB  1 
ATOM   2865 C CG  . LYS A 1 364 ? -2.904  21.491  -15.663 1.00 107.26 ? 393 LYS A CG  1 
ATOM   2866 C CD  . LYS A 1 364 ? -4.342  21.129  -15.296 1.00 105.19 ? 393 LYS A CD  1 
ATOM   2867 C CE  . LYS A 1 364 ? -4.849  21.798  -14.046 1.00 100.07 ? 393 LYS A CE  1 
ATOM   2868 N NZ  . LYS A 1 364 ? -5.136  23.224  -14.232 1.00 96.88  ? 393 LYS A NZ  1 
ATOM   2869 N N   . ALA A 1 365 ? 1.053   21.115  -18.106 1.00 99.54  ? 394 ALA A N   1 
ATOM   2870 C CA  . ALA A 1 365 ? 2.160   20.176  -18.220 1.00 90.41  ? 394 ALA A CA  1 
ATOM   2871 C C   . ALA A 1 365 ? 3.317   20.589  -17.304 1.00 80.16  ? 394 ALA A C   1 
ATOM   2872 O O   . ALA A 1 365 ? 3.509   19.996  -16.243 1.00 85.87  ? 394 ALA A O   1 
ATOM   2873 C CB  . ALA A 1 365 ? 2.585   20.078  -19.674 1.00 91.69  ? 394 ALA A CB  1 
ATOM   2874 N N   . LYS A 1 366 ? 4.079   21.615  -17.712 1.00 63.28  ? 395 LYS A N   1 
ATOM   2875 C CA  . LYS A 1 366 ? 5.331   21.991  -17.059 1.00 72.20  ? 395 LYS A CA  1 
ATOM   2876 C C   . LYS A 1 366 ? 6.500   21.286  -17.754 1.00 68.91  ? 395 LYS A C   1 
ATOM   2877 O O   . LYS A 1 366 ? 7.560   21.885  -17.915 1.00 69.13  ? 395 LYS A O   1 
ATOM   2878 C CB  . LYS A 1 366 ? 5.376   21.737  -15.543 1.00 72.29  ? 395 LYS A CB  1 
ATOM   2879 N N   . ASN A 1 367 ? 6.299   20.016  -18.148 1.00 72.48  ? 396 ASN A N   1 
ATOM   2880 C CA  . ASN A 1 367 ? 7.253   19.252  -18.943 1.00 68.68  ? 396 ASN A CA  1 
ATOM   2881 C C   . ASN A 1 367 ? 6.486   18.326  -19.899 1.00 66.85  ? 396 ASN A C   1 
ATOM   2882 O O   . ASN A 1 367 ? 6.129   17.197  -19.553 1.00 65.58  ? 396 ASN A O   1 
ATOM   2883 C CB  . ASN A 1 367 ? 8.228   18.518  -18.019 1.00 67.08  ? 396 ASN A CB  1 
ATOM   2884 C CG  . ASN A 1 367 ? 9.222   17.642  -18.743 1.00 65.73  ? 396 ASN A CG  1 
ATOM   2885 O OD1 . ASN A 1 367 ? 9.849   16.778  -18.111 1.00 75.88  ? 396 ASN A OD1 1 
ATOM   2886 N ND2 . ASN A 1 367 ? 9.382   17.833  -20.046 1.00 55.68  ? 396 ASN A ND2 1 
ATOM   2887 N N   . PRO A 1 368 ? 6.233   18.752  -21.156 1.00 66.85  ? 397 PRO A N   1 
ATOM   2888 C CA  . PRO A 1 368 ? 5.454   17.946  -22.109 1.00 64.68  ? 397 PRO A CA  1 
ATOM   2889 C C   . PRO A 1 368 ? 6.240   16.850  -22.823 1.00 57.47  ? 397 PRO A C   1 
ATOM   2890 O O   . PRO A 1 368 ? 5.712   16.190  -23.714 1.00 50.23  ? 397 PRO A O   1 
ATOM   2891 C CB  . PRO A 1 368 ? 4.982   19.024  -23.116 1.00 67.42  ? 397 PRO A CB  1 
ATOM   2892 C CG  . PRO A 1 368 ? 6.121   20.031  -23.146 1.00 64.41  ? 397 PRO A CG  1 
ATOM   2893 C CD  . PRO A 1 368 ? 6.720   20.013  -21.740 1.00 65.69  ? 397 PRO A CD  1 
ATOM   2894 N N   . TRP A 1 369 ? 7.519   16.698  -22.449 1.00 51.62  ? 398 TRP A N   1 
ATOM   2895 C CA  . TRP A 1 369 ? 8.447   15.846  -23.177 1.00 48.59  ? 398 TRP A CA  1 
ATOM   2896 C C   . TRP A 1 369 ? 8.626   14.532  -22.434 1.00 37.58  ? 398 TRP A C   1 
ATOM   2897 O O   . TRP A 1 369 ? 8.453   14.464  -21.211 1.00 38.99  ? 398 TRP A O   1 
ATOM   2898 C CB  . TRP A 1 369 ? 9.786   16.577  -23.383 1.00 51.50  ? 398 TRP A CB  1 
ATOM   2899 C CG  . TRP A 1 369 ? 9.597   17.868  -24.130 1.00 44.83  ? 398 TRP A CG  1 
ATOM   2900 C CD1 . TRP A 1 369 ? 9.592   19.145  -23.642 1.00 43.76  ? 398 TRP A CD1 1 
ATOM   2901 C CD2 . TRP A 1 369 ? 9.306   17.967  -25.537 1.00 40.69  ? 398 TRP A CD2 1 
ATOM   2902 N NE1 . TRP A 1 369 ? 9.348   20.032  -24.660 1.00 39.05  ? 398 TRP A NE1 1 
ATOM   2903 C CE2 . TRP A 1 369 ? 9.156   19.339  -25.826 1.00 39.75  ? 398 TRP A CE2 1 
ATOM   2904 C CE3 . TRP A 1 369 ? 9.174   17.030  -26.573 1.00 45.00  ? 398 TRP A CE3 1 
ATOM   2905 C CZ2 . TRP A 1 369 ? 8.876   19.788  -27.113 1.00 39.44  ? 398 TRP A CZ2 1 
ATOM   2906 C CZ3 . TRP A 1 369 ? 8.898   17.482  -27.845 1.00 45.17  ? 398 TRP A CZ3 1 
ATOM   2907 C CH2 . TRP A 1 369 ? 8.752   18.840  -28.105 1.00 40.86  ? 398 TRP A CH2 1 
ATOM   2908 N N   . PRO A 1 370 ? 8.990   13.451  -23.148 1.00 39.80  ? 399 PRO A N   1 
ATOM   2909 C CA  . PRO A 1 370 ? 9.100   12.135  -22.524 1.00 38.79  ? 399 PRO A CA  1 
ATOM   2910 C C   . PRO A 1 370 ? 10.351  12.018  -21.665 1.00 33.66  ? 399 PRO A C   1 
ATOM   2911 O O   . PRO A 1 370 ? 11.359  12.656  -21.948 1.00 34.51  ? 399 PRO A O   1 
ATOM   2912 C CB  . PRO A 1 370 ? 9.100   11.194  -23.725 1.00 39.13  ? 399 PRO A CB  1 
ATOM   2913 C CG  . PRO A 1 370 ? 9.727   12.014  -24.836 1.00 40.11  ? 399 PRO A CG  1 
ATOM   2914 C CD  . PRO A 1 370 ? 9.327   13.436  -24.586 1.00 40.94  ? 399 PRO A CD  1 
ATOM   2915 N N   . ASN A 1 371 ? 10.262  11.209  -20.604 1.00 35.82  ? 400 ASN A N   1 
ATOM   2916 C CA  . ASN A 1 371 ? 11.416  10.788  -19.820 1.00 34.32  ? 400 ASN A CA  1 
ATOM   2917 C C   . ASN A 1 371 ? 11.836  9.373   -20.248 1.00 35.92  ? 400 ASN A C   1 
ATOM   2918 O O   . ASN A 1 371 ? 11.173  8.767   -21.082 1.00 34.48  ? 400 ASN A O   1 
ATOM   2919 C CB  . ASN A 1 371 ? 11.083  10.884  -18.334 1.00 37.13  ? 400 ASN A CB  1 
ATOM   2920 C CG  . ASN A 1 371 ? 9.906   10.009  -17.976 1.00 43.27  ? 400 ASN A CG  1 
ATOM   2921 O OD1 . ASN A 1 371 ? 9.937   8.788   -18.199 1.00 46.09  ? 400 ASN A OD1 1 
ATOM   2922 N ND2 . ASN A 1 371 ? 8.845   10.615  -17.464 1.00 43.35  ? 400 ASN A ND2 1 
ATOM   2923 N N   . VAL A 1 372 ? 12.911  8.841   -19.618 1.00 36.36  ? 401 VAL A N   1 
ATOM   2924 C CA  . VAL A 1 372 ? 13.541  7.566   -19.954 1.00 36.98  ? 401 VAL A CA  1 
ATOM   2925 C C   . VAL A 1 372 ? 12.511  6.434   -19.959 1.00 36.32  ? 401 VAL A C   1 
ATOM   2926 O O   . VAL A 1 372 ? 12.541  5.586   -20.840 1.00 38.78  ? 401 VAL A O   1 
ATOM   2927 C CB  . VAL A 1 372 ? 14.730  7.248   -19.009 1.00 39.15  ? 401 VAL A CB  1 
ATOM   2928 C CG1 . VAL A 1 372 ? 14.353  7.160   -17.535 1.00 38.28  ? 401 VAL A CG1 1 
ATOM   2929 C CG2 . VAL A 1 372 ? 15.463  5.968   -19.395 1.00 41.86  ? 401 VAL A CG2 1 
ATOM   2930 N N   . ASP A 1 373 ? 11.572  6.439   -19.007 1.00 37.61  ? 402 ASP A N   1 
ATOM   2931 C CA  . ASP A 1 373 ? 10.699  5.295   -18.763 1.00 33.10  ? 402 ASP A CA  1 
ATOM   2932 C C   . ASP A 1 373 ? 9.671   5.127   -19.892 1.00 35.62  ? 402 ASP A C   1 
ATOM   2933 O O   . ASP A 1 373 ? 9.077   4.068   -20.036 1.00 33.36  ? 402 ASP A O   1 
ATOM   2934 C CB  . ASP A 1 373 ? 10.029  5.399   -17.408 1.00 35.59  ? 402 ASP A CB  1 
ATOM   2935 C CG  . ASP A 1 373 ? 11.006  5.384   -16.231 1.00 41.08  ? 402 ASP A CG  1 
ATOM   2936 O OD1 . ASP A 1 373 ? 11.738  4.366   -16.058 1.00 43.19  ? 402 ASP A OD1 1 
ATOM   2937 O OD2 . ASP A 1 373 ? 11.046  6.397   -15.488 1.00 45.02  ? 402 ASP A OD2 1 
ATOM   2938 N N   . ALA A 1 374 ? 9.510   6.152   -20.735 1.00 36.56  ? 403 ALA A N   1 
ATOM   2939 C CA  . ALA A 1 374 ? 8.604   6.068   -21.873 1.00 35.60  ? 403 ALA A CA  1 
ATOM   2940 C C   . ALA A 1 374 ? 9.095   5.065   -22.921 1.00 39.73  ? 403 ALA A C   1 
ATOM   2941 O O   . ALA A 1 374 ? 8.286   4.544   -23.693 1.00 39.77  ? 403 ALA A O   1 
ATOM   2942 C CB  . ALA A 1 374 ? 8.430   7.444   -22.469 1.00 36.50  ? 403 ALA A CB  1 
ATOM   2943 N N   . HIS A 1 375 ? 10.410  4.788   -22.929 1.00 37.32  ? 404 HIS A N   1 
ATOM   2944 C CA  . HIS A 1 375 ? 11.047  4.106   -24.049 1.00 34.99  ? 404 HIS A CA  1 
ATOM   2945 C C   . HIS A 1 375 ? 11.624  2.739   -23.690 1.00 39.01  ? 404 HIS A C   1 
ATOM   2946 O O   . HIS A 1 375 ? 11.869  1.962   -24.616 1.00 41.20  ? 404 HIS A O   1 
ATOM   2947 C CB  . HIS A 1 375 ? 12.111  4.985   -24.706 1.00 32.06  ? 404 HIS A CB  1 
ATOM   2948 C CG  . HIS A 1 375 ? 12.173  4.792   -26.191 1.00 32.76  ? 404 HIS A CG  1 
ATOM   2949 N ND1 . HIS A 1 375 ? 12.245  3.543   -26.760 1.00 34.94  ? 404 HIS A ND1 1 
ATOM   2950 C CD2 . HIS A 1 375 ? 12.112  5.666   -27.206 1.00 33.56  ? 404 HIS A CD2 1 
ATOM   2951 C CE1 . HIS A 1 375 ? 12.206  3.679   -28.087 1.00 39.22  ? 404 HIS A CE1 1 
ATOM   2952 N NE2 . HIS A 1 375 ? 12.151  4.967   -28.372 1.00 34.94  ? 404 HIS A NE2 1 
ATOM   2953 N N   . SER A 1 376 ? 11.858  2.423   -22.396 1.00 32.83  ? 405 SER A N   1 
ATOM   2954 C CA  . SER A 1 376 ? 12.651  1.237   -22.043 1.00 33.20  ? 405 SER A CA  1 
ATOM   2955 C C   . SER A 1 376 ? 11.885  -0.101  -22.158 1.00 33.44  ? 405 SER A C   1 
ATOM   2956 O O   . SER A 1 376 ? 12.426  -1.093  -22.628 1.00 32.05  ? 405 SER A O   1 
ATOM   2957 C CB  . SER A 1 376 ? 13.289  1.421   -20.670 1.00 31.43  ? 405 SER A CB  1 
ATOM   2958 O OG  . SER A 1 376 ? 12.667  2.514   -20.027 1.00 37.24  ? 405 SER A OG  1 
ATOM   2959 N N   . GLY A 1 377 ? 10.614  -0.134  -21.759 1.00 32.95  ? 406 GLY A N   1 
ATOM   2960 C CA  . GLY A 1 377 ? 9.818   -1.341  -21.760 1.00 32.63  ? 406 GLY A CA  1 
ATOM   2961 C C   . GLY A 1 377 ? 9.750   -1.993  -23.141 1.00 36.02  ? 406 GLY A C   1 
ATOM   2962 O O   . GLY A 1 377 ? 9.935   -3.191  -23.277 1.00 33.23  ? 406 GLY A O   1 
ATOM   2963 N N   . VAL A 1 378 ? 9.495   -1.202  -24.179 1.00 38.75  ? 407 VAL A N   1 
ATOM   2964 C CA  . VAL A 1 378 ? 9.301   -1.805  -25.487 1.00 39.50  ? 407 VAL A CA  1 
ATOM   2965 C C   . VAL A 1 378 ? 10.635  -2.343  -26.018 1.00 35.22  ? 407 VAL A C   1 
ATOM   2966 O O   . VAL A 1 378 ? 10.634  -3.315  -26.748 1.00 42.45  ? 407 VAL A O   1 
ATOM   2967 C CB  . VAL A 1 378 ? 8.620   -0.813  -26.436 1.00 39.87  ? 407 VAL A CB  1 
ATOM   2968 C CG1 . VAL A 1 378 ? 7.240   -0.445  -25.910 1.00 41.86  ? 407 VAL A CG1 1 
ATOM   2969 C CG2 . VAL A 1 378 ? 9.467   0.431   -26.675 1.00 39.93  ? 407 VAL A CG2 1 
ATOM   2970 N N   . LEU A 1 379 ? 11.779  -1.766  -25.610 1.00 38.18  ? 408 LEU A N   1 
ATOM   2971 C CA  . LEU A 1 379 ? 13.091  -2.318  -25.950 1.00 33.64  ? 408 LEU A CA  1 
ATOM   2972 C C   . LEU A 1 379 ? 13.314  -3.652  -25.235 1.00 35.65  ? 408 LEU A C   1 
ATOM   2973 O O   . LEU A 1 379 ? 13.723  -4.631  -25.863 1.00 36.88  ? 408 LEU A O   1 
ATOM   2974 C CB  . LEU A 1 379 ? 14.232  -1.345  -25.665 1.00 35.97  ? 408 LEU A CB  1 
ATOM   2975 C CG  . LEU A 1 379 ? 14.284  -0.096  -26.547 1.00 39.90  ? 408 LEU A CG  1 
ATOM   2976 C CD1 . LEU A 1 379 ? 15.310  0.918   -26.086 1.00 36.18  ? 408 LEU A CD1 1 
ATOM   2977 C CD2 . LEU A 1 379 ? 14.578  -0.505  -27.978 1.00 47.75  ? 408 LEU A CD2 1 
ATOM   2978 N N   . LEU A 1 380 ? 13.004  -3.726  -23.929 1.00 35.12  ? 409 LEU A N   1 
ATOM   2979 C CA  . LEU A 1 380 ? 13.156  -4.982  -23.197 1.00 29.66  ? 409 LEU A CA  1 
ATOM   2980 C C   . LEU A 1 380 ? 12.242  -6.070  -23.761 1.00 31.95  ? 409 LEU A C   1 
ATOM   2981 O O   . LEU A 1 380 ? 12.700  -7.178  -24.021 1.00 30.00  ? 409 LEU A O   1 
ATOM   2982 C CB  . LEU A 1 380 ? 12.916  -4.755  -21.699 1.00 30.55  ? 409 LEU A CB  1 
ATOM   2983 C CG  . LEU A 1 380 ? 13.917  -3.820  -21.011 1.00 29.77  ? 409 LEU A CG  1 
ATOM   2984 C CD1 . LEU A 1 380 ? 13.437  -3.430  -19.636 1.00 33.88  ? 409 LEU A CD1 1 
ATOM   2985 C CD2 . LEU A 1 380 ? 15.280  -4.495  -20.919 1.00 30.17  ? 409 LEU A CD2 1 
ATOM   2986 N N   . GLN A 1 381 ? 10.936  -5.773  -23.878 1.00 35.10  ? 410 GLN A N   1 
ATOM   2987 C CA  . GLN A 1 381 ? 9.968   -6.733  -24.388 1.00 36.24  ? 410 GLN A CA  1 
ATOM   2988 C C   . GLN A 1 381 ? 10.391  -7.234  -25.778 1.00 35.36  ? 410 GLN A C   1 
ATOM   2989 O O   . GLN A 1 381 ? 10.257  -8.406  -26.079 1.00 34.53  ? 410 GLN A O   1 
ATOM   2990 C CB  . GLN A 1 381 ? 8.578   -6.097  -24.339 1.00 42.07  ? 410 GLN A CB  1 
ATOM   2991 C CG  . GLN A 1 381 ? 7.478   -6.901  -25.017 1.00 46.55  ? 410 GLN A CG  1 
ATOM   2992 C CD  . GLN A 1 381 ? 6.105   -6.314  -24.771 1.00 51.65  ? 410 GLN A CD  1 
ATOM   2993 O OE1 . GLN A 1 381 ? 5.593   -5.527  -25.573 1.00 55.83  ? 410 GLN A OE1 1 
ATOM   2994 N NE2 . GLN A 1 381 ? 5.526   -6.641  -23.623 1.00 53.76  ? 410 GLN A NE2 1 
ATOM   2995 N N   . TYR A 1 382 ? 10.991  -6.383  -26.596 1.00 36.72  ? 411 TYR A N   1 
ATOM   2996 C CA  . TYR A 1 382 ? 11.382  -6.790  -27.934 1.00 39.70  ? 411 TYR A CA  1 
ATOM   2997 C C   . TYR A 1 382 ? 12.279  -8.029  -27.881 1.00 43.51  ? 411 TYR A C   1 
ATOM   2998 O O   . TYR A 1 382 ? 12.116  -8.932  -28.706 1.00 44.37  ? 411 TYR A O   1 
ATOM   2999 C CB  . TYR A 1 382 ? 12.050  -5.612  -28.648 1.00 37.68  ? 411 TYR A CB  1 
ATOM   3000 C CG  . TYR A 1 382 ? 12.475  -5.964  -30.065 1.00 41.19  ? 411 TYR A CG  1 
ATOM   3001 C CD1 . TYR A 1 382 ? 11.543  -6.044  -31.097 1.00 44.66  ? 411 TYR A CD1 1 
ATOM   3002 C CD2 . TYR A 1 382 ? 13.801  -6.267  -30.355 1.00 47.49  ? 411 TYR A CD2 1 
ATOM   3003 C CE1 . TYR A 1 382 ? 11.925  -6.376  -32.389 1.00 46.14  ? 411 TYR A CE1 1 
ATOM   3004 C CE2 . TYR A 1 382 ? 14.196  -6.612  -31.636 1.00 48.25  ? 411 TYR A CE2 1 
ATOM   3005 C CZ  . TYR A 1 382 ? 13.253  -6.668  -32.651 1.00 48.23  ? 411 TYR A CZ  1 
ATOM   3006 O OH  . TYR A 1 382 ? 13.669  -7.017  -33.892 1.00 49.95  ? 411 TYR A OH  1 
ATOM   3007 N N   . TYR A 1 383 ? 13.219  -8.075  -26.906 1.00 35.02  ? 412 TYR A N   1 
ATOM   3008 C CA  . TYR A 1 383 ? 14.295  -9.049  -26.906 1.00 32.90  ? 412 TYR A CA  1 
ATOM   3009 C C   . TYR A 1 383 ? 13.913  -10.290 -26.103 1.00 33.28  ? 412 TYR A C   1 
ATOM   3010 O O   . TYR A 1 383 ? 14.733  -11.193 -25.963 1.00 38.49  ? 412 TYR A O   1 
ATOM   3011 C CB  . TYR A 1 383 ? 15.580  -8.361  -26.426 1.00 35.08  ? 412 TYR A CB  1 
ATOM   3012 C CG  . TYR A 1 383 ? 16.240  -7.518  -27.494 1.00 33.79  ? 412 TYR A CG  1 
ATOM   3013 C CD1 . TYR A 1 383 ? 16.839  -8.102  -28.606 1.00 35.20  ? 412 TYR A CD1 1 
ATOM   3014 C CD2 . TYR A 1 383 ? 16.224  -6.130  -27.428 1.00 36.29  ? 412 TYR A CD2 1 
ATOM   3015 C CE1 . TYR A 1 383 ? 17.431  -7.325  -29.591 1.00 34.19  ? 412 TYR A CE1 1 
ATOM   3016 C CE2 . TYR A 1 383 ? 16.819  -5.348  -28.399 1.00 35.23  ? 412 TYR A CE2 1 
ATOM   3017 C CZ  . TYR A 1 383 ? 17.406  -5.944  -29.504 1.00 35.27  ? 412 TYR A CZ  1 
ATOM   3018 O OH  . TYR A 1 383 ? 17.978  -5.144  -30.463 1.00 36.19  ? 412 TYR A OH  1 
ATOM   3019 N N   . GLY A 1 384 ? 12.680  -10.346 -25.574 1.00 33.66  ? 413 GLY A N   1 
ATOM   3020 C CA  . GLY A 1 384 ? 12.162  -11.564 -24.972 1.00 35.08  ? 413 GLY A CA  1 
ATOM   3021 C C   . GLY A 1 384 ? 11.991  -11.445 -23.456 1.00 38.53  ? 413 GLY A C   1 
ATOM   3022 O O   . GLY A 1 384 ? 11.534  -12.388 -22.809 1.00 40.66  ? 413 GLY A O   1 
ATOM   3023 N N   . MET A 1 385 ? 12.350  -10.266 -22.920 1.00 36.53  ? 414 MET A N   1 
ATOM   3024 C CA  . MET A 1 385 ? 12.315  -9.983  -21.495 1.00 34.87  ? 414 MET A CA  1 
ATOM   3025 C C   . MET A 1 385 ? 11.005  -9.284  -21.174 1.00 33.56  ? 414 MET A C   1 
ATOM   3026 O O   . MET A 1 385 ? 10.962  -8.057  -21.155 1.00 34.82  ? 414 MET A O   1 
ATOM   3027 C CB  . MET A 1 385 ? 13.538  -9.117  -21.125 1.00 34.18  ? 414 MET A CB  1 
ATOM   3028 C CG  . MET A 1 385 ? 13.365  -8.311  -19.859 1.00 41.33  ? 414 MET A CG  1 
ATOM   3029 S SD  . MET A 1 385 ? 14.609  -8.499  -18.571 1.00 37.82  ? 414 MET A SD  1 
ATOM   3030 C CE  . MET A 1 385 ? 16.009  -9.568  -18.934 1.00 35.98  ? 414 MET A CE  1 
ATOM   3031 N N   . THR A 1 386 ? 9.967   -10.081 -20.891 1.00 32.90  ? 415 THR A N   1 
ATOM   3032 C CA  . THR A 1 386 ? 8.603   -9.612  -20.811 1.00 34.78  ? 415 THR A CA  1 
ATOM   3033 C C   . THR A 1 386 ? 8.149   -9.594  -19.358 1.00 35.44  ? 415 THR A C   1 
ATOM   3034 O O   . THR A 1 386 ? 6.985   -9.314  -19.087 1.00 32.34  ? 415 THR A O   1 
ATOM   3035 C CB  . THR A 1 386 ? 7.685   -10.543 -21.609 1.00 41.64  ? 415 THR A CB  1 
ATOM   3036 O OG1 . THR A 1 386 ? 7.806   -11.788 -20.923 1.00 42.22  ? 415 THR A OG1 1 
ATOM   3037 C CG2 . THR A 1 386 ? 8.054   -10.636 -23.080 1.00 44.11  ? 415 THR A CG2 1 
ATOM   3038 N N   . GLU A 1 387 ? 9.055   -9.940  -18.439 1.00 37.15  ? 416 GLU A N   1 
ATOM   3039 C CA  . GLU A 1 387 ? 8.679   -10.054 -17.044 1.00 36.44  ? 416 GLU A CA  1 
ATOM   3040 C C   . GLU A 1 387 ? 8.811   -8.675  -16.396 1.00 34.47  ? 416 GLU A C   1 
ATOM   3041 O O   . GLU A 1 387 ? 9.828   -8.354  -15.790 1.00 29.95  ? 416 GLU A O   1 
ATOM   3042 C CB  . GLU A 1 387 ? 9.519   -11.138 -16.377 1.00 36.74  ? 416 GLU A CB  1 
ATOM   3043 C CG  . GLU A 1 387 ? 9.356   -12.514 -17.016 1.00 34.54  ? 416 GLU A CG  1 
ATOM   3044 C CD  . GLU A 1 387 ? 10.353  -12.871 -18.092 1.00 34.19  ? 416 GLU A CD  1 
ATOM   3045 O OE1 . GLU A 1 387 ? 10.318  -14.040 -18.541 1.00 38.02  ? 416 GLU A OE1 1 
ATOM   3046 O OE2 . GLU A 1 387 ? 11.162  -12.009 -18.478 1.00 32.03  ? 416 GLU A OE2 1 
ATOM   3047 N N   . MET A 1 388 ? 7.743   -7.887  -16.527 1.00 32.82  ? 417 MET A N   1 
ATOM   3048 C CA  . MET A 1 388 ? 7.724   -6.484  -16.157 1.00 31.01  ? 417 MET A CA  1 
ATOM   3049 C C   . MET A 1 388 ? 8.170   -6.251  -14.720 1.00 29.28  ? 417 MET A C   1 
ATOM   3050 O O   . MET A 1 388 ? 8.798   -5.249  -14.458 1.00 31.69  ? 417 MET A O   1 
ATOM   3051 C CB  . MET A 1 388 ? 6.314   -5.911  -16.311 1.00 31.37  ? 417 MET A CB  1 
ATOM   3052 C CG  . MET A 1 388 ? 5.933   -5.774  -17.755 1.00 40.95  ? 417 MET A CG  1 
ATOM   3053 S SD  . MET A 1 388 ? 4.351   -4.928  -17.862 1.00 41.98  ? 417 MET A SD  1 
ATOM   3054 C CE  . MET A 1 388 ? 4.019   -5.778  -19.413 1.00 54.78  ? 417 MET A CE  1 
ATOM   3055 N N   . ASN A 1 389 ? 7.751   -7.114  -13.808 1.00 30.06  ? 418 ASN A N   1 
ATOM   3056 C CA  . ASN A 1 389 ? 8.111   -7.018  -12.401 1.00 33.17  ? 418 ASN A CA  1 
ATOM   3057 C C   . ASN A 1 389 ? 9.630   -7.014  -12.194 1.00 32.66  ? 418 ASN A C   1 
ATOM   3058 O O   . ASN A 1 389 ? 10.079  -6.566  -11.144 1.00 34.32  ? 418 ASN A O   1 
ATOM   3059 C CB  . ASN A 1 389 ? 7.489   -8.190  -11.646 1.00 33.95  ? 418 ASN A CB  1 
ATOM   3060 C CG  . ASN A 1 389 ? 6.026   -7.977  -11.349 1.00 40.50  ? 418 ASN A CG  1 
ATOM   3061 O OD1 . ASN A 1 389 ? 5.459   -6.941  -11.704 1.00 40.48  ? 418 ASN A OD1 1 
ATOM   3062 N ND2 . ASN A 1 389 ? 5.408   -8.933  -10.674 1.00 44.36  ? 418 ASN A ND2 1 
ATOM   3063 N N   . TYR A 1 390 ? 10.402  -7.523  -13.176 1.00 24.97  ? 419 TYR A N   1 
ATOM   3064 C CA  . TYR A 1 390 ? 11.862  -7.627  -13.103 1.00 26.30  ? 419 TYR A CA  1 
ATOM   3065 C C   . TYR A 1 390 ? 12.575  -6.358  -13.579 1.00 25.55  ? 419 TYR A C   1 
ATOM   3066 O O   . TYR A 1 390 ? 13.763  -6.129  -13.311 1.00 23.72  ? 419 TYR A O   1 
ATOM   3067 C CB  . TYR A 1 390 ? 12.338  -8.842  -13.929 1.00 24.63  ? 419 TYR A CB  1 
ATOM   3068 C CG  . TYR A 1 390 ? 13.822  -9.128  -13.762 1.00 24.07  ? 419 TYR A CG  1 
ATOM   3069 C CD1 . TYR A 1 390 ? 14.290  -9.771  -12.626 1.00 24.59  ? 419 TYR A CD1 1 
ATOM   3070 C CD2 . TYR A 1 390 ? 14.770  -8.690  -14.680 1.00 22.90  ? 419 TYR A CD2 1 
ATOM   3071 C CE1 . TYR A 1 390 ? 15.632  -10.026 -12.452 1.00 22.09  ? 419 TYR A CE1 1 
ATOM   3072 C CE2 . TYR A 1 390 ? 16.125  -8.939  -14.505 1.00 22.92  ? 419 TYR A CE2 1 
ATOM   3073 C CZ  . TYR A 1 390 ? 16.559  -9.610  -13.388 1.00 22.52  ? 419 TYR A CZ  1 
ATOM   3074 O OH  . TYR A 1 390 ? 17.886  -9.896  -13.191 1.00 22.75  ? 419 TYR A OH  1 
ATOM   3075 N N   . TYR A 1 391 ? 11.880  -5.520  -14.351 1.00 27.97  ? 420 TYR A N   1 
ATOM   3076 C CA  . TYR A 1 391 ? 12.518  -4.389  -15.012 1.00 27.65  ? 420 TYR A CA  1 
ATOM   3077 C C   . TYR A 1 391 ? 13.267  -3.460  -14.054 1.00 26.77  ? 420 TYR A C   1 
ATOM   3078 O O   . TYR A 1 391 ? 14.324  -2.925  -14.396 1.00 27.18  ? 420 TYR A O   1 
ATOM   3079 C CB  . TYR A 1 391 ? 11.481  -3.550  -15.759 1.00 31.86  ? 420 TYR A CB  1 
ATOM   3080 C CG  . TYR A 1 391 ? 10.903  -4.242  -16.993 1.00 31.84  ? 420 TYR A CG  1 
ATOM   3081 C CD1 . TYR A 1 391 ? 11.376  -5.468  -17.419 1.00 32.64  ? 420 TYR A CD1 1 
ATOM   3082 C CD2 . TYR A 1 391 ? 9.915   -3.631  -17.758 1.00 33.42  ? 420 TYR A CD2 1 
ATOM   3083 C CE1 . TYR A 1 391 ? 10.885  -6.064  -18.574 1.00 36.79  ? 420 TYR A CE1 1 
ATOM   3084 C CE2 . TYR A 1 391 ? 9.425   -4.211  -18.918 1.00 35.45  ? 420 TYR A CE2 1 
ATOM   3085 C CZ  . TYR A 1 391 ? 9.903   -5.446  -19.319 1.00 34.62  ? 420 TYR A CZ  1 
ATOM   3086 O OH  . TYR A 1 391 ? 9.446   -6.074  -20.440 1.00 36.93  ? 420 TYR A OH  1 
ATOM   3087 N N   . THR A 1 392 ? 12.722  -3.246  -12.864 1.00 22.86  ? 421 THR A N   1 
ATOM   3088 C CA  . THR A 1 392 ? 13.340  -2.319  -11.931 1.00 24.62  ? 421 THR A CA  1 
ATOM   3089 C C   . THR A 1 392 ? 14.637  -2.908  -11.341 1.00 22.27  ? 421 THR A C   1 
ATOM   3090 O O   . THR A 1 392 ? 15.521  -2.168  -10.878 1.00 22.25  ? 421 THR A O   1 
ATOM   3091 C CB  . THR A 1 392 ? 12.341  -1.936  -10.851 1.00 23.92  ? 421 THR A CB  1 
ATOM   3092 O OG1 . THR A 1 392 ? 11.150  -1.512  -11.530 1.00 25.42  ? 421 THR A OG1 1 
ATOM   3093 C CG2 . THR A 1 392 ? 12.915  -0.847  -9.963  1.00 28.48  ? 421 THR A CG2 1 
ATOM   3094 N N   . VAL A 1 393 ? 14.800  -4.231  -11.419 1.00 23.26  ? 422 VAL A N   1 
ATOM   3095 C CA  . VAL A 1 393 ? 16.034  -4.882  -10.984 1.00 22.97  ? 422 VAL A CA  1 
ATOM   3096 C C   . VAL A 1 393 ? 17.170  -4.394  -11.883 1.00 19.80  ? 422 VAL A C   1 
ATOM   3097 O O   . VAL A 1 393 ? 18.216  -4.008  -11.399 1.00 21.72  ? 422 VAL A O   1 
ATOM   3098 C CB  . VAL A 1 393 ? 15.960  -6.434  -10.925 1.00 22.58  ? 422 VAL A CB  1 
ATOM   3099 C CG1 . VAL A 1 393 ? 17.329  -7.063  -10.704 1.00 21.94  ? 422 VAL A CG1 1 
ATOM   3100 C CG2 . VAL A 1 393 ? 15.018  -6.939  -9.826  1.00 22.96  ? 422 VAL A CG2 1 
ATOM   3101 N N   . LEU A 1 394 ? 16.946  -4.308  -13.198 1.00 20.82  ? 423 LEU A N   1 
ATOM   3102 C CA  . LEU A 1 394 ? 17.935  -3.773  -14.112 1.00 20.80  ? 423 LEU A CA  1 
ATOM   3103 C C   . LEU A 1 394 ? 18.307  -2.327  -13.799 1.00 18.80  ? 423 LEU A C   1 
ATOM   3104 O O   . LEU A 1 394 ? 19.482  -1.969  -13.820 1.00 20.05  ? 423 LEU A O   1 
ATOM   3105 C CB  . LEU A 1 394 ? 17.391  -3.878  -15.547 1.00 24.30  ? 423 LEU A CB  1 
ATOM   3106 C CG  . LEU A 1 394 ? 17.060  -5.297  -16.016 1.00 26.86  ? 423 LEU A CG  1 
ATOM   3107 C CD1 . LEU A 1 394 ? 16.431  -5.253  -17.404 1.00 29.77  ? 423 LEU A CD1 1 
ATOM   3108 C CD2 . LEU A 1 394 ? 18.338  -6.132  -16.026 1.00 27.01  ? 423 LEU A CD2 1 
ATOM   3109 N N   . PHE A 1 395 ? 17.306  -1.500  -13.518 1.00 20.11  ? 424 PHE A N   1 
ATOM   3110 C CA  . PHE A 1 395 ? 17.529  -0.127  -13.103 1.00 19.24  ? 424 PHE A CA  1 
ATOM   3111 C C   . PHE A 1 395 ? 18.435  -0.133  -11.875 1.00 19.66  ? 424 PHE A C   1 
ATOM   3112 O O   . PHE A 1 395 ? 19.415  0.590   -11.828 1.00 22.63  ? 424 PHE A O   1 
ATOM   3113 C CB  . PHE A 1 395 ? 16.141  0.471   -12.880 1.00 20.22  ? 424 PHE A CB  1 
ATOM   3114 C CG  . PHE A 1 395 ? 16.008  1.979   -12.795 1.00 22.41  ? 424 PHE A CG  1 
ATOM   3115 C CD1 . PHE A 1 395 ? 17.042  2.797   -12.391 1.00 24.24  ? 424 PHE A CD1 1 
ATOM   3116 C CD2 . PHE A 1 395 ? 14.785  2.580   -13.085 1.00 28.39  ? 424 PHE A CD2 1 
ATOM   3117 C CE1 . PHE A 1 395 ? 16.901  4.183   -12.344 1.00 24.18  ? 424 PHE A CE1 1 
ATOM   3118 C CE2 . PHE A 1 395 ? 14.655  3.975   -13.066 1.00 29.23  ? 424 PHE A CE2 1 
ATOM   3119 C CZ  . PHE A 1 395 ? 15.719  4.762   -12.669 1.00 28.88  ? 424 PHE A CZ  1 
ATOM   3120 N N   . GLY A 1 396 ? 18.076  -0.923  -10.864 1.00 21.15  ? 425 GLY A N   1 
ATOM   3121 C CA  . GLY A 1 396 ? 18.860  -1.018  -9.650  1.00 19.96  ? 425 GLY A CA  1 
ATOM   3122 C C   . GLY A 1 396 ? 20.338  -1.346  -9.897  1.00 21.63  ? 425 GLY A C   1 
ATOM   3123 O O   . GLY A 1 396 ? 21.221  -0.714  -9.320  1.00 22.79  ? 425 GLY A O   1 
ATOM   3124 N N   . VAL A 1 397 ? 20.623  -2.383  -10.701 1.00 20.72  ? 426 VAL A N   1 
ATOM   3125 C CA  . VAL A 1 397 ? 22.004  -2.759  -11.008 1.00 23.28  ? 426 VAL A CA  1 
ATOM   3126 C C   . VAL A 1 397 ? 22.778  -1.588  -11.639 1.00 21.29  ? 426 VAL A C   1 
ATOM   3127 O O   . VAL A 1 397 ? 23.950  -1.293  -11.297 1.00 19.53  ? 426 VAL A O   1 
ATOM   3128 C CB  . VAL A 1 397 ? 21.949  -3.973  -11.934 1.00 20.95  ? 426 VAL A CB  1 
ATOM   3129 C CG1 . VAL A 1 397 ? 23.321  -4.303  -12.534 1.00 21.69  ? 426 VAL A CG1 1 
ATOM   3130 C CG2 . VAL A 1 397 ? 21.355  -5.174  -11.232 1.00 23.54  ? 426 VAL A CG2 1 
ATOM   3131 N N   . SER A 1 398 ? 22.144  -0.933  -12.611 1.00 22.00  ? 427 SER A N   1 
ATOM   3132 C CA  . SER A 1 398 ? 22.692  0.290   -13.191 1.00 21.27  ? 427 SER A CA  1 
ATOM   3133 C C   . SER A 1 398 ? 23.018  1.344   -12.136 1.00 19.22  ? 427 SER A C   1 
ATOM   3134 O O   . SER A 1 398 ? 24.129  1.891   -12.078 1.00 19.64  ? 427 SER A O   1 
ATOM   3135 C CB  . SER A 1 398 ? 21.772  0.866   -14.224 1.00 18.98  ? 427 SER A CB  1 
ATOM   3136 O OG  . SER A 1 398 ? 22.332  2.055   -14.773 1.00 17.65  ? 427 SER A OG  1 
ATOM   3137 N N   . ARG A 1 399 ? 22.001  1.686   -11.363 1.00 19.61  ? 428 ARG A N   1 
ATOM   3138 C CA  . ARG A 1 399 ? 22.120  2.771   -10.384 1.00 21.51  ? 428 ARG A CA  1 
ATOM   3139 C C   . ARG A 1 399 ? 23.223  2.544   -9.320  1.00 19.14  ? 428 ARG A C   1 
ATOM   3140 O O   . ARG A 1 399 ? 23.694  3.508   -8.737  1.00 19.18  ? 428 ARG A O   1 
ATOM   3141 C CB  . ARG A 1 399 ? 20.733  2.957   -9.750  1.00 20.71  ? 428 ARG A CB  1 
ATOM   3142 C CG  . ARG A 1 399 ? 20.607  4.152   -8.811  1.00 21.08  ? 428 ARG A CG  1 
ATOM   3143 C CD  . ARG A 1 399 ? 21.096  5.490   -9.387  1.00 22.53  ? 428 ARG A CD  1 
ATOM   3144 N NE  . ARG A 1 399 ? 20.607  5.891   -10.714 1.00 23.98  ? 428 ARG A NE  1 
ATOM   3145 C CZ  . ARG A 1 399 ? 19.495  6.621   -10.971 1.00 24.18  ? 428 ARG A CZ  1 
ATOM   3146 N NH1 . ARG A 1 399 ? 18.734  7.056   -9.967  1.00 21.09  ? 428 ARG A NH1 1 
ATOM   3147 N NH2 . ARG A 1 399 ? 19.168  6.914   -12.235 1.00 22.96  ? 428 ARG A NH2 1 
ATOM   3148 N N   . ALA A 1 400 ? 23.580  1.298   -9.001  1.00 17.38  ? 429 ALA A N   1 
ATOM   3149 C CA  . ALA A 1 400 ? 24.732  1.005   -8.142  1.00 18.12  ? 429 ALA A CA  1 
ATOM   3150 C C   . ALA A 1 400 ? 25.983  1.764   -8.560  1.00 17.92  ? 429 ALA A C   1 
ATOM   3151 O O   . ALA A 1 400 ? 26.747  2.248   -7.723  1.00 18.56  ? 429 ALA A O   1 
ATOM   3152 C CB  . ALA A 1 400 ? 25.025  -0.480  -8.149  1.00 19.67  ? 429 ALA A CB  1 
ATOM   3153 N N   . LEU A 1 401 ? 26.207  1.861   -9.875  1.00 19.31  ? 430 LEU A N   1 
ATOM   3154 C CA  . LEU A 1 401 ? 27.405  2.508   -10.382 1.00 19.54  ? 430 LEU A CA  1 
ATOM   3155 C C   . LEU A 1 401 ? 27.452  3.954   -9.919  1.00 18.90  ? 430 LEU A C   1 
ATOM   3156 O O   . LEU A 1 401 ? 28.469  4.403   -9.389  1.00 20.55  ? 430 LEU A O   1 
ATOM   3157 C CB  . LEU A 1 401 ? 27.409  2.425   -11.905 1.00 19.31  ? 430 LEU A CB  1 
ATOM   3158 C CG  . LEU A 1 401 ? 27.430  1.002   -12.465 1.00 21.38  ? 430 LEU A CG  1 
ATOM   3159 C CD1 . LEU A 1 401 ? 27.418  1.083   -13.976 1.00 23.67  ? 430 LEU A CD1 1 
ATOM   3160 C CD2 . LEU A 1 401 ? 28.582  0.179   -11.965 1.00 24.43  ? 430 LEU A CD2 1 
ATOM   3161 N N   . GLY A 1 402 ? 26.335  4.667   -10.081 1.00 17.42  ? 431 GLY A N   1 
ATOM   3162 C CA  . GLY A 1 402 ? 26.329  6.079   -9.693  1.00 17.84  ? 431 GLY A CA  1 
ATOM   3163 C C   . GLY A 1 402 ? 26.419  6.287   -8.177  1.00 17.78  ? 431 GLY A C   1 
ATOM   3164 O O   . GLY A 1 402 ? 27.224  7.087   -7.675  1.00 17.41  ? 431 GLY A O   1 
ATOM   3165 N N   . VAL A 1 403 ? 25.563  5.582   -7.441  1.00 18.24  ? 432 VAL A N   1 
ATOM   3166 C CA  . VAL A 1 403 ? 25.453  5.856   -6.015  1.00 19.01  ? 432 VAL A CA  1 
ATOM   3167 C C   . VAL A 1 403 ? 26.696  5.400   -5.245  1.00 17.90  ? 432 VAL A C   1 
ATOM   3168 O O   . VAL A 1 403 ? 27.098  6.050   -4.286  1.00 19.92  ? 432 VAL A O   1 
ATOM   3169 C CB  . VAL A 1 403 ? 24.138  5.313   -5.412  1.00 19.69  ? 432 VAL A CB  1 
ATOM   3170 C CG1 . VAL A 1 403 ? 22.931  5.757   -6.222  1.00 20.11  ? 432 VAL A CG1 1 
ATOM   3171 C CG2 . VAL A 1 403 ? 24.090  3.809   -5.226  1.00 19.00  ? 432 VAL A CG2 1 
ATOM   3172 N N   . LEU A 1 404 ? 27.314  4.288   -5.663  1.00 19.32  ? 433 LEU A N   1 
ATOM   3173 C CA  . LEU A 1 404 ? 28.545  3.793   -5.054  1.00 18.36  ? 433 LEU A CA  1 
ATOM   3174 C C   . LEU A 1 404 ? 29.719  4.681   -5.439  1.00 17.98  ? 433 LEU A C   1 
ATOM   3175 O O   . LEU A 1 404 ? 30.575  4.960   -4.600  1.00 18.42  ? 433 LEU A O   1 
ATOM   3176 C CB  . LEU A 1 404 ? 28.785  2.309   -5.379  1.00 18.45  ? 433 LEU A CB  1 
ATOM   3177 C CG  . LEU A 1 404 ? 27.677  1.354   -4.919  1.00 18.52  ? 433 LEU A CG  1 
ATOM   3178 C CD1 . LEU A 1 404 ? 27.893  -0.040  -5.381  1.00 18.41  ? 433 LEU A CD1 1 
ATOM   3179 C CD2 . LEU A 1 404 ? 27.579  1.363   -3.404  1.00 20.86  ? 433 LEU A CD2 1 
ATOM   3180 N N   . ALA A 1 405 ? 29.793  5.145   -6.703  1.00 19.34  ? 434 ALA A N   1 
ATOM   3181 C CA  . ALA A 1 405 ? 30.814  6.108   -7.039  1.00 17.02  ? 434 ALA A CA  1 
ATOM   3182 C C   . ALA A 1 405 ? 30.736  7.297   -6.105  1.00 19.44  ? 434 ALA A C   1 
ATOM   3183 O O   . ALA A 1 405 ? 31.754  7.841   -5.709  1.00 20.17  ? 434 ALA A O   1 
ATOM   3184 C CB  . ALA A 1 405 ? 30.713  6.573   -8.475  1.00 18.97  ? 434 ALA A CB  1 
ATOM   3185 N N   . GLN A 1 406 ? 29.525  7.775   -5.819  1.00 18.47  ? 435 GLN A N   1 
ATOM   3186 C CA  . GLN A 1 406 ? 29.401  8.974   -5.025  1.00 19.16  ? 435 GLN A CA  1 
ATOM   3187 C C   . GLN A 1 406 ? 29.738  8.598   -3.577  1.00 18.98  ? 435 GLN A C   1 
ATOM   3188 O O   . GLN A 1 406 ? 30.393  9.354   -2.862  1.00 18.88  ? 435 GLN A O   1 
ATOM   3189 C CB  . GLN A 1 406 ? 28.015  9.600   -5.083  1.00 20.35  ? 435 GLN A CB  1 
ATOM   3190 C CG  . GLN A 1 406 ? 27.813  10.756  -4.103  1.00 20.40  ? 435 GLN A CG  1 
ATOM   3191 C CD  . GLN A 1 406 ? 28.829  11.882  -4.241  1.00 23.31  ? 435 GLN A CD  1 
ATOM   3192 O OE1 . GLN A 1 406 ? 29.128  12.376  -5.325  1.00 26.14  ? 435 GLN A OE1 1 
ATOM   3193 N NE2 . GLN A 1 406 ? 29.393  12.330  -3.136  1.00 25.50  ? 435 GLN A NE2 1 
ATOM   3194 N N   . LEU A 1 407 ? 29.335  7.406   -3.149  1.00 19.35  ? 436 LEU A N   1 
ATOM   3195 C CA  . LEU A 1 407 ? 29.549  7.008   -1.746  1.00 18.62  ? 436 LEU A CA  1 
ATOM   3196 C C   . LEU A 1 407 ? 31.050  6.968   -1.406  1.00 17.50  ? 436 LEU A C   1 
ATOM   3197 O O   . LEU A 1 407 ? 31.467  7.316   -0.327  1.00 19.17  ? 436 LEU A O   1 
ATOM   3198 C CB  . LEU A 1 407 ? 28.895  5.645   -1.530  1.00 19.67  ? 436 LEU A CB  1 
ATOM   3199 C CG  . LEU A 1 407 ? 28.944  5.127   -0.080  1.00 20.33  ? 436 LEU A CG  1 
ATOM   3200 C CD1 . LEU A 1 407 ? 28.089  5.987   0.803   1.00 20.72  ? 436 LEU A CD1 1 
ATOM   3201 C CD2 . LEU A 1 407 ? 28.508  3.701   0.044   1.00 22.31  ? 436 LEU A CD2 1 
ATOM   3202 N N   . ILE A 1 408 ? 31.884  6.529   -2.348  1.00 18.59  ? 437 ILE A N   1 
ATOM   3203 C CA  . ILE A 1 408 ? 33.325  6.580   -2.182  1.00 18.56  ? 437 ILE A CA  1 
ATOM   3204 C C   . ILE A 1 408 ? 33.745  8.023   -1.887  1.00 18.45  ? 437 ILE A C   1 
ATOM   3205 O O   . ILE A 1 408 ? 34.487  8.297   -0.945  1.00 20.15  ? 437 ILE A O   1 
ATOM   3206 C CB  . ILE A 1 408 ? 34.015  5.969   -3.416  1.00 19.94  ? 437 ILE A CB  1 
ATOM   3207 C CG1 . ILE A 1 408 ? 33.676  4.460   -3.537  1.00 20.64  ? 437 ILE A CG1 1 
ATOM   3208 C CG2 . ILE A 1 408 ? 35.535  6.196   -3.366  1.00 20.58  ? 437 ILE A CG2 1 
ATOM   3209 C CD1 . ILE A 1 408 ? 34.009  3.853   -4.877  1.00 20.47  ? 437 ILE A CD1 1 
ATOM   3210 N N   . TRP A 1 409 ? 33.307  8.939   -2.733  1.00 20.63  ? 438 TRP A N   1 
ATOM   3211 C CA  . TRP A 1 409 ? 33.639  10.340  -2.563  1.00 21.05  ? 438 TRP A CA  1 
ATOM   3212 C C   . TRP A 1 409 ? 33.096  10.964  -1.273  1.00 19.01  ? 438 TRP A C   1 
ATOM   3213 O O   . TRP A 1 409 ? 33.766  11.787  -0.691  1.00 17.20  ? 438 TRP A O   1 
ATOM   3214 C CB  . TRP A 1 409 ? 33.210  11.081  -3.831  1.00 22.50  ? 438 TRP A CB  1 
ATOM   3215 C CG  . TRP A 1 409 ? 34.256  10.981  -4.900  1.00 23.60  ? 438 TRP A CG  1 
ATOM   3216 C CD1 . TRP A 1 409 ? 34.276  10.174  -6.006  1.00 25.65  ? 438 TRP A CD1 1 
ATOM   3217 C CD2 . TRP A 1 409 ? 35.522  11.670  -4.888  1.00 22.72  ? 438 TRP A CD2 1 
ATOM   3218 N NE1 . TRP A 1 409 ? 35.448  10.343  -6.702  1.00 21.42  ? 438 TRP A NE1 1 
ATOM   3219 C CE2 . TRP A 1 409 ? 36.223  11.254  -6.038  1.00 23.56  ? 438 TRP A CE2 1 
ATOM   3220 C CE3 . TRP A 1 409 ? 36.101  12.622  -4.044  1.00 25.87  ? 438 TRP A CE3 1 
ATOM   3221 C CZ2 . TRP A 1 409 ? 37.492  11.756  -6.346  1.00 23.94  ? 438 TRP A CZ2 1 
ATOM   3222 C CZ3 . TRP A 1 409 ? 37.361  13.112  -4.345  1.00 26.89  ? 438 TRP A CZ3 1 
ATOM   3223 C CH2 . TRP A 1 409 ? 38.025  12.695  -5.497  1.00 26.21  ? 438 TRP A CH2 1 
ATOM   3224 N N   . SER A 1 410 ? 31.829  10.724  -0.905  1.00 17.46  ? 439 SER A N   1 
ATOM   3225 C CA  . SER A 1 410 ? 31.289  11.230  0.342   1.00 19.86  ? 439 SER A CA  1 
ATOM   3226 C C   . SER A 1 410 ? 32.186  10.890  1.534   1.00 18.81  ? 439 SER A C   1 
ATOM   3227 O O   . SER A 1 410 ? 32.497  11.765  2.371   1.00 20.57  ? 439 SER A O   1 
ATOM   3228 C CB  . SER A 1 410 ? 29.860  10.703  0.552   1.00 21.43  ? 439 SER A CB  1 
ATOM   3229 O OG  . SER A 1 410 ? 29.085  11.024  -0.605  1.00 22.03  ? 439 SER A OG  1 
ATOM   3230 N N   . ARG A 1 411 ? 32.663  9.652   1.582   1.00 17.50  ? 440 ARG A N   1 
ATOM   3231 C CA  . ARG A 1 411 ? 33.542  9.209   2.655   1.00 18.89  ? 440 ARG A CA  1 
ATOM   3232 C C   . ARG A 1 411 ? 34.948  9.811   2.499   1.00 20.31  ? 440 ARG A C   1 
ATOM   3233 O O   . ARG A 1 411 ? 35.541  10.252  3.480   1.00 21.35  ? 440 ARG A O   1 
ATOM   3234 C CB  . ARG A 1 411 ? 33.556  7.684   2.707   1.00 20.40  ? 440 ARG A CB  1 
ATOM   3235 C CG  . ARG A 1 411 ? 32.249  7.032   3.145   1.00 20.35  ? 440 ARG A CG  1 
ATOM   3236 C CD  . ARG A 1 411 ? 31.699  7.377   4.545   1.00 20.84  ? 440 ARG A CD  1 
ATOM   3237 N NE  . ARG A 1 411 ? 31.121  8.727   4.687   1.00 19.04  ? 440 ARG A NE  1 
ATOM   3238 C CZ  . ARG A 1 411 ? 29.974  9.117   4.126   1.00 21.04  ? 440 ARG A CZ  1 
ATOM   3239 N NH1 . ARG A 1 411 ? 29.327  8.289   3.337   1.00 22.67  ? 440 ARG A NH1 1 
ATOM   3240 N NH2 . ARG A 1 411 ? 29.505  10.349  4.263   1.00 20.84  ? 440 ARG A NH2 1 
ATOM   3241 N N   . ALA A 1 412 ? 35.431  9.944   1.256   1.00 18.85  ? 441 ALA A N   1 
ATOM   3242 C CA  . ALA A 1 412 ? 36.721  10.561  1.010   1.00 19.21  ? 441 ALA A CA  1 
ATOM   3243 C C   . ALA A 1 412 ? 36.770  12.016  1.475   1.00 21.17  ? 441 ALA A C   1 
ATOM   3244 O O   . ALA A 1 412 ? 37.793  12.466  2.016   1.00 21.32  ? 441 ALA A O   1 
ATOM   3245 C CB  . ALA A 1 412 ? 37.041  10.502  -0.475  1.00 19.16  ? 441 ALA A CB  1 
ATOM   3246 N N   . LEU A 1 413 ? 35.670  12.747  1.231   1.00 21.16  ? 442 LEU A N   1 
ATOM   3247 C CA  . LEU A 1 413 ? 35.545  14.149  1.567   1.00 22.52  ? 442 LEU A CA  1 
ATOM   3248 C C   . LEU A 1 413 ? 35.019  14.365  2.975   1.00 22.25  ? 442 LEU A C   1 
ATOM   3249 O O   . LEU A 1 413 ? 34.882  15.513  3.427   1.00 24.27  ? 442 LEU A O   1 
ATOM   3250 C CB  . LEU A 1 413 ? 34.679  14.839  0.517   1.00 24.17  ? 442 LEU A CB  1 
ATOM   3251 C CG  . LEU A 1 413 ? 35.163  14.695  -0.939  1.00 26.21  ? 442 LEU A CG  1 
ATOM   3252 C CD1 . LEU A 1 413 ? 34.166  15.216  -1.951  1.00 26.58  ? 442 LEU A CD1 1 
ATOM   3253 C CD2 . LEU A 1 413 ? 36.537  15.325  -1.210  1.00 24.77  ? 442 LEU A CD2 1 
ATOM   3254 N N   . GLY A 1 414 ? 34.738  13.278  3.686   1.00 22.71  ? 443 GLY A N   1 
ATOM   3255 C CA  . GLY A 1 414 ? 34.376  13.403  5.094   1.00 24.75  ? 443 GLY A CA  1 
ATOM   3256 C C   . GLY A 1 414 ? 33.008  14.053  5.297   1.00 24.87  ? 443 GLY A C   1 
ATOM   3257 O O   . GLY A 1 414 ? 32.778  14.713  6.304   1.00 27.25  ? 443 GLY A O   1 
ATOM   3258 N N   . PHE A 1 415 ? 32.080  13.854  4.364   1.00 21.58  ? 444 PHE A N   1 
ATOM   3259 C CA  . PHE A 1 415 ? 30.707  14.334  4.513   1.00 19.55  ? 444 PHE A CA  1 
ATOM   3260 C C   . PHE A 1 415 ? 30.093  13.772  5.791   1.00 20.47  ? 444 PHE A C   1 
ATOM   3261 O O   . PHE A 1 415 ? 30.209  12.590  6.086   1.00 20.92  ? 444 PHE A O   1 
ATOM   3262 C CB  . PHE A 1 415 ? 29.870  13.980  3.288   1.00 19.97  ? 444 PHE A CB  1 
ATOM   3263 C CG  . PHE A 1 415 ? 30.109  14.724  1.977   1.00 21.03  ? 444 PHE A CG  1 
ATOM   3264 C CD1 . PHE A 1 415 ? 31.134  15.638  1.813   1.00 20.99  ? 444 PHE A CD1 1 
ATOM   3265 C CD2 . PHE A 1 415 ? 29.314  14.460  0.877   1.00 22.57  ? 444 PHE A CD2 1 
ATOM   3266 C CE1 . PHE A 1 415 ? 31.328  16.273  0.616   1.00 23.54  ? 444 PHE A CE1 1 
ATOM   3267 C CE2 . PHE A 1 415 ? 29.533  15.081  -0.340  1.00 21.85  ? 444 PHE A CE2 1 
ATOM   3268 C CZ  . PHE A 1 415 ? 30.511  16.022  -0.451  1.00 23.82  ? 444 PHE A CZ  1 
ATOM   3269 N N   . PRO A 1 416 ? 29.466  14.623  6.635   1.00 20.70  ? 445 PRO A N   1 
ATOM   3270 C CA  . PRO A 1 416 ? 28.929  14.173  7.906   1.00 19.76  ? 445 PRO A CA  1 
ATOM   3271 C C   . PRO A 1 416 ? 27.563  13.529  7.743   1.00 19.17  ? 445 PRO A C   1 
ATOM   3272 O O   . PRO A 1 416 ? 26.977  13.524  6.669   1.00 19.35  ? 445 PRO A O   1 
ATOM   3273 C CB  . PRO A 1 416 ? 28.886  15.490  8.749   1.00 19.88  ? 445 PRO A CB  1 
ATOM   3274 C CG  . PRO A 1 416 ? 28.519  16.520  7.724   1.00 20.79  ? 445 PRO A CG  1 
ATOM   3275 C CD  . PRO A 1 416 ? 29.270  16.083  6.428   1.00 21.85  ? 445 PRO A CD  1 
ATOM   3276 N N   . LEU A 1 417 ? 27.036  13.110  8.883   1.00 17.58  ? 446 LEU A N   1 
ATOM   3277 C CA  . LEU A 1 417 ? 25.682  12.599  8.980   1.00 18.18  ? 446 LEU A CA  1 
ATOM   3278 C C   . LEU A 1 417 ? 24.684  13.603  8.435   1.00 21.14  ? 446 LEU A C   1 
ATOM   3279 O O   . LEU A 1 417 ? 24.715  14.803  8.729   1.00 20.57  ? 446 LEU A O   1 
ATOM   3280 C CB  . LEU A 1 417 ? 25.486  12.292  10.457  1.00 20.43  ? 446 LEU A CB  1 
ATOM   3281 C CG  . LEU A 1 417 ? 24.171  11.647  10.889  1.00 24.33  ? 446 LEU A CG  1 
ATOM   3282 C CD1 . LEU A 1 417 ? 24.160  10.199  10.471  1.00 27.25  ? 446 LEU A CD1 1 
ATOM   3283 C CD2 . LEU A 1 417 ? 24.011  11.788  12.434  1.00 26.93  ? 446 LEU A CD2 1 
ATOM   3284 N N   . GLU A 1 418 ? 23.777  13.095  7.600   1.00 20.04  ? 447 GLU A N   1 
ATOM   3285 C CA  . GLU A 1 418 ? 22.684  13.911  7.110   1.00 21.77  ? 447 GLU A CA  1 
ATOM   3286 C C   . GLU A 1 418 ? 21.628  13.982  8.217   1.00 22.98  ? 447 GLU A C   1 
ATOM   3287 O O   . GLU A 1 418 ? 21.071  12.965  8.598   1.00 21.11  ? 447 GLU A O   1 
ATOM   3288 C CB  . GLU A 1 418 ? 22.164  13.338  5.787   1.00 20.36  ? 447 GLU A CB  1 
ATOM   3289 C CG  . GLU A 1 418 ? 21.017  14.162  5.250   1.00 20.52  ? 447 GLU A CG  1 
ATOM   3290 C CD  . GLU A 1 418 ? 20.552  13.840  3.851   1.00 25.65  ? 447 GLU A CD  1 
ATOM   3291 O OE1 . GLU A 1 418 ? 19.294  13.817  3.637   1.00 24.55  ? 447 GLU A OE1 1 
ATOM   3292 O OE2 . GLU A 1 418 ? 21.423  13.684  2.974   1.00 23.67  ? 447 GLU A OE2 1 
ATOM   3293 N N   . ARG A 1 419 ? 21.337  15.191  8.696   1.00 22.80  ? 448 ARG A N   1 
ATOM   3294 C CA  . ARG A 1 419 ? 20.422  15.371  9.813   1.00 27.94  ? 448 ARG A CA  1 
ATOM   3295 C C   . ARG A 1 419 ? 19.767  16.756  9.690   1.00 30.36  ? 448 ARG A C   1 
ATOM   3296 O O   . ARG A 1 419 ? 20.105  17.710  10.402  1.00 25.13  ? 448 ARG A O   1 
ATOM   3297 C CB  . ARG A 1 419 ? 21.229  15.247  11.117  1.00 39.60  ? 448 ARG A CB  1 
ATOM   3298 C CG  . ARG A 1 419 ? 20.502  14.508  12.238  1.00 52.60  ? 448 ARG A CG  1 
ATOM   3299 C CD  . ARG A 1 419 ? 19.550  15.359  13.086  1.00 62.90  ? 448 ARG A CD  1 
ATOM   3300 N NE  . ARG A 1 419 ? 18.765  14.583  14.066  1.00 64.70  ? 448 ARG A NE  1 
ATOM   3301 C CZ  . ARG A 1 419 ? 17.501  14.847  14.427  1.00 70.86  ? 448 ARG A CZ  1 
ATOM   3302 N NH1 . ARG A 1 419 ? 16.860  14.097  15.323  1.00 62.29  ? 448 ARG A NH1 1 
ATOM   3303 N NH2 . ARG A 1 419 ? 16.878  15.886  13.885  1.00 76.34  ? 448 ARG A NH2 1 
ATOM   3304 N N   . PRO A 1 420 ? 18.789  16.921  8.779   1.00 25.30  ? 449 PRO A N   1 
ATOM   3305 C CA  . PRO A 1 420 ? 17.973  18.127  8.763   1.00 25.15  ? 449 PRO A CA  1 
ATOM   3306 C C   . PRO A 1 420 ? 17.157  18.192  10.047  1.00 26.20  ? 449 PRO A C   1 
ATOM   3307 O O   . PRO A 1 420 ? 17.037  17.198  10.776  1.00 22.10  ? 449 PRO A O   1 
ATOM   3308 C CB  . PRO A 1 420 ? 17.094  17.938  7.505   1.00 22.83  ? 449 PRO A CB  1 
ATOM   3309 C CG  . PRO A 1 420 ? 16.944  16.422  7.429   1.00 23.45  ? 449 PRO A CG  1 
ATOM   3310 C CD  . PRO A 1 420 ? 18.336  15.930  7.802   1.00 24.54  ? 449 PRO A CD  1 
ATOM   3311 N N   . LYS A 1 421 ? 16.603  19.375  10.302  1.00 24.25  ? 450 LYS A N   1 
ATOM   3312 C CA  . LYS A 1 421 ? 15.661  19.574  11.397  1.00 27.20  ? 450 LYS A CA  1 
ATOM   3313 C C   . LYS A 1 421 ? 14.242  19.351  10.883  1.00 22.61  ? 450 LYS A C   1 
ATOM   3314 O O   . LYS A 1 421 ? 13.887  19.814  9.797   1.00 23.69  ? 450 LYS A O   1 
ATOM   3315 C CB  . LYS A 1 421 ? 15.868  20.993  11.963  1.00 28.08  ? 450 LYS A CB  1 
ATOM   3316 C CG  . LYS A 1 421 ? 14.947  21.360  13.105  1.00 28.02  ? 450 LYS A CG  1 
ATOM   3317 C CD  . LYS A 1 421 ? 15.228  20.544  14.353  1.00 32.06  ? 450 LYS A CD  1 
ATOM   3318 C CE  . LYS A 1 421 ? 14.435  21.042  15.531  1.00 32.29  ? 450 LYS A CE  1 
ATOM   3319 N NZ  . LYS A 1 421 ? 14.697  20.068  16.588  1.00 33.24  ? 450 LYS A NZ  1 
ATOM   3320 N N   . SER A 1 422 ? 13.444  18.578  11.639  1.00 19.34  ? 451 SER A N   1 
ATOM   3321 C CA  . SER A 1 422 ? 12.038  18.427  11.358  1.00 21.07  ? 451 SER A CA  1 
ATOM   3322 C C   . SER A 1 422 ? 11.273  19.404  12.228  1.00 20.03  ? 451 SER A C   1 
ATOM   3323 O O   . SER A 1 422 ? 11.773  19.811  13.264  1.00 20.07  ? 451 SER A O   1 
ATOM   3324 C CB  . SER A 1 422 ? 11.532  17.007  11.526  1.00 21.88  ? 451 SER A CB  1 
ATOM   3325 O OG  . SER A 1 422 ? 11.424  16.569  12.873  1.00 18.77  ? 451 SER A OG  1 
ATOM   3326 N N   . MET A 1 423 ? 10.047  19.683  11.809  1.00 22.91  ? 452 MET A N   1 
ATOM   3327 C CA  . MET A 1 423 ? 9.095   20.401  12.621  1.00 25.19  ? 452 MET A CA  1 
ATOM   3328 C C   . MET A 1 423 ? 7.734   19.797  12.420  1.00 22.64  ? 452 MET A C   1 
ATOM   3329 O O   . MET A 1 423 ? 7.443   19.283  11.336  1.00 23.02  ? 452 MET A O   1 
ATOM   3330 C CB  . MET A 1 423 ? 8.948   21.847  12.148  1.00 28.48  ? 452 MET A CB  1 
ATOM   3331 C CG  . MET A 1 423 ? 10.218  22.592  12.041  1.00 29.80  ? 452 MET A CG  1 
ATOM   3332 S SD  . MET A 1 423 ? 10.802  23.032  13.668  1.00 37.31  ? 452 MET A SD  1 
ATOM   3333 C CE  . MET A 1 423 ? 9.778   24.492  14.007  1.00 37.00  ? 452 MET A CE  1 
ATOM   3334 N N   . SER A 1 424 ? 6.922   19.870  13.468  1.00 24.12  ? 453 SER A N   1 
ATOM   3335 C CA  . SER A 1 424 ? 5.508   19.572  13.372  1.00 26.30  ? 453 SER A CA  1 
ATOM   3336 C C   . SER A 1 424 ? 4.776   20.774  12.794  1.00 26.93  ? 453 SER A C   1 
ATOM   3337 O O   . SER A 1 424 ? 5.295   21.888  12.850  1.00 23.17  ? 453 SER A O   1 
ATOM   3338 C CB  . SER A 1 424 ? 4.916   19.249  14.724  1.00 27.58  ? 453 SER A CB  1 
ATOM   3339 O OG  . SER A 1 424 ? 4.904   20.404  15.560  1.00 25.61  ? 453 SER A OG  1 
ATOM   3340 N N   . THR A 1 425 ? 3.534   20.527  12.359  1.00 26.28  ? 454 THR A N   1 
ATOM   3341 C CA  . THR A 1 425 ? 2.665   21.578  11.875  1.00 29.97  ? 454 THR A CA  1 
ATOM   3342 C C   . THR A 1 425 ? 2.496   22.620  12.985  1.00 30.84  ? 454 THR A C   1 
ATOM   3343 O O   . THR A 1 425 ? 2.694   23.817  12.748  1.00 31.75  ? 454 THR A O   1 
ATOM   3344 C CB  . THR A 1 425 ? 1.341   20.985  11.400  1.00 28.91  ? 454 THR A CB  1 
ATOM   3345 O OG1 . THR A 1 425 ? 1.580   20.242  10.202  1.00 26.06  ? 454 THR A OG1 1 
ATOM   3346 C CG2 . THR A 1 425 ? 0.294   22.036  11.058  1.00 28.86  ? 454 THR A CG2 1 
ATOM   3347 N N   . GLU A 1 426 ? 2.176   22.141  14.196  1.00 30.78  ? 455 GLU A N   1 
ATOM   3348 C CA  . GLU A 1 426 ? 2.012   22.987  15.370  1.00 36.52  ? 455 GLU A CA  1 
ATOM   3349 C C   . GLU A 1 426 ? 3.268   23.805  15.651  1.00 32.39  ? 455 GLU A C   1 
ATOM   3350 O O   . GLU A 1 426 ? 3.176   24.995  15.962  1.00 31.16  ? 455 GLU A O   1 
ATOM   3351 C CB  . GLU A 1 426 ? 1.638   22.096  16.556  1.00 41.95  ? 455 GLU A CB  1 
ATOM   3352 C CG  . GLU A 1 426 ? 1.695   22.775  17.919  1.00 57.31  ? 455 GLU A CG  1 
ATOM   3353 C CD  . GLU A 1 426 ? 1.715   21.822  19.122  1.00 76.65  ? 455 GLU A CD  1 
ATOM   3354 O OE1 . GLU A 1 426 ? 1.912   22.374  20.236  1.00 83.67  ? 455 GLU A OE1 1 
ATOM   3355 O OE2 . GLU A 1 426 ? 1.554   20.566  18.989  1.00 65.22  ? 455 GLU A OE2 1 
ATOM   3356 N N   . GLY A 1 427 ? 4.436   23.158  15.624  1.00 29.60  ? 456 GLY A N   1 
ATOM   3357 C CA  . GLY A 1 427 ? 5.704   23.809  15.907  1.00 25.66  ? 456 GLY A CA  1 
ATOM   3358 C C   . GLY A 1 427 ? 6.022   24.828  14.814  1.00 28.46  ? 456 GLY A C   1 
ATOM   3359 O O   . GLY A 1 427 ? 6.575   25.894  15.074  1.00 28.52  ? 456 GLY A O   1 
ATOM   3360 N N   . LEU A 1 428 ? 5.661   24.499  13.568  1.00 27.09  ? 457 LEU A N   1 
ATOM   3361 C CA  . LEU A 1 428 ? 5.996   25.382  12.458  1.00 28.64  ? 457 LEU A CA  1 
ATOM   3362 C C   . LEU A 1 428 ? 5.117   26.615  12.588  1.00 27.78  ? 457 LEU A C   1 
ATOM   3363 O O   . LEU A 1 428 ? 5.581   27.707  12.345  1.00 30.29  ? 457 LEU A O   1 
ATOM   3364 C CB  . LEU A 1 428 ? 5.727   24.750  11.097  1.00 26.84  ? 457 LEU A CB  1 
ATOM   3365 C CG  . LEU A 1 428 ? 6.835   24.813  10.048  1.00 28.40  ? 457 LEU A CG  1 
ATOM   3366 C CD1 . LEU A 1 428 ? 6.112   24.615  8.770   1.00 29.68  ? 457 LEU A CD1 1 
ATOM   3367 C CD2 . LEU A 1 428 ? 7.853   25.935  10.001  1.00 26.39  ? 457 LEU A CD2 1 
ATOM   3368 N N   . MET A 1 429 ? 3.834   26.379  12.868  1.00 30.41  ? 458 MET A N   1 
ATOM   3369 C CA  . MET A 1 429 ? 2.885   27.467  13.080  1.00 32.31  ? 458 MET A CA  1 
ATOM   3370 C C   . MET A 1 429 ? 3.433   28.450  14.128  1.00 34.72  ? 458 MET A C   1 
ATOM   3371 O O   . MET A 1 429 ? 3.428   29.672  13.911  1.00 27.31  ? 458 MET A O   1 
ATOM   3372 C CB  . MET A 1 429 ? 1.533   26.897  13.509  1.00 30.31  ? 458 MET A CB  1 
ATOM   3373 C CG  . MET A 1 429 ? 0.718   26.318  12.386  1.00 33.38  ? 458 MET A CG  1 
ATOM   3374 S SD  . MET A 1 429 ? -0.831  25.655  13.035  1.00 41.83  ? 458 MET A SD  1 
ATOM   3375 C CE  . MET A 1 429 ? -1.525  25.019  11.515  1.00 41.65  ? 458 MET A CE  1 
ATOM   3376 N N   . LYS A 1 430 ? 3.937   27.910  15.250  1.00 31.99  ? 459 LYS A N   1 
ATOM   3377 C CA  . LYS A 1 430 ? 4.463   28.735  16.318  1.00 35.22  ? 459 LYS A CA  1 
ATOM   3378 C C   . LYS A 1 430 ? 5.751   29.401  15.892  1.00 35.87  ? 459 LYS A C   1 
ATOM   3379 O O   . LYS A 1 430 ? 5.984   30.552  16.220  1.00 32.80  ? 459 LYS A O   1 
ATOM   3380 C CB  . LYS A 1 430 ? 4.697   27.944  17.612  1.00 43.77  ? 459 LYS A CB  1 
ATOM   3381 C CG  . LYS A 1 430 ? 3.381   27.470  18.209  1.00 50.40  ? 459 LYS A CG  1 
ATOM   3382 C CD  . LYS A 1 430 ? 3.295   27.559  19.729  1.00 62.86  ? 459 LYS A CD  1 
ATOM   3383 C CE  . LYS A 1 430 ? 4.145   26.562  20.438  1.00 72.39  ? 459 LYS A CE  1 
ATOM   3384 N NZ  . LYS A 1 430 ? 3.632   25.196  20.267  1.00 77.22  ? 459 LYS A NZ  1 
ATOM   3385 N N   . PHE A 1 431 ? 6.596   28.676  15.157  1.00 30.60  ? 460 PHE A N   1 
ATOM   3386 C CA  . PHE A 1 431 ? 7.831   29.258  14.698  1.00 32.58  ? 460 PHE A CA  1 
ATOM   3387 C C   . PHE A 1 431 ? 7.543   30.449  13.794  1.00 32.60  ? 460 PHE A C   1 
ATOM   3388 O O   . PHE A 1 431 ? 8.212   31.486  13.913  1.00 33.02  ? 460 PHE A O   1 
ATOM   3389 C CB  . PHE A 1 431 ? 8.667   28.209  13.958  1.00 33.50  ? 460 PHE A CB  1 
ATOM   3390 C CG  . PHE A 1 431 ? 9.999   28.759  13.487  1.00 32.91  ? 460 PHE A CG  1 
ATOM   3391 C CD1 . PHE A 1 431 ? 11.042  28.969  14.393  1.00 33.22  ? 460 PHE A CD1 1 
ATOM   3392 C CD2 . PHE A 1 431 ? 10.195  29.097  12.157  1.00 33.27  ? 460 PHE A CD2 1 
ATOM   3393 C CE1 . PHE A 1 431 ? 12.246  29.515  13.973  1.00 31.72  ? 460 PHE A CE1 1 
ATOM   3394 C CE2 . PHE A 1 431 ? 11.399  29.644  11.747  1.00 35.87  ? 460 PHE A CE2 1 
ATOM   3395 C CZ  . PHE A 1 431 ? 12.423  29.849  12.661  1.00 35.42  ? 460 PHE A CZ  1 
ATOM   3396 N N   . VAL A 1 432 ? 6.625   30.283  12.840  1.00 31.70  ? 461 VAL A N   1 
ATOM   3397 C CA  . VAL A 1 432 ? 6.354   31.378  11.915  1.00 37.40  ? 461 VAL A CA  1 
ATOM   3398 C C   . VAL A 1 432 ? 5.710   32.566  12.659  1.00 37.39  ? 461 VAL A C   1 
ATOM   3399 O O   . VAL A 1 432 ? 6.120   33.715  12.451  1.00 32.64  ? 461 VAL A O   1 
ATOM   3400 C CB  . VAL A 1 432 ? 5.520   30.984  10.684  1.00 41.38  ? 461 VAL A CB  1 
ATOM   3401 C CG1 . VAL A 1 432 ? 6.193   29.893  9.868   1.00 41.58  ? 461 VAL A CG1 1 
ATOM   3402 C CG2 . VAL A 1 432 ? 4.106   30.580  11.035  1.00 50.27  ? 461 VAL A CG2 1 
ATOM   3403 N N   . ASP A 1 433 ? 4.771   32.293  13.578  1.00 36.47  ? 462 ASP A N   1 
ATOM   3404 C CA  . ASP A 1 433 ? 4.114   33.356  14.331  1.00 48.85  ? 462 ASP A CA  1 
ATOM   3405 C C   . ASP A 1 433 ? 5.100   34.146  15.208  1.00 56.16  ? 462 ASP A C   1 
ATOM   3406 O O   . ASP A 1 433 ? 4.763   35.249  15.617  1.00 60.40  ? 462 ASP A O   1 
ATOM   3407 C CB  . ASP A 1 433 ? 2.913   32.866  15.132  1.00 44.86  ? 462 ASP A CB  1 
ATOM   3408 C CG  . ASP A 1 433 ? 1.698   32.429  14.313  1.00 52.67  ? 462 ASP A CG  1 
ATOM   3409 O OD1 . ASP A 1 433 ? 1.713   32.636  13.071  1.00 55.99  ? 462 ASP A OD1 1 
ATOM   3410 O OD2 . ASP A 1 433 ? 0.736   31.873  14.910  1.00 55.19  ? 462 ASP A OD2 1 
ATOM   3411 N N   . SER A 1 434 ? 6.323   33.648  15.457  1.00 52.13  ? 463 SER A N   1 
ATOM   3412 C CA  . SER A 1 434 ? 7.232   34.303  16.392  1.00 52.64  ? 463 SER A CA  1 
ATOM   3413 C C   . SER A 1 434 ? 8.268   35.174  15.655  1.00 42.98  ? 463 SER A C   1 
ATOM   3414 O O   . SER A 1 434 ? 8.351   35.041  14.401  1.00 45.83  ? 463 SER A O   1 
ATOM   3415 C CB  . SER A 1 434 ? 7.910   33.284  17.282  1.00 54.70  ? 463 SER A CB  1 
ATOM   3416 O OG  . SER A 1 434 ? 8.976   32.637  16.596  1.00 51.90  ? 463 SER A OG  1 
ATOM   3417 N N   . SER B 1 1   ? -14.863 3.792   18.833  1.00 57.66  ? 30  SER B N   1 
ATOM   3418 C CA  . SER B 1 1   ? -14.734 3.777   20.327  1.00 64.74  ? 30  SER B CA  1 
ATOM   3419 C C   . SER B 1 1   ? -13.422 3.110   20.777  1.00 67.18  ? 30  SER B C   1 
ATOM   3420 O O   . SER B 1 1   ? -12.606 3.648   21.558  1.00 47.91  ? 30  SER B O   1 
ATOM   3421 C CB  . SER B 1 1   ? -15.935 3.071   20.934  1.00 67.82  ? 30  SER B CB  1 
ATOM   3422 O OG  . SER B 1 1   ? -15.886 3.082   22.354  1.00 69.24  ? 30  SER B OG  1 
ATOM   3423 N N   . THR B 1 2   ? -13.256 1.871   20.316  1.00 61.80  ? 31  THR B N   1 
ATOM   3424 C CA  . THR B 1 2   ? -12.020 1.148   20.536  1.00 66.10  ? 31  THR B CA  1 
ATOM   3425 C C   . THR B 1 2   ? -11.291 1.019   19.202  1.00 57.06  ? 31  THR B C   1 
ATOM   3426 O O   . THR B 1 2   ? -10.060 0.920   19.238  1.00 50.82  ? 31  THR B O   1 
ATOM   3427 C CB  . THR B 1 2   ? -12.256 -0.201  21.221  1.00 64.26  ? 31  THR B CB  1 
ATOM   3428 O OG1 . THR B 1 2   ? -13.494 -0.733  20.747  1.00 70.20  ? 31  THR B OG1 1 
ATOM   3429 C CG2 . THR B 1 2   ? -12.303 -0.074  22.737  1.00 63.76  ? 31  THR B CG2 1 
ATOM   3430 N N   . ASN B 1 3   ? -12.018 1.056   18.061  1.00 42.91  ? 32  ASN B N   1 
ATOM   3431 C CA  . ASN B 1 3   ? -11.357 0.775   16.785  1.00 41.59  ? 32  ASN B CA  1 
ATOM   3432 C C   . ASN B 1 3   ? -10.571 2.016   16.353  1.00 29.35  ? 32  ASN B C   1 
ATOM   3433 O O   . ASN B 1 3   ? -11.125 2.980   15.819  1.00 24.69  ? 32  ASN B O   1 
ATOM   3434 C CB  . ASN B 1 3   ? -12.250 0.216   15.682  1.00 39.75  ? 32  ASN B CB  1 
ATOM   3435 C CG  . ASN B 1 3   ? -11.448 -0.542  14.626  1.00 46.05  ? 32  ASN B CG  1 
ATOM   3436 O OD1 . ASN B 1 3   ? -10.308 -0.199  14.269  1.00 39.14  ? 32  ASN B OD1 1 
ATOM   3437 N ND2 . ASN B 1 3   ? -11.992 -1.635  14.126  1.00 48.53  ? 32  ASN B ND2 1 
ATOM   3438 N N   . LEU B 1 4   ? -9.245  1.936   16.556  1.00 27.13  ? 33  LEU B N   1 
ATOM   3439 C CA  . LEU B 1 4   ? -8.332  3.028   16.236  1.00 24.37  ? 33  LEU B CA  1 
ATOM   3440 C C   . LEU B 1 4   ? -8.502  3.464   14.783  1.00 22.55  ? 33  LEU B C   1 
ATOM   3441 O O   . LEU B 1 4   ? -8.351  4.636   14.469  1.00 27.52  ? 33  LEU B O   1 
ATOM   3442 C CB  . LEU B 1 4   ? -6.917  2.516   16.507  1.00 23.35  ? 33  LEU B CB  1 
ATOM   3443 C CG  . LEU B 1 4   ? -5.767  3.456   16.184  1.00 23.67  ? 33  LEU B CG  1 
ATOM   3444 C CD1 . LEU B 1 4   ? -5.808  4.780   16.867  1.00 23.50  ? 33  LEU B CD1 1 
ATOM   3445 C CD2 . LEU B 1 4   ? -4.451  2.722   16.563  1.00 25.06  ? 33  LEU B CD2 1 
ATOM   3446 N N   . LYS B 1 5   ? -8.769  2.527   13.888  1.00 22.07  ? 34  LYS B N   1 
ATOM   3447 C CA  . LYS B 1 5   ? -8.895  2.876   12.490  1.00 23.57  ? 34  LYS B CA  1 
ATOM   3448 C C   . LYS B 1 5   ? -10.032 3.872   12.257  1.00 24.58  ? 34  LYS B C   1 
ATOM   3449 O O   . LYS B 1 5   ? -9.940  4.739   11.386  1.00 20.62  ? 34  LYS B O   1 
ATOM   3450 C CB  . LYS B 1 5   ? -9.053  1.656   11.587  1.00 24.40  ? 34  LYS B CB  1 
ATOM   3451 C CG  . LYS B 1 5   ? -8.921  1.980   10.107  1.00 25.23  ? 34  LYS B CG  1 
ATOM   3452 C CD  . LYS B 1 5   ? -8.815  0.711   9.271   1.00 30.28  ? 34  LYS B CD  1 
ATOM   3453 C CE  . LYS B 1 5   ? -8.489  1.003   7.873   1.00 29.31  ? 34  LYS B CE  1 
ATOM   3454 N NZ  . LYS B 1 5   ? -8.759  -0.198  7.102   1.00 30.20  ? 34  LYS B NZ  1 
ATOM   3455 N N   . ASP B 1 6   ? -11.153 3.718   12.964  1.00 25.68  ? 35  ASP B N   1 
ATOM   3456 C CA  . ASP B 1 6   ? -12.267 4.630   12.762  1.00 25.11  ? 35  ASP B CA  1 
ATOM   3457 C C   . ASP B 1 6   ? -12.014 5.951   13.471  1.00 19.73  ? 35  ASP B C   1 
ATOM   3458 O O   . ASP B 1 6   ? -12.454 6.985   13.009  1.00 21.21  ? 35  ASP B O   1 
ATOM   3459 C CB  . ASP B 1 6   ? -13.560 3.980   13.205  1.00 28.59  ? 35  ASP B CB  1 
ATOM   3460 C CG  . ASP B 1 6   ? -13.927 2.797   12.322  1.00 36.68  ? 35  ASP B CG  1 
ATOM   3461 O OD1 . ASP B 1 6   ? -14.076 3.026   11.098  1.00 42.60  ? 35  ASP B OD1 1 
ATOM   3462 O OD2 . ASP B 1 6   ? -13.989 1.672   12.852  1.00 37.81  ? 35  ASP B OD2 1 
ATOM   3463 N N   . ILE B 1 7   ? -11.333 5.898   14.617  1.00 21.69  ? 36  ILE B N   1 
ATOM   3464 C CA  . ILE B 1 7   ? -10.987 7.102   15.337  1.00 25.88  ? 36  ILE B CA  1 
ATOM   3465 C C   . ILE B 1 7   ? -10.033 7.922   14.461  1.00 25.98  ? 36  ILE B C   1 
ATOM   3466 O O   . ILE B 1 7   ? -10.153 9.144   14.361  1.00 24.00  ? 36  ILE B O   1 
ATOM   3467 C CB  . ILE B 1 7   ? -10.393 6.745   16.709  1.00 29.13  ? 36  ILE B CB  1 
ATOM   3468 C CG1 . ILE B 1 7   ? -11.493 6.242   17.614  1.00 29.43  ? 36  ILE B CG1 1 
ATOM   3469 C CG2 . ILE B 1 7   ? -9.648  7.922   17.339  1.00 32.06  ? 36  ILE B CG2 1 
ATOM   3470 C CD1 . ILE B 1 7   ? -11.024 5.418   18.804  1.00 30.99  ? 36  ILE B CD1 1 
ATOM   3471 N N   . LEU B 1 8   ? -9.089  7.232   13.808  1.00 26.27  ? 37  LEU B N   1 
ATOM   3472 C CA  . LEU B 1 8   ? -8.163  7.900   12.912  1.00 25.21  ? 37  LEU B CA  1 
ATOM   3473 C C   . LEU B 1 8   ? -8.916  8.465   11.711  1.00 23.86  ? 37  LEU B C   1 
ATOM   3474 O O   . LEU B 1 8   ? -8.705  9.634   11.353  1.00 25.81  ? 37  LEU B O   1 
ATOM   3475 C CB  . LEU B 1 8   ? -7.056  6.913   12.566  1.00 27.85  ? 37  LEU B CB  1 
ATOM   3476 C CG  . LEU B 1 8   ? -5.906  7.447   11.722  1.00 32.76  ? 37  LEU B CG  1 
ATOM   3477 C CD1 . LEU B 1 8   ? -5.266  8.715   12.296  1.00 34.33  ? 37  LEU B CD1 1 
ATOM   3478 C CD2 . LEU B 1 8   ? -4.900  6.324   11.563  1.00 34.02  ? 37  LEU B CD2 1 
ATOM   3479 N N   . ALA B 1 9   ? -9.867  7.707   11.130  1.00 22.53  ? 38  ALA B N   1 
ATOM   3480 C CA  . ALA B 1 9   ? -10.661 8.229   10.024  1.00 24.50  ? 38  ALA B CA  1 
ATOM   3481 C C   . ALA B 1 9   ? -11.341 9.552   10.376  1.00 24.73  ? 38  ALA B C   1 
ATOM   3482 O O   . ALA B 1 9   ? -11.462 10.425  9.524   1.00 25.48  ? 38  ALA B O   1 
ATOM   3483 C CB  . ALA B 1 9   ? -11.647 7.220   9.514   1.00 26.29  ? 38  ALA B CB  1 
ATOM   3484 N N   . ASP B 1 10  ? -11.754 9.736   11.631  1.00 26.38  ? 39  ASP B N   1 
ATOM   3485 C CA  . ASP B 1 10  ? -12.470 10.944  12.030  1.00 29.19  ? 39  ASP B CA  1 
ATOM   3486 C C   . ASP B 1 10  ? -11.505 12.103  12.272  1.00 28.78  ? 39  ASP B C   1 
ATOM   3487 O O   . ASP B 1 10  ? -11.897 13.240  12.068  1.00 29.38  ? 39  ASP B O   1 
ATOM   3488 C CB  . ASP B 1 10  ? -13.433 10.702  13.184  1.00 31.13  ? 39  ASP B CB  1 
ATOM   3489 C CG  . ASP B 1 10  ? -14.630 9.792   12.894  1.00 36.91  ? 39  ASP B CG  1 
ATOM   3490 O OD1 . ASP B 1 10  ? -14.985 9.569   11.713  1.00 37.78  ? 39  ASP B OD1 1 
ATOM   3491 O OD2 . ASP B 1 10  ? -15.199 9.284   13.856  1.00 39.56  ? 39  ASP B OD2 1 
ATOM   3492 N N   . LEU B 1 11  ? -10.246 11.817  12.660  1.00 24.70  ? 40  LEU B N   1 
ATOM   3493 C CA  . LEU B 1 11  ? -9.222  12.819  12.926  1.00 25.03  ? 40  LEU B CA  1 
ATOM   3494 C C   . LEU B 1 11  ? -8.591  13.366  11.635  1.00 25.56  ? 40  LEU B C   1 
ATOM   3495 O O   . LEU B 1 11  ? -8.178  14.509  11.581  1.00 24.43  ? 40  LEU B O   1 
ATOM   3496 C CB  . LEU B 1 11  ? -8.151  12.183  13.790  1.00 27.47  ? 40  LEU B CB  1 
ATOM   3497 C CG  . LEU B 1 11  ? -8.478  11.949  15.264  1.00 33.31  ? 40  LEU B CG  1 
ATOM   3498 C CD1 . LEU B 1 11  ? -7.248  11.293  15.919  1.00 35.74  ? 40  LEU B CD1 1 
ATOM   3499 C CD2 . LEU B 1 11  ? -8.830  13.206  16.038  1.00 36.28  ? 40  LEU B CD2 1 
ATOM   3500 N N   . ILE B 1 12  ? -8.555  12.586  10.555  1.00 25.84  ? 41  ILE B N   1 
ATOM   3501 C CA  . ILE B 1 12  ? -7.749  12.964  9.409   1.00 26.32  ? 41  ILE B CA  1 
ATOM   3502 C C   . ILE B 1 12  ? -8.281  14.224  8.726   1.00 30.57  ? 41  ILE B C   1 
ATOM   3503 O O   . ILE B 1 12  ? -7.489  15.152  8.521   1.00 27.36  ? 41  ILE B O   1 
ATOM   3504 C CB  . ILE B 1 12  ? -7.576  11.782  8.470   1.00 23.36  ? 41  ILE B CB  1 
ATOM   3505 C CG1 . ILE B 1 12  ? -6.523  10.818  9.055   1.00 23.02  ? 41  ILE B CG1 1 
ATOM   3506 C CG2 . ILE B 1 12  ? -7.224  12.254  7.064   1.00 25.76  ? 41  ILE B CG2 1 
ATOM   3507 C CD1 . ILE B 1 12  ? -6.535  9.437   8.454   1.00 23.19  ? 41  ILE B CD1 1 
ATOM   3508 N N   . PRO B 1 13  ? -9.602  14.354  8.414   1.00 28.80  ? 42  PRO B N   1 
ATOM   3509 C CA  . PRO B 1 13  ? -10.110 15.581  7.761   1.00 30.58  ? 42  PRO B CA  1 
ATOM   3510 C C   . PRO B 1 13  ? -9.814  16.878  8.528   1.00 27.13  ? 42  PRO B C   1 
ATOM   3511 O O   . PRO B 1 13  ? -9.475  17.914  7.942   1.00 25.77  ? 42  PRO B O   1 
ATOM   3512 C CB  . PRO B 1 13  ? -11.641 15.301  7.619   1.00 31.82  ? 42  PRO B CB  1 
ATOM   3513 C CG  . PRO B 1 13  ? -11.735 13.766  7.621   1.00 31.52  ? 42  PRO B CG  1 
ATOM   3514 C CD  . PRO B 1 13  ? -10.642 13.330  8.597   1.00 29.40  ? 42  PRO B CD  1 
ATOM   3515 N N   . LYS B 1 14  ? -9.827  16.802  9.854   1.00 27.25  ? 43  LYS B N   1 
ATOM   3516 C CA  . LYS B 1 14  ? -9.557  17.977  10.669  1.00 31.80  ? 43  LYS B CA  1 
ATOM   3517 C C   . LYS B 1 14  ? -8.101  18.429  10.495  1.00 33.02  ? 43  LYS B C   1 
ATOM   3518 O O   . LYS B 1 14  ? -7.809  19.621  10.474  1.00 27.47  ? 43  LYS B O   1 
ATOM   3519 C CB  . LYS B 1 14  ? -9.766  17.661  12.155  1.00 37.60  ? 43  LYS B CB  1 
ATOM   3520 C CG  . LYS B 1 14  ? -11.191 17.286  12.587  1.00 48.51  ? 43  LYS B CG  1 
ATOM   3521 C CD  . LYS B 1 14  ? -11.250 16.948  14.077  1.00 56.90  ? 43  LYS B CD  1 
ATOM   3522 C CE  . LYS B 1 14  ? -12.596 16.984  14.734  1.00 63.08  ? 43  LYS B CE  1 
ATOM   3523 N NZ  . LYS B 1 14  ? -13.389 15.800  14.410  1.00 65.97  ? 43  LYS B NZ  1 
ATOM   3524 N N   . GLU B 1 15  ? -7.176  17.464  10.398  1.00 28.44  ? 44  GLU B N   1 
ATOM   3525 C CA  . GLU B 1 15  ? -5.764  17.777  10.310  1.00 26.32  ? 44  GLU B CA  1 
ATOM   3526 C C   . GLU B 1 15  ? -5.409  18.241  8.894   1.00 27.45  ? 44  GLU B C   1 
ATOM   3527 O O   . GLU B 1 15  ? -4.550  19.092  8.727   1.00 30.03  ? 44  GLU B O   1 
ATOM   3528 C CB  . GLU B 1 15  ? -4.984  16.538  10.719  1.00 29.64  ? 44  GLU B CB  1 
ATOM   3529 C CG  . GLU B 1 15  ? -3.577  16.832  11.196  1.00 39.56  ? 44  GLU B CG  1 
ATOM   3530 C CD  . GLU B 1 15  ? -3.577  17.829  12.331  1.00 39.92  ? 44  GLU B CD  1 
ATOM   3531 O OE1 . GLU B 1 15  ? -4.346  17.665  13.293  1.00 42.40  ? 44  GLU B OE1 1 
ATOM   3532 O OE2 . GLU B 1 15  ? -2.803  18.779  12.182  1.00 48.38  ? 44  GLU B OE2 1 
ATOM   3533 N N   . GLN B 1 16  ? -6.061  17.668  7.889   1.00 22.78  ? 45  GLN B N   1 
ATOM   3534 C CA  . GLN B 1 16  ? -5.916  18.108  6.521   1.00 26.85  ? 45  GLN B CA  1 
ATOM   3535 C C   . GLN B 1 16  ? -6.314  19.575  6.396   1.00 29.26  ? 45  GLN B C   1 
ATOM   3536 O O   . GLN B 1 16  ? -5.600  20.347  5.790   1.00 27.04  ? 45  GLN B O   1 
ATOM   3537 C CB  . GLN B 1 16  ? -6.786  17.284  5.600   1.00 26.79  ? 45  GLN B CB  1 
ATOM   3538 C CG  . GLN B 1 16  ? -6.307  15.849  5.446   1.00 27.54  ? 45  GLN B CG  1 
ATOM   3539 C CD  . GLN B 1 16  ? -7.246  14.953  4.666   1.00 29.09  ? 45  GLN B CD  1 
ATOM   3540 O OE1 . GLN B 1 16  ? -8.454  15.158  4.602   1.00 30.87  ? 45  GLN B OE1 1 
ATOM   3541 N NE2 . GLN B 1 16  ? -6.711  13.923  4.049   1.00 28.21  ? 45  GLN B NE2 1 
ATOM   3542 N N   . ALA B 1 17  ? -7.480  19.920  6.931   1.00 31.96  ? 46  ALA B N   1 
ATOM   3543 C CA  . ALA B 1 17  ? -7.994  21.275  6.857   1.00 29.66  ? 46  ALA B CA  1 
ATOM   3544 C C   . ALA B 1 17  ? -7.032  22.239  7.544   1.00 29.13  ? 46  ALA B C   1 
ATOM   3545 O O   . ALA B 1 17  ? -6.775  23.325  7.020   1.00 30.01  ? 46  ALA B O   1 
ATOM   3546 C CB  . ALA B 1 17  ? -9.369  21.330  7.471   1.00 26.94  ? 46  ALA B CB  1 
ATOM   3547 N N   . ARG B 1 18  ? -6.520  21.847  8.714   1.00 28.59  ? 47  ARG B N   1 
ATOM   3548 C CA  . ARG B 1 18  ? -5.645  22.693  9.491   1.00 31.17  ? 47  ARG B CA  1 
ATOM   3549 C C   . ARG B 1 18  ? -4.354  22.959  8.726   1.00 31.13  ? 47  ARG B C   1 
ATOM   3550 O O   . ARG B 1 18  ? -3.843  24.076  8.749   1.00 29.89  ? 47  ARG B O   1 
ATOM   3551 C CB  . ARG B 1 18  ? -5.412  22.049  10.857  1.00 34.91  ? 47  ARG B CB  1 
ATOM   3552 C CG  . ARG B 1 18  ? -4.412  22.769  11.737  1.00 40.14  ? 47  ARG B CG  1 
ATOM   3553 C CD  . ARG B 1 18  ? -4.425  22.181  13.156  1.00 50.47  ? 47  ARG B CD  1 
ATOM   3554 N NE  . ARG B 1 18  ? -3.055  22.185  13.682  1.00 58.52  ? 47  ARG B NE  1 
ATOM   3555 C CZ  . ARG B 1 18  ? -2.680  22.139  14.960  1.00 61.94  ? 47  ARG B CZ  1 
ATOM   3556 N NH1 . ARG B 1 18  ? -3.579  22.103  15.934  1.00 61.21  ? 47  ARG B NH1 1 
ATOM   3557 N NH2 . ARG B 1 18  ? -1.388  22.107  15.253  1.00 54.54  ? 47  ARG B NH2 1 
ATOM   3558 N N   . ILE B 1 19  ? -3.832  21.932  8.046   1.00 25.35  ? 48  ILE B N   1 
ATOM   3559 C CA  . ILE B 1 19  ? -2.649  22.105  7.236   1.00 27.71  ? 48  ILE B CA  1 
ATOM   3560 C C   . ILE B 1 19  ? -2.945  22.989  6.019   1.00 29.01  ? 48  ILE B C   1 
ATOM   3561 O O   . ILE B 1 19  ? -2.131  23.843  5.681   1.00 28.46  ? 48  ILE B O   1 
ATOM   3562 C CB  . ILE B 1 19  ? -2.061  20.728  6.841   1.00 27.09  ? 48  ILE B CB  1 
ATOM   3563 C CG1 . ILE B 1 19  ? -1.364  20.108  8.030   1.00 28.74  ? 48  ILE B CG1 1 
ATOM   3564 C CG2 . ILE B 1 19  ? -1.121  20.835  5.636   1.00 24.80  ? 48  ILE B CG2 1 
ATOM   3565 C CD1 . ILE B 1 19  ? -0.947  18.651  7.832   1.00 32.96  ? 48  ILE B CD1 1 
ATOM   3566 N N   . LYS B 1 20  ? -4.023  22.701  5.300   1.00 28.42  ? 49  LYS B N   1 
ATOM   3567 C CA  . LYS B 1 20  ? -4.400  23.497  4.138   1.00 37.41  ? 49  LYS B CA  1 
ATOM   3568 C C   . LYS B 1 20  ? -4.508  24.982  4.525   1.00 32.18  ? 49  LYS B C   1 
ATOM   3569 O O   . LYS B 1 20  ? -4.018  25.846  3.801   1.00 30.34  ? 49  LYS B O   1 
ATOM   3570 C CB  . LYS B 1 20  ? -5.720  22.962  3.575   1.00 36.81  ? 49  LYS B CB  1 
ATOM   3571 C CG  . LYS B 1 20  ? -6.208  23.507  2.243   1.00 40.38  ? 49  LYS B CG  1 
ATOM   3572 C CD  . LYS B 1 20  ? -7.535  22.820  1.883   1.00 43.05  ? 49  LYS B CD  1 
ATOM   3573 C CE  . LYS B 1 20  ? -8.466  23.624  1.023   1.00 54.03  ? 49  LYS B CE  1 
ATOM   3574 N NZ  . LYS B 1 20  ? -8.180  23.446  -0.404  1.00 57.92  ? 49  LYS B NZ  1 
ATOM   3575 N N   . THR B 1 21  ? -5.132  25.262  5.663   1.00 31.79  ? 50  THR B N   1 
ATOM   3576 C CA  . THR B 1 21  ? -5.306  26.627  6.140   1.00 36.08  ? 50  THR B CA  1 
ATOM   3577 C C   . THR B 1 21  ? -3.940  27.270  6.361   1.00 30.97  ? 50  THR B C   1 
ATOM   3578 O O   . THR B 1 21  ? -3.722  28.390  5.963   1.00 32.45  ? 50  THR B O   1 
ATOM   3579 C CB  . THR B 1 21  ? -6.143  26.666  7.421   1.00 34.54  ? 50  THR B CB  1 
ATOM   3580 O OG1 . THR B 1 21  ? -7.468  26.262  7.082   1.00 34.63  ? 50  THR B OG1 1 
ATOM   3581 C CG2 . THR B 1 21  ? -6.244  28.050  8.022   1.00 34.59  ? 50  THR B CG2 1 
ATOM   3582 N N   . PHE B 1 22  ? -3.022  26.572  7.010   1.00 27.13  ? 51  PHE B N   1 
ATOM   3583 C CA  . PHE B 1 22  ? -1.723  27.153  7.303   1.00 27.46  ? 51  PHE B CA  1 
ATOM   3584 C C   . PHE B 1 22  ? -0.911  27.404  6.034   1.00 23.92  ? 51  PHE B C   1 
ATOM   3585 O O   . PHE B 1 22  ? -0.223  28.410  5.902   1.00 24.54  ? 51  PHE B O   1 
ATOM   3586 C CB  . PHE B 1 22  ? -1.021  26.197  8.256   1.00 26.82  ? 51  PHE B CB  1 
ATOM   3587 C CG  . PHE B 1 22  ? 0.390   26.605  8.593   1.00 26.13  ? 51  PHE B CG  1 
ATOM   3588 C CD1 . PHE B 1 22  ? 0.661   27.896  9.037   1.00 28.32  ? 51  PHE B CD1 1 
ATOM   3589 C CD2 . PHE B 1 22  ? 1.437   25.693  8.487   1.00 25.81  ? 51  PHE B CD2 1 
ATOM   3590 C CE1 . PHE B 1 22  ? 1.956   28.274  9.319   1.00 27.28  ? 51  PHE B CE1 1 
ATOM   3591 C CE2 . PHE B 1 22  ? 2.723   26.075  8.787   1.00 27.63  ? 51  PHE B CE2 1 
ATOM   3592 C CZ  . PHE B 1 22  ? 2.975   27.361  9.211   1.00 32.49  ? 51  PHE B CZ  1 
ATOM   3593 N N   . ARG B 1 23  ? -0.960  26.473  5.105   1.00 24.58  ? 52  ARG B N   1 
ATOM   3594 C CA  . ARG B 1 23  ? -0.259  26.637  3.844   1.00 23.98  ? 52  ARG B CA  1 
ATOM   3595 C C   . ARG B 1 23  ? -0.850  27.787  3.023   1.00 29.63  ? 52  ARG B C   1 
ATOM   3596 O O   . ARG B 1 23  ? -0.141  28.475  2.273   1.00 26.45  ? 52  ARG B O   1 
ATOM   3597 C CB  . ARG B 1 23  ? -0.242  25.328  3.044   1.00 23.55  ? 52  ARG B CB  1 
ATOM   3598 C CG  . ARG B 1 23  ? 0.618   24.228  3.656   1.00 26.06  ? 52  ARG B CG  1 
ATOM   3599 C CD  . ARG B 1 23  ? 0.588   22.947  2.824   1.00 27.80  ? 52  ARG B CD  1 
ATOM   3600 N NE  . ARG B 1 23  ? 1.267   23.189  1.557   1.00 33.05  ? 52  ARG B NE  1 
ATOM   3601 C CZ  . ARG B 1 23  ? 1.677   22.233  0.733   1.00 41.02  ? 52  ARG B CZ  1 
ATOM   3602 N NH1 . ARG B 1 23  ? 1.121   21.043  0.843   1.00 38.50  ? 52  ARG B NH1 1 
ATOM   3603 N NH2 . ARG B 1 23  ? 2.646   22.475  -0.166  1.00 38.82  ? 52  ARG B NH2 1 
ATOM   3604 N N   . GLN B 1 24  ? -2.168  27.974  3.116   1.00 27.25  ? 53  GLN B N   1 
ATOM   3605 C CA  . GLN B 1 24  ? -2.825  29.053  2.384   1.00 32.94  ? 53  GLN B CA  1 
ATOM   3606 C C   . GLN B 1 24  ? -2.515  30.408  3.032   1.00 29.54  ? 53  GLN B C   1 
ATOM   3607 O O   . GLN B 1 24  ? -2.586  31.448  2.381   1.00 33.53  ? 53  GLN B O   1 
ATOM   3608 C CB  . GLN B 1 24  ? -4.329  28.803  2.297   1.00 34.64  ? 53  GLN B CB  1 
ATOM   3609 C CG  . GLN B 1 24  ? -4.740  27.906  1.139   1.00 36.97  ? 53  GLN B CG  1 
ATOM   3610 C CD  . GLN B 1 24  ? -6.222  27.592  1.197   1.00 45.03  ? 53  GLN B CD  1 
ATOM   3611 O OE1 . GLN B 1 24  ? -6.908  27.806  2.210   1.00 42.49  ? 53  GLN B OE1 1 
ATOM   3612 N NE2 . GLN B 1 24  ? -6.711  27.045  0.101   1.00 52.33  ? 53  GLN B NE2 1 
ATOM   3613 N N   . GLN B 1 25  ? -2.180  30.404  4.322   1.00 24.76  ? 54  GLN B N   1 
ATOM   3614 C CA  . GLN B 1 25  ? -1.825  31.624  5.008   1.00 26.73  ? 54  GLN B CA  1 
ATOM   3615 C C   . GLN B 1 25  ? -0.339  31.929  4.839   1.00 28.04  ? 54  GLN B C   1 
ATOM   3616 O O   . GLN B 1 25  ? 0.051   33.097  4.925   1.00 27.13  ? 54  GLN B O   1 
ATOM   3617 C CB  . GLN B 1 25  ? -1.896  31.605  6.532   1.00 29.44  ? 54  GLN B CB  1 
ATOM   3618 C CG  . GLN B 1 25  ? -3.247  31.828  7.167   1.00 41.65  ? 54  GLN B CG  1 
ATOM   3619 C CD  . GLN B 1 25  ? -3.151  31.829  8.677   1.00 38.66  ? 54  GLN B CD  1 
ATOM   3620 O OE1 . GLN B 1 25  ? -4.114  32.131  9.368   1.00 44.12  ? 54  GLN B OE1 1 
ATOM   3621 N NE2 . GLN B 1 25  ? -2.016  31.415  9.215   1.00 42.92  ? 54  GLN B NE2 1 
ATOM   3622 N N   . HIS B 1 26  ? 0.500   30.886  4.737   1.00 25.48  ? 55  HIS B N   1 
ATOM   3623 C CA  . HIS B 1 26  ? 1.932   31.082  4.928   1.00 26.10  ? 55  HIS B CA  1 
ATOM   3624 C C   . HIS B 1 26  ? 2.812   30.232  4.031   1.00 23.91  ? 55  HIS B C   1 
ATOM   3625 O O   . HIS B 1 26  ? 4.001   30.167  4.294   1.00 26.29  ? 55  HIS B O   1 
ATOM   3626 C CB  . HIS B 1 26  ? 2.358   30.742  6.356   1.00 28.28  ? 55  HIS B CB  1 
ATOM   3627 C CG  . HIS B 1 26  ? 2.058   31.794  7.343   1.00 28.31  ? 55  HIS B CG  1 
ATOM   3628 N ND1 . HIS B 1 26  ? 2.715   33.004  7.358   1.00 30.66  ? 55  HIS B ND1 1 
ATOM   3629 C CD2 . HIS B 1 26  ? 1.170   31.812  8.327   1.00 32.42  ? 55  HIS B CD2 1 
ATOM   3630 C CE1 . HIS B 1 26  ? 2.280   33.695  8.399   1.00 32.72  ? 55  HIS B CE1 1 
ATOM   3631 N NE2 . HIS B 1 26  ? 1.327   32.990  8.991   1.00 31.35  ? 55  HIS B NE2 1 
ATOM   3632 N N   . GLY B 1 27  ? 2.262   29.638  2.970   1.00 28.68  ? 56  GLY B N   1 
ATOM   3633 C CA  . GLY B 1 27  ? 3.026   28.741  2.114   1.00 29.16  ? 56  GLY B CA  1 
ATOM   3634 C C   . GLY B 1 27  ? 4.342   29.359  1.621   1.00 30.89  ? 56  GLY B C   1 
ATOM   3635 O O   . GLY B 1 27  ? 5.394   28.684  1.543   1.00 24.88  ? 56  GLY B O   1 
ATOM   3636 N N   . LYS B 1 28  ? 4.293   30.660  1.288   1.00 31.37  ? 57  LYS B N   1 
ATOM   3637 C CA  . LYS B 1 28  ? 5.448   31.349  0.740   1.00 27.77  ? 57  LYS B CA  1 
ATOM   3638 C C   . LYS B 1 28  ? 6.325   31.969  1.828   1.00 24.70  ? 57  LYS B C   1 
ATOM   3639 O O   . LYS B 1 28  ? 7.381   32.486  1.503   1.00 28.36  ? 57  LYS B O   1 
ATOM   3640 C CB  . LYS B 1 28  ? 5.047   32.371  -0.325  1.00 28.22  ? 57  LYS B CB  1 
ATOM   3641 C CG  . LYS B 1 28  ? 4.351   31.811  -1.578  1.00 31.51  ? 57  LYS B CG  1 
ATOM   3642 C CD  . LYS B 1 28  ? 3.756   32.973  -2.376  1.00 39.15  ? 57  LYS B CD  1 
ATOM   3643 C CE  . LYS B 1 28  ? 3.055   32.595  -3.628  1.00 49.12  ? 57  LYS B CE  1 
ATOM   3644 N NZ  . LYS B 1 28  ? 2.748   33.781  -4.452  1.00 53.49  ? 57  LYS B NZ  1 
ATOM   3645 N N   . THR B 1 29  ? 5.984   31.842  3.105   1.00 23.13  ? 58  THR B N   1 
ATOM   3646 C CA  . THR B 1 29  ? 6.788   32.474  4.138   1.00 26.70  ? 58  THR B CA  1 
ATOM   3647 C C   . THR B 1 29  ? 8.152   31.778  4.265   1.00 28.59  ? 58  THR B C   1 
ATOM   3648 O O   . THR B 1 29  ? 8.247   30.547  4.348   1.00 26.86  ? 58  THR B O   1 
ATOM   3649 C CB  . THR B 1 29  ? 6.038   32.448  5.469   1.00 28.10  ? 58  THR B CB  1 
ATOM   3650 O OG1 . THR B 1 29  ? 4.843   33.181  5.231   1.00 29.53  ? 58  THR B OG1 1 
ATOM   3651 C CG2 . THR B 1 29  ? 6.876   32.994  6.609   1.00 27.83  ? 58  THR B CG2 1 
ATOM   3652 N N   . VAL B 1 30  ? 9.209   32.583  4.301   1.00 27.94  ? 59  VAL B N   1 
ATOM   3653 C CA  . VAL B 1 30  ? 10.560  32.094  4.504   1.00 29.77  ? 59  VAL B CA  1 
ATOM   3654 C C   . VAL B 1 30  ? 10.759  31.678  5.952   1.00 30.16  ? 59  VAL B C   1 
ATOM   3655 O O   . VAL B 1 30  ? 10.535  32.453  6.878   1.00 28.24  ? 59  VAL B O   1 
ATOM   3656 C CB  . VAL B 1 30  ? 11.623  33.114  4.081   1.00 31.29  ? 59  VAL B CB  1 
ATOM   3657 C CG1 . VAL B 1 30  ? 13.008  32.682  4.514   1.00 30.57  ? 59  VAL B CG1 1 
ATOM   3658 C CG2 . VAL B 1 30  ? 11.569  33.386  2.578   1.00 31.86  ? 59  VAL B CG2 1 
ATOM   3659 N N   . VAL B 1 31  ? 11.203  30.426  6.147   1.00 28.26  ? 60  VAL B N   1 
ATOM   3660 C CA  . VAL B 1 31  ? 11.480  29.978  7.499   1.00 29.35  ? 60  VAL B CA  1 
ATOM   3661 C C   . VAL B 1 31  ? 12.972  29.780  7.753   1.00 27.94  ? 60  VAL B C   1 
ATOM   3662 O O   . VAL B 1 31  ? 13.348  29.559  8.893   1.00 29.27  ? 60  VAL B O   1 
ATOM   3663 C CB  . VAL B 1 31  ? 10.727  28.707  7.880   1.00 30.34  ? 60  VAL B CB  1 
ATOM   3664 C CG1 . VAL B 1 31  ? 9.265   29.032  8.170   1.00 35.06  ? 60  VAL B CG1 1 
ATOM   3665 C CG2 . VAL B 1 31  ? 10.912  27.622  6.844   1.00 30.32  ? 60  VAL B CG2 1 
ATOM   3666 N N   . GLY B 1 32  ? 13.791  29.784  6.713   1.00 27.20  ? 61  GLY B N   1 
ATOM   3667 C CA  . GLY B 1 32  ? 15.214  29.591  6.900   1.00 27.23  ? 61  GLY B CA  1 
ATOM   3668 C C   . GLY B 1 32  ? 15.957  29.856  5.599   1.00 32.18  ? 61  GLY B C   1 
ATOM   3669 O O   . GLY B 1 32  ? 15.351  29.933  4.520   1.00 29.87  ? 61  GLY B O   1 
ATOM   3670 N N   . GLN B 1 33  ? 17.273  29.993  5.738   1.00 30.54  ? 62  GLN B N   1 
ATOM   3671 C CA  . GLN B 1 33  ? 18.181  30.194  4.621   1.00 34.82  ? 62  GLN B CA  1 
ATOM   3672 C C   . GLN B 1 33  ? 19.035  28.927  4.452   1.00 32.56  ? 62  GLN B C   1 
ATOM   3673 O O   . GLN B 1 33  ? 19.311  28.199  5.415   1.00 31.17  ? 62  GLN B O   1 
ATOM   3674 C CB  . GLN B 1 33  ? 19.091  31.394  4.869   1.00 43.08  ? 62  GLN B CB  1 
ATOM   3675 C CG  . GLN B 1 33  ? 18.382  32.635  5.407   1.00 50.50  ? 62  GLN B CG  1 
ATOM   3676 C CD  . GLN B 1 33  ? 17.653  33.418  4.339   1.00 55.72  ? 62  GLN B CD  1 
ATOM   3677 O OE1 . GLN B 1 33  ? 16.452  33.700  4.443   1.00 57.55  ? 62  GLN B OE1 1 
ATOM   3678 N NE2 . GLN B 1 33  ? 18.389  33.802  3.307   1.00 59.95  ? 62  GLN B NE2 1 
ATOM   3679 N N   . ILE B 1 34  ? 19.419  28.645  3.216   1.00 27.59  ? 63  ILE B N   1 
ATOM   3680 C CA  . ILE B 1 34  ? 20.366  27.582  2.935   1.00 29.56  ? 63  ILE B CA  1 
ATOM   3681 C C   . ILE B 1 34  ? 21.720  28.183  2.568   1.00 25.82  ? 63  ILE B C   1 
ATOM   3682 O O   . ILE B 1 34  ? 21.815  28.973  1.632   1.00 29.39  ? 63  ILE B O   1 
ATOM   3683 C CB  . ILE B 1 34  ? 19.872  26.710  1.773   1.00 30.52  ? 63  ILE B CB  1 
ATOM   3684 C CG1 . ILE B 1 34  ? 18.442  26.209  2.005   1.00 33.89  ? 63  ILE B CG1 1 
ATOM   3685 C CG2 . ILE B 1 34  ? 20.856  25.565  1.562   1.00 27.50  ? 63  ILE B CG2 1 
ATOM   3686 C CD1 . ILE B 1 34  ? 17.750  25.708  0.752   1.00 40.21  ? 63  ILE B CD1 1 
ATOM   3687 N N   . THR B 1 35  ? 22.767  27.779  3.278   1.00 26.31  ? 64  THR B N   1 
ATOM   3688 C CA  . THR B 1 35  ? 24.132  28.173  2.951   1.00 26.07  ? 64  THR B CA  1 
ATOM   3689 C C   . THR B 1 35  ? 24.885  27.018  2.287   1.00 30.12  ? 64  THR B C   1 
ATOM   3690 O O   . THR B 1 35  ? 24.495  25.858  2.369   1.00 27.46  ? 64  THR B O   1 
ATOM   3691 C CB  . THR B 1 35  ? 24.875  28.611  4.200   1.00 28.12  ? 64  THR B CB  1 
ATOM   3692 O OG1 . THR B 1 35  ? 24.858  27.462  5.032   1.00 27.71  ? 64  THR B OG1 1 
ATOM   3693 C CG2 . THR B 1 35  ? 24.205  29.804  4.883   1.00 31.96  ? 64  THR B CG2 1 
ATOM   3694 N N   . VAL B 1 36  ? 26.006  27.365  1.669   1.00 26.34  ? 65  VAL B N   1 
ATOM   3695 C CA  . VAL B 1 36  ? 26.931  26.386  1.131   1.00 26.99  ? 65  VAL B CA  1 
ATOM   3696 C C   . VAL B 1 36  ? 27.313  25.386  2.222   1.00 27.65  ? 65  VAL B C   1 
ATOM   3697 O O   . VAL B 1 36  ? 27.356  24.173  1.953   1.00 31.31  ? 65  VAL B O   1 
ATOM   3698 C CB  . VAL B 1 36  ? 28.149  27.129  0.553   1.00 26.98  ? 65  VAL B CB  1 
ATOM   3699 C CG1 . VAL B 1 36  ? 29.345  26.209  0.315   1.00 30.51  ? 65  VAL B CG1 1 
ATOM   3700 C CG2 . VAL B 1 36  ? 27.767  27.846  -0.740  1.00 28.11  ? 65  VAL B CG2 1 
ATOM   3701 N N   . ASP B 1 37  ? 27.619  25.897  3.426   1.00 26.17  ? 66  ASP B N   1 
ATOM   3702 C CA  . ASP B 1 37  ? 28.007  25.084  4.559   1.00 27.29  ? 66  ASP B CA  1 
ATOM   3703 C C   . ASP B 1 37  ? 26.931  24.070  4.932   1.00 28.59  ? 66  ASP B C   1 
ATOM   3704 O O   . ASP B 1 37  ? 27.252  22.983  5.353   1.00 24.65  ? 66  ASP B O   1 
ATOM   3705 C CB  . ASP B 1 37  ? 28.324  25.901  5.805   1.00 32.80  ? 66  ASP B CB  1 
ATOM   3706 C CG  . ASP B 1 37  ? 29.774  26.359  5.959   1.00 42.27  ? 66  ASP B CG  1 
ATOM   3707 O OD1 . ASP B 1 37  ? 30.665  25.747  5.300   1.00 36.92  ? 66  ASP B OD1 1 
ATOM   3708 O OD2 . ASP B 1 37  ? 30.002  27.323  6.747   1.00 44.37  ? 66  ASP B OD2 1 
ATOM   3709 N N   . MET B 1 38  ? 25.652  24.446  4.849   1.00 28.68  ? 67  MET B N   1 
ATOM   3710 C CA  . MET B 1 38  ? 24.604  23.500  5.174   1.00 28.66  ? 67  MET B CA  1 
ATOM   3711 C C   . MET B 1 38  ? 24.595  22.349  4.177   1.00 26.49  ? 67  MET B C   1 
ATOM   3712 O O   . MET B 1 38  ? 24.331  21.208  4.554   1.00 27.48  ? 67  MET B O   1 
ATOM   3713 C CB  . MET B 1 38  ? 23.210  24.153  5.210   1.00 27.71  ? 67  MET B CB  1 
ATOM   3714 C CG  . MET B 1 38  ? 23.035  25.054  6.392   1.00 31.94  ? 67  MET B CG  1 
ATOM   3715 S SD  . MET B 1 38  ? 21.598  26.136  6.196   1.00 35.40  ? 67  MET B SD  1 
ATOM   3716 C CE  . MET B 1 38  ? 21.668  26.899  7.829   1.00 35.61  ? 67  MET B CE  1 
ATOM   3717 N N   . MET B 1 39  ? 24.833  22.662  2.894   1.00 26.47  ? 68  MET B N   1 
ATOM   3718 C CA  . MET B 1 39  ? 24.885  21.638  1.880   1.00 24.38  ? 68  MET B CA  1 
ATOM   3719 C C   . MET B 1 39  ? 26.033  20.639  2.105   1.00 26.90  ? 68  MET B C   1 
ATOM   3720 O O   . MET B 1 39  ? 25.853  19.420  1.915   1.00 28.12  ? 68  MET B O   1 
ATOM   3721 C CB  . MET B 1 39  ? 24.975  22.326  0.533   1.00 24.85  ? 68  MET B CB  1 
ATOM   3722 C CG  . MET B 1 39  ? 23.764  23.126  0.248   1.00 27.51  ? 68  MET B CG  1 
ATOM   3723 S SD  . MET B 1 39  ? 23.881  23.798  -1.405  1.00 29.21  ? 68  MET B SD  1 
ATOM   3724 C CE  . MET B 1 39  ? 23.819  22.335  -2.456  1.00 30.41  ? 68  MET B CE  1 
ATOM   3725 N N   . TYR B 1 40  ? 27.226  21.142  2.467   1.00 24.94  ? 69  TYR B N   1 
ATOM   3726 C CA  . TYR B 1 40  ? 28.372  20.304  2.774   1.00 26.18  ? 69  TYR B CA  1 
ATOM   3727 C C   . TYR B 1 40  ? 28.182  19.626  4.139   1.00 27.97  ? 69  TYR B C   1 
ATOM   3728 O O   . TYR B 1 40  ? 28.726  18.547  4.353   1.00 28.90  ? 69  TYR B O   1 
ATOM   3729 C CB  . TYR B 1 40  ? 29.699  21.078  2.729   1.00 23.85  ? 69  TYR B CB  1 
ATOM   3730 C CG  . TYR B 1 40  ? 30.209  21.336  1.321   1.00 21.33  ? 69  TYR B CG  1 
ATOM   3731 C CD1 . TYR B 1 40  ? 30.766  20.320  0.568   1.00 23.07  ? 69  TYR B CD1 1 
ATOM   3732 C CD2 . TYR B 1 40  ? 30.157  22.590  0.767   1.00 20.69  ? 69  TYR B CD2 1 
ATOM   3733 C CE1 . TYR B 1 40  ? 31.207  20.529  -0.719  1.00 25.84  ? 69  TYR B CE1 1 
ATOM   3734 C CE2 . TYR B 1 40  ? 30.602  22.831  -0.522  1.00 25.63  ? 69  TYR B CE2 1 
ATOM   3735 C CZ  . TYR B 1 40  ? 31.153  21.804  -1.263  1.00 27.27  ? 69  TYR B CZ  1 
ATOM   3736 O OH  . TYR B 1 40  ? 31.594  22.015  -2.528  1.00 26.63  ? 69  TYR B OH  1 
ATOM   3737 N N   . GLY B 1 41  ? 27.376  20.207  5.022   1.00 23.50  ? 70  GLY B N   1 
ATOM   3738 C CA  . GLY B 1 41  ? 27.293  19.725  6.404   1.00 24.57  ? 70  GLY B CA  1 
ATOM   3739 C C   . GLY B 1 41  ? 26.037  18.892  6.714   1.00 23.84  ? 70  GLY B C   1 
ATOM   3740 O O   . GLY B 1 41  ? 25.563  18.852  7.847   1.00 21.60  ? 70  GLY B O   1 
ATOM   3741 N N   . GLY B 1 42  ? 25.506  18.174  5.727   1.00 24.23  ? 71  GLY B N   1 
ATOM   3742 C CA  . GLY B 1 42  ? 24.478  17.183  6.018   1.00 24.40  ? 71  GLY B CA  1 
ATOM   3743 C C   . GLY B 1 42  ? 23.177  17.853  6.415   1.00 22.03  ? 71  GLY B C   1 
ATOM   3744 O O   . GLY B 1 42  ? 22.454  17.336  7.254   1.00 24.00  ? 71  GLY B O   1 
ATOM   3745 N N   . MET B 1 43  ? 22.919  19.027  5.830   1.00 22.85  ? 72  MET B N   1 
ATOM   3746 C CA  . MET B 1 43  ? 21.710  19.800  6.074   1.00 23.37  ? 72  MET B CA  1 
ATOM   3747 C C   . MET B 1 43  ? 21.579  20.233  7.547   1.00 27.58  ? 72  MET B C   1 
ATOM   3748 O O   . MET B 1 43  ? 20.482  20.524  8.000   1.00 24.24  ? 72  MET B O   1 
ATOM   3749 C CB  . MET B 1 43  ? 20.442  19.018  5.718   1.00 26.29  ? 72  MET B CB  1 
ATOM   3750 C CG  . MET B 1 43  ? 20.447  18.365  4.355   1.00 26.44  ? 72  MET B CG  1 
ATOM   3751 S SD  . MET B 1 43  ? 18.867  17.536  4.045   1.00 33.36  ? 72  MET B SD  1 
ATOM   3752 C CE  . MET B 1 43  ? 19.013  16.814  2.394   1.00 34.29  ? 72  MET B CE  1 
ATOM   3753 N N   . ARG B 1 44  ? 22.676  20.308  8.294   1.00 27.89  ? 73  ARG B N   1 
ATOM   3754 C CA  . ARG B 1 44  ? 22.606  20.692  9.691   1.00 34.05  ? 73  ARG B CA  1 
ATOM   3755 C C   . ARG B 1 44  ? 22.000  22.097  9.842   1.00 31.75  ? 73  ARG B C   1 
ATOM   3756 O O   . ARG B 1 44  ? 22.457  23.048  9.225   1.00 33.80  ? 73  ARG B O   1 
ATOM   3757 C CB  . ARG B 1 44  ? 24.017  20.653  10.289  1.00 36.66  ? 73  ARG B CB  1 
ATOM   3758 C CG  . ARG B 1 44  ? 24.039  20.783  11.811  1.00 51.48  ? 73  ARG B CG  1 
ATOM   3759 C CD  . ARG B 1 44  ? 25.460  21.047  12.334  1.00 65.66  ? 73  ARG B CD  1 
ATOM   3760 N NE  . ARG B 1 44  ? 26.385  20.055  11.772  1.00 77.07  ? 73  ARG B NE  1 
ATOM   3761 C CZ  . ARG B 1 44  ? 27.164  20.214  10.689  1.00 85.84  ? 73  ARG B CZ  1 
ATOM   3762 N NH1 . ARG B 1 44  ? 27.362  21.416  10.164  1.00 89.57  ? 73  ARG B NH1 1 
ATOM   3763 N NH2 . ARG B 1 44  ? 27.760  19.161  10.142  1.00 75.51  ? 73  ARG B NH2 1 
ATOM   3764 N N   . GLY B 1 45  ? 20.959  22.197  10.665  1.00 34.68  ? 74  GLY B N   1 
ATOM   3765 C CA  . GLY B 1 45  ? 20.313  23.461  10.967  1.00 39.98  ? 74  GLY B CA  1 
ATOM   3766 C C   . GLY B 1 45  ? 19.222  23.823  9.954   1.00 45.41  ? 74  GLY B C   1 
ATOM   3767 O O   . GLY B 1 45  ? 18.559  24.861  10.079  1.00 42.39  ? 74  GLY B O   1 
ATOM   3768 N N   . MET B 1 46  ? 19.033  22.973  8.941   1.00 34.01  ? 75  MET B N   1 
ATOM   3769 C CA  . MET B 1 46  ? 18.111  23.302  7.886   1.00 30.84  ? 75  MET B CA  1 
ATOM   3770 C C   . MET B 1 46  ? 16.763  22.659  8.239   1.00 27.43  ? 75  MET B C   1 
ATOM   3771 O O   . MET B 1 46  ? 16.657  21.457  8.435   1.00 26.68  ? 75  MET B O   1 
ATOM   3772 C CB  . MET B 1 46  ? 18.775  22.906  6.560   1.00 32.20  ? 75  MET B CB  1 
ATOM   3773 C CG  . MET B 1 46  ? 17.894  22.721  5.351   1.00 40.75  ? 75  MET B CG  1 
ATOM   3774 S SD  . MET B 1 46  ? 18.776  22.188  3.856   1.00 41.17  ? 75  MET B SD  1 
ATOM   3775 C CE  . MET B 1 46  ? 20.277  23.022  4.322   1.00 32.37  ? 75  MET B CE  1 
ATOM   3776 N N   . LYS B 1 47  ? 15.715  23.463  8.308   1.00 25.98  ? 76  LYS B N   1 
ATOM   3777 C CA  . LYS B 1 47  ? 14.362  22.953  8.515   1.00 27.99  ? 76  LYS B CA  1 
ATOM   3778 C C   . LYS B 1 47  ? 13.914  22.318  7.209   1.00 27.58  ? 76  LYS B C   1 
ATOM   3779 O O   . LYS B 1 47  ? 13.661  23.035  6.259   1.00 38.16  ? 76  LYS B O   1 
ATOM   3780 C CB  . LYS B 1 47  ? 13.408  24.066  8.975   1.00 32.22  ? 76  LYS B CB  1 
ATOM   3781 C CG  . LYS B 1 47  ? 13.832  24.730  10.270  1.00 33.78  ? 76  LYS B CG  1 
ATOM   3782 C CD  . LYS B 1 47  ? 12.828  25.729  10.837  1.00 41.35  ? 76  LYS B CD  1 
ATOM   3783 C CE  . LYS B 1 47  ? 13.049  26.060  12.305  1.00 41.81  ? 76  LYS B CE  1 
ATOM   3784 N NZ  . LYS B 1 47  ? 14.413  26.572  12.578  1.00 41.13  ? 76  LYS B NZ  1 
ATOM   3785 N N   . GLY B 1 48  ? 13.872  20.981  7.131   1.00 24.25  ? 77  GLY B N   1 
ATOM   3786 C CA  . GLY B 1 48  ? 13.726  20.317  5.849   1.00 23.10  ? 77  GLY B CA  1 
ATOM   3787 C C   . GLY B 1 48  ? 12.403  19.567  5.657   1.00 23.10  ? 77  GLY B C   1 
ATOM   3788 O O   . GLY B 1 48  ? 12.011  19.291  4.510   1.00 26.92  ? 77  GLY B O   1 
ATOM   3789 N N   . LEU B 1 49  ? 11.756  19.145  6.741   1.00 20.09  ? 78  LEU B N   1 
ATOM   3790 C CA  . LEU B 1 49  ? 10.590  18.282  6.622   1.00 23.86  ? 78  LEU B CA  1 
ATOM   3791 C C   . LEU B 1 49  ? 9.614   18.454  7.780   1.00 23.35  ? 78  LEU B C   1 
ATOM   3792 O O   . LEU B 1 49  ? 9.962   18.918  8.845   1.00 21.44  ? 78  LEU B O   1 
ATOM   3793 C CB  . LEU B 1 49  ? 11.014  16.825  6.506   1.00 28.34  ? 78  LEU B CB  1 
ATOM   3794 C CG  . LEU B 1 49  ? 11.652  16.222  7.755   1.00 28.93  ? 78  LEU B CG  1 
ATOM   3795 C CD1 . LEU B 1 49  ? 11.542  14.724  7.756   1.00 32.64  ? 78  LEU B CD1 1 
ATOM   3796 C CD2 . LEU B 1 49  ? 13.097  16.677  7.820   1.00 29.00  ? 78  LEU B CD2 1 
ATOM   3797 N N   . VAL B 1 50  ? 8.381   18.047  7.516   1.00 24.33  ? 79  VAL B N   1 
ATOM   3798 C CA  . VAL B 1 50  ? 7.331   18.059  8.503   1.00 24.73  ? 79  VAL B CA  1 
ATOM   3799 C C   . VAL B 1 50  ? 7.120   16.632  8.990   1.00 24.99  ? 79  VAL B C   1 
ATOM   3800 O O   . VAL B 1 50  ? 6.949   15.710  8.193   1.00 22.15  ? 79  VAL B O   1 
ATOM   3801 C CB  . VAL B 1 50  ? 6.031   18.672  7.934   1.00 25.86  ? 79  VAL B CB  1 
ATOM   3802 C CG1 . VAL B 1 50  ? 4.921   18.660  8.990   1.00 24.90  ? 79  VAL B CG1 1 
ATOM   3803 C CG2 . VAL B 1 50  ? 6.272   20.108  7.440   1.00 22.79  ? 79  VAL B CG2 1 
ATOM   3804 N N   . TYR B 1 51  ? 7.118   16.517  10.307  1.00 24.07  ? 80  TYR B N   1 
ATOM   3805 C CA  . TYR B 1 51  ? 7.061   15.263  11.019  1.00 24.55  ? 80  TYR B CA  1 
ATOM   3806 C C   . TYR B 1 51  ? 6.265   15.530  12.308  1.00 22.07  ? 80  TYR B C   1 
ATOM   3807 O O   . TYR B 1 51  ? 6.648   16.327  13.138  1.00 23.15  ? 80  TYR B O   1 
ATOM   3808 C CB  . TYR B 1 51  ? 8.518   14.820  11.171  1.00 26.42  ? 80  TYR B CB  1 
ATOM   3809 C CG  . TYR B 1 51  ? 8.682   13.379  11.620  1.00 22.89  ? 80  TYR B CG  1 
ATOM   3810 C CD1 . TYR B 1 51  ? 8.595   13.055  12.969  1.00 25.23  ? 80  TYR B CD1 1 
ATOM   3811 C CD2 . TYR B 1 51  ? 8.936   12.362  10.730  1.00 24.00  ? 80  TYR B CD2 1 
ATOM   3812 C CE1 . TYR B 1 51  ? 8.808   11.764  13.418  1.00 25.45  ? 80  TYR B CE1 1 
ATOM   3813 C CE2 . TYR B 1 51  ? 9.064   11.043  11.158  1.00 22.71  ? 80  TYR B CE2 1 
ATOM   3814 C CZ  . TYR B 1 51  ? 8.998   10.753  12.508  1.00 22.53  ? 80  TYR B CZ  1 
ATOM   3815 O OH  . TYR B 1 51  ? 9.143   9.490   12.993  1.00 25.72  ? 80  TYR B OH  1 
ATOM   3816 N N   . GLU B 1 52  ? 5.102   14.890  12.424  1.00 23.71  ? 81  GLU B N   1 
ATOM   3817 C CA  . GLU B 1 52  ? 4.059   15.380  13.321  1.00 25.43  ? 81  GLU B CA  1 
ATOM   3818 C C   . GLU B 1 52  ? 4.115   14.749  14.720  1.00 25.00  ? 81  GLU B C   1 
ATOM   3819 O O   . GLU B 1 52  ? 3.587   15.320  15.676  1.00 24.76  ? 81  GLU B O   1 
ATOM   3820 C CB  . GLU B 1 52  ? 2.700   15.052  12.691  1.00 27.21  ? 81  GLU B CB  1 
ATOM   3821 C CG  . GLU B 1 52  ? 2.472   15.647  11.303  1.00 30.66  ? 81  GLU B CG  1 
ATOM   3822 C CD  . GLU B 1 52  ? 2.225   17.151  11.341  1.00 35.69  ? 81  GLU B CD  1 
ATOM   3823 O OE1 . GLU B 1 52  ? 2.569   17.843  12.325  1.00 33.48  ? 81  GLU B OE1 1 
ATOM   3824 O OE2 . GLU B 1 52  ? 1.742   17.659  10.317  1.00 35.94  ? 81  GLU B OE2 1 
ATOM   3825 N N   . THR B 1 53  ? 4.747   13.581  14.831  1.00 25.37  ? 82  THR B N   1 
ATOM   3826 C CA  . THR B 1 53  ? 4.514   12.675  15.946  1.00 23.94  ? 82  THR B CA  1 
ATOM   3827 C C   . THR B 1 53  ? 5.315   13.106  17.163  1.00 27.58  ? 82  THR B C   1 
ATOM   3828 O O   . THR B 1 53  ? 4.847   12.904  18.264  1.00 24.29  ? 82  THR B O   1 
ATOM   3829 C CB  . THR B 1 53  ? 4.792   11.218  15.558  1.00 24.82  ? 82  THR B CB  1 
ATOM   3830 O OG1 . THR B 1 53  ? 6.001   11.053  14.829  1.00 21.57  ? 82  THR B OG1 1 
ATOM   3831 C CG2 . THR B 1 53  ? 3.714   10.643  14.661  1.00 24.68  ? 82  THR B CG2 1 
ATOM   3832 N N   . SER B 1 54  ? 6.491   13.714  16.986  1.00 25.90  ? 83  SER B N   1 
ATOM   3833 C CA  . SER B 1 54  ? 7.304   14.087  18.126  1.00 24.34  ? 83  SER B CA  1 
ATOM   3834 C C   . SER B 1 54  ? 8.146   15.306  17.790  1.00 25.53  ? 83  SER B C   1 
ATOM   3835 O O   . SER B 1 54  ? 8.427   15.532  16.624  1.00 24.68  ? 83  SER B O   1 
ATOM   3836 C CB  . SER B 1 54  ? 8.165   12.956  18.607  1.00 25.78  ? 83  SER B CB  1 
ATOM   3837 O OG  . SER B 1 54  ? 9.174   12.592  17.680  1.00 23.40  ? 83  SER B OG  1 
ATOM   3838 N N   . VAL B 1 55  ? 8.482   16.066  18.845  1.00 26.95  ? 84  VAL B N   1 
ATOM   3839 C CA  . VAL B 1 55  ? 9.224   17.308  18.783  1.00 26.36  ? 84  VAL B CA  1 
ATOM   3840 C C   . VAL B 1 55  ? 10.178  17.376  19.964  1.00 25.24  ? 84  VAL B C   1 
ATOM   3841 O O   . VAL B 1 55  ? 9.796   17.087  21.100  1.00 27.21  ? 84  VAL B O   1 
ATOM   3842 C CB  . VAL B 1 55  ? 8.225   18.495  18.797  1.00 27.79  ? 84  VAL B CB  1 
ATOM   3843 C CG1 . VAL B 1 55  ? 8.939   19.840  18.846  1.00 29.21  ? 84  VAL B CG1 1 
ATOM   3844 C CG2 . VAL B 1 55  ? 7.279   18.512  17.602  1.00 29.38  ? 84  VAL B CG2 1 
ATOM   3845 N N   . LEU B 1 56  ? 11.415  17.825  19.723  1.00 28.70  ? 85  LEU B N   1 
ATOM   3846 C CA  . LEU B 1 56  ? 12.380  18.028  20.800  1.00 31.54  ? 85  LEU B CA  1 
ATOM   3847 C C   . LEU B 1 56  ? 12.193  19.378  21.519  1.00 40.95  ? 85  LEU B C   1 
ATOM   3848 O O   . LEU B 1 56  ? 12.594  20.430  21.031  1.00 35.64  ? 85  LEU B O   1 
ATOM   3849 C CB  . LEU B 1 56  ? 13.787  17.924  20.220  1.00 35.67  ? 85  LEU B CB  1 
ATOM   3850 C CG  . LEU B 1 56  ? 14.929  18.069  21.237  1.00 42.16  ? 85  LEU B CG  1 
ATOM   3851 C CD1 . LEU B 1 56  ? 14.831  17.091  22.395  1.00 37.85  ? 85  LEU B CD1 1 
ATOM   3852 C CD2 . LEU B 1 56  ? 16.260  17.924  20.501  1.00 44.28  ? 85  LEU B CD2 1 
ATOM   3853 N N   . ASP B 1 57  ? 11.679  19.341  22.755  1.00 41.23  ? 86  ASP B N   1 
ATOM   3854 C CA  . ASP B 1 57  ? 11.579  20.525  23.601  1.00 38.23  ? 86  ASP B CA  1 
ATOM   3855 C C   . ASP B 1 57  ? 12.940  20.775  24.255  1.00 43.98  ? 86  ASP B C   1 
ATOM   3856 O O   . ASP B 1 57  ? 13.462  19.952  25.013  1.00 46.07  ? 86  ASP B O   1 
ATOM   3857 C CB  . ASP B 1 57  ? 10.453  20.333  24.609  1.00 40.96  ? 86  ASP B CB  1 
ATOM   3858 C CG  . ASP B 1 57  ? 10.090  21.527  25.483  1.00 45.82  ? 86  ASP B CG  1 
ATOM   3859 O OD1 . ASP B 1 57  ? 11.017  22.259  25.905  1.00 42.55  ? 86  ASP B OD1 1 
ATOM   3860 O OD2 . ASP B 1 57  ? 8.892   21.671  25.773  1.00 47.59  ? 86  ASP B OD2 1 
ATOM   3861 N N   . PRO B 1 58  ? 13.582  21.929  24.000  1.00 48.26  ? 87  PRO B N   1 
ATOM   3862 C CA  . PRO B 1 58  ? 14.979  22.105  24.412  1.00 47.30  ? 87  PRO B CA  1 
ATOM   3863 C C   . PRO B 1 58  ? 15.155  22.371  25.911  1.00 54.48  ? 87  PRO B C   1 
ATOM   3864 O O   . PRO B 1 58  ? 16.279  22.414  26.412  1.00 45.99  ? 87  PRO B O   1 
ATOM   3865 C CB  . PRO B 1 58  ? 15.424  23.272  23.522  1.00 44.52  ? 87  PRO B CB  1 
ATOM   3866 C CG  . PRO B 1 58  ? 14.152  24.098  23.370  1.00 47.42  ? 87  PRO B CG  1 
ATOM   3867 C CD  . PRO B 1 58  ? 13.001  23.105  23.329  1.00 46.99  ? 87  PRO B CD  1 
ATOM   3868 N N   . ASP B 1 59  ? 14.048  22.511  26.644  1.00 54.59  ? 88  ASP B N   1 
ATOM   3869 C CA  . ASP B 1 59  ? 14.144  22.607  28.095  1.00 68.90  ? 88  ASP B CA  1 
ATOM   3870 C C   . ASP B 1 59  ? 13.503  21.398  28.785  1.00 68.81  ? 88  ASP B C   1 
ATOM   3871 O O   . ASP B 1 59  ? 13.546  21.335  30.013  1.00 62.58  ? 88  ASP B O   1 
ATOM   3872 C CB  . ASP B 1 59  ? 13.654  23.956  28.614  1.00 84.68  ? 88  ASP B CB  1 
ATOM   3873 C CG  . ASP B 1 59  ? 12.366  24.499  28.010  1.00 103.28 ? 88  ASP B CG  1 
ATOM   3874 O OD1 . ASP B 1 59  ? 12.350  24.730  26.779  1.00 118.75 ? 88  ASP B OD1 1 
ATOM   3875 O OD2 . ASP B 1 59  ? 11.395  24.698  28.778  1.00 111.76 ? 88  ASP B OD2 1 
ATOM   3876 N N   . GLU B 1 60  ? 12.924  20.447  28.021  1.00 58.43  ? 89  GLU B N   1 
ATOM   3877 C CA  . GLU B 1 60  ? 12.178  19.340  28.612  1.00 53.87  ? 89  GLU B CA  1 
ATOM   3878 C C   . GLU B 1 60  ? 12.446  17.984  27.942  1.00 52.44  ? 89  GLU B C   1 
ATOM   3879 O O   . GLU B 1 60  ? 11.926  16.966  28.419  1.00 53.94  ? 89  GLU B O   1 
ATOM   3880 C CB  . GLU B 1 60  ? 10.670  19.589  28.573  1.00 57.89  ? 89  GLU B CB  1 
ATOM   3881 C CG  . GLU B 1 60  ? 10.242  20.925  29.179  1.00 69.55  ? 89  GLU B CG  1 
ATOM   3882 C CD  . GLU B 1 60  ? 10.386  21.063  30.688  1.00 78.36  ? 89  GLU B CD  1 
ATOM   3883 O OE1 . GLU B 1 60  ? 10.596  20.042  31.401  1.00 67.29  ? 89  GLU B OE1 1 
ATOM   3884 O OE2 . GLU B 1 60  ? 10.299  22.229  31.143  1.00 84.17  ? 89  GLU B OE2 1 
ATOM   3885 N N   . GLY B 1 61  ? 13.215  17.964  26.837  1.00 41.30  ? 90  GLY B N   1 
ATOM   3886 C CA  . GLY B 1 61  ? 13.491  16.745  26.098  1.00 37.95  ? 90  GLY B CA  1 
ATOM   3887 C C   . GLY B 1 61  ? 12.367  16.426  25.115  1.00 36.91  ? 90  GLY B C   1 
ATOM   3888 O O   . GLY B 1 61  ? 11.541  17.284  24.813  1.00 32.11  ? 90  GLY B O   1 
ATOM   3889 N N   . ILE B 1 62  ? 12.338  15.183  24.627  1.00 30.56  ? 91  ILE B N   1 
ATOM   3890 C CA  . ILE B 1 62  ? 11.437  14.829  23.551  1.00 27.19  ? 91  ILE B CA  1 
ATOM   3891 C C   . ILE B 1 62  ? 10.010  14.944  24.075  1.00 29.47  ? 91  ILE B C   1 
ATOM   3892 O O   . ILE B 1 62  ? 9.744   14.544  25.205  1.00 32.62  ? 91  ILE B O   1 
ATOM   3893 C CB  . ILE B 1 62  ? 11.765  13.416  23.007  1.00 31.01  ? 91  ILE B CB  1 
ATOM   3894 C CG1 . ILE B 1 62  ? 11.024  13.101  21.691  1.00 30.37  ? 91  ILE B CG1 1 
ATOM   3895 C CG2 . ILE B 1 62  ? 11.528  12.327  24.057  1.00 30.61  ? 91  ILE B CG2 1 
ATOM   3896 C CD1 . ILE B 1 62  ? 11.463  13.975  20.535  1.00 32.65  ? 91  ILE B CD1 1 
ATOM   3897 N N   . ARG B 1 63  ? 9.111   15.515  23.260  1.00 26.92  ? 92  ARG B N   1 
ATOM   3898 C CA  . ARG B 1 63  ? 7.679   15.436  23.520  1.00 26.59  ? 92  ARG B CA  1 
ATOM   3899 C C   . ARG B 1 63  ? 7.003   14.596  22.441  1.00 25.98  ? 92  ARG B C   1 
ATOM   3900 O O   . ARG B 1 63  ? 7.260   14.782  21.255  1.00 25.01  ? 92  ARG B O   1 
ATOM   3901 C CB  . ARG B 1 63  ? 7.005   16.816  23.558  1.00 28.13  ? 92  ARG B CB  1 
ATOM   3902 C CG  . ARG B 1 63  ? 7.356   17.597  24.820  1.00 36.99  ? 92  ARG B CG  1 
ATOM   3903 C CD  . ARG B 1 63  ? 6.836   19.048  24.802  1.00 37.86  ? 92  ARG B CD  1 
ATOM   3904 N NE  . ARG B 1 63  ? 7.168   19.773  26.028  1.00 41.85  ? 92  ARG B NE  1 
ATOM   3905 C CZ  . ARG B 1 63  ? 6.580   19.667  27.222  1.00 45.44  ? 92  ARG B CZ  1 
ATOM   3906 N NH1 . ARG B 1 63  ? 5.480   18.946  27.418  1.00 47.03  ? 92  ARG B NH1 1 
ATOM   3907 N NH2 . ARG B 1 63  ? 7.120   20.303  28.236  1.00 44.33  ? 92  ARG B NH2 1 
ATOM   3908 N N   . PHE B 1 64  ? 6.095   13.727  22.879  1.00 26.23  ? 93  PHE B N   1 
ATOM   3909 C CA  . PHE B 1 64  ? 5.318   12.857  22.015  1.00 27.51  ? 93  PHE B CA  1 
ATOM   3910 C C   . PHE B 1 64  ? 3.928   13.467  21.908  1.00 26.56  ? 93  PHE B C   1 
ATOM   3911 O O   . PHE B 1 64  ? 3.211   13.474  22.887  1.00 28.27  ? 93  PHE B O   1 
ATOM   3912 C CB  . PHE B 1 64  ? 5.229   11.437  22.605  1.00 26.80  ? 93  PHE B CB  1 
ATOM   3913 C CG  . PHE B 1 64  ? 6.554   10.716  22.838  1.00 29.33  ? 93  PHE B CG  1 
ATOM   3914 C CD1 . PHE B 1 64  ? 7.565   10.725  21.881  1.00 29.99  ? 93  PHE B CD1 1 
ATOM   3915 C CD2 . PHE B 1 64  ? 6.781   10.015  24.016  1.00 29.18  ? 93  PHE B CD2 1 
ATOM   3916 C CE1 . PHE B 1 64  ? 8.765   10.052  22.094  1.00 27.92  ? 93  PHE B CE1 1 
ATOM   3917 C CE2 . PHE B 1 64  ? 7.977   9.333   24.212  1.00 31.95  ? 93  PHE B CE2 1 
ATOM   3918 C CZ  . PHE B 1 64  ? 8.976   9.368   23.274  1.00 25.31  ? 93  PHE B CZ  1 
ATOM   3919 N N   . ARG B 1 65  ? 3.565   13.993  20.727  1.00 25.55  ? 94  ARG B N   1 
ATOM   3920 C CA  . ARG B 1 65  ? 2.309   14.707  20.568  1.00 24.10  ? 94  ARG B CA  1 
ATOM   3921 C C   . ARG B 1 65  ? 2.071   15.636  21.754  1.00 28.75  ? 94  ARG B C   1 
ATOM   3922 O O   . ARG B 1 65  ? 0.950   15.702  22.247  1.00 28.05  ? 94  ARG B O   1 
ATOM   3923 C CB  . ARG B 1 65  ? 1.100   13.790  20.355  1.00 24.91  ? 94  ARG B CB  1 
ATOM   3924 C CG  . ARG B 1 65  ? 1.136   12.982  19.068  1.00 25.88  ? 94  ARG B CG  1 
ATOM   3925 C CD  . ARG B 1 65  ? 0.920   13.828  17.794  1.00 27.77  ? 94  ARG B CD  1 
ATOM   3926 N NE  . ARG B 1 65  ? 0.690   12.921  16.661  1.00 26.85  ? 94  ARG B NE  1 
ATOM   3927 C CZ  . ARG B 1 65  ? 0.253   13.262  15.447  1.00 28.95  ? 94  ARG B CZ  1 
ATOM   3928 N NH1 . ARG B 1 65  ? 0.004   14.529  15.163  1.00 26.91  ? 94  ARG B NH1 1 
ATOM   3929 N NH2 . ARG B 1 65  ? 0.062   12.327  14.512  1.00 29.81  ? 94  ARG B NH2 1 
ATOM   3930 N N   . GLY B 1 66  ? 3.126   16.369  22.160  1.00 29.63  ? 95  GLY B N   1 
ATOM   3931 C CA  . GLY B 1 66  ? 3.037   17.425  23.161  1.00 29.31  ? 95  GLY B CA  1 
ATOM   3932 C C   . GLY B 1 66  ? 3.318   16.945  24.590  1.00 33.88  ? 95  GLY B C   1 
ATOM   3933 O O   . GLY B 1 66  ? 3.518   17.803  25.464  1.00 32.03  ? 95  GLY B O   1 
ATOM   3934 N N   . PHE B 1 67  ? 3.360   15.613  24.821  1.00 26.48  ? 96  PHE B N   1 
ATOM   3935 C CA  . PHE B 1 67  ? 3.544   15.066  26.166  1.00 27.59  ? 96  PHE B CA  1 
ATOM   3936 C C   . PHE B 1 67  ? 5.005   14.711  26.403  1.00 29.54  ? 96  PHE B C   1 
ATOM   3937 O O   . PHE B 1 67  ? 5.654   14.062  25.579  1.00 27.98  ? 96  PHE B O   1 
ATOM   3938 C CB  . PHE B 1 67  ? 2.660   13.858  26.452  1.00 28.38  ? 96  PHE B CB  1 
ATOM   3939 C CG  . PHE B 1 67  ? 1.172   14.181  26.421  1.00 31.97  ? 96  PHE B CG  1 
ATOM   3940 C CD1 . PHE B 1 67  ? 0.465   14.197  25.228  1.00 33.70  ? 96  PHE B CD1 1 
ATOM   3941 C CD2 . PHE B 1 67  ? 0.492   14.493  27.582  1.00 35.15  ? 96  PHE B CD2 1 
ATOM   3942 C CE1 . PHE B 1 67  ? -0.891  14.456  25.200  1.00 34.43  ? 96  PHE B CE1 1 
ATOM   3943 C CE2 . PHE B 1 67  ? -0.867  14.760  27.549  1.00 38.53  ? 96  PHE B CE2 1 
ATOM   3944 C CZ  . PHE B 1 67  ? -1.553  14.748  26.358  1.00 40.57  ? 96  PHE B CZ  1 
ATOM   3945 N N   . SER B 1 68  ? 5.551   15.179  27.522  1.00 27.21  ? 97  SER B N   1 
ATOM   3946 C CA  . SER B 1 68  ? 6.939   14.882  27.859  1.00 29.84  ? 97  SER B CA  1 
ATOM   3947 C C   . SER B 1 68  ? 7.015   13.447  28.366  1.00 24.08  ? 97  SER B C   1 
ATOM   3948 O O   . SER B 1 68  ? 6.002   12.833  28.648  1.00 28.29  ? 97  SER B O   1 
ATOM   3949 C CB  . SER B 1 68  ? 7.477   15.827  28.901  1.00 33.91  ? 97  SER B CB  1 
ATOM   3950 O OG  . SER B 1 68  ? 6.863   15.447  30.120  1.00 34.52  ? 97  SER B OG  1 
ATOM   3951 N N   . ILE B 1 69  ? 8.224   12.929  28.546  1.00 24.40  ? 98  ILE B N   1 
ATOM   3952 C CA  . ILE B 1 69  ? 8.396   11.577  29.026  1.00 28.21  ? 98  ILE B CA  1 
ATOM   3953 C C   . ILE B 1 69  ? 7.759   11.434  30.413  1.00 27.07  ? 98  ILE B C   1 
ATOM   3954 O O   . ILE B 1 69  ? 6.970   10.510  30.637  1.00 27.52  ? 98  ILE B O   1 
ATOM   3955 C CB  . ILE B 1 69  ? 9.886   11.177  29.022  1.00 31.26  ? 98  ILE B CB  1 
ATOM   3956 C CG1 . ILE B 1 69  ? 10.458  11.099  27.597  1.00 33.42  ? 98  ILE B CG1 1 
ATOM   3957 C CG2 . ILE B 1 69  ? 10.088  9.871   29.793  1.00 32.42  ? 98  ILE B CG2 1 
ATOM   3958 C CD1 . ILE B 1 69  ? 9.981   9.916   26.829  1.00 34.50  ? 98  ILE B CD1 1 
ATOM   3959 N N   . PRO B 1 70  ? 8.110   12.303  31.382  1.00 29.52  ? 99  PRO B N   1 
ATOM   3960 C CA  . PRO B 1 70  ? 7.466   12.250  32.705  1.00 33.46  ? 99  PRO B CA  1 
ATOM   3961 C C   . PRO B 1 70  ? 5.946   12.214  32.638  1.00 31.36  ? 99  PRO B C   1 
ATOM   3962 O O   . PRO B 1 70  ? 5.326   11.470  33.382  1.00 32.98  ? 99  PRO B O   1 
ATOM   3963 C CB  . PRO B 1 70  ? 8.032   13.502  33.401  1.00 32.77  ? 99  PRO B CB  1 
ATOM   3964 C CG  . PRO B 1 70  ? 9.427   13.553  32.836  1.00 31.88  ? 99  PRO B CG  1 
ATOM   3965 C CD  . PRO B 1 70  ? 9.217   13.297  31.325  1.00 30.34  ? 99  PRO B CD  1 
ATOM   3966 N N   . GLU B 1 71  ? 5.349   12.959  31.696  1.00 32.21  ? 100 GLU B N   1 
ATOM   3967 C CA  . GLU B 1 71  ? 3.901   13.004  31.552  1.00 33.07  ? 100 GLU B CA  1 
ATOM   3968 C C   . GLU B 1 71  ? 3.373   11.692  30.973  1.00 32.30  ? 100 GLU B C   1 
ATOM   3969 O O   . GLU B 1 71  ? 2.311   11.221  31.393  1.00 34.46  ? 100 GLU B O   1 
ATOM   3970 C CB  . GLU B 1 71  ? 3.491   14.174  30.658  1.00 38.01  ? 100 GLU B CB  1 
ATOM   3971 C CG  . GLU B 1 71  ? 3.596   15.513  31.386  1.00 40.13  ? 100 GLU B CG  1 
ATOM   3972 C CD  . GLU B 1 71  ? 3.567   16.751  30.503  1.00 45.68  ? 100 GLU B CD  1 
ATOM   3973 O OE1 . GLU B 1 71  ? 3.394   17.866  31.056  1.00 55.45  ? 100 GLU B OE1 1 
ATOM   3974 O OE2 . GLU B 1 71  ? 3.775   16.622  29.277  1.00 42.10  ? 100 GLU B OE2 1 
ATOM   3975 N N   . CYS B 1 72  ? 4.109   11.090  30.007  1.00 29.49  ? 101 CYS B N   1 
ATOM   3976 C CA  . CYS B 1 72  ? 3.725   9.767   29.510  1.00 28.70  ? 101 CYS B CA  1 
ATOM   3977 C C   . CYS B 1 72  ? 3.798   8.699   30.604  1.00 30.07  ? 101 CYS B C   1 
ATOM   3978 O O   . CYS B 1 72  ? 2.931   7.835   30.684  1.00 30.96  ? 101 CYS B O   1 
ATOM   3979 C CB  . CYS B 1 72  ? 4.559   9.344   28.305  1.00 31.06  ? 101 CYS B CB  1 
ATOM   3980 S SG  . CYS B 1 72  ? 4.230   10.413  26.880  1.00 33.20  ? 101 CYS B SG  1 
ATOM   3981 N N   . GLN B 1 73  ? 4.844   8.730   31.432  1.00 31.05  ? 102 GLN B N   1 
ATOM   3982 C CA  . GLN B 1 73  ? 4.936   7.841   32.585  1.00 35.19  ? 102 GLN B CA  1 
ATOM   3983 C C   . GLN B 1 73  ? 3.718   7.976   33.501  1.00 35.30  ? 102 GLN B C   1 
ATOM   3984 O O   . GLN B 1 73  ? 3.192   6.980   33.952  1.00 36.61  ? 102 GLN B O   1 
ATOM   3985 C CB  . GLN B 1 73  ? 6.209   8.093   33.391  1.00 35.35  ? 102 GLN B CB  1 
ATOM   3986 C CG  . GLN B 1 73  ? 7.463   7.574   32.707  1.00 39.90  ? 102 GLN B CG  1 
ATOM   3987 C CD  . GLN B 1 73  ? 8.724   7.972   33.442  1.00 47.74  ? 102 GLN B CD  1 
ATOM   3988 O OE1 . GLN B 1 73  ? 9.213   9.101   33.333  1.00 50.32  ? 102 GLN B OE1 1 
ATOM   3989 N NE2 . GLN B 1 73  ? 9.254   7.046   34.219  1.00 53.32  ? 102 GLN B NE2 1 
ATOM   3990 N N   . LYS B 1 74  ? 3.249   9.198   33.772  1.00 37.05  ? 103 LYS B N   1 
ATOM   3991 C CA  . LYS B 1 74  ? 2.070   9.359   34.611  1.00 36.40  ? 103 LYS B CA  1 
ATOM   3992 C C   . LYS B 1 74  ? 0.799   8.861   33.921  1.00 33.99  ? 103 LYS B C   1 
ATOM   3993 O O   . LYS B 1 74  ? -0.028  8.205   34.551  1.00 34.29  ? 103 LYS B O   1 
ATOM   3994 C CB  . LYS B 1 74  ? 1.810   10.813  35.027  1.00 40.51  ? 103 LYS B CB  1 
ATOM   3995 C CG  . LYS B 1 74  ? 2.772   11.337  36.078  1.00 51.97  ? 103 LYS B CG  1 
ATOM   3996 C CD  . LYS B 1 74  ? 2.362   12.667  36.710  1.00 52.96  ? 103 LYS B CD  1 
ATOM   3997 C CE  . LYS B 1 74  ? 3.383   13.115  37.725  1.00 56.31  ? 103 LYS B CE  1 
ATOM   3998 N NZ  . LYS B 1 74  ? 4.703   13.337  37.129  1.00 53.66  ? 103 LYS B NZ  1 
ATOM   3999 N N   . LEU B 1 75  ? 0.608   9.210   32.644  1.00 29.88  ? 104 LEU B N   1 
ATOM   4000 C CA  . LEU B 1 75  ? -0.717  9.177   32.031  1.00 30.35  ? 104 LEU B CA  1 
ATOM   4001 C C   . LEU B 1 75  ? -0.989  7.908   31.229  1.00 29.51  ? 104 LEU B C   1 
ATOM   4002 O O   . LEU B 1 75  ? -2.150  7.482   31.153  1.00 29.98  ? 104 LEU B O   1 
ATOM   4003 C CB  . LEU B 1 75  ? -0.841  10.389  31.109  1.00 38.45  ? 104 LEU B CB  1 
ATOM   4004 C CG  . LEU B 1 75  ? -0.943  11.752  31.801  1.00 41.30  ? 104 LEU B CG  1 
ATOM   4005 C CD1 . LEU B 1 75  ? -0.707  12.904  30.826  1.00 38.99  ? 104 LEU B CD1 1 
ATOM   4006 C CD2 . LEU B 1 75  ? -2.316  11.849  32.459  1.00 48.02  ? 104 LEU B CD2 1 
ATOM   4007 N N   . LEU B 1 76  ? 0.029   7.367   30.532  1.00 27.33  ? 105 LEU B N   1 
ATOM   4008 C CA  . LEU B 1 76  ? -0.194  6.209   29.677  1.00 29.05  ? 105 LEU B CA  1 
ATOM   4009 C C   . LEU B 1 76  ? -0.614  5.015   30.542  1.00 31.70  ? 105 LEU B C   1 
ATOM   4010 O O   . LEU B 1 76  ? -0.164  4.898   31.677  1.00 33.02  ? 105 LEU B O   1 
ATOM   4011 C CB  . LEU B 1 76  ? 1.044   5.904   28.840  1.00 28.13  ? 105 LEU B CB  1 
ATOM   4012 C CG  . LEU B 1 76  ? 1.372   6.890   27.716  1.00 30.27  ? 105 LEU B CG  1 
ATOM   4013 C CD1 . LEU B 1 76  ? 2.680   6.481   27.053  1.00 32.73  ? 105 LEU B CD1 1 
ATOM   4014 C CD2 . LEU B 1 76  ? 0.281   6.939   26.648  1.00 25.15  ? 105 LEU B CD2 1 
ATOM   4015 N N   . PRO B 1 77  ? -1.546  4.154   30.064  1.00 32.56  ? 106 PRO B N   1 
ATOM   4016 C CA  . PRO B 1 77  ? -1.846  2.887   30.728  1.00 32.64  ? 106 PRO B CA  1 
ATOM   4017 C C   . PRO B 1 77  ? -0.627  2.019   31.003  1.00 34.20  ? 106 PRO B C   1 
ATOM   4018 O O   . PRO B 1 77  ? 0.261   1.905   30.158  1.00 31.33  ? 106 PRO B O   1 
ATOM   4019 C CB  . PRO B 1 77  ? -2.815  2.224   29.755  1.00 35.22  ? 106 PRO B CB  1 
ATOM   4020 C CG  . PRO B 1 77  ? -3.558  3.410   29.173  1.00 32.77  ? 106 PRO B CG  1 
ATOM   4021 C CD  . PRO B 1 77  ? -2.475  4.442   28.956  1.00 30.45  ? 106 PRO B CD  1 
ATOM   4022 N N   . LYS B 1 78  ? -0.666  1.353   32.165  1.00 30.29  ? 107 LYS B N   1 
ATOM   4023 C CA  . LYS B 1 78  ? 0.340   0.394   32.589  1.00 30.82  ? 107 LYS B CA  1 
ATOM   4024 C C   . LYS B 1 78  ? -0.270  -0.990  32.435  1.00 28.54  ? 107 LYS B C   1 
ATOM   4025 O O   . LYS B 1 78  ? -1.475  -1.111  32.236  1.00 34.22  ? 107 LYS B O   1 
ATOM   4026 C CB  . LYS B 1 78  ? 0.714   0.762   34.031  1.00 35.32  ? 107 LYS B CB  1 
ATOM   4027 C CG  . LYS B 1 78  ? 1.319   2.164   34.125  1.00 40.07  ? 107 LYS B CG  1 
ATOM   4028 C CD  . LYS B 1 78  ? 1.055   2.888   35.437  1.00 56.00  ? 107 LYS B CD  1 
ATOM   4029 C CE  . LYS B 1 78  ? 1.871   4.152   35.612  1.00 55.97  ? 107 LYS B CE  1 
ATOM   4030 N NZ  . LYS B 1 78  ? 1.746   5.024   34.441  1.00 54.70  ? 107 LYS B NZ  1 
ATOM   4031 N N   . ALA B 1 79  ? 0.560   -2.034  32.421  1.00 30.97  ? 108 ALA B N   1 
ATOM   4032 C CA  . ALA B 1 79  ? 0.049   -3.377  32.586  1.00 31.47  ? 108 ALA B CA  1 
ATOM   4033 C C   . ALA B 1 79  ? -0.519  -3.444  34.005  1.00 40.10  ? 108 ALA B C   1 
ATOM   4034 O O   . ALA B 1 79  ? -0.073  -2.725  34.907  1.00 32.73  ? 108 ALA B O   1 
ATOM   4035 C CB  . ALA B 1 79  ? 1.110   -4.432  32.411  1.00 33.70  ? 108 ALA B CB  1 
ATOM   4036 N N   . LYS B 1 80  ? -1.521  -4.292  34.176  1.00 43.14  ? 109 LYS B N   1 
ATOM   4037 C CA  . LYS B 1 80  ? -2.123  -4.471  35.480  1.00 54.24  ? 109 LYS B CA  1 
ATOM   4038 C C   . LYS B 1 80  ? -1.051  -5.126  36.359  1.00 54.02  ? 109 LYS B C   1 
ATOM   4039 O O   . LYS B 1 80  ? -0.407  -6.113  35.984  1.00 51.04  ? 109 LYS B O   1 
ATOM   4040 C CB  . LYS B 1 80  ? -3.526  -5.012  35.171  1.00 66.10  ? 109 LYS B CB  1 
ATOM   4041 C CG  . LYS B 1 80  ? -3.930  -6.197  35.963  1.00 85.79  ? 109 LYS B CG  1 
ATOM   4042 C CD  . LYS B 1 80  ? -3.312  -7.494  35.448  1.00 101.11 ? 109 LYS B CD  1 
ATOM   4043 C CE  . LYS B 1 80  ? -2.765  -8.370  36.542  1.00 117.31 ? 109 LYS B CE  1 
ATOM   4044 N NZ  . LYS B 1 80  ? -3.112  -7.903  37.890  1.00 122.49 ? 109 LYS B NZ  1 
ATOM   4045 N N   . GLY B 1 81  ? -0.752  -4.452  37.469  1.00 53.03  ? 110 GLY B N   1 
ATOM   4046 C CA  . GLY B 1 81  ? 0.324   -4.845  38.359  1.00 63.44  ? 110 GLY B CA  1 
ATOM   4047 C C   . GLY B 1 81  ? 1.626   -4.102  38.063  1.00 64.42  ? 110 GLY B C   1 
ATOM   4048 O O   . GLY B 1 81  ? 2.634   -4.327  38.740  1.00 53.86  ? 110 GLY B O   1 
ATOM   4049 N N   . GLY B 1 82  ? 1.586   -3.208  37.063  1.00 57.92  ? 111 GLY B N   1 
ATOM   4050 C CA  . GLY B 1 82  ? 2.800   -2.681  36.457  1.00 49.04  ? 111 GLY B CA  1 
ATOM   4051 C C   . GLY B 1 82  ? 2.976   -1.217  36.826  1.00 41.48  ? 111 GLY B C   1 
ATOM   4052 O O   . GLY B 1 82  ? 2.039   -0.598  37.308  1.00 38.23  ? 111 GLY B O   1 
ATOM   4053 N N   . GLU B 1 83  ? 4.200   -0.706  36.660  1.00 36.19  ? 112 GLU B N   1 
ATOM   4054 C CA  . GLU B 1 83  ? 4.497   0.701   36.868  1.00 38.34  ? 112 GLU B CA  1 
ATOM   4055 C C   . GLU B 1 83  ? 4.914   1.384   35.561  1.00 33.99  ? 112 GLU B C   1 
ATOM   4056 O O   . GLU B 1 83  ? 5.060   2.594   35.523  1.00 35.94  ? 112 GLU B O   1 
ATOM   4057 C CB  . GLU B 1 83  ? 5.696   0.918   37.794  1.00 42.50  ? 112 GLU B CB  1 
ATOM   4058 C CG  . GLU B 1 83  ? 5.613   0.194   39.137  1.00 53.74  ? 112 GLU B CG  1 
ATOM   4059 C CD  . GLU B 1 83  ? 6.680   0.661   40.126  1.00 61.05  ? 112 GLU B CD  1 
ATOM   4060 O OE1 . GLU B 1 83  ? 6.278   1.151   41.201  1.00 73.93  ? 112 GLU B OE1 1 
ATOM   4061 O OE2 . GLU B 1 83  ? 7.899   0.586   39.831  1.00 65.25  ? 112 GLU B OE2 1 
ATOM   4062 N N   . GLU B 1 84  ? 5.214   0.626   34.514  1.00 30.78  ? 113 GLU B N   1 
ATOM   4063 C CA  . GLU B 1 84  ? 5.836   1.234   33.345  1.00 33.98  ? 113 GLU B CA  1 
ATOM   4064 C C   . GLU B 1 84  ? 4.816   1.428   32.221  1.00 28.84  ? 113 GLU B C   1 
ATOM   4065 O O   . GLU B 1 84  ? 3.989   0.556   31.993  1.00 29.03  ? 113 GLU B O   1 
ATOM   4066 C CB  . GLU B 1 84  ? 7.031   0.376   32.915  1.00 32.95  ? 113 GLU B CB  1 
ATOM   4067 C CG  . GLU B 1 84  ? 8.181   0.391   33.922  1.00 33.90  ? 113 GLU B CG  1 
ATOM   4068 C CD  . GLU B 1 84  ? 8.699   1.752   34.363  1.00 36.86  ? 113 GLU B CD  1 
ATOM   4069 O OE1 . GLU B 1 84  ? 8.442   2.788   33.716  1.00 35.69  ? 113 GLU B OE1 1 
ATOM   4070 O OE2 . GLU B 1 84  ? 9.349   1.778   35.448  1.00 43.17  ? 113 GLU B OE2 1 
ATOM   4071 N N   . PRO B 1 85  ? 4.886   2.540   31.442  1.00 31.00  ? 114 PRO B N   1 
ATOM   4072 C CA  . PRO B 1 85  ? 3.951   2.771   30.324  1.00 26.67  ? 114 PRO B CA  1 
ATOM   4073 C C   . PRO B 1 85  ? 4.061   1.689   29.254  1.00 25.06  ? 114 PRO B C   1 
ATOM   4074 O O   . PRO B 1 85  ? 5.168   1.275   28.909  1.00 27.65  ? 114 PRO B O   1 
ATOM   4075 C CB  . PRO B 1 85  ? 4.344   4.147   29.760  1.00 28.61  ? 114 PRO B CB  1 
ATOM   4076 C CG  . PRO B 1 85  ? 5.794   4.325   30.169  1.00 32.05  ? 114 PRO B CG  1 
ATOM   4077 C CD  . PRO B 1 85  ? 5.959   3.552   31.502  1.00 28.37  ? 114 PRO B CD  1 
ATOM   4078 N N   . LEU B 1 86  ? 2.905   1.199   28.800  1.00 25.05  ? 115 LEU B N   1 
ATOM   4079 C CA  . LEU B 1 86  ? 2.836   0.209   27.750  1.00 25.82  ? 115 LEU B CA  1 
ATOM   4080 C C   . LEU B 1 86  ? 3.070   0.894   26.404  1.00 26.67  ? 115 LEU B C   1 
ATOM   4081 O O   . LEU B 1 86  ? 2.420   1.887   26.128  1.00 26.51  ? 115 LEU B O   1 
ATOM   4082 C CB  . LEU B 1 86  ? 1.489   -0.492  27.739  1.00 28.18  ? 115 LEU B CB  1 
ATOM   4083 C CG  . LEU B 1 86  ? 1.137   -1.301  28.988  1.00 33.40  ? 115 LEU B CG  1 
ATOM   4084 C CD1 . LEU B 1 86  ? -0.020  -2.240  28.665  1.00 39.52  ? 115 LEU B CD1 1 
ATOM   4085 C CD2 . LEU B 1 86  ? 2.313   -2.083  29.473  1.00 34.79  ? 115 LEU B CD2 1 
ATOM   4086 N N   . PRO B 1 87  ? 4.005   0.373   25.573  1.00 23.44  ? 116 PRO B N   1 
ATOM   4087 C CA  . PRO B 1 87  ? 4.234   0.869   24.211  1.00 25.74  ? 116 PRO B CA  1 
ATOM   4088 C C   . PRO B 1 87  ? 2.997   0.970   23.323  1.00 23.95  ? 116 PRO B C   1 
ATOM   4089 O O   . PRO B 1 87  ? 2.960   1.834   22.455  1.00 23.08  ? 116 PRO B O   1 
ATOM   4090 C CB  . PRO B 1 87  ? 5.268   -0.063  23.584  1.00 25.16  ? 116 PRO B CB  1 
ATOM   4091 C CG  . PRO B 1 87  ? 5.593   -1.078  24.639  1.00 26.37  ? 116 PRO B CG  1 
ATOM   4092 C CD  . PRO B 1 87  ? 4.950   -0.664  25.945  1.00 22.26  ? 116 PRO B CD  1 
ATOM   4093 N N   . GLU B 1 88  ? 2.008   0.103   23.554  1.00 23.12  ? 117 GLU B N   1 
ATOM   4094 C CA  . GLU B 1 88  ? 0.729   0.195   22.876  1.00 23.78  ? 117 GLU B CA  1 
ATOM   4095 C C   . GLU B 1 88  ? 0.147   1.590   23.072  1.00 24.69  ? 117 GLU B C   1 
ATOM   4096 O O   . GLU B 1 88  ? -0.341  2.183   22.124  1.00 23.30  ? 117 GLU B O   1 
ATOM   4097 C CB  . GLU B 1 88  ? -0.339  -0.772  23.408  1.00 26.24  ? 117 GLU B CB  1 
ATOM   4098 C CG  . GLU B 1 88  ? -0.098  -2.237  23.055  1.00 27.26  ? 117 GLU B CG  1 
ATOM   4099 C CD  . GLU B 1 88  ? 0.755   -3.065  24.010  1.00 25.54  ? 117 GLU B CD  1 
ATOM   4100 O OE1 . GLU B 1 88  ? 1.728   -2.523  24.562  1.00 22.78  ? 117 GLU B OE1 1 
ATOM   4101 O OE2 . GLU B 1 88  ? 0.486   -4.306  24.102  1.00 27.56  ? 117 GLU B OE2 1 
ATOM   4102 N N   . GLY B 1 89  ? 0.170   2.068   24.322  1.00 26.68  ? 118 GLY B N   1 
ATOM   4103 C CA  . GLY B 1 89  ? -0.356  3.372   24.676  1.00 24.13  ? 118 GLY B CA  1 
ATOM   4104 C C   . GLY B 1 89  ? 0.353   4.487   23.928  1.00 24.28  ? 118 GLY B C   1 
ATOM   4105 O O   . GLY B 1 89  ? -0.288  5.434   23.497  1.00 23.47  ? 118 GLY B O   1 
ATOM   4106 N N   . LEU B 1 90  ? 1.685   4.398   23.889  1.00 22.80  ? 119 LEU B N   1 
ATOM   4107 C CA  . LEU B 1 90  ? 2.532   5.349   23.207  1.00 22.59  ? 119 LEU B CA  1 
ATOM   4108 C C   . LEU B 1 90  ? 2.104   5.437   21.742  1.00 22.16  ? 119 LEU B C   1 
ATOM   4109 O O   . LEU B 1 90  ? 2.018   6.528   21.177  1.00 23.26  ? 119 LEU B O   1 
ATOM   4110 C CB  . LEU B 1 90  ? 3.992   4.911   23.440  1.00 24.14  ? 119 LEU B CB  1 
ATOM   4111 C CG  . LEU B 1 90  ? 5.083   5.710   22.744  1.00 24.52  ? 119 LEU B CG  1 
ATOM   4112 C CD1 . LEU B 1 90  ? 5.153   5.416   21.253  1.00 29.11  ? 119 LEU B CD1 1 
ATOM   4113 C CD2 . LEU B 1 90  ? 4.864   7.196   22.937  1.00 29.18  ? 119 LEU B CD2 1 
ATOM   4114 N N   . PHE B 1 91  ? 1.887   4.288   21.111  1.00 20.72  ? 120 PHE B N   1 
ATOM   4115 C CA  . PHE B 1 91  ? 1.570   4.267   19.708  1.00 20.29  ? 120 PHE B CA  1 
ATOM   4116 C C   . PHE B 1 91  ? 0.220   4.929   19.457  1.00 23.39  ? 120 PHE B C   1 
ATOM   4117 O O   . PHE B 1 91  ? 0.071   5.661   18.464  1.00 20.30  ? 120 PHE B O   1 
ATOM   4118 C CB  . PHE B 1 91  ? 1.604   2.840   19.160  1.00 20.51  ? 120 PHE B CB  1 
ATOM   4119 C CG  . PHE B 1 91  ? 1.227   2.739   17.691  1.00 17.40  ? 120 PHE B CG  1 
ATOM   4120 C CD1 . PHE B 1 91  ? 2.151   3.054   16.715  1.00 18.62  ? 120 PHE B CD1 1 
ATOM   4121 C CD2 . PHE B 1 91  ? -0.028  2.287   17.289  1.00 17.99  ? 120 PHE B CD2 1 
ATOM   4122 C CE1 . PHE B 1 91  ? 1.816   2.950   15.373  1.00 19.80  ? 120 PHE B CE1 1 
ATOM   4123 C CE2 . PHE B 1 91  ? -0.349  2.173   15.951  1.00 20.24  ? 120 PHE B CE2 1 
ATOM   4124 C CZ  . PHE B 1 91  ? 0.557   2.546   15.000  1.00 20.17  ? 120 PHE B CZ  1 
ATOM   4125 N N   . TRP B 1 92  ? -0.746  4.626   20.331  1.00 20.74  ? 121 TRP B N   1 
ATOM   4126 C CA  . TRP B 1 92  ? -2.084  5.189   20.252  1.00 21.51  ? 121 TRP B CA  1 
ATOM   4127 C C   . TRP B 1 92  ? -1.939  6.697   20.344  1.00 20.14  ? 121 TRP B C   1 
ATOM   4128 O O   . TRP B 1 92  ? -2.551  7.402   19.556  1.00 22.48  ? 121 TRP B O   1 
ATOM   4129 C CB  . TRP B 1 92  ? -2.970  4.659   21.389  1.00 20.61  ? 121 TRP B CB  1 
ATOM   4130 C CG  . TRP B 1 92  ? -4.409  5.112   21.296  1.00 21.30  ? 121 TRP B CG  1 
ATOM   4131 C CD1 . TRP B 1 92  ? -4.923  6.329   21.613  1.00 22.62  ? 121 TRP B CD1 1 
ATOM   4132 C CD2 . TRP B 1 92  ? -5.525  4.316   20.876  1.00 21.72  ? 121 TRP B CD2 1 
ATOM   4133 N NE1 . TRP B 1 92  ? -6.271  6.375   21.347  1.00 21.49  ? 121 TRP B NE1 1 
ATOM   4134 C CE2 . TRP B 1 92  ? -6.675  5.144   20.937  1.00 21.98  ? 121 TRP B CE2 1 
ATOM   4135 C CE3 . TRP B 1 92  ? -5.677  2.990   20.484  1.00 23.50  ? 121 TRP B CE3 1 
ATOM   4136 C CZ2 . TRP B 1 92  ? -7.940  4.691   20.568  1.00 23.91  ? 121 TRP B CZ2 1 
ATOM   4137 C CZ3 . TRP B 1 92  ? -6.940  2.521   20.172  1.00 24.12  ? 121 TRP B CZ3 1 
ATOM   4138 C CH2 . TRP B 1 92  ? -8.048  3.378   20.178  1.00 23.70  ? 121 TRP B CH2 1 
ATOM   4139 N N   . LEU B 1 93  ? -1.070  7.156   21.262  1.00 19.06  ? 122 LEU B N   1 
ATOM   4140 C CA  . LEU B 1 93  ? -0.839  8.577   21.437  1.00 19.73  ? 122 LEU B CA  1 
ATOM   4141 C C   . LEU B 1 93  ? -0.269  9.193   20.149  1.00 21.61  ? 122 LEU B C   1 
ATOM   4142 O O   . LEU B 1 93  ? -0.628  10.324  19.764  1.00 20.62  ? 122 LEU B O   1 
ATOM   4143 C CB  . LEU B 1 93  ? 0.035   8.879   22.647  1.00 21.26  ? 122 LEU B CB  1 
ATOM   4144 C CG  . LEU B 1 93  ? 0.531   10.312  22.805  1.00 23.59  ? 122 LEU B CG  1 
ATOM   4145 C CD1 . LEU B 1 93  ? -0.574  11.363  22.914  1.00 24.97  ? 122 LEU B CD1 1 
ATOM   4146 C CD2 . LEU B 1 93  ? 1.395   10.340  24.013  1.00 27.37  ? 122 LEU B CD2 1 
ATOM   4147 N N   . LEU B 1 94  ? 0.715   8.519   19.562  1.00 23.35  ? 123 LEU B N   1 
ATOM   4148 C CA  . LEU B 1 94  ? 1.387   9.090   18.403  1.00 22.18  ? 123 LEU B CA  1 
ATOM   4149 C C   . LEU B 1 94  ? 0.392   9.168   17.251  1.00 21.22  ? 123 LEU B C   1 
ATOM   4150 O O   . LEU B 1 94  ? 0.405   10.132  16.506  1.00 23.03  ? 123 LEU B O   1 
ATOM   4151 C CB  . LEU B 1 94  ? 2.628   8.268   18.025  1.00 21.38  ? 123 LEU B CB  1 
ATOM   4152 C CG  . LEU B 1 94  ? 3.776   8.313   19.041  1.00 21.84  ? 123 LEU B CG  1 
ATOM   4153 C CD1 . LEU B 1 94  ? 5.026   7.654   18.486  1.00 24.02  ? 123 LEU B CD1 1 
ATOM   4154 C CD2 . LEU B 1 94  ? 4.096   9.706   19.475  1.00 24.69  ? 123 LEU B CD2 1 
ATOM   4155 N N   . VAL B 1 95  ? -0.460  8.164   17.110  1.00 21.02  ? 124 VAL B N   1 
ATOM   4156 C CA  . VAL B 1 95  ? -1.410  8.122   16.004  1.00 26.65  ? 124 VAL B CA  1 
ATOM   4157 C C   . VAL B 1 95  ? -2.531  9.156   16.167  1.00 24.56  ? 124 VAL B C   1 
ATOM   4158 O O   . VAL B 1 95  ? -2.963  9.775   15.177  1.00 22.66  ? 124 VAL B O   1 
ATOM   4159 C CB  . VAL B 1 95  ? -2.049  6.727   15.843  1.00 26.43  ? 124 VAL B CB  1 
ATOM   4160 C CG1 . VAL B 1 95  ? -3.175  6.764   14.810  1.00 26.66  ? 124 VAL B CG1 1 
ATOM   4161 C CG2 . VAL B 1 95  ? -1.035  5.693   15.436  1.00 29.43  ? 124 VAL B CG2 1 
ATOM   4162 N N   . THR B 1 96  ? -3.054  9.307   17.401  1.00 25.82  ? 125 THR B N   1 
ATOM   4163 C CA  . THR B 1 96  ? -4.307  10.030  17.585  1.00 24.00  ? 125 THR B CA  1 
ATOM   4164 C C   . THR B 1 96  ? -4.073  11.416  18.179  1.00 26.67  ? 125 THR B C   1 
ATOM   4165 O O   . THR B 1 96  ? -4.940  12.274  18.080  1.00 24.56  ? 125 THR B O   1 
ATOM   4166 C CB  . THR B 1 96  ? -5.281  9.268   18.482  1.00 23.57  ? 125 THR B CB  1 
ATOM   4167 O OG1 . THR B 1 96  ? -4.751  9.294   19.811  1.00 22.45  ? 125 THR B OG1 1 
ATOM   4168 C CG2 . THR B 1 96  ? -5.623  7.900   17.922  1.00 24.27  ? 125 THR B CG2 1 
ATOM   4169 N N   . GLY B 1 97  ? -2.964  11.597  18.887  1.00 27.49  ? 126 GLY B N   1 
ATOM   4170 C CA  . GLY B 1 97  ? -2.724  12.830  19.622  1.00 26.30  ? 126 GLY B CA  1 
ATOM   4171 C C   . GLY B 1 97  ? -3.390  12.799  20.989  1.00 25.18  ? 126 GLY B C   1 
ATOM   4172 O O   . GLY B 1 97  ? -3.268  13.769  21.730  1.00 25.88  ? 126 GLY B O   1 
ATOM   4173 N N   . HIS B 1 98  ? -4.006  11.664  21.329  1.00 25.74  ? 127 HIS B N   1 
ATOM   4174 C CA  . HIS B 1 98  ? -4.767  11.536  22.565  1.00 29.26  ? 127 HIS B CA  1 
ATOM   4175 C C   . HIS B 1 98  ? -4.147  10.429  23.430  1.00 27.74  ? 127 HIS B C   1 
ATOM   4176 O O   . HIS B 1 98  ? -3.739  9.403   22.901  1.00 26.46  ? 127 HIS B O   1 
ATOM   4177 C CB  . HIS B 1 98  ? -6.235  11.166  22.275  1.00 30.73  ? 127 HIS B CB  1 
ATOM   4178 C CG  . HIS B 1 98  ? -7.040  12.247  21.644  1.00 42.84  ? 127 HIS B CG  1 
ATOM   4179 N ND1 . HIS B 1 98  ? -7.583  13.281  22.376  1.00 49.48  ? 127 HIS B ND1 1 
ATOM   4180 C CD2 . HIS B 1 98  ? -7.407  12.456  20.370  1.00 48.46  ? 127 HIS B CD2 1 
ATOM   4181 C CE1 . HIS B 1 98  ? -8.244  14.095  21.558  1.00 53.14  ? 127 HIS B CE1 1 
ATOM   4182 N NE2 . HIS B 1 98  ? -8.154  13.612  20.334  1.00 52.67  ? 127 HIS B NE2 1 
ATOM   4183 N N   . ILE B 1 99  ? -4.134  10.621  24.747  1.00 27.31  ? 128 ILE B N   1 
ATOM   4184 C CA  . ILE B 1 99  ? -3.838  9.566   25.711  1.00 29.04  ? 128 ILE B CA  1 
ATOM   4185 C C   . ILE B 1 99  ? -4.943  8.542   25.619  1.00 27.60  ? 128 ILE B C   1 
ATOM   4186 O O   . ILE B 1 99  ? -6.119  8.898   25.769  1.00 27.99  ? 128 ILE B O   1 
ATOM   4187 C CB  . ILE B 1 99  ? -3.751  10.096  27.158  1.00 29.22  ? 128 ILE B CB  1 
ATOM   4188 C CG1 . ILE B 1 99  ? -2.679  11.158  27.307  1.00 27.66  ? 128 ILE B CG1 1 
ATOM   4189 C CG2 . ILE B 1 99  ? -3.526  8.942   28.146  1.00 30.44  ? 128 ILE B CG2 1 
ATOM   4190 C CD1 . ILE B 1 99  ? -1.278  10.686  27.003  1.00 28.90  ? 128 ILE B CD1 1 
ATOM   4191 N N   . PRO B 1 100 ? -4.641  7.247   25.372  1.00 25.09  ? 129 PRO B N   1 
ATOM   4192 C CA  . PRO B 1 100 ? -5.692  6.224   25.333  1.00 23.68  ? 129 PRO B CA  1 
ATOM   4193 C C   . PRO B 1 100 ? -6.225  5.887   26.728  1.00 27.79  ? 129 PRO B C   1 
ATOM   4194 O O   . PRO B 1 100 ? -5.526  6.100   27.721  1.00 26.54  ? 129 PRO B O   1 
ATOM   4195 C CB  . PRO B 1 100 ? -4.935  5.014   24.762  1.00 25.69  ? 129 PRO B CB  1 
ATOM   4196 C CG  . PRO B 1 100 ? -3.583  5.197   25.315  1.00 24.63  ? 129 PRO B CG  1 
ATOM   4197 C CD  . PRO B 1 100 ? -3.296  6.675   25.189  1.00 23.69  ? 129 PRO B CD  1 
ATOM   4198 N N   . THR B 1 101 ? -7.433  5.313   26.762  1.00 31.24  ? 130 THR B N   1 
ATOM   4199 C CA  . THR B 1 101 ? -7.970  4.696   27.964  1.00 37.63  ? 130 THR B CA  1 
ATOM   4200 C C   . THR B 1 101 ? -7.333  3.326   28.100  1.00 37.81  ? 130 THR B C   1 
ATOM   4201 O O   . THR B 1 101 ? -6.829  2.794   27.119  1.00 37.35  ? 130 THR B O   1 
ATOM   4202 C CB  . THR B 1 101 ? -9.489  4.515   27.858  1.00 36.52  ? 130 THR B CB  1 
ATOM   4203 O OG1 . THR B 1 101 ? -9.728  3.592   26.797  1.00 34.63  ? 130 THR B OG1 1 
ATOM   4204 C CG2 . THR B 1 101 ? -10.230 5.806   27.569  1.00 40.67  ? 130 THR B CG2 1 
ATOM   4205 N N   . GLU B 1 102 ? -7.524  2.700   29.267  1.00 37.66  ? 131 GLU B N   1 
ATOM   4206 C CA  . GLU B 1 102 ? -7.104  1.325   29.480  1.00 37.61  ? 131 GLU B CA  1 
ATOM   4207 C C   . GLU B 1 102 ? -7.708  0.374   28.450  1.00 34.06  ? 131 GLU B C   1 
ATOM   4208 O O   . GLU B 1 102 ? -7.002  -0.476  27.943  1.00 32.43  ? 131 GLU B O   1 
ATOM   4209 C CB  . GLU B 1 102 ? -7.464  0.876   30.899  1.00 42.62  ? 131 GLU B CB  1 
ATOM   4210 C CG  . GLU B 1 102 ? -6.847  1.777   31.964  1.00 53.57  ? 131 GLU B CG  1 
ATOM   4211 C CD  . GLU B 1 102 ? -5.575  1.284   32.634  1.00 65.37  ? 131 GLU B CD  1 
ATOM   4212 O OE1 . GLU B 1 102 ? -4.802  0.497   32.046  1.00 79.22  ? 131 GLU B OE1 1 
ATOM   4213 O OE2 . GLU B 1 102 ? -5.390  1.678   33.803  1.00 70.50  ? 131 GLU B OE2 1 
ATOM   4214 N N   . GLU B 1 103 ? -9.012  0.510   28.149  1.00 33.51  ? 132 GLU B N   1 
ATOM   4215 C CA  . GLU B 1 103 ? -9.726  -0.335  27.201  1.00 35.23  ? 132 GLU B CA  1 
ATOM   4216 C C   . GLU B 1 103 ? -9.185  -0.213  25.762  1.00 31.12  ? 132 GLU B C   1 
ATOM   4217 O O   . GLU B 1 103 ? -9.138  -1.189  25.020  1.00 31.43  ? 132 GLU B O   1 
ATOM   4218 C CB  . GLU B 1 103 ? -11.225 0.014   27.243  1.00 43.94  ? 132 GLU B CB  1 
ATOM   4219 C CG  . GLU B 1 103 ? -11.921 -0.333  28.566  1.00 58.18  ? 132 GLU B CG  1 
ATOM   4220 C CD  . GLU B 1 103 ? -11.777 0.590   29.790  1.00 70.27  ? 132 GLU B CD  1 
ATOM   4221 O OE1 . GLU B 1 103 ? -10.927 1.521   29.850  1.00 66.31  ? 132 GLU B OE1 1 
ATOM   4222 O OE2 . GLU B 1 103 ? -12.578 0.373   30.732  1.00 71.81  ? 132 GLU B OE2 1 
ATOM   4223 N N   . GLN B 1 104 ? -8.790  0.983   25.345  1.00 27.94  ? 133 GLN B N   1 
ATOM   4224 C CA  . GLN B 1 104 ? -8.220  1.166   24.026  1.00 32.09  ? 133 GLN B CA  1 
ATOM   4225 C C   . GLN B 1 104 ? -6.861  0.452   23.954  1.00 27.51  ? 133 GLN B C   1 
ATOM   4226 O O   . GLN B 1 104 ? -6.593  -0.279  22.998  1.00 27.76  ? 133 GLN B O   1 
ATOM   4227 C CB  . GLN B 1 104 ? -8.124  2.667   23.759  1.00 30.47  ? 133 GLN B CB  1 
ATOM   4228 C CG  . GLN B 1 104 ? -9.469  3.322   23.487  1.00 30.04  ? 133 GLN B CG  1 
ATOM   4229 C CD  . GLN B 1 104 ? -9.430  4.829   23.538  1.00 27.70  ? 133 GLN B CD  1 
ATOM   4230 O OE1 . GLN B 1 104 ? -8.549  5.465   24.130  1.00 30.94  ? 133 GLN B OE1 1 
ATOM   4231 N NE2 . GLN B 1 104 ? -10.421 5.415   22.893  1.00 29.73  ? 133 GLN B NE2 1 
ATOM   4232 N N   . VAL B 1 105 ? -6.046  0.606   24.995  1.00 26.20  ? 134 VAL B N   1 
ATOM   4233 C CA  . VAL B 1 105 ? -4.783  -0.115  25.038  1.00 29.24  ? 134 VAL B CA  1 
ATOM   4234 C C   . VAL B 1 105 ? -5.025  -1.620  24.981  1.00 30.86  ? 134 VAL B C   1 
ATOM   4235 O O   . VAL B 1 105 ? -4.321  -2.310  24.275  1.00 25.82  ? 134 VAL B O   1 
ATOM   4236 C CB  . VAL B 1 105 ? -3.942  0.309   26.257  1.00 31.05  ? 134 VAL B CB  1 
ATOM   4237 C CG1 . VAL B 1 105 ? -2.728  -0.578  26.452  1.00 34.85  ? 134 VAL B CG1 1 
ATOM   4238 C CG2 . VAL B 1 105 ? -3.501  1.750   26.103  1.00 33.85  ? 134 VAL B CG2 1 
ATOM   4239 N N   . SER B 1 106 ? -5.998  -2.158  25.743  1.00 30.44  ? 135 SER B N   1 
ATOM   4240 C CA  A SER B 1 106 ? -6.260  -3.592  25.724  0.50 30.06  ? 135 SER B CA  1 
ATOM   4241 C CA  B SER B 1 106 ? -6.270  -3.590  25.731  0.50 29.41  ? 135 SER B CA  1 
ATOM   4242 C C   . SER B 1 106 ? -6.709  -4.042  24.339  1.00 31.33  ? 135 SER B C   1 
ATOM   4243 O O   . SER B 1 106 ? -6.346  -5.122  23.879  1.00 30.52  ? 135 SER B O   1 
ATOM   4244 C CB  A SER B 1 106 ? -7.293  -3.995  26.747  0.50 33.79  ? 135 SER B CB  1 
ATOM   4245 C CB  B SER B 1 106 ? -7.311  -3.957  26.783  0.50 32.15  ? 135 SER B CB  1 
ATOM   4246 O OG  A SER B 1 106 ? -7.587  -5.379  26.606  0.50 31.79  ? 135 SER B OG  1 
ATOM   4247 O OG  B SER B 1 106 ? -6.798  -3.803  28.103  0.50 28.57  ? 135 SER B OG  1 
ATOM   4248 N N   . TRP B 1 107 ? -7.520  -3.220  23.675  1.00 30.92  ? 136 TRP B N   1 
ATOM   4249 C CA  . TRP B 1 107 ? -7.945  -3.544  22.335  1.00 34.05  ? 136 TRP B CA  1 
ATOM   4250 C C   . TRP B 1 107 ? -6.702  -3.607  21.435  1.00 30.67  ? 136 TRP B C   1 
ATOM   4251 O O   . TRP B 1 107 ? -6.601  -4.485  20.596  1.00 31.86  ? 136 TRP B O   1 
ATOM   4252 C CB  . TRP B 1 107 ? -8.945  -2.499  21.842  1.00 32.99  ? 136 TRP B CB  1 
ATOM   4253 C CG  . TRP B 1 107 ? -9.304  -2.669  20.401  1.00 33.19  ? 136 TRP B CG  1 
ATOM   4254 C CD1 . TRP B 1 107 ? -10.345 -3.389  19.901  1.00 33.78  ? 136 TRP B CD1 1 
ATOM   4255 C CD2 . TRP B 1 107 ? -8.596  -2.127  19.264  1.00 30.94  ? 136 TRP B CD2 1 
ATOM   4256 N NE1 . TRP B 1 107 ? -10.340 -3.331  18.541  1.00 33.13  ? 136 TRP B NE1 1 
ATOM   4257 C CE2 . TRP B 1 107 ? -9.273  -2.582  18.119  1.00 33.02  ? 136 TRP B CE2 1 
ATOM   4258 C CE3 . TRP B 1 107 ? -7.462  -1.330  19.105  1.00 31.60  ? 136 TRP B CE3 1 
ATOM   4259 C CZ2 . TRP B 1 107 ? -8.862  -2.249  16.838  1.00 32.37  ? 136 TRP B CZ2 1 
ATOM   4260 C CZ3 . TRP B 1 107 ? -7.018  -1.055  17.830  1.00 32.83  ? 136 TRP B CZ3 1 
ATOM   4261 C CH2 . TRP B 1 107 ? -7.710  -1.501  16.713  1.00 32.60  ? 136 TRP B CH2 1 
ATOM   4262 N N   . LEU B 1 108 ? -5.790  -2.649  21.594  1.00 28.25  ? 137 LEU B N   1 
ATOM   4263 C CA  . LEU B 1 108 ? -4.612  -2.594  20.739  1.00 26.54  ? 137 LEU B CA  1 
ATOM   4264 C C   . LEU B 1 108 ? -3.709  -3.803  20.992  1.00 26.26  ? 137 LEU B C   1 
ATOM   4265 O O   . LEU B 1 108 ? -3.327  -4.472  20.034  1.00 26.37  ? 137 LEU B O   1 
ATOM   4266 C CB  . LEU B 1 108 ? -3.892  -1.249  20.875  1.00 25.09  ? 137 LEU B CB  1 
ATOM   4267 C CG  . LEU B 1 108 ? -2.737  -0.994  19.892  1.00 24.44  ? 137 LEU B CG  1 
ATOM   4268 C CD1 . LEU B 1 108 ? -3.063  -1.271  18.448  1.00 23.28  ? 137 LEU B CD1 1 
ATOM   4269 C CD2 . LEU B 1 108 ? -2.244  0.446   20.005  1.00 24.41  ? 137 LEU B CD2 1 
ATOM   4270 N N   . SER B 1 109 ? -3.429  -4.168  22.267  1.00 23.45  ? 138 SER B N   1 
ATOM   4271 C CA  . SER B 1 109 ? -2.678  -5.387  22.553  1.00 25.36  ? 138 SER B CA  1 
ATOM   4272 C C   . SER B 1 109 ? -3.241  -6.611  21.829  1.00 26.30  ? 138 SER B C   1 
ATOM   4273 O O   . SER B 1 109 ? -2.501  -7.435  21.259  1.00 28.19  ? 138 SER B O   1 
ATOM   4274 C CB  . SER B 1 109 ? -2.606  -5.670  24.046  1.00 27.30  ? 138 SER B CB  1 
ATOM   4275 O OG  . SER B 1 109 ? -1.995  -4.599  24.733  1.00 26.01  ? 138 SER B OG  1 
ATOM   4276 N N   . LYS B 1 110 ? -4.567  -6.759  21.858  1.00 27.05  ? 139 LYS B N   1 
ATOM   4277 C CA  . LYS B 1 110 ? -5.171  -7.937  21.255  1.00 29.92  ? 139 LYS B CA  1 
ATOM   4278 C C   . LYS B 1 110 ? -5.077  -7.844  19.742  1.00 28.23  ? 139 LYS B C   1 
ATOM   4279 O O   . LYS B 1 110 ? -4.983  -8.856  19.079  1.00 31.47  ? 139 LYS B O   1 
ATOM   4280 C CB  . LYS B 1 110 ? -6.654  -8.099  21.619  1.00 37.72  ? 139 LYS B CB  1 
ATOM   4281 C CG  . LYS B 1 110 ? -6.828  -8.465  23.079  1.00 44.26  ? 139 LYS B CG  1 
ATOM   4282 C CD  . LYS B 1 110 ? -8.268  -8.523  23.565  1.00 51.12  ? 139 LYS B CD  1 
ATOM   4283 C CE  . LYS B 1 110 ? -8.280  -8.658  25.049  1.00 54.58  ? 139 LYS B CE  1 
ATOM   4284 N NZ  . LYS B 1 110 ? -9.466  -7.998  25.601  1.00 63.16  ? 139 LYS B NZ  1 
ATOM   4285 N N   . GLU B 1 111 ? -5.172  -6.645  19.186  1.00 25.17  ? 140 GLU B N   1 
ATOM   4286 C CA  . GLU B 1 111 ? -5.018  -6.518  17.747  1.00 27.29  ? 140 GLU B CA  1 
ATOM   4287 C C   . GLU B 1 111 ? -3.628  -6.977  17.340  1.00 26.60  ? 140 GLU B C   1 
ATOM   4288 O O   . GLU B 1 111 ? -3.469  -7.700  16.357  1.00 29.66  ? 140 GLU B O   1 
ATOM   4289 C CB  . GLU B 1 111 ? -5.279  -5.087  17.301  1.00 33.95  ? 140 GLU B CB  1 
ATOM   4290 C CG  . GLU B 1 111 ? -6.761  -4.791  17.084  1.00 43.49  ? 140 GLU B CG  1 
ATOM   4291 C CD  . GLU B 1 111 ? -7.384  -5.542  15.919  1.00 43.55  ? 140 GLU B CD  1 
ATOM   4292 O OE1 . GLU B 1 111 ? -7.004  -5.278  14.746  1.00 50.54  ? 140 GLU B OE1 1 
ATOM   4293 O OE2 . GLU B 1 111 ? -8.209  -6.416  16.199  1.00 48.10  ? 140 GLU B OE2 1 
ATOM   4294 N N   . TRP B 1 112 ? -2.603  -6.597  18.096  1.00 25.03  ? 141 TRP B N   1 
ATOM   4295 C CA  . TRP B 1 112 ? -1.271  -6.979  17.650  1.00 26.76  ? 141 TRP B CA  1 
ATOM   4296 C C   . TRP B 1 112 ? -1.017  -8.481  17.850  1.00 29.00  ? 141 TRP B C   1 
ATOM   4297 O O   . TRP B 1 112 ? -0.431  -9.114  16.976  1.00 29.70  ? 141 TRP B O   1 
ATOM   4298 C CB  . TRP B 1 112 ? -0.231  -6.091  18.336  1.00 24.43  ? 141 TRP B CB  1 
ATOM   4299 C CG  . TRP B 1 112 ? -0.199  -4.674  17.823  1.00 23.79  ? 141 TRP B CG  1 
ATOM   4300 C CD1 . TRP B 1 112 ? -0.787  -4.164  16.700  1.00 25.15  ? 141 TRP B CD1 1 
ATOM   4301 C CD2 . TRP B 1 112 ? 0.508   -3.579  18.421  1.00 22.96  ? 141 TRP B CD2 1 
ATOM   4302 N NE1 . TRP B 1 112 ? -0.542  -2.826  16.588  1.00 22.24  ? 141 TRP B NE1 1 
ATOM   4303 C CE2 . TRP B 1 112 ? 0.258   -2.437  17.621  1.00 23.87  ? 141 TRP B CE2 1 
ATOM   4304 C CE3 . TRP B 1 112 ? 1.281   -3.439  19.581  1.00 26.43  ? 141 TRP B CE3 1 
ATOM   4305 C CZ2 . TRP B 1 112 ? 0.770   -1.177  17.928  1.00 23.68  ? 141 TRP B CZ2 1 
ATOM   4306 C CZ3 . TRP B 1 112 ? 1.805   -2.192  19.878  1.00 24.93  ? 141 TRP B CZ3 1 
ATOM   4307 C CH2 . TRP B 1 112 ? 1.529   -1.083  19.077  1.00 25.24  ? 141 TRP B CH2 1 
ATOM   4308 N N   . ALA B 1 113 ? -1.581  -9.095  18.913  1.00 27.12  ? 142 ALA B N   1 
ATOM   4309 C CA  . ALA B 1 113 ? -1.472  -10.539 19.118  1.00 28.27  ? 142 ALA B CA  1 
ATOM   4310 C C   . ALA B 1 113 ? -2.078  -11.329 17.954  1.00 27.58  ? 142 ALA B C   1 
ATOM   4311 O O   . ALA B 1 113 ? -1.456  -12.267 17.458  1.00 31.28  ? 142 ALA B O   1 
ATOM   4312 C CB  . ALA B 1 113 ? -2.125  -10.928 20.438  1.00 27.53  ? 142 ALA B CB  1 
ATOM   4313 N N   . LYS B 1 114 ? -3.240  -10.877 17.459  1.00 30.79  ? 143 LYS B N   1 
ATOM   4314 C CA  . LYS B 1 114 ? -3.932  -11.505 16.347  1.00 33.85  ? 143 LYS B CA  1 
ATOM   4315 C C   . LYS B 1 114 ? -3.133  -11.425 15.057  1.00 31.74  ? 143 LYS B C   1 
ATOM   4316 O O   . LYS B 1 114 ? -3.290  -12.303 14.231  1.00 27.29  ? 143 LYS B O   1 
ATOM   4317 C CB  . LYS B 1 114 ? -5.242  -10.820 15.938  1.00 38.93  ? 143 LYS B CB  1 
ATOM   4318 C CG  . LYS B 1 114 ? -6.463  -11.035 16.812  1.00 49.92  ? 143 LYS B CG  1 
ATOM   4319 C CD  . LYS B 1 114 ? -7.655  -10.268 16.243  1.00 55.01  ? 143 LYS B CD  1 
ATOM   4320 C CE  . LYS B 1 114 ? -8.742  -9.994  17.242  1.00 69.55  ? 143 LYS B CE  1 
ATOM   4321 N NZ  . LYS B 1 114 ? -9.659  -8.941  16.785  1.00 67.48  ? 143 LYS B NZ  1 
ATOM   4322 N N   . ARG B 1 115 ? -2.309  -10.376 14.862  1.00 29.75  ? 144 ARG B N   1 
ATOM   4323 C CA  . ARG B 1 115 ? -1.650  -10.154 13.566  1.00 27.37  ? 144 ARG B CA  1 
ATOM   4324 C C   . ARG B 1 115 ? -0.205  -10.672 13.524  1.00 29.33  ? 144 ARG B C   1 
ATOM   4325 O O   . ARG B 1 115 ? 0.493   -10.461 12.535  1.00 29.71  ? 144 ARG B O   1 
ATOM   4326 C CB  . ARG B 1 115 ? -1.640  -8.656  13.208  1.00 29.41  ? 144 ARG B CB  1 
ATOM   4327 C CG  . ARG B 1 115 ? -3.004  -7.972  13.156  1.00 29.43  ? 144 ARG B CG  1 
ATOM   4328 C CD  . ARG B 1 115 ? -2.895  -6.475  13.223  1.00 28.00  ? 144 ARG B CD  1 
ATOM   4329 N NE  . ARG B 1 115 ? -4.173  -5.813  12.951  1.00 29.09  ? 144 ARG B NE  1 
ATOM   4330 C CZ  . ARG B 1 115 ? -4.581  -5.225  11.838  1.00 27.51  ? 144 ARG B CZ  1 
ATOM   4331 N NH1 . ARG B 1 115 ? -3.888  -5.346  10.721  1.00 28.55  ? 144 ARG B NH1 1 
ATOM   4332 N NH2 . ARG B 1 115 ? -5.736  -4.559  11.825  1.00 30.08  ? 144 ARG B NH2 1 
ATOM   4333 N N   . ALA B 1 116 ? 0.223   -11.408 14.546  1.00 28.07  ? 145 ALA B N   1 
ATOM   4334 C CA  . ALA B 1 116 ? 1.632   -11.619 14.843  1.00 33.24  ? 145 ALA B CA  1 
ATOM   4335 C C   . ALA B 1 116 ? 2.292   -12.750 14.039  1.00 35.38  ? 145 ALA B C   1 
ATOM   4336 O O   . ALA B 1 116 ? 3.521   -12.859 14.066  1.00 40.47  ? 145 ALA B O   1 
ATOM   4337 C CB  . ALA B 1 116 ? 1.778   -11.818 16.333  1.00 33.24  ? 145 ALA B CB  1 
ATOM   4338 N N   . ALA B 1 117 ? 1.522   -13.537 13.277  1.00 33.10  ? 146 ALA B N   1 
ATOM   4339 C CA  . ALA B 1 117 ? 2.022   -14.723 12.597  1.00 33.04  ? 146 ALA B CA  1 
ATOM   4340 C C   . ALA B 1 117 ? 3.037   -14.365 11.521  1.00 29.62  ? 146 ALA B C   1 
ATOM   4341 O O   . ALA B 1 117 ? 2.770   -13.493 10.707  1.00 30.32  ? 146 ALA B O   1 
ATOM   4342 C CB  . ALA B 1 117 ? 0.866   -15.491 11.959  1.00 35.48  ? 146 ALA B CB  1 
ATOM   4343 N N   . LEU B 1 118 ? 4.137   -15.120 11.471  1.00 30.46  ? 147 LEU B N   1 
ATOM   4344 C CA  . LEU B 1 118 ? 5.103   -15.008 10.392  1.00 31.17  ? 147 LEU B CA  1 
ATOM   4345 C C   . LEU B 1 118 ? 4.786   -15.964 9.239   1.00 32.34  ? 147 LEU B C   1 
ATOM   4346 O O   . LEU B 1 118 ? 4.566   -17.156 9.433   1.00 34.41  ? 147 LEU B O   1 
ATOM   4347 C CB  . LEU B 1 118 ? 6.509   -15.250 10.919  1.00 31.24  ? 147 LEU B CB  1 
ATOM   4348 C CG  . LEU B 1 118 ? 7.041   -14.265 11.965  1.00 28.97  ? 147 LEU B CG  1 
ATOM   4349 C CD1 . LEU B 1 118 ? 8.502   -14.577 12.265  1.00 28.58  ? 147 LEU B CD1 1 
ATOM   4350 C CD2 . LEU B 1 118 ? 6.876   -12.820 11.540  1.00 26.03  ? 147 LEU B CD2 1 
ATOM   4351 N N   . PRO B 1 119 ? 4.873   -15.510 7.974   1.00 30.70  ? 148 PRO B N   1 
ATOM   4352 C CA  . PRO B 1 119 ? 4.901   -16.452 6.853   1.00 30.82  ? 148 PRO B CA  1 
ATOM   4353 C C   . PRO B 1 119 ? 6.128   -17.359 6.893   1.00 34.29  ? 148 PRO B C   1 
ATOM   4354 O O   . PRO B 1 119 ? 7.215   -16.980 7.355   1.00 27.71  ? 148 PRO B O   1 
ATOM   4355 C CB  . PRO B 1 119 ? 4.865   -15.617 5.579   1.00 31.86  ? 148 PRO B CB  1 
ATOM   4356 C CG  . PRO B 1 119 ? 5.188   -14.186 6.029   1.00 31.73  ? 148 PRO B CG  1 
ATOM   4357 C CD  . PRO B 1 119 ? 4.989   -14.100 7.557   1.00 29.49  ? 148 PRO B CD  1 
ATOM   4358 N N   . SER B 1 120 ? 5.954   -18.574 6.361   1.00 32.31  ? 149 SER B N   1 
ATOM   4359 C CA  . SER B 1 120 ? 6.978   -19.586 6.543   1.00 34.30  ? 149 SER B CA  1 
ATOM   4360 C C   . SER B 1 120 ? 8.247   -19.176 5.794   1.00 26.60  ? 149 SER B C   1 
ATOM   4361 O O   . SER B 1 120 ? 9.334   -19.428 6.289   1.00 29.24  ? 149 SER B O   1 
ATOM   4362 C CB  . SER B 1 120 ? 6.468   -20.965 6.167   1.00 36.98  ? 149 SER B CB  1 
ATOM   4363 O OG  . SER B 1 120 ? 6.541   -21.189 4.776   1.00 43.18  ? 149 SER B OG  1 
ATOM   4364 N N   . HIS B 1 121 ? 8.135   -18.482 4.649   1.00 27.09  ? 150 HIS B N   1 
ATOM   4365 C CA  . HIS B 1 121 ? 9.343   -18.141 3.905   1.00 26.62  ? 150 HIS B CA  1 
ATOM   4366 C C   . HIS B 1 121 ? 10.280  -17.253 4.739   1.00 25.68  ? 150 HIS B C   1 
ATOM   4367 O O   . HIS B 1 121 ? 11.499  -17.348 4.619   1.00 28.51  ? 150 HIS B O   1 
ATOM   4368 C CB  . HIS B 1 121 ? 9.046   -17.539 2.529   1.00 26.97  ? 150 HIS B CB  1 
ATOM   4369 C CG  . HIS B 1 121 ? 8.669   -16.101 2.503   1.00 27.13  ? 150 HIS B CG  1 
ATOM   4370 N ND1 . HIS B 1 121 ? 7.390   -15.641 2.745   1.00 28.36  ? 150 HIS B ND1 1 
ATOM   4371 C CD2 . HIS B 1 121 ? 9.417   -15.039 2.239   1.00 26.74  ? 150 HIS B CD2 1 
ATOM   4372 C CE1 . HIS B 1 121 ? 7.370   -14.341 2.613   1.00 29.61  ? 150 HIS B CE1 1 
ATOM   4373 N NE2 . HIS B 1 121 ? 8.589   -13.953 2.264   1.00 31.06  ? 150 HIS B NE2 1 
ATOM   4374 N N   . VAL B 1 122 ? 9.717   -16.438 5.630   1.00 27.16  ? 151 VAL B N   1 
ATOM   4375 C CA  . VAL B 1 122 ? 10.529  -15.622 6.523   1.00 29.11  ? 151 VAL B CA  1 
ATOM   4376 C C   . VAL B 1 122 ? 11.095  -16.461 7.678   1.00 26.45  ? 151 VAL B C   1 
ATOM   4377 O O   . VAL B 1 122 ? 12.253  -16.304 8.044   1.00 33.25  ? 151 VAL B O   1 
ATOM   4378 C CB  . VAL B 1 122 ? 9.688   -14.429 7.013   1.00 28.27  ? 151 VAL B CB  1 
ATOM   4379 C CG1 . VAL B 1 122 ? 10.386  -13.665 8.140   1.00 24.78  ? 151 VAL B CG1 1 
ATOM   4380 C CG2 . VAL B 1 122 ? 9.303   -13.535 5.843   1.00 28.09  ? 151 VAL B CG2 1 
ATOM   4381 N N   . VAL B 1 123 ? 10.312  -17.371 8.244   1.00 29.38  ? 152 VAL B N   1 
ATOM   4382 C CA  . VAL B 1 123 ? 10.815  -18.297 9.248   1.00 27.64  ? 152 VAL B CA  1 
ATOM   4383 C C   . VAL B 1 123 ? 12.017  -19.073 8.683   1.00 29.49  ? 152 VAL B C   1 
ATOM   4384 O O   . VAL B 1 123 ? 13.085  -19.114 9.305   1.00 27.06  ? 152 VAL B O   1 
ATOM   4385 C CB  . VAL B 1 123 ? 9.693   -19.231 9.729   1.00 29.03  ? 152 VAL B CB  1 
ATOM   4386 C CG1 . VAL B 1 123 ? 10.231  -20.311 10.674  1.00 30.72  ? 152 VAL B CG1 1 
ATOM   4387 C CG2 . VAL B 1 123 ? 8.549   -18.443 10.354  1.00 29.73  ? 152 VAL B CG2 1 
ATOM   4388 N N   . THR B 1 124 ? 11.844  -19.636 7.478   1.00 27.95  ? 153 THR B N   1 
ATOM   4389 C CA  . THR B 1 124 ? 12.874  -20.371 6.740   1.00 31.62  ? 153 THR B CA  1 
ATOM   4390 C C   . THR B 1 124 ? 14.159  -19.551 6.580   1.00 34.48  ? 153 THR B C   1 
ATOM   4391 O O   . THR B 1 124 ? 15.275  -20.046 6.797   1.00 29.40  ? 153 THR B O   1 
ATOM   4392 C CB  . THR B 1 124 ? 12.308  -20.723 5.356   1.00 31.53  ? 153 THR B CB  1 
ATOM   4393 O OG1 . THR B 1 124 ? 11.453  -21.796 5.684   1.00 34.21  ? 153 THR B OG1 1 
ATOM   4394 C CG2 . THR B 1 124 ? 13.337  -21.141 4.312   1.00 34.82  ? 153 THR B CG2 1 
ATOM   4395 N N   . MET B 1 125 ? 13.993  -18.325 6.064   1.00 32.72  ? 154 MET B N   1 
ATOM   4396 C CA  . MET B 1 125 ? 15.110  -17.433 5.778   1.00 29.44  ? 154 MET B CA  1 
ATOM   4397 C C   . MET B 1 125 ? 15.847  -17.098 7.074   1.00 24.37  ? 154 MET B C   1 
ATOM   4398 O O   . MET B 1 125 ? 17.066  -17.062 7.139   1.00 23.64  ? 154 MET B O   1 
ATOM   4399 C CB  . MET B 1 125 ? 14.539  -16.148 5.154   1.00 32.07  ? 154 MET B CB  1 
ATOM   4400 C CG  . MET B 1 125 ? 15.527  -15.190 4.543   1.00 38.73  ? 154 MET B CG  1 
ATOM   4401 S SD  . MET B 1 125 ? 14.664  -13.639 4.172   1.00 44.15  ? 154 MET B SD  1 
ATOM   4402 C CE  . MET B 1 125 ? 15.875  -12.353 4.443   1.00 57.32  ? 154 MET B CE  1 
ATOM   4403 N N   . LEU B 1 126 ? 15.108  -16.837 8.131   1.00 22.54  ? 155 LEU B N   1 
ATOM   4404 C CA  . LEU B 1 126 ? 15.750  -16.499 9.401   1.00 24.30  ? 155 LEU B CA  1 
ATOM   4405 C C   . LEU B 1 126 ? 16.518  -17.703 9.935   1.00 28.66  ? 155 LEU B C   1 
ATOM   4406 O O   . LEU B 1 126 ? 17.634  -17.560 10.433  1.00 27.20  ? 155 LEU B O   1 
ATOM   4407 C CB  . LEU B 1 126 ? 14.706  -16.024 10.404  1.00 24.60  ? 155 LEU B CB  1 
ATOM   4408 C CG  . LEU B 1 126 ? 14.187  -14.600 10.224  1.00 28.06  ? 155 LEU B CG  1 
ATOM   4409 C CD1 . LEU B 1 126 ? 12.991  -14.343 11.103  1.00 27.71  ? 155 LEU B CD1 1 
ATOM   4410 C CD2 . LEU B 1 126 ? 15.336  -13.612 10.535  1.00 32.83  ? 155 LEU B CD2 1 
ATOM   4411 N N   . ASP B 1 127 ? 15.882  -18.876 9.803   1.00 26.23  ? 156 ASP B N   1 
ATOM   4412 C CA  . ASP B 1 127 ? 16.452  -20.141 10.218  1.00 30.83  ? 156 ASP B CA  1 
ATOM   4413 C C   . ASP B 1 127 ? 17.680  -20.502 9.400   1.00 27.77  ? 156 ASP B C   1 
ATOM   4414 O O   . ASP B 1 127 ? 18.525  -21.202 9.925   1.00 30.84  ? 156 ASP B O   1 
ATOM   4415 C CB  . ASP B 1 127 ? 15.415  -21.256 10.253  1.00 28.96  ? 156 ASP B CB  1 
ATOM   4416 C CG  . ASP B 1 127 ? 14.419  -21.154 11.408  1.00 33.70  ? 156 ASP B CG  1 
ATOM   4417 O OD1 . ASP B 1 127 ? 14.611  -20.305 12.312  1.00 33.91  ? 156 ASP B OD1 1 
ATOM   4418 O OD2 . ASP B 1 127 ? 13.414  -21.907 11.399  1.00 34.94  ? 156 ASP B OD2 1 
ATOM   4419 N N   . ASN B 1 128 ? 17.822  -19.979 8.173   1.00 27.64  ? 157 ASN B N   1 
ATOM   4420 C CA  . ASN B 1 128 ? 18.990  -20.277 7.381   1.00 28.06  ? 157 ASN B CA  1 
ATOM   4421 C C   . ASN B 1 128 ? 20.117  -19.268 7.548   1.00 28.53  ? 157 ASN B C   1 
ATOM   4422 O O   . ASN B 1 128 ? 21.194  -19.538 7.089   1.00 29.43  ? 157 ASN B O   1 
ATOM   4423 C CB  . ASN B 1 128 ? 18.662  -20.527 5.924   1.00 33.53  ? 157 ASN B CB  1 
ATOM   4424 C CG  . ASN B 1 128 ? 17.996  -21.877 5.736   1.00 37.50  ? 157 ASN B CG  1 
ATOM   4425 O OD1 . ASN B 1 128 ? 18.488  -22.880 6.245   1.00 44.77  ? 157 ASN B OD1 1 
ATOM   4426 N ND2 . ASN B 1 128 ? 16.895  -21.940 5.013   1.00 37.52  ? 157 ASN B ND2 1 
ATOM   4427 N N   . PHE B 1 129 ? 19.907  -18.106 8.180   1.00 26.15  ? 158 PHE B N   1 
ATOM   4428 C CA  . PHE B 1 129 ? 20.960  -17.122 8.240   1.00 25.77  ? 158 PHE B CA  1 
ATOM   4429 C C   . PHE B 1 129 ? 22.133  -17.638 9.081   1.00 24.05  ? 158 PHE B C   1 
ATOM   4430 O O   . PHE B 1 129 ? 21.940  -18.191 10.146  1.00 26.21  ? 158 PHE B O   1 
ATOM   4431 C CB  . PHE B 1 129 ? 20.356  -15.836 8.809   1.00 27.57  ? 158 PHE B CB  1 
ATOM   4432 C CG  . PHE B 1 129 ? 19.584  -14.918 7.867   1.00 26.95  ? 158 PHE B CG  1 
ATOM   4433 C CD1 . PHE B 1 129 ? 19.835  -14.893 6.495   1.00 28.48  ? 158 PHE B CD1 1 
ATOM   4434 C CD2 . PHE B 1 129 ? 18.694  -14.012 8.387   1.00 26.50  ? 158 PHE B CD2 1 
ATOM   4435 C CE1 . PHE B 1 129 ? 19.154  -14.017 5.663   1.00 28.55  ? 158 PHE B CE1 1 
ATOM   4436 C CE2 . PHE B 1 129 ? 18.044  -13.112 7.560   1.00 27.00  ? 158 PHE B CE2 1 
ATOM   4437 C CZ  . PHE B 1 129 ? 18.244  -13.147 6.208   1.00 25.94  ? 158 PHE B CZ  1 
ATOM   4438 N N   . PRO B 1 130 ? 23.403  -17.390 8.683   1.00 27.22  ? 159 PRO B N   1 
ATOM   4439 C CA  . PRO B 1 130 ? 24.579  -17.757 9.488   1.00 26.07  ? 159 PRO B CA  1 
ATOM   4440 C C   . PRO B 1 130 ? 24.812  -16.817 10.671  1.00 29.43  ? 159 PRO B C   1 
ATOM   4441 O O   . PRO B 1 130 ? 24.273  -15.690 10.703  1.00 27.76  ? 159 PRO B O   1 
ATOM   4442 C CB  . PRO B 1 130 ? 25.689  -17.623 8.433   1.00 26.08  ? 159 PRO B CB  1 
ATOM   4443 C CG  . PRO B 1 130 ? 25.269  -16.428 7.633   1.00 25.91  ? 159 PRO B CG  1 
ATOM   4444 C CD  . PRO B 1 130 ? 23.777  -16.635 7.485   1.00 27.61  ? 159 PRO B CD  1 
ATOM   4445 N N   . THR B 1 131 ? 25.602  -17.283 11.657  1.00 26.76  ? 160 THR B N   1 
ATOM   4446 C CA  . THR B 1 131 ? 25.852  -16.501 12.863  1.00 29.17  ? 160 THR B CA  1 
ATOM   4447 C C   . THR B 1 131 ? 26.746  -15.288 12.619  1.00 26.30  ? 160 THR B C   1 
ATOM   4448 O O   . THR B 1 131 ? 26.766  -14.393 13.459  1.00 26.61  ? 160 THR B O   1 
ATOM   4449 C CB  . THR B 1 131 ? 26.428  -17.358 13.992  1.00 32.28  ? 160 THR B CB  1 
ATOM   4450 O OG1 . THR B 1 131 ? 27.730  -17.741 13.585  1.00 33.27  ? 160 THR B OG1 1 
ATOM   4451 C CG2 . THR B 1 131 ? 25.543  -18.542 14.274  1.00 32.51  ? 160 THR B CG2 1 
ATOM   4452 N N   . ASN B 1 132 ? 27.406  -15.179 11.459  1.00 27.11  ? 161 ASN B N   1 
ATOM   4453 C CA  . ASN B 1 132 ? 28.232  -14.013 11.189  1.00 29.47  ? 161 ASN B CA  1 
ATOM   4454 C C   . ASN B 1 132 ? 27.440  -12.915 10.460  1.00 25.75  ? 161 ASN B C   1 
ATOM   4455 O O   . ASN B 1 132 ? 28.011  -11.925 10.042  1.00 27.50  ? 161 ASN B O   1 
ATOM   4456 C CB  . ASN B 1 132 ? 29.500  -14.416 10.447  1.00 30.69  ? 161 ASN B CB  1 
ATOM   4457 C CG  . ASN B 1 132 ? 29.207  -15.033 9.094   1.00 33.62  ? 161 ASN B CG  1 
ATOM   4458 O OD1 . ASN B 1 132 ? 28.186  -15.691 8.929   1.00 39.49  ? 161 ASN B OD1 1 
ATOM   4459 N ND2 . ASN B 1 132 ? 30.021  -14.774 8.092   1.00 40.63  ? 161 ASN B ND2 1 
ATOM   4460 N N   . LEU B 1 133 ? 26.157  -13.139 10.184  1.00 24.38  ? 162 LEU B N   1 
ATOM   4461 C CA  . LEU B 1 133 ? 25.312  -12.072 9.663   1.00 21.64  ? 162 LEU B CA  1 
ATOM   4462 C C   . LEU B 1 133 ? 24.726  -11.333 10.855  1.00 19.99  ? 162 LEU B C   1 
ATOM   4463 O O   . LEU B 1 133 ? 23.982  -11.943 11.614  1.00 20.70  ? 162 LEU B O   1 
ATOM   4464 C CB  . LEU B 1 133 ? 24.226  -12.630 8.768   1.00 21.12  ? 162 LEU B CB  1 
ATOM   4465 C CG  . LEU B 1 133 ? 23.383  -11.607 8.008   1.00 23.01  ? 162 LEU B CG  1 
ATOM   4466 C CD1 . LEU B 1 133 ? 24.191  -10.742 7.087   1.00 22.34  ? 162 LEU B CD1 1 
ATOM   4467 C CD2 . LEU B 1 133 ? 22.323  -12.348 7.206   1.00 25.47  ? 162 LEU B CD2 1 
ATOM   4468 N N   . HIS B 1 134 ? 25.110  -10.047 10.987  1.00 21.01  ? 163 HIS B N   1 
ATOM   4469 C CA  . HIS B 1 134 ? 24.773  -9.168  12.108  1.00 22.71  ? 163 HIS B CA  1 
ATOM   4470 C C   . HIS B 1 134 ? 23.260  -9.163  12.347  1.00 23.11  ? 163 HIS B C   1 
ATOM   4471 O O   . HIS B 1 134 ? 22.491  -9.176  11.408  1.00 21.12  ? 163 HIS B O   1 
ATOM   4472 C CB  . HIS B 1 134 ? 25.268  -7.738  11.840  1.00 27.89  ? 163 HIS B CB  1 
ATOM   4473 C CG  . HIS B 1 134 ? 25.168  -6.819  13.021  1.00 30.25  ? 163 HIS B CG  1 
ATOM   4474 N ND1 . HIS B 1 134 ? 23.976  -6.245  13.438  1.00 29.31  ? 163 HIS B ND1 1 
ATOM   4475 C CD2 . HIS B 1 134 ? 26.119  -6.395  13.908  1.00 33.99  ? 163 HIS B CD2 1 
ATOM   4476 C CE1 . HIS B 1 134 ? 24.161  -5.553  14.553  1.00 29.98  ? 163 HIS B CE1 1 
ATOM   4477 N NE2 . HIS B 1 134 ? 25.481  -5.585  14.829  1.00 34.39  ? 163 HIS B NE2 1 
ATOM   4478 N N   . PRO B 1 135 ? 22.800  -9.161  13.607  1.00 21.44  ? 164 PRO B N   1 
ATOM   4479 C CA  . PRO B 1 135 ? 21.366  -9.159  13.910  1.00 21.20  ? 164 PRO B CA  1 
ATOM   4480 C C   . PRO B 1 135 ? 20.556  -8.100  13.168  1.00 20.32  ? 164 PRO B C   1 
ATOM   4481 O O   . PRO B 1 135 ? 19.391  -8.324  12.810  1.00 18.94  ? 164 PRO B O   1 
ATOM   4482 C CB  . PRO B 1 135 ? 21.350  -8.914  15.447  1.00 21.26  ? 164 PRO B CB  1 
ATOM   4483 C CG  . PRO B 1 135 ? 22.678  -9.294  15.934  1.00 25.22  ? 164 PRO B CG  1 
ATOM   4484 C CD  . PRO B 1 135 ? 23.650  -9.238  14.800  1.00 24.08  ? 164 PRO B CD  1 
ATOM   4485 N N   . MET B 1 136 ? 21.150  -6.892  12.993  1.00 21.36  ? 165 MET B N   1 
ATOM   4486 C CA  . MET B 1 136 ? 20.448  -5.802  12.304  1.00 19.99  ? 165 MET B CA  1 
ATOM   4487 C C   . MET B 1 136 ? 20.222  -6.105  10.813  1.00 18.98  ? 165 MET B C   1 
ATOM   4488 O O   . MET B 1 136 ? 19.203  -5.732  10.252  1.00 19.98  ? 165 MET B O   1 
ATOM   4489 C CB  . MET B 1 136 ? 21.185  -4.476  12.524  1.00 18.55  ? 165 MET B CB  1 
ATOM   4490 C CG  . MET B 1 136 ? 20.920  -3.848  13.908  1.00 19.99  ? 165 MET B CG  1 
ATOM   4491 S SD  . MET B 1 136 ? 19.191  -3.404  14.193  1.00 23.53  ? 165 MET B SD  1 
ATOM   4492 C CE  . MET B 1 136 ? 19.033  -2.088  12.981  1.00 22.19  ? 165 MET B CE  1 
ATOM   4493 N N   . SER B 1 137 ? 21.167  -6.800  10.190  1.00 20.00  ? 166 SER B N   1 
ATOM   4494 C CA  . SER B 1 137 ? 21.082  -7.193  8.798   1.00 21.08  ? 166 SER B CA  1 
ATOM   4495 C C   . SER B 1 137 ? 19.996  -8.244  8.655   1.00 20.08  ? 166 SER B C   1 
ATOM   4496 O O   . SER B 1 137 ? 19.236  -8.200  7.697   1.00 20.98  ? 166 SER B O   1 
ATOM   4497 C CB  . SER B 1 137 ? 22.389  -7.695  8.284   1.00 23.07  ? 166 SER B CB  1 
ATOM   4498 O OG  . SER B 1 137 ? 23.362  -6.680  8.464   1.00 24.18  ? 166 SER B OG  1 
ATOM   4499 N N   . GLN B 1 138 ? 19.909  -9.128  9.666   1.00 18.08  ? 167 GLN B N   1 
ATOM   4500 C CA  . GLN B 1 138 ? 18.891  -10.158 9.680   1.00 20.91  ? 167 GLN B CA  1 
ATOM   4501 C C   . GLN B 1 138 ? 17.519  -9.501  9.823   1.00 18.32  ? 167 GLN B C   1 
ATOM   4502 O O   . GLN B 1 138 ? 16.577  -9.912  9.157   1.00 19.78  ? 167 GLN B O   1 
ATOM   4503 C CB  . GLN B 1 138 ? 19.072  -11.192 10.789  1.00 20.21  ? 167 GLN B CB  1 
ATOM   4504 C CG  . GLN B 1 138 ? 20.400  -11.924 10.769  1.00 20.74  ? 167 GLN B CG  1 
ATOM   4505 C CD  . GLN B 1 138 ? 20.374  -13.219 11.552  1.00 22.68  ? 167 GLN B CD  1 
ATOM   4506 O OE1 . GLN B 1 138 ? 19.309  -13.805 11.793  1.00 22.34  ? 167 GLN B OE1 1 
ATOM   4507 N NE2 . GLN B 1 138 ? 21.555  -13.754 11.821  1.00 25.62  ? 167 GLN B NE2 1 
ATOM   4508 N N   . LEU B 1 139 ? 17.437  -8.442  10.645  1.00 19.54  ? 168 LEU B N   1 
ATOM   4509 C CA  . LEU B 1 139 ? 16.158  -7.775  10.889  1.00 19.19  ? 168 LEU B CA  1 
ATOM   4510 C C   . LEU B 1 139 ? 15.669  -7.099  9.615   1.00 18.81  ? 168 LEU B C   1 
ATOM   4511 O O   . LEU B 1 139 ? 14.536  -7.287  9.189   1.00 20.27  ? 168 LEU B O   1 
ATOM   4512 C CB  . LEU B 1 139 ? 16.301  -6.802  12.051  1.00 20.48  ? 168 LEU B CB  1 
ATOM   4513 C CG  . LEU B 1 139 ? 15.110  -5.896  12.340  1.00 22.36  ? 168 LEU B CG  1 
ATOM   4514 C CD1 . LEU B 1 139 ? 13.915  -6.725  12.742  1.00 24.30  ? 168 LEU B CD1 1 
ATOM   4515 C CD2 . LEU B 1 139 ? 15.425  -4.828  13.366  1.00 25.03  ? 168 LEU B CD2 1 
ATOM   4516 N N   . SER B 1 140 ? 16.580  -6.412  8.940   1.00 18.99  ? 169 SER B N   1 
ATOM   4517 C CA  . SER B 1 140 ? 16.274  -5.650  7.745   1.00 19.13  ? 169 SER B CA  1 
ATOM   4518 C C   . SER B 1 140 ? 15.892  -6.593  6.603   1.00 19.14  ? 169 SER B C   1 
ATOM   4519 O O   . SER B 1 140 ? 14.895  -6.377  5.917   1.00 19.86  ? 169 SER B O   1 
ATOM   4520 C CB  . SER B 1 140 ? 17.440  -4.729  7.347   1.00 20.23  ? 169 SER B CB  1 
ATOM   4521 O OG  . SER B 1 140 ? 17.088  -4.065  6.118   1.00 26.93  ? 169 SER B OG  1 
ATOM   4522 N N   . ALA B 1 141 ? 16.663  -7.657  6.406   1.00 17.81  ? 170 ALA B N   1 
ATOM   4523 C CA  . ALA B 1 141 ? 16.378  -8.616  5.356   1.00 19.46  ? 170 ALA B CA  1 
ATOM   4524 C C   . ALA B 1 141 ? 15.025  -9.318  5.540   1.00 20.02  ? 170 ALA B C   1 
ATOM   4525 O O   . ALA B 1 141 ? 14.250  -9.471  4.595   1.00 17.72  ? 170 ALA B O   1 
ATOM   4526 C CB  . ALA B 1 141 ? 17.531  -9.578  5.224   1.00 19.72  ? 170 ALA B CB  1 
ATOM   4527 N N   . ALA B 1 142 ? 14.697  -9.699  6.771   1.00 18.66  ? 171 ALA B N   1 
ATOM   4528 C CA  . ALA B 1 142 ? 13.431  -10.318 7.083   1.00 19.49  ? 171 ALA B CA  1 
ATOM   4529 C C   . ALA B 1 142 ? 12.258  -9.371  6.883   1.00 21.99  ? 171 ALA B C   1 
ATOM   4530 O O   . ALA B 1 142 ? 11.207  -9.772  6.390   1.00 24.16  ? 171 ALA B O   1 
ATOM   4531 C CB  . ALA B 1 142 ? 13.453  -10.823 8.501   1.00 19.37  ? 171 ALA B CB  1 
ATOM   4532 N N   . VAL B 1 143 ? 12.420  -8.085  7.261   1.00 21.41  ? 172 VAL B N   1 
ATOM   4533 C CA  . VAL B 1 143 ? 11.317  -7.166  7.110   1.00 20.73  ? 172 VAL B CA  1 
ATOM   4534 C C   . VAL B 1 143 ? 11.071  -6.932  5.621   1.00 19.28  ? 172 VAL B C   1 
ATOM   4535 O O   . VAL B 1 143 ? 9.941   -6.856  5.177   1.00 18.91  ? 172 VAL B O   1 
ATOM   4536 C CB  . VAL B 1 143 ? 11.560  -5.886  7.905   1.00 20.70  ? 172 VAL B CB  1 
ATOM   4537 C CG1 . VAL B 1 143 ? 10.542  -4.812  7.549   1.00 25.75  ? 172 VAL B CG1 1 
ATOM   4538 C CG2 . VAL B 1 143 ? 11.503  -6.171  9.400   1.00 19.81  ? 172 VAL B CG2 1 
ATOM   4539 N N   . THR B 1 144 ? 12.152  -6.861  4.854   1.00 19.58  ? 173 THR B N   1 
ATOM   4540 C CA  . THR B 1 144 ? 12.017  -6.685  3.415   1.00 20.67  ? 173 THR B CA  1 
ATOM   4541 C C   . THR B 1 144 ? 11.234  -7.845  2.840   1.00 19.69  ? 173 THR B C   1 
ATOM   4542 O O   . THR B 1 144 ? 10.319  -7.618  2.027   1.00 21.08  ? 173 THR B O   1 
ATOM   4543 C CB  . THR B 1 144 ? 13.380  -6.574  2.754   1.00 20.27  ? 173 THR B CB  1 
ATOM   4544 O OG1 . THR B 1 144 ? 13.898  -5.335  3.230   1.00 23.42  ? 173 THR B OG1 1 
ATOM   4545 C CG2 . THR B 1 144 ? 13.267  -6.573  1.241   1.00 20.10  ? 173 THR B CG2 1 
ATOM   4546 N N   . ALA B 1 145 ? 11.614  -9.055  3.249   1.00 21.61  ? 174 ALA B N   1 
ATOM   4547 C CA  . ALA B 1 145 ? 10.984  -10.277 2.762   1.00 22.49  ? 174 ALA B CA  1 
ATOM   4548 C C   . ALA B 1 145 ? 9.517   -10.361 3.163   1.00 23.55  ? 174 ALA B C   1 
ATOM   4549 O O   . ALA B 1 145 ? 8.724   -10.997 2.440   1.00 24.88  ? 174 ALA B O   1 
ATOM   4550 C CB  . ALA B 1 145 ? 11.755  -11.478 3.259   1.00 22.83  ? 174 ALA B CB  1 
ATOM   4551 N N   . LEU B 1 146 ? 9.142   -9.710  4.279   1.00 20.66  ? 175 LEU B N   1 
ATOM   4552 C CA  . LEU B 1 146 ? 7.745   -9.684  4.720   1.00 22.24  ? 175 LEU B CA  1 
ATOM   4553 C C   . LEU B 1 146 ? 6.865   -8.856  3.779   1.00 23.99  ? 175 LEU B C   1 
ATOM   4554 O O   . LEU B 1 146 ? 5.627   -8.848  3.887   1.00 25.77  ? 175 LEU B O   1 
ATOM   4555 C CB  . LEU B 1 146 ? 7.602   -9.132  6.136   1.00 23.67  ? 175 LEU B CB  1 
ATOM   4556 C CG  . LEU B 1 146 ? 7.883   -10.066 7.300   1.00 24.86  ? 175 LEU B CG  1 
ATOM   4557 C CD1 . LEU B 1 146 ? 8.034   -9.286  8.566   1.00 24.53  ? 175 LEU B CD1 1 
ATOM   4558 C CD2 . LEU B 1 146 ? 6.790   -11.075 7.530   1.00 27.09  ? 175 LEU B CD2 1 
ATOM   4559 N N   . ASN B 1 147 ? 7.461   -8.111  2.859   1.00 23.83  ? 176 ASN B N   1 
ATOM   4560 C CA  . ASN B 1 147 ? 6.631   -7.216  2.082   1.00 26.55  ? 176 ASN B CA  1 
ATOM   4561 C C   . ASN B 1 147 ? 5.791   -8.015  1.075   1.00 24.13  ? 176 ASN B C   1 
ATOM   4562 O O   . ASN B 1 147 ? 4.946   -7.449  0.416   1.00 22.19  ? 176 ASN B O   1 
ATOM   4563 C CB  . ASN B 1 147 ? 7.437   -6.118  1.397   1.00 24.12  ? 176 ASN B CB  1 
ATOM   4564 C CG  . ASN B 1 147 ? 7.448   -6.286  -0.091  1.00 28.42  ? 176 ASN B CG  1 
ATOM   4565 O OD1 . ASN B 1 147 ? 7.816   -7.355  -0.587  1.00 31.08  ? 176 ASN B OD1 1 
ATOM   4566 N ND2 . ASN B 1 147 ? 7.047   -5.249  -0.821  1.00 29.34  ? 176 ASN B ND2 1 
ATOM   4567 N N   . SER B 1 148 ? 6.018   -9.324  0.982   1.00 25.71  ? 177 SER B N   1 
ATOM   4568 C CA  . SER B 1 148 ? 5.106   -10.186 0.256   1.00 26.57  ? 177 SER B CA  1 
ATOM   4569 C C   . SER B 1 148 ? 3.733   -10.097 0.906   1.00 28.21  ? 177 SER B C   1 
ATOM   4570 O O   . SER B 1 148 ? 2.763   -10.425 0.272   1.00 30.62  ? 177 SER B O   1 
ATOM   4571 C CB  . SER B 1 148 ? 5.598   -11.613 0.214   1.00 26.01  ? 177 SER B CB  1 
ATOM   4572 O OG  . SER B 1 148 ? 5.718   -12.145 1.522   1.00 27.38  ? 177 SER B OG  1 
ATOM   4573 N N   . GLU B 1 149 ? 3.662   -9.615  2.157   1.00 27.70  ? 178 GLU B N   1 
ATOM   4574 C CA  . GLU B 1 149 ? 2.390   -9.510  2.845   1.00 33.27  ? 178 GLU B CA  1 
ATOM   4575 C C   . GLU B 1 149 ? 1.694   -8.165  2.650   1.00 31.94  ? 178 GLU B C   1 
ATOM   4576 O O   . GLU B 1 149 ? 0.677   -7.936  3.297   1.00 32.18  ? 178 GLU B O   1 
ATOM   4577 C CB  . GLU B 1 149 ? 2.677   -9.768  4.322   1.00 37.39  ? 178 GLU B CB  1 
ATOM   4578 C CG  . GLU B 1 149 ? 3.329   -11.119 4.612   1.00 45.17  ? 178 GLU B CG  1 
ATOM   4579 C CD  . GLU B 1 149 ? 2.654   -12.322 3.954   1.00 54.67  ? 178 GLU B CD  1 
ATOM   4580 O OE1 . GLU B 1 149 ? 1.582   -12.723 4.457   1.00 66.82  ? 178 GLU B OE1 1 
ATOM   4581 O OE2 . GLU B 1 149 ? 3.187   -12.865 2.947   1.00 60.66  ? 178 GLU B OE2 1 
ATOM   4582 N N   . SER B 1 150 ? 2.263   -7.246  1.839   1.00 29.90  ? 179 SER B N   1 
ATOM   4583 C CA  . SER B 1 150 ? 1.867   -5.848  1.882   1.00 27.95  ? 179 SER B CA  1 
ATOM   4584 C C   . SER B 1 150 ? 0.509   -5.663  1.208   1.00 26.41  ? 179 SER B C   1 
ATOM   4585 O O   . SER B 1 150 ? 0.400   -5.885  0.015   1.00 25.23  ? 179 SER B O   1 
ATOM   4586 C CB  . SER B 1 150 ? 2.852   -4.891  1.262   1.00 23.11  ? 179 SER B CB  1 
ATOM   4587 O OG  . SER B 1 150 ? 2.312   -3.586  1.333   1.00 23.30  ? 179 SER B OG  1 
ATOM   4588 N N   . ASN B 1 151 ? -0.473  -5.234  2.000   1.00 27.29  ? 180 ASN B N   1 
ATOM   4589 C CA  . ASN B 1 151 ? -1.805  -4.854  1.522   1.00 30.99  ? 180 ASN B CA  1 
ATOM   4590 C C   . ASN B 1 151 ? -1.685  -3.648  0.591   1.00 31.50  ? 180 ASN B C   1 
ATOM   4591 O O   . ASN B 1 151 ? -2.286  -3.589  -0.491  1.00 29.35  ? 180 ASN B O   1 
ATOM   4592 C CB  . ASN B 1 151 ? -2.715  -4.487  2.696   1.00 38.38  ? 180 ASN B CB  1 
ATOM   4593 C CG  . ASN B 1 151 ? -2.863  -5.554  3.766   1.00 41.70  ? 180 ASN B CG  1 
ATOM   4594 O OD1 . ASN B 1 151 ? -2.498  -5.364  4.955   1.00 40.74  ? 180 ASN B OD1 1 
ATOM   4595 N ND2 . ASN B 1 151 ? -3.399  -6.686  3.353   1.00 39.37  ? 180 ASN B ND2 1 
ATOM   4596 N N   . PHE B 1 152 ? -0.825  -2.692  1.000   1.00 30.19  ? 181 PHE B N   1 
ATOM   4597 C CA  . PHE B 1 152 ? -0.672  -1.436  0.286   1.00 30.62  ? 181 PHE B CA  1 
ATOM   4598 C C   . PHE B 1 152 ? -0.092  -1.691  -1.103  1.00 27.52  ? 181 PHE B C   1 
ATOM   4599 O O   . PHE B 1 152 ? -0.611  -1.196  -2.112  1.00 27.16  ? 181 PHE B O   1 
ATOM   4600 C CB  . PHE B 1 152 ? 0.147   -0.413  1.081   1.00 28.04  ? 181 PHE B CB  1 
ATOM   4601 C CG  . PHE B 1 152 ? 0.321   0.843   0.251   1.00 27.14  ? 181 PHE B CG  1 
ATOM   4602 C CD1 . PHE B 1 152 ? -0.690  1.779   0.183   1.00 27.67  ? 181 PHE B CD1 1 
ATOM   4603 C CD2 . PHE B 1 152 ? 1.479   1.080   -0.475  1.00 25.27  ? 181 PHE B CD2 1 
ATOM   4604 C CE1 . PHE B 1 152 ? -0.526  2.935   -0.546  1.00 28.83  ? 181 PHE B CE1 1 
ATOM   4605 C CE2 . PHE B 1 152 ? 1.629   2.225   -1.207  1.00 28.97  ? 181 PHE B CE2 1 
ATOM   4606 C CZ  . PHE B 1 152 ? 0.628   3.141   -1.265  1.00 28.80  ? 181 PHE B CZ  1 
ATOM   4607 N N   . ALA B 1 153 ? 0.956   -2.502  -1.188  1.00 28.81  ? 182 ALA B N   1 
ATOM   4608 C CA  . ALA B 1 153 ? 1.599   -2.696  -2.487  1.00 28.72  ? 182 ALA B CA  1 
ATOM   4609 C C   . ALA B 1 153 ? 0.590   -3.278  -3.497  1.00 33.03  ? 182 ALA B C   1 
ATOM   4610 O O   . ALA B 1 153 ? 0.621   -2.980  -4.690  1.00 35.08  ? 182 ALA B O   1 
ATOM   4611 C CB  . ALA B 1 153 ? 2.819   -3.594  -2.344  1.00 27.78  ? 182 ALA B CB  1 
ATOM   4612 N N   . ARG B 1 154 ? -0.296  -4.156  -3.029  1.00 34.16  ? 183 ARG B N   1 
ATOM   4613 C CA  . ARG B 1 154 ? -1.223  -4.835  -3.930  1.00 35.35  ? 183 ARG B CA  1 
ATOM   4614 C C   . ARG B 1 154 ? -2.349  -3.869  -4.297  1.00 35.08  ? 183 ARG B C   1 
ATOM   4615 O O   . ARG B 1 154 ? -2.762  -3.783  -5.455  1.00 33.87  ? 183 ARG B O   1 
ATOM   4616 C CB  . ARG B 1 154 ? -1.777  -6.125  -3.310  1.00 41.81  ? 183 ARG B CB  1 
ATOM   4617 C CG  . ARG B 1 154 ? -0.815  -7.306  -3.406  1.00 56.53  ? 183 ARG B CG  1 
ATOM   4618 C CD  . ARG B 1 154 ? -1.410  -8.706  -3.111  1.00 61.25  ? 183 ARG B CD  1 
ATOM   4619 N NE  . ARG B 1 154 ? -1.903  -8.895  -1.736  1.00 66.22  ? 183 ARG B NE  1 
ATOM   4620 C CZ  . ARG B 1 154 ? -1.162  -9.146  -0.642  1.00 71.23  ? 183 ARG B CZ  1 
ATOM   4621 N NH1 . ARG B 1 154 ? -1.735  -9.186  0.555   1.00 63.21  ? 183 ARG B NH1 1 
ATOM   4622 N NH2 . ARG B 1 154 ? 0.147   -9.340  -0.743  1.00 70.48  ? 183 ARG B NH2 1 
ATOM   4623 N N   . ALA B 1 155 ? -2.869  -3.133  -3.302  1.00 33.05  ? 184 ALA B N   1 
ATOM   4624 C CA  . ALA B 1 155 ? -3.931  -2.183  -3.620  1.00 36.61  ? 184 ALA B CA  1 
ATOM   4625 C C   . ALA B 1 155 ? -3.403  -1.149  -4.626  1.00 34.75  ? 184 ALA B C   1 
ATOM   4626 O O   . ALA B 1 155 ? -4.085  -0.806  -5.599  1.00 32.18  ? 184 ALA B O   1 
ATOM   4627 C CB  . ALA B 1 155 ? -4.475  -1.566  -2.363  1.00 32.37  ? 184 ALA B CB  1 
ATOM   4628 N N   . TYR B 1 156 ? -2.140  -0.718  -4.459  1.00 31.94  ? 185 TYR B N   1 
ATOM   4629 C CA  . TYR B 1 156 ? -1.615  0.327   -5.341  1.00 33.86  ? 185 TYR B CA  1 
ATOM   4630 C C   . TYR B 1 156 ? -1.588  -0.153  -6.784  1.00 32.05  ? 185 TYR B C   1 
ATOM   4631 O O   . TYR B 1 156 ? -1.908  0.583   -7.713  1.00 36.54  ? 185 TYR B O   1 
ATOM   4632 C CB  . TYR B 1 156 ? -0.196  0.796   -5.016  1.00 34.30  ? 185 TYR B CB  1 
ATOM   4633 C CG  . TYR B 1 156 ? 0.238   2.010   -5.824  1.00 32.27  ? 185 TYR B CG  1 
ATOM   4634 C CD1 . TYR B 1 156 ? 0.860   1.882   -7.068  1.00 33.14  ? 185 TYR B CD1 1 
ATOM   4635 C CD2 . TYR B 1 156 ? 0.036   3.293   -5.315  1.00 31.38  ? 185 TYR B CD2 1 
ATOM   4636 C CE1 . TYR B 1 156 ? 1.240   2.997   -7.794  1.00 31.31  ? 185 TYR B CE1 1 
ATOM   4637 C CE2 . TYR B 1 156 ? 0.418   4.408   -6.038  1.00 31.89  ? 185 TYR B CE2 1 
ATOM   4638 C CZ  . TYR B 1 156 ? 1.052   4.254   -7.247  1.00 31.15  ? 185 TYR B CZ  1 
ATOM   4639 O OH  . TYR B 1 156 ? 1.418   5.392   -7.888  1.00 40.25  ? 185 TYR B OH  1 
ATOM   4640 N N   . ALA B 1 157 ? -1.230  -1.420  -6.948  1.00 37.95  ? 186 ALA B N   1 
ATOM   4641 C CA  . ALA B 1 157 ? -1.138  -2.052  -8.249  1.00 36.01  ? 186 ALA B CA  1 
ATOM   4642 C C   . ALA B 1 157 ? -2.507  -2.070  -8.934  1.00 41.08  ? 186 ALA B C   1 
ATOM   4643 O O   . ALA B 1 157 ? -2.597  -1.934  -10.145 1.00 41.20  ? 186 ALA B O   1 
ATOM   4644 C CB  . ALA B 1 157 ? -0.575  -3.438  -8.034  1.00 37.55  ? 186 ALA B CB  1 
ATOM   4645 N N   . GLN B 1 158 ? -3.578  -2.190  -8.148  1.00 37.79  ? 187 GLN B N   1 
ATOM   4646 C CA  . GLN B 1 158 ? -4.935  -2.237  -8.678  1.00 37.39  ? 187 GLN B CA  1 
ATOM   4647 C C   . GLN B 1 158 ? -5.555  -0.857  -8.921  1.00 35.54  ? 187 GLN B C   1 
ATOM   4648 O O   . GLN B 1 158 ? -6.681  -0.787  -9.399  1.00 36.35  ? 187 GLN B O   1 
ATOM   4649 C CB  . GLN B 1 158 ? -5.802  -2.986  -7.676  1.00 38.26  ? 187 GLN B CB  1 
ATOM   4650 C CG  . GLN B 1 158 ? -5.314  -4.395  -7.370  1.00 41.51  ? 187 GLN B CG  1 
ATOM   4651 C CD  . GLN B 1 158 ? -6.099  -5.032  -6.245  1.00 49.85  ? 187 GLN B CD  1 
ATOM   4652 O OE1 . GLN B 1 158 ? -6.501  -4.374  -5.277  1.00 51.59  ? 187 GLN B OE1 1 
ATOM   4653 N NE2 . GLN B 1 158 ? -6.379  -6.319  -6.379  1.00 58.79  ? 187 GLN B NE2 1 
ATOM   4654 N N   . GLY B 1 159 ? -4.891  0.243   -8.520  1.00 32.91  ? 188 GLY B N   1 
ATOM   4655 C CA  . GLY B 1 159 ? -5.328  1.598   -8.833  1.00 28.77  ? 188 GLY B CA  1 
ATOM   4656 C C   . GLY B 1 159 ? -6.250  2.223   -7.776  1.00 33.97  ? 188 GLY B C   1 
ATOM   4657 O O   . GLY B 1 159 ? -7.159  3.007   -8.101  1.00 37.61  ? 188 GLY B O   1 
ATOM   4658 N N   . ILE B 1 160 ? -6.005  1.906   -6.502  1.00 28.24  ? 189 ILE B N   1 
ATOM   4659 C CA  . ILE B 1 160 ? -6.777  2.429   -5.391  1.00 29.55  ? 189 ILE B CA  1 
ATOM   4660 C C   . ILE B 1 160 ? -6.657  3.943   -5.382  1.00 28.54  ? 189 ILE B C   1 
ATOM   4661 O O   . ILE B 1 160 ? -5.620  4.494   -5.763  1.00 28.64  ? 189 ILE B O   1 
ATOM   4662 C CB  . ILE B 1 160 ? -6.318  1.795   -4.052  1.00 36.00  ? 189 ILE B CB  1 
ATOM   4663 C CG1 . ILE B 1 160 ? -7.305  2.062   -2.895  1.00 39.08  ? 189 ILE B CG1 1 
ATOM   4664 C CG2 . ILE B 1 160 ? -4.898  2.240   -3.642  1.00 32.67  ? 189 ILE B CG2 1 
ATOM   4665 C CD1 . ILE B 1 160 ? -8.591  1.281   -2.973  1.00 42.03  ? 189 ILE B CD1 1 
ATOM   4666 N N   . SER B 1 161 ? -7.735  4.613   -4.937  1.00 25.19  ? 190 SER B N   1 
ATOM   4667 C CA  . SER B 1 161 ? -7.753  6.066   -4.806  1.00 25.50  ? 190 SER B CA  1 
ATOM   4668 C C   . SER B 1 161 ? -6.716  6.515   -3.787  1.00 24.02  ? 190 SER B C   1 
ATOM   4669 O O   . SER B 1 161 ? -6.562  5.883   -2.739  1.00 26.03  ? 190 SER B O   1 
ATOM   4670 C CB  . SER B 1 161 ? -9.131  6.530   -4.390  1.00 24.01  ? 190 SER B CB  1 
ATOM   4671 O OG  . SER B 1 161 ? -9.105  7.828   -3.814  1.00 24.95  ? 190 SER B OG  1 
ATOM   4672 N N   . ARG B 1 162 ? -6.067  7.634   -4.066  1.00 27.82  ? 191 ARG B N   1 
ATOM   4673 C CA  . ARG B 1 162 ? -5.125  8.277   -3.164  1.00 32.23  ? 191 ARG B CA  1 
ATOM   4674 C C   . ARG B 1 162 ? -5.761  8.490   -1.785  1.00 28.95  ? 191 ARG B C   1 
ATOM   4675 O O   . ARG B 1 162 ? -5.061  8.481   -0.791  1.00 27.45  ? 191 ARG B O   1 
ATOM   4676 C CB  . ARG B 1 162 ? -4.742  9.692   -3.633  1.00 37.39  ? 191 ARG B CB  1 
ATOM   4677 C CG  . ARG B 1 162 ? -3.798  9.783   -4.821  1.00 54.05  ? 191 ARG B CG  1 
ATOM   4678 C CD  . ARG B 1 162 ? -3.420  11.232  -5.119  1.00 67.14  ? 191 ARG B CD  1 
ATOM   4679 N NE  . ARG B 1 162 ? -2.169  11.367  -5.882  1.00 82.04  ? 191 ARG B NE  1 
ATOM   4680 C CZ  . ARG B 1 162 ? -1.631  12.529  -6.289  1.00 96.86  ? 191 ARG B CZ  1 
ATOM   4681 N NH1 . ARG B 1 162 ? -2.211  13.685  -6.010  1.00 102.24 ? 191 ARG B NH1 1 
ATOM   4682 N NH2 . ARG B 1 162 ? -0.506  12.542  -6.983  1.00 101.07 ? 191 ARG B NH2 1 
ATOM   4683 N N   . THR B 1 163 ? -7.076  8.754   -1.736  1.00 26.35  ? 192 THR B N   1 
ATOM   4684 C CA  . THR B 1 163 ? -7.755  9.097   -0.497  1.00 29.43  ? 192 THR B CA  1 
ATOM   4685 C C   . THR B 1 163 ? -7.720  7.909   0.461   1.00 27.33  ? 192 THR B C   1 
ATOM   4686 O O   . THR B 1 163 ? -8.114  8.028   1.619   1.00 28.68  ? 192 THR B O   1 
ATOM   4687 C CB  . THR B 1 163 ? -9.216  9.496   -0.802  1.00 28.93  ? 192 THR B CB  1 
ATOM   4688 O OG1 . THR B 1 163 ? -9.873  8.366   -1.387  1.00 23.93  ? 192 THR B OG1 1 
ATOM   4689 C CG2 . THR B 1 163 ? -9.321  10.704  -1.703  1.00 30.15  ? 192 THR B CG2 1 
ATOM   4690 N N   . LYS B 1 164 ? -7.396  6.726   -0.068  1.00 24.80  ? 193 LYS B N   1 
ATOM   4691 C CA  . LYS B 1 164 ? -7.404  5.496   0.691   1.00 30.29  ? 193 LYS B CA  1 
ATOM   4692 C C   . LYS B 1 164 ? -6.010  4.980   1.067   1.00 25.40  ? 193 LYS B C   1 
ATOM   4693 O O   . LYS B 1 164 ? -5.903  4.008   1.823   1.00 24.03  ? 193 LYS B O   1 
ATOM   4694 C CB  . LYS B 1 164 ? -8.089  4.426   -0.158  1.00 34.96  ? 193 LYS B CB  1 
ATOM   4695 C CG  . LYS B 1 164 ? -9.563  4.712   -0.290  1.00 42.61  ? 193 LYS B CG  1 
ATOM   4696 C CD  . LYS B 1 164 ? -10.354 4.163   0.883   1.00 51.65  ? 193 LYS B CD  1 
ATOM   4697 C CE  . LYS B 1 164 ? -10.640 2.669   0.715   1.00 48.39  ? 193 LYS B CE  1 
ATOM   4698 N NZ  . LYS B 1 164 ? -11.430 2.183   1.855   1.00 46.59  ? 193 LYS B NZ  1 
ATOM   4699 N N   . TYR B 1 165 ? -4.947  5.602   0.555   1.00 22.55  ? 194 TYR B N   1 
ATOM   4700 C CA  . TYR B 1 165 ? -3.608  5.143   0.861   1.00 23.00  ? 194 TYR B CA  1 
ATOM   4701 C C   . TYR B 1 165 ? -3.416  4.924   2.358   1.00 22.55  ? 194 TYR B C   1 
ATOM   4702 O O   . TYR B 1 165 ? -2.890  3.906   2.743   1.00 28.24  ? 194 TYR B O   1 
ATOM   4703 C CB  . TYR B 1 165 ? -2.518  6.101   0.357   1.00 22.58  ? 194 TYR B CB  1 
ATOM   4704 C CG  . TYR B 1 165 ? -2.355  6.170   -1.155  1.00 21.83  ? 194 TYR B CG  1 
ATOM   4705 C CD1 . TYR B 1 165 ? -2.997  5.285   -1.998  1.00 23.11  ? 194 TYR B CD1 1 
ATOM   4706 C CD2 . TYR B 1 165 ? -1.461  7.076   -1.731  1.00 24.70  ? 194 TYR B CD2 1 
ATOM   4707 C CE1 . TYR B 1 165 ? -2.857  5.373   -3.380  1.00 25.55  ? 194 TYR B CE1 1 
ATOM   4708 C CE2 . TYR B 1 165 ? -1.308  7.166   -3.101  1.00 25.68  ? 194 TYR B CE2 1 
ATOM   4709 C CZ  . TYR B 1 165 ? -2.005  6.315   -3.921  1.00 27.25  ? 194 TYR B CZ  1 
ATOM   4710 O OH  . TYR B 1 165 ? -1.864  6.391   -5.260  1.00 31.87  ? 194 TYR B OH  1 
ATOM   4711 N N   . TRP B 1 166 ? -3.753  5.888   3.195   1.00 22.95  ? 195 TRP B N   1 
ATOM   4712 C CA  . TRP B 1 166 ? -3.502  5.779   4.623   1.00 23.89  ? 195 TRP B CA  1 
ATOM   4713 C C   . TRP B 1 166 ? -4.106  4.510   5.224   1.00 22.59  ? 195 TRP B C   1 
ATOM   4714 O O   . TRP B 1 166 ? -3.584  4.056   6.237   1.00 20.33  ? 195 TRP B O   1 
ATOM   4715 C CB  . TRP B 1 166 ? -3.991  7.027   5.368   1.00 23.80  ? 195 TRP B CB  1 
ATOM   4716 C CG  . TRP B 1 166 ? -5.488  7.053   5.567   1.00 23.80  ? 195 TRP B CG  1 
ATOM   4717 C CD1 . TRP B 1 166 ? -6.420  7.650   4.762   1.00 28.02  ? 195 TRP B CD1 1 
ATOM   4718 C CD2 . TRP B 1 166 ? -6.220  6.508   6.696   1.00 22.52  ? 195 TRP B CD2 1 
ATOM   4719 N NE1 . TRP B 1 166 ? -7.679  7.471   5.287   1.00 26.50  ? 195 TRP B NE1 1 
ATOM   4720 C CE2 . TRP B 1 166 ? -7.590  6.790   6.477   1.00 24.63  ? 195 TRP B CE2 1 
ATOM   4721 C CE3 . TRP B 1 166 ? -5.847  5.826   7.855   1.00 21.08  ? 195 TRP B CE3 1 
ATOM   4722 C CZ2 . TRP B 1 166 ? -8.588  6.410   7.385   1.00 24.60  ? 195 TRP B CZ2 1 
ATOM   4723 C CZ3 . TRP B 1 166 ? -6.825  5.438   8.746   1.00 23.72  ? 195 TRP B CZ3 1 
ATOM   4724 C CH2 . TRP B 1 166 ? -8.181  5.740   8.514   1.00 24.13  ? 195 TRP B CH2 1 
ATOM   4725 N N   . GLU B 1 167 ? -5.228  3.990   4.687   1.00 22.03  ? 196 GLU B N   1 
ATOM   4726 C CA  . GLU B 1 167 ? -5.874  2.832   5.277   1.00 24.81  ? 196 GLU B CA  1 
ATOM   4727 C C   . GLU B 1 167 ? -5.005  1.576   5.126   1.00 25.41  ? 196 GLU B C   1 
ATOM   4728 O O   . GLU B 1 167 ? -4.875  0.759   6.030   1.00 25.30  ? 196 GLU B O   1 
ATOM   4729 C CB  . GLU B 1 167 ? -7.272  2.617   4.676   1.00 26.05  ? 196 GLU B CB  1 
ATOM   4730 C CG  . GLU B 1 167 ? -8.252  3.707   5.086   1.00 30.29  ? 196 GLU B CG  1 
ATOM   4731 C CD  . GLU B 1 167 ? -9.659  3.478   4.561   1.00 38.33  ? 196 GLU B CD  1 
ATOM   4732 O OE1 . GLU B 1 167 ? -10.448 4.406   4.490   1.00 42.26  ? 196 GLU B OE1 1 
ATOM   4733 O OE2 . GLU B 1 167 ? -9.915  2.349   4.161   1.00 48.42  ? 196 GLU B OE2 1 
ATOM   4734 N N   . LEU B 1 168 ? -4.427  1.401   3.952   1.00 22.12  ? 197 LEU B N   1 
ATOM   4735 C CA  . LEU B 1 168 ? -3.644  0.221   3.682   1.00 24.49  ? 197 LEU B CA  1 
ATOM   4736 C C   . LEU B 1 168 ? -2.285  0.384   4.372   1.00 20.62  ? 197 LEU B C   1 
ATOM   4737 O O   . LEU B 1 168 ? -1.711  -0.599  4.781   1.00 22.60  ? 197 LEU B O   1 
ATOM   4738 C CB  . LEU B 1 168 ? -3.471  0.066   2.174   1.00 25.80  ? 197 LEU B CB  1 
ATOM   4739 C CG  . LEU B 1 168 ? -4.721  -0.223  1.351   1.00 33.26  ? 197 LEU B CG  1 
ATOM   4740 C CD1 . LEU B 1 168 ? -5.332  -1.581  1.662   1.00 30.73  ? 197 LEU B CD1 1 
ATOM   4741 C CD2 . LEU B 1 168 ? -5.731  0.898   1.494   1.00 38.18  ? 197 LEU B CD2 1 
ATOM   4742 N N   . ILE B 1 169 ? -1.772  1.612   4.466   1.00 21.07  ? 198 ILE B N   1 
ATOM   4743 C CA  . ILE B 1 169 ? -0.568  1.907   5.246   1.00 22.53  ? 198 ILE B CA  1 
ATOM   4744 C C   . ILE B 1 169 ? -0.805  1.553   6.715   1.00 21.03  ? 198 ILE B C   1 
ATOM   4745 O O   . ILE B 1 169 ? 0.036   0.929   7.368   1.00 21.62  ? 198 ILE B O   1 
ATOM   4746 C CB  . ILE B 1 169 ? -0.133  3.383   5.109   1.00 24.70  ? 198 ILE B CB  1 
ATOM   4747 C CG1 . ILE B 1 169 ? 0.244   3.725   3.700   1.00 27.13  ? 198 ILE B CG1 1 
ATOM   4748 C CG2 . ILE B 1 169 ? 0.991   3.733   6.073   1.00 26.65  ? 198 ILE B CG2 1 
ATOM   4749 C CD1 . ILE B 1 169 ? 1.419   2.958   3.138   1.00 29.05  ? 198 ILE B CD1 1 
ATOM   4750 N N   . TYR B 1 170 ? -1.974  1.927   7.210   1.00 21.65  ? 199 TYR B N   1 
ATOM   4751 C CA  . TYR B 1 170 ? -2.370  1.590   8.568   1.00 22.15  ? 199 TYR B CA  1 
ATOM   4752 C C   . TYR B 1 170 ? -2.315  0.064   8.757   1.00 21.07  ? 199 TYR B C   1 
ATOM   4753 O O   . TYR B 1 170 ? -1.733  -0.403  9.747   1.00 18.42  ? 199 TYR B O   1 
ATOM   4754 C CB  . TYR B 1 170 ? -3.702  2.270   8.956   1.00 23.02  ? 199 TYR B CB  1 
ATOM   4755 C CG  . TYR B 1 170 ? -4.352  1.682   10.211  1.00 21.06  ? 199 TYR B CG  1 
ATOM   4756 C CD1 . TYR B 1 170 ? -5.170  0.544   10.125  1.00 24.08  ? 199 TYR B CD1 1 
ATOM   4757 C CD2 . TYR B 1 170 ? -4.191  2.241   11.457  1.00 24.73  ? 199 TYR B CD2 1 
ATOM   4758 C CE1 . TYR B 1 170 ? -5.766  -0.022  11.242  1.00 21.08  ? 199 TYR B CE1 1 
ATOM   4759 C CE2 . TYR B 1 170 ? -4.785  1.688   12.584  1.00 22.12  ? 199 TYR B CE2 1 
ATOM   4760 C CZ  . TYR B 1 170 ? -5.583  0.550   12.474  1.00 23.23  ? 199 TYR B CZ  1 
ATOM   4761 O OH  . TYR B 1 170 ? -6.200  -0.040  13.561  1.00 23.82  ? 199 TYR B OH  1 
ATOM   4762 N N   . GLU B 1 171 ? -3.003  -0.695  7.889   1.00 23.34  ? 200 GLU B N   1 
ATOM   4763 C CA  . GLU B 1 171 ? -3.077  -2.152  8.005   1.00 23.31  ? 200 GLU B CA  1 
ATOM   4764 C C   . GLU B 1 171 ? -1.688  -2.790  7.982   1.00 20.98  ? 200 GLU B C   1 
ATOM   4765 O O   . GLU B 1 171 ? -1.412  -3.663  8.784   1.00 21.30  ? 200 GLU B O   1 
ATOM   4766 C CB  . GLU B 1 171 ? -3.953  -2.813  6.945   1.00 24.46  ? 200 GLU B CB  1 
ATOM   4767 C CG  . GLU B 1 171 ? -5.423  -2.457  7.118   1.00 24.22  ? 200 GLU B CG  1 
ATOM   4768 C CD  . GLU B 1 171 ? -6.076  -2.939  8.400   1.00 25.06  ? 200 GLU B CD  1 
ATOM   4769 O OE1 . GLU B 1 171 ? -7.083  -2.295  8.765   1.00 28.81  ? 200 GLU B OE1 1 
ATOM   4770 O OE2 . GLU B 1 171 ? -5.656  -3.928  9.010   1.00 27.66  ? 200 GLU B OE2 1 
ATOM   4771 N N   . ASP B 1 172 ? -0.864  -2.414  7.008   1.00 19.97  ? 201 ASP B N   1 
ATOM   4772 C CA  . ASP B 1 172 ? 0.467   -2.953  6.887   1.00 20.51  ? 201 ASP B CA  1 
ATOM   4773 C C   . ASP B 1 172 ? 1.292   -2.605  8.132   1.00 19.69  ? 201 ASP B C   1 
ATOM   4774 O O   . ASP B 1 172 ? 2.162   -3.381  8.488   1.00 19.99  ? 201 ASP B O   1 
ATOM   4775 C CB  . ASP B 1 172 ? 1.173   -2.525  5.609   1.00 22.43  ? 201 ASP B CB  1 
ATOM   4776 C CG  . ASP B 1 172 ? 0.686   -3.188  4.335   1.00 24.53  ? 201 ASP B CG  1 
ATOM   4777 O OD1 . ASP B 1 172 ? -0.141  -4.108  4.479   1.00 28.48  ? 201 ASP B OD1 1 
ATOM   4778 O OD2 . ASP B 1 172 ? 1.166   -2.829  3.225   1.00 23.69  ? 201 ASP B OD2 1 
ATOM   4779 N N   . SER B 1 173 ? 1.099   -1.414  8.708   1.00 23.03  ? 202 SER B N   1 
ATOM   4780 C CA  . SER B 1 173 ? 1.923   -0.943  9.812   1.00 21.79  ? 202 SER B CA  1 
ATOM   4781 C C   . SER B 1 173 ? 1.550   -1.726  11.062  1.00 22.62  ? 202 SER B C   1 
ATOM   4782 O O   . SER B 1 173 ? 2.408   -2.086  11.859  1.00 20.80  ? 202 SER B O   1 
ATOM   4783 C CB  . SER B 1 173 ? 1.808   0.537   10.083  1.00 21.42  ? 202 SER B CB  1 
ATOM   4784 O OG  . SER B 1 173 ? 2.291   1.327   9.006   1.00 23.35  ? 202 SER B OG  1 
ATOM   4785 N N   . MET B 1 174 ? 0.237   -1.921  11.272  1.00 22.45  ? 203 MET B N   1 
ATOM   4786 C CA  . MET B 1 174 ? -0.260  -2.787  12.340  1.00 23.95  ? 203 MET B CA  1 
ATOM   4787 C C   . MET B 1 174 ? 0.263   -4.222  12.228  1.00 22.34  ? 203 MET B C   1 
ATOM   4788 O O   . MET B 1 174 ? 0.665   -4.826  13.226  1.00 22.31  ? 203 MET B O   1 
ATOM   4789 C CB  . MET B 1 174 ? -1.799  -2.787  12.345  1.00 22.06  ? 203 MET B CB  1 
ATOM   4790 C CG  . MET B 1 174 ? -2.367  -1.440  12.765  1.00 22.83  ? 203 MET B CG  1 
ATOM   4791 S SD  . MET B 1 174 ? -2.341  -0.926  14.488  1.00 24.40  ? 203 MET B SD  1 
ATOM   4792 C CE  . MET B 1 174 ? -3.717  -1.971  15.024  1.00 25.32  ? 203 MET B CE  1 
ATOM   4793 N N   . ASP B 1 175 ? 0.251   -4.771  11.007  1.00 23.33  ? 204 ASP B N   1 
ATOM   4794 C CA  . ASP B 1 175 ? 0.784   -6.088  10.754  1.00 18.91  ? 204 ASP B CA  1 
ATOM   4795 C C   . ASP B 1 175 ? 2.281   -6.127  11.092  1.00 19.74  ? 204 ASP B C   1 
ATOM   4796 O O   . ASP B 1 175 ? 2.748   -7.071  11.704  1.00 19.10  ? 204 ASP B O   1 
ATOM   4797 C CB  . ASP B 1 175 ? 0.562   -6.486  9.303   1.00 23.04  ? 204 ASP B CB  1 
ATOM   4798 C CG  . ASP B 1 175 ? -0.883  -6.882  8.980   1.00 30.54  ? 204 ASP B CG  1 
ATOM   4799 O OD1 . ASP B 1 175 ? -1.656  -7.047  9.956   1.00 27.62  ? 204 ASP B OD1 1 
ATOM   4800 O OD2 . ASP B 1 175 ? -1.235  -6.976  7.777   1.00 27.07  ? 204 ASP B OD2 1 
ATOM   4801 N N   . LEU B 1 176 ? 3.019   -5.075  10.711  1.00 19.90  ? 205 LEU B N   1 
ATOM   4802 C CA  . LEU B 1 176 ? 4.456   -5.100  10.866  1.00 17.32  ? 205 LEU B CA  1 
ATOM   4803 C C   . LEU B 1 176 ? 4.784   -5.077  12.354  1.00 18.36  ? 205 LEU B C   1 
ATOM   4804 O O   . LEU B 1 176 ? 5.668   -5.815  12.786  1.00 18.58  ? 205 LEU B O   1 
ATOM   4805 C CB  . LEU B 1 176 ? 5.095   -3.965  10.075  1.00 18.28  ? 205 LEU B CB  1 
ATOM   4806 C CG  . LEU B 1 176 ? 6.597   -3.754  10.310  1.00 20.62  ? 205 LEU B CG  1 
ATOM   4807 C CD1 . LEU B 1 176 ? 7.452   -4.935  10.194  1.00 24.14  ? 205 LEU B CD1 1 
ATOM   4808 C CD2 . LEU B 1 176 ? 7.057   -2.695  9.304   1.00 24.56  ? 205 LEU B CD2 1 
ATOM   4809 N N   . ILE B 1 177 ? 4.221   -4.100  13.073  1.00 20.75  ? 206 ILE B N   1 
ATOM   4810 C CA  . ILE B 1 177 ? 4.454   -3.910  14.495  1.00 20.36  ? 206 ILE B CA  1 
ATOM   4811 C C   . ILE B 1 177 ? 4.150   -5.222  15.230  1.00 21.45  ? 206 ILE B C   1 
ATOM   4812 O O   . ILE B 1 177 ? 4.930   -5.633  16.083  1.00 21.00  ? 206 ILE B O   1 
ATOM   4813 C CB  . ILE B 1 177 ? 3.646   -2.733  15.063  1.00 20.40  ? 206 ILE B CB  1 
ATOM   4814 C CG1 . ILE B 1 177 ? 4.165   -1.413  14.548  1.00 22.31  ? 206 ILE B CG1 1 
ATOM   4815 C CG2 . ILE B 1 177 ? 3.660   -2.757  16.594  1.00 20.97  ? 206 ILE B CG2 1 
ATOM   4816 C CD1 . ILE B 1 177 ? 3.201   -0.263  14.761  1.00 25.73  ? 206 ILE B CD1 1 
ATOM   4817 N N   . ALA B 1 178 ? 3.068   -5.903  14.849  1.00 23.02  ? 207 ALA B N   1 
ATOM   4818 C CA  . ALA B 1 178 ? 2.705   -7.165  15.486  1.00 24.10  ? 207 ALA B CA  1 
ATOM   4819 C C   . ALA B 1 178 ? 3.724   -8.268  15.197  1.00 24.75  ? 207 ALA B C   1 
ATOM   4820 O O   . ALA B 1 178 ? 3.940   -9.143  16.029  1.00 25.14  ? 207 ALA B O   1 
ATOM   4821 C CB  . ALA B 1 178 ? 1.330   -7.575  15.033  1.00 24.20  ? 207 ALA B CB  1 
ATOM   4822 N N   . LYS B 1 179 ? 4.357   -8.229  14.025  1.00 20.64  ? 208 LYS B N   1 
ATOM   4823 C CA  . LYS B 1 179 ? 5.289   -9.257  13.606  1.00 22.44  ? 208 LYS B CA  1 
ATOM   4824 C C   . LYS B 1 179 ? 6.707   -9.069  14.145  1.00 20.96  ? 208 LYS B C   1 
ATOM   4825 O O   . LYS B 1 179 ? 7.430   -10.045 14.311  1.00 20.36  ? 208 LYS B O   1 
ATOM   4826 C CB  . LYS B 1 179 ? 5.256   -9.383  12.077  1.00 22.76  ? 208 LYS B CB  1 
ATOM   4827 C CG  . LYS B 1 179 ? 3.923   -9.987  11.627  1.00 27.20  ? 208 LYS B CG  1 
ATOM   4828 C CD  . LYS B 1 179 ? 3.608   -9.905  10.147  1.00 35.99  ? 208 LYS B CD  1 
ATOM   4829 C CE  . LYS B 1 179 ? 2.116   -10.139 9.945   1.00 39.66  ? 208 LYS B CE  1 
ATOM   4830 N NZ  . LYS B 1 179 ? 1.859   -10.114 8.517   1.00 52.59  ? 208 LYS B NZ  1 
ATOM   4831 N N   . LEU B 1 180 ? 7.094   -7.835  14.412  1.00 19.74  ? 209 LEU B N   1 
ATOM   4832 C CA  . LEU B 1 180 ? 8.459   -7.486  14.721  1.00 20.85  ? 209 LEU B CA  1 
ATOM   4833 C C   . LEU B 1 180 ? 9.007   -8.245  15.921  1.00 24.04  ? 209 LEU B C   1 
ATOM   4834 O O   . LEU B 1 180 ? 10.125  -8.740  15.835  1.00 22.11  ? 209 LEU B O   1 
ATOM   4835 C CB  . LEU B 1 180 ? 8.588   -5.977  14.938  1.00 19.81  ? 209 LEU B CB  1 
ATOM   4836 C CG  . LEU B 1 180 ? 8.829   -5.174  13.660  1.00 21.11  ? 209 LEU B CG  1 
ATOM   4837 C CD1 . LEU B 1 180 ? 8.628   -3.708  13.915  1.00 22.41  ? 209 LEU B CD1 1 
ATOM   4838 C CD2 . LEU B 1 180 ? 10.222  -5.508  13.206  1.00 21.30  ? 209 LEU B CD2 1 
ATOM   4839 N N   . PRO B 1 181 ? 8.286   -8.332  17.068  1.00 24.86  ? 210 PRO B N   1 
ATOM   4840 C CA  . PRO B 1 181 ? 8.751   -9.151  18.182  1.00 24.87  ? 210 PRO B CA  1 
ATOM   4841 C C   . PRO B 1 181 ? 9.060   -10.614 17.803  1.00 27.19  ? 210 PRO B C   1 
ATOM   4842 O O   . PRO B 1 181 ? 10.041  -11.177 18.288  1.00 26.11  ? 210 PRO B O   1 
ATOM   4843 C CB  . PRO B 1 181 ? 7.601   -9.037  19.166  1.00 28.76  ? 210 PRO B CB  1 
ATOM   4844 C CG  . PRO B 1 181 ? 6.884   -7.774  18.818  1.00 29.96  ? 210 PRO B CG  1 
ATOM   4845 C CD  . PRO B 1 181 ? 7.012   -7.644  17.320  1.00 26.49  ? 210 PRO B CD  1 
ATOM   4846 N N   . CYS B 1 182 ? 8.246   -11.199 16.903  1.00 26.50  ? 211 CYS B N   1 
ATOM   4847 C CA  . CYS B 1 182 ? 8.427   -12.548 16.376  1.00 26.27  ? 211 CYS B CA  1 
ATOM   4848 C C   . CYS B 1 182 ? 9.742   -12.669 15.595  1.00 26.39  ? 211 CYS B C   1 
ATOM   4849 O O   . CYS B 1 182 ? 10.577  -13.531 15.877  1.00 24.74  ? 211 CYS B O   1 
ATOM   4850 C CB  . CYS B 1 182 ? 7.223   -12.955 15.531  1.00 27.53  ? 211 CYS B CB  1 
ATOM   4851 S SG  . CYS B 1 182 ? 5.680   -13.022 16.498  1.00 37.20  ? 211 CYS B SG  1 
ATOM   4852 N N   . VAL B 1 183 ? 9.927   -11.772 14.626  1.00 22.79  ? 212 VAL B N   1 
ATOM   4853 C CA  . VAL B 1 183 ? 11.182  -11.659 13.903  1.00 22.35  ? 212 VAL B CA  1 
ATOM   4854 C C   . VAL B 1 183 ? 12.364  -11.434 14.852  1.00 19.62  ? 212 VAL B C   1 
ATOM   4855 O O   . VAL B 1 183 ? 13.386  -12.094 14.750  1.00 20.87  ? 212 VAL B O   1 
ATOM   4856 C CB  . VAL B 1 183 ? 11.111  -10.554 12.842  1.00 20.76  ? 212 VAL B CB  1 
ATOM   4857 C CG1 . VAL B 1 183 ? 12.472  -10.336 12.202  1.00 20.12  ? 212 VAL B CG1 1 
ATOM   4858 C CG2 . VAL B 1 183 ? 10.053  -10.847 11.799  1.00 21.68  ? 212 VAL B CG2 1 
ATOM   4859 N N   . ALA B 1 184 ? 12.287  -10.427 15.701  1.00 17.75  ? 213 ALA B N   1 
ATOM   4860 C CA  . ALA B 1 184 ? 13.385  -10.088 16.568  1.00 20.33  ? 213 ALA B CA  1 
ATOM   4861 C C   . ALA B 1 184 ? 13.728  -11.252 17.521  1.00 20.59  ? 213 ALA B C   1 
ATOM   4862 O O   . ALA B 1 184 ? 14.896  -11.466 17.824  1.00 19.81  ? 213 ALA B O   1 
ATOM   4863 C CB  . ALA B 1 184 ? 13.060  -8.842  17.319  1.00 20.66  ? 213 ALA B CB  1 
ATOM   4864 N N   . ALA B 1 185 ? 12.697  -11.979 18.000  1.00 20.71  ? 214 ALA B N   1 
ATOM   4865 C CA  . ALA B 1 185 ? 12.895  -13.079 18.917  1.00 22.27  ? 214 ALA B CA  1 
ATOM   4866 C C   . ALA B 1 185 ? 13.524  -14.256 18.194  1.00 21.66  ? 214 ALA B C   1 
ATOM   4867 O O   . ALA B 1 185 ? 14.415  -14.869 18.759  1.00 26.37  ? 214 ALA B O   1 
ATOM   4868 C CB  . ALA B 1 185 ? 11.601  -13.462 19.553  1.00 25.46  ? 214 ALA B CB  1 
ATOM   4869 N N   . LYS B 1 186 ? 13.070  -14.557 16.957  1.00 24.58  ? 215 LYS B N   1 
ATOM   4870 C CA  . LYS B 1 186 ? 13.681  -15.590 16.138  1.00 27.02  ? 215 LYS B CA  1 
ATOM   4871 C C   . LYS B 1 186 ? 15.163  -15.327 15.921  1.00 24.22  ? 215 LYS B C   1 
ATOM   4872 O O   . LYS B 1 186 ? 15.973  -16.258 15.994  1.00 20.91  ? 215 LYS B O   1 
ATOM   4873 C CB  . LYS B 1 186 ? 13.035  -15.737 14.759  1.00 30.92  ? 215 LYS B CB  1 
ATOM   4874 C CG  . LYS B 1 186 ? 13.188  -17.110 14.123  1.00 40.05  ? 215 LYS B CG  1 
ATOM   4875 C CD  . LYS B 1 186 ? 11.946  -18.014 14.170  1.00 43.70  ? 215 LYS B CD  1 
ATOM   4876 C CE  . LYS B 1 186 ? 12.277  -19.492 14.382  1.00 40.87  ? 215 LYS B CE  1 
ATOM   4877 N N   . ILE B 1 187 ? 15.536  -14.072 15.614  1.00 21.84  ? 216 ILE B N   1 
ATOM   4878 C CA  . ILE B 1 187 ? 16.960  -13.736 15.467  1.00 18.43  ? 216 ILE B CA  1 
ATOM   4879 C C   . ILE B 1 187 ? 17.726  -14.005 16.764  1.00 21.46  ? 216 ILE B C   1 
ATOM   4880 O O   . ILE B 1 187 ? 18.804  -14.622 16.753  1.00 24.76  ? 216 ILE B O   1 
ATOM   4881 C CB  . ILE B 1 187 ? 17.114  -12.267 15.025  1.00 20.01  ? 216 ILE B CB  1 
ATOM   4882 C CG1 . ILE B 1 187 ? 16.583  -12.053 13.607  1.00 19.69  ? 216 ILE B CG1 1 
ATOM   4883 C CG2 . ILE B 1 187 ? 18.557  -11.789 15.130  1.00 19.86  ? 216 ILE B CG2 1 
ATOM   4884 C CD1 . ILE B 1 187 ? 16.327  -10.589 13.316  1.00 20.36  ? 216 ILE B CD1 1 
ATOM   4885 N N   . TYR B 1 188 ? 17.212  -13.508 17.881  1.00 22.43  ? 217 TYR B N   1 
ATOM   4886 C CA  . TYR B 1 188 ? 17.876  -13.674 19.167  1.00 23.16  ? 217 TYR B CA  1 
ATOM   4887 C C   . TYR B 1 188 ? 18.127  -15.162 19.464  1.00 22.30  ? 217 TYR B C   1 
ATOM   4888 O O   . TYR B 1 188 ? 19.246  -15.541 19.860  1.00 24.27  ? 217 TYR B O   1 
ATOM   4889 C CB  . TYR B 1 188 ? 17.024  -13.044 20.280  1.00 23.47  ? 217 TYR B CB  1 
ATOM   4890 C CG  . TYR B 1 188 ? 17.705  -13.001 21.639  1.00 21.53  ? 217 TYR B CG  1 
ATOM   4891 C CD1 . TYR B 1 188 ? 18.690  -12.043 21.890  1.00 20.92  ? 217 TYR B CD1 1 
ATOM   4892 C CD2 . TYR B 1 188 ? 17.411  -13.922 22.652  1.00 23.85  ? 217 TYR B CD2 1 
ATOM   4893 C CE1 . TYR B 1 188 ? 19.349  -11.965 23.109  1.00 22.74  ? 217 TYR B CE1 1 
ATOM   4894 C CE2 . TYR B 1 188 ? 18.070  -13.863 23.877  1.00 27.11  ? 217 TYR B CE2 1 
ATOM   4895 C CZ  . TYR B 1 188 ? 19.044  -12.875 24.104  1.00 25.21  ? 217 TYR B CZ  1 
ATOM   4896 O OH  . TYR B 1 188 ? 19.744  -12.774 25.266  1.00 29.01  ? 217 TYR B OH  1 
ATOM   4897 N N   . ARG B 1 189 ? 17.074  -15.981 19.296  1.00 22.44  ? 218 ARG B N   1 
ATOM   4898 C CA  . ARG B 1 189 ? 17.100  -17.398 19.623  1.00 24.10  ? 218 ARG B CA  1 
ATOM   4899 C C   . ARG B 1 189 ? 18.010  -18.158 18.678  1.00 26.85  ? 218 ARG B C   1 
ATOM   4900 O O   . ARG B 1 189 ? 18.771  -19.022 19.133  1.00 28.78  ? 218 ARG B O   1 
ATOM   4901 C CB  . ARG B 1 189 ? 15.707  -18.035 19.693  1.00 26.66  ? 218 ARG B CB  1 
ATOM   4902 C CG  . ARG B 1 189 ? 14.970  -17.556 20.936  1.00 31.55  ? 218 ARG B CG  1 
ATOM   4903 C CD  . ARG B 1 189 ? 13.692  -18.284 21.375  1.00 33.39  ? 218 ARG B CD  1 
ATOM   4904 N NE  . ARG B 1 189 ? 14.150  -19.376 22.221  1.00 47.77  ? 218 ARG B NE  1 
ATOM   4905 C CZ  . ARG B 1 189 ? 13.706  -19.684 23.429  1.00 47.00  ? 218 ARG B CZ  1 
ATOM   4906 N NH1 . ARG B 1 189 ? 12.546  -19.220 23.847  1.00 47.63  ? 218 ARG B NH1 1 
ATOM   4907 N NH2 . ARG B 1 189 ? 14.427  -20.514 24.152  1.00 42.82  ? 218 ARG B NH2 1 
ATOM   4908 N N   . ASN B 1 190 ? 17.936  -17.863 17.373  1.00 25.16  ? 219 ASN B N   1 
ATOM   4909 C CA  . ASN B 1 190 ? 18.835  -18.472 16.404  1.00 24.38  ? 219 ASN B CA  1 
ATOM   4910 C C   . ASN B 1 190 ? 20.296  -18.121 16.668  1.00 24.19  ? 219 ASN B C   1 
ATOM   4911 O O   . ASN B 1 190 ? 21.154  -18.976 16.466  1.00 23.31  ? 219 ASN B O   1 
ATOM   4912 C CB  . ASN B 1 190 ? 18.477  -18.062 14.981  1.00 26.84  ? 219 ASN B CB  1 
ATOM   4913 C CG  . ASN B 1 190 ? 17.186  -18.701 14.551  1.00 28.94  ? 219 ASN B CG  1 
ATOM   4914 O OD1 . ASN B 1 190 ? 16.676  -19.578 15.259  1.00 30.04  ? 219 ASN B OD1 1 
ATOM   4915 N ND2 . ASN B 1 190 ? 16.678  -18.330 13.381  1.00 28.57  ? 219 ASN B ND2 1 
ATOM   4916 N N   . LEU B 1 191 ? 20.598  -16.899 17.122  1.00 20.25  ? 220 LEU B N   1 
ATOM   4917 C CA  . LEU B 1 191 ? 21.978  -16.499 17.373  1.00 20.84  ? 220 LEU B CA  1 
ATOM   4918 C C   . LEU B 1 191 ? 22.476  -16.968 18.734  1.00 23.72  ? 220 LEU B C   1 
ATOM   4919 O O   . LEU B 1 191 ? 23.619  -17.359 18.866  1.00 24.46  ? 220 LEU B O   1 
ATOM   4920 C CB  . LEU B 1 191 ? 22.151  -15.005 17.260  1.00 21.19  ? 220 LEU B CB  1 
ATOM   4921 C CG  . LEU B 1 191 ? 22.072  -14.470 15.809  1.00 24.36  ? 220 LEU B CG  1 
ATOM   4922 C CD1 . LEU B 1 191 ? 21.909  -12.951 15.799  1.00 25.97  ? 220 LEU B CD1 1 
ATOM   4923 C CD2 . LEU B 1 191 ? 23.264  -14.954 15.004  1.00 26.58  ? 220 LEU B CD2 1 
ATOM   4924 N N   . TYR B 1 192 ? 21.642  -16.898 19.757  1.00 24.26  ? 221 TYR B N   1 
ATOM   4925 C CA  . TYR B 1 192 ? 22.193  -17.017 21.094  1.00 27.33  ? 221 TYR B CA  1 
ATOM   4926 C C   . TYR B 1 192 ? 21.547  -18.098 21.947  1.00 30.60  ? 221 TYR B C   1 
ATOM   4927 O O   . TYR B 1 192 ? 21.863  -18.168 23.120  1.00 32.36  ? 221 TYR B O   1 
ATOM   4928 C CB  . TYR B 1 192 ? 21.978  -15.655 21.734  1.00 27.08  ? 221 TYR B CB  1 
ATOM   4929 C CG  . TYR B 1 192 ? 22.476  -14.485 20.901  1.00 30.01  ? 221 TYR B CG  1 
ATOM   4930 C CD1 . TYR B 1 192 ? 23.801  -14.394 20.496  1.00 30.38  ? 221 TYR B CD1 1 
ATOM   4931 C CD2 . TYR B 1 192 ? 21.594  -13.479 20.494  1.00 29.76  ? 221 TYR B CD2 1 
ATOM   4932 C CE1 . TYR B 1 192 ? 24.266  -13.304 19.773  1.00 29.12  ? 221 TYR B CE1 1 
ATOM   4933 C CE2 . TYR B 1 192 ? 22.032  -12.418 19.719  1.00 28.22  ? 221 TYR B CE2 1 
ATOM   4934 C CZ  . TYR B 1 192 ? 23.376  -12.309 19.388  1.00 32.51  ? 221 TYR B CZ  1 
ATOM   4935 O OH  . TYR B 1 192 ? 23.797  -11.248 18.644  1.00 27.76  ? 221 TYR B OH  1 
ATOM   4936 N N   . ARG B 1 193 ? 20.565  -18.827 21.422  1.00 32.51  ? 222 ARG B N   1 
ATOM   4937 C CA  . ARG B 1 193 ? 19.905  -19.905 22.160  1.00 34.52  ? 222 ARG B CA  1 
ATOM   4938 C C   . ARG B 1 193 ? 19.728  -21.129 21.254  1.00 31.50  ? 222 ARG B C   1 
ATOM   4939 O O   . ARG B 1 193 ? 18.680  -21.774 21.265  1.00 34.44  ? 222 ARG B O   1 
ATOM   4940 C CB  . ARG B 1 193 ? 18.571  -19.417 22.737  1.00 35.74  ? 222 ARG B CB  1 
ATOM   4941 C CG  . ARG B 1 193 ? 18.772  -18.286 23.732  1.00 39.32  ? 222 ARG B CG  1 
ATOM   4942 C CD  . ARG B 1 193 ? 18.477  -18.671 25.147  1.00 47.09  ? 222 ARG B CD  1 
ATOM   4943 N NE  . ARG B 1 193 ? 18.262  -17.503 26.006  1.00 53.09  ? 222 ARG B NE  1 
ATOM   4944 C CZ  . ARG B 1 193 ? 19.155  -16.564 26.303  1.00 52.67  ? 222 ARG B CZ  1 
ATOM   4945 N NH1 . ARG B 1 193 ? 20.329  -16.523 25.701  1.00 44.17  ? 222 ARG B NH1 1 
ATOM   4946 N NH2 . ARG B 1 193 ? 18.828  -15.615 27.163  1.00 54.84  ? 222 ARG B NH2 1 
ATOM   4947 N N   . GLU B 1 194 ? 20.737  -21.363 20.411  1.00 30.85  ? 223 GLU B N   1 
ATOM   4948 C CA  . GLU B 1 194 ? 20.925  -22.608 19.673  1.00 40.63  ? 223 GLU B CA  1 
ATOM   4949 C C   . GLU B 1 194 ? 19.762  -22.964 18.752  1.00 40.99  ? 223 GLU B C   1 
ATOM   4950 O O   . GLU B 1 194 ? 19.578  -24.131 18.385  1.00 36.80  ? 223 GLU B O   1 
ATOM   4951 C CB  . GLU B 1 194 ? 21.189  -23.758 20.649  1.00 44.81  ? 223 GLU B CB  1 
ATOM   4952 C CG  . GLU B 1 194 ? 22.518  -23.590 21.382  1.00 50.47  ? 223 GLU B CG  1 
ATOM   4953 C CD  . GLU B 1 194 ? 22.775  -24.726 22.346  1.00 63.65  ? 223 GLU B CD  1 
ATOM   4954 O OE1 . GLU B 1 194 ? 22.835  -24.483 23.579  1.00 73.16  ? 223 GLU B OE1 1 
ATOM   4955 O OE2 . GLU B 1 194 ? 22.871  -25.869 21.844  1.00 64.60  ? 223 GLU B OE2 1 
ATOM   4956 N N   . GLY B 1 195 ? 18.989  -21.965 18.326  1.00 39.43  ? 224 GLY B N   1 
ATOM   4957 C CA  . GLY B 1 195 ? 17.965  -22.214 17.323  1.00 33.85  ? 224 GLY B CA  1 
ATOM   4958 C C   . GLY B 1 195 ? 16.655  -22.697 17.924  1.00 30.30  ? 224 GLY B C   1 
ATOM   4959 O O   . GLY B 1 195 ? 15.745  -23.080 17.193  1.00 34.49  ? 224 GLY B O   1 
ATOM   4960 N N   . SER B 1 196 ? 16.529  -22.654 19.255  1.00 35.91  ? 225 SER B N   1 
ATOM   4961 C CA  . SER B 1 196 ? 15.286  -23.064 19.889  1.00 38.50  ? 225 SER B CA  1 
ATOM   4962 C C   . SER B 1 196 ? 14.125  -22.205 19.384  1.00 39.71  ? 225 SER B C   1 
ATOM   4963 O O   . SER B 1 196 ? 14.335  -21.078 18.940  1.00 38.94  ? 225 SER B O   1 
ATOM   4964 C CB  . SER B 1 196 ? 15.395  -23.031 21.403  1.00 39.28  ? 225 SER B CB  1 
ATOM   4965 O OG  . SER B 1 196 ? 15.897  -21.789 21.864  1.00 43.06  ? 225 SER B OG  1 
ATOM   4966 N N   . GLY B 1 197 ? 12.905  -22.740 19.501  1.00 38.30  ? 226 GLY B N   1 
ATOM   4967 C CA  . GLY B 1 197 ? 11.687  -22.089 19.046  1.00 35.59  ? 226 GLY B CA  1 
ATOM   4968 C C   . GLY B 1 197 ? 11.309  -20.890 19.920  1.00 37.19  ? 226 GLY B C   1 
ATOM   4969 O O   . GLY B 1 197 ? 11.691  -20.803 21.093  1.00 38.98  ? 226 GLY B O   1 
ATOM   4970 N N   . ILE B 1 198 ? 10.515  -19.975 19.339  1.00 33.37  ? 227 ILE B N   1 
ATOM   4971 C CA  . ILE B 1 198 ? 10.105  -18.766 20.038  1.00 39.04  ? 227 ILE B CA  1 
ATOM   4972 C C   . ILE B 1 198 ? 8.826   -19.028 20.816  1.00 36.46  ? 227 ILE B C   1 
ATOM   4973 O O   . ILE B 1 198 ? 8.471   -18.238 21.708  1.00 36.31  ? 227 ILE B O   1 
ATOM   4974 C CB  . ILE B 1 198 ? 9.946   -17.560 19.100  1.00 36.58  ? 227 ILE B CB  1 
ATOM   4975 C CG1 . ILE B 1 198 ? 8.943   -17.834 17.965  1.00 37.27  ? 227 ILE B CG1 1 
ATOM   4976 C CG2 . ILE B 1 198 ? 11.330  -17.125 18.618  1.00 36.42  ? 227 ILE B CG2 1 
ATOM   4977 C CD1 . ILE B 1 198 ? 8.706   -16.651 17.030  1.00 39.48  ? 227 ILE B CD1 1 
ATOM   4978 N N   . GLY B 1 199 ? 8.166   -20.137 20.466  1.00 38.82  ? 228 GLY B N   1 
ATOM   4979 C CA  . GLY B 1 199 ? 6.924   -20.506 21.126  1.00 39.94  ? 228 GLY B CA  1 
ATOM   4980 C C   . GLY B 1 199 ? 5.758   -19.675 20.603  1.00 42.09  ? 228 GLY B C   1 
ATOM   4981 O O   . GLY B 1 199 ? 5.794   -19.167 19.479  1.00 42.95  ? 228 GLY B O   1 
ATOM   4982 N N   . ALA B 1 200 ? 4.713   -19.554 21.433  1.00 40.74  ? 229 ALA B N   1 
ATOM   4983 C CA  . ALA B 1 200 ? 3.427   -19.073 20.959  1.00 44.06  ? 229 ALA B CA  1 
ATOM   4984 C C   . ALA B 1 200 ? 3.197   -17.651 21.468  1.00 40.87  ? 229 ALA B C   1 
ATOM   4985 O O   . ALA B 1 200 ? 3.793   -17.224 22.454  1.00 38.27  ? 229 ALA B O   1 
ATOM   4986 C CB  . ALA B 1 200 ? 2.313   -20.012 21.391  1.00 43.26  ? 229 ALA B CB  1 
ATOM   4987 N N   . ILE B 1 201 ? 2.372   -16.929 20.716  1.00 37.03  ? 230 ILE B N   1 
ATOM   4988 C CA  . ILE B 1 201 ? 1.744   -15.701 21.166  1.00 38.29  ? 230 ILE B CA  1 
ATOM   4989 C C   . ILE B 1 201 ? 0.597   -16.038 22.112  1.00 42.44  ? 230 ILE B C   1 
ATOM   4990 O O   . ILE B 1 201 ? -0.218  -16.914 21.826  1.00 44.26  ? 230 ILE B O   1 
ATOM   4991 C CB  . ILE B 1 201 ? 1.230   -14.913 19.945  1.00 38.43  ? 230 ILE B CB  1 
ATOM   4992 C CG1 . ILE B 1 201 ? 2.389   -14.314 19.149  1.00 40.05  ? 230 ILE B CG1 1 
ATOM   4993 C CG2 . ILE B 1 201 ? 0.202   -13.863 20.359  1.00 37.80  ? 230 ILE B CG2 1 
ATOM   4994 C CD1 . ILE B 1 201 ? 3.236   -13.319 19.928  1.00 39.38  ? 230 ILE B CD1 1 
ATOM   4995 N N   . ASP B 1 202 ? 0.498   -15.276 23.195  1.00 38.85  ? 231 ASP B N   1 
ATOM   4996 C CA  . ASP B 1 202 ? -0.670  -15.312 24.046  1.00 38.47  ? 231 ASP B CA  1 
ATOM   4997 C C   . ASP B 1 202 ? -1.553  -14.102 23.734  1.00 41.85  ? 231 ASP B C   1 
ATOM   4998 O O   . ASP B 1 202 ? -1.199  -12.957 24.018  1.00 39.93  ? 231 ASP B O   1 
ATOM   4999 C CB  . ASP B 1 202 ? -0.319  -15.497 25.511  1.00 41.38  ? 231 ASP B CB  1 
ATOM   5000 C CG  . ASP B 1 202 ? -1.538  -15.574 26.431  1.00 47.02  ? 231 ASP B CG  1 
ATOM   5001 O OD1 . ASP B 1 202 ? -2.675  -15.440 25.925  1.00 46.58  ? 231 ASP B OD1 1 
ATOM   5002 O OD2 . ASP B 1 202 ? -1.359  -15.782 27.639  1.00 45.85  ? 231 ASP B OD2 1 
ATOM   5003 N N   . SER B 1 203 ? -2.748  -14.413 23.213  1.00 44.18  ? 232 SER B N   1 
ATOM   5004 C CA  . SER B 1 203 ? -3.793  -13.469 22.856  1.00 45.84  ? 232 SER B CA  1 
ATOM   5005 C C   . SER B 1 203 ? -4.067  -12.434 23.943  1.00 46.21  ? 232 SER B C   1 
ATOM   5006 O O   . SER B 1 203 ? -4.573  -11.355 23.642  1.00 42.96  ? 232 SER B O   1 
ATOM   5007 C CB  . SER B 1 203 ? -5.047  -14.252 22.526  1.00 55.09  ? 232 SER B CB  1 
ATOM   5008 O OG  . SER B 1 203 ? -6.159  -13.390 22.347  1.00 68.21  ? 232 SER B OG  1 
ATOM   5009 N N   . ASN B 1 204 ? -3.794  -12.765 25.212  1.00 43.42  ? 233 ASN B N   1 
ATOM   5010 C CA  . ASN B 1 204 ? -4.225  -11.921 26.311  1.00 40.68  ? 233 ASN B CA  1 
ATOM   5011 C C   . ASN B 1 204 ? -3.054  -11.178 26.947  1.00 38.55  ? 233 ASN B C   1 
ATOM   5012 O O   . ASN B 1 204 ? -3.256  -10.516 27.946  1.00 38.88  ? 233 ASN B O   1 
ATOM   5013 C CB  . ASN B 1 204 ? -4.967  -12.741 27.370  1.00 47.76  ? 233 ASN B CB  1 
ATOM   5014 C CG  . ASN B 1 204 ? -6.310  -13.220 26.869  1.00 49.32  ? 233 ASN B CG  1 
ATOM   5015 O OD1 . ASN B 1 204 ? -7.098  -12.424 26.341  1.00 55.11  ? 233 ASN B OD1 1 
ATOM   5016 N ND2 . ASN B 1 204 ? -6.567  -14.514 26.969  1.00 53.24  ? 233 ASN B ND2 1 
ATOM   5017 N N   . LEU B 1 205 ? -1.835  -11.279 26.395  1.00 38.51  ? 234 LEU B N   1 
ATOM   5018 C CA  . LEU B 1 205 ? -0.709  -10.519 26.936  1.00 39.90  ? 234 LEU B CA  1 
ATOM   5019 C C   . LEU B 1 205 ? -0.443  -9.274  26.085  1.00 34.31  ? 234 LEU B C   1 
ATOM   5020 O O   . LEU B 1 205 ? -0.713  -9.268  24.880  1.00 35.76  ? 234 LEU B O   1 
ATOM   5021 C CB  . LEU B 1 205 ? 0.567   -11.358 26.979  1.00 42.66  ? 234 LEU B CB  1 
ATOM   5022 C CG  . LEU B 1 205 ? 0.495   -12.680 27.742  1.00 44.74  ? 234 LEU B CG  1 
ATOM   5023 C CD1 . LEU B 1 205 ? 1.826   -13.406 27.581  1.00 41.81  ? 234 LEU B CD1 1 
ATOM   5024 C CD2 . LEU B 1 205 ? 0.149   -12.416 29.191  1.00 46.22  ? 234 LEU B CD2 1 
ATOM   5025 N N   . ASP B 1 206 ? 0.131   -8.241  26.715  1.00 28.04  ? 235 ASP B N   1 
ATOM   5026 C CA  . ASP B 1 206 ? 0.607   -7.082  25.978  1.00 30.37  ? 235 ASP B CA  1 
ATOM   5027 C C   . ASP B 1 206 ? 1.810   -7.493  25.122  1.00 27.68  ? 235 ASP B C   1 
ATOM   5028 O O   . ASP B 1 206 ? 2.398   -8.554  25.333  1.00 29.16  ? 235 ASP B O   1 
ATOM   5029 C CB  . ASP B 1 206 ? 0.944   -5.910  26.897  1.00 27.98  ? 235 ASP B CB  1 
ATOM   5030 C CG  . ASP B 1 206 ? 2.044   -6.151  27.925  1.00 32.69  ? 235 ASP B CG  1 
ATOM   5031 O OD1 . ASP B 1 206 ? 1.775   -6.841  28.922  1.00 37.54  ? 235 ASP B OD1 1 
ATOM   5032 O OD2 . ASP B 1 206 ? 3.169   -5.652  27.756  1.00 28.96  ? 235 ASP B OD2 1 
ATOM   5033 N N   . TRP B 1 207 ? 2.145   -6.619  24.167  1.00 27.83  ? 236 TRP B N   1 
ATOM   5034 C CA  . TRP B 1 207 ? 3.169   -6.780  23.135  1.00 24.79  ? 236 TRP B CA  1 
ATOM   5035 C C   . TRP B 1 207 ? 4.559   -7.027  23.745  1.00 24.48  ? 236 TRP B C   1 
ATOM   5036 O O   . TRP B 1 207 ? 5.252   -7.963  23.349  1.00 25.45  ? 236 TRP B O   1 
ATOM   5037 C CB  . TRP B 1 207 ? 3.110   -5.478  22.310  1.00 25.32  ? 236 TRP B CB  1 
ATOM   5038 C CG  . TRP B 1 207 ? 3.928   -5.352  21.047  1.00 22.58  ? 236 TRP B CG  1 
ATOM   5039 C CD1 . TRP B 1 207 ? 3.726   -6.010  19.873  1.00 25.06  ? 236 TRP B CD1 1 
ATOM   5040 C CD2 . TRP B 1 207 ? 4.990   -4.388  20.786  1.00 22.13  ? 236 TRP B CD2 1 
ATOM   5041 N NE1 . TRP B 1 207 ? 4.606   -5.560  18.915  1.00 23.64  ? 236 TRP B NE1 1 
ATOM   5042 C CE2 . TRP B 1 207 ? 5.360   -4.535  19.435  1.00 19.99  ? 236 TRP B CE2 1 
ATOM   5043 C CE3 . TRP B 1 207 ? 5.595   -3.381  21.538  1.00 23.92  ? 236 TRP B CE3 1 
ATOM   5044 C CZ2 . TRP B 1 207 ? 6.353   -3.749  18.857  1.00 23.63  ? 236 TRP B CZ2 1 
ATOM   5045 C CZ3 . TRP B 1 207 ? 6.565   -2.575  20.962  1.00 22.96  ? 236 TRP B CZ3 1 
ATOM   5046 C CH2 . TRP B 1 207 ? 6.914   -2.739  19.625  1.00 23.05  ? 236 TRP B CH2 1 
ATOM   5047 N N   . SER B 1 208 ? 4.943   -6.212  24.740  1.00 26.13  ? 237 SER B N   1 
ATOM   5048 C CA  . SER B 1 208 ? 6.237   -6.333  25.410  1.00 25.01  ? 237 SER B CA  1 
ATOM   5049 C C   . SER B 1 208 ? 6.394   -7.689  26.107  1.00 23.81  ? 237 SER B C   1 
ATOM   5050 O O   . SER B 1 208 ? 7.474   -8.282  26.139  1.00 23.51  ? 237 SER B O   1 
ATOM   5051 C CB  . SER B 1 208 ? 6.451   -5.263  26.429  1.00 24.39  ? 237 SER B CB  1 
ATOM   5052 O OG  . SER B 1 208 ? 6.408   -3.955  25.908  1.00 22.76  ? 237 SER B OG  1 
ATOM   5053 N N   . HIS B 1 209 ? 5.308   -8.177  26.701  1.00 26.39  ? 238 HIS B N   1 
ATOM   5054 C CA  . HIS B 1 209 ? 5.321   -9.449  27.418  1.00 24.93  ? 238 HIS B CA  1 
ATOM   5055 C C   . HIS B 1 209 ? 5.422   -10.622 26.446  1.00 24.34  ? 238 HIS B C   1 
ATOM   5056 O O   . HIS B 1 209 ? 6.124   -11.584 26.707  1.00 25.48  ? 238 HIS B O   1 
ATOM   5057 C CB  . HIS B 1 209 ? 4.089   -9.574  28.335  1.00 30.95  ? 238 HIS B CB  1 
ATOM   5058 C CG  . HIS B 1 209 ? 4.184   -10.629 29.398  1.00 34.09  ? 238 HIS B CG  1 
ATOM   5059 N ND1 . HIS B 1 209 ? 3.214   -10.819 30.363  1.00 39.78  ? 238 HIS B ND1 1 
ATOM   5060 C CD2 . HIS B 1 209 ? 5.111   -11.571 29.632  1.00 39.04  ? 238 HIS B CD2 1 
ATOM   5061 C CE1 . HIS B 1 209 ? 3.564   -11.822 31.159  1.00 39.33  ? 238 HIS B CE1 1 
ATOM   5062 N NE2 . HIS B 1 209 ? 4.725   -12.276 30.749  1.00 38.83  ? 238 HIS B NE2 1 
ATOM   5063 N N   . ASN B 1 210 ? 4.666   -10.583 25.342  1.00 23.95  ? 239 ASN B N   1 
ATOM   5064 C CA  . ASN B 1 210 ? 4.788   -11.591 24.313  1.00 24.63  ? 239 ASN B CA  1 
ATOM   5065 C C   . ASN B 1 210 ? 6.214   -11.585 23.789  1.00 27.28  ? 239 ASN B C   1 
ATOM   5066 O O   . ASN B 1 210 ? 6.770   -12.663 23.536  1.00 24.30  ? 239 ASN B O   1 
ATOM   5067 C CB  . ASN B 1 210 ? 3.798   -11.403 23.168  1.00 27.40  ? 239 ASN B CB  1 
ATOM   5068 C CG  . ASN B 1 210 ? 2.450   -12.015 23.482  1.00 31.69  ? 239 ASN B CG  1 
ATOM   5069 O OD1 . ASN B 1 210 ? 2.365   -13.154 23.967  1.00 33.18  ? 239 ASN B OD1 1 
ATOM   5070 N ND2 . ASN B 1 210 ? 1.392   -11.291 23.187  1.00 30.80  ? 239 ASN B ND2 1 
ATOM   5071 N N   . PHE B 1 211 ? 6.803   -10.366 23.674  1.00 24.41  ? 240 PHE B N   1 
ATOM   5072 C CA  . PHE B 1 211 ? 8.176   -10.254 23.203  1.00 23.57  ? 240 PHE B CA  1 
ATOM   5073 C C   . PHE B 1 211 ? 9.136   -10.935 24.184  1.00 22.72  ? 240 PHE B C   1 
ATOM   5074 O O   . PHE B 1 211 ? 9.932   -11.754 23.769  1.00 25.92  ? 240 PHE B O   1 
ATOM   5075 C CB  . PHE B 1 211 ? 8.584   -8.781  22.985  1.00 23.09  ? 240 PHE B CB  1 
ATOM   5076 C CG  . PHE B 1 211 ? 9.918   -8.527  22.287  1.00 22.02  ? 240 PHE B CG  1 
ATOM   5077 C CD1 . PHE B 1 211 ? 10.514  -9.477  21.478  1.00 21.03  ? 240 PHE B CD1 1 
ATOM   5078 C CD2 . PHE B 1 211 ? 10.567  -7.304  22.449  1.00 25.43  ? 240 PHE B CD2 1 
ATOM   5079 C CE1 . PHE B 1 211 ? 11.732  -9.254  20.876  1.00 22.83  ? 240 PHE B CE1 1 
ATOM   5080 C CE2 . PHE B 1 211 ? 11.767  -7.058  21.807  1.00 25.60  ? 240 PHE B CE2 1 
ATOM   5081 C CZ  . PHE B 1 211 ? 12.355  -8.042  21.038  1.00 26.50  ? 240 PHE B CZ  1 
ATOM   5082 N N   . THR B 1 212 ? 9.105   -10.569 25.478  1.00 23.47  ? 241 THR B N   1 
ATOM   5083 C CA  . THR B 1 212 ? 10.057  -11.119 26.422  1.00 26.35  ? 241 THR B CA  1 
ATOM   5084 C C   . THR B 1 212 ? 9.825   -12.627 26.587  1.00 26.42  ? 241 THR B C   1 
ATOM   5085 O O   . THR B 1 212 ? 10.798  -13.337 26.803  1.00 26.35  ? 241 THR B O   1 
ATOM   5086 C CB  . THR B 1 212 ? 10.094  -10.401 27.776  1.00 27.43  ? 241 THR B CB  1 
ATOM   5087 O OG1 . THR B 1 212 ? 8.803   -10.454 28.354  1.00 28.14  ? 241 THR B OG1 1 
ATOM   5088 C CG2 . THR B 1 212 ? 10.542  -8.949  27.673  1.00 26.98  ? 241 THR B CG2 1 
ATOM   5089 N N   . ASN B 1 213 ? 8.584   -13.122 26.412  1.00 25.41  ? 242 ASN B N   1 
ATOM   5090 C CA  . ASN B 1 213 ? 8.322   -14.563 26.373  1.00 24.84  ? 242 ASN B CA  1 
ATOM   5091 C C   . ASN B 1 213 ? 9.033   -15.259 25.212  1.00 27.56  ? 242 ASN B C   1 
ATOM   5092 O O   . ASN B 1 213 ? 9.680   -16.281 25.423  1.00 29.95  ? 242 ASN B O   1 
ATOM   5093 C CB  . ASN B 1 213 ? 6.853   -14.956 26.229  1.00 28.39  ? 242 ASN B CB  1 
ATOM   5094 C CG  . ASN B 1 213 ? 6.040   -14.869 27.506  1.00 30.38  ? 242 ASN B CG  1 
ATOM   5095 O OD1 . ASN B 1 213 ? 6.532   -14.421 28.551  1.00 30.36  ? 242 ASN B OD1 1 
ATOM   5096 N ND2 . ASN B 1 213 ? 4.758   -15.196 27.389  1.00 28.59  ? 242 ASN B ND2 1 
ATOM   5097 N N   . MET B 1 214 ? 8.945   -14.688 24.005  1.00 23.47  ? 243 MET B N   1 
ATOM   5098 C CA  . MET B 1 214 ? 9.563   -15.279 22.830  1.00 25.61  ? 243 MET B CA  1 
ATOM   5099 C C   . MET B 1 214 ? 11.081  -15.236 22.915  1.00 22.93  ? 243 MET B C   1 
ATOM   5100 O O   . MET B 1 214 ? 11.744  -16.105 22.377  1.00 26.92  ? 243 MET B O   1 
ATOM   5101 C CB  . MET B 1 214 ? 9.088   -14.580 21.552  1.00 24.40  ? 243 MET B CB  1 
ATOM   5102 C CG  . MET B 1 214 ? 7.594   -14.749 21.321  1.00 26.03  ? 243 MET B CG  1 
ATOM   5103 S SD  . MET B 1 214 ? 6.976   -14.102 19.758  1.00 30.76  ? 243 MET B SD  1 
ATOM   5104 C CE  . MET B 1 214 ? 6.776   -12.353 20.118  1.00 31.11  ? 243 MET B CE  1 
ATOM   5105 N N   . LEU B 1 215 ? 11.642  -14.202 23.537  1.00 23.08  ? 244 LEU B N   1 
ATOM   5106 C CA  . LEU B 1 215 ? 13.064  -14.135 23.807  1.00 24.35  ? 244 LEU B CA  1 
ATOM   5107 C C   . LEU B 1 215 ? 13.514  -15.233 24.783  1.00 27.01  ? 244 LEU B C   1 
ATOM   5108 O O   . LEU B 1 215 ? 14.709  -15.478 24.875  1.00 26.44  ? 244 LEU B O   1 
ATOM   5109 C CB  . LEU B 1 215 ? 13.446  -12.764 24.372  1.00 23.02  ? 244 LEU B CB  1 
ATOM   5110 C CG  . LEU B 1 215 ? 13.366  -11.573 23.400  1.00 26.28  ? 244 LEU B CG  1 
ATOM   5111 C CD1 . LEU B 1 215 ? 13.498  -10.281 24.167  1.00 25.42  ? 244 LEU B CD1 1 
ATOM   5112 C CD2 . LEU B 1 215 ? 14.452  -11.680 22.326  1.00 24.63  ? 244 LEU B CD2 1 
ATOM   5113 N N   . GLY B 1 216 ? 12.592  -15.747 25.610  1.00 27.89  ? 245 GLY B N   1 
ATOM   5114 C CA  . GLY B 1 216 ? 12.891  -16.787 26.584  1.00 31.58  ? 245 GLY B CA  1 
ATOM   5115 C C   . GLY B 1 216 ? 13.144  -16.242 27.998  1.00 33.95  ? 245 GLY B C   1 
ATOM   5116 O O   . GLY B 1 216 ? 13.743  -16.923 28.820  1.00 34.22  ? 245 GLY B O   1 
ATOM   5117 N N   . TYR B 1 217 ? 12.737  -15.004 28.273  1.00 31.05  ? 246 TYR B N   1 
ATOM   5118 C CA  . TYR B 1 217 ? 12.920  -14.403 29.581  1.00 32.40  ? 246 TYR B CA  1 
ATOM   5119 C C   . TYR B 1 217 ? 11.625  -14.613 30.361  1.00 34.50  ? 246 TYR B C   1 
ATOM   5120 O O   . TYR B 1 217 ? 10.574  -14.817 29.767  1.00 37.34  ? 246 TYR B O   1 
ATOM   5121 C CB  . TYR B 1 217 ? 13.320  -12.929 29.466  1.00 33.79  ? 246 TYR B CB  1 
ATOM   5122 C CG  . TYR B 1 217 ? 14.740  -12.715 28.948  1.00 30.54  ? 246 TYR B CG  1 
ATOM   5123 C CD1 . TYR B 1 217 ? 15.048  -12.884 27.604  1.00 29.84  ? 246 TYR B CD1 1 
ATOM   5124 C CD2 . TYR B 1 217 ? 15.751  -12.287 29.790  1.00 32.70  ? 246 TYR B CD2 1 
ATOM   5125 C CE1 . TYR B 1 217 ? 16.322  -12.687 27.132  1.00 26.84  ? 246 TYR B CE1 1 
ATOM   5126 C CE2 . TYR B 1 217 ? 17.033  -12.054 29.331  1.00 31.87  ? 246 TYR B CE2 1 
ATOM   5127 C CZ  . TYR B 1 217 ? 17.313  -12.262 27.995  1.00 30.60  ? 246 TYR B CZ  1 
ATOM   5128 O OH  . TYR B 1 217 ? 18.578  -12.086 27.544  1.00 29.06  ? 246 TYR B OH  1 
ATOM   5129 N N   . THR B 1 218 ? 11.692  -14.557 31.695  1.00 43.09  ? 247 THR B N   1 
ATOM   5130 C CA  . THR B 1 218 ? 10.519  -14.845 32.502  1.00 45.47  ? 247 THR B CA  1 
ATOM   5131 C C   . THR B 1 218 ? 10.247  -13.749 33.533  1.00 46.12  ? 247 THR B C   1 
ATOM   5132 O O   . THR B 1 218 ? 9.104   -13.492 33.919  1.00 67.94  ? 247 THR B O   1 
ATOM   5133 C CB  . THR B 1 218 ? 10.781  -16.224 33.100  1.00 61.37  ? 247 THR B CB  1 
ATOM   5134 O OG1 . THR B 1 218 ? 12.168  -16.231 33.458  1.00 61.18  ? 247 THR B OG1 1 
ATOM   5135 C CG2 . THR B 1 218 ? 10.467  -17.315 32.088  1.00 55.85  ? 247 THR B CG2 1 
ATOM   5136 N N   . ASP B 1 219 ? 11.322  -13.110 33.948  1.00 40.61  ? 248 ASP B N   1 
ATOM   5137 C CA  . ASP B 1 219 ? 11.410  -11.982 34.865  1.00 34.12  ? 248 ASP B CA  1 
ATOM   5138 C C   . ASP B 1 219 ? 10.441  -10.813 34.626  1.00 33.94  ? 248 ASP B C   1 
ATOM   5139 O O   . ASP B 1 219 ? 10.515  -10.068 33.637  1.00 30.16  ? 248 ASP B O   1 
ATOM   5140 C CB  . ASP B 1 219 ? 12.869  -11.618 34.716  1.00 37.63  ? 248 ASP B CB  1 
ATOM   5141 C CG  . ASP B 1 219 ? 13.438  -10.579 35.636  1.00 36.56  ? 248 ASP B CG  1 
ATOM   5142 O OD1 . ASP B 1 219 ? 12.655  -9.786  36.180  1.00 38.33  ? 248 ASP B OD1 1 
ATOM   5143 O OD2 . ASP B 1 219 ? 14.666  -10.610 35.754  1.00 43.02  ? 248 ASP B OD2 1 
ATOM   5144 N N   . HIS B 1 220 ? 9.593   -10.543 35.632  1.00 32.35  ? 249 HIS B N   1 
ATOM   5145 C CA  . HIS B 1 220 ? 8.615   -9.471  35.611  1.00 32.46  ? 249 HIS B CA  1 
ATOM   5146 C C   . HIS B 1 220 ? 9.324   -8.127  35.472  1.00 32.41  ? 249 HIS B C   1 
ATOM   5147 O O   . HIS B 1 220 ? 8.861   -7.263  34.738  1.00 34.62  ? 249 HIS B O   1 
ATOM   5148 C CB  . HIS B 1 220 ? 7.728   -9.501  36.864  1.00 33.65  ? 249 HIS B CB  1 
ATOM   5149 C CG  . HIS B 1 220 ? 6.897   -8.258  37.063  1.00 33.97  ? 249 HIS B CG  1 
ATOM   5150 N ND1 . HIS B 1 220 ? 5.826   -7.911  36.268  1.00 39.12  ? 249 HIS B ND1 1 
ATOM   5151 C CD2 . HIS B 1 220 ? 7.030   -7.243  37.939  1.00 37.60  ? 249 HIS B CD2 1 
ATOM   5152 C CE1 . HIS B 1 220 ? 5.300   -6.756  36.696  1.00 36.76  ? 249 HIS B CE1 1 
ATOM   5153 N NE2 . HIS B 1 220 ? 6.011   -6.329  37.709  1.00 36.77  ? 249 HIS B NE2 1 
ATOM   5154 N N   . GLN B 1 221 ? 10.488  -7.974  36.111  1.00 30.57  ? 250 GLN B N   1 
ATOM   5155 C CA  . GLN B 1 221 ? 11.181  -6.696  36.095  1.00 36.69  ? 250 GLN B CA  1 
ATOM   5156 C C   . GLN B 1 221 ? 11.775  -6.433  34.708  1.00 31.51  ? 250 GLN B C   1 
ATOM   5157 O O   . GLN B 1 221 ? 11.839  -5.279  34.294  1.00 28.26  ? 250 GLN B O   1 
ATOM   5158 C CB  . GLN B 1 221 ? 12.235  -6.564  37.189  1.00 43.76  ? 250 GLN B CB  1 
ATOM   5159 C CG  . GLN B 1 221 ? 11.656  -6.299  38.574  1.00 55.34  ? 250 GLN B CG  1 
ATOM   5160 C CD  . GLN B 1 221 ? 10.543  -5.259  38.591  1.00 70.48  ? 250 GLN B CD  1 
ATOM   5161 O OE1 . GLN B 1 221 ? 10.680  -4.133  38.087  1.00 70.47  ? 250 GLN B OE1 1 
ATOM   5162 N NE2 . GLN B 1 221 ? 9.407   -5.623  39.173  1.00 68.32  ? 250 GLN B NE2 1 
ATOM   5163 N N   . PHE B 1 222 ? 12.166  -7.500  34.003  1.00 28.65  ? 251 PHE B N   1 
ATOM   5164 C CA  . PHE B 1 222 ? 12.720  -7.354  32.655  1.00 29.14  ? 251 PHE B CA  1 
ATOM   5165 C C   . PHE B 1 222 ? 11.589  -6.987  31.694  1.00 26.37  ? 251 PHE B C   1 
ATOM   5166 O O   . PHE B 1 222 ? 11.801  -6.178  30.801  1.00 29.47  ? 251 PHE B O   1 
ATOM   5167 C CB  . PHE B 1 222 ? 13.451  -8.593  32.141  1.00 27.38  ? 251 PHE B CB  1 
ATOM   5168 C CG  . PHE B 1 222 ? 13.971  -8.507  30.715  1.00 29.78  ? 251 PHE B CG  1 
ATOM   5169 C CD1 . PHE B 1 222 ? 14.965  -7.584  30.375  1.00 28.46  ? 251 PHE B CD1 1 
ATOM   5170 C CD2 . PHE B 1 222 ? 13.489  -9.344  29.719  1.00 29.93  ? 251 PHE B CD2 1 
ATOM   5171 C CE1 . PHE B 1 222 ? 15.439  -7.499  29.083  1.00 26.42  ? 251 PHE B CE1 1 
ATOM   5172 C CE2 . PHE B 1 222 ? 14.026  -9.286  28.443  1.00 27.68  ? 251 PHE B CE2 1 
ATOM   5173 C CZ  . PHE B 1 222 ? 14.993  -8.356  28.139  1.00 24.85  ? 251 PHE B CZ  1 
ATOM   5174 N N   . THR B 1 223 ? 10.386  -7.542  31.880  1.00 27.58  ? 252 THR B N   1 
ATOM   5175 C CA  . THR B 1 223 ? 9.266   -7.170  31.040  1.00 27.37  ? 252 THR B CA  1 
ATOM   5176 C C   . THR B 1 223 ? 8.914   -5.695  31.284  1.00 31.58  ? 252 THR B C   1 
ATOM   5177 O O   . THR B 1 223 ? 8.664   -4.965  30.330  1.00 29.77  ? 252 THR B O   1 
ATOM   5178 C CB  . THR B 1 223 ? 8.113   -8.140  31.205  1.00 27.00  ? 252 THR B CB  1 
ATOM   5179 O OG1 . THR B 1 223 ? 8.595   -9.416  30.770  1.00 26.69  ? 252 THR B OG1 1 
ATOM   5180 C CG2 . THR B 1 223 ? 6.963   -7.796  30.293  1.00 27.27  ? 252 THR B CG2 1 
ATOM   5181 N N   . GLU B 1 224 ? 8.999   -5.212  32.534  1.00 27.87  ? 253 GLU B N   1 
ATOM   5182 C CA  . GLU B 1 224 ? 8.751   -3.809  32.855  1.00 27.94  ? 253 GLU B CA  1 
ATOM   5183 C C   . GLU B 1 224 ? 9.796   -2.899  32.214  1.00 26.22  ? 253 GLU B C   1 
ATOM   5184 O O   . GLU B 1 224 ? 9.458   -1.809  31.738  1.00 25.53  ? 253 GLU B O   1 
ATOM   5185 C CB  . GLU B 1 224 ? 8.718   -3.552  34.364  1.00 28.99  ? 253 GLU B CB  1 
ATOM   5186 C CG  . GLU B 1 224 ? 7.459   -4.106  35.019  1.00 32.42  ? 253 GLU B CG  1 
ATOM   5187 C CD  . GLU B 1 224 ? 6.279   -3.189  34.770  1.00 33.04  ? 253 GLU B CD  1 
ATOM   5188 O OE1 . GLU B 1 224 ? 5.490   -3.469  33.832  1.00 30.77  ? 253 GLU B OE1 1 
ATOM   5189 O OE2 . GLU B 1 224 ? 6.215   -2.147  35.471  1.00 36.83  ? 253 GLU B OE2 1 
ATOM   5190 N N   . LEU B 1 225 ? 11.061  -3.333  32.230  1.00 23.51  ? 254 LEU B N   1 
ATOM   5191 C CA  . LEU B 1 225 ? 12.139  -2.576  31.617  1.00 24.84  ? 254 LEU B CA  1 
ATOM   5192 C C   . LEU B 1 225 ? 11.875  -2.482  30.107  1.00 23.69  ? 254 LEU B C   1 
ATOM   5193 O O   . LEU B 1 225 ? 12.042  -1.418  29.516  1.00 22.94  ? 254 LEU B O   1 
ATOM   5194 C CB  . LEU B 1 225 ? 13.511  -3.190  31.879  1.00 25.39  ? 254 LEU B CB  1 
ATOM   5195 C CG  . LEU B 1 225 ? 14.641  -2.565  31.062  1.00 26.40  ? 254 LEU B CG  1 
ATOM   5196 C CD1 . LEU B 1 225 ? 14.932  -1.155  31.532  1.00 26.23  ? 254 LEU B CD1 1 
ATOM   5197 C CD2 . LEU B 1 225 ? 15.877  -3.458  31.102  1.00 28.13  ? 254 LEU B CD2 1 
ATOM   5198 N N   . THR B 1 226 ? 11.424  -3.584  29.513  1.00 24.26  ? 255 THR B N   1 
ATOM   5199 C CA  . THR B 1 226 ? 11.178  -3.652  28.073  1.00 25.62  ? 255 THR B CA  1 
ATOM   5200 C C   . THR B 1 226 ? 10.033  -2.712  27.688  1.00 26.38  ? 255 THR B C   1 
ATOM   5201 O O   . THR B 1 226 ? 10.141  -1.990  26.679  1.00 26.80  ? 255 THR B O   1 
ATOM   5202 C CB  . THR B 1 226 ? 10.884  -5.085  27.654  1.00 24.66  ? 255 THR B CB  1 
ATOM   5203 O OG1 . THR B 1 226 ? 12.066  -5.804  27.986  1.00 24.62  ? 255 THR B OG1 1 
ATOM   5204 C CG2 . THR B 1 226 ? 10.598  -5.228  26.164  1.00 28.59  ? 255 THR B CG2 1 
ATOM   5205 N N   . ARG B 1 227 ? 8.979   -2.681  28.519  1.00 22.47  ? 256 ARG B N   1 
ATOM   5206 C CA  . ARG B 1 227 ? 7.864   -1.756  28.353  1.00 25.26  ? 256 ARG B CA  1 
ATOM   5207 C C   . ARG B 1 227 ? 8.358   -0.320  28.305  1.00 24.65  ? 256 ARG B C   1 
ATOM   5208 O O   . ARG B 1 227 ? 8.030   0.399   27.354  1.00 23.85  ? 256 ARG B O   1 
ATOM   5209 C CB  . ARG B 1 227 ? 6.766   -1.809  29.422  1.00 24.02  ? 256 ARG B CB  1 
ATOM   5210 C CG  . ARG B 1 227 ? 6.051   -3.138  29.329  1.00 24.24  ? 256 ARG B CG  1 
ATOM   5211 C CD  . ARG B 1 227 ? 5.264   -3.465  30.605  1.00 24.84  ? 256 ARG B CD  1 
ATOM   5212 N NE  . ARG B 1 227 ? 4.446   -4.664  30.366  1.00 27.83  ? 256 ARG B NE  1 
ATOM   5213 C CZ  . ARG B 1 227 ? 4.117   -5.615  31.266  1.00 28.38  ? 256 ARG B CZ  1 
ATOM   5214 N NH1 . ARG B 1 227 ? 4.656   -5.607  32.448  1.00 27.08  ? 256 ARG B NH1 1 
ATOM   5215 N NH2 . ARG B 1 227 ? 3.253   -6.556  30.968  1.00 27.67  ? 256 ARG B NH2 1 
ATOM   5216 N N   . LEU B 1 228 ? 9.168   0.063   29.296  1.00 23.25  ? 257 LEU B N   1 
ATOM   5217 C CA  . LEU B 1 228 ? 9.716   1.403   29.357  1.00 23.60  ? 257 LEU B CA  1 
ATOM   5218 C C   . LEU B 1 228 ? 10.602  1.667   28.136  1.00 22.98  ? 257 LEU B C   1 
ATOM   5219 O O   . LEU B 1 228 ? 10.513  2.745   27.574  1.00 26.40  ? 257 LEU B O   1 
ATOM   5220 C CB  . LEU B 1 228 ? 10.498  1.594   30.653  1.00 26.72  ? 257 LEU B CB  1 
ATOM   5221 C CG  . LEU B 1 228 ? 11.140  2.953   30.891  1.00 26.27  ? 257 LEU B CG  1 
ATOM   5222 C CD1 . LEU B 1 228 ? 10.101  4.029   31.016  1.00 27.69  ? 257 LEU B CD1 1 
ATOM   5223 C CD2 . LEU B 1 228 ? 12.003  2.933   32.149  1.00 29.11  ? 257 LEU B CD2 1 
ATOM   5224 N N   . TYR B 1 229 ? 11.525  0.752   27.833  1.00 24.31  ? 258 TYR B N   1 
ATOM   5225 C CA  . TYR B 1 229 ? 12.548  0.929   26.798  1.00 25.31  ? 258 TYR B CA  1 
ATOM   5226 C C   . TYR B 1 229 ? 11.883  1.135   25.436  1.00 23.30  ? 258 TYR B C   1 
ATOM   5227 O O   . TYR B 1 229 ? 12.303  1.999   24.672  1.00 25.42  ? 258 TYR B O   1 
ATOM   5228 C CB  . TYR B 1 229 ? 13.489  -0.286  26.819  1.00 26.14  ? 258 TYR B CB  1 
ATOM   5229 C CG  . TYR B 1 229 ? 14.580  -0.230  25.758  1.00 27.34  ? 258 TYR B CG  1 
ATOM   5230 C CD1 . TYR B 1 229 ? 14.258  -0.468  24.440  1.00 30.08  ? 258 TYR B CD1 1 
ATOM   5231 C CD2 . TYR B 1 229 ? 15.903  0.063   26.046  1.00 32.31  ? 258 TYR B CD2 1 
ATOM   5232 C CE1 . TYR B 1 229 ? 15.193  -0.425  23.442  1.00 31.37  ? 258 TYR B CE1 1 
ATOM   5233 C CE2 . TYR B 1 229 ? 16.860  0.128   25.037  1.00 33.43  ? 258 TYR B CE2 1 
ATOM   5234 C CZ  . TYR B 1 229 ? 16.494  -0.099  23.725  1.00 35.67  ? 258 TYR B CZ  1 
ATOM   5235 O OH  . TYR B 1 229 ? 17.317  -0.085  22.630  1.00 36.26  ? 258 TYR B OH  1 
ATOM   5236 N N   . LEU B 1 230 ? 10.857  0.331   25.127  1.00 24.46  ? 259 LEU B N   1 
ATOM   5237 C CA  . LEU B 1 230 ? 10.148  0.382   23.862  1.00 23.32  ? 259 LEU B CA  1 
ATOM   5238 C C   . LEU B 1 230 ? 9.324   1.668   23.749  1.00 24.11  ? 259 LEU B C   1 
ATOM   5239 O O   . LEU B 1 230 ? 9.173   2.192   22.666  1.00 20.87  ? 259 LEU B O   1 
ATOM   5240 C CB  . LEU B 1 230 ? 9.275   -0.859  23.697  1.00 23.80  ? 259 LEU B CB  1 
ATOM   5241 C CG  . LEU B 1 230 ? 10.070  -2.169  23.583  1.00 24.27  ? 259 LEU B CG  1 
ATOM   5242 C CD1 . LEU B 1 230 ? 9.123   -3.365  23.464  1.00 25.68  ? 259 LEU B CD1 1 
ATOM   5243 C CD2 . LEU B 1 230 ? 11.066  -2.134  22.414  1.00 26.94  ? 259 LEU B CD2 1 
ATOM   5244 N N   . THR B 1 231 ? 8.845   2.201   24.869  1.00 21.52  ? 260 THR B N   1 
ATOM   5245 C CA  . THR B 1 231 ? 8.117   3.454   24.900  1.00 22.17  ? 260 THR B CA  1 
ATOM   5246 C C   . THR B 1 231 ? 9.094   4.602   24.621  1.00 21.65  ? 260 THR B C   1 
ATOM   5247 O O   . THR B 1 231 ? 8.855   5.405   23.729  1.00 26.11  ? 260 THR B O   1 
ATOM   5248 C CB  . THR B 1 231 ? 7.357   3.597   26.234  1.00 22.41  ? 260 THR B CB  1 
ATOM   5249 O OG1 . THR B 1 231 ? 6.326   2.610   26.244  1.00 22.11  ? 260 THR B OG1 1 
ATOM   5250 C CG2 . THR B 1 231 ? 6.737   4.982   26.375  1.00 24.37  ? 260 THR B CG2 1 
ATOM   5251 N N   . ILE B 1 232 ? 10.221  4.680   25.326  1.00 22.40  ? 261 ILE B N   1 
ATOM   5252 C CA  . ILE B 1 232 ? 11.035  5.885   25.282  1.00 25.51  ? 261 ILE B CA  1 
ATOM   5253 C C   . ILE B 1 232 ? 11.908  5.988   24.034  1.00 25.44  ? 261 ILE B C   1 
ATOM   5254 O O   . ILE B 1 232 ? 12.355  7.087   23.723  1.00 25.35  ? 261 ILE B O   1 
ATOM   5255 C CB  . ILE B 1 232 ? 11.881  6.074   26.554  1.00 26.99  ? 261 ILE B CB  1 
ATOM   5256 C CG1 . ILE B 1 232 ? 12.979  5.040   26.699  1.00 28.77  ? 261 ILE B CG1 1 
ATOM   5257 C CG2 . ILE B 1 232 ? 10.942  6.128   27.751  1.00 26.93  ? 261 ILE B CG2 1 
ATOM   5258 C CD1 . ILE B 1 232 ? 13.734  5.109   28.032  1.00 31.42  ? 261 ILE B CD1 1 
ATOM   5259 N N   . HIS B 1 233 ? 12.219  4.878   23.371  1.00 23.52  ? 262 HIS B N   1 
ATOM   5260 C CA  . HIS B 1 233 ? 13.026  4.973   22.160  1.00 24.89  ? 262 HIS B CA  1 
ATOM   5261 C C   . HIS B 1 233 ? 12.155  5.095   20.909  1.00 21.77  ? 262 HIS B C   1 
ATOM   5262 O O   . HIS B 1 233 ? 12.690  5.087   19.808  1.00 18.96  ? 262 HIS B O   1 
ATOM   5263 C CB  . HIS B 1 233 ? 13.957  3.760   22.058  1.00 26.98  ? 262 HIS B CB  1 
ATOM   5264 C CG  . HIS B 1 233 ? 15.104  3.803   23.010  1.00 33.86  ? 262 HIS B CG  1 
ATOM   5265 N ND1 . HIS B 1 233 ? 14.938  3.472   24.340  1.00 36.48  ? 262 HIS B ND1 1 
ATOM   5266 C CD2 . HIS B 1 233 ? 16.416  4.037   22.847  1.00 38.60  ? 262 HIS B CD2 1 
ATOM   5267 C CE1 . HIS B 1 233 ? 16.110  3.577   24.970  1.00 40.05  ? 262 HIS B CE1 1 
ATOM   5268 N NE2 . HIS B 1 233 ? 17.021  3.899   24.081  1.00 41.59  ? 262 HIS B NE2 1 
ATOM   5269 N N   . SER B 1 234 ? 10.836  5.230   21.080  1.00 19.78  ? 263 SER B N   1 
ATOM   5270 C CA  . SER B 1 234 ? 9.855   5.055   20.022  1.00 18.72  ? 263 SER B CA  1 
ATOM   5271 C C   . SER B 1 234 ? 9.987   6.080   18.896  1.00 19.86  ? 263 SER B C   1 
ATOM   5272 O O   . SER B 1 234 ? 9.732   5.761   17.738  1.00 19.12  ? 263 SER B O   1 
ATOM   5273 C CB  . SER B 1 234 ? 8.492   5.044   20.598  1.00 19.40  ? 263 SER B CB  1 
ATOM   5274 O OG  . SER B 1 234 ? 8.141   6.288   21.195  1.00 21.29  ? 263 SER B OG  1 
ATOM   5275 N N   . ASP B 1 235 ? 10.344  7.318   19.239  1.00 20.94  ? 264 ASP B N   1 
ATOM   5276 C CA  . ASP B 1 235 ? 10.343  8.404   18.274  1.00 24.42  ? 264 ASP B CA  1 
ATOM   5277 C C   . ASP B 1 235 ? 11.271  9.491   18.791  1.00 23.48  ? 264 ASP B C   1 
ATOM   5278 O O   . ASP B 1 235 ? 11.364  9.701   20.006  1.00 23.51  ? 264 ASP B O   1 
ATOM   5279 C CB  . ASP B 1 235 ? 8.914   8.910   18.021  1.00 23.38  ? 264 ASP B CB  1 
ATOM   5280 C CG  . ASP B 1 235 ? 8.678   9.453   16.612  1.00 26.74  ? 264 ASP B CG  1 
ATOM   5281 O OD1 . ASP B 1 235 ? 9.161   8.812   15.653  1.00 23.26  ? 264 ASP B OD1 1 
ATOM   5282 O OD2 . ASP B 1 235 ? 8.056   10.534  16.484  1.00 29.26  ? 264 ASP B OD2 1 
ATOM   5283 N N   . HIS B 1 236 ? 11.976  10.146  17.869  1.00 22.42  ? 265 HIS B N   1 
ATOM   5284 C CA  . HIS B 1 236 ? 12.788  11.299  18.196  1.00 20.77  ? 265 HIS B CA  1 
ATOM   5285 C C   . HIS B 1 236 ? 12.867  12.300  17.038  1.00 22.39  ? 265 HIS B C   1 
ATOM   5286 O O   . HIS B 1 236 ? 13.963  12.579  16.502  1.00 21.21  ? 265 HIS B O   1 
ATOM   5287 C CB  . HIS B 1 236 ? 14.170  10.839  18.668  1.00 23.44  ? 265 HIS B CB  1 
ATOM   5288 C CG  . HIS B 1 236 ? 14.851  11.825  19.559  1.00 29.19  ? 265 HIS B CG  1 
ATOM   5289 N ND1 . HIS B 1 236 ? 15.576  12.912  19.119  1.00 38.76  ? 265 HIS B ND1 1 
ATOM   5290 C CD2 . HIS B 1 236 ? 14.919  11.855  20.891  1.00 32.22  ? 265 HIS B CD2 1 
ATOM   5291 C CE1 . HIS B 1 236 ? 16.085  13.542  20.175  1.00 41.22  ? 265 HIS B CE1 1 
ATOM   5292 N NE2 . HIS B 1 236 ? 15.667  12.922  21.257  1.00 34.40  ? 265 HIS B NE2 1 
ATOM   5293 N N   . GLU B 1 237 ? 11.711  12.826  16.639  1.00 22.92  ? 266 GLU B N   1 
ATOM   5294 C CA  . GLU B 1 237 ? 11.632  13.789  15.530  1.00 25.24  ? 266 GLU B CA  1 
ATOM   5295 C C   . GLU B 1 237 ? 11.920  13.058  14.215  1.00 23.55  ? 266 GLU B C   1 
ATOM   5296 O O   . GLU B 1 237 ? 12.145  11.848  14.189  1.00 21.69  ? 266 GLU B O   1 
ATOM   5297 C CB  . GLU B 1 237 ? 12.580  14.995  15.669  1.00 26.24  ? 266 GLU B CB  1 
ATOM   5298 C CG  . GLU B 1 237 ? 12.280  15.929  16.845  1.00 35.58  ? 266 GLU B CG  1 
ATOM   5299 C CD  . GLU B 1 237 ? 12.863  17.361  16.829  1.00 40.82  ? 266 GLU B CD  1 
ATOM   5300 O OE1 . GLU B 1 237 ? 13.961  17.558  16.235  1.00 36.33  ? 266 GLU B OE1 1 
ATOM   5301 O OE2 . GLU B 1 237 ? 12.221  18.306  17.412  1.00 31.50  ? 266 GLU B OE2 1 
ATOM   5302 N N   . GLY B 1 238 ? 11.924  13.811  13.115  1.00 24.74  ? 267 GLY B N   1 
ATOM   5303 C CA  . GLY B 1 238 ? 11.966  13.242  11.790  1.00 22.24  ? 267 GLY B CA  1 
ATOM   5304 C C   . GLY B 1 238 ? 13.369  13.223  11.200  1.00 22.71  ? 267 GLY B C   1 
ATOM   5305 O O   . GLY B 1 238 ? 13.572  12.596  10.136  1.00 22.20  ? 267 GLY B O   1 
ATOM   5306 N N   . GLY B 1 239 ? 14.283  13.986  11.823  1.00 21.52  ? 268 GLY B N   1 
ATOM   5307 C CA  . GLY B 1 239 ? 15.573  14.292  11.200  1.00 24.58  ? 268 GLY B CA  1 
ATOM   5308 C C   . GLY B 1 239 ? 16.662  13.252  11.498  1.00 24.94  ? 268 GLY B C   1 
ATOM   5309 O O   . GLY B 1 239 ? 17.728  13.292  10.906  1.00 23.70  ? 268 GLY B O   1 
ATOM   5310 N N   . ASN B 1 240 ? 16.423  12.333  12.440  1.00 21.40  ? 269 ASN B N   1 
ATOM   5311 C CA  . ASN B 1 240 ? 17.370  11.276  12.736  1.00 21.15  ? 269 ASN B CA  1 
ATOM   5312 C C   . ASN B 1 240 ? 17.348  10.337  11.525  1.00 20.98  ? 269 ASN B C   1 
ATOM   5313 O O   . ASN B 1 240 ? 16.367  10.295  10.783  1.00 20.21  ? 269 ASN B O   1 
ATOM   5314 C CB  . ASN B 1 240 ? 17.059  10.628  14.086  1.00 23.04  ? 269 ASN B CB  1 
ATOM   5315 C CG  . ASN B 1 240 ? 15.785  9.815   14.022  1.00 23.59  ? 269 ASN B CG  1 
ATOM   5316 O OD1 . ASN B 1 240 ? 15.712  8.723   13.437  1.00 24.41  ? 269 ASN B OD1 1 
ATOM   5317 N ND2 . ASN B 1 240 ? 14.739  10.340  14.610  1.00 26.01  ? 269 ASN B ND2 1 
ATOM   5318 N N   A VAL B 1 241 ? 18.424  9.567   11.342  0.50 21.90  ? 270 VAL B N   1 
ATOM   5319 N N   B VAL B 1 241 ? 18.422  9.575   11.329  0.50 23.62  ? 270 VAL B N   1 
ATOM   5320 C CA  A VAL B 1 241 ? 18.638  8.856   10.098  0.50 19.95  ? 270 VAL B CA  1 
ATOM   5321 C CA  B VAL B 1 241 ? 18.612  8.895   10.066  0.50 23.03  ? 270 VAL B CA  1 
ATOM   5322 C C   A VAL B 1 241 ? 17.523  7.835   9.891   0.50 19.17  ? 270 VAL B C   1 
ATOM   5323 C C   B VAL B 1 241 ? 17.538  7.823   9.881   0.50 20.67  ? 270 VAL B C   1 
ATOM   5324 O O   A VAL B 1 241 ? 17.052  7.662   8.775   0.50 18.60  ? 270 VAL B O   1 
ATOM   5325 O O   B VAL B 1 241 ? 17.100  7.608   8.758   0.50 19.68  ? 270 VAL B O   1 
ATOM   5326 C CB  A VAL B 1 241 ? 20.014  8.174   9.979   0.50 18.92  ? 270 VAL B CB  1 
ATOM   5327 C CB  B VAL B 1 241 ? 20.021  8.300   9.899   0.50 24.98  ? 270 VAL B CB  1 
ATOM   5328 C CG1 A VAL B 1 241 ? 20.182  7.471   8.629   0.50 16.49  ? 270 VAL B CG1 1 
ATOM   5329 C CG1 B VAL B 1 241 ? 21.069  9.362   9.612   0.50 29.92  ? 270 VAL B CG1 1 
ATOM   5330 C CG2 A VAL B 1 241 ? 21.129  9.179   10.165  0.50 22.40  ? 270 VAL B CG2 1 
ATOM   5331 C CG2 B VAL B 1 241 ? 20.410  7.494   11.107  0.50 25.16  ? 270 VAL B CG2 1 
ATOM   5332 N N   . SER B 1 242 ? 17.148  7.129   10.950  1.00 18.26  ? 271 SER B N   1 
ATOM   5333 C CA  . SER B 1 242 ? 16.128  6.090   10.800  1.00 19.14  ? 271 SER B CA  1 
ATOM   5334 C C   . SER B 1 242 ? 14.754  6.684   10.480  1.00 19.10  ? 271 SER B C   1 
ATOM   5335 O O   . SER B 1 242 ? 14.103  6.276   9.497   1.00 20.56  ? 271 SER B O   1 
ATOM   5336 C CB  . SER B 1 242 ? 16.135  5.115   11.964  1.00 21.60  ? 271 SER B CB  1 
ATOM   5337 O OG  . SER B 1 242 ? 15.776  5.693   13.197  1.00 22.45  ? 271 SER B OG  1 
ATOM   5338 N N   . ALA B 1 243 ? 14.357  7.766   11.161  1.00 17.35  ? 272 ALA B N   1 
ATOM   5339 C CA  . ALA B 1 243 ? 13.077  8.382   10.823  1.00 17.22  ? 272 ALA B CA  1 
ATOM   5340 C C   . ALA B 1 243 ? 13.109  8.981   9.411   1.00 16.03  ? 272 ALA B C   1 
ATOM   5341 O O   . ALA B 1 243 ? 12.191  8.765   8.644   1.00 16.03  ? 272 ALA B O   1 
ATOM   5342 C CB  . ALA B 1 243 ? 12.645  9.425   11.834  1.00 17.20  ? 272 ALA B CB  1 
ATOM   5343 N N   . HIS B 1 244 ? 14.181  9.711   9.101   1.00 17.13  ? 273 HIS B N   1 
ATOM   5344 C CA  . HIS B 1 244 ? 14.280  10.374  7.827   1.00 16.59  ? 273 HIS B CA  1 
ATOM   5345 C C   . HIS B 1 244 ? 14.245  9.334   6.709   1.00 17.75  ? 273 HIS B C   1 
ATOM   5346 O O   . HIS B 1 244 ? 13.630  9.554   5.645   1.00 16.62  ? 273 HIS B O   1 
ATOM   5347 C CB  . HIS B 1 244 ? 15.464  11.347  7.810   1.00 19.70  ? 273 HIS B CB  1 
ATOM   5348 C CG  . HIS B 1 244 ? 15.570  12.145  6.554   1.00 21.05  ? 273 HIS B CG  1 
ATOM   5349 N ND1 . HIS B 1 244 ? 16.710  12.841  6.215   1.00 20.91  ? 273 HIS B ND1 1 
ATOM   5350 C CD2 . HIS B 1 244 ? 14.682  12.376  5.561   1.00 20.36  ? 273 HIS B CD2 1 
ATOM   5351 C CE1 . HIS B 1 244 ? 16.514  13.447  5.045   1.00 20.31  ? 273 HIS B CE1 1 
ATOM   5352 N NE2 . HIS B 1 244 ? 15.318  13.147  4.616   1.00 20.59  ? 273 HIS B NE2 1 
ATOM   5353 N N   . THR B 1 245 ? 14.989  8.238   6.902   1.00 17.49  ? 274 THR B N   1 
ATOM   5354 C CA  . THR B 1 245 ? 15.045  7.220   5.865   1.00 16.14  ? 274 THR B CA  1 
ATOM   5355 C C   . THR B 1 245 ? 13.645  6.658   5.614   1.00 14.68  ? 274 THR B C   1 
ATOM   5356 O O   . THR B 1 245 ? 13.204  6.499   4.493   1.00 15.18  ? 274 THR B O   1 
ATOM   5357 C CB  . THR B 1 245 ? 16.058  6.146   6.287   1.00 16.48  ? 274 THR B CB  1 
ATOM   5358 O OG1 . THR B 1 245 ? 17.361  6.748   6.345   1.00 15.82  ? 274 THR B OG1 1 
ATOM   5359 C CG2 . THR B 1 245 ? 16.083  4.993   5.305   1.00 16.64  ? 274 THR B CG2 1 
ATOM   5360 N N   . SER B 1 246 ? 12.909  6.365   6.683   1.00 15.66  ? 275 SER B N   1 
ATOM   5361 C CA  . SER B 1 246 ? 11.581  5.811   6.522   1.00 17.19  ? 275 SER B CA  1 
ATOM   5362 C C   . SER B 1 246 ? 10.707  6.783   5.746   1.00 15.32  ? 275 SER B C   1 
ATOM   5363 O O   . SER B 1 246 ? 9.852   6.393   4.968   1.00 16.52  ? 275 SER B O   1 
ATOM   5364 C CB  . SER B 1 246 ? 10.985  5.423   7.855   1.00 18.22  ? 275 SER B CB  1 
ATOM   5365 O OG  . SER B 1 246 ? 10.475  6.516   8.599   1.00 23.72  ? 275 SER B OG  1 
ATOM   5366 N N   . HIS B 1 247 ? 10.871  8.067   6.075   1.00 18.10  ? 276 HIS B N   1 
ATOM   5367 C CA  . HIS B 1 247 ? 10.103  9.148   5.523   1.00 17.00  ? 276 HIS B CA  1 
ATOM   5368 C C   . HIS B 1 247 ? 10.361  9.248   4.033   1.00 16.01  ? 276 HIS B C   1 
ATOM   5369 O O   . HIS B 1 247 ? 9.432   9.379   3.244   1.00 18.74  ? 276 HIS B O   1 
ATOM   5370 C CB  . HIS B 1 247 ? 10.473  10.438  6.278   1.00 18.14  ? 276 HIS B CB  1 
ATOM   5371 C CG  . HIS B 1 247 ? 9.585   11.590  5.962   1.00 22.23  ? 276 HIS B CG  1 
ATOM   5372 N ND1 . HIS B 1 247 ? 8.308   11.670  6.488   1.00 22.79  ? 276 HIS B ND1 1 
ATOM   5373 C CD2 . HIS B 1 247 ? 9.761   12.710  5.246   1.00 25.67  ? 276 HIS B CD2 1 
ATOM   5374 C CE1 . HIS B 1 247 ? 7.746   12.806  6.114   1.00 24.54  ? 276 HIS B CE1 1 
ATOM   5375 N NE2 . HIS B 1 247 ? 8.609   13.457  5.362   1.00 26.39  ? 276 HIS B NE2 1 
ATOM   5376 N N   . LEU B 1 248 ? 11.659  9.210   3.691   1.00 15.51  ? 277 LEU B N   1 
ATOM   5377 C CA  . LEU B 1 248 ? 12.111  9.420   2.347   1.00 14.34  ? 277 LEU B CA  1 
ATOM   5378 C C   . LEU B 1 248 ? 11.671  8.239   1.477   1.00 15.20  ? 277 LEU B C   1 
ATOM   5379 O O   . LEU B 1 248 ? 11.114  8.453   0.420   1.00 17.10  ? 277 LEU B O   1 
ATOM   5380 C CB  . LEU B 1 248 ? 13.632  9.576   2.404   1.00 16.74  ? 277 LEU B CB  1 
ATOM   5381 C CG  . LEU B 1 248 ? 14.327  9.421   1.047   1.00 17.18  ? 277 LEU B CG  1 
ATOM   5382 C CD1 . LEU B 1 248 ? 13.796  10.460  0.110   1.00 20.17  ? 277 LEU B CD1 1 
ATOM   5383 C CD2 . LEU B 1 248 ? 15.821  9.520   1.246   1.00 20.47  ? 277 LEU B CD2 1 
ATOM   5384 N N   . VAL B 1 249 ? 11.889  6.998   1.967   1.00 15.85  ? 278 VAL B N   1 
ATOM   5385 C CA  . VAL B 1 249 ? 11.548  5.815   1.213   1.00 14.76  ? 278 VAL B CA  1 
ATOM   5386 C C   . VAL B 1 249 ? 10.010  5.701   1.151   1.00 17.51  ? 278 VAL B C   1 
ATOM   5387 O O   . VAL B 1 249 ? 9.429   5.429   0.092   1.00 15.51  ? 278 VAL B O   1 
ATOM   5388 C CB  . VAL B 1 249 ? 12.232  4.565   1.811   1.00 17.39  ? 278 VAL B CB  1 
ATOM   5389 C CG1 . VAL B 1 249 ? 11.660  3.249   1.308   1.00 17.95  ? 278 VAL B CG1 1 
ATOM   5390 C CG2 . VAL B 1 249 ? 13.740  4.569   1.569   1.00 19.22  ? 278 VAL B CG2 1 
ATOM   5391 N N   . GLY B 1 250 ? 9.330   6.030   2.238   1.00 16.31  ? 279 GLY B N   1 
ATOM   5392 C CA  . GLY B 1 250 ? 7.859   6.055   2.206   1.00 17.05  ? 279 GLY B CA  1 
ATOM   5393 C C   . GLY B 1 250 ? 7.277   7.054   1.190   1.00 18.30  ? 279 GLY B C   1 
ATOM   5394 O O   . GLY B 1 250 ? 6.187   6.826   0.674   1.00 17.41  ? 279 GLY B O   1 
ATOM   5395 N N   . SER B 1 251 ? 7.960   8.203   0.990   1.00 16.55  ? 280 SER B N   1 
ATOM   5396 C CA  . SER B 1 251 ? 7.489   9.252   0.114   1.00 18.68  ? 280 SER B CA  1 
ATOM   5397 C C   . SER B 1 251 ? 7.429   8.758   -1.335  1.00 17.79  ? 280 SER B C   1 
ATOM   5398 O O   . SER B 1 251 ? 6.704   9.332   -2.140  1.00 20.25  ? 280 SER B O   1 
ATOM   5399 C CB  . SER B 1 251 ? 8.356   10.496  0.246   1.00 17.95  ? 280 SER B CB  1 
ATOM   5400 O OG  . SER B 1 251 ? 9.560   10.360  -0.519  1.00 16.44  ? 280 SER B OG  1 
ATOM   5401 N N   . ALA B 1 252 ? 8.119   7.676   -1.665  1.00 17.66  ? 281 ALA B N   1 
ATOM   5402 C CA  . ALA B 1 252 ? 8.020   7.069   -2.997  1.00 17.00  ? 281 ALA B CA  1 
ATOM   5403 C C   . ALA B 1 252 ? 6.904   6.033   -3.093  1.00 18.44  ? 281 ALA B C   1 
ATOM   5404 O O   . ALA B 1 252 ? 6.750   5.362   -4.107  1.00 18.31  ? 281 ALA B O   1 
ATOM   5405 C CB  . ALA B 1 252 ? 9.333   6.455   -3.352  1.00 18.56  ? 281 ALA B CB  1 
ATOM   5406 N N   . LEU B 1 253 ? 6.088   5.930   -2.032  1.00 18.60  ? 282 LEU B N   1 
ATOM   5407 C CA  . LEU B 1 253 ? 4.980   5.012   -1.918  1.00 19.15  ? 282 LEU B CA  1 
ATOM   5408 C C   . LEU B 1 253 ? 5.454   3.569   -1.748  1.00 21.27  ? 282 LEU B C   1 
ATOM   5409 O O   . LEU B 1 253 ? 4.703   2.639   -2.007  1.00 17.77  ? 282 LEU B O   1 
ATOM   5410 C CB  . LEU B 1 253 ? 3.931   5.179   -3.021  1.00 22.42  ? 282 LEU B CB  1 
ATOM   5411 C CG  . LEU B 1 253 ? 3.275   6.553   -3.070  1.00 23.32  ? 282 LEU B CG  1 
ATOM   5412 C CD1 . LEU B 1 253 ? 2.156   6.663   -4.071  1.00 23.26  ? 282 LEU B CD1 1 
ATOM   5413 C CD2 . LEU B 1 253 ? 2.767   6.895   -1.683  1.00 25.08  ? 282 LEU B CD2 1 
ATOM   5414 N N   . SER B 1 254 ? 6.721   3.369   -1.348  1.00 22.13  ? 283 SER B N   1 
ATOM   5415 C CA  . SER B 1 254 ? 7.136   2.059   -0.866  1.00 21.12  ? 283 SER B CA  1 
ATOM   5416 C C   . SER B 1 254 ? 6.312   1.772   0.382   1.00 23.26  ? 283 SER B C   1 
ATOM   5417 O O   . SER B 1 254 ? 6.039   2.703   1.185   1.00 24.47  ? 283 SER B O   1 
ATOM   5418 C CB  . SER B 1 254 ? 8.621   2.042   -0.598  1.00 21.43  ? 283 SER B CB  1 
ATOM   5419 O OG  . SER B 1 254 ? 9.374   2.421   -1.748  1.00 23.67  ? 283 SER B OG  1 
ATOM   5420 N N   . ASP B 1 255 ? 5.871   0.509   0.502   1.00 21.55  ? 284 ASP B N   1 
ATOM   5421 C CA  . ASP B 1 255 ? 5.033   0.077   1.616   1.00 22.09  ? 284 ASP B CA  1 
ATOM   5422 C C   . ASP B 1 255 ? 5.803   0.159   2.941   1.00 19.27  ? 284 ASP B C   1 
ATOM   5423 O O   . ASP B 1 255 ? 7.025   0.391   3.001   1.00 18.80  ? 284 ASP B O   1 
ATOM   5424 C CB  . ASP B 1 255 ? 4.419   -1.287  1.327   1.00 23.45  ? 284 ASP B CB  1 
ATOM   5425 C CG  . ASP B 1 255 ? 5.412   -2.434  1.266   1.00 28.62  ? 284 ASP B CG  1 
ATOM   5426 O OD1 . ASP B 1 255 ? 6.040   -2.678  2.294   1.00 28.06  ? 284 ASP B OD1 1 
ATOM   5427 O OD2 . ASP B 1 255 ? 5.653   -2.963  0.157   1.00 23.82  ? 284 ASP B OD2 1 
ATOM   5428 N N   . PRO B 1 256 ? 5.110   -0.001  4.084   1.00 17.65  ? 285 PRO B N   1 
ATOM   5429 C CA  . PRO B 1 256 ? 5.745   0.086   5.377   1.00 18.08  ? 285 PRO B CA  1 
ATOM   5430 C C   . PRO B 1 256 ? 6.897   -0.884  5.586   1.00 19.57  ? 285 PRO B C   1 
ATOM   5431 O O   . PRO B 1 256 ? 7.808   -0.587  6.351   1.00 18.10  ? 285 PRO B O   1 
ATOM   5432 C CB  . PRO B 1 256 ? 4.579   -0.138  6.363   1.00 19.07  ? 285 PRO B CB  1 
ATOM   5433 C CG  . PRO B 1 256 ? 3.405   0.341   5.568   1.00 19.98  ? 285 PRO B CG  1 
ATOM   5434 C CD  . PRO B 1 256 ? 3.646   -0.209  4.190   1.00 19.71  ? 285 PRO B CD  1 
ATOM   5435 N N   . TYR B 1 257 ? 6.809   -2.092  4.986   1.00 20.83  ? 286 TYR B N   1 
ATOM   5436 C CA  . TYR B 1 257 ? 7.872   -3.071  5.167   1.00 22.34  ? 286 TYR B CA  1 
ATOM   5437 C C   . TYR B 1 257 ? 9.175   -2.558  4.548   1.00 19.38  ? 286 TYR B C   1 
ATOM   5438 O O   . TYR B 1 257 ? 10.235  -2.560  5.187   1.00 19.61  ? 286 TYR B O   1 
ATOM   5439 C CB  . TYR B 1 257 ? 7.502   -4.445  4.609   1.00 22.08  ? 286 TYR B CB  1 
ATOM   5440 C CG  . TYR B 1 257 ? 6.279   -5.062  5.282   1.00 26.00  ? 286 TYR B CG  1 
ATOM   5441 C CD1 . TYR B 1 257 ? 6.390   -5.809  6.451   1.00 23.56  ? 286 TYR B CD1 1 
ATOM   5442 C CD2 . TYR B 1 257 ? 5.012   -4.911  4.742   1.00 25.39  ? 286 TYR B CD2 1 
ATOM   5443 C CE1 . TYR B 1 257 ? 5.286   -6.375  7.054   1.00 21.12  ? 286 TYR B CE1 1 
ATOM   5444 C CE2 . TYR B 1 257 ? 3.898   -5.486  5.338   1.00 22.80  ? 286 TYR B CE2 1 
ATOM   5445 C CZ  . TYR B 1 257 ? 4.037   -6.237  6.489   1.00 23.67  ? 286 TYR B CZ  1 
ATOM   5446 O OH  . TYR B 1 257 ? 2.927   -6.793  7.102   1.00 24.70  ? 286 TYR B OH  1 
ATOM   5447 N N   . LEU B 1 258 ? 9.104   -2.084  3.300   1.00 18.15  ? 287 LEU B N   1 
ATOM   5448 C CA  . LEU B 1 258 ? 10.297  -1.589  2.648   1.00 18.07  ? 287 LEU B CA  1 
ATOM   5449 C C   . LEU B 1 258 ? 10.838  -0.319  3.330   1.00 17.67  ? 287 LEU B C   1 
ATOM   5450 O O   . LEU B 1 258 ? 12.070  -0.092  3.427   1.00 17.28  ? 287 LEU B O   1 
ATOM   5451 C CB  . LEU B 1 258 ? 9.907   -1.321  1.204   1.00 20.01  ? 287 LEU B CB  1 
ATOM   5452 C CG  . LEU B 1 258 ? 9.480   -2.534  0.360   1.00 20.32  ? 287 LEU B CG  1 
ATOM   5453 C CD1 . LEU B 1 258 ? 9.238   -2.116  -1.053  1.00 20.97  ? 287 LEU B CD1 1 
ATOM   5454 C CD2 . LEU B 1 258 ? 10.485  -3.621  0.450   1.00 21.57  ? 287 LEU B CD2 1 
ATOM   5455 N N   . SER B 1 259 ? 9.907   0.549   3.765   1.00 17.70  ? 288 SER B N   1 
ATOM   5456 C CA  . SER B 1 259 ? 10.283  1.791   4.411   1.00 17.78  ? 288 SER B CA  1 
ATOM   5457 C C   . SER B 1 259 ? 11.005  1.499   5.716   1.00 19.41  ? 288 SER B C   1 
ATOM   5458 O O   . SER B 1 259 ? 11.999  2.148   6.050   1.00 18.74  ? 288 SER B O   1 
ATOM   5459 C CB  . SER B 1 259 ? 9.030   2.663   4.656   1.00 18.67  ? 288 SER B CB  1 
ATOM   5460 O OG  . SER B 1 259 ? 8.432   2.875   3.390   1.00 23.94  ? 288 SER B OG  1 
ATOM   5461 N N   . PHE B 1 260 ? 10.429  0.576   6.488   1.00 18.46  ? 289 PHE B N   1 
ATOM   5462 C CA  . PHE B 1 260 ? 10.987  0.254   7.786   1.00 18.45  ? 289 PHE B CA  1 
ATOM   5463 C C   . PHE B 1 260 ? 12.335  -0.459  7.633   1.00 17.56  ? 289 PHE B C   1 
ATOM   5464 O O   . PHE B 1 260 ? 13.303  -0.125  8.334   1.00 17.41  ? 289 PHE B O   1 
ATOM   5465 C CB  . PHE B 1 260 ? 9.980   -0.549  8.601   1.00 20.51  ? 289 PHE B CB  1 
ATOM   5466 C CG  . PHE B 1 260 ? 10.559  -0.839  9.982   1.00 17.68  ? 289 PHE B CG  1 
ATOM   5467 C CD1 . PHE B 1 260 ? 10.701  0.203   10.897  1.00 21.42  ? 289 PHE B CD1 1 
ATOM   5468 C CD2 . PHE B 1 260 ? 11.019  -2.086  10.337  1.00 17.67  ? 289 PHE B CD2 1 
ATOM   5469 C CE1 . PHE B 1 260 ? 11.205  -0.038  12.160  1.00 19.45  ? 289 PHE B CE1 1 
ATOM   5470 C CE2 . PHE B 1 260 ? 11.545  -2.322  11.602  1.00 20.22  ? 289 PHE B CE2 1 
ATOM   5471 C CZ  . PHE B 1 260 ? 11.605  -1.314  12.508  1.00 20.33  ? 289 PHE B CZ  1 
ATOM   5472 N N   . ALA B 1 261 ? 12.450  -1.327  6.630   1.00 17.05  ? 290 ALA B N   1 
ATOM   5473 C CA  . ALA B 1 261 ? 13.710  -2.035  6.429   1.00 20.08  ? 290 ALA B CA  1 
ATOM   5474 C C   . ALA B 1 261 ? 14.824  -1.061  6.080   1.00 18.16  ? 290 ALA B C   1 
ATOM   5475 O O   . ALA B 1 261 ? 15.971  -1.226  6.519   1.00 17.07  ? 290 ALA B O   1 
ATOM   5476 C CB  . ALA B 1 261 ? 13.584  -3.079  5.369   1.00 20.31  ? 290 ALA B CB  1 
ATOM   5477 N N   . ALA B 1 262 ? 14.518  -0.097  5.208   1.00 19.60  ? 291 ALA B N   1 
ATOM   5478 C CA  . ALA B 1 262 ? 15.500  0.899   4.813   1.00 22.62  ? 291 ALA B CA  1 
ATOM   5479 C C   . ALA B 1 262 ? 15.926  1.668   6.065   1.00 19.89  ? 291 ALA B C   1 
ATOM   5480 O O   . ALA B 1 262 ? 17.111  1.890   6.271   1.00 17.40  ? 291 ALA B O   1 
ATOM   5481 C CB  . ALA B 1 262 ? 14.939  1.824   3.719   1.00 19.64  ? 291 ALA B CB  1 
ATOM   5482 N N   . ALA B 1 263 ? 14.951  2.052   6.901   1.00 17.87  ? 292 ALA B N   1 
ATOM   5483 C CA  . ALA B 1 263 ? 15.213  2.701   8.172   1.00 18.47  ? 292 ALA B CA  1 
ATOM   5484 C C   . ALA B 1 263 ? 16.198  1.923   9.054   1.00 18.35  ? 292 ALA B C   1 
ATOM   5485 O O   . ALA B 1 263 ? 17.036  2.508   9.748   1.00 17.31  ? 292 ALA B O   1 
ATOM   5486 C CB  . ALA B 1 263 ? 13.949  2.963   8.971   1.00 18.67  ? 292 ALA B CB  1 
ATOM   5487 N N   . MET B 1 264 ? 16.093  0.601   9.012   1.00 19.00  ? 293 MET B N   1 
ATOM   5488 C CA  . MET B 1 264 ? 16.898  -0.249  9.868   1.00 18.17  ? 293 MET B CA  1 
ATOM   5489 C C   . MET B 1 264 ? 18.319  -0.308  9.327   1.00 18.97  ? 293 MET B C   1 
ATOM   5490 O O   . MET B 1 264 ? 19.276  -0.357  10.087  1.00 21.66  ? 293 MET B O   1 
ATOM   5491 C CB  . MET B 1 264 ? 16.328  -1.658  9.999   1.00 17.72  ? 293 MET B CB  1 
ATOM   5492 C CG  . MET B 1 264 ? 15.043  -1.720  10.759  1.00 19.61  ? 293 MET B CG  1 
ATOM   5493 S SD  . MET B 1 264 ? 15.116  -1.132  12.468  1.00 22.45  ? 293 MET B SD  1 
ATOM   5494 C CE  . MET B 1 264 ? 14.648  0.594   12.290  1.00 27.66  ? 293 MET B CE  1 
ATOM   5495 N N   . ASN B 1 265 ? 18.458  -0.168  8.021   1.00 17.71  ? 294 ASN B N   1 
ATOM   5496 C CA  . ASN B 1 265 ? 19.784  -0.053  7.442   1.00 18.47  ? 294 ASN B CA  1 
ATOM   5497 C C   . ASN B 1 265 ? 20.448  1.233   7.912   1.00 16.35  ? 294 ASN B C   1 
ATOM   5498 O O   . ASN B 1 265 ? 21.657  1.242   8.086   1.00 18.91  ? 294 ASN B O   1 
ATOM   5499 C CB  . ASN B 1 265 ? 19.736  -0.264  5.925   1.00 19.68  ? 294 ASN B CB  1 
ATOM   5500 C CG  . ASN B 1 265 ? 19.613  -1.727  5.511   1.00 25.81  ? 294 ASN B CG  1 
ATOM   5501 O OD1 . ASN B 1 265 ? 19.433  -2.634  6.322   1.00 27.37  ? 294 ASN B OD1 1 
ATOM   5502 N ND2 . ASN B 1 265 ? 19.696  -2.015  4.233   1.00 28.16  ? 294 ASN B ND2 1 
ATOM   5503 N N   . GLY B 1 266 ? 19.694  2.324   8.081   1.00 16.24  ? 295 GLY B N   1 
ATOM   5504 C CA  . GLY B 1 266 ? 20.217  3.579   8.586   1.00 17.52  ? 295 GLY B CA  1 
ATOM   5505 C C   . GLY B 1 266 ? 20.532  3.479   10.068  1.00 19.31  ? 295 GLY B C   1 
ATOM   5506 O O   . GLY B 1 266 ? 21.610  3.863   10.484  1.00 20.12  ? 295 GLY B O   1 
ATOM   5507 N N   . LEU B 1 267 ? 19.648  2.822   10.824  1.00 18.14  ? 296 LEU B N   1 
ATOM   5508 C CA  . LEU B 1 267 ? 19.868  2.602   12.245  1.00 21.03  ? 296 LEU B CA  1 
ATOM   5509 C C   . LEU B 1 267 ? 21.102  1.735   12.516  1.00 23.64  ? 296 LEU B C   1 
ATOM   5510 O O   . LEU B 1 267 ? 21.746  1.900   13.556  1.00 23.09  ? 296 LEU B O   1 
ATOM   5511 C CB  . LEU B 1 267 ? 18.619  1.999   12.885  1.00 21.01  ? 296 LEU B CB  1 
ATOM   5512 C CG  . LEU B 1 267 ? 18.639  1.907   14.422  1.00 24.89  ? 296 LEU B CG  1 
ATOM   5513 C CD1 . LEU B 1 267 ? 18.733  3.340   14.998  1.00 25.36  ? 296 LEU B CD1 1 
ATOM   5514 C CD2 . LEU B 1 267 ? 17.382  1.234   14.934  1.00 22.59  ? 296 LEU B CD2 1 
ATOM   5515 N N   . ALA B 1 268 ? 21.475  0.887   11.546  1.00 23.05  ? 297 ALA B N   1 
ATOM   5516 C CA  . ALA B 1 268 ? 22.573  -0.041  11.731  1.00 22.25  ? 297 ALA B CA  1 
ATOM   5517 C C   . ALA B 1 268 ? 23.892  0.718   11.608  1.00 23.62  ? 297 ALA B C   1 
ATOM   5518 O O   . ALA B 1 268 ? 24.932  0.154   11.913  1.00 25.02  ? 297 ALA B O   1 
ATOM   5519 C CB  . ALA B 1 268 ? 22.469  -1.201  10.753  1.00 20.80  ? 297 ALA B CB  1 
ATOM   5520 N N   . GLY B 1 269 ? 23.842  1.962   11.127  1.00 21.26  ? 298 GLY B N   1 
ATOM   5521 C CA  . GLY B 1 269 ? 25.051  2.716   10.918  1.00 24.57  ? 298 GLY B CA  1 
ATOM   5522 C C   . GLY B 1 269 ? 25.708  2.998   12.269  1.00 25.12  ? 298 GLY B C   1 
ATOM   5523 O O   . GLY B 1 269 ? 25.021  3.351   13.237  1.00 26.55  ? 298 GLY B O   1 
ATOM   5524 N N   . PRO B 1 270 ? 27.047  2.886   12.360  1.00 25.15  ? 299 PRO B N   1 
ATOM   5525 C CA  . PRO B 1 270 ? 27.750  3.186   13.606  1.00 30.20  ? 299 PRO B CA  1 
ATOM   5526 C C   . PRO B 1 270 ? 27.490  4.563   14.224  1.00 34.22  ? 299 PRO B C   1 
ATOM   5527 O O   . PRO B 1 270 ? 27.546  4.703   15.447  1.00 38.04  ? 299 PRO B O   1 
ATOM   5528 C CB  . PRO B 1 270 ? 29.245  2.984   13.273  1.00 32.12  ? 299 PRO B CB  1 
ATOM   5529 C CG  . PRO B 1 270 ? 29.280  2.227   11.955  1.00 30.23  ? 299 PRO B CG  1 
ATOM   5530 C CD  . PRO B 1 270 ? 27.922  2.353   11.312  1.00 28.80  ? 299 PRO B CD  1 
ATOM   5531 N N   . LEU B 1 271 ? 27.183  5.571   13.408  1.00 32.70  ? 300 LEU B N   1 
ATOM   5532 C CA  . LEU B 1 271 ? 26.876  6.904   13.936  1.00 38.32  ? 300 LEU B CA  1 
ATOM   5533 C C   . LEU B 1 271 ? 25.410  7.085   14.353  1.00 41.99  ? 300 LEU B C   1 
ATOM   5534 O O   . LEU B 1 271 ? 25.087  8.176   14.833  1.00 47.09  ? 300 LEU B O   1 
ATOM   5535 C CB  . LEU B 1 271 ? 27.196  7.994   12.915  1.00 32.21  ? 300 LEU B CB  1 
ATOM   5536 C CG  . LEU B 1 271 ? 28.664  8.219   12.571  1.00 30.15  ? 300 LEU B CG  1 
ATOM   5537 C CD1 . LEU B 1 271 ? 28.774  9.431   11.643  1.00 28.95  ? 300 LEU B CD1 1 
ATOM   5538 C CD2 . LEU B 1 271 ? 29.535  8.413   13.808  1.00 39.11  ? 300 LEU B CD2 1 
ATOM   5539 N N   . HIS B 1 272 ? 24.520  6.107   14.096  1.00 41.00  ? 301 HIS B N   1 
ATOM   5540 C CA  . HIS B 1 272 ? 23.117  6.206   14.525  1.00 47.17  ? 301 HIS B CA  1 
ATOM   5541 C C   . HIS B 1 272 ? 22.769  5.256   15.683  1.00 47.96  ? 301 HIS B C   1 
ATOM   5542 O O   . HIS B 1 272 ? 22.236  5.678   16.710  1.00 50.01  ? 301 HIS B O   1 
ATOM   5543 C CB  . HIS B 1 272 ? 22.122  5.923   13.383  1.00 46.13  ? 301 HIS B CB  1 
ATOM   5544 C CG  . HIS B 1 272 ? 20.703  6.310   13.729  1.00 42.82  ? 301 HIS B CG  1 
ATOM   5545 N ND1 . HIS B 1 272 ? 20.421  7.045   14.850  1.00 39.21  ? 301 HIS B ND1 1 
ATOM   5546 C CD2 . HIS B 1 272 ? 19.485  6.106   13.148  1.00 47.98  ? 301 HIS B CD2 1 
ATOM   5547 C CE1 . HIS B 1 272 ? 19.107  7.267   14.944  1.00 45.18  ? 301 HIS B CE1 1 
ATOM   5548 N NE2 . HIS B 1 272 ? 18.499  6.726   13.911  1.00 31.39  ? 301 HIS B NE2 1 
ATOM   5549 N N   . GLY B 1 273 ? 23.034  3.957   15.526  1.00 42.94  ? 302 GLY B N   1 
ATOM   5550 C CA  . GLY B 1 273 ? 22.436  2.993   16.433  1.00 54.89  ? 302 GLY B CA  1 
ATOM   5551 C C   . GLY B 1 273 ? 23.424  2.201   17.290  1.00 47.66  ? 302 GLY B C   1 
ATOM   5552 O O   . GLY B 1 273 ? 22.995  1.204   17.870  1.00 44.99  ? 302 GLY B O   1 
ATOM   5553 N N   . LEU B 1 274 ? 24.693  2.640   17.421  1.00 49.67  ? 303 LEU B N   1 
ATOM   5554 C CA  . LEU B 1 274 ? 25.688  1.857   18.153  1.00 50.84  ? 303 LEU B CA  1 
ATOM   5555 C C   . LEU B 1 274 ? 26.210  2.535   19.423  1.00 54.65  ? 303 LEU B C   1 
ATOM   5556 O O   . LEU B 1 274 ? 27.263  2.173   19.935  1.00 64.15  ? 303 LEU B O   1 
ATOM   5557 C CB  . LEU B 1 274 ? 26.849  1.505   17.236  1.00 56.88  ? 303 LEU B CB  1 
ATOM   5558 C CG  . LEU B 1 274 ? 26.799  0.093   16.646  1.00 65.88  ? 303 LEU B CG  1 
ATOM   5559 C CD1 . LEU B 1 274 ? 25.836  -0.011  15.450  1.00 64.36  ? 303 LEU B CD1 1 
ATOM   5560 C CD2 . LEU B 1 274 ? 28.220  -0.313  16.287  1.00 69.01  ? 303 LEU B CD2 1 
ATOM   5561 N N   . ALA B 1 275 ? 25.455  3.465   19.989  1.00 49.12  ? 304 ALA B N   1 
ATOM   5562 C CA  . ALA B 1 275 ? 25.922  4.235   21.127  1.00 44.91  ? 304 ALA B CA  1 
ATOM   5563 C C   . ALA B 1 275 ? 25.777  3.439   22.424  1.00 44.62  ? 304 ALA B C   1 
ATOM   5564 O O   . ALA B 1 275 ? 26.514  3.656   23.384  1.00 48.16  ? 304 ALA B O   1 
ATOM   5565 C CB  . ALA B 1 275 ? 25.115  5.511   21.183  1.00 44.70  ? 304 ALA B CB  1 
ATOM   5566 N N   . ASN B 1 276 ? 24.748  2.591   22.467  1.00 36.84  ? 305 ASN B N   1 
ATOM   5567 C CA  . ASN B 1 276 ? 24.446  1.737   23.602  1.00 40.55  ? 305 ASN B CA  1 
ATOM   5568 C C   . ASN B 1 276 ? 25.657  0.858   23.890  1.00 38.01  ? 305 ASN B C   1 
ATOM   5569 O O   . ASN B 1 276 ? 26.186  0.816   25.009  1.00 37.71  ? 305 ASN B O   1 
ATOM   5570 C CB  . ASN B 1 276 ? 23.204  0.901   23.284  1.00 38.96  ? 305 ASN B CB  1 
ATOM   5571 C CG  . ASN B 1 276 ? 22.704  0.123   24.465  1.00 37.63  ? 305 ASN B CG  1 
ATOM   5572 O OD1 . ASN B 1 276 ? 23.488  -0.215  25.364  1.00 37.68  ? 305 ASN B OD1 1 
ATOM   5573 N ND2 . ASN B 1 276 ? 21.419  -0.212  24.447  1.00 36.60  ? 305 ASN B ND2 1 
ATOM   5574 N N   . GLN B 1 277 ? 26.103  0.212   22.819  1.00 37.34  ? 306 GLN B N   1 
ATOM   5575 C CA  . GLN B 1 277 ? 27.201  -0.739  22.847  1.00 39.62  ? 306 GLN B CA  1 
ATOM   5576 C C   . GLN B 1 277 ? 28.499  -0.082  23.300  1.00 40.04  ? 306 GLN B C   1 
ATOM   5577 O O   . GLN B 1 277 ? 29.167  -0.602  24.196  1.00 40.76  ? 306 GLN B O   1 
ATOM   5578 C CB  . GLN B 1 277 ? 27.314  -1.392  21.471  1.00 46.04  ? 306 GLN B CB  1 
ATOM   5579 C CG  . GLN B 1 277 ? 26.121  -2.285  21.142  1.00 45.36  ? 306 GLN B CG  1 
ATOM   5580 C CD  . GLN B 1 277 ? 24.978  -1.599  20.408  1.00 46.88  ? 306 GLN B CD  1 
ATOM   5581 O OE1 . GLN B 1 277 ? 24.597  -0.443  20.681  1.00 39.42  ? 306 GLN B OE1 1 
ATOM   5582 N NE2 . GLN B 1 277 ? 24.390  -2.355  19.482  1.00 41.29  ? 306 GLN B NE2 1 
ATOM   5583 N N   . GLU B 1 278 ? 28.845  1.058   22.706  1.00 46.78  ? 307 GLU B N   1 
ATOM   5584 C CA  . GLU B 1 278 ? 30.109  1.726   23.010  1.00 50.70  ? 307 GLU B CA  1 
ATOM   5585 C C   . GLU B 1 278 ? 30.159  2.076   24.501  1.00 44.48  ? 307 GLU B C   1 
ATOM   5586 O O   . GLU B 1 278 ? 31.155  1.865   25.186  1.00 42.00  ? 307 GLU B O   1 
ATOM   5587 C CB  . GLU B 1 278 ? 30.276  2.924   22.073  1.00 49.78  ? 307 GLU B CB  1 
ATOM   5588 C CG  . GLU B 1 278 ? 30.380  2.502   20.608  1.00 58.97  ? 307 GLU B CG  1 
ATOM   5589 C CD  . GLU B 1 278 ? 30.422  3.598   19.549  1.00 73.08  ? 307 GLU B CD  1 
ATOM   5590 O OE1 . GLU B 1 278 ? 30.235  4.790   19.900  1.00 81.48  ? 307 GLU B OE1 1 
ATOM   5591 O OE2 . GLU B 1 278 ? 30.673  3.260   18.359  1.00 76.36  ? 307 GLU B OE2 1 
ATOM   5592 N N   . VAL B 1 279 ? 29.044  2.556   25.039  1.00 44.06  ? 308 VAL B N   1 
ATOM   5593 C CA  . VAL B 1 279 ? 29.035  2.882   26.451  1.00 42.39  ? 308 VAL B CA  1 
ATOM   5594 C C   . VAL B 1 279 ? 29.352  1.621   27.253  1.00 42.42  ? 308 VAL B C   1 
ATOM   5595 O O   . VAL B 1 279 ? 30.242  1.643   28.101  1.00 44.55  ? 308 VAL B O   1 
ATOM   5596 C CB  . VAL B 1 279 ? 27.728  3.551   26.901  1.00 41.62  ? 308 VAL B CB  1 
ATOM   5597 C CG1 . VAL B 1 279 ? 27.696  3.786   28.410  1.00 38.29  ? 308 VAL B CG1 1 
ATOM   5598 C CG2 . VAL B 1 279 ? 27.476  4.855   26.149  1.00 42.67  ? 308 VAL B CG2 1 
ATOM   5599 N N   . LEU B 1 280 ? 28.635  0.523   26.988  1.00 40.11  ? 309 LEU B N   1 
ATOM   5600 C CA  . LEU B 1 280 ? 28.740  -0.661  27.835  1.00 39.89  ? 309 LEU B CA  1 
ATOM   5601 C C   . LEU B 1 280 ? 30.166  -1.211  27.812  1.00 40.53  ? 309 LEU B C   1 
ATOM   5602 O O   . LEU B 1 280 ? 30.654  -1.697  28.835  1.00 35.33  ? 309 LEU B O   1 
ATOM   5603 C CB  . LEU B 1 280 ? 27.749  -1.759  27.459  1.00 35.19  ? 309 LEU B CB  1 
ATOM   5604 C CG  . LEU B 1 280 ? 27.757  -2.995  28.362  1.00 35.06  ? 309 LEU B CG  1 
ATOM   5605 C CD1 . LEU B 1 280 ? 27.555  -2.628  29.835  1.00 36.60  ? 309 LEU B CD1 1 
ATOM   5606 C CD2 . LEU B 1 280 ? 26.679  -3.996  27.936  1.00 37.26  ? 309 LEU B CD2 1 
ATOM   5607 N N   . VAL B 1 281 ? 30.779  -1.239  26.624  1.00 40.65  ? 310 VAL B N   1 
ATOM   5608 C CA  . VAL B 1 281 ? 32.148  -1.705  26.491  1.00 43.48  ? 310 VAL B CA  1 
ATOM   5609 C C   . VAL B 1 281 ? 33.043  -0.896  27.422  1.00 43.93  ? 310 VAL B C   1 
ATOM   5610 O O   . VAL B 1 281 ? 33.897  -1.448  28.113  1.00 40.43  ? 310 VAL B O   1 
ATOM   5611 C CB  . VAL B 1 281 ? 32.627  -1.578  25.034  1.00 49.01  ? 310 VAL B CB  1 
ATOM   5612 C CG1 . VAL B 1 281 ? 34.128  -1.819  24.915  1.00 51.13  ? 310 VAL B CG1 1 
ATOM   5613 C CG2 . VAL B 1 281 ? 31.853  -2.505  24.095  1.00 49.39  ? 310 VAL B CG2 1 
ATOM   5614 N N   . TRP B 1 282 ? 32.821  0.425   27.425  1.00 46.70  ? 311 TRP B N   1 
ATOM   5615 C CA  . TRP B 1 282 ? 33.656  1.343   28.171  1.00 43.43  ? 311 TRP B CA  1 
ATOM   5616 C C   . TRP B 1 282 ? 33.455  1.141   29.665  1.00 46.19  ? 311 TRP B C   1 
ATOM   5617 O O   . TRP B 1 282 ? 34.433  1.142   30.424  1.00 42.08  ? 311 TRP B O   1 
ATOM   5618 C CB  . TRP B 1 282 ? 33.351  2.784   27.765  1.00 44.64  ? 311 TRP B CB  1 
ATOM   5619 C CG  . TRP B 1 282 ? 34.302  3.772   28.371  1.00 45.60  ? 311 TRP B CG  1 
ATOM   5620 C CD1 . TRP B 1 282 ? 35.579  4.064   27.979  1.00 51.41  ? 311 TRP B CD1 1 
ATOM   5621 C CD2 . TRP B 1 282 ? 34.020  4.632   29.495  1.00 52.42  ? 311 TRP B CD2 1 
ATOM   5622 N NE1 . TRP B 1 282 ? 36.113  5.036   28.791  1.00 52.30  ? 311 TRP B NE1 1 
ATOM   5623 C CE2 . TRP B 1 282 ? 35.179  5.408   29.721  1.00 48.70  ? 311 TRP B CE2 1 
ATOM   5624 C CE3 . TRP B 1 282 ? 32.903  4.825   30.313  1.00 51.19  ? 311 TRP B CE3 1 
ATOM   5625 C CZ2 . TRP B 1 282 ? 35.248  6.346   30.746  1.00 50.26  ? 311 TRP B CZ2 1 
ATOM   5626 C CZ3 . TRP B 1 282 ? 32.966  5.774   31.307  1.00 53.37  ? 311 TRP B CZ3 1 
ATOM   5627 C CH2 . TRP B 1 282 ? 34.128  6.517   31.522  1.00 50.38  ? 311 TRP B CH2 1 
ATOM   5628 N N   . LEU B 1 283 ? 32.181  0.990   30.079  1.00 34.83  ? 312 LEU B N   1 
ATOM   5629 C CA  . LEU B 1 283 ? 31.894  0.681   31.471  1.00 35.28  ? 312 LEU B CA  1 
ATOM   5630 C C   . LEU B 1 283 ? 32.580  -0.616  31.897  1.00 34.28  ? 312 LEU B C   1 
ATOM   5631 O O   . LEU B 1 283 ? 33.185  -0.662  32.971  1.00 37.04  ? 312 LEU B O   1 
ATOM   5632 C CB  . LEU B 1 283 ? 30.395  0.596   31.724  1.00 36.31  ? 312 LEU B CB  1 
ATOM   5633 C CG  . LEU B 1 283 ? 29.591  1.866   31.445  1.00 37.52  ? 312 LEU B CG  1 
ATOM   5634 C CD1 . LEU B 1 283 ? 28.127  1.485   31.350  1.00 39.44  ? 312 LEU B CD1 1 
ATOM   5635 C CD2 . LEU B 1 283 ? 29.841  2.911   32.510  1.00 38.06  ? 312 LEU B CD2 1 
ATOM   5636 N N   . THR B 1 284 ? 32.430  -1.690  31.103  1.00 37.07  ? 313 THR B N   1 
ATOM   5637 C CA  . THR B 1 284 ? 33.027  -2.982  31.443  1.00 41.64  ? 313 THR B CA  1 
ATOM   5638 C C   . THR B 1 284 ? 34.529  -2.786  31.689  1.00 49.64  ? 313 THR B C   1 
ATOM   5639 O O   . THR B 1 284 ? 35.054  -3.095  32.766  1.00 47.53  ? 313 THR B O   1 
ATOM   5640 C CB  . THR B 1 284 ? 32.776  -4.023  30.343  1.00 44.14  ? 313 THR B CB  1 
ATOM   5641 O OG1 . THR B 1 284 ? 31.396  -3.988  29.985  1.00 49.54  ? 313 THR B OG1 1 
ATOM   5642 C CG2 . THR B 1 284 ? 33.108  -5.440  30.783  1.00 39.26  ? 313 THR B CG2 1 
ATOM   5643 N N   . GLN B 1 285 ? 35.207  -2.216  30.689  1.00 47.99  ? 314 GLN B N   1 
ATOM   5644 C CA  . GLN B 1 285 ? 36.647  -2.090  30.746  1.00 50.13  ? 314 GLN B CA  1 
ATOM   5645 C C   . GLN B 1 285 ? 37.022  -1.244  31.966  1.00 46.59  ? 314 GLN B C   1 
ATOM   5646 O O   . GLN B 1 285 ? 37.931  -1.592  32.716  1.00 49.41  ? 314 GLN B O   1 
ATOM   5647 C CB  . GLN B 1 285 ? 37.164  -1.612  29.390  1.00 55.21  ? 314 GLN B CB  1 
ATOM   5648 C CG  . GLN B 1 285 ? 37.148  -0.105  29.201  1.00 66.39  ? 314 GLN B CG  1 
ATOM   5649 C CD  . GLN B 1 285 ? 38.386  0.352   28.476  1.00 76.13  ? 314 GLN B CD  1 
ATOM   5650 O OE1 . GLN B 1 285 ? 38.650  -0.075  27.347  1.00 83.30  ? 314 GLN B OE1 1 
ATOM   5651 N NE2 . GLN B 1 285 ? 39.175  1.186   29.139  1.00 81.42  ? 314 GLN B NE2 1 
ATOM   5652 N N   . LEU B 1 286 ? 36.250  -0.187  32.224  1.00 45.49  ? 315 LEU B N   1 
ATOM   5653 C CA  . LEU B 1 286 ? 36.496  0.675   33.364  1.00 45.09  ? 315 LEU B CA  1 
ATOM   5654 C C   . LEU B 1 286 ? 36.453  -0.155  34.646  1.00 49.15  ? 315 LEU B C   1 
ATOM   5655 O O   . LEU B 1 286 ? 37.454  -0.190  35.362  1.00 50.42  ? 315 LEU B O   1 
ATOM   5656 C CB  . LEU B 1 286 ? 35.481  1.815   33.405  1.00 48.46  ? 315 LEU B CB  1 
ATOM   5657 C CG  . LEU B 1 286 ? 35.885  3.075   34.180  1.00 49.87  ? 315 LEU B CG  1 
ATOM   5658 C CD1 . LEU B 1 286 ? 34.657  3.917   34.537  1.00 48.16  ? 315 LEU B CD1 1 
ATOM   5659 C CD2 . LEU B 1 286 ? 36.700  2.814   35.419  1.00 50.31  ? 315 LEU B CD2 1 
ATOM   5660 N N   . GLN B 1 287 ? 35.300  -0.797  34.926  1.00 43.48  ? 316 GLN B N   1 
ATOM   5661 C CA  . GLN B 1 287 ? 35.037  -1.414  36.221  1.00 50.30  ? 316 GLN B CA  1 
ATOM   5662 C C   . GLN B 1 287 ? 36.052  -2.523  36.522  1.00 60.32  ? 316 GLN B C   1 
ATOM   5663 O O   . GLN B 1 287 ? 36.376  -2.766  37.687  1.00 54.88  ? 316 GLN B O   1 
ATOM   5664 C CB  . GLN B 1 287 ? 33.634  -2.019  36.323  1.00 50.32  ? 316 GLN B CB  1 
ATOM   5665 C CG  . GLN B 1 287 ? 33.341  -2.593  37.702  1.00 53.95  ? 316 GLN B CG  1 
ATOM   5666 C CD  . GLN B 1 287 ? 31.871  -2.812  37.968  1.00 55.92  ? 316 GLN B CD  1 
ATOM   5667 O OE1 . GLN B 1 287 ? 31.321  -3.883  37.687  1.00 55.68  ? 316 GLN B OE1 1 
ATOM   5668 N NE2 . GLN B 1 287 ? 31.238  -1.821  38.581  1.00 62.18  ? 316 GLN B NE2 1 
ATOM   5669 N N   . LYS B 1 288 ? 36.535  -3.203  35.472  1.00 58.44  ? 317 LYS B N   1 
ATOM   5670 C CA  . LYS B 1 288 ? 37.511  -4.272  35.632  1.00 63.73  ? 317 LYS B CA  1 
ATOM   5671 C C   . LYS B 1 288 ? 38.856  -3.675  36.066  1.00 67.34  ? 317 LYS B C   1 
ATOM   5672 O O   . LYS B 1 288 ? 39.634  -4.330  36.762  1.00 60.84  ? 317 LYS B O   1 
ATOM   5673 C CB  . LYS B 1 288 ? 37.634  -5.079  34.332  1.00 64.62  ? 317 LYS B CB  1 
ATOM   5674 C CG  . LYS B 1 288 ? 38.721  -4.576  33.385  1.00 76.57  ? 317 LYS B CG  1 
ATOM   5675 C CD  . LYS B 1 288 ? 38.571  -4.936  31.909  1.00 82.43  ? 317 LYS B CD  1 
ATOM   5676 C CE  . LYS B 1 288 ? 39.645  -4.350  31.010  1.00 77.04  ? 317 LYS B CE  1 
ATOM   5677 N NZ  . LYS B 1 288 ? 40.033  -2.969  31.328  1.00 76.86  ? 317 LYS B NZ  1 
ATOM   5678 N N   . GLU B 1 289 ? 39.117  -2.423  35.656  1.00 60.86  ? 318 GLU B N   1 
ATOM   5679 C CA  . GLU B 1 289 ? 40.423  -1.809  35.834  1.00 64.26  ? 318 GLU B CA  1 
ATOM   5680 C C   . GLU B 1 289 ? 40.529  -1.055  37.161  1.00 60.05  ? 318 GLU B C   1 
ATOM   5681 O O   . GLU B 1 289 ? 41.630  -0.952  37.682  1.00 71.06  ? 318 GLU B O   1 
ATOM   5682 C CB  . GLU B 1 289 ? 40.740  -0.851  34.689  1.00 67.52  ? 318 GLU B CB  1 
ATOM   5683 C CG  . GLU B 1 289 ? 42.228  -0.765  34.377  1.00 69.14  ? 318 GLU B CG  1 
ATOM   5684 C CD  . GLU B 1 289 ? 42.562  0.546   33.703  1.00 77.45  ? 318 GLU B CD  1 
ATOM   5685 O OE1 . GLU B 1 289 ? 42.720  0.579   32.463  1.00 77.85  ? 318 GLU B OE1 1 
ATOM   5686 O OE2 . GLU B 1 289 ? 42.659  1.541   34.454  1.00 73.76  ? 318 GLU B OE2 1 
ATOM   5687 N N   . VAL B 1 290 ? 39.418  -0.526  37.702  1.00 50.17  ? 319 VAL B N   1 
ATOM   5688 C CA  . VAL B 1 290 ? 39.456  0.224   38.952  1.00 53.22  ? 319 VAL B CA  1 
ATOM   5689 C C   . VAL B 1 290 ? 38.750  -0.537  40.078  1.00 47.30  ? 319 VAL B C   1 
ATOM   5690 O O   . VAL B 1 290 ? 38.838  -0.119  41.227  1.00 50.52  ? 319 VAL B O   1 
ATOM   5691 C CB  . VAL B 1 290 ? 38.888  1.655   38.831  1.00 58.44  ? 319 VAL B CB  1 
ATOM   5692 C CG1 . VAL B 1 290 ? 39.657  2.495   37.808  1.00 59.72  ? 319 VAL B CG1 1 
ATOM   5693 C CG2 . VAL B 1 290 ? 37.392  1.661   38.520  1.00 59.88  ? 319 VAL B CG2 1 
ATOM   5694 N N   . GLY B 1 291 ? 38.041  -1.629  39.764  1.00 51.31  ? 320 GLY B N   1 
ATOM   5695 C CA  . GLY B 1 291 ? 37.308  -2.397  40.766  1.00 54.41  ? 320 GLY B CA  1 
ATOM   5696 C C   . GLY B 1 291 ? 35.926  -1.800  41.079  1.00 59.01  ? 320 GLY B C   1 
ATOM   5697 O O   . GLY B 1 291 ? 35.669  -0.609  40.841  1.00 50.56  ? 320 GLY B O   1 
ATOM   5698 N N   . LYS B 1 292 ? 35.068  -2.647  41.673  1.00 59.66  ? 321 LYS B N   1 
ATOM   5699 C CA  . LYS B 1 292 ? 33.688  -2.315  42.015  1.00 64.15  ? 321 LYS B CA  1 
ATOM   5700 C C   . LYS B 1 292 ? 33.628  -1.260  43.114  1.00 67.44  ? 321 LYS B C   1 
ATOM   5701 O O   . LYS B 1 292 ? 32.810  -0.346  43.042  1.00 70.73  ? 321 LYS B O   1 
ATOM   5702 C CB  . LYS B 1 292 ? 32.915  -3.556  42.482  1.00 61.01  ? 321 LYS B CB  1 
ATOM   5703 C CG  . LYS B 1 292 ? 32.749  -4.594  41.393  1.00 60.45  ? 321 LYS B CG  1 
ATOM   5704 C CD  . LYS B 1 292 ? 32.223  -5.961  41.822  1.00 62.28  ? 321 LYS B CD  1 
ATOM   5705 C CE  . LYS B 1 292 ? 32.518  -6.980  40.755  1.00 59.52  ? 321 LYS B CE  1 
ATOM   5706 N NZ  . LYS B 1 292 ? 31.994  -6.577  39.445  1.00 62.65  ? 321 LYS B NZ  1 
ATOM   5707 N N   . ASP B 1 293 ? 34.514  -1.388  44.111  1.00 69.18  ? 322 ASP B N   1 
ATOM   5708 C CA  . ASP B 1 293 ? 34.515  -0.527  45.286  1.00 71.80  ? 322 ASP B CA  1 
ATOM   5709 C C   . ASP B 1 293 ? 35.322  0.753   45.046  1.00 67.76  ? 322 ASP B C   1 
ATOM   5710 O O   . ASP B 1 293 ? 35.924  1.280   45.980  1.00 73.70  ? 322 ASP B O   1 
ATOM   5711 C CB  . ASP B 1 293 ? 35.056  -1.269  46.504  1.00 76.28  ? 322 ASP B CB  1 
ATOM   5712 C CG  . ASP B 1 293 ? 34.192  -2.392  47.064  1.00 80.49  ? 322 ASP B CG  1 
ATOM   5713 O OD1 . ASP B 1 293 ? 33.128  -2.674  46.472  1.00 71.20  ? 322 ASP B OD1 1 
ATOM   5714 O OD2 . ASP B 1 293 ? 34.585  -2.966  48.107  1.00 90.18  ? 322 ASP B OD2 1 
ATOM   5715 N N   . VAL B 1 294 ? 35.283  1.294   43.822  1.00 63.45  ? 323 VAL B N   1 
ATOM   5716 C CA  . VAL B 1 294 ? 36.089  2.454   43.465  1.00 54.63  ? 323 VAL B CA  1 
ATOM   5717 C C   . VAL B 1 294 ? 35.526  3.696   44.161  1.00 55.47  ? 323 VAL B C   1 
ATOM   5718 O O   . VAL B 1 294 ? 34.314  3.871   44.253  1.00 53.12  ? 323 VAL B O   1 
ATOM   5719 C CB  . VAL B 1 294 ? 36.152  2.638   41.935  1.00 56.37  ? 323 VAL B CB  1 
ATOM   5720 C CG1 . VAL B 1 294 ? 34.766  2.828   41.314  1.00 49.40  ? 323 VAL B CG1 1 
ATOM   5721 C CG2 . VAL B 1 294 ? 37.070  3.789   41.528  1.00 57.41  ? 323 VAL B CG2 1 
ATOM   5722 N N   . SER B 1 295 ? 36.424  4.556   44.658  1.00 54.12  ? 324 SER B N   1 
ATOM   5723 C CA  . SER B 1 295 ? 36.018  5.778   45.332  1.00 64.48  ? 324 SER B CA  1 
ATOM   5724 C C   . SER B 1 295 ? 35.817  6.881   44.291  1.00 60.77  ? 324 SER B C   1 
ATOM   5725 O O   . SER B 1 295 ? 36.315  6.781   43.165  1.00 60.62  ? 324 SER B O   1 
ATOM   5726 C CB  . SER B 1 295 ? 37.000  6.187   46.445  1.00 64.69  ? 324 SER B CB  1 
ATOM   5727 O OG  . SER B 1 295 ? 38.270  6.580   45.948  1.00 70.14  ? 324 SER B OG  1 
ATOM   5728 N N   . ASP B 1 296 ? 35.074  7.926   44.685  1.00 61.83  ? 325 ASP B N   1 
ATOM   5729 C CA  . ASP B 1 296 ? 34.767  9.043   43.802  1.00 65.87  ? 325 ASP B CA  1 
ATOM   5730 C C   . ASP B 1 296 ? 36.057  9.659   43.270  1.00 61.14  ? 325 ASP B C   1 
ATOM   5731 O O   . ASP B 1 296 ? 36.175  9.935   42.072  1.00 51.50  ? 325 ASP B O   1 
ATOM   5732 C CB  . ASP B 1 296 ? 33.911  10.094  44.491  1.00 65.85  ? 325 ASP B CB  1 
ATOM   5733 C CG  . ASP B 1 296 ? 32.493  9.663   44.847  1.00 73.59  ? 325 ASP B CG  1 
ATOM   5734 O OD1 . ASP B 1 296 ? 32.162  8.470   44.648  1.00 72.67  ? 325 ASP B OD1 1 
ATOM   5735 O OD2 . ASP B 1 296 ? 31.723  10.532  45.307  1.00 71.12  ? 325 ASP B OD2 1 
ATOM   5736 N N   . GLU B 1 297 ? 37.019  9.839   44.180  1.00 60.50  ? 326 GLU B N   1 
ATOM   5737 C CA  . GLU B 1 297 ? 38.258  10.546  43.895  1.00 67.89  ? 326 GLU B CA  1 
ATOM   5738 C C   . GLU B 1 297 ? 39.055  9.853   42.795  1.00 61.37  ? 326 GLU B C   1 
ATOM   5739 O O   . GLU B 1 297 ? 39.598  10.510  41.903  1.00 61.90  ? 326 GLU B O   1 
ATOM   5740 C CB  . GLU B 1 297 ? 39.145  10.577  45.142  1.00 70.00  ? 326 GLU B CB  1 
ATOM   5741 C CG  . GLU B 1 297 ? 38.549  11.390  46.285  1.00 70.57  ? 326 GLU B CG  1 
ATOM   5742 C CD  . GLU B 1 297 ? 39.449  11.397  47.501  1.00 75.93  ? 326 GLU B CD  1 
ATOM   5743 O OE1 . GLU B 1 297 ? 38.932  11.046  48.582  1.00 77.18  ? 326 GLU B OE1 1 
ATOM   5744 O OE2 . GLU B 1 297 ? 40.656  11.729  47.364  1.00 76.85  ? 326 GLU B OE2 1 
ATOM   5745 N N   . LYS B 1 298 ? 39.177  8.528   42.919  1.00 57.68  ? 327 LYS B N   1 
ATOM   5746 C CA  . LYS B 1 298 ? 39.975  7.753   41.986  1.00 59.30  ? 327 LYS B CA  1 
ATOM   5747 C C   . LYS B 1 298 ? 39.225  7.660   40.654  1.00 61.38  ? 327 LYS B C   1 
ATOM   5748 O O   . LYS B 1 298 ? 39.854  7.672   39.594  1.00 59.76  ? 327 LYS B O   1 
ATOM   5749 C CB  . LYS B 1 298 ? 40.310  6.393   42.607  1.00 63.79  ? 327 LYS B CB  1 
ATOM   5750 C CG  . LYS B 1 298 ? 41.553  5.726   42.031  1.00 73.45  ? 327 LYS B CG  1 
ATOM   5751 C CD  . LYS B 1 298 ? 41.309  4.940   40.750  1.00 80.06  ? 327 LYS B CD  1 
ATOM   5752 C CE  . LYS B 1 298 ? 42.551  4.698   39.957  1.00 85.01  ? 327 LYS B CE  1 
ATOM   5753 N NZ  . LYS B 1 298 ? 43.645  4.216   40.802  1.00 91.89  ? 327 LYS B NZ  1 
ATOM   5754 N N   . LEU B 1 299 ? 37.886  7.571   40.722  1.00 55.11  ? 328 LEU B N   1 
ATOM   5755 C CA  . LEU B 1 299 ? 37.061  7.517   39.521  1.00 56.68  ? 328 LEU B CA  1 
ATOM   5756 C C   . LEU B 1 299 ? 37.182  8.853   38.791  1.00 54.40  ? 328 LEU B C   1 
ATOM   5757 O O   . LEU B 1 299 ? 37.434  8.863   37.588  1.00 52.52  ? 328 LEU B O   1 
ATOM   5758 C CB  . LEU B 1 299 ? 35.604  7.157   39.827  1.00 54.47  ? 328 LEU B CB  1 
ATOM   5759 C CG  . LEU B 1 299 ? 34.647  7.098   38.626  1.00 55.29  ? 328 LEU B CG  1 
ATOM   5760 C CD1 . LEU B 1 299 ? 35.103  6.129   37.536  1.00 53.63  ? 328 LEU B CD1 1 
ATOM   5761 C CD2 . LEU B 1 299 ? 33.255  6.737   39.108  1.00 50.37  ? 328 LEU B CD2 1 
ATOM   5762 N N   . ARG B 1 300 ? 37.074  9.959   39.546  1.00 54.51  ? 329 ARG B N   1 
ATOM   5763 C CA  . ARG B 1 300 ? 37.315  11.303  39.034  1.00 57.60  ? 329 ARG B CA  1 
ATOM   5764 C C   . ARG B 1 300 ? 38.674  11.365  38.332  1.00 64.25  ? 329 ARG B C   1 
ATOM   5765 O O   . ARG B 1 300 ? 38.781  11.871  37.211  1.00 56.93  ? 329 ARG B O   1 
ATOM   5766 C CB  . ARG B 1 300 ? 37.227  12.333  40.170  1.00 63.94  ? 329 ARG B CB  1 
ATOM   5767 C CG  . ARG B 1 300 ? 36.830  13.739  39.739  1.00 68.21  ? 329 ARG B CG  1 
ATOM   5768 C CD  . ARG B 1 300 ? 36.492  14.694  40.903  1.00 78.67  ? 329 ARG B CD  1 
ATOM   5769 N NE  . ARG B 1 300 ? 35.341  14.350  41.756  1.00 87.87  ? 329 ARG B NE  1 
ATOM   5770 C CZ  . ARG B 1 300 ? 35.297  14.372  43.101  1.00 87.96  ? 329 ARG B CZ  1 
ATOM   5771 N NH1 . ARG B 1 300 ? 36.399  14.501  43.829  1.00 88.60  ? 329 ARG B NH1 1 
ATOM   5772 N NH2 . ARG B 1 300 ? 34.137  14.236  43.721  1.00 79.44  ? 329 ARG B NH2 1 
ATOM   5773 N N   . ASP B 1 301 ? 39.703  10.809  38.992  1.00 61.61  ? 330 ASP B N   1 
ATOM   5774 C CA  . ASP B 1 301 ? 41.047  10.771  38.444  1.00 63.14  ? 330 ASP B CA  1 
ATOM   5775 C C   . ASP B 1 301 ? 41.033  10.093  37.070  1.00 64.09  ? 330 ASP B C   1 
ATOM   5776 O O   . ASP B 1 301 ? 41.611  10.622  36.119  1.00 72.59  ? 330 ASP B O   1 
ATOM   5777 C CB  . ASP B 1 301 ? 42.001  10.156  39.460  1.00 75.32  ? 330 ASP B CB  1 
ATOM   5778 C CG  . ASP B 1 301 ? 43.419  9.910   38.968  1.00 85.74  ? 330 ASP B CG  1 
ATOM   5779 O OD1 . ASP B 1 301 ? 44.129  10.910  38.713  1.00 96.17  ? 330 ASP B OD1 1 
ATOM   5780 O OD2 . ASP B 1 301 ? 43.791  8.721   38.828  1.00 91.31  ? 330 ASP B OD2 1 
ATOM   5781 N N   . TYR B 1 302 ? 40.356  8.938   36.967  1.00 56.58  ? 331 TYR B N   1 
ATOM   5782 C CA  . TYR B 1 302 ? 40.287  8.163   35.735  1.00 57.09  ? 331 TYR B CA  1 
ATOM   5783 C C   . TYR B 1 302 ? 39.669  8.982   34.601  1.00 63.01  ? 331 TYR B C   1 
ATOM   5784 O O   . TYR B 1 302 ? 40.119  8.881   33.458  1.00 53.86  ? 331 TYR B O   1 
ATOM   5785 C CB  . TYR B 1 302 ? 39.454  6.885   35.894  1.00 61.65  ? 331 TYR B CB  1 
ATOM   5786 C CG  . TYR B 1 302 ? 39.385  5.974   34.667  1.00 66.32  ? 331 TYR B CG  1 
ATOM   5787 C CD1 . TYR B 1 302 ? 38.371  6.102   33.716  1.00 65.34  ? 331 TYR B CD1 1 
ATOM   5788 C CD2 . TYR B 1 302 ? 40.317  4.955   34.475  1.00 65.88  ? 331 TYR B CD2 1 
ATOM   5789 C CE1 . TYR B 1 302 ? 38.307  5.272   32.605  1.00 68.51  ? 331 TYR B CE1 1 
ATOM   5790 C CE2 . TYR B 1 302 ? 40.256  4.111   33.376  1.00 68.88  ? 331 TYR B CE2 1 
ATOM   5791 C CZ  . TYR B 1 302 ? 39.255  4.274   32.435  1.00 67.49  ? 331 TYR B CZ  1 
ATOM   5792 O OH  . TYR B 1 302 ? 39.210  3.447   31.355  1.00 58.83  ? 331 TYR B OH  1 
ATOM   5793 N N   . ILE B 1 303 ? 38.614  9.754   34.911  1.00 59.78  ? 332 ILE B N   1 
ATOM   5794 C CA  . ILE B 1 303 ? 37.879  10.473  33.881  1.00 54.79  ? 332 ILE B CA  1 
ATOM   5795 C C   . ILE B 1 303 ? 38.789  11.547  33.273  1.00 60.01  ? 332 ILE B C   1 
ATOM   5796 O O   . ILE B 1 303 ? 38.841  11.689  32.041  1.00 54.82  ? 332 ILE B O   1 
ATOM   5797 C CB  . ILE B 1 303 ? 36.550  11.036  34.432  1.00 51.79  ? 332 ILE B CB  1 
ATOM   5798 C CG1 . ILE B 1 303 ? 35.696  9.964   35.119  1.00 53.23  ? 332 ILE B CG1 1 
ATOM   5799 C CG2 . ILE B 1 303 ? 35.751  11.735  33.337  1.00 56.06  ? 332 ILE B CG2 1 
ATOM   5800 C CD1 . ILE B 1 303 ? 35.283  8.821   34.206  1.00 55.83  ? 332 ILE B CD1 1 
ATOM   5801 N N   . TRP B 1 304 ? 39.500  12.283  34.151  1.00 57.90  ? 333 TRP B N   1 
ATOM   5802 C CA  . TRP B 1 304 ? 40.456  13.308  33.746  1.00 63.84  ? 333 TRP B CA  1 
ATOM   5803 C C   . TRP B 1 304 ? 41.520  12.715  32.824  1.00 63.77  ? 333 TRP B C   1 
ATOM   5804 O O   . TRP B 1 304 ? 41.837  13.300  31.795  1.00 58.69  ? 333 TRP B O   1 
ATOM   5805 C CB  . TRP B 1 304 ? 41.101  14.002  34.964  1.00 61.17  ? 333 TRP B CB  1 
ATOM   5806 C CG  . TRP B 1 304 ? 40.454  15.313  35.336  1.00 69.29  ? 333 TRP B CG  1 
ATOM   5807 C CD1 . TRP B 1 304 ? 39.961  15.680  36.557  1.00 74.13  ? 333 TRP B CD1 1 
ATOM   5808 C CD2 . TRP B 1 304 ? 40.240  16.445  34.461  1.00 77.99  ? 333 TRP B CD2 1 
ATOM   5809 N NE1 . TRP B 1 304 ? 39.446  16.948  36.505  1.00 77.30  ? 333 TRP B NE1 1 
ATOM   5810 C CE2 . TRP B 1 304 ? 39.602  17.444  35.234  1.00 81.38  ? 333 TRP B CE2 1 
ATOM   5811 C CE3 . TRP B 1 304 ? 40.513  16.706  33.111  1.00 75.66  ? 333 TRP B CE3 1 
ATOM   5812 C CZ2 . TRP B 1 304 ? 39.245  18.679  34.694  1.00 81.99  ? 333 TRP B CZ2 1 
ATOM   5813 C CZ3 . TRP B 1 304 ? 40.152  17.924  32.580  1.00 79.73  ? 333 TRP B CZ3 1 
ATOM   5814 C CH2 . TRP B 1 304 ? 39.527  18.895  33.363  1.00 83.00  ? 333 TRP B CH2 1 
ATOM   5815 N N   . ASN B 1 305 ? 42.048  11.542  33.186  1.00 69.94  ? 334 ASN B N   1 
ATOM   5816 C CA  . ASN B 1 305 ? 43.057  10.885  32.373  1.00 76.63  ? 334 ASN B CA  1 
ATOM   5817 C C   . ASN B 1 305 ? 42.472  10.555  30.999  1.00 74.24  ? 334 ASN B C   1 
ATOM   5818 O O   . ASN B 1 305 ? 43.138  10.730  29.975  1.00 86.63  ? 334 ASN B O   1 
ATOM   5819 C CB  . ASN B 1 305 ? 43.623  9.651   33.069  1.00 77.93  ? 334 ASN B CB  1 
ATOM   5820 C CG  . ASN B 1 305 ? 44.434  9.968   34.308  1.00 81.24  ? 334 ASN B CG  1 
ATOM   5821 O OD1 . ASN B 1 305 ? 45.005  9.049   34.909  1.00 75.52  ? 334 ASN B OD1 1 
ATOM   5822 N ND2 . ASN B 1 305 ? 44.507  11.230  34.720  1.00 78.25  ? 334 ASN B ND2 1 
ATOM   5823 N N   . THR B 1 306 ? 41.220  10.085  30.987  1.00 63.76  ? 335 THR B N   1 
ATOM   5824 C CA  . THR B 1 306 ? 40.539  9.728   29.753  1.00 62.75  ? 335 THR B CA  1 
ATOM   5825 C C   . THR B 1 306 ? 40.514  10.950  28.839  1.00 59.69  ? 335 THR B C   1 
ATOM   5826 O O   . THR B 1 306 ? 40.913  10.882  27.679  1.00 57.54  ? 335 THR B O   1 
ATOM   5827 C CB  . THR B 1 306 ? 39.127  9.220   30.063  1.00 62.87  ? 335 THR B CB  1 
ATOM   5828 O OG1 . THR B 1 306 ? 39.268  7.962   30.721  1.00 66.49  ? 335 THR B OG1 1 
ATOM   5829 C CG2 . THR B 1 306 ? 38.276  9.039   28.819  1.00 64.39  ? 335 THR B CG2 1 
ATOM   5830 N N   . LEU B 1 307 ? 40.050  12.072  29.391  1.00 61.31  ? 336 LEU B N   1 
ATOM   5831 C CA  . LEU B 1 307 ? 39.878  13.289  28.613  1.00 73.98  ? 336 LEU B CA  1 
ATOM   5832 C C   . LEU B 1 307 ? 41.210  14.005  28.346  1.00 70.31  ? 336 LEU B C   1 
ATOM   5833 O O   . LEU B 1 307 ? 41.317  14.738  27.368  1.00 68.24  ? 336 LEU B O   1 
ATOM   5834 C CB  . LEU B 1 307 ? 38.864  14.157  29.356  1.00 70.31  ? 336 LEU B CB  1 
ATOM   5835 C CG  . LEU B 1 307 ? 37.446  13.576  29.402  1.00 65.77  ? 336 LEU B CG  1 
ATOM   5836 C CD1 . LEU B 1 307 ? 36.704  14.008  30.655  1.00 69.11  ? 336 LEU B CD1 1 
ATOM   5837 C CD2 . LEU B 1 307 ? 36.666  13.969  28.156  1.00 62.52  ? 336 LEU B CD2 1 
ATOM   5838 N N   . ASN B 1 308 ? 42.244  13.758  29.163  1.00 67.14  ? 337 ASN B N   1 
ATOM   5839 C CA  . ASN B 1 308 ? 43.566  14.312  28.888  1.00 76.95  ? 337 ASN B CA  1 
ATOM   5840 C C   . ASN B 1 308 ? 44.252  13.599  27.721  1.00 76.62  ? 337 ASN B C   1 
ATOM   5841 O O   . ASN B 1 308 ? 45.355  13.986  27.349  1.00 72.49  ? 337 ASN B O   1 
ATOM   5842 C CB  . ASN B 1 308 ? 44.490  14.279  30.104  1.00 75.46  ? 337 ASN B CB  1 
ATOM   5843 C CG  . ASN B 1 308 ? 44.331  15.498  30.983  1.00 72.55  ? 337 ASN B CG  1 
ATOM   5844 O OD1 . ASN B 1 308 ? 44.140  16.609  30.479  1.00 73.60  ? 337 ASN B OD1 1 
ATOM   5845 N ND2 . ASN B 1 308 ? 44.402  15.318  32.293  1.00 71.48  ? 337 ASN B ND2 1 
ATOM   5846 N N   . SER B 1 309 ? 43.627  12.545  27.178  1.00 81.19  ? 338 SER B N   1 
ATOM   5847 C CA  . SER B 1 309 ? 44.151  11.843  26.014  1.00 79.29  ? 338 SER B CA  1 
ATOM   5848 C C   . SER B 1 309 ? 43.243  12.052  24.797  1.00 73.12  ? 338 SER B C   1 
ATOM   5849 O O   . SER B 1 309 ? 43.353  11.324  23.814  1.00 74.81  ? 338 SER B O   1 
ATOM   5850 C CB  . SER B 1 309 ? 44.368  10.383  26.344  1.00 81.06  ? 338 SER B CB  1 
ATOM   5851 O OG  . SER B 1 309 ? 43.497  9.959   27.387  1.00 83.26  ? 338 SER B OG  1 
ATOM   5852 N N   . GLY B 1 310 ? 42.399  13.097  24.853  1.00 72.21  ? 339 GLY B N   1 
ATOM   5853 C CA  . GLY B 1 310 ? 41.395  13.385  23.837  1.00 69.04  ? 339 GLY B CA  1 
ATOM   5854 C C   . GLY B 1 310 ? 40.530  12.164  23.512  1.00 71.70  ? 339 GLY B C   1 
ATOM   5855 O O   . GLY B 1 310 ? 40.194  11.925  22.354  1.00 68.10  ? 339 GLY B O   1 
ATOM   5856 N N   . ARG B 1 311 ? 40.185  11.387  24.546  1.00 76.64  ? 340 ARG B N   1 
ATOM   5857 C CA  . ARG B 1 311 ? 39.239  10.290  24.424  1.00 75.57  ? 340 ARG B CA  1 
ATOM   5858 C C   . ARG B 1 311 ? 37.909  10.769  24.998  1.00 67.32  ? 340 ARG B C   1 
ATOM   5859 O O   . ARG B 1 311 ? 37.892  11.517  25.973  1.00 68.87  ? 340 ARG B O   1 
ATOM   5860 C CB  . ARG B 1 311 ? 39.708  9.045   25.186  1.00 87.46  ? 340 ARG B CB  1 
ATOM   5861 C CG  . ARG B 1 311 ? 41.176  8.668   25.025  1.00 95.59  ? 340 ARG B CG  1 
ATOM   5862 C CD  . ARG B 1 311 ? 41.588  7.398   25.777  1.00 103.78 ? 340 ARG B CD  1 
ATOM   5863 N NE  . ARG B 1 311 ? 40.730  7.046   26.920  1.00 112.78 ? 340 ARG B NE  1 
ATOM   5864 C CZ  . ARG B 1 311 ? 41.070  6.413   28.047  1.00 105.00 ? 340 ARG B CZ  1 
ATOM   5865 N NH1 . ARG B 1 311 ? 40.128  6.094   28.925  1.00 101.14 ? 340 ARG B NH1 1 
ATOM   5866 N NH2 . ARG B 1 311 ? 42.328  6.088   28.297  1.00 103.19 ? 340 ARG B NH2 1 
ATOM   5867 N N   . VAL B 1 312 ? 36.803  10.340  24.384  1.00 62.33  ? 341 VAL B N   1 
ATOM   5868 C CA  . VAL B 1 312 ? 35.477  10.793  24.780  1.00 61.75  ? 341 VAL B CA  1 
ATOM   5869 C C   . VAL B 1 312 ? 35.043  10.001  26.006  1.00 59.02  ? 341 VAL B C   1 
ATOM   5870 O O   . VAL B 1 312 ? 35.494  8.876   26.198  1.00 52.06  ? 341 VAL B O   1 
ATOM   5871 C CB  . VAL B 1 312 ? 34.444  10.643  23.646  1.00 62.51  ? 341 VAL B CB  1 
ATOM   5872 C CG1 . VAL B 1 312 ? 34.857  11.454  22.421  1.00 61.35  ? 341 VAL B CG1 1 
ATOM   5873 C CG2 . VAL B 1 312 ? 34.190  9.179   23.279  1.00 57.48  ? 341 VAL B CG2 1 
ATOM   5874 N N   . VAL B 1 313 ? 34.193  10.615  26.833  1.00 55.01  ? 342 VAL B N   1 
ATOM   5875 C CA  . VAL B 1 313 ? 33.476  9.892   27.866  1.00 57.34  ? 342 VAL B CA  1 
ATOM   5876 C C   . VAL B 1 313 ? 32.162  9.421   27.246  1.00 54.95  ? 342 VAL B C   1 
ATOM   5877 O O   . VAL B 1 313 ? 31.220  10.201  27.195  1.00 58.22  ? 342 VAL B O   1 
ATOM   5878 C CB  . VAL B 1 313 ? 33.221  10.733  29.135  1.00 61.59  ? 342 VAL B CB  1 
ATOM   5879 C CG1 . VAL B 1 313 ? 32.290  10.016  30.108  1.00 61.60  ? 342 VAL B CG1 1 
ATOM   5880 C CG2 . VAL B 1 313 ? 34.523  11.123  29.839  1.00 65.26  ? 342 VAL B CG2 1 
ATOM   5881 N N   . PRO B 1 314 ? 32.042  8.163   26.750  1.00 49.40  ? 343 PRO B N   1 
ATOM   5882 C CA  . PRO B 1 314 ? 30.836  7.755   26.024  1.00 51.45  ? 343 PRO B CA  1 
ATOM   5883 C C   . PRO B 1 314 ? 29.522  8.001   26.772  1.00 48.33  ? 343 PRO B C   1 
ATOM   5884 O O   . PRO B 1 314 ? 29.386  7.753   27.986  1.00 42.06  ? 343 PRO B O   1 
ATOM   5885 C CB  . PRO B 1 314 ? 31.060  6.272   25.665  1.00 49.66  ? 343 PRO B CB  1 
ATOM   5886 C CG  . PRO B 1 314 ? 32.287  5.844   26.456  1.00 53.08  ? 343 PRO B CG  1 
ATOM   5887 C CD  . PRO B 1 314 ? 33.068  7.104   26.767  1.00 49.24  ? 343 PRO B CD  1 
ATOM   5888 N N   . GLY B 1 315 ? 28.569  8.556   26.015  1.00 42.35  ? 344 GLY B N   1 
ATOM   5889 C CA  . GLY B 1 315 ? 27.209  8.721   26.483  1.00 41.19  ? 344 GLY B CA  1 
ATOM   5890 C C   . GLY B 1 315 ? 26.998  10.015  27.259  1.00 43.81  ? 344 GLY B C   1 
ATOM   5891 O O   . GLY B 1 315 ? 25.926  10.165  27.849  1.00 49.99  ? 344 GLY B O   1 
ATOM   5892 N N   . TYR B 1 316 ? 28.025  10.896  27.285  1.00 50.23  ? 345 TYR B N   1 
ATOM   5893 C CA  . TYR B 1 316 ? 27.944  12.251  27.832  1.00 49.04  ? 345 TYR B CA  1 
ATOM   5894 C C   . TYR B 1 316 ? 28.276  13.248  26.716  1.00 57.97  ? 345 TYR B C   1 
ATOM   5895 O O   . TYR B 1 316 ? 29.353  13.176  26.116  1.00 51.75  ? 345 TYR B O   1 
ATOM   5896 C CB  . TYR B 1 316 ? 28.884  12.411  29.034  1.00 45.39  ? 345 TYR B CB  1 
ATOM   5897 C CG  . TYR B 1 316 ? 28.371  11.762  30.318  1.00 49.25  ? 345 TYR B CG  1 
ATOM   5898 C CD1 . TYR B 1 316 ? 28.451  10.381  30.518  1.00 45.89  ? 345 TYR B CD1 1 
ATOM   5899 C CD2 . TYR B 1 316 ? 27.805  12.525  31.330  1.00 46.82  ? 345 TYR B CD2 1 
ATOM   5900 C CE1 . TYR B 1 316 ? 27.968  9.783   31.674  1.00 44.77  ? 345 TYR B CE1 1 
ATOM   5901 C CE2 . TYR B 1 316 ? 27.324  11.937  32.492  1.00 50.94  ? 345 TYR B CE2 1 
ATOM   5902 C CZ  . TYR B 1 316 ? 27.413  10.566  32.669  1.00 42.53  ? 345 TYR B CZ  1 
ATOM   5903 O OH  . TYR B 1 316 ? 26.922  10.023  33.813  1.00 49.96  ? 345 TYR B OH  1 
ATOM   5904 N N   . GLY B 1 317 ? 27.348  14.182  26.455  1.00 77.44  ? 346 GLY B N   1 
ATOM   5905 C CA  . GLY B 1 317 ? 27.338  14.971  25.226  1.00 91.70  ? 346 GLY B CA  1 
ATOM   5906 C C   . GLY B 1 317 ? 26.307  14.429  24.234  1.00 101.81 ? 346 GLY B C   1 
ATOM   5907 O O   . GLY B 1 317 ? 25.863  13.292  24.368  1.00 110.62 ? 346 GLY B O   1 
ATOM   5908 N N   . HIS B 1 318 ? 25.921  15.249  23.246  1.00 120.79 ? 347 HIS B N   1 
ATOM   5909 C CA  . HIS B 1 318 ? 24.868  14.889  22.303  1.00 139.88 ? 347 HIS B CA  1 
ATOM   5910 C C   . HIS B 1 318 ? 24.939  15.811  21.084  1.00 145.72 ? 347 HIS B C   1 
ATOM   5911 O O   . HIS B 1 318 ? 25.831  16.652  21.003  1.00 157.07 ? 347 HIS B O   1 
ATOM   5912 C CB  . HIS B 1 318 ? 23.496  14.957  22.991  1.00 156.38 ? 347 HIS B CB  1 
ATOM   5913 C CG  . HIS B 1 318 ? 22.411  14.133  22.362  1.00 174.86 ? 347 HIS B CG  1 
ATOM   5914 N ND1 . HIS B 1 318 ? 22.562  12.810  21.999  1.00 181.01 ? 347 HIS B ND1 1 
ATOM   5915 C CD2 . HIS B 1 318 ? 21.138  14.447  22.068  1.00 179.30 ? 347 HIS B CD2 1 
ATOM   5916 C CE1 . HIS B 1 318 ? 21.423  12.360  21.490  1.00 176.52 ? 347 HIS B CE1 1 
ATOM   5917 N NE2 . HIS B 1 318 ? 20.544  13.338  21.520  1.00 174.58 ? 347 HIS B NE2 1 
ATOM   5918 N N   . ALA B 1 319 ? 24.003  15.635  20.136  1.00 148.19 ? 348 ALA B N   1 
ATOM   5919 C CA  . ALA B 1 319 ? 23.857  16.524  18.991  1.00 144.90 ? 348 ALA B CA  1 
ATOM   5920 C C   . ALA B 1 319 ? 23.008  17.741  19.368  1.00 160.08 ? 348 ALA B C   1 
ATOM   5921 O O   . ALA B 1 319 ? 23.508  18.864  19.346  1.00 168.16 ? 348 ALA B O   1 
ATOM   5922 C CB  . ALA B 1 319 ? 23.265  15.775  17.817  1.00 132.53 ? 348 ALA B CB  1 
ATOM   5923 N N   . VAL B 1 320 ? 21.728  17.512  19.711  1.00 160.98 ? 349 VAL B N   1 
ATOM   5924 C CA  . VAL B 1 320 ? 20.809  18.580  20.088  1.00 144.03 ? 349 VAL B CA  1 
ATOM   5925 C C   . VAL B 1 320 ? 20.173  18.231  21.439  1.00 139.21 ? 349 VAL B C   1 
ATOM   5926 O O   . VAL B 1 320 ? 19.391  17.287  21.530  1.00 130.74 ? 349 VAL B O   1 
ATOM   5927 C CB  . VAL B 1 320 ? 19.765  18.850  18.978  1.00 127.69 ? 349 VAL B CB  1 
ATOM   5928 C CG1 . VAL B 1 320 ? 19.094  17.580  18.452  1.00 118.18 ? 349 VAL B CG1 1 
ATOM   5929 C CG2 . VAL B 1 320 ? 18.732  19.896  19.392  1.00 118.85 ? 349 VAL B CG2 1 
ATOM   5930 N N   . LEU B 1 321 ? 20.539  18.990  22.487  1.00 130.81 ? 350 LEU B N   1 
ATOM   5931 C CA  . LEU B 1 321 ? 20.091  18.729  23.851  1.00 132.52 ? 350 LEU B CA  1 
ATOM   5932 C C   . LEU B 1 321 ? 20.458  19.939  24.709  1.00 106.52 ? 350 LEU B C   1 
ATOM   5933 O O   . LEU B 1 321 ? 20.984  20.908  24.171  1.00 100.41 ? 350 LEU B O   1 
ATOM   5934 C CB  . LEU B 1 321 ? 20.755  17.452  24.370  1.00 158.59 ? 350 LEU B CB  1 
ATOM   5935 C CG  . LEU B 1 321 ? 19.831  16.351  24.910  1.00 184.02 ? 350 LEU B CG  1 
ATOM   5936 C CD1 . LEU B 1 321 ? 20.686  15.252  25.528  1.00 183.08 ? 350 LEU B CD1 1 
ATOM   5937 C CD2 . LEU B 1 321 ? 18.776  16.816  25.909  1.00 190.40 ? 350 LEU B CD2 1 
ATOM   5938 N N   . ARG B 1 322 ? 20.219  19.880  26.031  1.00 88.62  ? 351 ARG B N   1 
ATOM   5939 C CA  . ARG B 1 322 ? 20.607  21.010  26.925  1.00 87.70  ? 351 ARG B CA  1 
ATOM   5940 C C   . ARG B 1 322 ? 20.524  20.657  28.423  1.00 90.69  ? 351 ARG B C   1 
ATOM   5941 O O   . ARG B 1 322 ? 20.750  21.578  29.239  1.00 89.17  ? 351 ARG B O   1 
ATOM   5942 C CB  . ARG B 1 322 ? 19.697  22.221  26.688  1.00 93.77  ? 351 ARG B CB  1 
ATOM   5943 N N   . LYS B 1 323 ? 20.242  19.402  28.782  1.00 94.42  ? 352 LYS B N   1 
ATOM   5944 C CA  . LYS B 1 323 ? 20.067  19.008  30.179  1.00 78.62  ? 352 LYS B CA  1 
ATOM   5945 C C   . LYS B 1 323 ? 20.055  17.477  30.226  1.00 69.56  ? 352 LYS B C   1 
ATOM   5946 O O   . LYS B 1 323 ? 20.013  16.854  29.166  1.00 71.93  ? 352 LYS B O   1 
ATOM   5947 C CB  . LYS B 1 323 ? 18.732  19.530  30.723  1.00 78.11  ? 352 LYS B CB  1 
ATOM   5948 C CG  . LYS B 1 323 ? 18.611  19.709  32.229  1.00 77.49  ? 352 LYS B CG  1 
ATOM   5949 C CD  . LYS B 1 323 ? 17.522  18.886  32.918  1.00 85.52  ? 352 LYS B CD  1 
ATOM   5950 C CE  . LYS B 1 323 ? 16.241  18.617  32.168  1.00 86.02  ? 352 LYS B CE  1 
ATOM   5951 N NZ  . LYS B 1 323 ? 15.303  19.739  32.208  1.00 86.33  ? 352 LYS B NZ  1 
ATOM   5952 N N   . THR B 1 324 ? 19.944  16.854  31.409  1.00 57.76  ? 353 THR B N   1 
ATOM   5953 C CA  . THR B 1 324 ? 19.910  15.398  31.482  1.00 54.69  ? 353 THR B CA  1 
ATOM   5954 C C   . THR B 1 324 ? 18.688  14.926  30.686  1.00 50.69  ? 353 THR B C   1 
ATOM   5955 O O   . THR B 1 324 ? 17.558  15.329  30.971  1.00 49.28  ? 353 THR B O   1 
ATOM   5956 C CB  . THR B 1 324 ? 19.905  14.877  32.923  1.00 54.85  ? 353 THR B CB  1 
ATOM   5957 O OG1 . THR B 1 324 ? 21.213  14.985  33.488  1.00 46.76  ? 353 THR B OG1 1 
ATOM   5958 C CG2 . THR B 1 324 ? 19.557  13.400  33.014  1.00 60.36  ? 353 THR B CG2 1 
ATOM   5959 N N   . ASP B 1 325 ? 18.943  14.127  29.643  1.00 47.49  ? 354 ASP B N   1 
ATOM   5960 C CA  . ASP B 1 325 ? 17.888  13.559  28.822  1.00 46.27  ? 354 ASP B CA  1 
ATOM   5961 C C   . ASP B 1 325 ? 16.904  12.856  29.748  1.00 44.15  ? 354 ASP B C   1 
ATOM   5962 O O   . ASP B 1 325 ? 17.274  11.968  30.506  1.00 43.19  ? 354 ASP B O   1 
ATOM   5963 C CB  . ASP B 1 325 ? 18.481  12.660  27.751  1.00 51.12  ? 354 ASP B CB  1 
ATOM   5964 C CG  . ASP B 1 325 ? 17.513  11.987  26.785  1.00 55.14  ? 354 ASP B CG  1 
ATOM   5965 O OD1 . ASP B 1 325 ? 16.297  12.010  27.051  1.00 50.80  ? 354 ASP B OD1 1 
ATOM   5966 O OD2 . ASP B 1 325 ? 17.996  11.433  25.766  1.00 63.73  ? 354 ASP B OD2 1 
ATOM   5967 N N   . PRO B 1 326 ? 15.608  13.220  29.741  1.00 42.41  ? 355 PRO B N   1 
ATOM   5968 C CA  . PRO B 1 326 ? 14.647  12.544  30.614  1.00 46.08  ? 355 PRO B CA  1 
ATOM   5969 C C   . PRO B 1 326 ? 14.591  11.043  30.306  1.00 39.94  ? 355 PRO B C   1 
ATOM   5970 O O   . PRO B 1 326 ? 14.097  10.278  31.126  1.00 39.95  ? 355 PRO B O   1 
ATOM   5971 C CB  . PRO B 1 326 ? 13.306  13.285  30.360  1.00 44.37  ? 355 PRO B CB  1 
ATOM   5972 C CG  . PRO B 1 326 ? 13.505  13.894  28.996  1.00 43.53  ? 355 PRO B CG  1 
ATOM   5973 C CD  . PRO B 1 326 ? 14.992  14.234  28.880  1.00 42.20  ? 355 PRO B CD  1 
ATOM   5974 N N   . ARG B 1 327 ? 15.108  10.646  29.138  1.00 34.60  ? 356 ARG B N   1 
ATOM   5975 C CA  . ARG B 1 327 ? 15.188  9.241   28.737  1.00 38.27  ? 356 ARG B CA  1 
ATOM   5976 C C   . ARG B 1 327 ? 16.210  8.504   29.612  1.00 38.31  ? 356 ARG B C   1 
ATOM   5977 O O   . ARG B 1 327 ? 16.042  7.312   29.890  1.00 36.35  ? 356 ARG B O   1 
ATOM   5978 C CB  . ARG B 1 327 ? 15.475  9.099   27.232  1.00 38.48  ? 356 ARG B CB  1 
ATOM   5979 C CG  . ARG B 1 327 ? 14.370  9.597   26.300  1.00 42.97  ? 356 ARG B CG  1 
ATOM   5980 C CD  . ARG B 1 327 ? 14.578  9.332   24.790  1.00 43.43  ? 356 ARG B CD  1 
ATOM   5981 N NE  . ARG B 1 327 ? 15.823  9.880   24.242  1.00 38.36  ? 356 ARG B NE  1 
ATOM   5982 C CZ  . ARG B 1 327 ? 16.379  9.737   23.040  1.00 43.15  ? 356 ARG B CZ  1 
ATOM   5983 N NH1 . ARG B 1 327 ? 15.840  9.001   22.070  1.00 41.22  ? 356 ARG B NH1 1 
ATOM   5984 N NH2 . ARG B 1 327 ? 17.533  10.353  22.805  1.00 46.65  ? 356 ARG B NH2 1 
ATOM   5985 N N   . TYR B 1 328 ? 17.257  9.208   30.075  1.00 39.54  ? 357 TYR B N   1 
ATOM   5986 C CA  . TYR B 1 328 ? 18.213  8.676   31.046  1.00 37.19  ? 357 TYR B CA  1 
ATOM   5987 C C   . TYR B 1 328 ? 17.595  8.610   32.438  1.00 38.33  ? 357 TYR B C   1 
ATOM   5988 O O   . TYR B 1 328 ? 17.640  7.558   33.088  1.00 36.77  ? 357 TYR B O   1 
ATOM   5989 C CB  . TYR B 1 328 ? 19.463  9.552   31.098  1.00 38.72  ? 357 TYR B CB  1 
ATOM   5990 C CG  . TYR B 1 328 ? 20.515  9.173   32.136  1.00 39.10  ? 357 TYR B CG  1 
ATOM   5991 C CD1 . TYR B 1 328 ? 20.381  9.556   33.466  1.00 42.80  ? 357 TYR B CD1 1 
ATOM   5992 C CD2 . TYR B 1 328 ? 21.671  8.482   31.779  1.00 43.43  ? 357 TYR B CD2 1 
ATOM   5993 C CE1 . TYR B 1 328 ? 21.356  9.267   34.413  1.00 43.90  ? 357 TYR B CE1 1 
ATOM   5994 C CE2 . TYR B 1 328 ? 22.651  8.175   32.716  1.00 46.37  ? 357 TYR B CE2 1 
ATOM   5995 C CZ  . TYR B 1 328 ? 22.493  8.573   34.036  1.00 45.18  ? 357 TYR B CZ  1 
ATOM   5996 O OH  . TYR B 1 328 ? 23.429  8.247   34.972  1.00 39.76  ? 357 TYR B OH  1 
ATOM   5997 N N   . THR B 1 329 ? 17.033  9.742   32.887  1.00 34.65  ? 358 THR B N   1 
ATOM   5998 C CA  . THR B 1 329 ? 16.474  9.878   34.219  1.00 38.28  ? 358 THR B CA  1 
ATOM   5999 C C   . THR B 1 329 ? 15.482  8.748   34.456  1.00 38.15  ? 358 THR B C   1 
ATOM   6000 O O   . THR B 1 329 ? 15.443  8.100   35.502  1.00 38.60  ? 358 THR B O   1 
ATOM   6001 C CB  . THR B 1 329 ? 15.796  11.248  34.317  1.00 37.84  ? 358 THR B CB  1 
ATOM   6002 O OG1 . THR B 1 329 ? 16.929  12.093  34.179  1.00 49.57  ? 358 THR B OG1 1 
ATOM   6003 C CG2 . THR B 1 329 ? 15.061  11.471  35.624  1.00 36.81  ? 358 THR B CG2 1 
ATOM   6004 N N   . CYS B 1 330 ? 14.644  8.555   33.450  1.00 37.32  ? 359 CYS B N   1 
ATOM   6005 C CA  . CYS B 1 330 ? 13.655  7.502   33.429  1.00 41.70  ? 359 CYS B CA  1 
ATOM   6006 C C   . CYS B 1 330 ? 14.280  6.128   33.790  1.00 37.60  ? 359 CYS B C   1 
ATOM   6007 O O   . CYS B 1 330 ? 13.744  5.353   34.594  1.00 38.11  ? 359 CYS B O   1 
ATOM   6008 C CB  . CYS B 1 330 ? 12.967  7.768   32.091  1.00 48.82  ? 359 CYS B CB  1 
ATOM   6009 S SG  . CYS B 1 330 ? 12.619  6.301   31.137  1.00 58.12  ? 359 CYS B SG  1 
ATOM   6010 N N   . GLN B 1 331 ? 15.433  5.805   33.220  1.00 34.70  ? 360 GLN B N   1 
ATOM   6011 C CA  . GLN B 1 331 ? 16.075  4.520   33.471  1.00 38.87  ? 360 GLN B CA  1 
ATOM   6012 C C   . GLN B 1 331 ? 16.761  4.530   34.851  1.00 38.81  ? 360 GLN B C   1 
ATOM   6013 O O   . GLN B 1 331 ? 16.793  3.524   35.562  1.00 35.71  ? 360 GLN B O   1 
ATOM   6014 C CB  . GLN B 1 331 ? 17.043  4.236   32.320  1.00 38.13  ? 360 GLN B CB  1 
ATOM   6015 C CG  . GLN B 1 331 ? 16.369  4.053   30.969  1.00 39.14  ? 360 GLN B CG  1 
ATOM   6016 C CD  . GLN B 1 331 ? 17.335  3.736   29.844  1.00 46.90  ? 360 GLN B CD  1 
ATOM   6017 O OE1 . GLN B 1 331 ? 17.739  2.587   29.627  1.00 44.99  ? 360 GLN B OE1 1 
ATOM   6018 N NE2 . GLN B 1 331 ? 17.683  4.755   29.075  1.00 49.58  ? 360 GLN B NE2 1 
ATOM   6019 N N   . ARG B 1 332 ? 17.287  5.693   35.244  1.00 35.78  ? 361 ARG B N   1 
ATOM   6020 C CA  . ARG B 1 332 ? 17.912  5.867   36.542  1.00 35.13  ? 361 ARG B CA  1 
ATOM   6021 C C   . ARG B 1 332 ? 16.921  5.546   37.649  1.00 40.24  ? 361 ARG B C   1 
ATOM   6022 O O   . ARG B 1 332 ? 17.246  4.783   38.554  1.00 43.61  ? 361 ARG B O   1 
ATOM   6023 C CB  . ARG B 1 332 ? 18.470  7.285   36.665  1.00 41.47  ? 361 ARG B CB  1 
ATOM   6024 C CG  . ARG B 1 332 ? 19.091  7.587   38.020  1.00 40.35  ? 361 ARG B CG  1 
ATOM   6025 C CD  . ARG B 1 332 ? 19.749  8.963   38.040  1.00 42.60  ? 361 ARG B CD  1 
ATOM   6026 N NE  . ARG B 1 332 ? 19.995  9.293   39.452  1.00 42.78  ? 361 ARG B NE  1 
ATOM   6027 C CZ  . ARG B 1 332 ? 21.031  8.851   40.165  1.00 51.90  ? 361 ARG B CZ  1 
ATOM   6028 N NH1 . ARG B 1 332 ? 22.049  8.240   39.579  1.00 52.71  ? 361 ARG B NH1 1 
ATOM   6029 N NH2 . ARG B 1 332 ? 21.070  9.037   41.475  1.00 47.92  ? 361 ARG B NH2 1 
ATOM   6030 N N   . GLU B 1 333 ? 15.723  6.145   37.586  1.00 40.10  ? 362 GLU B N   1 
ATOM   6031 C CA  . GLU B 1 333 ? 14.679  5.886   38.568  1.00 40.39  ? 362 GLU B CA  1 
ATOM   6032 C C   . GLU B 1 333 ? 14.350  4.391   38.594  1.00 39.47  ? 362 GLU B C   1 
ATOM   6033 O O   . GLU B 1 333 ? 14.131  3.818   39.663  1.00 32.59  ? 362 GLU B O   1 
ATOM   6034 C CB  . GLU B 1 333 ? 13.398  6.662   38.259  1.00 44.80  ? 362 GLU B CB  1 
ATOM   6035 C CG  . GLU B 1 333 ? 13.561  8.178   38.381  1.00 58.50  ? 362 GLU B CG  1 
ATOM   6036 C CD  . GLU B 1 333 ? 12.575  9.033   37.585  1.00 65.66  ? 362 GLU B CD  1 
ATOM   6037 O OE1 . GLU B 1 333 ? 11.637  8.492   36.932  1.00 61.21  ? 362 GLU B OE1 1 
ATOM   6038 O OE2 . GLU B 1 333 ? 12.773  10.271  37.613  1.00 75.32  ? 362 GLU B OE2 1 
ATOM   6039 N N   . PHE B 1 334 ? 14.303  3.764   37.406  1.00 35.90  ? 363 PHE B N   1 
ATOM   6040 C CA  . PHE B 1 334 ? 13.985  2.344   37.305  1.00 33.74  ? 363 PHE B CA  1 
ATOM   6041 C C   . PHE B 1 334 ? 14.965  1.512   38.153  1.00 33.43  ? 363 PHE B C   1 
ATOM   6042 O O   . PHE B 1 334 ? 14.571  0.617   38.941  1.00 29.99  ? 363 PHE B O   1 
ATOM   6043 C CB  . PHE B 1 334 ? 14.055  1.889   35.845  1.00 29.83  ? 363 PHE B CB  1 
ATOM   6044 C CG  . PHE B 1 334 ? 13.629  0.441   35.682  1.00 32.95  ? 363 PHE B CG  1 
ATOM   6045 C CD1 . PHE B 1 334 ? 14.555  -0.588  35.796  1.00 32.71  ? 363 PHE B CD1 1 
ATOM   6046 C CD2 . PHE B 1 334 ? 12.305  0.114   35.456  1.00 30.31  ? 363 PHE B CD2 1 
ATOM   6047 C CE1 . PHE B 1 334 ? 14.160  -1.907  35.672  1.00 32.39  ? 363 PHE B CE1 1 
ATOM   6048 C CE2 . PHE B 1 334 ? 11.923  -1.209  35.331  1.00 34.17  ? 363 PHE B CE2 1 
ATOM   6049 C CZ  . PHE B 1 334 ? 12.850  -2.214  35.442  1.00 35.10  ? 363 PHE B CZ  1 
ATOM   6050 N N   . ALA B 1 335 ? 16.245  1.822   37.935  1.00 33.05  ? 364 ALA B N   1 
ATOM   6051 C CA  . ALA B 1 335 ? 17.363  1.099   38.520  1.00 40.36  ? 364 ALA B CA  1 
ATOM   6052 C C   . ALA B 1 335 ? 17.418  1.303   40.040  1.00 38.86  ? 364 ALA B C   1 
ATOM   6053 O O   . ALA B 1 335 ? 17.647  0.324   40.767  1.00 34.85  ? 364 ALA B O   1 
ATOM   6054 C CB  . ALA B 1 335 ? 18.652  1.527   37.859  1.00 41.05  ? 364 ALA B CB  1 
ATOM   6055 N N   . LEU B 1 336 ? 17.159  2.546   40.485  1.00 34.76  ? 365 LEU B N   1 
ATOM   6056 C CA  . LEU B 1 336 ? 17.229  2.931   41.891  1.00 40.51  ? 365 LEU B CA  1 
ATOM   6057 C C   . LEU B 1 336 ? 16.144  2.169   42.645  1.00 39.19  ? 365 LEU B C   1 
ATOM   6058 O O   . LEU B 1 336 ? 16.331  1.789   43.798  1.00 42.17  ? 365 LEU B O   1 
ATOM   6059 C CB  . LEU B 1 336 ? 17.069  4.434   42.126  1.00 42.79  ? 365 LEU B CB  1 
ATOM   6060 C CG  . LEU B 1 336 ? 18.224  5.354   41.716  1.00 42.87  ? 365 LEU B CG  1 
ATOM   6061 C CD1 . LEU B 1 336 ? 17.724  6.791   41.712  1.00 39.14  ? 365 LEU B CD1 1 
ATOM   6062 C CD2 . LEU B 1 336 ? 19.431  5.278   42.665  1.00 49.53  ? 365 LEU B CD2 1 
ATOM   6063 N N   . LYS B 1 337 ? 15.029  1.888   41.964  1.00 35.34  ? 366 LYS B N   1 
ATOM   6064 C CA  . LYS B 1 337 ? 13.951  1.117   42.546  1.00 42.25  ? 366 LYS B CA  1 
ATOM   6065 C C   . LYS B 1 337 ? 14.279  -0.378  42.595  1.00 41.38  ? 366 LYS B C   1 
ATOM   6066 O O   . LYS B 1 337 ? 13.963  -1.025  43.590  1.00 40.57  ? 366 LYS B O   1 
ATOM   6067 C CB  . LYS B 1 337 ? 12.635  1.272   41.780  1.00 44.31  ? 366 LYS B CB  1 
ATOM   6068 C CG  . LYS B 1 337 ? 11.729  2.370   42.227  1.00 52.52  ? 366 LYS B CG  1 
ATOM   6069 C CD  . LYS B 1 337 ? 10.580  2.550   41.247  1.00 60.25  ? 366 LYS B CD  1 
ATOM   6070 C CE  . LYS B 1 337 ? 10.253  3.984   40.984  1.00 63.64  ? 366 LYS B CE  1 
ATOM   6071 N NZ  . LYS B 1 337 ? 9.451   4.087   39.766  1.00 66.59  ? 366 LYS B NZ  1 
ATOM   6072 N N   . HIS B 1 338 ? 14.860  -0.937  41.527  1.00 36.85  ? 367 HIS B N   1 
ATOM   6073 C CA  . HIS B 1 338 ? 14.777  -2.376  41.305  1.00 36.18  ? 367 HIS B CA  1 
ATOM   6074 C C   . HIS B 1 338 ? 16.130  -3.078  41.421  1.00 35.06  ? 367 HIS B C   1 
ATOM   6075 O O   . HIS B 1 338 ? 16.146  -4.262  41.715  1.00 37.17  ? 367 HIS B O   1 
ATOM   6076 C CB  . HIS B 1 338 ? 14.130  -2.728  39.950  1.00 35.36  ? 367 HIS B CB  1 
ATOM   6077 C CG  . HIS B 1 338 ? 12.717  -2.278  39.810  1.00 38.50  ? 367 HIS B CG  1 
ATOM   6078 N ND1 . HIS B 1 338 ? 11.716  -2.614  40.702  1.00 38.63  ? 367 HIS B ND1 1 
ATOM   6079 C CD2 . HIS B 1 338 ? 12.139  -1.477  38.879  1.00 36.15  ? 367 HIS B CD2 1 
ATOM   6080 C CE1 . HIS B 1 338 ? 10.581  -2.051  40.319  1.00 38.87  ? 367 HIS B CE1 1 
ATOM   6081 N NE2 . HIS B 1 338 ? 10.820  -1.360  39.210  1.00 37.52  ? 367 HIS B NE2 1 
ATOM   6082 N N   . LEU B 1 339 ? 17.236  -2.391  41.142  1.00 32.40  ? 368 LEU B N   1 
ATOM   6083 C CA  . LEU B 1 339 ? 18.558  -2.997  41.254  1.00 32.81  ? 368 LEU B CA  1 
ATOM   6084 C C   . LEU B 1 339 ? 19.534  -2.023  41.890  1.00 33.70  ? 368 LEU B C   1 
ATOM   6085 O O   . LEU B 1 339 ? 20.579  -1.788  41.323  1.00 34.76  ? 368 LEU B O   1 
ATOM   6086 C CB  . LEU B 1 339 ? 19.110  -3.383  39.881  1.00 34.58  ? 368 LEU B CB  1 
ATOM   6087 C CG  . LEU B 1 339 ? 19.053  -2.286  38.821  1.00 32.29  ? 368 LEU B CG  1 
ATOM   6088 C CD1 . LEU B 1 339 ? 20.317  -2.242  38.012  1.00 31.31  ? 368 LEU B CD1 1 
ATOM   6089 C CD2 . LEU B 1 339 ? 17.844  -2.490  37.897  1.00 33.10  ? 368 LEU B CD2 1 
ATOM   6090 N N   . PRO B 1 340 ? 19.259  -1.435  43.074  1.00 32.76  ? 369 PRO B N   1 
ATOM   6091 C CA  . PRO B 1 340 ? 20.210  -0.491  43.665  1.00 35.71  ? 369 PRO B CA  1 
ATOM   6092 C C   . PRO B 1 340 ? 21.549  -1.109  44.092  1.00 35.91  ? 369 PRO B C   1 
ATOM   6093 O O   . PRO B 1 340 ? 22.540  -0.399  44.224  1.00 39.79  ? 369 PRO B O   1 
ATOM   6094 C CB  . PRO B 1 340 ? 19.415  0.134   44.853  1.00 35.48  ? 369 PRO B CB  1 
ATOM   6095 C CG  . PRO B 1 340 ? 18.329  -0.883  45.201  1.00 34.57  ? 369 PRO B CG  1 
ATOM   6096 C CD  . PRO B 1 340 ? 18.068  -1.665  43.908  1.00 36.42  ? 369 PRO B CD  1 
ATOM   6097 N N   . ASN B 1 341 ? 21.599  -2.434  44.284  1.00 37.33  ? 370 ASN B N   1 
ATOM   6098 C CA  . ASN B 1 341 ? 22.821  -3.057  44.780  1.00 42.32  ? 370 ASN B CA  1 
ATOM   6099 C C   . ASN B 1 341 ? 23.743  -3.446  43.622  1.00 40.38  ? 370 ASN B C   1 
ATOM   6100 O O   . ASN B 1 341 ? 24.922  -3.691  43.861  1.00 39.62  ? 370 ASN B O   1 
ATOM   6101 C CB  . ASN B 1 341 ? 22.546  -4.253  45.688  1.00 41.43  ? 370 ASN B CB  1 
ATOM   6102 C CG  . ASN B 1 341 ? 21.826  -3.854  46.958  1.00 43.87  ? 370 ASN B CG  1 
ATOM   6103 O OD1 . ASN B 1 341 ? 22.374  -3.126  47.789  1.00 49.69  ? 370 ASN B OD1 1 
ATOM   6104 N ND2 . ASN B 1 341 ? 20.593  -4.304  47.123  1.00 42.80  ? 370 ASN B ND2 1 
ATOM   6105 N N   . ASP B 1 342 ? 23.220  -3.509  42.380  1.00 36.10  ? 371 ASP B N   1 
ATOM   6106 C CA  . ASP B 1 342 ? 24.012  -3.974  41.243  1.00 36.16  ? 371 ASP B CA  1 
ATOM   6107 C C   . ASP B 1 342 ? 25.274  -3.121  41.108  1.00 34.26  ? 371 ASP B C   1 
ATOM   6108 O O   . ASP B 1 342 ? 25.188  -1.899  41.183  1.00 35.33  ? 371 ASP B O   1 
ATOM   6109 C CB  . ASP B 1 342 ? 23.249  -3.959  39.924  1.00 36.41  ? 371 ASP B CB  1 
ATOM   6110 C CG  . ASP B 1 342 ? 24.120  -4.387  38.743  1.00 40.16  ? 371 ASP B CG  1 
ATOM   6111 O OD1 . ASP B 1 342 ? 24.545  -5.572  38.736  1.00 34.37  ? 371 ASP B OD1 1 
ATOM   6112 O OD2 . ASP B 1 342 ? 24.458  -3.524  37.903  1.00 42.27  ? 371 ASP B OD2 1 
ATOM   6113 N N   . PRO B 1 343 ? 26.485  -3.729  40.993  1.00 39.70  ? 372 PRO B N   1 
ATOM   6114 C CA  . PRO B 1 343 ? 27.737  -2.974  40.801  1.00 37.81  ? 372 PRO B CA  1 
ATOM   6115 C C   . PRO B 1 343 ? 27.853  -2.041  39.591  1.00 39.97  ? 372 PRO B C   1 
ATOM   6116 O O   . PRO B 1 343 ? 28.268  -0.881  39.735  1.00 40.20  ? 372 PRO B O   1 
ATOM   6117 C CB  . PRO B 1 343 ? 28.832  -4.067  40.739  1.00 39.16  ? 372 PRO B CB  1 
ATOM   6118 C CG  . PRO B 1 343 ? 28.218  -5.311  41.352  1.00 39.63  ? 372 PRO B CG  1 
ATOM   6119 C CD  . PRO B 1 343 ? 26.715  -5.174  41.170  1.00 39.59  ? 372 PRO B CD  1 
ATOM   6120 N N   . MET B 1 344 ? 27.539  -2.545  38.386  1.00 39.51  ? 373 MET B N   1 
ATOM   6121 C CA  . MET B 1 344 ? 27.669  -1.743  37.175  1.00 38.17  ? 373 MET B CA  1 
ATOM   6122 C C   . MET B 1 344 ? 26.689  -0.572  37.234  1.00 38.22  ? 373 MET B C   1 
ATOM   6123 O O   . MET B 1 344 ? 27.023  0.551   36.846  1.00 32.18  ? 373 MET B O   1 
ATOM   6124 C CB  . MET B 1 344 ? 27.408  -2.544  35.886  1.00 42.89  ? 373 MET B CB  1 
ATOM   6125 C CG  . MET B 1 344 ? 28.521  -3.544  35.524  1.00 52.38  ? 373 MET B CG  1 
ATOM   6126 S SD  . MET B 1 344 ? 30.031  -2.817  34.829  1.00 58.67  ? 373 MET B SD  1 
ATOM   6127 C CE  . MET B 1 344 ? 29.445  -2.362  33.190  1.00 57.17  ? 373 MET B CE  1 
ATOM   6128 N N   . PHE B 1 345 ? 25.463  -0.825  37.710  1.00 38.95  ? 374 PHE B N   1 
ATOM   6129 C CA  . PHE B 1 345 ? 24.546  0.287   37.892  1.00 38.11  ? 374 PHE B CA  1 
ATOM   6130 C C   . PHE B 1 345 ? 25.186  1.301   38.857  1.00 42.13  ? 374 PHE B C   1 
ATOM   6131 O O   . PHE B 1 345 ? 25.200  2.497   38.576  1.00 40.50  ? 374 PHE B O   1 
ATOM   6132 C CB  . PHE B 1 345 ? 23.164  -0.158  38.387  1.00 40.45  ? 374 PHE B CB  1 
ATOM   6133 C CG  . PHE B 1 345 ? 22.380  1.036   38.898  1.00 38.93  ? 374 PHE B CG  1 
ATOM   6134 C CD1 . PHE B 1 345 ? 22.316  2.203   38.140  1.00 42.42  ? 374 PHE B CD1 1 
ATOM   6135 C CD2 . PHE B 1 345 ? 21.847  1.043   40.190  1.00 43.91  ? 374 PHE B CD2 1 
ATOM   6136 C CE1 . PHE B 1 345 ? 21.662  3.326   38.634  1.00 50.34  ? 374 PHE B CE1 1 
ATOM   6137 C CE2 . PHE B 1 345 ? 21.214  2.180   40.688  1.00 48.92  ? 374 PHE B CE2 1 
ATOM   6138 C CZ  . PHE B 1 345 ? 21.112  3.315   39.901  1.00 46.73  ? 374 PHE B CZ  1 
ATOM   6139 N N   . LYS B 1 346 ? 25.741  0.833   39.993  1.00 42.94  ? 375 LYS B N   1 
ATOM   6140 C CA  . LYS B 1 346 ? 26.323  1.749   40.978  1.00 42.39  ? 375 LYS B CA  1 
ATOM   6141 C C   . LYS B 1 346 ? 27.461  2.565   40.355  1.00 39.97  ? 375 LYS B C   1 
ATOM   6142 O O   . LYS B 1 346 ? 27.649  3.727   40.703  1.00 45.84  ? 375 LYS B O   1 
ATOM   6143 C CB  . LYS B 1 346 ? 26.809  1.067   42.263  1.00 42.21  ? 375 LYS B CB  1 
ATOM   6144 C CG  . LYS B 1 346 ? 25.693  0.490   43.141  1.00 46.54  ? 375 LYS B CG  1 
ATOM   6145 C CD  . LYS B 1 346 ? 26.013  0.492   44.626  1.00 50.95  ? 375 LYS B CD  1 
ATOM   6146 C CE  . LYS B 1 346 ? 27.278  -0.235  44.920  1.00 54.31  ? 375 LYS B CE  1 
ATOM   6147 N NZ  . LYS B 1 346 ? 27.326  -0.558  46.347  1.00 57.54  ? 375 LYS B NZ  1 
ATOM   6148 N N   . LEU B 1 347 ? 28.178  1.988   39.389  1.00 45.26  ? 376 LEU B N   1 
ATOM   6149 C CA  . LEU B 1 347 ? 29.185  2.747   38.654  1.00 41.79  ? 376 LEU B CA  1 
ATOM   6150 C C   . LEU B 1 347 ? 28.486  3.810   37.806  1.00 42.68  ? 376 LEU B C   1 
ATOM   6151 O O   . LEU B 1 347 ? 28.851  4.986   37.886  1.00 38.82  ? 376 LEU B O   1 
ATOM   6152 C CB  . LEU B 1 347 ? 30.092  1.839   37.826  1.00 42.58  ? 376 LEU B CB  1 
ATOM   6153 C CG  . LEU B 1 347 ? 31.070  2.529   36.863  1.00 44.53  ? 376 LEU B CG  1 
ATOM   6154 C CD1 . LEU B 1 347 ? 32.060  3.466   37.547  1.00 43.12  ? 376 LEU B CD1 1 
ATOM   6155 C CD2 . LEU B 1 347 ? 31.833  1.453   36.076  1.00 44.51  ? 376 LEU B CD2 1 
ATOM   6156 N N   . VAL B 1 348 ? 27.420  3.423   37.074  1.00 37.38  ? 377 VAL B N   1 
ATOM   6157 C CA  . VAL B 1 348 ? 26.757  4.377   36.200  1.00 39.12  ? 377 VAL B CA  1 
ATOM   6158 C C   . VAL B 1 348 ? 26.188  5.523   37.036  1.00 36.79  ? 377 VAL B C   1 
ATOM   6159 O O   . VAL B 1 348 ? 26.352  6.678   36.676  1.00 32.82  ? 377 VAL B O   1 
ATOM   6160 C CB  . VAL B 1 348 ? 25.709  3.708   35.298  1.00 41.37  ? 377 VAL B CB  1 
ATOM   6161 C CG1 . VAL B 1 348 ? 24.790  4.716   34.624  1.00 40.65  ? 377 VAL B CG1 1 
ATOM   6162 C CG2 . VAL B 1 348 ? 26.394  2.820   34.264  1.00 39.97  ? 377 VAL B CG2 1 
ATOM   6163 N N   . ALA B 1 349 ? 25.645  5.216   38.222  1.00 42.96  ? 378 ALA B N   1 
ATOM   6164 C CA  . ALA B 1 349 ? 25.194  6.257   39.142  1.00 40.95  ? 378 ALA B CA  1 
ATOM   6165 C C   . ALA B 1 349 ? 26.375  7.073   39.653  1.00 40.89  ? 378 ALA B C   1 
ATOM   6166 O O   . ALA B 1 349 ? 26.228  8.257   39.927  1.00 47.56  ? 378 ALA B O   1 
ATOM   6167 C CB  . ALA B 1 349 ? 24.410  5.665   40.298  1.00 42.34  ? 378 ALA B CB  1 
ATOM   6168 N N   . GLN B 1 350 ? 27.541  6.440   39.813  1.00 47.89  ? 379 GLN B N   1 
ATOM   6169 C CA  . GLN B 1 350 ? 28.730  7.157   40.262  1.00 51.14  ? 379 GLN B CA  1 
ATOM   6170 C C   . GLN B 1 350 ? 29.273  8.070   39.148  1.00 46.91  ? 379 GLN B C   1 
ATOM   6171 O O   . GLN B 1 350 ? 29.684  9.204   39.394  1.00 42.20  ? 379 GLN B O   1 
ATOM   6172 C CB  . GLN B 1 350 ? 29.727  6.112   40.757  1.00 51.36  ? 379 GLN B CB  1 
ATOM   6173 C CG  . GLN B 1 350 ? 30.807  6.653   41.683  1.00 55.33  ? 379 GLN B CG  1 
ATOM   6174 C CD  . GLN B 1 350 ? 31.732  5.561   42.170  1.00 55.38  ? 379 GLN B CD  1 
ATOM   6175 O OE1 . GLN B 1 350 ? 31.678  4.413   41.705  1.00 48.85  ? 379 GLN B OE1 1 
ATOM   6176 N NE2 . GLN B 1 350 ? 32.586  5.918   43.118  1.00 57.59  ? 379 GLN B NE2 1 
ATOM   6177 N N   . LEU B 1 351 ? 29.231  7.603   37.897  1.00 46.59  ? 380 LEU B N   1 
ATOM   6178 C CA  . LEU B 1 351 ? 29.669  8.421   36.773  1.00 43.95  ? 380 LEU B CA  1 
ATOM   6179 C C   . LEU B 1 351 ? 28.757  9.629   36.587  1.00 49.81  ? 380 LEU B C   1 
ATOM   6180 O O   . LEU B 1 351 ? 29.180  10.637  36.030  1.00 53.72  ? 380 LEU B O   1 
ATOM   6181 C CB  . LEU B 1 351 ? 29.674  7.574   35.510  1.00 47.71  ? 380 LEU B CB  1 
ATOM   6182 C CG  . LEU B 1 351 ? 30.857  6.625   35.333  1.00 47.72  ? 380 LEU B CG  1 
ATOM   6183 C CD1 . LEU B 1 351 ? 30.579  5.622   34.231  1.00 45.08  ? 380 LEU B CD1 1 
ATOM   6184 C CD2 . LEU B 1 351 ? 32.120  7.422   35.039  1.00 48.42  ? 380 LEU B CD2 1 
ATOM   6185 N N   . TYR B 1 352 ? 27.487  9.512   37.002  1.00 54.61  ? 381 TYR B N   1 
ATOM   6186 C CA  . TYR B 1 352 ? 26.532  10.603  36.844  1.00 58.48  ? 381 TYR B CA  1 
ATOM   6187 C C   . TYR B 1 352 ? 26.834  11.737  37.827  1.00 56.66  ? 381 TYR B C   1 
ATOM   6188 O O   . TYR B 1 352 ? 26.669  12.898  37.493  1.00 50.56  ? 381 TYR B O   1 
ATOM   6189 C CB  . TYR B 1 352 ? 25.108  10.083  37.049  1.00 59.38  ? 381 TYR B CB  1 
ATOM   6190 C CG  . TYR B 1 352 ? 24.010  11.110  36.802  1.00 58.59  ? 381 TYR B CG  1 
ATOM   6191 C CD1 . TYR B 1 352 ? 24.024  11.915  35.669  1.00 56.56  ? 381 TYR B CD1 1 
ATOM   6192 C CD2 . TYR B 1 352 ? 22.973  11.283  37.717  1.00 59.52  ? 381 TYR B CD2 1 
ATOM   6193 C CE1 . TYR B 1 352 ? 23.027  12.849  35.442  1.00 57.77  ? 381 TYR B CE1 1 
ATOM   6194 C CE2 . TYR B 1 352 ? 21.970  12.214  37.500  1.00 58.04  ? 381 TYR B CE2 1 
ATOM   6195 C CZ  . TYR B 1 352 ? 21.997  12.991  36.354  1.00 58.51  ? 381 TYR B CZ  1 
ATOM   6196 O OH  . TYR B 1 352 ? 21.012  13.897  36.117  1.00 69.06  ? 381 TYR B OH  1 
ATOM   6197 N N   . LYS B 1 353 ? 27.298  11.394  39.034  1.00 63.94  ? 382 LYS B N   1 
ATOM   6198 C CA  . LYS B 1 353 ? 27.559  12.381  40.071  1.00 63.83  ? 382 LYS B CA  1 
ATOM   6199 C C   . LYS B 1 353 ? 28.854  13.137  39.805  1.00 55.09  ? 382 LYS B C   1 
ATOM   6200 O O   . LYS B 1 353 ? 29.056  14.170  40.416  1.00 53.96  ? 382 LYS B O   1 
ATOM   6201 C CB  . LYS B 1 353 ? 27.804  11.758  41.448  1.00 72.57  ? 382 LYS B CB  1 
ATOM   6202 C CG  . LYS B 1 353 ? 26.702  10.903  42.046  1.00 80.72  ? 382 LYS B CG  1 
ATOM   6203 C CD  . LYS B 1 353 ? 27.254  9.916   43.071  1.00 87.79  ? 382 LYS B CD  1 
ATOM   6204 C CE  . LYS B 1 353 ? 28.130  10.537  44.127  1.00 86.25  ? 382 LYS B CE  1 
ATOM   6205 N NZ  . LYS B 1 353 ? 29.179  9.608   44.557  1.00 91.57  ? 382 LYS B NZ  1 
ATOM   6206 N N   . ILE B 1 354 ? 29.713  12.610  38.918  1.00 57.35  ? 383 ILE B N   1 
ATOM   6207 C CA  . ILE B 1 354 ? 31.096  13.050  38.778  1.00 56.23  ? 383 ILE B CA  1 
ATOM   6208 C C   . ILE B 1 354 ? 31.410  13.521  37.354  1.00 56.52  ? 383 ILE B C   1 
ATOM   6209 O O   . ILE B 1 354 ? 32.206  14.433  37.167  1.00 46.48  ? 383 ILE B O   1 
ATOM   6210 C CB  . ILE B 1 354 ? 32.045  11.905  39.192  1.00 55.53  ? 383 ILE B CB  1 
ATOM   6211 C CG1 . ILE B 1 354 ? 31.903  11.564  40.683  1.00 56.10  ? 383 ILE B CG1 1 
ATOM   6212 C CG2 . ILE B 1 354 ? 33.495  12.213  38.810  1.00 50.48  ? 383 ILE B CG2 1 
ATOM   6213 C CD1 . ILE B 1 354 ? 32.577  10.266  41.080  1.00 63.94  ? 383 ILE B CD1 1 
ATOM   6214 N N   . VAL B 1 355 ? 30.884  12.846  36.329  1.00 57.53  ? 384 VAL B N   1 
ATOM   6215 C CA  . VAL B 1 355 ? 31.362  13.085  34.971  1.00 54.39  ? 384 VAL B CA  1 
ATOM   6216 C C   . VAL B 1 355 ? 30.982  14.495  34.522  1.00 53.71  ? 384 VAL B C   1 
ATOM   6217 O O   . VAL B 1 355 ? 31.806  15.185  33.909  1.00 50.10  ? 384 VAL B O   1 
ATOM   6218 C CB  . VAL B 1 355 ? 30.900  12.012  33.964  1.00 49.20  ? 384 VAL B CB  1 
ATOM   6219 C CG1 . VAL B 1 355 ? 30.957  12.486  32.510  1.00 48.75  ? 384 VAL B CG1 1 
ATOM   6220 C CG2 . VAL B 1 355 ? 31.740  10.748  34.141  1.00 48.11  ? 384 VAL B CG2 1 
ATOM   6221 N N   . PRO B 1 356 ? 29.681  15.003  34.973  1.00 57.86  ? 385 PRO B N   1 
ATOM   6222 C CA  . PRO B 1 356 ? 29.464  16.239  34.230  1.00 65.63  ? 385 PRO B CA  1 
ATOM   6223 C C   . PRO B 1 356 ? 30.686  17.130  34.248  1.00 67.21  ? 385 PRO B C   1 
ATOM   6224 O O   . PRO B 1 356 ? 30.727  17.822  33.238  1.00 58.25  ? 385 PRO B O   1 
ATOM   6225 C CB  . PRO B 1 356 ? 28.254  16.792  34.946  1.00 65.46  ? 385 PRO B CB  1 
ATOM   6226 C CG  . PRO B 1 356 ? 27.366  15.580  35.041  1.00 59.57  ? 385 PRO B CG  1 
ATOM   6227 C CD  . PRO B 1 356 ? 28.350  14.471  35.363  1.00 58.85  ? 385 PRO B CD  1 
ATOM   6228 N N   . ASN B 1 357 ? 31.529  17.126  35.405  1.00 85.36  ? 386 ASN B N   1 
ATOM   6229 C CA  . ASN B 1 357 ? 32.842  17.783  35.348  1.00 84.85  ? 386 ASN B CA  1 
ATOM   6230 C C   . ASN B 1 357 ? 33.147  18.423  33.992  1.00 91.20  ? 386 ASN B C   1 
ATOM   6231 O O   . ASN B 1 357 ? 34.169  18.112  33.374  1.00 70.77  ? 386 ASN B O   1 
ATOM   6232 C CB  . ASN B 1 357 ? 34.006  16.822  35.597  1.00 80.26  ? 386 ASN B CB  1 
ATOM   6233 C CG  . ASN B 1 357 ? 34.462  16.772  37.033  1.00 94.48  ? 386 ASN B CG  1 
ATOM   6234 O OD1 . ASN B 1 357 ? 35.345  15.971  37.362  1.00 90.36  ? 386 ASN B OD1 1 
ATOM   6235 N ND2 . ASN B 1 357 ? 33.908  17.617  37.892  1.00 101.78 ? 386 ASN B ND2 1 
ATOM   6236 N N   . VAL B 1 358 ? 32.256  19.340  33.582  1.00 98.09  ? 387 VAL B N   1 
ATOM   6237 C CA  . VAL B 1 358 ? 32.473  20.348  32.557  1.00 94.78  ? 387 VAL B CA  1 
ATOM   6238 C C   . VAL B 1 358 ? 33.086  19.731  31.294  1.00 95.63  ? 387 VAL B C   1 
ATOM   6239 O O   . VAL B 1 358 ? 34.251  19.350  31.270  1.00 87.64  ? 387 VAL B O   1 
ATOM   6240 C CB  . VAL B 1 358 ? 33.316  21.511  33.129  1.00 102.19 ? 387 VAL B CB  1 
ATOM   6241 C CG1 . VAL B 1 358 ? 32.851  22.866  32.615  1.00 104.61 ? 387 VAL B CG1 1 
ATOM   6242 C CG2 . VAL B 1 358 ? 33.303  21.555  34.654  1.00 108.64 ? 387 VAL B CG2 1 
ATOM   6243 N N   . LEU B 1 359 ? 32.259  19.627  30.240  1.00 121.76 ? 388 LEU B N   1 
ATOM   6244 C CA  . LEU B 1 359 ? 32.716  19.537  28.856  1.00 125.78 ? 388 LEU B CA  1 
ATOM   6245 C C   . LEU B 1 359 ? 32.820  20.943  28.257  1.00 124.18 ? 388 LEU B C   1 
ATOM   6246 O O   . LEU B 1 359 ? 33.062  21.092  27.055  1.00 112.70 ? 388 LEU B O   1 
ATOM   6247 C CB  . LEU B 1 359 ? 31.772  18.661  28.029  1.00 123.20 ? 388 LEU B CB  1 
ATOM   6248 C CG  . LEU B 1 359 ? 32.177  17.191  27.867  1.00 116.53 ? 388 LEU B CG  1 
ATOM   6249 C CD1 . LEU B 1 359 ? 32.368  16.457  29.193  1.00 105.22 ? 388 LEU B CD1 1 
ATOM   6250 C CD2 . LEU B 1 359 ? 31.141  16.494  27.000  1.00 113.74 ? 388 LEU B CD2 1 
ATOM   6251 N N   . LEU B 1 360 ? 32.581  21.949  29.117  1.00 118.10 ? 389 LEU B N   1 
ATOM   6252 C CA  . LEU B 1 360 ? 32.874  23.351  28.860  1.00 115.11 ? 389 LEU B CA  1 
ATOM   6253 C C   . LEU B 1 360 ? 34.249  23.699  29.449  1.00 105.90 ? 389 LEU B C   1 
ATOM   6254 O O   . LEU B 1 360 ? 34.755  24.795  29.222  1.00 107.12 ? 389 LEU B O   1 
ATOM   6255 C CB  . LEU B 1 360 ? 31.770  24.252  29.430  1.00 121.11 ? 389 LEU B CB  1 
ATOM   6256 C CG  . LEU B 1 360 ? 30.343  23.678  29.494  1.00 120.42 ? 389 LEU B CG  1 
ATOM   6257 C CD1 . LEU B 1 360 ? 30.011  23.162  30.896  1.00 121.25 ? 389 LEU B CD1 1 
ATOM   6258 C CD2 . LEU B 1 360 ? 29.274  24.673  29.044  1.00 109.14 ? 389 LEU B CD2 1 
ATOM   6259 N N   . GLU B 1 361 ? 34.870  22.718  30.107  1.00 95.78  ? 390 GLU B N   1 
ATOM   6260 C CA  . GLU B 1 361 ? 36.282  22.930  30.500  1.00 90.83  ? 390 GLU B CA  1 
ATOM   6261 C C   . GLU B 1 361 ? 37.012  22.879  29.156  1.00 91.23  ? 390 GLU B C   1 
ATOM   6262 O O   . GLU B 1 361 ? 38.201  23.261  29.102  1.00 80.75  ? 390 GLU B O   1 
ATOM   6263 C CB  . GLU B 1 361 ? 36.774  21.829  31.435  1.00 82.00  ? 390 GLU B CB  1 
ATOM   6264 C CG  . GLU B 1 361 ? 37.009  22.305  32.865  1.00 72.98  ? 390 GLU B CG  1 
ATOM   6265 C CD  . GLU B 1 361 ? 36.816  21.207  33.895  1.00 72.00  ? 390 GLU B CD  1 
ATOM   6266 O OE1 . GLU B 1 361 ? 37.052  21.467  35.092  1.00 60.36  ? 390 GLU B OE1 1 
ATOM   6267 O OE2 . GLU B 1 361 ? 36.425  20.090  33.496  1.00 95.40  ? 390 GLU B OE2 1 
ATOM   6268 N N   . GLN B 1 362 ? 36.304  22.423  28.112  1.00 108.53 ? 391 GLN B N   1 
ATOM   6269 C CA  . GLN B 1 362 ? 36.874  22.353  26.781  1.00 117.98 ? 391 GLN B CA  1 
ATOM   6270 C C   . GLN B 1 362 ? 36.323  23.512  25.950  1.00 122.17 ? 391 GLN B C   1 
ATOM   6271 O O   . GLN B 1 362 ? 37.067  24.427  25.597  1.00 114.37 ? 391 GLN B O   1 
ATOM   6272 C CB  . GLN B 1 362 ? 36.557  20.979  26.187  1.00 117.18 ? 391 GLN B CB  1 
ATOM   6273 C CG  . GLN B 1 362 ? 37.669  20.439  25.293  1.00 119.97 ? 391 GLN B CG  1 
ATOM   6274 C CD  . GLN B 1 362 ? 37.216  19.385  24.307  1.00 121.43 ? 391 GLN B CD  1 
ATOM   6275 O OE1 . GLN B 1 362 ? 38.000  18.919  23.472  1.00 109.89 ? 391 GLN B OE1 1 
ATOM   6276 N NE2 . GLN B 1 362 ? 35.946  19.006  24.383  1.00 128.18 ? 391 GLN B NE2 1 
ATOM   6277 N N   . GLY B 1 363 ? 35.009  23.476  25.685  1.00 127.10 ? 392 GLY B N   1 
ATOM   6278 C CA  . GLY B 1 363 ? 34.366  24.391  24.753  1.00 130.52 ? 392 GLY B CA  1 
ATOM   6279 C C   . GLY B 1 363 ? 33.987  23.702  23.440  1.00 134.71 ? 392 GLY B C   1 
ATOM   6280 O O   . GLY B 1 363 ? 33.242  24.271  22.645  1.00 133.47 ? 392 GLY B O   1 
ATOM   6281 N N   . LYS B 1 364 ? 34.485  22.471  23.233  1.00 146.11 ? 393 LYS B N   1 
ATOM   6282 C CA  . LYS B 1 364 ? 34.372  21.768  21.960  1.00 147.29 ? 393 LYS B CA  1 
ATOM   6283 C C   . LYS B 1 364 ? 33.370  20.617  22.089  1.00 144.70 ? 393 LYS B C   1 
ATOM   6284 O O   . LYS B 1 364 ? 33.649  19.498  21.654  1.00 142.66 ? 393 LYS B O   1 
ATOM   6285 C CB  . LYS B 1 364 ? 35.735  21.220  21.499  1.00 141.17 ? 393 LYS B CB  1 
ATOM   6286 C CG  . LYS B 1 364 ? 36.978  21.999  21.924  1.00 138.35 ? 393 LYS B CG  1 
ATOM   6287 C CD  . LYS B 1 364 ? 38.301  21.391  21.466  1.00 138.45 ? 393 LYS B CD  1 
ATOM   6288 C CE  . LYS B 1 364 ? 38.554  21.538  19.999  1.00 141.06 ? 393 LYS B CE  1 
ATOM   6289 N NZ  . LYS B 1 364 ? 38.641  22.944  19.595  1.00 143.54 ? 393 LYS B NZ  1 
ATOM   6290 N N   . ALA B 1 365 ? 32.175  20.954  23.006  1.00 139.48 ? 394 ALA B N   1 
ATOM   6291 C CA  . ALA B 1 365 ? 31.193  19.881  22.940  1.00 129.87 ? 394 ALA B CA  1 
ATOM   6292 C C   . ALA B 1 365 ? 29.796  20.454  22.696  1.00 127.05 ? 394 ALA B C   1 
ATOM   6293 O O   . ALA B 1 365 ? 29.438  20.725  21.550  1.00 118.60 ? 394 ALA B O   1 
ATOM   6294 C CB  . ALA B 1 365 ? 31.272  19.046  24.203  1.00 125.97 ? 394 ALA B CB  1 
ATOM   6295 N N   . LYS B 1 366 ? 29.127  20.878  23.794  1.00 132.76 ? 395 LYS B N   1 
ATOM   6296 C CA  . LYS B 1 366 ? 27.787  21.443  23.722  1.00 134.02 ? 395 LYS B CA  1 
ATOM   6297 C C   . LYS B 1 366 ? 26.935  21.032  24.925  1.00 138.54 ? 395 LYS B C   1 
ATOM   6298 O O   . LYS B 1 366 ? 25.880  21.626  25.132  1.00 149.73 ? 395 LYS B O   1 
ATOM   6299 C CB  . LYS B 1 366 ? 27.027  21.057  22.444  1.00 122.16 ? 395 LYS B CB  1 
ATOM   6300 N N   . ASN B 1 367 ? 27.354  20.019  25.705  1.00 130.25 ? 396 ASN B N   1 
ATOM   6301 C CA  . ASN B 1 367 ? 26.537  19.568  26.824  1.00 119.05 ? 396 ASN B CA  1 
ATOM   6302 C C   . ASN B 1 367 ? 27.315  18.623  27.740  1.00 101.98 ? 396 ASN B C   1 
ATOM   6303 O O   . ASN B 1 367 ? 27.932  17.680  27.257  1.00 105.69 ? 396 ASN B O   1 
ATOM   6304 C CB  . ASN B 1 367 ? 25.278  18.868  26.320  1.00 127.36 ? 396 ASN B CB  1 
ATOM   6305 C CG  . ASN B 1 367 ? 24.086  19.141  27.203  1.00 130.33 ? 396 ASN B CG  1 
ATOM   6306 O OD1 . ASN B 1 367 ? 23.397  18.205  27.623  1.00 144.15 ? 396 ASN B OD1 1 
ATOM   6307 N ND2 . ASN B 1 367 ? 23.819  20.411  27.472  1.00 125.88 ? 396 ASN B ND2 1 
ATOM   6308 N N   . PRO B 1 368 ? 27.293  18.823  29.084  1.00 86.29  ? 397 PRO B N   1 
ATOM   6309 C CA  . PRO B 1 368 ? 27.916  17.887  30.027  1.00 82.32  ? 397 PRO B CA  1 
ATOM   6310 C C   . PRO B 1 368 ? 27.004  16.845  30.673  1.00 74.39  ? 397 PRO B C   1 
ATOM   6311 O O   . PRO B 1 368 ? 27.303  16.361  31.765  1.00 73.94  ? 397 PRO B O   1 
ATOM   6312 C CB  . PRO B 1 368 ? 28.410  18.907  31.066  1.00 80.16  ? 397 PRO B CB  1 
ATOM   6313 C CG  . PRO B 1 368 ? 27.234  19.842  31.198  1.00 79.69  ? 397 PRO B CG  1 
ATOM   6314 C CD  . PRO B 1 368 ? 26.723  19.994  29.772  1.00 80.02  ? 397 PRO B CD  1 
ATOM   6315 N N   . TRP B 1 369 ? 25.893  16.512  30.001  1.00 67.13  ? 398 TRP B N   1 
ATOM   6316 C CA  . TRP B 1 369 ? 24.871  15.647  30.566  1.00 58.25  ? 398 TRP B CA  1 
ATOM   6317 C C   . TRP B 1 369 ? 24.771  14.353  29.763  1.00 54.46  ? 398 TRP B C   1 
ATOM   6318 O O   . TRP B 1 369 ? 25.044  14.336  28.560  1.00 46.66  ? 398 TRP B O   1 
ATOM   6319 C CB  . TRP B 1 369 ? 23.526  16.382  30.612  1.00 64.81  ? 398 TRP B CB  1 
ATOM   6320 C CG  . TRP B 1 369 ? 23.603  17.702  31.332  1.00 71.76  ? 398 TRP B CG  1 
ATOM   6321 C CD1 . TRP B 1 369 ? 23.476  18.948  30.796  1.00 72.64  ? 398 TRP B CD1 1 
ATOM   6322 C CD2 . TRP B 1 369 ? 23.850  17.894  32.740  1.00 74.74  ? 398 TRP B CD2 1 
ATOM   6323 N NE1 . TRP B 1 369 ? 23.604  19.900  31.769  1.00 76.76  ? 398 TRP B NE1 1 
ATOM   6324 C CE2 . TRP B 1 369 ? 23.836  19.285  32.972  1.00 81.41  ? 398 TRP B CE2 1 
ATOM   6325 C CE3 . TRP B 1 369 ? 24.073  17.032  33.818  1.00 82.10  ? 398 TRP B CE3 1 
ATOM   6326 C CZ2 . TRP B 1 369 ? 24.038  19.828  34.240  1.00 84.06  ? 398 TRP B CZ2 1 
ATOM   6327 C CZ3 . TRP B 1 369 ? 24.273  17.571  35.071  1.00 90.01  ? 398 TRP B CZ3 1 
ATOM   6328 C CH2 . TRP B 1 369 ? 24.253  18.950  35.278  1.00 84.59  ? 398 TRP B CH2 1 
ATOM   6329 N N   . PRO B 1 370 ? 24.399  13.221  30.411  1.00 52.99  ? 399 PRO B N   1 
ATOM   6330 C CA  . PRO B 1 370 ? 24.387  11.925  29.730  1.00 50.19  ? 399 PRO B CA  1 
ATOM   6331 C C   . PRO B 1 370 ? 23.111  11.786  28.906  1.00 49.05  ? 399 PRO B C   1 
ATOM   6332 O O   . PRO B 1 370 ? 22.057  12.218  29.365  1.00 47.17  ? 399 PRO B O   1 
ATOM   6333 C CB  . PRO B 1 370 ? 24.434  10.933  30.903  1.00 52.99  ? 399 PRO B CB  1 
ATOM   6334 C CG  . PRO B 1 370 ? 23.680  11.642  32.028  1.00 53.37  ? 399 PRO B CG  1 
ATOM   6335 C CD  . PRO B 1 370 ? 23.959  13.129  31.818  1.00 50.01  ? 399 PRO B CD  1 
ATOM   6336 N N   . ASN B 1 371 ? 23.221  11.162  27.724  1.00 53.46  ? 400 ASN B N   1 
ATOM   6337 C CA  . ASN B 1 371 ? 22.073  10.874  26.870  1.00 55.36  ? 400 ASN B CA  1 
ATOM   6338 C C   . ASN B 1 371 ? 21.481  9.502   27.224  1.00 56.38  ? 400 ASN B C   1 
ATOM   6339 O O   . ASN B 1 371 ? 21.900  8.858   28.194  1.00 53.37  ? 400 ASN B O   1 
ATOM   6340 C CB  . ASN B 1 371 ? 22.433  11.043  25.396  1.00 56.10  ? 400 ASN B CB  1 
ATOM   6341 C CG  . ASN B 1 371 ? 23.107  9.840   24.778  1.00 67.07  ? 400 ASN B CG  1 
ATOM   6342 O OD1 . ASN B 1 371 ? 22.575  8.726   24.839  1.00 66.50  ? 400 ASN B OD1 1 
ATOM   6343 N ND2 . ASN B 1 371 ? 24.251  10.045  24.141  1.00 71.80  ? 400 ASN B ND2 1 
ATOM   6344 N N   . VAL B 1 372 ? 20.486  9.064   26.426  1.00 56.32  ? 401 VAL B N   1 
ATOM   6345 C CA  . VAL B 1 372 ? 19.726  7.852   26.710  1.00 46.82  ? 401 VAL B CA  1 
ATOM   6346 C C   . VAL B 1 372 ? 20.671  6.648   26.808  1.00 41.93  ? 401 VAL B C   1 
ATOM   6347 O O   . VAL B 1 372 ? 20.517  5.845   27.716  1.00 42.54  ? 401 VAL B O   1 
ATOM   6348 C CB  . VAL B 1 372 ? 18.568  7.595   25.711  1.00 47.67  ? 401 VAL B CB  1 
ATOM   6349 C CG1 . VAL B 1 372 ? 18.985  7.576   24.238  1.00 42.26  ? 401 VAL B CG1 1 
ATOM   6350 C CG2 . VAL B 1 372 ? 17.812  6.308   26.035  1.00 56.01  ? 401 VAL B CG2 1 
ATOM   6351 N N   . ASP B 1 373 ? 21.663  6.573   25.914  1.00 40.49  ? 402 ASP B N   1 
ATOM   6352 C CA  . ASP B 1 373 ? 22.510  5.401   25.696  1.00 46.00  ? 402 ASP B CA  1 
ATOM   6353 C C   . ASP B 1 373 ? 23.533  5.172   26.822  1.00 48.62  ? 402 ASP B C   1 
ATOM   6354 O O   . ASP B 1 373 ? 24.155  4.115   26.877  1.00 40.03  ? 402 ASP B O   1 
ATOM   6355 C CB  . ASP B 1 373 ? 23.186  5.493   24.336  1.00 50.56  ? 402 ASP B CB  1 
ATOM   6356 C CG  . ASP B 1 373 ? 22.226  5.554   23.147  1.00 57.91  ? 402 ASP B CG  1 
ATOM   6357 O OD1 . ASP B 1 373 ? 21.276  4.725   23.119  1.00 68.26  ? 402 ASP B OD1 1 
ATOM   6358 O OD2 . ASP B 1 373 ? 22.435  6.405   22.242  1.00 56.55  ? 402 ASP B OD2 1 
ATOM   6359 N N   . ALA B 1 374 ? 23.679  6.126   27.753  1.00 41.43  ? 403 ALA B N   1 
ATOM   6360 C CA  . ALA B 1 374 ? 24.590  5.958   28.871  1.00 46.51  ? 403 ALA B CA  1 
ATOM   6361 C C   . ALA B 1 374 ? 24.014  5.017   29.934  1.00 44.98  ? 403 ALA B C   1 
ATOM   6362 O O   . ALA B 1 374 ? 24.738  4.596   30.844  1.00 44.91  ? 403 ALA B O   1 
ATOM   6363 C CB  . ALA B 1 374 ? 24.909  7.305   29.481  1.00 45.46  ? 403 ALA B CB  1 
ATOM   6364 N N   . HIS B 1 375 ? 22.711  4.718   29.856  1.00 37.49  ? 404 HIS B N   1 
ATOM   6365 C CA  . HIS B 1 375 ? 22.092  3.937   30.906  1.00 38.03  ? 404 HIS B CA  1 
ATOM   6366 C C   . HIS B 1 375 ? 21.537  2.613   30.402  1.00 35.46  ? 404 HIS B C   1 
ATOM   6367 O O   . HIS B 1 375 ? 21.248  1.753   31.215  1.00 38.72  ? 404 HIS B O   1 
ATOM   6368 C CB  . HIS B 1 375 ? 20.985  4.716   31.623  1.00 36.75  ? 404 HIS B CB  1 
ATOM   6369 C CG  . HIS B 1 375 ? 20.938  4.463   33.092  1.00 36.53  ? 404 HIS B CG  1 
ATOM   6370 N ND1 . HIS B 1 375 ? 20.839  3.192   33.604  1.00 39.96  ? 404 HIS B ND1 1 
ATOM   6371 C CD2 . HIS B 1 375 ? 20.952  5.294   34.175  1.00 35.67  ? 404 HIS B CD2 1 
ATOM   6372 C CE1 . HIS B 1 375 ? 20.779  3.268   34.946  1.00 41.33  ? 404 HIS B CE1 1 
ATOM   6373 N NE2 . HIS B 1 375 ? 20.828  4.526   35.305  1.00 33.16  ? 404 HIS B NE2 1 
ATOM   6374 N N   . SER B 1 376 ? 21.382  2.423   29.090  1.00 31.93  ? 405 SER B N   1 
ATOM   6375 C CA  . SER B 1 376 ? 20.532  1.316   28.657  1.00 33.36  ? 405 SER B CA  1 
ATOM   6376 C C   . SER B 1 376 ? 21.249  -0.036  28.781  1.00 27.35  ? 405 SER B C   1 
ATOM   6377 O O   . SER B 1 376 ? 20.660  -1.006  29.241  1.00 30.08  ? 405 SER B O   1 
ATOM   6378 C CB  . SER B 1 376 ? 19.935  1.595   27.263  1.00 31.90  ? 405 SER B CB  1 
ATOM   6379 O OG  . SER B 1 376 ? 20.968  1.804   26.304  1.00 45.89  ? 405 SER B OG  1 
ATOM   6380 N N   . GLY B 1 377 ? 22.526  -0.102  28.401  1.00 28.71  ? 406 GLY B N   1 
ATOM   6381 C CA  . GLY B 1 377 ? 23.334  -1.315  28.427  1.00 26.31  ? 406 GLY B CA  1 
ATOM   6382 C C   . GLY B 1 377 ? 23.429  -2.004  29.791  1.00 28.94  ? 406 GLY B C   1 
ATOM   6383 O O   . GLY B 1 377 ? 23.345  -3.233  29.869  1.00 29.57  ? 406 GLY B O   1 
ATOM   6384 N N   . VAL B 1 378 ? 23.680  -1.239  30.855  1.00 29.55  ? 407 VAL B N   1 
ATOM   6385 C CA  . VAL B 1 378 ? 23.801  -1.810  32.185  1.00 30.79  ? 407 VAL B CA  1 
ATOM   6386 C C   . VAL B 1 378 ? 22.495  -2.481  32.586  1.00 30.46  ? 407 VAL B C   1 
ATOM   6387 O O   . VAL B 1 378 ? 22.515  -3.578  33.138  1.00 30.75  ? 407 VAL B O   1 
ATOM   6388 C CB  . VAL B 1 378 ? 24.260  -0.755  33.198  1.00 38.10  ? 407 VAL B CB  1 
ATOM   6389 C CG1 . VAL B 1 378 ? 25.697  -0.320  32.888  1.00 38.74  ? 407 VAL B CG1 1 
ATOM   6390 C CG2 . VAL B 1 378 ? 23.346  0.470   33.218  1.00 38.82  ? 407 VAL B CG2 1 
ATOM   6391 N N   . LEU B 1 379 ? 21.355  -1.895  32.204  1.00 29.03  ? 408 LEU B N   1 
ATOM   6392 C CA  . LEU B 1 379 ? 20.082  -2.488  32.575  1.00 27.63  ? 408 LEU B CA  1 
ATOM   6393 C C   . LEU B 1 379 ? 19.861  -3.774  31.805  1.00 26.28  ? 408 LEU B C   1 
ATOM   6394 O O   . LEU B 1 379 ? 19.477  -4.787  32.386  1.00 22.57  ? 408 LEU B O   1 
ATOM   6395 C CB  . LEU B 1 379 ? 18.960  -1.466  32.390  1.00 30.16  ? 408 LEU B CB  1 
ATOM   6396 C CG  . LEU B 1 379 ? 19.116  -0.191  33.214  1.00 32.64  ? 408 LEU B CG  1 
ATOM   6397 C CD1 . LEU B 1 379 ? 17.950  0.749   33.073  1.00 34.28  ? 408 LEU B CD1 1 
ATOM   6398 C CD2 . LEU B 1 379 ? 19.279  -0.615  34.699  1.00 38.16  ? 408 LEU B CD2 1 
ATOM   6399 N N   . LEU B 1 380 ? 20.091  -3.745  30.476  1.00 25.11  ? 409 LEU B N   1 
ATOM   6400 C CA  . LEU B 1 380 ? 19.936  -4.969  29.691  1.00 25.50  ? 409 LEU B CA  1 
ATOM   6401 C C   . LEU B 1 380 ? 20.830  -6.087  30.249  1.00 24.75  ? 409 LEU B C   1 
ATOM   6402 O O   . LEU B 1 380 ? 20.394  -7.232  30.421  1.00 26.72  ? 409 LEU B O   1 
ATOM   6403 C CB  . LEU B 1 380 ? 20.229  -4.650  28.213  1.00 23.50  ? 409 LEU B CB  1 
ATOM   6404 C CG  . LEU B 1 380 ? 19.269  -3.645  27.587  1.00 23.82  ? 409 LEU B CG  1 
ATOM   6405 C CD1 . LEU B 1 380 ? 19.771  -3.224  26.215  1.00 23.93  ? 409 LEU B CD1 1 
ATOM   6406 C CD2 . LEU B 1 380 ? 17.855  -4.258  27.505  1.00 25.05  ? 409 LEU B CD2 1 
ATOM   6407 N N   . GLN B 1 381 ? 22.099  -5.763  30.490  1.00 28.33  ? 410 GLN B N   1 
ATOM   6408 C CA  . GLN B 1 381 ? 23.059  -6.759  30.955  1.00 32.04  ? 410 GLN B CA  1 
ATOM   6409 C C   . GLN B 1 381 ? 22.648  -7.344  32.327  1.00 28.47  ? 410 GLN B C   1 
ATOM   6410 O O   . GLN B 1 381 ? 22.656  -8.560  32.498  1.00 25.13  ? 410 GLN B O   1 
ATOM   6411 C CB  . GLN B 1 381 ? 24.441  -6.110  30.955  1.00 34.83  ? 410 GLN B CB  1 
ATOM   6412 C CG  . GLN B 1 381 ? 25.562  -7.082  31.294  1.00 42.84  ? 410 GLN B CG  1 
ATOM   6413 C CD  . GLN B 1 381 ? 26.873  -6.371  31.546  1.00 47.40  ? 410 GLN B CD  1 
ATOM   6414 O OE1 . GLN B 1 381 ? 27.132  -5.853  32.641  1.00 53.95  ? 410 GLN B OE1 1 
ATOM   6415 N NE2 . GLN B 1 381 ? 27.710  -6.331  30.522  1.00 44.46  ? 410 GLN B NE2 1 
ATOM   6416 N N   . TYR B 1 382 ? 22.138  -6.495  33.222  1.00 28.80  ? 411 TYR B N   1 
ATOM   6417 C CA  . TYR B 1 382 ? 21.686  -6.880  34.549  1.00 29.32  ? 411 TYR B CA  1 
ATOM   6418 C C   . TYR B 1 382 ? 20.647  -7.987  34.449  1.00 31.66  ? 411 TYR B C   1 
ATOM   6419 O O   . TYR B 1 382 ? 20.659  -8.880  35.292  1.00 31.18  ? 411 TYR B O   1 
ATOM   6420 C CB  . TYR B 1 382 ? 21.120  -5.689  35.341  1.00 28.66  ? 411 TYR B CB  1 
ATOM   6421 C CG  . TYR B 1 382 ? 20.577  -6.110  36.705  1.00 29.79  ? 411 TYR B CG  1 
ATOM   6422 C CD1 . TYR B 1 382 ? 21.437  -6.353  37.771  1.00 29.76  ? 411 TYR B CD1 1 
ATOM   6423 C CD2 . TYR B 1 382 ? 19.206  -6.278  36.932  1.00 32.70  ? 411 TYR B CD2 1 
ATOM   6424 C CE1 . TYR B 1 382 ? 20.955  -6.719  39.024  1.00 27.84  ? 411 TYR B CE1 1 
ATOM   6425 C CE2 . TYR B 1 382 ? 18.718  -6.658  38.176  1.00 32.65  ? 411 TYR B CE2 1 
ATOM   6426 C CZ  . TYR B 1 382 ? 19.599  -6.879  39.233  1.00 29.77  ? 411 TYR B CZ  1 
ATOM   6427 O OH  . TYR B 1 382 ? 19.100  -7.274  40.474  1.00 33.17  ? 411 TYR B OH  1 
ATOM   6428 N N   . TYR B 1 383 ? 19.771  -7.923  33.422  1.00 27.02  ? 412 TYR B N   1 
ATOM   6429 C CA  . TYR B 1 383 ? 18.662  -8.843  33.261  1.00 26.16  ? 412 TYR B CA  1 
ATOM   6430 C C   . TYR B 1 383 ? 19.069  -10.048 32.434  1.00 24.96  ? 412 TYR B C   1 
ATOM   6431 O O   . TYR B 1 383 ? 18.235  -10.934 32.210  1.00 27.14  ? 412 TYR B O   1 
ATOM   6432 C CB  . TYR B 1 383 ? 17.406  -8.133  32.719  1.00 24.27  ? 412 TYR B CB  1 
ATOM   6433 C CG  . TYR B 1 383 ? 16.781  -7.305  33.827  1.00 26.85  ? 412 TYR B CG  1 
ATOM   6434 C CD1 . TYR B 1 383 ? 16.144  -7.935  34.894  1.00 29.44  ? 412 TYR B CD1 1 
ATOM   6435 C CD2 . TYR B 1 383 ? 16.873  -5.925  33.858  1.00 27.54  ? 412 TYR B CD2 1 
ATOM   6436 C CE1 . TYR B 1 383 ? 15.618  -7.214  35.945  1.00 27.65  ? 412 TYR B CE1 1 
ATOM   6437 C CE2 . TYR B 1 383 ? 16.368  -5.194  34.923  1.00 28.79  ? 412 TYR B CE2 1 
ATOM   6438 C CZ  . TYR B 1 383 ? 15.726  -5.839  35.965  1.00 26.49  ? 412 TYR B CZ  1 
ATOM   6439 O OH  . TYR B 1 383 ? 15.173  -5.121  36.993  1.00 28.32  ? 412 TYR B OH  1 
ATOM   6440 N N   . GLY B 1 384 ? 20.342  -10.117 32.035  1.00 26.71  ? 413 GLY B N   1 
ATOM   6441 C CA  . GLY B 1 384 ? 20.846  -11.310 31.370  1.00 29.27  ? 413 GLY B CA  1 
ATOM   6442 C C   . GLY B 1 384 ? 20.922  -11.197 29.841  1.00 28.39  ? 413 GLY B C   1 
ATOM   6443 O O   . GLY B 1 384 ? 21.320  -12.138 29.183  1.00 33.22  ? 413 GLY B O   1 
ATOM   6444 N N   . MET B 1 385 ? 20.538  -10.041 29.300  1.00 31.02  ? 414 MET B N   1 
ATOM   6445 C CA  . MET B 1 385 ? 20.645  -9.675  27.885  1.00 30.67  ? 414 MET B CA  1 
ATOM   6446 C C   . MET B 1 385 ? 22.025  -9.078  27.652  1.00 26.36  ? 414 MET B C   1 
ATOM   6447 O O   . MET B 1 385 ? 22.197  -7.848  27.721  1.00 25.00  ? 414 MET B O   1 
ATOM   6448 C CB  . MET B 1 385 ? 19.504  -8.690  27.602  1.00 34.03  ? 414 MET B CB  1 
ATOM   6449 C CG  . MET B 1 385 ? 19.600  -7.786  26.405  1.00 44.27  ? 414 MET B CG  1 
ATOM   6450 S SD  . MET B 1 385 ? 18.783  -8.389  24.921  1.00 38.47  ? 414 MET B SD  1 
ATOM   6451 C CE  . MET B 1 385 ? 17.248  -9.306  25.136  1.00 31.65  ? 414 MET B CE  1 
ATOM   6452 N N   . THR B 1 386 ? 23.006  -9.972  27.449  1.00 27.97  ? 415 THR B N   1 
ATOM   6453 C CA  . THR B 1 386 ? 24.416  -9.606  27.383  1.00 30.55  ? 415 THR B CA  1 
ATOM   6454 C C   . THR B 1 386 ? 24.924  -9.535  25.933  1.00 32.34  ? 415 THR B C   1 
ATOM   6455 O O   . THR B 1 386 ? 26.029  -9.027  25.683  1.00 32.24  ? 415 THR B O   1 
ATOM   6456 C CB  . THR B 1 386 ? 25.271  -10.569 28.192  1.00 33.09  ? 415 THR B CB  1 
ATOM   6457 O OG1 . THR B 1 386 ? 25.091  -11.841 27.582  1.00 33.43  ? 415 THR B OG1 1 
ATOM   6458 C CG2 . THR B 1 386 ? 24.895  -10.619 29.663  1.00 32.38  ? 415 THR B CG2 1 
ATOM   6459 N N   . GLU B 1 387 ? 24.134  -9.987  24.961  1.00 26.14  ? 416 GLU B N   1 
ATOM   6460 C CA  . GLU B 1 387 ? 24.606  -10.010 23.566  1.00 26.52  ? 416 GLU B CA  1 
ATOM   6461 C C   . GLU B 1 387 ? 24.504  -8.616  22.937  1.00 25.82  ? 416 GLU B C   1 
ATOM   6462 O O   . GLU B 1 387 ? 23.447  -8.212  22.425  1.00 25.66  ? 416 GLU B O   1 
ATOM   6463 C CB  . GLU B 1 387 ? 23.783  -11.051 22.828  1.00 25.03  ? 416 GLU B CB  1 
ATOM   6464 C CG  . GLU B 1 387 ? 23.865  -12.428 23.473  1.00 28.69  ? 416 GLU B CG  1 
ATOM   6465 C CD  . GLU B 1 387 ? 22.814  -12.630 24.542  1.00 32.51  ? 416 GLU B CD  1 
ATOM   6466 O OE1 . GLU B 1 387 ? 22.745  -13.806 24.938  1.00 34.09  ? 416 GLU B OE1 1 
ATOM   6467 O OE2 . GLU B 1 387 ? 22.035  -11.683 24.917  1.00 29.35  ? 416 GLU B OE2 1 
ATOM   6468 N N   . MET B 1 388 ? 25.594  -7.847  23.039  1.00 26.65  ? 417 MET B N   1 
ATOM   6469 C CA  . MET B 1 388 ? 25.544  -6.422  22.754  1.00 27.01  ? 417 MET B CA  1 
ATOM   6470 C C   . MET B 1 388 ? 25.271  -6.162  21.266  1.00 24.76  ? 417 MET B C   1 
ATOM   6471 O O   . MET B 1 388 ? 24.729  -5.122  20.933  1.00 21.90  ? 417 MET B O   1 
ATOM   6472 C CB  . MET B 1 388 ? 26.848  -5.698  23.140  1.00 28.15  ? 417 MET B CB  1 
ATOM   6473 C CG  . MET B 1 388 ? 27.197  -5.806  24.578  1.00 31.67  ? 417 MET B CG  1 
ATOM   6474 S SD  . MET B 1 388 ? 28.678  -4.791  24.735  1.00 42.42  ? 417 MET B SD  1 
ATOM   6475 C CE  . MET B 1 388 ? 29.703  -5.808  25.806  1.00 52.42  ? 417 MET B CE  1 
ATOM   6476 N N   . ASN B 1 389 ? 25.627  -7.103  20.395  1.00 25.63  ? 418 ASN B N   1 
ATOM   6477 C CA  . ASN B 1 389 ? 25.348  -6.990  18.965  1.00 27.72  ? 418 ASN B CA  1 
ATOM   6478 C C   . ASN B 1 389 ? 23.847  -6.989  18.666  1.00 27.43  ? 418 ASN B C   1 
ATOM   6479 O O   . ASN B 1 389 ? 23.447  -6.633  17.576  1.00 30.04  ? 418 ASN B O   1 
ATOM   6480 C CB  . ASN B 1 389 ? 25.940  -8.152  18.177  1.00 34.43  ? 418 ASN B CB  1 
ATOM   6481 C CG  . ASN B 1 389 ? 27.391  -7.941  17.812  1.00 37.37  ? 418 ASN B CG  1 
ATOM   6482 O OD1 . ASN B 1 389 ? 28.020  -6.976  18.248  1.00 42.30  ? 418 ASN B OD1 1 
ATOM   6483 N ND2 . ASN B 1 389 ? 27.930  -8.827  16.994  1.00 47.19  ? 418 ASN B ND2 1 
ATOM   6484 N N   . TYR B 1 390 ? 23.020  -7.400  19.621  1.00 24.46  ? 419 TYR B N   1 
ATOM   6485 C CA  . TYR B 1 390 ? 21.569  -7.413  19.455  1.00 21.95  ? 419 TYR B CA  1 
ATOM   6486 C C   . TYR B 1 390 ? 20.891  -6.114  19.945  1.00 20.10  ? 419 TYR B C   1 
ATOM   6487 O O   . TYR B 1 390 ? 19.712  -5.876  19.688  1.00 19.11  ? 419 TYR B O   1 
ATOM   6488 C CB  . TYR B 1 390 ? 21.099  -8.606  20.278  1.00 21.92  ? 419 TYR B CB  1 
ATOM   6489 C CG  . TYR B 1 390 ? 19.610  -8.864  20.088  1.00 19.66  ? 419 TYR B CG  1 
ATOM   6490 C CD1 . TYR B 1 390 ? 19.140  -9.524  18.963  1.00 20.13  ? 419 TYR B CD1 1 
ATOM   6491 C CD2 . TYR B 1 390 ? 18.701  -8.543  21.065  1.00 20.89  ? 419 TYR B CD2 1 
ATOM   6492 C CE1 . TYR B 1 390 ? 17.800  -9.783  18.783  1.00 19.71  ? 419 TYR B CE1 1 
ATOM   6493 C CE2 . TYR B 1 390 ? 17.345  -8.775  20.893  1.00 22.20  ? 419 TYR B CE2 1 
ATOM   6494 C CZ  . TYR B 1 390 ? 16.885  -9.377  19.738  1.00 19.65  ? 419 TYR B CZ  1 
ATOM   6495 O OH  . TYR B 1 390 ? 15.560  -9.663  19.565  1.00 21.90  ? 419 TYR B OH  1 
ATOM   6496 N N   . TYR B 1 391 ? 21.603  -5.265  20.693  1.00 19.19  ? 420 TYR B N   1 
ATOM   6497 C CA  . TYR B 1 391 ? 20.969  -4.136  21.351  1.00 22.21  ? 420 TYR B CA  1 
ATOM   6498 C C   . TYR B 1 391 ? 20.262  -3.205  20.363  1.00 21.61  ? 420 TYR B C   1 
ATOM   6499 O O   . TYR B 1 391 ? 19.167  -2.746  20.631  1.00 20.56  ? 420 TYR B O   1 
ATOM   6500 C CB  . TYR B 1 391 ? 21.955  -3.340  22.204  1.00 22.99  ? 420 TYR B CB  1 
ATOM   6501 C CG  . TYR B 1 391 ? 22.454  -4.025  23.466  1.00 24.39  ? 420 TYR B CG  1 
ATOM   6502 C CD1 . TYR B 1 391 ? 21.978  -5.263  23.865  1.00 21.27  ? 420 TYR B CD1 1 
ATOM   6503 C CD2 . TYR B 1 391 ? 23.366  -3.383  24.293  1.00 22.71  ? 420 TYR B CD2 1 
ATOM   6504 C CE1 . TYR B 1 391 ? 22.432  -5.879  25.017  1.00 25.70  ? 420 TYR B CE1 1 
ATOM   6505 C CE2 . TYR B 1 391 ? 23.819  -3.974  25.463  1.00 24.43  ? 420 TYR B CE2 1 
ATOM   6506 C CZ  . TYR B 1 391 ? 23.366  -5.235  25.808  1.00 27.46  ? 420 TYR B CZ  1 
ATOM   6507 O OH  . TYR B 1 391 ? 23.761  -5.816  26.973  1.00 27.39  ? 420 TYR B OH  1 
ATOM   6508 N N   . THR B 1 392 ? 20.839  -2.996  19.187  1.00 23.30  ? 421 THR B N   1 
ATOM   6509 C CA  . THR B 1 392 ? 20.230  -2.112  18.213  1.00 22.30  ? 421 THR B CA  1 
ATOM   6510 C C   . THR B 1 392 ? 18.916  -2.711  17.675  1.00 21.73  ? 421 THR B C   1 
ATOM   6511 O O   . THR B 1 392 ? 18.051  -1.945  17.282  1.00 19.89  ? 421 THR B O   1 
ATOM   6512 C CB  . THR B 1 392 ? 21.241  -1.775  17.128  1.00 23.74  ? 421 THR B CB  1 
ATOM   6513 O OG1 . THR B 1 392 ? 22.440  -1.298  17.752  1.00 25.03  ? 421 THR B OG1 1 
ATOM   6514 C CG2 . THR B 1 392 ? 20.746  -0.652  16.234  1.00 28.88  ? 421 THR B CG2 1 
ATOM   6515 N N   . VAL B 1 393 ? 18.720  -4.044  17.732  1.00 19.23  ? 422 VAL B N   1 
ATOM   6516 C CA  . VAL B 1 393 ? 17.460  -4.665  17.317  1.00 18.91  ? 422 VAL B CA  1 
ATOM   6517 C C   . VAL B 1 393 ? 16.316  -4.200  18.230  1.00 20.09  ? 422 VAL B C   1 
ATOM   6518 O O   . VAL B 1 393 ? 15.197  -3.924  17.774  1.00 17.49  ? 422 VAL B O   1 
ATOM   6519 C CB  . VAL B 1 393 ? 17.593  -6.200  17.255  1.00 19.66  ? 422 VAL B CB  1 
ATOM   6520 C CG1 . VAL B 1 393 ? 16.283  -6.912  16.969  1.00 21.01  ? 422 VAL B CG1 1 
ATOM   6521 C CG2 . VAL B 1 393 ? 18.604  -6.598  16.186  1.00 21.60  ? 422 VAL B CG2 1 
ATOM   6522 N N   . LEU B 1 394 ? 16.619  -4.069  19.521  1.00 18.87  ? 423 LEU B N   1 
ATOM   6523 C CA  . LEU B 1 394 ? 15.645  -3.568  20.474  1.00 22.98  ? 423 LEU B CA  1 
ATOM   6524 C C   . LEU B 1 394 ? 15.270  -2.104  20.188  1.00 20.48  ? 423 LEU B C   1 
ATOM   6525 O O   . LEU B 1 394 ? 14.099  -1.731  20.239  1.00 19.72  ? 423 LEU B O   1 
ATOM   6526 C CB  . LEU B 1 394 ? 16.213  -3.697  21.885  1.00 24.94  ? 423 LEU B CB  1 
ATOM   6527 C CG  . LEU B 1 394 ? 16.397  -5.122  22.390  1.00 26.91  ? 423 LEU B CG  1 
ATOM   6528 C CD1 . LEU B 1 394 ? 17.061  -5.037  23.766  1.00 27.49  ? 423 LEU B CD1 1 
ATOM   6529 C CD2 . LEU B 1 394 ? 15.081  -5.890  22.436  1.00 25.68  ? 423 LEU B CD2 1 
ATOM   6530 N N   . PHE B 1 395 ? 16.257  -1.271  19.922  1.00 20.23  ? 424 PHE B N   1 
ATOM   6531 C CA  . PHE B 1 395 ? 16.027  0.093   19.476  1.00 22.52  ? 424 PHE B CA  1 
ATOM   6532 C C   . PHE B 1 395 ? 15.137  0.108   18.227  1.00 20.94  ? 424 PHE B C   1 
ATOM   6533 O O   . PHE B 1 395 ? 14.198  0.888   18.140  1.00 22.79  ? 424 PHE B O   1 
ATOM   6534 C CB  . PHE B 1 395 ? 17.384  0.738   19.197  1.00 26.75  ? 424 PHE B CB  1 
ATOM   6535 C CG  . PHE B 1 395 ? 17.511  2.252   19.049  1.00 27.03  ? 424 PHE B CG  1 
ATOM   6536 C CD1 . PHE B 1 395 ? 16.459  3.071   18.699  1.00 33.19  ? 424 PHE B CD1 1 
ATOM   6537 C CD2 . PHE B 1 395 ? 18.747  2.865   19.259  1.00 35.46  ? 424 PHE B CD2 1 
ATOM   6538 C CE1 . PHE B 1 395 ? 16.619  4.463   18.573  1.00 33.05  ? 424 PHE B CE1 1 
ATOM   6539 C CE2 . PHE B 1 395 ? 18.914  4.250   19.118  1.00 34.85  ? 424 PHE B CE2 1 
ATOM   6540 C CZ  . PHE B 1 395 ? 17.842  5.043   18.780  1.00 33.95  ? 424 PHE B CZ  1 
ATOM   6541 N N   . GLY B 1 396 ? 15.417  -0.764  17.264  1.00 19.11  ? 425 GLY B N   1 
ATOM   6542 C CA  . GLY B 1 396 ? 14.675  -0.844  16.021  1.00 18.12  ? 425 GLY B CA  1 
ATOM   6543 C C   . GLY B 1 396 ? 13.212  -1.246  16.218  1.00 19.55  ? 425 GLY B C   1 
ATOM   6544 O O   . GLY B 1 396 ? 12.318  -0.654  15.613  1.00 19.31  ? 425 GLY B O   1 
ATOM   6545 N N   . VAL B 1 397 ? 12.948  -2.204  17.115  1.00 18.29  ? 426 VAL B N   1 
ATOM   6546 C CA  . VAL B 1 397 ? 11.583  -2.583  17.422  1.00 19.12  ? 426 VAL B CA  1 
ATOM   6547 C C   . VAL B 1 397 ? 10.850  -1.375  18.054  1.00 21.49  ? 426 VAL B C   1 
ATOM   6548 O O   . VAL B 1 397 ? 9.710   -1.054  17.712  1.00 24.98  ? 426 VAL B O   1 
ATOM   6549 C CB  . VAL B 1 397 ? 11.558  -3.841  18.293  1.00 20.01  ? 426 VAL B CB  1 
ATOM   6550 C CG1 . VAL B 1 397 ? 10.174  -4.108  18.869  1.00 20.55  ? 426 VAL B CG1 1 
ATOM   6551 C CG2 . VAL B 1 397 ? 12.082  -5.072  17.586  1.00 21.23  ? 426 VAL B CG2 1 
ATOM   6552 N N   . SER B 1 398 ? 11.501  -0.651  18.947  1.00 20.21  ? 427 SER B N   1 
ATOM   6553 C CA  . SER B 1 398 ? 10.936  0.549   19.518  1.00 20.70  ? 427 SER B CA  1 
ATOM   6554 C C   . SER B 1 398 ? 10.589  1.597   18.455  1.00 20.17  ? 427 SER B C   1 
ATOM   6555 O O   . SER B 1 398 ? 9.465   2.098   18.409  1.00 18.94  ? 427 SER B O   1 
ATOM   6556 C CB  . SER B 1 398 ? 11.826  1.129   20.542  1.00 19.45  ? 427 SER B CB  1 
ATOM   6557 O OG  . SER B 1 398 ? 11.215  2.273   21.124  1.00 20.37  ? 427 SER B OG  1 
ATOM   6558 N N   . ARG B 1 399 ? 11.595  1.958   17.672  1.00 18.79  ? 428 ARG B N   1 
ATOM   6559 C CA  . ARG B 1 399 ? 11.495  2.982   16.635  1.00 21.09  ? 428 ARG B CA  1 
ATOM   6560 C C   . ARG B 1 399 ? 10.420  2.702   15.582  1.00 20.01  ? 428 ARG B C   1 
ATOM   6561 O O   . ARG B 1 399 ? 9.862   3.634   15.006  1.00 20.27  ? 428 ARG B O   1 
ATOM   6562 C CB  . ARG B 1 399 ? 12.881  3.181   15.987  1.00 19.88  ? 428 ARG B CB  1 
ATOM   6563 C CG  . ARG B 1 399 ? 13.020  4.425   15.118  1.00 21.18  ? 428 ARG B CG  1 
ATOM   6564 C CD  . ARG B 1 399 ? 12.436  5.667   15.734  1.00 20.04  ? 428 ARG B CD  1 
ATOM   6565 N NE  . ARG B 1 399 ? 12.999  6.044   17.038  1.00 22.83  ? 428 ARG B NE  1 
ATOM   6566 C CZ  . ARG B 1 399 ? 14.112  6.798   17.211  1.00 23.56  ? 428 ARG B CZ  1 
ATOM   6567 N NH1 . ARG B 1 399 ? 14.806  7.260   16.186  1.00 22.54  ? 428 ARG B NH1 1 
ATOM   6568 N NH2 . ARG B 1 399 ? 14.473  7.136   18.420  1.00 23.11  ? 428 ARG B NH2 1 
ATOM   6569 N N   . ALA B 1 400 ? 10.070  1.443   15.341  1.00 20.03  ? 429 ALA B N   1 
ATOM   6570 C CA  . ALA B 1 400 ? 8.909   1.134   14.517  1.00 20.75  ? 429 ALA B CA  1 
ATOM   6571 C C   . ALA B 1 400 ? 7.680   1.955   14.918  1.00 18.75  ? 429 ALA B C   1 
ATOM   6572 O O   . ALA B 1 400 ? 6.901   2.364   14.053  1.00 18.43  ? 429 ALA B O   1 
ATOM   6573 C CB  . ALA B 1 400 ? 8.568   -0.357  14.569  1.00 20.01  ? 429 ALA B CB  1 
ATOM   6574 N N   . LEU B 1 401 ? 7.462   2.113   16.219  1.00 19.54  ? 430 LEU B N   1 
ATOM   6575 C CA  . LEU B 1 401 ? 6.252   2.732   16.710  1.00 20.98  ? 430 LEU B CA  1 
ATOM   6576 C C   . LEU B 1 401 ? 6.146   4.168   16.224  1.00 21.12  ? 430 LEU B C   1 
ATOM   6577 O O   . LEU B 1 401 ? 5.118   4.551   15.654  1.00 22.64  ? 430 LEU B O   1 
ATOM   6578 C CB  . LEU B 1 401 ? 6.187   2.637   18.234  1.00 20.79  ? 430 LEU B CB  1 
ATOM   6579 C CG  . LEU B 1 401 ? 6.155   1.208   18.766  1.00 22.05  ? 430 LEU B CG  1 
ATOM   6580 C CD1 . LEU B 1 401 ? 6.152   1.300   20.268  1.00 24.05  ? 430 LEU B CD1 1 
ATOM   6581 C CD2 . LEU B 1 401 ? 5.044   0.350   18.260  1.00 27.88  ? 430 LEU B CD2 1 
ATOM   6582 N N   . GLY B 1 402 ? 7.256   4.900   16.328  1.00 18.78  ? 431 GLY B N   1 
ATOM   6583 C CA  . GLY B 1 402 ? 7.248   6.277   15.909  1.00 18.86  ? 431 GLY B CA  1 
ATOM   6584 C C   . GLY B 1 402 ? 7.194   6.414   14.390  1.00 18.10  ? 431 GLY B C   1 
ATOM   6585 O O   . GLY B 1 402 ? 6.399   7.166   13.857  1.00 18.02  ? 431 GLY B O   1 
ATOM   6586 N N   . VAL B 1 403 ? 8.080   5.729   13.675  1.00 17.76  ? 432 VAL B N   1 
ATOM   6587 C CA  . VAL B 1 403 ? 8.180   6.006   12.260  1.00 18.15  ? 432 VAL B CA  1 
ATOM   6588 C C   . VAL B 1 403 ? 6.944   5.527   11.489  1.00 18.82  ? 432 VAL B C   1 
ATOM   6589 O O   . VAL B 1 403 ? 6.591   6.097   10.454  1.00 18.73  ? 432 VAL B O   1 
ATOM   6590 C CB  . VAL B 1 403 ? 9.470   5.483   11.632  1.00 19.71  ? 432 VAL B CB  1 
ATOM   6591 C CG1 . VAL B 1 403 ? 10.671  6.085   12.350  1.00 20.73  ? 432 VAL B CG1 1 
ATOM   6592 C CG2 . VAL B 1 403 ? 9.470   3.980   11.555  1.00 19.32  ? 432 VAL B CG2 1 
ATOM   6593 N N   . LEU B 1 404 ? 6.301   4.452   11.941  1.00 18.82  ? 433 LEU B N   1 
ATOM   6594 C CA  . LEU B 1 404 ? 5.058   3.979   11.331  1.00 19.40  ? 433 LEU B CA  1 
ATOM   6595 C C   . LEU B 1 404 ? 3.844   4.837   11.703  1.00 19.80  ? 433 LEU B C   1 
ATOM   6596 O O   . LEU B 1 404 ? 2.959   5.047   10.891  1.00 19.71  ? 433 LEU B O   1 
ATOM   6597 C CB  . LEU B 1 404 ? 4.836   2.511   11.678  1.00 20.32  ? 433 LEU B CB  1 
ATOM   6598 C CG  . LEU B 1 404 ? 5.902   1.541   11.155  1.00 19.60  ? 433 LEU B CG  1 
ATOM   6599 C CD1 . LEU B 1 404 ? 5.565   0.160   11.623  1.00 21.19  ? 433 LEU B CD1 1 
ATOM   6600 C CD2 . LEU B 1 404 ? 6.038   1.610   9.582   1.00 20.01  ? 433 LEU B CD2 1 
ATOM   6601 N N   . ALA B 1 405 ? 3.763   5.338   12.927  1.00 22.96  ? 434 ALA B N   1 
ATOM   6602 C CA  . ALA B 1 405 ? 2.713   6.277   13.265  1.00 19.63  ? 434 ALA B CA  1 
ATOM   6603 C C   . ALA B 1 405 ? 2.845   7.469   12.310  1.00 22.98  ? 434 ALA B C   1 
ATOM   6604 O O   . ALA B 1 405 ? 1.849   7.911   11.781  1.00 24.64  ? 434 ALA B O   1 
ATOM   6605 C CB  . ALA B 1 405 ? 2.765   6.646   14.743  1.00 19.75  ? 434 ALA B CB  1 
ATOM   6606 N N   . GLN B 1 406 ? 4.069   7.938   12.023  1.00 19.69  ? 435 GLN B N   1 
ATOM   6607 C CA  . GLN B 1 406 ? 4.247   9.090   11.163  1.00 21.73  ? 435 GLN B CA  1 
ATOM   6608 C C   . GLN B 1 406 ? 3.925   8.703   9.720   1.00 19.96  ? 435 GLN B C   1 
ATOM   6609 O O   . GLN B 1 406 ? 3.305   9.493   9.007   1.00 19.32  ? 435 GLN B O   1 
ATOM   6610 C CB  . GLN B 1 406 ? 5.631   9.727   11.188  1.00 24.74  ? 435 GLN B CB  1 
ATOM   6611 C CG  . GLN B 1 406 ? 5.818   10.849  10.168  1.00 26.88  ? 435 GLN B CG  1 
ATOM   6612 C CD  . GLN B 1 406 ? 4.845   12.008  10.308  1.00 26.22  ? 435 GLN B CD  1 
ATOM   6613 O OE1 . GLN B 1 406 ? 4.526   12.460  11.418  1.00 24.77  ? 435 GLN B OE1 1 
ATOM   6614 N NE2 . GLN B 1 406 ? 4.368   12.508  9.176   1.00 24.02  ? 435 GLN B NE2 1 
ATOM   6615 N N   . LEU B 1 407 ? 4.345   7.499   9.290   1.00 18.52  ? 436 LEU B N   1 
ATOM   6616 C CA  . LEU B 1 407 ? 4.100   7.077   7.916   1.00 19.60  ? 436 LEU B CA  1 
ATOM   6617 C C   . LEU B 1 407 ? 2.591   7.069   7.614   1.00 19.50  ? 436 LEU B C   1 
ATOM   6618 O O   . LEU B 1 407 ? 2.178   7.491   6.542   1.00 20.43  ? 436 LEU B O   1 
ATOM   6619 C CB  . LEU B 1 407 ? 4.732   5.708   7.724   1.00 20.17  ? 436 LEU B CB  1 
ATOM   6620 C CG  . LEU B 1 407 ? 4.694   5.142   6.314   1.00 22.92  ? 436 LEU B CG  1 
ATOM   6621 C CD1 . LEU B 1 407 ? 5.543   6.037   5.410   1.00 22.27  ? 436 LEU B CD1 1 
ATOM   6622 C CD2 . LEU B 1 407 ? 5.201   3.734   6.251   1.00 24.65  ? 436 LEU B CD2 1 
ATOM   6623 N N   . ILE B 1 408 ? 1.761   6.565   8.533   1.00 18.78  ? 437 ILE B N   1 
ATOM   6624 C CA  . ILE B 1 408 ? 0.310   6.652   8.349   1.00 18.81  ? 437 ILE B CA  1 
ATOM   6625 C C   . ILE B 1 408 ? -0.141  8.091   8.074   1.00 18.26  ? 437 ILE B C   1 
ATOM   6626 O O   . ILE B 1 408 ? -0.858  8.356   7.107   1.00 19.84  ? 437 ILE B O   1 
ATOM   6627 C CB  . ILE B 1 408 ? -0.457  6.023   9.525   1.00 23.37  ? 437 ILE B CB  1 
ATOM   6628 C CG1 . ILE B 1 408 ? -0.091  4.603   9.771   1.00 22.07  ? 437 ILE B CG1 1 
ATOM   6629 C CG2 . ILE B 1 408 ? -1.975  6.131   9.304   1.00 22.31  ? 437 ILE B CG2 1 
ATOM   6630 C CD1 . ILE B 1 408 ? -0.297  4.150   11.196  1.00 21.32  ? 437 ILE B CD1 1 
ATOM   6631 N N   . TRP B 1 409 ? 0.354   9.037   8.851   1.00 20.76  ? 438 TRP B N   1 
ATOM   6632 C CA  . TRP B 1 409 ? -0.034  10.430  8.718   1.00 20.93  ? 438 TRP B CA  1 
ATOM   6633 C C   . TRP B 1 409 ? 0.530   11.065  7.456   1.00 21.90  ? 438 TRP B C   1 
ATOM   6634 O O   . TRP B 1 409 ? -0.158  11.832  6.820   1.00 20.46  ? 438 TRP B O   1 
ATOM   6635 C CB  . TRP B 1 409 ? 0.393   11.210  9.970   1.00 23.04  ? 438 TRP B CB  1 
ATOM   6636 C CG  . TRP B 1 409 ? -0.645  11.053  11.035  1.00 25.15  ? 438 TRP B CG  1 
ATOM   6637 C CD1 . TRP B 1 409 ? -0.677  10.202  12.118  1.00 23.18  ? 438 TRP B CD1 1 
ATOM   6638 C CD2 . TRP B 1 409 ? -1.916  11.733  11.006  1.00 24.97  ? 438 TRP B CD2 1 
ATOM   6639 N NE1 . TRP B 1 409 ? -1.868  10.370  12.789  1.00 24.75  ? 438 TRP B NE1 1 
ATOM   6640 C CE2 . TRP B 1 409 ? -2.646  11.280  12.123  1.00 24.75  ? 438 TRP B CE2 1 
ATOM   6641 C CE3 . TRP B 1 409 ? -2.501  12.672  10.154  1.00 26.84  ? 438 TRP B CE3 1 
ATOM   6642 C CZ2 . TRP B 1 409 ? -3.920  11.768  12.403  1.00 24.50  ? 438 TRP B CZ2 1 
ATOM   6643 C CZ3 . TRP B 1 409 ? -3.777  13.112  10.404  1.00 27.90  ? 438 TRP B CZ3 1 
ATOM   6644 C CH2 . TRP B 1 409 ? -4.459  12.681  11.540  1.00 28.72  ? 438 TRP B CH2 1 
ATOM   6645 N N   . SER B 1 410 ? 1.748   10.703  7.049   1.00 20.90  ? 439 SER B N   1 
ATOM   6646 C CA  . SER B 1 410 ? 2.323   11.293  5.841   1.00 19.33  ? 439 SER B CA  1 
ATOM   6647 C C   . SER B 1 410 ? 1.444   10.962  4.647   1.00 18.88  ? 439 SER B C   1 
ATOM   6648 O O   . SER B 1 410 ? 1.232   11.796  3.776   1.00 21.02  ? 439 SER B O   1 
ATOM   6649 C CB  . SER B 1 410 ? 3.762   10.862  5.604   1.00 17.61  ? 439 SER B CB  1 
ATOM   6650 O OG  . SER B 1 410 ? 4.592   11.231  6.678   1.00 17.51  ? 439 SER B OG  1 
ATOM   6651 N N   . ARG B 1 411 ? 0.957   9.729   4.550   1.00 21.84  ? 440 ARG B N   1 
ATOM   6652 C CA  . ARG B 1 411 ? 0.102   9.357   3.426   1.00 19.96  ? 440 ARG B CA  1 
ATOM   6653 C C   . ARG B 1 411 ? -1.303  9.934   3.598   1.00 21.49  ? 440 ARG B C   1 
ATOM   6654 O O   . ARG B 1 411 ? -1.908  10.389  2.630   1.00 22.13  ? 440 ARG B O   1 
ATOM   6655 C CB  . ARG B 1 411 ? 0.044   7.850   3.310   1.00 19.70  ? 440 ARG B CB  1 
ATOM   6656 C CG  . ARG B 1 411 ? 1.413   7.210   3.174   1.00 22.04  ? 440 ARG B CG  1 
ATOM   6657 C CD  . ARG B 1 411 ? 1.936   7.358   1.744   1.00 22.30  ? 440 ARG B CD  1 
ATOM   6658 N NE  . ARG B 1 411 ? 2.534   8.681   1.558   1.00 25.09  ? 440 ARG B NE  1 
ATOM   6659 C CZ  . ARG B 1 411 ? 3.668   9.071   2.085   1.00 23.33  ? 440 ARG B CZ  1 
ATOM   6660 N NH1 . ARG B 1 411 ? 4.338   8.270   2.880   1.00 26.00  ? 440 ARG B NH1 1 
ATOM   6661 N NH2 . ARG B 1 411 ? 4.118   10.266  1.824   1.00 21.12  ? 440 ARG B NH2 1 
ATOM   6662 N N   . ALA B 1 412 ? -1.821  9.917   4.834   1.00 20.98  ? 441 ALA B N   1 
ATOM   6663 C CA  . ALA B 1 412 ? -3.106  10.559  5.106   1.00 22.77  ? 441 ALA B CA  1 
ATOM   6664 C C   . ALA B 1 412 ? -3.110  12.019  4.659   1.00 22.07  ? 441 ALA B C   1 
ATOM   6665 O O   . ALA B 1 412 ? -4.149  12.514  4.216   1.00 24.46  ? 441 ALA B O   1 
ATOM   6666 C CB  . ALA B 1 412 ? -3.473  10.506  6.596   1.00 20.94  ? 441 ALA B CB  1 
ATOM   6667 N N   . LEU B 1 413 ? -1.992  12.710  4.868   1.00 20.04  ? 442 LEU B N   1 
ATOM   6668 C CA  . LEU B 1 413 ? -1.876  14.120  4.583   1.00 22.41  ? 442 LEU B CA  1 
ATOM   6669 C C   . LEU B 1 413 ? -1.386  14.371  3.162   1.00 22.30  ? 442 LEU B C   1 
ATOM   6670 O O   . LEU B 1 413 ? -1.285  15.524  2.763   1.00 24.98  ? 442 LEU B O   1 
ATOM   6671 C CB  . LEU B 1 413 ? -0.962  14.762  5.609   1.00 23.91  ? 442 LEU B CB  1 
ATOM   6672 C CG  . LEU B 1 413 ? -1.451  14.722  7.061   1.00 22.14  ? 442 LEU B CG  1 
ATOM   6673 C CD1 . LEU B 1 413 ? -0.409  15.267  8.023   1.00 24.28  ? 442 LEU B CD1 1 
ATOM   6674 C CD2 . LEU B 1 413 ? -2.761  15.477  7.171   1.00 21.93  ? 442 LEU B CD2 1 
ATOM   6675 N N   . GLY B 1 414 ? -1.094  13.306  2.422   1.00 20.89  ? 443 GLY B N   1 
ATOM   6676 C CA  . GLY B 1 414 ? -0.759  13.415  1.012   1.00 21.77  ? 443 GLY B CA  1 
ATOM   6677 C C   . GLY B 1 414 ? 0.629   14.019  0.805   1.00 22.17  ? 443 GLY B C   1 
ATOM   6678 O O   . GLY B 1 414 ? 0.911   14.549  -0.268  1.00 24.52  ? 443 GLY B O   1 
ATOM   6679 N N   . PHE B 1 415 ? 1.549   13.812  1.752   1.00 20.74  ? 444 PHE B N   1 
ATOM   6680 C CA  . PHE B 1 415 ? 2.909   14.310  1.568   1.00 20.18  ? 444 PHE B CA  1 
ATOM   6681 C C   . PHE B 1 415 ? 3.489   13.752  0.280   1.00 19.61  ? 444 PHE B C   1 
ATOM   6682 O O   . PHE B 1 415 ? 3.394   12.543  0.041   1.00 21.29  ? 444 PHE B O   1 
ATOM   6683 C CB  . PHE B 1 415 ? 3.893   13.989  2.682   1.00 20.49  ? 444 PHE B CB  1 
ATOM   6684 C CG  . PHE B 1 415 ? 3.623   14.715  3.994   1.00 21.96  ? 444 PHE B CG  1 
ATOM   6685 C CD1 . PHE B 1 415 ? 2.649   15.694  4.085   1.00 24.03  ? 444 PHE B CD1 1 
ATOM   6686 C CD2 . PHE B 1 415 ? 4.352   14.421  5.132   1.00 23.01  ? 444 PHE B CD2 1 
ATOM   6687 C CE1 . PHE B 1 415 ? 2.442   16.361  5.283   1.00 25.24  ? 444 PHE B CE1 1 
ATOM   6688 C CE2 . PHE B 1 415 ? 4.130   15.096  6.319   1.00 21.88  ? 444 PHE B CE2 1 
ATOM   6689 C CZ  . PHE B 1 415 ? 3.175   16.048  6.388   1.00 22.94  ? 444 PHE B CZ  1 
ATOM   6690 N N   . PRO B 1 416 ? 4.123   14.593  -0.565  1.00 19.65  ? 445 PRO B N   1 
ATOM   6691 C CA  . PRO B 1 416 ? 4.672   14.142  -1.842  1.00 21.36  ? 445 PRO B CA  1 
ATOM   6692 C C   . PRO B 1 416 ? 6.065   13.509  -1.711  1.00 19.23  ? 445 PRO B C   1 
ATOM   6693 O O   . PRO B 1 416 ? 6.641   13.463  -0.637  1.00 17.67  ? 445 PRO B O   1 
ATOM   6694 C CB  . PRO B 1 416 ? 4.740   15.430  -2.651  1.00 21.79  ? 445 PRO B CB  1 
ATOM   6695 C CG  . PRO B 1 416 ? 5.164   16.438  -1.593  1.00 23.58  ? 445 PRO B CG  1 
ATOM   6696 C CD  . PRO B 1 416 ? 4.435   16.002  -0.304  1.00 21.16  ? 445 PRO B CD  1 
ATOM   6697 N N   . LEU B 1 417 ? 6.555   13.021  -2.849  1.00 18.37  ? 446 LEU B N   1 
ATOM   6698 C CA  . LEU B 1 417 ? 7.921   12.528  -2.973  1.00 19.49  ? 446 LEU B CA  1 
ATOM   6699 C C   . LEU B 1 417 ? 8.931   13.547  -2.458  1.00 21.40  ? 446 LEU B C   1 
ATOM   6700 O O   . LEU B 1 417 ? 8.879   14.726  -2.819  1.00 19.52  ? 446 LEU B O   1 
ATOM   6701 C CB  . LEU B 1 417 ? 8.130   12.243  -4.448  1.00 21.91  ? 446 LEU B CB  1 
ATOM   6702 C CG  . LEU B 1 417 ? 9.441   11.569  -4.852  1.00 23.31  ? 446 LEU B CG  1 
ATOM   6703 C CD1 . LEU B 1 417 ? 9.469   10.077  -4.548  1.00 24.62  ? 446 LEU B CD1 1 
ATOM   6704 C CD2 . LEU B 1 417 ? 9.660   11.742  -6.350  1.00 27.40  ? 446 LEU B CD2 1 
ATOM   6705 N N   . GLU B 1 418 ? 9.854   13.070  -1.616  1.00 20.43  ? 447 GLU B N   1 
ATOM   6706 C CA  . GLU B 1 418 ? 10.943  13.897  -1.138  1.00 21.31  ? 447 GLU B CA  1 
ATOM   6707 C C   . GLU B 1 418 ? 11.989  13.878  -2.240  1.00 21.14  ? 447 GLU B C   1 
ATOM   6708 O O   . GLU B 1 418 ? 12.422  12.812  -2.658  1.00 21.44  ? 447 GLU B O   1 
ATOM   6709 C CB  . GLU B 1 418 ? 11.459  13.366  0.196   1.00 20.13  ? 447 GLU B CB  1 
ATOM   6710 C CG  . GLU B 1 418 ? 12.683  14.148  0.676   1.00 21.69  ? 447 GLU B CG  1 
ATOM   6711 C CD  . GLU B 1 418 ? 13.121  13.810  2.089   1.00 26.95  ? 447 GLU B CD  1 
ATOM   6712 O OE1 . GLU B 1 418 ? 14.356  13.786  2.339   1.00 25.68  ? 447 GLU B OE1 1 
ATOM   6713 O OE2 . GLU B 1 418 ? 12.253  13.589  2.958   1.00 26.82  ? 447 GLU B OE2 1 
ATOM   6714 N N   . ARG B 1 419 ? 12.382  15.057  -2.711  1.00 21.92  ? 448 ARG B N   1 
ATOM   6715 C CA  . ARG B 1 419 ? 13.256  15.187  -3.864  1.00 26.59  ? 448 ARG B CA  1 
ATOM   6716 C C   . ARG B 1 419 ? 13.870  16.576  -3.759  1.00 25.50  ? 448 ARG B C   1 
ATOM   6717 O O   . ARG B 1 419 ? 13.464  17.492  -4.461  1.00 29.21  ? 448 ARG B O   1 
ATOM   6718 C CB  . ARG B 1 419 ? 12.480  15.084  -5.187  1.00 30.94  ? 448 ARG B CB  1 
ATOM   6719 C CG  . ARG B 1 419 ? 13.177  14.563  -6.447  1.00 40.12  ? 448 ARG B CG  1 
ATOM   6720 C CD  . ARG B 1 419 ? 14.472  15.210  -6.958  1.00 43.55  ? 448 ARG B CD  1 
ATOM   6721 N NE  . ARG B 1 419 ? 15.120  14.511  -8.095  1.00 41.18  ? 448 ARG B NE  1 
ATOM   6722 C CZ  . ARG B 1 419 ? 16.361  14.757  -8.550  1.00 46.20  ? 448 ARG B CZ  1 
ATOM   6723 N NH1 . ARG B 1 419 ? 16.881  14.033  -9.547  1.00 42.82  ? 448 ARG B NH1 1 
ATOM   6724 N NH2 . ARG B 1 419 ? 17.102  15.702  -7.962  1.00 50.25  ? 448 ARG B NH2 1 
ATOM   6725 N N   . PRO B 1 420 ? 14.865  16.773  -2.884  1.00 25.66  ? 449 PRO B N   1 
ATOM   6726 C CA  . PRO B 1 420 ? 15.651  18.011  -2.861  1.00 22.91  ? 449 PRO B CA  1 
ATOM   6727 C C   . PRO B 1 420 ? 16.511  18.090  -4.135  1.00 24.75  ? 449 PRO B C   1 
ATOM   6728 O O   . PRO B 1 420 ? 16.562  17.157  -4.906  1.00 24.60  ? 449 PRO B O   1 
ATOM   6729 C CB  . PRO B 1 420 ? 16.484  17.887  -1.591  1.00 22.00  ? 449 PRO B CB  1 
ATOM   6730 C CG  . PRO B 1 420 ? 16.666  16.400  -1.464  1.00 25.38  ? 449 PRO B CG  1 
ATOM   6731 C CD  . PRO B 1 420 ? 15.394  15.737  -1.977  1.00 26.02  ? 449 PRO B CD  1 
ATOM   6732 N N   . LYS B 1 421 ? 17.152  19.233  -4.371  1.00 23.18  ? 450 LYS B N   1 
ATOM   6733 C CA  . LYS B 1 421 ? 18.053  19.439  -5.495  1.00 25.37  ? 450 LYS B CA  1 
ATOM   6734 C C   . LYS B 1 421 ? 19.473  19.276  -4.955  1.00 22.53  ? 450 LYS B C   1 
ATOM   6735 O O   . LYS B 1 421 ? 19.800  19.742  -3.885  1.00 27.64  ? 450 LYS B O   1 
ATOM   6736 C CB  . LYS B 1 421 ? 17.854  20.869  -6.038  1.00 31.33  ? 450 LYS B CB  1 
ATOM   6737 C CG  . LYS B 1 421 ? 18.742  21.297  -7.194  1.00 31.38  ? 450 LYS B CG  1 
ATOM   6738 C CD  . LYS B 1 421 ? 18.398  20.528  -8.463  1.00 36.91  ? 450 LYS B CD  1 
ATOM   6739 C CE  . LYS B 1 421 ? 19.339  20.819  -9.614  1.00 40.29  ? 450 LYS B CE  1 
ATOM   6740 N NZ  . LYS B 1 421 ? 19.004  19.885  -10.692 1.00 42.03  ? 450 LYS B NZ  1 
ATOM   6741 N N   . SER B 1 422 ? 20.297  18.515  -5.641  1.00 21.84  ? 451 SER B N   1 
ATOM   6742 C CA  . SER B 1 422 ? 21.710  18.436  -5.345  1.00 19.82  ? 451 SER B CA  1 
ATOM   6743 C C   . SER B 1 422 ? 22.469  19.343  -6.285  1.00 20.86  ? 451 SER B C   1 
ATOM   6744 O O   . SER B 1 422 ? 21.973  19.709  -7.356  1.00 19.96  ? 451 SER B O   1 
ATOM   6745 C CB  . SER B 1 422 ? 22.226  17.034  -5.493  1.00 21.53  ? 451 SER B CB  1 
ATOM   6746 O OG  . SER B 1 422 ? 22.219  16.607  -6.846  1.00 20.87  ? 451 SER B OG  1 
ATOM   6747 N N   . MET B 1 423 ? 23.706  19.629  -5.887  1.00 21.78  ? 452 MET B N   1 
ATOM   6748 C CA  . MET B 1 423 ? 24.642  20.363  -6.723  1.00 22.41  ? 452 MET B CA  1 
ATOM   6749 C C   . MET B 1 423 ? 26.004  19.739  -6.540  1.00 20.18  ? 452 MET B C   1 
ATOM   6750 O O   . MET B 1 423 ? 26.278  19.216  -5.462  1.00 22.34  ? 452 MET B O   1 
ATOM   6751 C CB  . MET B 1 423 ? 24.846  21.792  -6.231  1.00 25.88  ? 452 MET B CB  1 
ATOM   6752 C CG  . MET B 1 423 ? 23.574  22.601  -6.141  1.00 34.70  ? 452 MET B CG  1 
ATOM   6753 S SD  . MET B 1 423 ? 23.023  23.050  -7.793  1.00 48.35  ? 452 MET B SD  1 
ATOM   6754 C CE  . MET B 1 423 ? 24.087  24.502  -7.886  1.00 49.76  ? 452 MET B CE  1 
ATOM   6755 N N   . SER B 1 424 ? 26.881  19.876  -7.524  1.00 19.78  ? 453 SER B N   1 
ATOM   6756 C CA  . SER B 1 424 ? 28.267  19.499  -7.335  1.00 22.74  ? 453 SER B CA  1 
ATOM   6757 C C   . SER B 1 424 ? 29.087  20.693  -6.840  1.00 23.18  ? 453 SER B C   1 
ATOM   6758 O O   . SER B 1 424 ? 28.635  21.848  -6.873  1.00 25.89  ? 453 SER B O   1 
ATOM   6759 C CB  . SER B 1 424 ? 28.849  18.935  -8.606  1.00 27.60  ? 453 SER B CB  1 
ATOM   6760 O OG  . SER B 1 424 ? 28.964  19.956  -9.584  1.00 23.53  ? 453 SER B OG  1 
ATOM   6761 N N   . THR B 1 425 ? 30.286  20.378  -6.342  1.00 24.60  ? 454 THR B N   1 
ATOM   6762 C CA  . THR B 1 425 ? 31.228  21.397  -5.926  1.00 29.23  ? 454 THR B CA  1 
ATOM   6763 C C   . THR B 1 425 ? 31.462  22.369  -7.093  1.00 30.45  ? 454 THR B C   1 
ATOM   6764 O O   . THR B 1 425 ? 31.369  23.576  -6.906  1.00 31.56  ? 454 THR B O   1 
ATOM   6765 C CB  . THR B 1 425 ? 32.524  20.764  -5.439  1.00 27.93  ? 454 THR B CB  1 
ATOM   6766 O OG1 . THR B 1 425 ? 32.292  20.076  -4.199  1.00 25.12  ? 454 THR B OG1 1 
ATOM   6767 C CG2 . THR B 1 425 ? 33.569  21.854  -5.242  1.00 28.23  ? 454 THR B CG2 1 
ATOM   6768 N N   . GLU B 1 426 ? 31.768  21.823  -8.282  1.00 29.94  ? 455 GLU B N   1 
ATOM   6769 C CA  . GLU B 1 426 ? 31.908  22.631  -9.493  1.00 35.51  ? 455 GLU B CA  1 
ATOM   6770 C C   . GLU B 1 426 ? 30.664  23.507  -9.666  1.00 36.48  ? 455 GLU B C   1 
ATOM   6771 O O   . GLU B 1 426 ? 30.764  24.727  -9.796  1.00 38.15  ? 455 GLU B O   1 
ATOM   6772 C CB  . GLU B 1 426 ? 32.165  21.654  -10.645 1.00 42.83  ? 455 GLU B CB  1 
ATOM   6773 C CG  . GLU B 1 426 ? 32.298  22.254  -12.046 1.00 56.53  ? 455 GLU B CG  1 
ATOM   6774 C CD  . GLU B 1 426 ? 32.555  21.226  -13.166 1.00 76.83  ? 455 GLU B CD  1 
ATOM   6775 O OE1 . GLU B 1 426 ? 33.194  21.634  -14.169 1.00 87.22  ? 455 GLU B OE1 1 
ATOM   6776 O OE2 . GLU B 1 426 ? 32.120  20.041  -13.100 1.00 70.84  ? 455 GLU B OE2 1 
ATOM   6777 N N   . GLY B 1 427 ? 29.487  22.866  -9.685  1.00 31.25  ? 456 GLY B N   1 
ATOM   6778 C CA  . GLY B 1 427 ? 28.227  23.556  -9.867  1.00 30.56  ? 456 GLY B CA  1 
ATOM   6779 C C   . GLY B 1 427 ? 28.014  24.696  -8.889  1.00 31.97  ? 456 GLY B C   1 
ATOM   6780 O O   . GLY B 1 427 ? 27.565  25.757  -9.291  1.00 36.50  ? 456 GLY B O   1 
ATOM   6781 N N   . LEU B 1 428 ? 28.304  24.445  -7.607  1.00 28.95  ? 457 LEU B N   1 
ATOM   6782 C CA  . LEU B 1 428 ? 28.145  25.408  -6.541  1.00 31.21  ? 457 LEU B CA  1 
ATOM   6783 C C   . LEU B 1 428 ? 29.093  26.588  -6.656  1.00 36.30  ? 457 LEU B C   1 
ATOM   6784 O O   . LEU B 1 428 ? 28.677  27.679  -6.280  1.00 35.82  ? 457 LEU B O   1 
ATOM   6785 C CB  . LEU B 1 428 ? 28.370  24.777  -5.168  1.00 28.85  ? 457 LEU B CB  1 
ATOM   6786 C CG  . LEU B 1 428 ? 27.136  24.510  -4.316  1.00 30.68  ? 457 LEU B CG  1 
ATOM   6787 C CD1 . LEU B 1 428 ? 27.620  23.977  -2.959  1.00 29.51  ? 457 LEU B CD1 1 
ATOM   6788 C CD2 . LEU B 1 428 ? 26.197  25.644  -4.105  1.00 28.33  ? 457 LEU B CD2 1 
ATOM   6789 N N   . MET B 1 429 ? 30.369  26.319  -6.990  1.00 34.27  ? 458 MET B N   1 
ATOM   6790 C CA  . MET B 1 429 ? 31.375  27.359  -7.170  1.00 36.60  ? 458 MET B CA  1 
ATOM   6791 C C   . MET B 1 429 ? 30.924  28.315  -8.274  1.00 39.21  ? 458 MET B C   1 
ATOM   6792 O O   . MET B 1 429 ? 31.028  29.538  -8.121  1.00 42.88  ? 458 MET B O   1 
ATOM   6793 C CB  . MET B 1 429 ? 32.744  26.777  -7.556  1.00 36.93  ? 458 MET B CB  1 
ATOM   6794 C CG  . MET B 1 429 ? 33.501  26.087  -6.447  1.00 42.18  ? 458 MET B CG  1 
ATOM   6795 S SD  . MET B 1 429 ? 34.948  25.169  -7.045  1.00 48.69  ? 458 MET B SD  1 
ATOM   6796 C CE  . MET B 1 429 ? 35.462  24.773  -5.369  1.00 56.25  ? 458 MET B CE  1 
ATOM   6797 N N   . LYS B 1 430 ? 30.370  27.758  -9.355  1.00 39.83  ? 459 LYS B N   1 
ATOM   6798 C CA  . LYS B 1 430 ? 29.782  28.569  -10.415 1.00 42.83  ? 459 LYS B CA  1 
ATOM   6799 C C   . LYS B 1 430 ? 28.569  29.350  -9.912  1.00 46.84  ? 459 LYS B C   1 
ATOM   6800 O O   . LYS B 1 430 ? 28.438  30.527  -10.204 1.00 44.53  ? 459 LYS B O   1 
ATOM   6801 C CB  . LYS B 1 430 ? 29.368  27.772  -11.658 1.00 46.03  ? 459 LYS B CB  1 
ATOM   6802 C CG  . LYS B 1 430 ? 30.513  27.237  -12.481 1.00 51.88  ? 459 LYS B CG  1 
ATOM   6803 C CD  . LYS B 1 430 ? 30.177  27.004  -13.954 1.00 65.11  ? 459 LYS B CD  1 
ATOM   6804 C CE  . LYS B 1 430 ? 29.357  25.782  -14.282 1.00 69.74  ? 459 LYS B CE  1 
ATOM   6805 N NZ  . LYS B 1 430 ? 30.118  24.538  -14.114 1.00 74.78  ? 459 LYS B NZ  1 
ATOM   6806 N N   . PHE B 1 431 ? 27.667  28.687  -9.187  1.00 50.80  ? 460 PHE B N   1 
ATOM   6807 C CA  . PHE B 1 431 ? 26.449  29.299  -8.689  1.00 48.78  ? 460 PHE B CA  1 
ATOM   6808 C C   . PHE B 1 431 ? 26.772  30.503  -7.813  1.00 50.39  ? 460 PHE B C   1 
ATOM   6809 O O   . PHE B 1 431 ? 26.107  31.513  -7.977  1.00 58.47  ? 460 PHE B O   1 
ATOM   6810 C CB  . PHE B 1 431 ? 25.588  28.268  -7.954  1.00 53.59  ? 460 PHE B CB  1 
ATOM   6811 C CG  . PHE B 1 431 ? 24.214  28.782  -7.552  1.00 52.07  ? 460 PHE B CG  1 
ATOM   6812 C CD1 . PHE B 1 431 ? 23.137  28.682  -8.426  1.00 54.53  ? 460 PHE B CD1 1 
ATOM   6813 C CD2 . PHE B 1 431 ? 24.019  29.418  -6.329  1.00 55.65  ? 460 PHE B CD2 1 
ATOM   6814 C CE1 . PHE B 1 431 ? 21.891  29.183  -8.074  1.00 57.80  ? 460 PHE B CE1 1 
ATOM   6815 C CE2 . PHE B 1 431 ? 22.766  29.908  -5.976  1.00 58.16  ? 460 PHE B CE2 1 
ATOM   6816 C CZ  . PHE B 1 431 ? 21.708  29.800  -6.853  1.00 54.95  ? 460 PHE B CZ  1 
ATOM   6817 N N   . VAL B 1 432 ? 27.774  30.407  -6.917  1.00 52.12  ? 461 VAL B N   1 
ATOM   6818 C CA  . VAL B 1 432 ? 28.103  31.489  -5.990  1.00 58.79  ? 461 VAL B CA  1 
ATOM   6819 C C   . VAL B 1 432 ? 28.745  32.672  -6.718  1.00 62.19  ? 461 VAL B C   1 
ATOM   6820 O O   . VAL B 1 432 ? 28.643  33.789  -6.217  1.00 56.99  ? 461 VAL B O   1 
ATOM   6821 C CB  . VAL B 1 432 ? 28.983  31.157  -4.765  1.00 55.49  ? 461 VAL B CB  1 
ATOM   6822 C CG1 . VAL B 1 432 ? 28.392  30.023  -3.934  1.00 57.08  ? 461 VAL B CG1 1 
ATOM   6823 C CG2 . VAL B 1 432 ? 30.434  30.881  -5.134  1.00 62.67  ? 461 VAL B CG2 1 
ATOM   6824 N N   . ASP B 1 433 ? 29.464  32.428  -7.826  1.00 62.89  ? 462 ASP B N   1 
ATOM   6825 C CA  . ASP B 1 433 ? 30.034  33.502  -8.639  1.00 69.73  ? 462 ASP B CA  1 
ATOM   6826 C C   . ASP B 1 433 ? 28.936  34.245  -9.404  1.00 66.99  ? 462 ASP B C   1 
ATOM   6827 O O   . ASP B 1 433 ? 28.915  35.471  -9.423  1.00 66.62  ? 462 ASP B O   1 
ATOM   6828 C CB  . ASP B 1 433 ? 31.125  33.009  -9.580  1.00 64.97  ? 462 ASP B CB  1 
ATOM   6829 C CG  . ASP B 1 433 ? 32.449  32.671  -8.912  1.00 71.97  ? 462 ASP B CG  1 
ATOM   6830 O OD1 . ASP B 1 433 ? 32.476  32.629  -7.653  1.00 81.92  ? 462 ASP B OD1 1 
ATOM   6831 O OD2 . ASP B 1 433 ? 33.444  32.470  -9.648  1.00 62.57  ? 462 ASP B OD2 1 
ATOM   6832 N N   . SER B 1 434 ? 28.029  33.499  -10.043 1.00 69.72  ? 463 SER B N   1 
ATOM   6833 C CA  . SER B 1 434 ? 26.794  34.075  -10.550 1.00 68.18  ? 463 SER B CA  1 
ATOM   6834 C C   . SER B 1 434 ? 25.860  34.347  -9.358  1.00 67.53  ? 463 SER B C   1 
ATOM   6835 O O   . SER B 1 434 ? 24.941  35.173  -9.515  1.00 68.35  ? 463 SER B O   1 
ATOM   6836 C CB  . SER B 1 434 ? 26.140  33.184  -11.583 1.00 67.58  ? 463 SER B CB  1 
ATOM   6837 O OG  . SER B 1 434 ? 25.316  32.194  -10.982 1.00 72.45  ? 463 SER B OG  1 
HETATM 6838 C C1  . CIT C 2 .   ? 14.552  11.293  -10.479 1.00 47.88  ? 501 CIT A C1  1 
HETATM 6839 O O1  . CIT C 2 .   ? 15.563  11.701  -11.153 1.00 52.25  ? 501 CIT A O1  1 
HETATM 6840 O O2  . CIT C 2 .   ? 14.000  11.967  -9.555  1.00 44.38  ? 501 CIT A O2  1 
HETATM 6841 C C2  . CIT C 2 .   ? 13.966  9.913   -10.746 1.00 40.92  ? 501 CIT A C2  1 
HETATM 6842 C C3  . CIT C 2 .   ? 14.520  9.129   -11.948 1.00 48.83  ? 501 CIT A C3  1 
HETATM 6843 O O7  . CIT C 2 .   ? 14.412  9.896   -13.145 1.00 49.68  ? 501 CIT A O7  1 
HETATM 6844 C C4  . CIT C 2 .   ? 13.672  7.866   -12.086 1.00 51.49  ? 501 CIT A C4  1 
HETATM 6845 C C5  . CIT C 2 .   ? 12.818  7.817   -13.334 1.00 57.39  ? 501 CIT A C5  1 
HETATM 6846 O O3  . CIT C 2 .   ? 12.238  6.733   -13.572 1.00 59.77  ? 501 CIT A O3  1 
HETATM 6847 O O4  . CIT C 2 .   ? 12.735  8.864   -14.051 1.00 59.43  ? 501 CIT A O4  1 
HETATM 6848 C C6  . CIT C 2 .   ? 16.006  8.707   -11.738 1.00 42.48  ? 501 CIT A C6  1 
HETATM 6849 O O5  . CIT C 2 .   ? 16.664  8.454   -12.750 1.00 37.47  ? 501 CIT A O5  1 
HETATM 6850 O O6  . CIT C 2 .   ? 16.435  8.616   -10.589 1.00 34.60  ? 501 CIT A O6  1 
HETATM 6851 N N1A . COA D 3 .   ? 0.160   13.652  -18.283 1.00 94.73  ? 502 COA A N1A 1 
HETATM 6852 C C2A . COA D 3 .   ? -0.792  14.336  -17.632 1.00 90.67  ? 502 COA A C2A 1 
HETATM 6853 N N3A . COA D 3 .   ? -0.661  15.271  -16.693 1.00 96.01  ? 502 COA A N3A 1 
HETATM 6854 C C4A . COA D 3 .   ? 0.637   15.496  -16.419 1.00 97.45  ? 502 COA A C4A 1 
HETATM 6855 C C5A . COA D 3 .   ? 1.724   14.875  -16.999 1.00 93.48  ? 502 COA A C5A 1 
HETATM 6856 C C6A . COA D 3 .   ? 1.461   13.898  -17.980 1.00 92.16  ? 502 COA A C6A 1 
HETATM 6857 N N6A . COA D 3 .   ? 2.410   13.222  -18.621 1.00 90.08  ? 502 COA A N6A 1 
HETATM 6858 N N7A . COA D 3 .   ? 2.904   15.372  -16.461 1.00 92.36  ? 502 COA A N7A 1 
HETATM 6859 C C8A . COA D 3 .   ? 2.519   16.263  -15.577 1.00 92.08  ? 502 COA A C8A 1 
HETATM 6860 N N9A . COA D 3 .   ? 1.150   16.388  -15.512 1.00 94.67  ? 502 COA A N9A 1 
HETATM 6861 C C1B . COA D 3 .   ? 0.373   17.255  -14.619 1.00 94.14  ? 502 COA A C1B 1 
HETATM 6862 C C2B . COA D 3 .   ? 0.714   17.102  -13.139 1.00 97.11  ? 502 COA A C2B 1 
HETATM 6863 O O2B . COA D 3 .   ? 0.174   15.940  -12.551 1.00 91.51  ? 502 COA A O2B 1 
HETATM 6864 C C3B . COA D 3 .   ? 0.090   18.391  -12.604 1.00 102.01 ? 502 COA A C3B 1 
HETATM 6865 O O3B . COA D 3 .   ? -1.328  18.258  -12.514 1.00 111.20 ? 502 COA A O3B 1 
HETATM 6866 P P3B . COA D 3 .   ? -2.066  19.188  -11.412 1.00 118.74 ? 502 COA A P3B 1 
HETATM 6867 O O7A . COA D 3 .   ? -2.122  18.386  -10.109 1.00 94.36  ? 502 COA A O7A 1 
HETATM 6868 O O8A . COA D 3 .   ? -3.439  19.411  -12.023 1.00 111.04 ? 502 COA A O8A 1 
HETATM 6869 O O9A . COA D 3 .   ? -1.298  20.489  -11.259 1.00 112.60 ? 502 COA A O9A 1 
HETATM 6870 C C4B . COA D 3 .   ? 0.475   19.394  -13.696 1.00 100.41 ? 502 COA A C4B 1 
HETATM 6871 O O4B . COA D 3 .   ? 0.657   18.604  -14.902 1.00 93.51  ? 502 COA A O4B 1 
HETATM 6872 C C5B . COA D 3 .   ? 1.723   20.203  -13.431 1.00 94.06  ? 502 COA A C5B 1 
HETATM 6873 O O5B . COA D 3 .   ? 2.509   19.567  -12.386 1.00 88.36  ? 502 COA A O5B 1 
HETATM 6874 P P1A . COA D 3 .   ? 4.042   19.133  -12.612 1.00 82.46  ? 502 COA A P1A 1 
HETATM 6875 O O1A . COA D 3 .   ? 4.939   20.281  -12.291 1.00 71.44  ? 502 COA A O1A 1 
HETATM 6876 O O2A . COA D 3 .   ? 4.186   18.484  -13.948 1.00 75.18  ? 502 COA A O2A 1 
HETATM 6877 O O3A . COA D 3 .   ? 4.133   18.046  -11.432 1.00 88.66  ? 502 COA A O3A 1 
HETATM 6878 P P2A . COA D 3 .   ? 5.203   17.144  -10.645 1.00 81.68  ? 502 COA A P2A 1 
HETATM 6879 O O4A . COA D 3 .   ? 6.586   17.705  -10.807 1.00 75.53  ? 502 COA A O4A 1 
HETATM 6880 O O5A . COA D 3 .   ? 4.682   16.927  -9.254  1.00 73.61  ? 502 COA A O5A 1 
HETATM 6881 O O6A . COA D 3 .   ? 5.034   15.777  -11.487 1.00 75.84  ? 502 COA A O6A 1 
HETATM 6882 C CBP . COA D 3 .   ? 5.782   13.712  -12.597 1.00 63.46  ? 502 COA A CBP 1 
HETATM 6883 C CCP . COA D 3 .   ? 6.195   15.093  -12.070 1.00 70.45  ? 502 COA A CCP 1 
HETATM 6884 C CDP . COA D 3 .   ? 7.010   13.053  -13.235 1.00 59.19  ? 502 COA A CDP 1 
HETATM 6885 C CEP . COA D 3 .   ? 5.321   12.837  -11.420 1.00 63.85  ? 502 COA A CEP 1 
HETATM 6886 C CAP . COA D 3 .   ? 4.646   13.837  -13.632 1.00 62.22  ? 502 COA A CAP 1 
HETATM 6887 O OAP . COA D 3 .   ? 5.094   14.559  -14.791 1.00 53.69  ? 502 COA A OAP 1 
HETATM 6888 C C9P . COA D 3 .   ? 4.017   12.508  -14.051 1.00 63.90  ? 502 COA A C9P 1 
HETATM 6889 O O9P . COA D 3 .   ? 2.952   12.172  -13.539 1.00 62.77  ? 502 COA A O9P 1 
HETATM 6890 N N8P . COA D 3 .   ? 4.629   11.769  -14.972 1.00 63.94  ? 502 COA A N8P 1 
HETATM 6891 C C7P . COA D 3 .   ? 4.111   10.487  -15.449 1.00 61.76  ? 502 COA A C7P 1 
HETATM 6892 C C6P . COA D 3 .   ? 4.762   9.295   -14.755 1.00 58.18  ? 502 COA A C6P 1 
HETATM 6893 C C5P . COA D 3 .   ? 6.212   9.134   -15.175 1.00 57.09  ? 502 COA A C5P 1 
HETATM 6894 O O5P . COA D 3 .   ? 6.500   9.056   -16.367 1.00 49.32  ? 502 COA A O5P 1 
HETATM 6895 N N4P . COA D 3 .   ? 7.145   9.111   -14.203 1.00 57.45  ? 502 COA A N4P 1 
HETATM 6896 C C3P . COA D 3 .   ? 8.567   8.875   -14.428 1.00 67.95  ? 502 COA A C3P 1 
HETATM 6897 C C2P . COA D 3 .   ? 9.446   9.979   -13.862 1.00 73.55  ? 502 COA A C2P 1 
HETATM 6898 S S1P . COA D 3 .   ? 10.111  9.646   -12.206 1.00 85.20  ? 502 COA A S1P 1 
HETATM 6899 O O1  . OAA E 4 .   ? 18.239  11.764  17.560  1.00 70.09  ? 501 OAA B O1  1 
HETATM 6900 O O2  . OAA E 4 .   ? 19.529  12.750  19.123  1.00 64.83  ? 501 OAA B O2  1 
HETATM 6901 O O4  . OAA E 4 .   ? 16.780  8.646   19.086  1.00 39.06  ? 501 OAA B O4  1 
HETATM 6902 O O5  . OAA E 4 .   ? 17.156  8.726   16.971  1.00 32.94  ? 501 OAA B O5  1 
HETATM 6903 O O3  . OAA E 4 .   ? 19.679  8.808   17.610  1.00 64.98  ? 501 OAA B O3  1 
HETATM 6904 C C1  . OAA E 4 .   ? 18.962  11.721  18.600  1.00 73.72  ? 501 OAA B C1  1 
HETATM 6905 C C2  . OAA E 4 .   ? 19.147  10.357  19.276  1.00 59.11  ? 501 OAA B C2  1 
HETATM 6906 C C3  . OAA E 4 .   ? 18.794  9.241   18.334  1.00 62.41  ? 501 OAA B C3  1 
HETATM 6907 C C4  . OAA E 4 .   ? 17.541  8.825   18.126  1.00 48.79  ? 501 OAA B C4  1 
HETATM 6908 O O   . HOH F 5 .   ? 7.867   -17.416 -10.819 1.00 48.42  ? 601 HOH A O   1 
HETATM 6909 O O   . HOH F 5 .   ? 34.388  16.819  -5.254  1.00 44.41  ? 602 HOH A O   1 
HETATM 6910 O O   . HOH F 5 .   ? 21.996  9.755   -27.777 1.00 44.94  ? 603 HOH A O   1 
HETATM 6911 O O   . HOH F 5 .   ? 25.539  16.369  -25.972 1.00 30.60  ? 604 HOH A O   1 
HETATM 6912 O O   . HOH F 5 .   ? 29.795  -4.293  -19.624 1.00 25.21  ? 605 HOH A O   1 
HETATM 6913 O O   . HOH F 5 .   ? 8.541   -15.718 -17.976 1.00 47.78  ? 606 HOH A O   1 
HETATM 6914 O O   . HOH F 5 .   ? 42.121  -3.181  -4.605  1.00 31.35  ? 607 HOH A O   1 
HETATM 6915 O O   . HOH F 5 .   ? 44.752  10.053  -0.841  1.00 33.73  ? 608 HOH A O   1 
HETATM 6916 O O   . HOH F 5 .   ? 7.372   18.429  -8.521  1.00 51.11  ? 609 HOH A O   1 
HETATM 6917 O O   . HOH F 5 .   ? 6.618   8.164   -26.578 1.00 37.46  ? 610 HOH A O   1 
HETATM 6918 O O   . HOH F 5 .   ? 11.345  -14.263 -21.104 1.00 38.02  ? 611 HOH A O   1 
HETATM 6919 O O   . HOH F 5 .   ? 47.725  13.916  -4.915  1.00 40.71  ? 612 HOH A O   1 
HETATM 6920 O O   . HOH F 5 .   ? 22.786  3.354   -30.239 1.00 42.92  ? 613 HOH A O   1 
HETATM 6921 O O   . HOH F 5 .   ? 7.663   -12.461 -7.445  1.00 34.09  ? 614 HOH A O   1 
HETATM 6922 O O   . HOH F 5 .   ? 41.899  -1.169  17.345  1.00 48.27  ? 615 HOH A O   1 
HETATM 6923 O O   . HOH F 5 .   ? 3.685   19.566  17.992  1.00 34.82  ? 616 HOH A O   1 
HETATM 6924 O O   . HOH F 5 .   ? 33.627  7.915   12.681  1.00 39.42  ? 617 HOH A O   1 
HETATM 6925 O O   . HOH F 5 .   ? 6.922   -4.398  -10.206 1.00 38.72  ? 618 HOH A O   1 
HETATM 6926 O O   . HOH F 5 .   ? 36.801  4.333   12.765  1.00 35.52  ? 619 HOH A O   1 
HETATM 6927 O O   . HOH F 5 .   ? 11.040  20.084  15.712  1.00 32.02  ? 620 HOH A O   1 
HETATM 6928 O O   . HOH F 5 .   ? 21.819  9.306   -8.889  1.00 23.92  ? 621 HOH A O   1 
HETATM 6929 O O   . HOH F 5 .   ? 18.554  12.394  8.446   1.00 22.06  ? 622 HOH A O   1 
HETATM 6930 O O   . HOH F 5 .   ? 14.944  -16.313 -6.073  1.00 33.94  ? 623 HOH A O   1 
HETATM 6931 O O   . HOH F 5 .   ? 37.889  8.328   -25.412 1.00 34.67  ? 624 HOH A O   1 
HETATM 6932 O O   . HOH F 5 .   ? 36.009  -5.256  -21.108 1.00 37.87  ? 625 HOH A O   1 
HETATM 6933 O O   . HOH F 5 .   ? 29.906  -2.038  -26.926 1.00 33.58  ? 626 HOH A O   1 
HETATM 6934 O O   . HOH F 5 .   ? 41.818  7.856   -17.903 1.00 34.91  ? 627 HOH A O   1 
HETATM 6935 O O   . HOH F 5 .   ? 19.819  19.797  11.921  1.00 31.90  ? 628 HOH A O   1 
HETATM 6936 O O   . HOH F 5 .   ? 29.373  10.431  7.975   1.00 23.12  ? 629 HOH A O   1 
HETATM 6937 O O   . HOH F 5 .   ? 37.301  -7.483  -0.898  1.00 52.47  ? 630 HOH A O   1 
HETATM 6938 O O   . HOH F 5 .   ? 15.191  12.303  -2.400  1.00 19.89  ? 631 HOH A O   1 
HETATM 6939 O O   . HOH F 5 .   ? 48.713  1.659   -9.676  1.00 48.81  ? 632 HOH A O   1 
HETATM 6940 O O   . HOH F 5 .   ? 41.694  -1.797  -7.066  1.00 24.35  ? 633 HOH A O   1 
HETATM 6941 O O   . HOH F 5 .   ? 8.540   -4.052  -28.490 1.00 38.03  ? 634 HOH A O   1 
HETATM 6942 O O   . HOH F 5 .   ? 33.563  -8.266  -16.057 1.00 28.74  ? 635 HOH A O   1 
HETATM 6943 O O   . HOH F 5 .   ? 13.624  2.912   -17.609 1.00 28.59  ? 636 HOH A O   1 
HETATM 6944 O O   . HOH F 5 .   ? 26.287  14.164  4.197   1.00 24.07  ? 637 HOH A O   1 
HETATM 6945 O O   . HOH F 5 .   ? 26.786  10.203  -29.718 1.00 39.89  ? 638 HOH A O   1 
HETATM 6946 O O   . HOH F 5 .   ? 7.073   -1.400  -4.247  1.00 30.76  ? 639 HOH A O   1 
HETATM 6947 O O   . HOH F 5 .   ? 18.368  -6.493  -32.714 1.00 40.50  ? 640 HOH A O   1 
HETATM 6948 O O   . HOH F 5 .   ? 36.159  9.968   6.054   1.00 34.90  ? 641 HOH A O   1 
HETATM 6949 O O   . HOH F 5 .   ? 28.095  16.660  -14.385 1.00 24.24  ? 642 HOH A O   1 
HETATM 6950 O O   . HOH F 5 .   ? 15.195  -17.608 1.545   1.00 33.52  ? 643 HOH A O   1 
HETATM 6951 O O   . HOH F 5 .   ? 26.702  -8.851  8.889   1.00 23.10  ? 644 HOH A O   1 
HETATM 6952 O O   . HOH F 5 .   ? 24.102  0.078   -31.603 1.00 52.12  ? 645 HOH A O   1 
HETATM 6953 O O   . HOH F 5 .   ? 37.717  19.526  2.510   1.00 44.78  ? 646 HOH A O   1 
HETATM 6954 O O   . HOH F 5 .   ? 16.877  -5.168  2.996   1.00 38.32  ? 647 HOH A O   1 
HETATM 6955 O O   . HOH F 5 .   ? 20.952  11.458  -25.652 1.00 34.22  ? 648 HOH A O   1 
HETATM 6956 O O   . HOH F 5 .   ? 39.121  -11.686 -13.976 1.00 44.58  ? 649 HOH A O   1 
HETATM 6957 O O   . HOH F 5 .   ? 34.803  14.547  -6.727  1.00 26.11  ? 650 HOH A O   1 
HETATM 6958 O O   . HOH F 5 .   ? 22.924  14.024  -21.448 1.00 29.86  ? 651 HOH A O   1 
HETATM 6959 O O   . HOH F 5 .   ? 22.870  -23.114 -1.684  1.00 41.79  ? 652 HOH A O   1 
HETATM 6960 O O   . HOH F 5 .   ? 24.669  17.030  -8.087  1.00 21.74  ? 653 HOH A O   1 
HETATM 6961 O O   . HOH F 5 .   ? 9.952   17.952  3.207   1.00 23.64  ? 654 HOH A O   1 
HETATM 6962 O O   . HOH F 5 .   ? 34.990  -13.618 -6.261  1.00 36.61  ? 655 HOH A O   1 
HETATM 6963 O O   . HOH F 5 .   ? 32.101  -16.945 -22.415 1.00 52.00  ? 656 HOH A O   1 
HETATM 6964 O O   . HOH F 5 .   ? 42.114  26.038  2.583   1.00 57.76  ? 657 HOH A O   1 
HETATM 6965 O O   . HOH F 5 .   ? 29.170  5.053   4.338   1.00 20.43  ? 658 HOH A O   1 
HETATM 6966 O O   . HOH F 5 .   ? 8.503   1.509   -20.771 1.00 32.70  ? 659 HOH A O   1 
HETATM 6967 O O   . HOH F 5 .   ? 23.744  15.124  3.107   1.00 23.08  ? 660 HOH A O   1 
HETATM 6968 O O   . HOH F 5 .   ? 35.304  15.802  -15.727 1.00 34.66  ? 661 HOH A O   1 
HETATM 6969 O O   . HOH F 5 .   ? 10.074  -20.165 -13.429 1.00 38.68  ? 662 HOH A O   1 
HETATM 6970 O O   . HOH F 5 .   ? 11.843  15.007  -19.597 1.00 39.87  ? 663 HOH A O   1 
HETATM 6971 O O   . HOH F 5 .   ? 12.988  -3.472  -2.454  1.00 26.47  ? 664 HOH A O   1 
HETATM 6972 O O   . HOH F 5 .   ? 20.197  7.992   -15.029 1.00 29.36  ? 665 HOH A O   1 
HETATM 6973 O O   . HOH F 5 .   ? -4.057  16.739  -11.786 1.00 50.21  ? 666 HOH A O   1 
HETATM 6974 O O   . HOH F 5 .   ? 37.944  14.926  -17.699 1.00 44.84  ? 667 HOH A O   1 
HETATM 6975 O O   . HOH F 5 .   ? 11.966  -16.945 -6.175  1.00 31.75  ? 668 HOH A O   1 
HETATM 6976 O O   . HOH F 5 .   ? 32.637  10.596  6.035   1.00 30.32  ? 669 HOH A O   1 
HETATM 6977 O O   . HOH F 5 .   ? 2.236   0.205   -34.301 1.00 48.11  ? 670 HOH A O   1 
HETATM 6978 O O   . HOH F 5 .   ? 29.607  -15.700 -18.624 1.00 38.03  ? 671 HOH A O   1 
HETATM 6979 O O   . HOH F 5 .   ? 10.902  2.587   -14.097 1.00 39.35  ? 672 HOH A O   1 
HETATM 6980 O O   . HOH F 5 .   ? 26.850  9.349   -0.672  1.00 17.97  ? 673 HOH A O   1 
HETATM 6981 O O   . HOH F 5 .   ? 27.743  -1.211  8.255   1.00 26.08  ? 674 HOH A O   1 
HETATM 6982 O O   . HOH F 5 .   ? 32.218  13.469  8.726   1.00 41.01  ? 675 HOH A O   1 
HETATM 6983 O O   . HOH F 5 .   ? 27.471  11.791  3.028   1.00 25.40  ? 676 HOH A O   1 
HETATM 6984 O O   . HOH F 5 .   ? 2.061   17.865  1.522   1.00 31.10  ? 677 HOH A O   1 
HETATM 6985 O O   . HOH F 5 .   ? 3.841   6.524   -22.988 1.00 39.64  ? 678 HOH A O   1 
HETATM 6986 O O   . HOH F 5 .   ? 25.127  -2.580  -31.331 1.00 41.04  ? 679 HOH A O   1 
HETATM 6987 O O   . HOH F 5 .   ? 33.232  2.569   -21.313 1.00 26.03  ? 680 HOH A O   1 
HETATM 6988 O O   . HOH F 5 .   ? 17.114  26.121  -2.543  1.00 40.32  ? 681 HOH A O   1 
HETATM 6989 O O   . HOH F 5 .   ? 7.561   28.096  -1.962  1.00 36.55  ? 682 HOH A O   1 
HETATM 6990 O O   . HOH F 5 .   ? 26.859  9.093   2.148   1.00 18.77  ? 683 HOH A O   1 
HETATM 6991 O O   . HOH F 5 .   ? 32.588  16.195  -26.540 1.00 55.96  ? 684 HOH A O   1 
HETATM 6992 O O   . HOH F 5 .   ? 20.710  -17.977 4.141   1.00 31.10  ? 685 HOH A O   1 
HETATM 6993 O O   . HOH F 5 .   ? 25.677  7.653   -2.462  1.00 19.93  ? 686 HOH A O   1 
HETATM 6994 O O   . HOH F 5 .   ? 6.578   16.629  2.741   1.00 27.78  ? 687 HOH A O   1 
HETATM 6995 O O   . HOH F 5 .   ? 42.149  3.848   -25.225 1.00 41.12  ? 688 HOH A O   1 
HETATM 6996 O O   . HOH F 5 .   ? 8.473   1.728   -23.524 1.00 35.83  ? 689 HOH A O   1 
HETATM 6997 O O   . HOH F 5 .   ? 29.424  16.346  -11.978 1.00 28.71  ? 690 HOH A O   1 
HETATM 6998 O O   . HOH F 5 .   ? 38.898  12.891  -19.454 1.00 35.34  ? 691 HOH A O   1 
HETATM 6999 O O   . HOH F 5 .   ? 43.196  26.689  7.064   1.00 51.85  ? 692 HOH A O   1 
HETATM 7000 O O   . HOH F 5 .   ? 29.109  -17.325 -6.779  1.00 40.41  ? 693 HOH A O   1 
HETATM 7001 O O   . HOH F 5 .   ? 31.055  -9.231  -12.199 1.00 34.45  ? 694 HOH A O   1 
HETATM 7002 O O   . HOH F 5 .   ? 5.101   -9.121  -16.974 1.00 43.12  ? 695 HOH A O   1 
HETATM 7003 O O   . HOH F 5 .   ? 35.247  -16.795 -13.220 1.00 56.07  ? 696 HOH A O   1 
HETATM 7004 O O   . HOH F 5 .   ? 19.372  -19.841 -10.418 1.00 41.11  ? 697 HOH A O   1 
HETATM 7005 O O   . HOH F 5 .   ? 4.473   15.832  -6.638  1.00 47.09  ? 698 HOH A O   1 
HETATM 7006 O O   . HOH F 5 .   ? 6.042   5.863   -24.841 1.00 34.09  ? 699 HOH A O   1 
HETATM 7007 O O   . HOH F 5 .   ? 38.116  8.603   4.025   1.00 22.93  ? 700 HOH A O   1 
HETATM 7008 O O   . HOH F 5 .   ? 32.477  18.955  -8.449  1.00 31.49  ? 701 HOH A O   1 
HETATM 7009 O O   . HOH F 5 .   ? 41.801  8.084   -15.455 1.00 36.32  ? 702 HOH A O   1 
HETATM 7010 O O   . HOH F 5 .   ? 31.524  32.458  3.882   1.00 46.67  ? 703 HOH A O   1 
HETATM 7011 O O   . HOH F 5 .   ? 37.704  -7.748  7.440   1.00 47.95  ? 704 HOH A O   1 
HETATM 7012 O O   . HOH F 5 .   ? 39.454  10.669  3.563   1.00 37.55  ? 705 HOH A O   1 
HETATM 7013 O O   . HOH F 5 .   ? 33.569  18.029  2.811   1.00 46.93  ? 706 HOH A O   1 
HETATM 7014 O O   . HOH F 5 .   ? 18.477  13.395  -18.109 1.00 34.42  ? 707 HOH A O   1 
HETATM 7015 O O   . HOH F 5 .   ? 13.849  -20.309 -6.137  1.00 49.19  ? 708 HOH A O   1 
HETATM 7016 O O   . HOH F 5 .   ? 29.765  0.059   9.167   1.00 25.26  ? 709 HOH A O   1 
HETATM 7017 O O   . HOH F 5 .   ? 38.640  -13.743 -12.845 1.00 42.41  ? 710 HOH A O   1 
HETATM 7018 O O   . HOH F 5 .   ? 32.021  -18.199 -11.858 1.00 41.82  ? 711 HOH A O   1 
HETATM 7019 O O   . HOH F 5 .   ? 25.946  16.172  0.661   1.00 26.84  ? 712 HOH A O   1 
HETATM 7020 O O   . HOH F 5 .   ? 44.814  18.249  0.788   1.00 45.68  ? 713 HOH A O   1 
HETATM 7021 O O   . HOH F 5 .   ? 35.280  3.400   14.757  1.00 55.87  ? 714 HOH A O   1 
HETATM 7022 O O   . HOH F 5 .   ? 45.157  10.570  -10.268 1.00 33.70  ? 715 HOH A O   1 
HETATM 7023 O O   . HOH F 5 .   ? 15.519  29.253  -2.989  1.00 48.48  ? 716 HOH A O   1 
HETATM 7024 O O   . HOH F 5 .   ? 25.068  35.331  1.112   1.00 34.82  ? 717 HOH A O   1 
HETATM 7025 O O   . HOH F 5 .   ? 42.035  -6.578  -13.108 1.00 51.07  ? 718 HOH A O   1 
HETATM 7026 O O   . HOH F 5 .   ? 47.887  -3.061  -8.726  1.00 54.93  ? 719 HOH A O   1 
HETATM 7027 O O   . HOH F 5 .   ? 13.025  10.035  -7.071  1.00 27.18  ? 720 HOH A O   1 
HETATM 7028 O O   . HOH F 5 .   ? 27.323  -3.998  -32.662 1.00 52.44  ? 721 HOH A O   1 
HETATM 7029 O O   . HOH F 5 .   ? 10.439  -4.226  -3.312  1.00 31.17  ? 722 HOH A O   1 
HETATM 7030 O O   . HOH F 5 .   ? 31.824  -9.662  -14.695 1.00 30.08  ? 723 HOH A O   1 
HETATM 7031 O O   . HOH F 5 .   ? 41.150  -0.967  1.814   1.00 40.13  ? 724 HOH A O   1 
HETATM 7032 O O   . HOH F 5 .   ? 28.656  13.407  11.419  1.00 27.77  ? 725 HOH A O   1 
HETATM 7033 O O   . HOH F 5 .   ? 45.623  -4.859  -10.279 1.00 39.75  ? 726 HOH A O   1 
HETATM 7034 O O   . HOH F 5 .   ? 44.172  -11.950 -8.928  1.00 59.54  ? 727 HOH A O   1 
HETATM 7035 O O   . HOH F 5 .   ? 34.310  -6.221  -23.670 1.00 45.84  ? 728 HOH A O   1 
HETATM 7036 O O   . HOH F 5 .   ? 30.229  -15.963 -23.860 1.00 44.80  ? 729 HOH A O   1 
HETATM 7037 O O   . HOH F 5 .   ? 3.777   -15.934 -7.151  1.00 55.30  ? 730 HOH A O   1 
HETATM 7038 O O   . HOH F 5 .   ? 40.969  -16.246 -15.156 1.00 56.09  ? 731 HOH A O   1 
HETATM 7039 O O   . HOH F 5 .   ? 39.831  -6.743  -1.680  1.00 46.15  ? 732 HOH A O   1 
HETATM 7040 O O   . HOH F 5 .   ? 16.944  24.659  -6.697  1.00 46.44  ? 733 HOH A O   1 
HETATM 7041 O O   . HOH F 5 .   ? 8.890   -13.370 -24.013 1.00 52.29  ? 734 HOH A O   1 
HETATM 7042 O O   . HOH F 5 .   ? 10.170  12.458  -12.230 1.00 49.13  ? 735 HOH A O   1 
HETATM 7043 O O   . HOH F 5 .   ? 16.565  -19.338 3.078   1.00 36.81  ? 736 HOH A O   1 
HETATM 7044 O O   . HOH F 5 .   ? 30.067  -19.056 2.316   1.00 32.25  ? 737 HOH A O   1 
HETATM 7045 O O   . HOH F 5 .   ? -2.815  6.432   -16.392 1.00 48.02  ? 738 HOH A O   1 
HETATM 7046 O O   . HOH F 5 .   ? 5.658   17.143  -16.481 1.00 52.24  ? 739 HOH A O   1 
HETATM 7047 O O   . HOH F 5 .   ? 36.451  -1.924  -28.754 1.00 52.79  ? 740 HOH A O   1 
HETATM 7048 O O   . HOH F 5 .   ? 8.386   21.524  15.728  1.00 25.15  ? 741 HOH A O   1 
HETATM 7049 O O   . HOH F 5 .   ? 35.068  20.176  3.767   1.00 44.19  ? 742 HOH A O   1 
HETATM 7050 O O   . HOH F 5 .   ? 6.817   -10.137 -14.174 1.00 37.16  ? 743 HOH A O   1 
HETATM 7051 O O   . HOH F 5 .   ? 44.798  -2.045  -4.775  1.00 36.52  ? 744 HOH A O   1 
HETATM 7052 O O   . HOH F 5 .   ? 32.753  16.366  9.053   1.00 57.42  ? 745 HOH A O   1 
HETATM 7053 O O   . HOH F 5 .   ? 12.093  0.128   -14.200 1.00 34.33  ? 746 HOH A O   1 
HETATM 7054 O O   . HOH F 5 .   ? 9.034   -2.769  -7.156  1.00 52.24  ? 747 HOH A O   1 
HETATM 7055 O O   . HOH F 5 .   ? 8.389   -17.481 -16.085 1.00 45.60  ? 748 HOH A O   1 
HETATM 7056 O O   . HOH F 5 .   ? 27.199  -5.610  10.273  1.00 39.82  ? 749 HOH A O   1 
HETATM 7057 O O   . HOH F 5 .   ? 9.562   -10.166 -30.361 1.00 60.28  ? 750 HOH A O   1 
HETATM 7058 O O   . HOH F 5 .   ? -3.926  4.549   -16.398 1.00 49.22  ? 751 HOH A O   1 
HETATM 7059 O O   . HOH F 5 .   ? 41.468  16.072  -12.107 1.00 46.44  ? 752 HOH A O   1 
HETATM 7060 O O   . HOH F 5 .   ? 30.471  -0.870  11.474  1.00 34.91  ? 753 HOH A O   1 
HETATM 7061 O O   . HOH F 5 .   ? 34.859  -11.956 -3.783  1.00 48.30  ? 754 HOH A O   1 
HETATM 7062 O O   . HOH F 5 .   ? 40.591  12.623  12.562  1.00 52.73  ? 755 HOH A O   1 
HETATM 7063 O O   . HOH F 5 .   ? 42.496  19.467  2.647   1.00 36.85  ? 756 HOH A O   1 
HETATM 7064 O O   . HOH F 5 .   ? 8.461   -3.944  -4.691  1.00 41.44  ? 757 HOH A O   1 
HETATM 7065 O O   . HOH F 5 .   ? 42.671  -5.773  -4.672  1.00 40.03  ? 758 HOH A O   1 
HETATM 7066 O O   . HOH F 5 .   ? 35.131  5.916   16.268  1.00 56.88  ? 759 HOH A O   1 
HETATM 7067 O O   . HOH F 5 .   ? 38.216  -8.697  10.215  1.00 59.30  ? 760 HOH A O   1 
HETATM 7068 O O   . HOH F 5 .   ? 31.159  11.344  9.633   1.00 36.81  ? 761 HOH A O   1 
HETATM 7069 O O   . HOH F 5 .   ? 27.800  19.085  -15.012 1.00 36.40  ? 762 HOH A O   1 
HETATM 7070 O O   . HOH F 5 .   ? 6.769   -16.673 -14.691 1.00 57.02  ? 763 HOH A O   1 
HETATM 7071 O O   . HOH F 5 .   ? 47.143  18.461  -2.559  1.00 52.13  ? 764 HOH A O   1 
HETATM 7072 O O   . HOH F 5 .   ? 11.456  22.273  17.474  1.00 37.49  ? 765 HOH A O   1 
HETATM 7073 O O   . HOH F 5 .   ? 35.732  2.991   17.206  1.00 56.49  ? 766 HOH A O   1 
HETATM 7074 O O   . HOH F 5 .   ? 35.371  16.534  -13.001 1.00 41.89  ? 767 HOH A O   1 
HETATM 7075 O O   . HOH F 5 .   ? 9.041   23.540  17.609  1.00 43.92  ? 768 HOH A O   1 
HETATM 7076 O O   . HOH F 5 .   ? 36.174  17.245  -17.829 1.00 47.86  ? 769 HOH A O   1 
HETATM 7077 O O   . HOH F 5 .   ? 47.948  16.466  -4.096  1.00 49.33  ? 770 HOH A O   1 
HETATM 7078 O O   . HOH F 5 .   ? 5.531   12.142  -7.778  1.00 35.28  ? 771 HOH A O   1 
HETATM 7079 O O   . HOH F 5 .   ? 37.452  4.986   17.923  1.00 49.15  ? 772 HOH A O   1 
HETATM 7080 O O   . HOH G 5 .   ? -0.249  -10.254 7.649   1.00 43.43  ? 601 HOH B O   1 
HETATM 7081 O O   . HOH G 5 .   ? 9.184   0.361   37.913  1.00 41.46  ? 602 HOH B O   1 
HETATM 7082 O O   . HOH G 5 .   ? 19.684  0.072   22.478  1.00 40.46  ? 603 HOH B O   1 
HETATM 7083 O O   . HOH G 5 .   ? 24.482  -7.398  40.293  1.00 33.79  ? 604 HOH B O   1 
HETATM 7084 O O   . HOH G 5 .   ? 26.334  -1.328  10.612  1.00 31.57  ? 605 HOH B O   1 
HETATM 7085 O O   . HOH G 5 .   ? 26.648  -4.330  16.544  1.00 41.04  ? 606 HOH B O   1 
HETATM 7086 O O   . HOH G 5 .   ? 19.642  3.646   24.570  1.00 42.71  ? 607 HOH B O   1 
HETATM 7087 O O   . HOH G 5 .   ? 31.585  18.364  38.138  1.00 50.60  ? 608 HOH B O   1 
HETATM 7088 O O   . HOH G 5 .   ? -8.150  -1.818  -11.089 1.00 53.67  ? 609 HOH B O   1 
HETATM 7089 O O   . HOH G 5 .   ? 0.675   -6.732  6.079   1.00 27.49  ? 610 HOH B O   1 
HETATM 7090 O O   . HOH G 5 .   ? -10.995 -2.807  25.296  1.00 52.14  ? 611 HOH B O   1 
HETATM 7091 O O   . HOH G 5 .   ? -1.205  19.916  13.704  1.00 52.04  ? 612 HOH B O   1 
HETATM 7092 O O   . HOH G 5 .   ? -8.603  24.677  -2.550  1.00 52.28  ? 613 HOH B O   1 
HETATM 7093 O O   . HOH G 5 .   ? 1.608   16.815  16.062  1.00 37.83  ? 614 HOH B O   1 
HETATM 7094 O O   . HOH G 5 .   ? -8.120  -1.670  13.241  1.00 27.68  ? 615 HOH B O   1 
HETATM 7095 O O   . HOH G 5 .   ? -4.334  8.697   31.621  1.00 38.69  ? 616 HOH B O   1 
HETATM 7096 O O   . HOH G 5 .   ? 20.752  -23.262 5.144   1.00 36.79  ? 617 HOH B O   1 
HETATM 7097 O O   . HOH G 5 .   ? -3.259  4.722   -6.691  1.00 38.77  ? 618 HOH B O   1 
HETATM 7098 O O   . HOH G 5 .   ? 22.265  7.091   36.930  1.00 37.07  ? 619 HOH B O   1 
HETATM 7099 O O   . HOH G 5 .   ? 10.678  14.289  27.573  1.00 34.35  ? 620 HOH B O   1 
HETATM 7100 O O   . HOH G 5 .   ? 29.883  19.035  -11.789 1.00 33.48  ? 621 HOH B O   1 
HETATM 7101 O O   . HOH G 5 .   ? 25.763  28.149  7.337   1.00 37.14  ? 622 HOH B O   1 
HETATM 7102 O O   . HOH G 5 .   ? 18.551  -16.138 12.582  1.00 30.11  ? 623 HOH B O   1 
HETATM 7103 O O   . HOH G 5 .   ? 23.105  -4.341  9.534   1.00 31.62  ? 624 HOH B O   1 
HETATM 7104 O O   . HOH G 5 .   ? 25.820  -11.638 17.080  1.00 33.10  ? 625 HOH B O   1 
HETATM 7105 O O   . HOH G 5 .   ? -3.696  -7.167  6.983   1.00 42.57  ? 626 HOH B O   1 
HETATM 7106 O O   . HOH G 5 .   ? 25.589  -12.202 14.216  1.00 32.32  ? 627 HOH B O   1 
HETATM 7107 O O   . HOH G 5 .   ? 22.115  -14.057 27.450  1.00 30.80  ? 628 HOH B O   1 
HETATM 7108 O O   . HOH G 5 .   ? 13.088  8.601   21.622  1.00 34.83  ? 629 HOH B O   1 
HETATM 7109 O O   . HOH G 5 .   ? 8.361   -12.698 29.612  1.00 30.43  ? 630 HOH B O   1 
HETATM 7110 O O   . HOH G 5 .   ? -8.528  -3.082  10.794  1.00 30.31  ? 631 HOH B O   1 
HETATM 7111 O O   . HOH G 5 .   ? 43.053  12.830  21.689  1.00 61.52  ? 632 HOH B O   1 
HETATM 7112 O O   . HOH G 5 .   ? 3.367   -1.653  33.266  1.00 31.57  ? 633 HOH B O   1 
HETATM 7113 O O   . HOH G 5 .   ? 3.737   -15.241 24.785  1.00 34.90  ? 634 HOH B O   1 
HETATM 7114 O O   . HOH G 5 .   ? 3.649   -3.921  25.832  1.00 25.56  ? 635 HOH B O   1 
HETATM 7115 O O   . HOH G 5 .   ? -7.543  0.170   33.647  1.00 51.05  ? 636 HOH B O   1 
HETATM 7116 O O   . HOH G 5 .   ? -1.745  15.918  21.784  1.00 42.57  ? 637 HOH B O   1 
HETATM 7117 O O   . HOH G 5 .   ? 7.423   14.001  1.835   1.00 22.20  ? 638 HOH B O   1 
HETATM 7118 O O   . HOH G 5 .   ? 4.134   -7.361  -2.108  1.00 44.11  ? 639 HOH B O   1 
HETATM 7119 O O   . HOH G 5 .   ? 30.711  5.149   16.492  1.00 46.42  ? 640 HOH B O   1 
HETATM 7120 O O   . HOH G 5 .   ? 1.119   13.260  -2.584  1.00 34.80  ? 641 HOH B O   1 
HETATM 7121 O O   . HOH G 5 .   ? -11.042 10.017  6.926   1.00 38.71  ? 642 HOH B O   1 
HETATM 7122 O O   . HOH G 5 .   ? 6.286   -17.556 23.331  1.00 37.45  ? 643 HOH B O   1 
HETATM 7123 O O   . HOH G 5 .   ? 11.763  9.364   15.093  1.00 23.55  ? 644 HOH B O   1 
HETATM 7124 O O   . HOH G 5 .   ? -2.744  2.039   33.903  1.00 33.80  ? 645 HOH B O   1 
HETATM 7125 O O   . HOH G 5 .   ? 25.886  25.972  -11.363 1.00 38.17  ? 646 HOH B O   1 
HETATM 7126 O O   . HOH G 5 .   ? 4.028   16.550  18.014  1.00 34.67  ? 647 HOH B O   1 
HETATM 7127 O O   . HOH G 5 .   ? 4.288   10.456  -1.819  1.00 20.88  ? 648 HOH B O   1 
HETATM 7128 O O   . HOH G 5 .   ? 6.854   9.235   3.992   1.00 19.12  ? 649 HOH B O   1 
HETATM 7129 O O   . HOH G 5 .   ? 15.059  28.089  10.454  1.00 37.63  ? 650 HOH B O   1 
HETATM 7130 O O   . HOH G 5 .   ? 21.892  3.052   21.106  1.00 38.89  ? 651 HOH B O   1 
HETATM 7131 O O   . HOH G 5 .   ? 8.133   -16.005 33.748  1.00 48.81  ? 652 HOH B O   1 
HETATM 7132 O O   . HOH G 5 .   ? 22.469  -9.586  37.167  1.00 30.51  ? 653 HOH B O   1 
HETATM 7133 O O   . HOH G 5 .   ? -9.538  14.966  18.451  1.00 56.62  ? 654 HOH B O   1 
HETATM 7134 O O   . HOH G 5 .   ? 20.481  -3.374  8.701   1.00 26.48  ? 655 HOH B O   1 
HETATM 7135 O O   . HOH G 5 .   ? 9.488   -8.067  40.326  1.00 45.56  ? 656 HOH B O   1 
HETATM 7136 O O   . HOH G 5 .   ? 4.483   5.107   1.881   1.00 19.97  ? 657 HOH B O   1 
HETATM 7137 O O   . HOH G 5 .   ? -3.683  -16.912 22.760  1.00 45.23  ? 658 HOH B O   1 
HETATM 7138 O O   . HOH G 5 .   ? -2.838  10.277  0.090   1.00 38.07  ? 659 HOH B O   1 
HETATM 7139 O O   . HOH G 5 .   ? -3.993  -7.508  -2.758  1.00 63.37  ? 660 HOH B O   1 
HETATM 7140 O O   . HOH G 5 .   ? 0.192   2.714   27.572  1.00 26.00  ? 661 HOH B O   1 
HETATM 7141 O O   . HOH G 5 .   ? 13.733  19.647  -6.095  1.00 33.20  ? 662 HOH B O   1 
HETATM 7142 O O   . HOH G 5 .   ? -7.792  -0.748  4.619   1.00 35.66  ? 663 HOH B O   1 
HETATM 7143 O O   . HOH G 5 .   ? -15.959 11.996  10.954  1.00 46.89  ? 664 HOH B O   1 
HETATM 7144 O O   . HOH G 5 .   ? 6.797   9.433   6.872   1.00 21.02  ? 665 HOH B O   1 
HETATM 7145 O O   . HOH G 5 .   ? 34.588  7.524   47.345  1.00 54.21  ? 666 HOH B O   1 
HETATM 7146 O O   . HOH G 5 .   ? 1.128   10.391  -0.049  1.00 25.29  ? 667 HOH B O   1 
HETATM 7147 O O   . HOH G 5 .   ? -4.513  26.085  10.491  1.00 34.89  ? 668 HOH B O   1 
HETATM 7148 O O   . HOH G 5 .   ? 14.440  11.659  39.297  1.00 48.18  ? 669 HOH B O   1 
HETATM 7149 O O   . HOH G 5 .   ? -0.758  17.102  11.335  1.00 34.86  ? 670 HOH B O   1 
HETATM 7150 O O   . HOH G 5 .   ? -4.024  19.566  3.663   1.00 41.68  ? 671 HOH B O   1 
HETATM 7151 O O   . HOH G 5 .   ? 9.058   17.104  14.255  1.00 23.20  ? 672 HOH B O   1 
HETATM 7152 O O   . HOH G 5 .   ? -4.800  -4.755  -0.605  1.00 43.84  ? 673 HOH B O   1 
HETATM 7153 O O   . HOH G 5 .   ? 6.859   -9.086  -2.536  1.00 27.75  ? 674 HOH B O   1 
HETATM 7154 O O   . HOH G 5 .   ? 18.267  30.251  8.321   1.00 39.53  ? 675 HOH B O   1 
HETATM 7155 O O   . HOH G 5 .   ? 8.834   35.329  4.004   1.00 33.25  ? 676 HOH B O   1 
HETATM 7156 O O   . HOH G 5 .   ? 5.933   -1.183  -1.972  1.00 29.07  ? 677 HOH B O   1 
HETATM 7157 O O   . HOH G 5 .   ? 18.411  12.186  36.541  1.00 55.75  ? 678 HOH B O   1 
HETATM 7158 O O   . HOH G 5 .   ? 14.141  -19.521 16.626  1.00 33.13  ? 679 HOH B O   1 
HETATM 7159 O O   . HOH G 5 .   ? 30.518  -0.425  41.338  1.00 44.40  ? 680 HOH B O   1 
HETATM 7160 O O   . HOH G 5 .   ? 7.920   7.668   8.548   1.00 18.86  ? 681 HOH B O   1 
HETATM 7161 O O   . HOH G 5 .   ? 1.433   35.189  3.658   1.00 27.20  ? 682 HOH B O   1 
HETATM 7162 O O   . HOH G 5 .   ? -1.383  -13.611 12.634  1.00 40.20  ? 683 HOH B O   1 
HETATM 7163 O O   . HOH G 5 .   ? -3.504  -8.861  24.770  1.00 41.83  ? 684 HOH B O   1 
HETATM 7164 O O   . HOH G 5 .   ? -6.551  8.778   -6.601  1.00 35.65  ? 685 HOH B O   1 
HETATM 7165 O O   . HOH G 5 .   ? -17.758 8.847   12.744  1.00 32.02  ? 686 HOH B O   1 
HETATM 7166 O O   . HOH G 5 .   ? 23.577  -19.966 19.979  1.00 37.58  ? 687 HOH B O   1 
HETATM 7167 O O   . HOH G 5 .   ? 18.212  -17.354 4.558   1.00 32.08  ? 688 HOH B O   1 
HETATM 7168 O O   . HOH G 5 .   ? -10.631 -5.568  14.976  1.00 55.01  ? 689 HOH B O   1 
HETATM 7169 O O   . HOH G 5 .   ? -2.224  9.013   36.186  1.00 52.27  ? 690 HOH B O   1 
HETATM 7170 O O   . HOH G 5 .   ? -8.605  -6.509  19.025  1.00 51.68  ? 691 HOH B O   1 
HETATM 7171 O O   . HOH G 5 .   ? 27.725  -7.857  27.667  1.00 53.87  ? 692 HOH B O   1 
HETATM 7172 O O   . HOH G 5 .   ? -0.461  33.219  11.217  1.00 30.14  ? 693 HOH B O   1 
HETATM 7173 O O   . HOH G 5 .   ? 25.126  -3.822  48.178  1.00 53.27  ? 694 HOH B O   1 
HETATM 7174 O O   . HOH G 5 .   ? 23.665  17.812  2.844   1.00 25.08  ? 695 HOH B O   1 
HETATM 7175 O O   . HOH G 5 .   ? 20.541  10.211  13.179  1.00 28.79  ? 696 HOH B O   1 
HETATM 7176 O O   . HOH G 5 .   ? 3.807   0.073   -2.956  1.00 30.47  ? 697 HOH B O   1 
HETATM 7177 O O   . HOH G 5 .   ? 24.476  -4.398  35.082  1.00 28.64  ? 698 HOH B O   1 
HETATM 7178 O O   . HOH G 5 .   ? 9.848   15.166  2.776   1.00 22.78  ? 699 HOH B O   1 
HETATM 7179 O O   . HOH G 5 .   ? 21.263  -16.940 12.653  1.00 28.21  ? 700 HOH B O   1 
HETATM 7180 O O   . HOH G 5 .   ? -9.365  26.403  -0.826  1.00 58.09  ? 701 HOH B O   1 
HETATM 7181 O O   . HOH G 5 .   ? 26.562  10.442  15.841  1.00 43.28  ? 702 HOH B O   1 
HETATM 7182 O O   . HOH G 5 .   ? 7.645   16.184  5.294   1.00 29.10  ? 703 HOH B O   1 
HETATM 7183 O O   . HOH G 5 .   ? 15.944  -12.353 33.265  1.00 42.56  ? 704 HOH B O   1 
HETATM 7184 O O   . HOH G 5 .   ? -4.197  15.478  23.876  1.00 46.70  ? 705 HOH B O   1 
HETATM 7185 O O   . HOH G 5 .   ? 8.640   32.902  -1.073  1.00 38.37  ? 706 HOH B O   1 
HETATM 7186 O O   . HOH G 5 .   ? 1.352   19.329  14.495  1.00 34.06  ? 707 HOH B O   1 
HETATM 7187 O O   . HOH G 5 .   ? -12.297 1.947   9.076   1.00 47.57  ? 708 HOH B O   1 
HETATM 7188 O O   . HOH G 5 .   ? -1.078  14.505  12.471  1.00 30.97  ? 709 HOH B O   1 
HETATM 7189 O O   . HOH G 5 .   ? 16.643  24.706  12.832  1.00 43.78  ? 710 HOH B O   1 
HETATM 7190 O O   . HOH G 5 .   ? 6.184   11.915  3.064   1.00 24.12  ? 711 HOH B O   1 
HETATM 7191 O O   . HOH G 5 .   ? 31.576  17.924  4.474   1.00 34.77  ? 712 HOH B O   1 
HETATM 7192 O O   . HOH G 5 .   ? 16.407  26.285  8.697   1.00 39.70  ? 713 HOH B O   1 
HETATM 7193 O O   . HOH G 5 .   ? 15.541  -24.425 4.254   1.00 41.06  ? 714 HOH B O   1 
HETATM 7194 O O   . HOH G 5 .   ? 24.056  -2.599  15.674  1.00 41.17  ? 715 HOH B O   1 
HETATM 7195 O O   . HOH G 5 .   ? 5.389   16.888  20.361  1.00 24.88  ? 716 HOH B O   1 
HETATM 7196 O O   . HOH G 5 .   ? 26.902  16.543  3.219   1.00 29.81  ? 717 HOH B O   1 
HETATM 7197 O O   . HOH G 5 .   ? -3.903  16.723  3.357   1.00 41.78  ? 718 HOH B O   1 
HETATM 7198 O O   . HOH G 5 .   ? 26.781  -9.780  20.901  1.00 41.42  ? 719 HOH B O   1 
HETATM 7199 O O   . HOH G 5 .   ? 19.934  27.370  10.894  1.00 49.43  ? 720 HOH B O   1 
HETATM 7200 O O   . HOH G 5 .   ? 24.980  -15.631 24.212  1.00 41.94  ? 721 HOH B O   1 
HETATM 7201 O O   . HOH G 5 .   ? 9.243   -21.731 3.649   1.00 32.04  ? 722 HOH B O   1 
HETATM 7202 O O   . HOH G 5 .   ? -0.457  30.413  11.556  1.00 51.47  ? 723 HOH B O   1 
HETATM 7203 O O   . HOH G 5 .   ? -8.492  8.378   21.511  1.00 39.11  ? 724 HOH B O   1 
HETATM 7204 O O   . HOH G 5 .   ? 27.750  -9.263  29.851  1.00 59.96  ? 725 HOH B O   1 
HETATM 7205 O O   . HOH G 5 .   ? 22.307  -4.406  50.513  1.00 45.63  ? 726 HOH B O   1 
HETATM 7206 O O   . HOH G 5 .   ? -5.243  13.269  25.672  1.00 36.06  ? 727 HOH B O   1 
HETATM 7207 O O   . HOH G 5 .   ? 24.483  -2.521  13.234  1.00 46.19  ? 728 HOH B O   1 
HETATM 7208 O O   . HOH G 5 .   ? -4.417  8.756   2.182   1.00 23.78  ? 729 HOH B O   1 
HETATM 7209 O O   . HOH G 5 .   ? 26.223  19.227  14.681  1.00 54.98  ? 730 HOH B O   1 
HETATM 7210 O O   . HOH G 5 .   ? -11.718 10.733  16.411  1.00 35.02  ? 731 HOH B O   1 
HETATM 7211 O O   . HOH G 5 .   ? 25.832  21.425  -9.915  1.00 28.69  ? 732 HOH B O   1 
HETATM 7212 O O   . HOH G 5 .   ? 0.465   10.271  -4.839  1.00 42.89  ? 733 HOH B O   1 
HETATM 7213 O O   . HOH G 5 .   ? 4.828   13.100  -5.349  1.00 28.43  ? 734 HOH B O   1 
HETATM 7214 O O   . HOH G 5 .   ? 3.087   -1.263  -5.194  1.00 44.20  ? 735 HOH B O   1 
HETATM 7215 O O   . HOH G 5 .   ? -1.493  12.952  -3.110  1.00 43.92  ? 736 HOH B O   1 
HETATM 7216 O O   . HOH G 5 .   ? 6.272   -5.519  -3.802  1.00 38.65  ? 737 HOH B O   1 
HETATM 7217 O O   . HOH G 5 .   ? 21.900  -26.148 17.952  1.00 53.38  ? 738 HOH B O   1 
HETATM 7218 O O   . HOH G 5 .   ? -12.430 13.221  15.857  1.00 45.94  ? 739 HOH B O   1 
HETATM 7219 O O   . HOH G 5 .   ? 37.418  16.907  39.484  1.00 59.29  ? 740 HOH B O   1 
HETATM 7220 O O   . HOH G 5 .   ? 28.488  -9.075  23.050  1.00 43.69  ? 741 HOH B O   1 
HETATM 7221 O O   . HOH G 5 .   ? -5.625  -5.744  5.412   1.00 50.67  ? 742 HOH B O   1 
HETATM 7222 O O   . HOH G 5 .   ? 0.036   18.341  3.443   1.00 41.16  ? 743 HOH B O   1 
HETATM 7223 O O   . HOH G 5 .   ? 11.441  -24.959 17.678  1.00 55.16  ? 744 HOH B O   1 
HETATM 7224 O O   . HOH G 5 .   ? 10.118  -20.936 16.285  1.00 45.65  ? 745 HOH B O   1 
HETATM 7225 O O   . HOH G 5 .   ? -1.580  20.089  2.349   1.00 39.70  ? 746 HOH B O   1 
HETATM 7226 O O   . HOH G 5 .   ? 2.779   18.643  34.142  1.00 62.75  ? 747 HOH B O   1 
HETATM 7227 O O   . HOH G 5 .   ? 29.606  -16.112 5.110   1.00 49.61  ? 748 HOH B O   1 
HETATM 7228 O O   . HOH G 5 .   ? 33.686  25.230  -11.304 1.00 50.18  ? 749 HOH B O   1 
HETATM 7229 O O   . HOH G 5 .   ? -17.886 4.979   18.084  1.00 44.41  ? 750 HOH B O   1 
HETATM 7230 O O   . HOH G 5 .   ? 2.825   -17.644 25.945  1.00 48.09  ? 751 HOH B O   1 
HETATM 7231 O O   . HOH G 5 .   ? 26.195  -24.744 24.302  1.00 47.46  ? 752 HOH B O   1 
HETATM 7232 O O   . HOH G 5 .   ? 29.546  -2.397  44.374  1.00 56.96  ? 753 HOH B O   1 
HETATM 7233 O O   . HOH G 5 .   ? 25.764  -23.606 21.707  1.00 56.41  ? 754 HOH B O   1 
HETATM 7234 O O   . HOH G 5 .   ? 9.934   22.729  20.294  1.00 49.27  ? 755 HOH B O   1 
HETATM 7235 O O   . HOH G 5 .   ? -11.112 -2.525  10.746  1.00 43.66  ? 756 HOH B O   1 
HETATM 7236 O O   . HOH G 5 .   ? 0.499   16.587  32.911  1.00 48.83  ? 757 HOH B O   1 
HETATM 7237 O O   . HOH G 5 .   ? 28.209  -3.106  14.239  1.00 46.63  ? 758 HOH B O   1 
HETATM 7238 O O   . HOH G 5 .   ? 26.822  22.468  -12.310 1.00 47.11  ? 759 HOH B O   1 
HETATM 7239 O O   . HOH G 5 .   ? 25.272  -3.833  10.846  1.00 30.81  ? 760 HOH B O   1 
HETATM 7240 O O   . HOH G 5 .   ? 20.895  30.800  7.662   1.00 58.59  ? 761 HOH B O   1 
HETATM 7241 O O   . HOH G 5 .   ? 5.612   35.846  1.330   1.00 37.43  ? 762 HOH B O   1 
HETATM 7242 O O   . HOH G 5 .   ? 2.358   11.216  -3.536  1.00 37.99  ? 763 HOH B O   1 
HETATM 7243 O O   . HOH G 5 .   ? 2.963   11.674  -8.752  1.00 42.36  ? 764 HOH B O   1 
HETATM 7244 O O   . HOH G 5 .   ? 20.434  26.389  13.286  1.00 55.49  ? 765 HOH B O   1 
HETATM 7245 O O   . HOH G 5 .   ? 17.279  29.874  11.067  1.00 50.22  ? 766 HOH B O   1 
HETATM 7246 O O   . HOH G 5 .   ? 29.331  -10.327 28.477  1.00 58.67  ? 767 HOH B O   1 
HETATM 7247 O O   . HOH G 5 .   ? -2.386  -15.622 11.153  1.00 53.38  ? 768 HOH B O   1 
HETATM 7248 O O   . HOH G 5 .   ? 6.900   31.669  -4.741  1.00 48.30  ? 769 HOH B O   1 
HETATM 7249 O O   . HOH G 5 .   ? 30.592  -8.561  26.783  1.00 61.94  ? 770 HOH B O   1 
HETATM 7250 O O   . HOH G 5 .   ? 8.390   31.112  -2.919  1.00 50.69  ? 771 HOH B O   1 
HETATM 7251 O O   . HOH G 5 .   ? 25.345  15.723  14.254  1.00 45.63  ? 772 HOH B O   1 
HETATM 7252 O O   . HOH G 5 .   ? 31.603  -11.116 26.842  1.00 59.16  ? 773 HOH B O   1 
# 
