data_8ZVR
# 
_entry.id   8ZVR 
# 
_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   8ZVR         pdb_00008zvr 10.2210/pdb8zvr/pdb 
WWPDB D_1300048624 ?            ?                   
# 
_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                        8ZVR 
_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 2' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Yang, L.Y.' 1 0000-0003-1550-6947 
primary 'Fang, Y.J.' 2 0009-0009-0272-0830 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Citrate synthase, mitochondrial' 48632.547 2   2.3.3.1 ? ? ? 
2 non-polymer syn 'COENZYME A'                      767.534   1   ?       ? ? ? 
3 non-polymer syn 'ACETYL GROUP'                    44.053    1   ?       ? ? ? 
4 non-polymer syn 'OXALOACETATE ION'                131.064   1   ?       ? ? ? 
5 water       nat water                             18.015    357 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Citrate (Si)-synthase' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;STNLKDILADLIPKEQARIKTFRQQHGKTVVGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGFSIPECQKLLPKAK
GGEEPLPEGLFWLLVTGHIPTEEQVSWLSKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAVTALNSESNFARAYAQGI
SRTKYWELIYEDSMDLIAKLPCVAAKIYRNLYREGSGIGAIDSNLDWSHNFTNMLGYTDHQFTELTRLYLTIHSDHEGGN
VSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTQLQKEVGKDVSDEKLRDYIWNTLNSGRVVPGYGHAV
LRKTDPRYTCQREFALKHLPNDPMFKLVAQLYKIVPNVLLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRA
LGVLAQLIWSRALGFPLERPKSMSTEGLMKFVDS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;STNLKDILADLIPKEQARIKTFRQQHGKTVVGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGFSIPECQKLLPKAK
GGEEPLPEGLFWLLVTGHIPTEEQVSWLSKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAVTALNSESNFARAYAQGI
SRTKYWELIYEDSMDLIAKLPCVAAKIYRNLYREGSGIGAIDSNLDWSHNFTNMLGYTDHQFTELTRLYLTIHSDHEGGN
VSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTQLQKEVGKDVSDEKLRDYIWNTLNSGRVVPGYGHAV
LRKTDPRYTCQREFALKHLPNDPMFKLVAQLYKIVPNVLLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRA
LGVLAQLIWSRALGFPLERPKSMSTEGLMKFVDS
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'COENZYME A'       COA 
3 'ACETYL GROUP'     ACE 
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 
ACE non-polymer         . 'ACETYL GROUP'     ? 'C2 H4 O'             44.053  
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 
COA non-polymer         . 'COENZYME A'       ? 'C21 H36 N7 O16 P3 S' 767.534 
CYS 'L-peptide linking' y CYSTEINE           ? 'C3 H7 N O2 S'        121.158 
GLN 'L-peptide linking' y GLUTAMINE          ? 'C5 H10 N2 O3'        146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'    ? 'C5 H9 N O4'          147.129 
GLY 'peptide linking'   y GLYCINE            ? 'C2 H5 N O2'          75.067  
HIS 'L-peptide linking' y HISTIDINE          ? 'C6 H10 N3 O2 1'      156.162 
HOH non-polymer         . WATER              ? 'H2 O'                18.015  
ILE 'L-peptide linking' y ISOLEUCINE         ? 'C6 H13 N O2'         131.173 
LEU 'L-peptide linking' y LEUCINE            ? 'C6 H13 N O2'         131.173 
LYS 'L-peptide linking' y LYSINE             ? 'C6 H15 N2 O2 1'      147.195 
MET 'L-peptide linking' y METHIONINE         ? 'C5 H11 N O2 S'       149.211 
OAA non-polymer         . 'OXALOACETATE ION' ? 'C4 H3 O5 -1'         131.064 
PHE 'L-peptide linking' y PHENYLALANINE      ? 'C9 H11 N O2'         165.189 
PRO 'L-peptide linking' y PROLINE            ? 'C5 H9 N O2'          115.130 
SER 'L-peptide linking' y SERINE             ? 'C3 H7 N O3'          105.093 
THR 'L-peptide linking' y THREONINE          ? 'C4 H9 N O3'          119.119 
TRP 'L-peptide linking' y TRYPTOPHAN         ? 'C11 H12 N2 O2'       204.225 
TYR 'L-peptide linking' y TYROSINE           ? 'C9 H11 N O3'         181.189 
VAL 'L-peptide linking' y VALINE             ? 'C5 H11 N O2'         117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   30  30  SER SER A . n 
A 1 2   THR 2   31  31  THR THR A . n 
A 1 3   ASN 3   32  32  ASN ASN A . n 
A 1 4   LEU 4   33  33  LEU LEU A . n 
A 1 5   LYS 5   34  34  LYS LYS A . n 
A 1 6   ASP 6   35  35  ASP ASP A . n 
A 1 7   ILE 7   36  36  ILE ILE A . n 
A 1 8   LEU 8   37  37  LEU LEU A . n 
A 1 9   ALA 9   38  38  ALA ALA A . n 
A 1 10  ASP 10  39  39  ASP ASP A . n 
A 1 11  LEU 11  40  40  LEU LEU A . n 
A 1 12  ILE 12  41  41  ILE ILE A . n 
A 1 13  PRO 13  42  42  PRO PRO A . n 
A 1 14  LYS 14  43  43  LYS LYS A . n 
A 1 15  GLU 15  44  44  GLU GLU A . n 
A 1 16  GLN 16  45  45  GLN GLN A . n 
A 1 17  ALA 17  46  46  ALA ALA A . n 
A 1 18  ARG 18  47  47  ARG ARG A . n 
A 1 19  ILE 19  48  48  ILE ILE A . n 
A 1 20  LYS 20  49  49  LYS LYS A . n 
A 1 21  THR 21  50  50  THR THR A . n 
A 1 22  PHE 22  51  51  PHE PHE A . n 
A 1 23  ARG 23  52  52  ARG ARG A . n 
A 1 24  GLN 24  53  53  GLN GLN A . n 
A 1 25  GLN 25  54  54  GLN GLN A . n 
A 1 26  HIS 26  55  55  HIS HIS A . n 
A 1 27  GLY 27  56  56  GLY GLY A . n 
A 1 28  LYS 28  57  57  LYS LYS A . n 
A 1 29  THR 29  58  58  THR THR A . n 
A 1 30  VAL 30  59  59  VAL VAL A . n 
A 1 31  VAL 31  60  60  VAL VAL A . n 
A 1 32  GLY 32  61  61  GLY GLY A . n 
A 1 33  GLN 33  62  62  GLN GLN A . n 
A 1 34  ILE 34  63  63  ILE ILE A . n 
A 1 35  THR 35  64  64  THR THR A . n 
A 1 36  VAL 36  65  65  VAL VAL A . n 
A 1 37  ASP 37  66  66  ASP ASP A . n 
A 1 38  MET 38  67  67  MET MET A . n 
A 1 39  MET 39  68  68  MET MET A . n 
A 1 40  TYR 40  69  69  TYR TYR A . n 
A 1 41  GLY 41  70  70  GLY GLY A . n 
A 1 42  GLY 42  71  71  GLY GLY A . n 
A 1 43  MET 43  72  72  MET MET A . n 
A 1 44  ARG 44  73  73  ARG ARG A . n 
A 1 45  GLY 45  74  74  GLY GLY A . n 
A 1 46  MET 46  75  75  MET MET A . n 
A 1 47  LYS 47  76  76  LYS LYS A . n 
A 1 48  GLY 48  77  77  GLY GLY A . n 
A 1 49  LEU 49  78  78  LEU LEU A . n 
A 1 50  VAL 50  79  79  VAL VAL A . n 
A 1 51  TYR 51  80  80  TYR TYR A . n 
A 1 52  GLU 52  81  81  GLU GLU A . n 
A 1 53  THR 53  82  82  THR THR A . n 
A 1 54  SER 54  83  83  SER SER A . n 
A 1 55  VAL 55  84  84  VAL VAL A . n 
A 1 56  LEU 56  85  85  LEU LEU A . n 
A 1 57  ASP 57  86  86  ASP ASP A . n 
A 1 58  PRO 58  87  87  PRO PRO A . n 
A 1 59  ASP 59  88  88  ASP ASP A . n 
A 1 60  GLU 60  89  89  GLU GLU A . n 
A 1 61  GLY 61  90  90  GLY GLY A . n 
A 1 62  ILE 62  91  91  ILE ILE A . n 
A 1 63  ARG 63  92  92  ARG ARG A . n 
A 1 64  PHE 64  93  93  PHE PHE A . n 
A 1 65  ARG 65  94  94  ARG ARG A . n 
A 1 66  GLY 66  95  95  GLY GLY A . n 
A 1 67  PHE 67  96  96  PHE PHE A . n 
A 1 68  SER 68  97  97  SER SER A . n 
A 1 69  ILE 69  98  98  ILE ILE A . n 
A 1 70  PRO 70  99  99  PRO PRO A . n 
A 1 71  GLU 71  100 100 GLU GLU A . n 
A 1 72  CYS 72  101 101 CYS CYS A . n 
A 1 73  GLN 73  102 102 GLN GLN A . n 
A 1 74  LYS 74  103 103 LYS LYS A . n 
A 1 75  LEU 75  104 104 LEU LEU A . n 
A 1 76  LEU 76  105 105 LEU LEU A . n 
A 1 77  PRO 77  106 106 PRO PRO A . n 
A 1 78  LYS 78  107 107 LYS LYS A . n 
A 1 79  ALA 79  108 108 ALA ALA A . n 
A 1 80  LYS 80  109 109 LYS LYS A . n 
A 1 81  GLY 81  110 110 GLY GLY A . n 
A 1 82  GLY 82  111 111 GLY GLY A . n 
A 1 83  GLU 83  112 112 GLU GLU A . n 
A 1 84  GLU 84  113 113 GLU GLU A . n 
A 1 85  PRO 85  114 114 PRO PRO A . n 
A 1 86  LEU 86  115 115 LEU LEU A . n 
A 1 87  PRO 87  116 116 PRO PRO A . n 
A 1 88  GLU 88  117 117 GLU GLU A . n 
A 1 89  GLY 89  118 118 GLY GLY A . n 
A 1 90  LEU 90  119 119 LEU LEU A . n 
A 1 91  PHE 91  120 120 PHE PHE A . n 
A 1 92  TRP 92  121 121 TRP TRP A . n 
A 1 93  LEU 93  122 122 LEU LEU A . n 
A 1 94  LEU 94  123 123 LEU LEU A . n 
A 1 95  VAL 95  124 124 VAL VAL A . n 
A 1 96  THR 96  125 125 THR THR A . n 
A 1 97  GLY 97  126 126 GLY GLY A . n 
A 1 98  HIS 98  127 127 HIS HIS A . n 
A 1 99  ILE 99  128 128 ILE ILE A . n 
A 1 100 PRO 100 129 129 PRO PRO A . n 
A 1 101 THR 101 130 130 THR THR A . n 
A 1 102 GLU 102 131 131 GLU GLU A . n 
A 1 103 GLU 103 132 132 GLU GLU A . n 
A 1 104 GLN 104 133 133 GLN GLN A . n 
A 1 105 VAL 105 134 134 VAL VAL A . n 
A 1 106 SER 106 135 135 SER SER A . n 
A 1 107 TRP 107 136 136 TRP TRP A . n 
A 1 108 LEU 108 137 137 LEU LEU A . n 
A 1 109 SER 109 138 138 SER SER A . n 
A 1 110 LYS 110 139 139 LYS LYS A . n 
A 1 111 GLU 111 140 140 GLU GLU A . n 
A 1 112 TRP 112 141 141 TRP TRP A . n 
A 1 113 ALA 113 142 142 ALA ALA A . n 
A 1 114 LYS 114 143 143 LYS LYS A . n 
A 1 115 ARG 115 144 144 ARG ARG A . n 
A 1 116 ALA 116 145 145 ALA ALA A . n 
A 1 117 ALA 117 146 146 ALA ALA A . n 
A 1 118 LEU 118 147 147 LEU LEU A . n 
A 1 119 PRO 119 148 148 PRO PRO A . n 
A 1 120 SER 120 149 149 SER SER A . n 
A 1 121 HIS 121 150 150 HIS HIS A . n 
A 1 122 VAL 122 151 151 VAL VAL A . n 
A 1 123 VAL 123 152 152 VAL VAL A . n 
A 1 124 THR 124 153 153 THR THR A . n 
A 1 125 MET 125 154 154 MET MET A . n 
A 1 126 LEU 126 155 155 LEU LEU A . n 
A 1 127 ASP 127 156 156 ASP ASP A . n 
A 1 128 ASN 128 157 157 ASN ASN A . n 
A 1 129 PHE 129 158 158 PHE PHE A . n 
A 1 130 PRO 130 159 159 PRO PRO A . n 
A 1 131 THR 131 160 160 THR THR A . n 
A 1 132 ASN 132 161 161 ASN ASN A . n 
A 1 133 LEU 133 162 162 LEU LEU A . n 
A 1 134 HIS 134 163 163 HIS HIS A . n 
A 1 135 PRO 135 164 164 PRO PRO A . n 
A 1 136 MET 136 165 165 MET MET A . n 
A 1 137 SER 137 166 166 SER SER A . n 
A 1 138 GLN 138 167 167 GLN GLN A . n 
A 1 139 LEU 139 168 168 LEU LEU A . n 
A 1 140 SER 140 169 169 SER SER A . n 
A 1 141 ALA 141 170 170 ALA ALA A . n 
A 1 142 ALA 142 171 171 ALA ALA A . n 
A 1 143 VAL 143 172 172 VAL VAL A . n 
A 1 144 THR 144 173 173 THR THR A . n 
A 1 145 ALA 145 174 174 ALA ALA A . n 
A 1 146 LEU 146 175 175 LEU LEU A . n 
A 1 147 ASN 147 176 176 ASN ASN A . n 
A 1 148 SER 148 177 177 SER SER A . n 
A 1 149 GLU 149 178 178 GLU GLU A . n 
A 1 150 SER 150 179 179 SER SER A . n 
A 1 151 ASN 151 180 180 ASN ASN A . n 
A 1 152 PHE 152 181 181 PHE PHE A . n 
A 1 153 ALA 153 182 182 ALA ALA A . n 
A 1 154 ARG 154 183 183 ARG ARG A . n 
A 1 155 ALA 155 184 184 ALA ALA A . n 
A 1 156 TYR 156 185 185 TYR TYR A . n 
A 1 157 ALA 157 186 186 ALA ALA A . n 
A 1 158 GLN 158 187 187 GLN GLN A . n 
A 1 159 GLY 159 188 188 GLY GLY A . n 
A 1 160 ILE 160 189 189 ILE ILE A . n 
A 1 161 SER 161 190 190 SER SER A . n 
A 1 162 ARG 162 191 191 ARG ARG A . n 
A 1 163 THR 163 192 192 THR THR A . n 
A 1 164 LYS 164 193 193 LYS LYS A . n 
A 1 165 TYR 165 194 194 TYR TYR A . n 
A 1 166 TRP 166 195 195 TRP TRP A . n 
A 1 167 GLU 167 196 196 GLU GLU A . n 
A 1 168 LEU 168 197 197 LEU LEU A . n 
A 1 169 ILE 169 198 198 ILE ILE A . n 
A 1 170 TYR 170 199 199 TYR TYR A . n 
A 1 171 GLU 171 200 200 GLU GLU A . n 
A 1 172 ASP 172 201 201 ASP ASP A . n 
A 1 173 SER 173 202 202 SER SER A . n 
A 1 174 MET 174 203 203 MET MET A . n 
A 1 175 ASP 175 204 204 ASP ASP A . n 
A 1 176 LEU 176 205 205 LEU LEU A . n 
A 1 177 ILE 177 206 206 ILE ILE A . n 
A 1 178 ALA 178 207 207 ALA ALA A . n 
A 1 179 LYS 179 208 208 LYS LYS A . n 
A 1 180 LEU 180 209 209 LEU LEU A . n 
A 1 181 PRO 181 210 210 PRO PRO A . n 
A 1 182 CYS 182 211 211 CYS CYS A . n 
A 1 183 VAL 183 212 212 VAL VAL A . n 
A 1 184 ALA 184 213 213 ALA ALA A . n 
A 1 185 ALA 185 214 214 ALA ALA A . n 
A 1 186 LYS 186 215 215 LYS LYS A . n 
A 1 187 ILE 187 216 216 ILE ILE A . n 
A 1 188 TYR 188 217 217 TYR TYR A . n 
A 1 189 ARG 189 218 218 ARG ARG A . n 
A 1 190 ASN 190 219 219 ASN ASN A . n 
A 1 191 LEU 191 220 220 LEU LEU A . n 
A 1 192 TYR 192 221 221 TYR TYR A . n 
A 1 193 ARG 193 222 222 ARG ARG A . n 
A 1 194 GLU 194 223 223 GLU GLU A . n 
A 1 195 GLY 195 224 224 GLY GLY A . n 
A 1 196 SER 196 225 225 SER SER A . n 
A 1 197 GLY 197 226 226 GLY GLY A . n 
A 1 198 ILE 198 227 227 ILE ILE A . n 
A 1 199 GLY 199 228 228 GLY GLY A . n 
A 1 200 ALA 200 229 229 ALA ALA A . n 
A 1 201 ILE 201 230 230 ILE ILE A . n 
A 1 202 ASP 202 231 231 ASP ASP A . n 
A 1 203 SER 203 232 232 SER SER A . n 
A 1 204 ASN 204 233 233 ASN ASN A . n 
A 1 205 LEU 205 234 234 LEU LEU A . n 
A 1 206 ASP 206 235 235 ASP ASP A . n 
A 1 207 TRP 207 236 236 TRP TRP A . n 
A 1 208 SER 208 237 237 SER SER A . n 
A 1 209 HIS 209 238 238 HIS HIS A . n 
A 1 210 ASN 210 239 239 ASN ASN A . n 
A 1 211 PHE 211 240 240 PHE PHE A . n 
A 1 212 THR 212 241 241 THR THR A . n 
A 1 213 ASN 213 242 242 ASN ASN A . n 
A 1 214 MET 214 243 243 MET MET A . n 
A 1 215 LEU 215 244 244 LEU LEU A . n 
A 1 216 GLY 216 245 245 GLY GLY A . n 
A 1 217 TYR 217 246 246 TYR TYR A . n 
A 1 218 THR 218 247 247 THR THR A . n 
A 1 219 ASP 219 248 248 ASP ASP A . n 
A 1 220 HIS 220 249 249 HIS HIS A . n 
A 1 221 GLN 221 250 250 GLN GLN A . n 
A 1 222 PHE 222 251 251 PHE PHE A . n 
A 1 223 THR 223 252 252 THR THR A . n 
A 1 224 GLU 224 253 253 GLU GLU A . n 
A 1 225 LEU 225 254 254 LEU LEU A . n 
A 1 226 THR 226 255 255 THR THR A . n 
A 1 227 ARG 227 256 256 ARG ARG A . n 
A 1 228 LEU 228 257 257 LEU LEU A . n 
A 1 229 TYR 229 258 258 TYR TYR A . n 
A 1 230 LEU 230 259 259 LEU LEU A . n 
A 1 231 THR 231 260 260 THR THR A . n 
A 1 232 ILE 232 261 261 ILE ILE A . n 
A 1 233 HIS 233 262 262 HIS HIS A . n 
A 1 234 SER 234 263 263 SER SER A . n 
A 1 235 ASP 235 264 264 ASP ASP A . n 
A 1 236 HIS 236 265 265 HIS HIS A . n 
A 1 237 GLU 237 266 266 GLU GLU A . n 
A 1 238 GLY 238 267 267 GLY GLY A . n 
A 1 239 GLY 239 268 268 GLY GLY A . n 
A 1 240 ASN 240 269 269 ASN ASN A . n 
A 1 241 VAL 241 270 270 VAL VAL A . n 
A 1 242 SER 242 271 271 SER SER A . n 
A 1 243 ALA 243 272 272 ALA ALA A . n 
A 1 244 HIS 244 273 273 HIS HIS A . n 
A 1 245 THR 245 274 274 THR THR A . n 
A 1 246 SER 246 275 275 SER SER A . n 
A 1 247 HIS 247 276 276 HIS HIS A . n 
A 1 248 LEU 248 277 277 LEU LEU A . n 
A 1 249 VAL 249 278 278 VAL VAL A . n 
A 1 250 GLY 250 279 279 GLY GLY A . n 
A 1 251 SER 251 280 280 SER SER A . n 
A 1 252 ALA 252 281 281 ALA ALA A . n 
A 1 253 LEU 253 282 282 LEU LEU A . n 
A 1 254 SER 254 283 283 SER SER A . n 
A 1 255 ASP 255 284 284 ASP ASP A . n 
A 1 256 PRO 256 285 285 PRO PRO A . n 
A 1 257 TYR 257 286 286 TYR TYR A . n 
A 1 258 LEU 258 287 287 LEU LEU A . n 
A 1 259 SER 259 288 288 SER SER A . n 
A 1 260 PHE 260 289 289 PHE PHE A . n 
A 1 261 ALA 261 290 290 ALA ALA A . n 
A 1 262 ALA 262 291 291 ALA ALA A . n 
A 1 263 ALA 263 292 292 ALA ALA A . n 
A 1 264 MET 264 293 293 MET MET A . n 
A 1 265 ASN 265 294 294 ASN ASN A . n 
A 1 266 GLY 266 295 295 GLY GLY A . n 
A 1 267 LEU 267 296 296 LEU LEU A . n 
A 1 268 ALA 268 297 297 ALA ALA A . n 
A 1 269 GLY 269 298 298 GLY GLY A . n 
A 1 270 PRO 270 299 299 PRO PRO A . n 
A 1 271 LEU 271 300 300 LEU LEU A . n 
A 1 272 HIS 272 301 301 HIS HIS A . n 
A 1 273 GLY 273 302 302 GLY GLY A . n 
A 1 274 LEU 274 303 303 LEU LEU A . n 
A 1 275 ALA 275 304 304 ALA ALA A . n 
A 1 276 ASN 276 305 305 ASN ASN A . n 
A 1 277 GLN 277 306 306 GLN GLN A . n 
A 1 278 GLU 278 307 307 GLU GLU A . n 
A 1 279 VAL 279 308 308 VAL VAL A . n 
A 1 280 LEU 280 309 309 LEU LEU A . n 
A 1 281 VAL 281 310 310 VAL VAL A . n 
A 1 282 TRP 282 311 311 TRP TRP A . n 
A 1 283 LEU 283 312 312 LEU LEU A . n 
A 1 284 THR 284 313 313 THR THR A . n 
A 1 285 GLN 285 314 314 GLN GLN A . n 
A 1 286 LEU 286 315 315 LEU LEU A . n 
A 1 287 GLN 287 316 316 GLN GLN A . n 
A 1 288 LYS 288 317 317 LYS LYS A . n 
A 1 289 GLU 289 318 318 GLU GLU A . n 
A 1 290 VAL 290 319 319 VAL VAL A . n 
A 1 291 GLY 291 320 320 GLY GLY A . n 
A 1 292 LYS 292 321 321 LYS LYS A . n 
A 1 293 ASP 293 322 322 ASP ASP A . n 
A 1 294 VAL 294 323 323 VAL VAL A . n 
A 1 295 SER 295 324 324 SER SER A . n 
A 1 296 ASP 296 325 325 ASP ASP A . n 
A 1 297 GLU 297 326 326 GLU GLU A . n 
A 1 298 LYS 298 327 327 LYS LYS A . n 
A 1 299 LEU 299 328 328 LEU LEU A . n 
A 1 300 ARG 300 329 329 ARG ARG A . n 
A 1 301 ASP 301 330 330 ASP ASP A . n 
A 1 302 TYR 302 331 331 TYR TYR A . n 
A 1 303 ILE 303 332 332 ILE ILE A . n 
A 1 304 TRP 304 333 333 TRP TRP A . n 
A 1 305 ASN 305 334 334 ASN ASN A . n 
A 1 306 THR 306 335 335 THR THR A . n 
A 1 307 LEU 307 336 336 LEU LEU A . n 
A 1 308 ASN 308 337 337 ASN ASN A . n 
A 1 309 SER 309 338 338 SER SER A . n 
A 1 310 GLY 310 339 339 GLY GLY A . n 
A 1 311 ARG 311 340 340 ARG ARG A . n 
A 1 312 VAL 312 341 341 VAL VAL A . n 
A 1 313 VAL 313 342 342 VAL VAL A . n 
A 1 314 PRO 314 343 343 PRO PRO A . n 
A 1 315 GLY 315 344 344 GLY GLY A . n 
A 1 316 TYR 316 345 345 TYR TYR A . n 
A 1 317 GLY 317 346 346 GLY GLY A . n 
A 1 318 HIS 318 347 347 HIS HIS A . n 
A 1 319 ALA 319 348 348 ALA ALA A . n 
A 1 320 VAL 320 349 349 VAL VAL A . n 
A 1 321 LEU 321 350 350 LEU LEU A . n 
A 1 322 ARG 322 351 351 ARG ARG A . n 
A 1 323 LYS 323 352 352 LYS LYS A . n 
A 1 324 THR 324 353 353 THR THR A . n 
A 1 325 ASP 325 354 354 ASP ASP A . n 
A 1 326 PRO 326 355 355 PRO PRO A . n 
A 1 327 ARG 327 356 356 ARG ARG A . n 
A 1 328 TYR 328 357 357 TYR TYR A . n 
A 1 329 THR 329 358 358 THR THR A . n 
A 1 330 CYS 330 359 359 CYS CYS A . n 
A 1 331 GLN 331 360 360 GLN GLN A . n 
A 1 332 ARG 332 361 361 ARG ARG A . n 
A 1 333 GLU 333 362 362 GLU GLU A . n 
A 1 334 PHE 334 363 363 PHE PHE A . n 
A 1 335 ALA 335 364 364 ALA ALA A . n 
A 1 336 LEU 336 365 365 LEU LEU A . n 
A 1 337 LYS 337 366 366 LYS LYS A . n 
A 1 338 HIS 338 367 367 HIS HIS A . n 
A 1 339 LEU 339 368 368 LEU LEU A . n 
A 1 340 PRO 340 369 369 PRO PRO A . n 
A 1 341 ASN 341 370 370 ASN ASN A . n 
A 1 342 ASP 342 371 371 ASP ASP A . n 
A 1 343 PRO 343 372 372 PRO PRO A . n 
A 1 344 MET 344 373 373 MET MET A . n 
A 1 345 PHE 345 374 374 PHE PHE A . n 
A 1 346 LYS 346 375 375 LYS LYS A . n 
A 1 347 LEU 347 376 376 LEU LEU A . n 
A 1 348 VAL 348 377 377 VAL VAL A . n 
A 1 349 ALA 349 378 378 ALA ALA A . n 
A 1 350 GLN 350 379 379 GLN GLN A . n 
A 1 351 LEU 351 380 380 LEU LEU A . n 
A 1 352 TYR 352 381 381 TYR TYR A . n 
A 1 353 LYS 353 382 382 LYS LYS A . n 
A 1 354 ILE 354 383 383 ILE ILE A . n 
A 1 355 VAL 355 384 384 VAL VAL A . n 
A 1 356 PRO 356 385 385 PRO PRO A . n 
A 1 357 ASN 357 386 386 ASN ASN A . n 
A 1 358 VAL 358 387 387 VAL VAL A . n 
A 1 359 LEU 359 388 388 LEU LEU A . n 
A 1 360 LEU 360 389 389 LEU LEU A . n 
A 1 361 GLU 361 390 390 GLU GLU A . n 
A 1 362 GLN 362 391 391 GLN GLN A . n 
A 1 363 GLY 363 392 392 GLY GLY A . n 
A 1 364 LYS 364 393 393 LYS LYS A . n 
A 1 365 ALA 365 394 394 ALA ALA A . n 
A 1 366 LYS 366 395 395 LYS LYS A . n 
A 1 367 ASN 367 396 396 ASN ASN A . n 
A 1 368 PRO 368 397 397 PRO PRO A . n 
A 1 369 TRP 369 398 398 TRP TRP A . n 
A 1 370 PRO 370 399 399 PRO PRO A . n 
A 1 371 ASN 371 400 400 ASN ASN A . n 
A 1 372 VAL 372 401 401 VAL VAL A . n 
A 1 373 ASP 373 402 402 ASP ASP A . n 
A 1 374 ALA 374 403 403 ALA ALA A . n 
A 1 375 HIS 375 404 404 HIS HIS A . n 
A 1 376 SER 376 405 405 SER SER A . n 
A 1 377 GLY 377 406 406 GLY GLY A . n 
A 1 378 VAL 378 407 407 VAL VAL A . n 
A 1 379 LEU 379 408 408 LEU LEU A . n 
A 1 380 LEU 380 409 409 LEU LEU A . n 
A 1 381 GLN 381 410 410 GLN GLN A . n 
A 1 382 TYR 382 411 411 TYR TYR A . n 
A 1 383 TYR 383 412 412 TYR TYR A . n 
A 1 384 GLY 384 413 413 GLY GLY A . n 
A 1 385 MET 385 414 414 MET MET A . n 
A 1 386 THR 386 415 415 THR THR A . n 
A 1 387 GLU 387 416 416 GLU GLU A . n 
A 1 388 MET 388 417 417 MET MET A . n 
A 1 389 ASN 389 418 418 ASN ASN A . n 
A 1 390 TYR 390 419 419 TYR TYR A . n 
A 1 391 TYR 391 420 420 TYR TYR A . n 
A 1 392 THR 392 421 421 THR THR A . n 
A 1 393 VAL 393 422 422 VAL VAL A . n 
A 1 394 LEU 394 423 423 LEU LEU A . n 
A 1 395 PHE 395 424 424 PHE PHE A . n 
A 1 396 GLY 396 425 425 GLY GLY A . n 
A 1 397 VAL 397 426 426 VAL VAL A . n 
A 1 398 SER 398 427 427 SER SER A . n 
A 1 399 ARG 399 428 428 ARG ARG A . n 
A 1 400 ALA 400 429 429 ALA ALA A . n 
A 1 401 LEU 401 430 430 LEU LEU A . n 
A 1 402 GLY 402 431 431 GLY GLY A . n 
A 1 403 VAL 403 432 432 VAL VAL A . n 
A 1 404 LEU 404 433 433 LEU LEU A . n 
A 1 405 ALA 405 434 434 ALA ALA A . n 
A 1 406 GLN 406 435 435 GLN GLN A . n 
A 1 407 LEU 407 436 436 LEU LEU A . n 
A 1 408 ILE 408 437 437 ILE ILE A . n 
A 1 409 TRP 409 438 438 TRP TRP A . n 
A 1 410 SER 410 439 439 SER SER A . n 
A 1 411 ARG 411 440 440 ARG ARG A . n 
A 1 412 ALA 412 441 441 ALA ALA A . n 
A 1 413 LEU 413 442 442 LEU LEU A . n 
A 1 414 GLY 414 443 443 GLY GLY A . n 
A 1 415 PHE 415 444 444 PHE PHE A . n 
A 1 416 PRO 416 445 445 PRO PRO A . n 
A 1 417 LEU 417 446 446 LEU LEU A . n 
A 1 418 GLU 418 447 447 GLU GLU A . n 
A 1 419 ARG 419 448 448 ARG ARG A . n 
A 1 420 PRO 420 449 449 PRO PRO A . n 
A 1 421 LYS 421 450 450 LYS LYS A . n 
A 1 422 SER 422 451 451 SER SER A . n 
A 1 423 MET 423 452 452 MET MET A . n 
A 1 424 SER 424 453 453 SER SER A . n 
A 1 425 THR 425 454 454 THR THR A . n 
A 1 426 GLU 426 455 455 GLU GLU A . n 
A 1 427 GLY 427 456 456 GLY GLY A . n 
A 1 428 LEU 428 457 457 LEU LEU A . n 
A 1 429 MET 429 458 458 MET MET A . n 
A 1 430 LYS 430 459 459 LYS LYS A . n 
A 1 431 PHE 431 460 460 PHE PHE A . n 
A 1 432 VAL 432 461 461 VAL VAL A . n 
A 1 433 ASP 433 462 462 ASP ASP A . n 
A 1 434 SER 434 463 463 SER SER A . n 
B 1 1   SER 1   30  30  SER SER B . n 
B 1 2   THR 2   31  31  THR THR B . n 
B 1 3   ASN 3   32  32  ASN ASN B . n 
B 1 4   LEU 4   33  33  LEU LEU B . n 
B 1 5   LYS 5   34  34  LYS LYS B . n 
B 1 6   ASP 6   35  35  ASP ASP B . n 
B 1 7   ILE 7   36  36  ILE ILE B . n 
B 1 8   LEU 8   37  37  LEU LEU B . n 
B 1 9   ALA 9   38  38  ALA ALA B . n 
B 1 10  ASP 10  39  39  ASP ASP B . n 
B 1 11  LEU 11  40  40  LEU LEU B . n 
B 1 12  ILE 12  41  41  ILE ILE B . n 
B 1 13  PRO 13  42  42  PRO PRO B . n 
B 1 14  LYS 14  43  43  LYS LYS B . n 
B 1 15  GLU 15  44  44  GLU GLU B . n 
B 1 16  GLN 16  45  45  GLN GLN B . n 
B 1 17  ALA 17  46  46  ALA ALA B . n 
B 1 18  ARG 18  47  47  ARG ARG B . n 
B 1 19  ILE 19  48  48  ILE ILE B . n 
B 1 20  LYS 20  49  49  LYS LYS B . n 
B 1 21  THR 21  50  50  THR THR B . n 
B 1 22  PHE 22  51  51  PHE PHE B . n 
B 1 23  ARG 23  52  52  ARG ARG B . n 
B 1 24  GLN 24  53  53  GLN GLN B . n 
B 1 25  GLN 25  54  54  GLN GLN B . n 
B 1 26  HIS 26  55  55  HIS HIS B . n 
B 1 27  GLY 27  56  56  GLY GLY B . n 
B 1 28  LYS 28  57  57  LYS LYS B . n 
B 1 29  THR 29  58  58  THR THR B . n 
B 1 30  VAL 30  59  59  VAL VAL B . n 
B 1 31  VAL 31  60  60  VAL VAL B . n 
B 1 32  GLY 32  61  61  GLY GLY B . n 
B 1 33  GLN 33  62  62  GLN GLN B . n 
B 1 34  ILE 34  63  63  ILE ILE B . n 
B 1 35  THR 35  64  64  THR THR B . n 
B 1 36  VAL 36  65  65  VAL VAL B . n 
B 1 37  ASP 37  66  66  ASP ASP B . n 
B 1 38  MET 38  67  67  MET MET B . n 
B 1 39  MET 39  68  68  MET MET B . n 
B 1 40  TYR 40  69  69  TYR TYR B . n 
B 1 41  GLY 41  70  70  GLY GLY B . n 
B 1 42  GLY 42  71  71  GLY GLY B . n 
B 1 43  MET 43  72  72  MET MET B . n 
B 1 44  ARG 44  73  73  ARG ARG B . n 
B 1 45  GLY 45  74  74  GLY GLY B . n 
B 1 46  MET 46  75  75  MET MET B . n 
B 1 47  LYS 47  76  76  LYS LYS B . n 
B 1 48  GLY 48  77  77  GLY GLY B . n 
B 1 49  LEU 49  78  78  LEU LEU B . n 
B 1 50  VAL 50  79  79  VAL VAL B . n 
B 1 51  TYR 51  80  80  TYR TYR B . n 
B 1 52  GLU 52  81  81  GLU GLU B . n 
B 1 53  THR 53  82  82  THR THR B . n 
B 1 54  SER 54  83  83  SER SER B . n 
B 1 55  VAL 55  84  84  VAL VAL B . n 
B 1 56  LEU 56  85  85  LEU LEU B . n 
B 1 57  ASP 57  86  86  ASP ASP B . n 
B 1 58  PRO 58  87  87  PRO PRO B . n 
B 1 59  ASP 59  88  88  ASP ASP B . n 
B 1 60  GLU 60  89  89  GLU GLU B . n 
B 1 61  GLY 61  90  90  GLY GLY B . n 
B 1 62  ILE 62  91  91  ILE ILE B . n 
B 1 63  ARG 63  92  92  ARG ARG B . n 
B 1 64  PHE 64  93  93  PHE PHE B . n 
B 1 65  ARG 65  94  94  ARG ARG B . n 
B 1 66  GLY 66  95  95  GLY GLY B . n 
B 1 67  PHE 67  96  96  PHE PHE B . n 
B 1 68  SER 68  97  97  SER SER B . n 
B 1 69  ILE 69  98  98  ILE ILE B . n 
B 1 70  PRO 70  99  99  PRO PRO B . n 
B 1 71  GLU 71  100 100 GLU GLU B . n 
B 1 72  CYS 72  101 101 CYS CYS B . n 
B 1 73  GLN 73  102 102 GLN GLN B . n 
B 1 74  LYS 74  103 103 LYS LYS B . n 
B 1 75  LEU 75  104 104 LEU LEU B . n 
B 1 76  LEU 76  105 105 LEU LEU B . n 
B 1 77  PRO 77  106 106 PRO PRO B . n 
B 1 78  LYS 78  107 107 LYS LYS B . n 
B 1 79  ALA 79  108 108 ALA ALA B . n 
B 1 80  LYS 80  109 109 LYS LYS B . n 
B 1 81  GLY 81  110 110 GLY GLY B . n 
B 1 82  GLY 82  111 111 GLY GLY B . n 
B 1 83  GLU 83  112 112 GLU GLU B . n 
B 1 84  GLU 84  113 113 GLU GLU B . n 
B 1 85  PRO 85  114 114 PRO PRO B . n 
B 1 86  LEU 86  115 115 LEU LEU B . n 
B 1 87  PRO 87  116 116 PRO PRO B . n 
B 1 88  GLU 88  117 117 GLU GLU B . n 
B 1 89  GLY 89  118 118 GLY GLY B . n 
B 1 90  LEU 90  119 119 LEU LEU B . n 
B 1 91  PHE 91  120 120 PHE PHE B . n 
B 1 92  TRP 92  121 121 TRP TRP B . n 
B 1 93  LEU 93  122 122 LEU LEU B . n 
B 1 94  LEU 94  123 123 LEU LEU B . n 
B 1 95  VAL 95  124 124 VAL VAL B . n 
B 1 96  THR 96  125 125 THR THR B . n 
B 1 97  GLY 97  126 126 GLY GLY B . n 
B 1 98  HIS 98  127 127 HIS HIS B . n 
B 1 99  ILE 99  128 128 ILE ILE B . n 
B 1 100 PRO 100 129 129 PRO PRO B . n 
B 1 101 THR 101 130 130 THR THR B . n 
B 1 102 GLU 102 131 131 GLU GLU B . n 
B 1 103 GLU 103 132 132 GLU GLU B . n 
B 1 104 GLN 104 133 133 GLN GLN B . n 
B 1 105 VAL 105 134 134 VAL VAL B . n 
B 1 106 SER 106 135 135 SER SER B . n 
B 1 107 TRP 107 136 136 TRP TRP B . n 
B 1 108 LEU 108 137 137 LEU LEU B . n 
B 1 109 SER 109 138 138 SER SER B . n 
B 1 110 LYS 110 139 139 LYS LYS B . n 
B 1 111 GLU 111 140 140 GLU GLU B . n 
B 1 112 TRP 112 141 141 TRP TRP B . n 
B 1 113 ALA 113 142 142 ALA ALA B . n 
B 1 114 LYS 114 143 143 LYS LYS B . n 
B 1 115 ARG 115 144 144 ARG ARG B . n 
B 1 116 ALA 116 145 145 ALA ALA B . n 
B 1 117 ALA 117 146 146 ALA ALA B . n 
B 1 118 LEU 118 147 147 LEU LEU B . n 
B 1 119 PRO 119 148 148 PRO PRO B . n 
B 1 120 SER 120 149 149 SER SER B . n 
B 1 121 HIS 121 150 150 HIS HIS B . n 
B 1 122 VAL 122 151 151 VAL VAL B . n 
B 1 123 VAL 123 152 152 VAL VAL B . n 
B 1 124 THR 124 153 153 THR THR B . n 
B 1 125 MET 125 154 154 MET MET B . n 
B 1 126 LEU 126 155 155 LEU LEU B . n 
B 1 127 ASP 127 156 156 ASP ASP B . n 
B 1 128 ASN 128 157 157 ASN ASN B . n 
B 1 129 PHE 129 158 158 PHE PHE B . n 
B 1 130 PRO 130 159 159 PRO PRO B . n 
B 1 131 THR 131 160 160 THR THR B . n 
B 1 132 ASN 132 161 161 ASN ASN B . n 
B 1 133 LEU 133 162 162 LEU LEU B . n 
B 1 134 HIS 134 163 163 HIS HIS B . n 
B 1 135 PRO 135 164 164 PRO PRO B . n 
B 1 136 MET 136 165 165 MET MET B . n 
B 1 137 SER 137 166 166 SER SER B . n 
B 1 138 GLN 138 167 167 GLN GLN B . n 
B 1 139 LEU 139 168 168 LEU LEU B . n 
B 1 140 SER 140 169 169 SER SER B . n 
B 1 141 ALA 141 170 170 ALA ALA B . n 
B 1 142 ALA 142 171 171 ALA ALA B . n 
B 1 143 VAL 143 172 172 VAL VAL B . n 
B 1 144 THR 144 173 173 THR THR B . n 
B 1 145 ALA 145 174 174 ALA ALA B . n 
B 1 146 LEU 146 175 175 LEU LEU B . n 
B 1 147 ASN 147 176 176 ASN ASN B . n 
B 1 148 SER 148 177 177 SER SER B . n 
B 1 149 GLU 149 178 178 GLU GLU B . n 
B 1 150 SER 150 179 179 SER SER B . n 
B 1 151 ASN 151 180 180 ASN ASN B . n 
B 1 152 PHE 152 181 181 PHE PHE B . n 
B 1 153 ALA 153 182 182 ALA ALA B . n 
B 1 154 ARG 154 183 183 ARG ARG B . n 
B 1 155 ALA 155 184 184 ALA ALA B . n 
B 1 156 TYR 156 185 185 TYR TYR B . n 
B 1 157 ALA 157 186 186 ALA ALA B . n 
B 1 158 GLN 158 187 187 GLN GLN B . n 
B 1 159 GLY 159 188 188 GLY GLY B . n 
B 1 160 ILE 160 189 189 ILE ILE B . n 
B 1 161 SER 161 190 190 SER SER B . n 
B 1 162 ARG 162 191 191 ARG ARG B . n 
B 1 163 THR 163 192 192 THR THR B . n 
B 1 164 LYS 164 193 193 LYS LYS B . n 
B 1 165 TYR 165 194 194 TYR TYR B . n 
B 1 166 TRP 166 195 195 TRP TRP B . n 
B 1 167 GLU 167 196 196 GLU GLU B . n 
B 1 168 LEU 168 197 197 LEU LEU B . n 
B 1 169 ILE 169 198 198 ILE ILE B . n 
B 1 170 TYR 170 199 199 TYR TYR B . n 
B 1 171 GLU 171 200 200 GLU GLU B . n 
B 1 172 ASP 172 201 201 ASP ASP B . n 
B 1 173 SER 173 202 202 SER SER B . n 
B 1 174 MET 174 203 203 MET MET B . n 
B 1 175 ASP 175 204 204 ASP ASP B . n 
B 1 176 LEU 176 205 205 LEU LEU B . n 
B 1 177 ILE 177 206 206 ILE ILE B . n 
B 1 178 ALA 178 207 207 ALA ALA B . n 
B 1 179 LYS 179 208 208 LYS LYS B . n 
B 1 180 LEU 180 209 209 LEU LEU B . n 
B 1 181 PRO 181 210 210 PRO PRO B . n 
B 1 182 CYS 182 211 211 CYS CYS B . n 
B 1 183 VAL 183 212 212 VAL VAL B . n 
B 1 184 ALA 184 213 213 ALA ALA B . n 
B 1 185 ALA 185 214 214 ALA ALA B . n 
B 1 186 LYS 186 215 215 LYS LYS B . n 
B 1 187 ILE 187 216 216 ILE ILE B . n 
B 1 188 TYR 188 217 217 TYR TYR B . n 
B 1 189 ARG 189 218 218 ARG ARG B . n 
B 1 190 ASN 190 219 219 ASN ASN B . n 
B 1 191 LEU 191 220 220 LEU LEU B . n 
B 1 192 TYR 192 221 221 TYR TYR B . n 
B 1 193 ARG 193 222 222 ARG ARG B . n 
B 1 194 GLU 194 223 223 GLU GLU B . n 
B 1 195 GLY 195 224 224 GLY GLY B . n 
B 1 196 SER 196 225 225 SER SER B . n 
B 1 197 GLY 197 226 226 GLY GLY B . n 
B 1 198 ILE 198 227 227 ILE ILE B . n 
B 1 199 GLY 199 228 228 GLY GLY B . n 
B 1 200 ALA 200 229 229 ALA ALA B . n 
B 1 201 ILE 201 230 230 ILE ILE B . n 
B 1 202 ASP 202 231 231 ASP ASP B . n 
B 1 203 SER 203 232 232 SER SER B . n 
B 1 204 ASN 204 233 233 ASN ASN B . n 
B 1 205 LEU 205 234 234 LEU LEU B . n 
B 1 206 ASP 206 235 235 ASP ASP B . n 
B 1 207 TRP 207 236 236 TRP TRP B . n 
B 1 208 SER 208 237 237 SER SER B . n 
B 1 209 HIS 209 238 238 HIS HIS B . n 
B 1 210 ASN 210 239 239 ASN ASN B . n 
B 1 211 PHE 211 240 240 PHE PHE B . n 
B 1 212 THR 212 241 241 THR THR B . n 
B 1 213 ASN 213 242 242 ASN ASN B . n 
B 1 214 MET 214 243 243 MET MET B . n 
B 1 215 LEU 215 244 244 LEU LEU B . n 
B 1 216 GLY 216 245 245 GLY GLY B . n 
B 1 217 TYR 217 246 246 TYR TYR B . n 
B 1 218 THR 218 247 247 THR THR B . n 
B 1 219 ASP 219 248 248 ASP ASP B . n 
B 1 220 HIS 220 249 249 HIS HIS B . n 
B 1 221 GLN 221 250 250 GLN GLN B . n 
B 1 222 PHE 222 251 251 PHE PHE B . n 
B 1 223 THR 223 252 252 THR THR B . n 
B 1 224 GLU 224 253 253 GLU GLU B . n 
B 1 225 LEU 225 254 254 LEU LEU B . n 
B 1 226 THR 226 255 255 THR THR B . n 
B 1 227 ARG 227 256 256 ARG ARG B . n 
B 1 228 LEU 228 257 257 LEU LEU B . n 
B 1 229 TYR 229 258 258 TYR TYR B . n 
B 1 230 LEU 230 259 259 LEU LEU B . n 
B 1 231 THR 231 260 260 THR THR B . n 
B 1 232 ILE 232 261 261 ILE ILE B . n 
B 1 233 HIS 233 262 262 HIS HIS B . n 
B 1 234 SER 234 263 263 SER SER B . n 
B 1 235 ASP 235 264 264 ASP ASP B . n 
B 1 236 HIS 236 265 265 HIS HIS B . n 
B 1 237 GLU 237 266 266 GLU GLU B . n 
B 1 238 GLY 238 267 267 GLY GLY B . n 
B 1 239 GLY 239 268 268 GLY GLY B . n 
B 1 240 ASN 240 269 269 ASN ASN B . n 
B 1 241 VAL 241 270 270 VAL VAL B . n 
B 1 242 SER 242 271 271 SER SER B . n 
B 1 243 ALA 243 272 272 ALA ALA B . n 
B 1 244 HIS 244 273 273 HIS HIS B . n 
B 1 245 THR 245 274 274 THR THR B . n 
B 1 246 SER 246 275 275 SER SER B . n 
B 1 247 HIS 247 276 276 HIS HIS B . n 
B 1 248 LEU 248 277 277 LEU LEU B . n 
B 1 249 VAL 249 278 278 VAL VAL B . n 
B 1 250 GLY 250 279 279 GLY GLY B . n 
B 1 251 SER 251 280 280 SER SER B . n 
B 1 252 ALA 252 281 281 ALA ALA B . n 
B 1 253 LEU 253 282 282 LEU LEU B . n 
B 1 254 SER 254 283 283 SER SER B . n 
B 1 255 ASP 255 284 284 ASP ASP B . n 
B 1 256 PRO 256 285 285 PRO PRO B . n 
B 1 257 TYR 257 286 286 TYR TYR B . n 
B 1 258 LEU 258 287 287 LEU LEU B . n 
B 1 259 SER 259 288 288 SER SER B . n 
B 1 260 PHE 260 289 289 PHE PHE B . n 
B 1 261 ALA 261 290 290 ALA ALA B . n 
B 1 262 ALA 262 291 291 ALA ALA B . n 
B 1 263 ALA 263 292 292 ALA ALA B . n 
B 1 264 MET 264 293 293 MET MET B . n 
B 1 265 ASN 265 294 294 ASN ASN B . n 
B 1 266 GLY 266 295 295 GLY GLY B . n 
B 1 267 LEU 267 296 296 LEU LEU B . n 
B 1 268 ALA 268 297 297 ALA ALA B . n 
B 1 269 GLY 269 298 298 GLY GLY B . n 
B 1 270 PRO 270 299 299 PRO PRO B . n 
B 1 271 LEU 271 300 300 LEU LEU B . n 
B 1 272 HIS 272 301 301 HIS HIS B . n 
B 1 273 GLY 273 302 302 GLY GLY B . n 
B 1 274 LEU 274 303 303 LEU LEU B . n 
B 1 275 ALA 275 304 304 ALA ALA B . n 
B 1 276 ASN 276 305 305 ASN ASN B . n 
B 1 277 GLN 277 306 306 GLN GLN B . n 
B 1 278 GLU 278 307 307 GLU GLU B . n 
B 1 279 VAL 279 308 308 VAL VAL B . n 
B 1 280 LEU 280 309 309 LEU LEU B . n 
B 1 281 VAL 281 310 310 VAL VAL B . n 
B 1 282 TRP 282 311 311 TRP TRP B . n 
B 1 283 LEU 283 312 312 LEU LEU B . n 
B 1 284 THR 284 313 313 THR THR B . n 
B 1 285 GLN 285 314 314 GLN GLN B . n 
B 1 286 LEU 286 315 315 LEU LEU B . n 
B 1 287 GLN 287 316 316 GLN GLN B . n 
B 1 288 LYS 288 317 317 LYS LYS B . n 
B 1 289 GLU 289 318 318 GLU GLU B . n 
B 1 290 VAL 290 319 319 VAL VAL B . n 
B 1 291 GLY 291 320 320 GLY GLY B . n 
B 1 292 LYS 292 321 321 LYS LYS B . n 
B 1 293 ASP 293 322 322 ASP ASP B . n 
B 1 294 VAL 294 323 323 VAL VAL B . n 
B 1 295 SER 295 324 324 SER SER B . n 
B 1 296 ASP 296 325 325 ASP ASP B . n 
B 1 297 GLU 297 326 326 GLU GLU B . n 
B 1 298 LYS 298 327 327 LYS LYS B . n 
B 1 299 LEU 299 328 328 LEU LEU B . n 
B 1 300 ARG 300 329 329 ARG ARG B . n 
B 1 301 ASP 301 330 330 ASP ASP B . n 
B 1 302 TYR 302 331 331 TYR TYR B . n 
B 1 303 ILE 303 332 332 ILE ILE B . n 
B 1 304 TRP 304 333 333 TRP TRP B . n 
B 1 305 ASN 305 334 334 ASN ASN B . n 
B 1 306 THR 306 335 335 THR THR B . n 
B 1 307 LEU 307 336 336 LEU LEU B . n 
B 1 308 ASN 308 337 337 ASN ASN B . n 
B 1 309 SER 309 338 338 SER SER B . n 
B 1 310 GLY 310 339 339 GLY GLY B . n 
B 1 311 ARG 311 340 340 ARG ARG B . n 
B 1 312 VAL 312 341 341 VAL VAL B . n 
B 1 313 VAL 313 342 342 VAL VAL B . n 
B 1 314 PRO 314 343 343 PRO PRO B . n 
B 1 315 GLY 315 344 344 GLY GLY B . n 
B 1 316 TYR 316 345 345 TYR TYR B . n 
B 1 317 GLY 317 346 346 GLY GLY B . n 
B 1 318 HIS 318 347 347 HIS HIS B . n 
B 1 319 ALA 319 348 348 ALA ALA B . n 
B 1 320 VAL 320 349 349 VAL VAL B . n 
B 1 321 LEU 321 350 350 LEU LEU B . n 
B 1 322 ARG 322 351 351 ARG ARG B . n 
B 1 323 LYS 323 352 352 LYS LYS B . n 
B 1 324 THR 324 353 353 THR THR B . n 
B 1 325 ASP 325 354 354 ASP ASP B . n 
B 1 326 PRO 326 355 355 PRO PRO B . n 
B 1 327 ARG 327 356 356 ARG ARG B . n 
B 1 328 TYR 328 357 357 TYR TYR B . n 
B 1 329 THR 329 358 358 THR THR B . n 
B 1 330 CYS 330 359 359 CYS CYS B . n 
B 1 331 GLN 331 360 360 GLN GLN B . n 
B 1 332 ARG 332 361 361 ARG ARG B . n 
B 1 333 GLU 333 362 362 GLU GLU B . n 
B 1 334 PHE 334 363 363 PHE PHE B . n 
B 1 335 ALA 335 364 364 ALA ALA B . n 
B 1 336 LEU 336 365 365 LEU LEU B . n 
B 1 337 LYS 337 366 366 LYS LYS B . n 
B 1 338 HIS 338 367 367 HIS HIS B . n 
B 1 339 LEU 339 368 368 LEU LEU B . n 
B 1 340 PRO 340 369 369 PRO PRO B . n 
B 1 341 ASN 341 370 370 ASN ASN B . n 
B 1 342 ASP 342 371 371 ASP ASP B . n 
B 1 343 PRO 343 372 372 PRO PRO B . n 
B 1 344 MET 344 373 373 MET MET B . n 
B 1 345 PHE 345 374 374 PHE PHE B . n 
B 1 346 LYS 346 375 375 LYS LYS B . n 
B 1 347 LEU 347 376 376 LEU LEU B . n 
B 1 348 VAL 348 377 377 VAL VAL B . n 
B 1 349 ALA 349 378 378 ALA ALA B . n 
B 1 350 GLN 350 379 379 GLN GLN B . n 
B 1 351 LEU 351 380 380 LEU LEU B . n 
B 1 352 TYR 352 381 381 TYR TYR B . n 
B 1 353 LYS 353 382 382 LYS LYS B . n 
B 1 354 ILE 354 383 383 ILE ILE B . n 
B 1 355 VAL 355 384 384 VAL VAL B . n 
B 1 356 PRO 356 385 385 PRO PRO B . n 
B 1 357 ASN 357 386 386 ASN ASN B . n 
B 1 358 VAL 358 387 387 VAL VAL B . n 
B 1 359 LEU 359 388 388 LEU LEU B . n 
B 1 360 LEU 360 389 389 LEU LEU B . n 
B 1 361 GLU 361 390 390 GLU GLU B . n 
B 1 362 GLN 362 391 391 GLN GLN B . n 
B 1 363 GLY 363 392 392 GLY GLY B . n 
B 1 364 LYS 364 393 393 LYS LYS B . n 
B 1 365 ALA 365 394 394 ALA ALA B . n 
B 1 366 LYS 366 395 395 LYS LYS B . n 
B 1 367 ASN 367 396 396 ASN ASN B . n 
B 1 368 PRO 368 397 397 PRO PRO B . n 
B 1 369 TRP 369 398 398 TRP TRP B . n 
B 1 370 PRO 370 399 399 PRO PRO B . n 
B 1 371 ASN 371 400 400 ASN ASN B . n 
B 1 372 VAL 372 401 401 VAL VAL B . n 
B 1 373 ASP 373 402 402 ASP ASP B . n 
B 1 374 ALA 374 403 403 ALA ALA B . n 
B 1 375 HIS 375 404 404 HIS HIS B . n 
B 1 376 SER 376 405 405 SER SER B . n 
B 1 377 GLY 377 406 406 GLY GLY B . n 
B 1 378 VAL 378 407 407 VAL VAL B . n 
B 1 379 LEU 379 408 408 LEU LEU B . n 
B 1 380 LEU 380 409 409 LEU LEU B . n 
B 1 381 GLN 381 410 410 GLN GLN B . n 
B 1 382 TYR 382 411 411 TYR TYR B . n 
B 1 383 TYR 383 412 412 TYR TYR B . n 
B 1 384 GLY 384 413 413 GLY GLY B . n 
B 1 385 MET 385 414 414 MET MET B . n 
B 1 386 THR 386 415 415 THR THR B . n 
B 1 387 GLU 387 416 416 GLU GLU B . n 
B 1 388 MET 388 417 417 MET MET B . n 
B 1 389 ASN 389 418 418 ASN ASN B . n 
B 1 390 TYR 390 419 419 TYR TYR B . n 
B 1 391 TYR 391 420 420 TYR TYR B . n 
B 1 392 THR 392 421 421 THR THR B . n 
B 1 393 VAL 393 422 422 VAL VAL B . n 
B 1 394 LEU 394 423 423 LEU LEU B . n 
B 1 395 PHE 395 424 424 PHE PHE B . n 
B 1 396 GLY 396 425 425 GLY GLY B . n 
B 1 397 VAL 397 426 426 VAL VAL B . n 
B 1 398 SER 398 427 427 SER SER B . n 
B 1 399 ARG 399 428 428 ARG ARG B . n 
B 1 400 ALA 400 429 429 ALA ALA B . n 
B 1 401 LEU 401 430 430 LEU LEU B . n 
B 1 402 GLY 402 431 431 GLY GLY B . n 
B 1 403 VAL 403 432 432 VAL VAL B . n 
B 1 404 LEU 404 433 433 LEU LEU B . n 
B 1 405 ALA 405 434 434 ALA ALA B . n 
B 1 406 GLN 406 435 435 GLN GLN B . n 
B 1 407 LEU 407 436 436 LEU LEU B . n 
B 1 408 ILE 408 437 437 ILE ILE B . n 
B 1 409 TRP 409 438 438 TRP TRP B . n 
B 1 410 SER 410 439 439 SER SER B . n 
B 1 411 ARG 411 440 440 ARG ARG B . n 
B 1 412 ALA 412 441 441 ALA ALA B . n 
B 1 413 LEU 413 442 442 LEU LEU B . n 
B 1 414 GLY 414 443 443 GLY GLY B . n 
B 1 415 PHE 415 444 444 PHE PHE B . n 
B 1 416 PRO 416 445 445 PRO PRO B . n 
B 1 417 LEU 417 446 446 LEU LEU B . n 
B 1 418 GLU 418 447 447 GLU GLU B . n 
B 1 419 ARG 419 448 448 ARG ARG B . n 
B 1 420 PRO 420 449 449 PRO PRO B . n 
B 1 421 LYS 421 450 450 LYS LYS B . n 
B 1 422 SER 422 451 451 SER SER B . n 
B 1 423 MET 423 452 452 MET MET B . n 
B 1 424 SER 424 453 453 SER SER B . n 
B 1 425 THR 425 454 454 THR THR B . n 
B 1 426 GLU 426 455 455 GLU GLU B . n 
B 1 427 GLY 427 456 456 GLY GLY B . n 
B 1 428 LEU 428 457 457 LEU LEU B . n 
B 1 429 MET 429 458 458 MET MET B . n 
B 1 430 LYS 430 459 459 LYS LYS B . n 
B 1 431 PHE 431 460 460 PHE PHE B . n 
B 1 432 VAL 432 461 461 VAL VAL B . n 
B 1 433 ASP 433 462 462 ASP ASP B . n 
B 1 434 SER 434 463 463 SER SER B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 COA 1   501 502 COA COA A . 
D 3 ACE 1   502 503 ACE ACE A . 
E 4 OAA 1   503 504 OAA OAA A . 
F 5 HOH 1   601 171 HOH HOH A . 
F 5 HOH 2   602 584 HOH HOH A . 
F 5 HOH 3   603 200 HOH HOH A . 
F 5 HOH 4   604 117 HOH HOH A . 
F 5 HOH 5   605 170 HOH HOH A . 
F 5 HOH 6   606 365 HOH HOH A . 
F 5 HOH 7   607 433 HOH HOH A . 
F 5 HOH 8   608 289 HOH HOH A . 
F 5 HOH 9   609 298 HOH HOH A . 
F 5 HOH 10  610 26  HOH HOH A . 
F 5 HOH 11  611 87  HOH HOH A . 
F 5 HOH 12  612 88  HOH HOH A . 
F 5 HOH 13  613 158 HOH HOH A . 
F 5 HOH 14  614 40  HOH HOH A . 
F 5 HOH 15  615 9   HOH HOH A . 
F 5 HOH 16  616 250 HOH HOH A . 
F 5 HOH 17  617 399 HOH HOH A . 
F 5 HOH 18  618 254 HOH HOH A . 
F 5 HOH 19  619 359 HOH HOH A . 
F 5 HOH 20  620 471 HOH HOH A . 
F 5 HOH 21  621 402 HOH HOH A . 
F 5 HOH 22  622 81  HOH HOH A . 
F 5 HOH 23  623 42  HOH HOH A . 
F 5 HOH 24  624 155 HOH HOH A . 
F 5 HOH 25  625 205 HOH HOH A . 
F 5 HOH 26  626 17  HOH HOH A . 
F 5 HOH 27  627 7   HOH HOH A . 
F 5 HOH 28  628 138 HOH HOH A . 
F 5 HOH 29  629 43  HOH HOH A . 
F 5 HOH 30  630 2   HOH HOH A . 
F 5 HOH 31  631 3   HOH HOH A . 
F 5 HOH 32  632 198 HOH HOH A . 
F 5 HOH 33  633 330 HOH HOH A . 
F 5 HOH 34  634 15  HOH HOH A . 
F 5 HOH 35  635 38  HOH HOH A . 
F 5 HOH 36  636 201 HOH HOH A . 
F 5 HOH 37  637 22  HOH HOH A . 
F 5 HOH 38  638 189 HOH HOH A . 
F 5 HOH 39  639 244 HOH HOH A . 
F 5 HOH 40  640 96  HOH HOH A . 
F 5 HOH 41  641 329 HOH HOH A . 
F 5 HOH 42  642 78  HOH HOH A . 
F 5 HOH 43  643 230 HOH HOH A . 
F 5 HOH 44  644 100 HOH HOH A . 
F 5 HOH 45  645 56  HOH HOH A . 
F 5 HOH 46  646 480 HOH HOH A . 
F 5 HOH 47  647 62  HOH HOH A . 
F 5 HOH 48  648 59  HOH HOH A . 
F 5 HOH 49  649 79  HOH HOH A . 
F 5 HOH 50  650 5   HOH HOH A . 
F 5 HOH 51  651 166 HOH HOH A . 
F 5 HOH 52  652 8   HOH HOH A . 
F 5 HOH 53  653 118 HOH HOH A . 
F 5 HOH 54  654 149 HOH HOH A . 
F 5 HOH 55  655 126 HOH HOH A . 
F 5 HOH 56  656 45  HOH HOH A . 
F 5 HOH 57  657 89  HOH HOH A . 
F 5 HOH 58  658 69  HOH HOH A . 
F 5 HOH 59  659 53  HOH HOH A . 
F 5 HOH 60  660 1   HOH HOH A . 
F 5 HOH 61  661 29  HOH HOH A . 
F 5 HOH 62  662 130 HOH HOH A . 
F 5 HOH 63  663 216 HOH HOH A . 
F 5 HOH 64  664 65  HOH HOH A . 
F 5 HOH 65  665 122 HOH HOH A . 
F 5 HOH 66  666 195 HOH HOH A . 
F 5 HOH 67  667 272 HOH HOH A . 
F 5 HOH 68  668 196 HOH HOH A . 
F 5 HOH 69  669 23  HOH HOH A . 
F 5 HOH 70  670 210 HOH HOH A . 
F 5 HOH 71  671 137 HOH HOH A . 
F 5 HOH 72  672 506 HOH HOH A . 
F 5 HOH 73  673 99  HOH HOH A . 
F 5 HOH 74  674 44  HOH HOH A . 
F 5 HOH 75  675 74  HOH HOH A . 
F 5 HOH 76  676 220 HOH HOH A . 
F 5 HOH 77  677 505 HOH HOH A . 
F 5 HOH 78  678 80  HOH HOH A . 
F 5 HOH 79  679 181 HOH HOH A . 
F 5 HOH 80  680 173 HOH HOH A . 
F 5 HOH 81  681 85  HOH HOH A . 
F 5 HOH 82  682 113 HOH HOH A . 
F 5 HOH 83  683 41  HOH HOH A . 
F 5 HOH 84  684 239 HOH HOH A . 
F 5 HOH 85  685 84  HOH HOH A . 
F 5 HOH 86  686 309 HOH HOH A . 
F 5 HOH 87  687 327 HOH HOH A . 
F 5 HOH 88  688 154 HOH HOH A . 
F 5 HOH 89  689 146 HOH HOH A . 
F 5 HOH 90  690 282 HOH HOH A . 
F 5 HOH 91  691 116 HOH HOH A . 
F 5 HOH 92  692 264 HOH HOH A . 
F 5 HOH 93  693 260 HOH HOH A . 
F 5 HOH 94  694 451 HOH HOH A . 
F 5 HOH 95  695 342 HOH HOH A . 
F 5 HOH 96  696 128 HOH HOH A . 
F 5 HOH 97  697 440 HOH HOH A . 
F 5 HOH 98  698 461 HOH HOH A . 
F 5 HOH 99  699 20  HOH HOH A . 
F 5 HOH 100 700 236 HOH HOH A . 
F 5 HOH 101 701 34  HOH HOH A . 
F 5 HOH 102 702 382 HOH HOH A . 
F 5 HOH 103 703 51  HOH HOH A . 
F 5 HOH 104 704 127 HOH HOH A . 
F 5 HOH 105 705 306 HOH HOH A . 
F 5 HOH 106 706 496 HOH HOH A . 
F 5 HOH 107 707 120 HOH HOH A . 
F 5 HOH 108 708 129 HOH HOH A . 
F 5 HOH 109 709 320 HOH HOH A . 
F 5 HOH 110 710 27  HOH HOH A . 
F 5 HOH 111 711 48  HOH HOH A . 
F 5 HOH 112 712 350 HOH HOH A . 
F 5 HOH 113 713 24  HOH HOH A . 
F 5 HOH 114 714 316 HOH HOH A . 
F 5 HOH 115 715 470 HOH HOH A . 
F 5 HOH 116 716 57  HOH HOH A . 
F 5 HOH 117 717 159 HOH HOH A . 
F 5 HOH 118 718 31  HOH HOH A . 
F 5 HOH 119 719 72  HOH HOH A . 
F 5 HOH 120 720 252 HOH HOH A . 
F 5 HOH 121 721 183 HOH HOH A . 
F 5 HOH 122 722 387 HOH HOH A . 
F 5 HOH 123 723 187 HOH HOH A . 
F 5 HOH 124 724 347 HOH HOH A . 
F 5 HOH 125 725 430 HOH HOH A . 
F 5 HOH 126 726 276 HOH HOH A . 
F 5 HOH 127 727 46  HOH HOH A . 
F 5 HOH 128 728 131 HOH HOH A . 
F 5 HOH 129 729 406 HOH HOH A . 
F 5 HOH 130 730 124 HOH HOH A . 
F 5 HOH 131 731 373 HOH HOH A . 
F 5 HOH 132 732 419 HOH HOH A . 
F 5 HOH 133 733 269 HOH HOH A . 
F 5 HOH 134 734 319 HOH HOH A . 
F 5 HOH 135 735 352 HOH HOH A . 
F 5 HOH 136 736 478 HOH HOH A . 
F 5 HOH 137 737 50  HOH HOH A . 
F 5 HOH 138 738 581 HOH HOH A . 
F 5 HOH 139 739 510 HOH HOH A . 
F 5 HOH 140 740 172 HOH HOH A . 
F 5 HOH 141 741 397 HOH HOH A . 
F 5 HOH 142 742 508 HOH HOH A . 
F 5 HOH 143 743 398 HOH HOH A . 
F 5 HOH 144 744 258 HOH HOH A . 
F 5 HOH 145 745 152 HOH HOH A . 
F 5 HOH 146 746 512 HOH HOH A . 
F 5 HOH 147 747 573 HOH HOH A . 
F 5 HOH 148 748 228 HOH HOH A . 
F 5 HOH 149 749 346 HOH HOH A . 
F 5 HOH 150 750 114 HOH HOH A . 
F 5 HOH 151 751 583 HOH HOH A . 
F 5 HOH 152 752 218 HOH HOH A . 
F 5 HOH 153 753 141 HOH HOH A . 
F 5 HOH 154 754 540 HOH HOH A . 
F 5 HOH 155 755 516 HOH HOH A . 
F 5 HOH 156 756 427 HOH HOH A . 
F 5 HOH 157 757 554 HOH HOH A . 
F 5 HOH 158 758 377 HOH HOH A . 
F 5 HOH 159 759 521 HOH HOH A . 
F 5 HOH 160 760 94  HOH HOH A . 
F 5 HOH 161 761 413 HOH HOH A . 
F 5 HOH 162 762 420 HOH HOH A . 
F 5 HOH 163 763 520 HOH HOH A . 
F 5 HOH 164 764 522 HOH HOH A . 
F 5 HOH 165 765 529 HOH HOH A . 
F 5 HOH 166 766 145 HOH HOH A . 
F 5 HOH 167 767 568 HOH HOH A . 
F 5 HOH 168 768 312 HOH HOH A . 
F 5 HOH 169 769 491 HOH HOH A . 
F 5 HOH 170 770 338 HOH HOH A . 
F 5 HOH 171 771 363 HOH HOH A . 
F 5 HOH 172 772 525 HOH HOH A . 
F 5 HOH 173 773 249 HOH HOH A . 
F 5 HOH 174 774 534 HOH HOH A . 
F 5 HOH 175 775 211 HOH HOH A . 
F 5 HOH 176 776 555 HOH HOH A . 
F 5 HOH 177 777 566 HOH HOH A . 
F 5 HOH 178 778 325 HOH HOH A . 
F 5 HOH 179 779 530 HOH HOH A . 
F 5 HOH 180 780 389 HOH HOH A . 
F 5 HOH 181 781 578 HOH HOH A . 
F 5 HOH 182 782 571 HOH HOH A . 
F 5 HOH 183 783 579 HOH HOH A . 
G 5 HOH 1   501 147 HOH HOH B . 
G 5 HOH 2   502 136 HOH HOH B . 
G 5 HOH 3   503 519 HOH HOH B . 
G 5 HOH 4   504 214 HOH HOH B . 
G 5 HOH 5   505 28  HOH HOH B . 
G 5 HOH 6   506 112 HOH HOH B . 
G 5 HOH 7   507 77  HOH HOH B . 
G 5 HOH 8   508 322 HOH HOH B . 
G 5 HOH 9   509 240 HOH HOH B . 
G 5 HOH 10  510 197 HOH HOH B . 
G 5 HOH 11  511 103 HOH HOH B . 
G 5 HOH 12  512 135 HOH HOH B . 
G 5 HOH 13  513 32  HOH HOH B . 
G 5 HOH 14  514 151 HOH HOH B . 
G 5 HOH 15  515 66  HOH HOH B . 
G 5 HOH 16  516 54  HOH HOH B . 
G 5 HOH 17  517 247 HOH HOH B . 
G 5 HOH 18  518 204 HOH HOH B . 
G 5 HOH 19  519 156 HOH HOH B . 
G 5 HOH 20  520 92  HOH HOH B . 
G 5 HOH 21  521 58  HOH HOH B . 
G 5 HOH 22  522 248 HOH HOH B . 
G 5 HOH 23  523 143 HOH HOH B . 
G 5 HOH 24  524 405 HOH HOH B . 
G 5 HOH 25  525 182 HOH HOH B . 
G 5 HOH 26  526 133 HOH HOH B . 
G 5 HOH 27  527 6   HOH HOH B . 
G 5 HOH 28  528 18  HOH HOH B . 
G 5 HOH 29  529 37  HOH HOH B . 
G 5 HOH 30  530 12  HOH HOH B . 
G 5 HOH 31  531 21  HOH HOH B . 
G 5 HOH 32  532 14  HOH HOH B . 
G 5 HOH 33  533 76  HOH HOH B . 
G 5 HOH 34  534 52  HOH HOH B . 
G 5 HOH 35  535 431 HOH HOH B . 
G 5 HOH 36  536 90  HOH HOH B . 
G 5 HOH 37  537 168 HOH HOH B . 
G 5 HOH 38  538 134 HOH HOH B . 
G 5 HOH 39  539 190 HOH HOH B . 
G 5 HOH 40  540 542 HOH HOH B . 
G 5 HOH 41  541 400 HOH HOH B . 
G 5 HOH 42  542 10  HOH HOH B . 
G 5 HOH 43  543 25  HOH HOH B . 
G 5 HOH 44  544 251 HOH HOH B . 
G 5 HOH 45  545 391 HOH HOH B . 
G 5 HOH 46  546 439 HOH HOH B . 
G 5 HOH 47  547 11  HOH HOH B . 
G 5 HOH 48  548 455 HOH HOH B . 
G 5 HOH 49  549 271 HOH HOH B . 
G 5 HOH 50  550 162 HOH HOH B . 
G 5 HOH 51  551 370 HOH HOH B . 
G 5 HOH 52  552 224 HOH HOH B . 
G 5 HOH 53  553 102 HOH HOH B . 
G 5 HOH 54  554 243 HOH HOH B . 
G 5 HOH 55  555 125 HOH HOH B . 
G 5 HOH 56  556 233 HOH HOH B . 
G 5 HOH 57  557 238 HOH HOH B . 
G 5 HOH 58  558 33  HOH HOH B . 
G 5 HOH 59  559 407 HOH HOH B . 
G 5 HOH 60  560 61  HOH HOH B . 
G 5 HOH 61  561 169 HOH HOH B . 
G 5 HOH 62  562 19  HOH HOH B . 
G 5 HOH 63  563 93  HOH HOH B . 
G 5 HOH 64  564 207 HOH HOH B . 
G 5 HOH 65  565 175 HOH HOH B . 
G 5 HOH 66  566 422 HOH HOH B . 
G 5 HOH 67  567 70  HOH HOH B . 
G 5 HOH 68  568 337 HOH HOH B . 
G 5 HOH 69  569 4   HOH HOH B . 
G 5 HOH 70  570 273 HOH HOH B . 
G 5 HOH 71  571 13  HOH HOH B . 
G 5 HOH 72  572 35  HOH HOH B . 
G 5 HOH 73  573 308 HOH HOH B . 
G 5 HOH 74  574 178 HOH HOH B . 
G 5 HOH 75  575 64  HOH HOH B . 
G 5 HOH 76  576 369 HOH HOH B . 
G 5 HOH 77  577 49  HOH HOH B . 
G 5 HOH 78  578 140 HOH HOH B . 
G 5 HOH 79  579 206 HOH HOH B . 
G 5 HOH 80  580 39  HOH HOH B . 
G 5 HOH 81  581 163 HOH HOH B . 
G 5 HOH 82  582 75  HOH HOH B . 
G 5 HOH 83  583 349 HOH HOH B . 
G 5 HOH 84  584 191 HOH HOH B . 
G 5 HOH 85  585 193 HOH HOH B . 
G 5 HOH 86  586 73  HOH HOH B . 
G 5 HOH 87  587 82  HOH HOH B . 
G 5 HOH 88  588 110 HOH HOH B . 
G 5 HOH 89  589 157 HOH HOH B . 
G 5 HOH 90  590 68  HOH HOH B . 
G 5 HOH 91  591 105 HOH HOH B . 
G 5 HOH 92  592 167 HOH HOH B . 
G 5 HOH 93  593 71  HOH HOH B . 
G 5 HOH 94  594 321 HOH HOH B . 
G 5 HOH 95  595 458 HOH HOH B . 
G 5 HOH 96  596 417 HOH HOH B . 
G 5 HOH 97  597 95  HOH HOH B . 
G 5 HOH 98  598 188 HOH HOH B . 
G 5 HOH 99  599 63  HOH HOH B . 
G 5 HOH 100 600 335 HOH HOH B . 
G 5 HOH 101 601 36  HOH HOH B . 
G 5 HOH 102 602 514 HOH HOH B . 
G 5 HOH 103 603 449 HOH HOH B . 
G 5 HOH 104 604 323 HOH HOH B . 
G 5 HOH 105 605 507 HOH HOH B . 
G 5 HOH 106 606 109 HOH HOH B . 
G 5 HOH 107 607 16  HOH HOH B . 
G 5 HOH 108 608 185 HOH HOH B . 
G 5 HOH 109 609 223 HOH HOH B . 
G 5 HOH 110 610 67  HOH HOH B . 
G 5 HOH 111 611 246 HOH HOH B . 
G 5 HOH 112 612 55  HOH HOH B . 
G 5 HOH 113 613 443 HOH HOH B . 
G 5 HOH 114 614 60  HOH HOH B . 
G 5 HOH 115 615 524 HOH HOH B . 
G 5 HOH 116 616 275 HOH HOH B . 
G 5 HOH 117 617 476 HOH HOH B . 
G 5 HOH 118 618 444 HOH HOH B . 
G 5 HOH 119 619 30  HOH HOH B . 
G 5 HOH 120 620 268 HOH HOH B . 
G 5 HOH 121 621 368 HOH HOH B . 
G 5 HOH 122 622 111 HOH HOH B . 
G 5 HOH 123 623 177 HOH HOH B . 
G 5 HOH 124 624 180 HOH HOH B . 
G 5 HOH 125 625 274 HOH HOH B . 
G 5 HOH 126 626 452 HOH HOH B . 
G 5 HOH 127 627 215 HOH HOH B . 
G 5 HOH 128 628 160 HOH HOH B . 
G 5 HOH 129 629 283 HOH HOH B . 
G 5 HOH 130 630 262 HOH HOH B . 
G 5 HOH 131 631 101 HOH HOH B . 
G 5 HOH 132 632 192 HOH HOH B . 
G 5 HOH 133 633 379 HOH HOH B . 
G 5 HOH 134 634 234 HOH HOH B . 
G 5 HOH 135 635 277 HOH HOH B . 
G 5 HOH 136 636 97  HOH HOH B . 
G 5 HOH 137 637 132 HOH HOH B . 
G 5 HOH 138 638 317 HOH HOH B . 
G 5 HOH 139 639 528 HOH HOH B . 
G 5 HOH 140 640 203 HOH HOH B . 
G 5 HOH 141 641 532 HOH HOH B . 
G 5 HOH 142 642 310 HOH HOH B . 
G 5 HOH 143 643 106 HOH HOH B . 
G 5 HOH 144 644 518 HOH HOH B . 
G 5 HOH 145 645 536 HOH HOH B . 
G 5 HOH 146 646 526 HOH HOH B . 
G 5 HOH 147 647 531 HOH HOH B . 
G 5 HOH 148 648 119 HOH HOH B . 
G 5 HOH 149 649 577 HOH HOH B . 
G 5 HOH 150 650 270 HOH HOH B . 
G 5 HOH 151 651 559 HOH HOH B . 
G 5 HOH 152 652 83  HOH HOH B . 
G 5 HOH 153 653 139 HOH HOH B . 
G 5 HOH 154 654 194 HOH HOH B . 
G 5 HOH 155 655 357 HOH HOH B . 
G 5 HOH 156 656 255 HOH HOH B . 
G 5 HOH 157 657 217 HOH HOH B . 
G 5 HOH 158 658 538 HOH HOH B . 
G 5 HOH 159 659 543 HOH HOH B . 
G 5 HOH 160 660 570 HOH HOH B . 
G 5 HOH 161 661 544 HOH HOH B . 
G 5 HOH 162 662 551 HOH HOH B . 
G 5 HOH 163 663 425 HOH HOH B . 
G 5 HOH 164 664 515 HOH HOH B . 
G 5 HOH 165 665 288 HOH HOH B . 
G 5 HOH 166 666 459 HOH HOH B . 
G 5 HOH 167 667 381 HOH HOH B . 
G 5 HOH 168 668 245 HOH HOH B . 
G 5 HOH 169 669 539 HOH HOH B . 
G 5 HOH 170 670 582 HOH HOH B . 
G 5 HOH 171 671 527 HOH HOH B . 
G 5 HOH 172 672 263 HOH HOH B . 
G 5 HOH 173 673 565 HOH HOH B . 
G 5 HOH 174 674 523 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 B LYS 215 ? NZ  ? B LYS 186 NZ  
3  1 Y 1 B GLU 318 ? CG  ? B GLU 289 CG  
4  1 Y 1 B GLU 318 ? CD  ? B GLU 289 CD  
5  1 Y 1 B GLU 318 ? OE1 ? B GLU 289 OE1 
6  1 Y 1 B GLU 318 ? OE2 ? B GLU 289 OE2 
7  1 Y 1 B ARG 329 ? CG  ? B ARG 300 CG  
8  1 Y 1 B ARG 329 ? CD  ? B ARG 300 CD  
9  1 Y 1 B ARG 329 ? NE  ? B ARG 300 NE  
10 1 Y 1 B ARG 329 ? CZ  ? B ARG 300 CZ  
11 1 Y 1 B ARG 329 ? NH1 ? B ARG 300 NH1 
12 1 Y 1 B ARG 329 ? NH2 ? B ARG 300 NH2 
13 1 Y 1 B TYR 331 ? CG  ? B TYR 302 CG  
14 1 Y 1 B TYR 331 ? CD1 ? B TYR 302 CD1 
15 1 Y 1 B TYR 331 ? CD2 ? B TYR 302 CD2 
16 1 Y 1 B TYR 331 ? CE1 ? B TYR 302 CE1 
17 1 Y 1 B TYR 331 ? CE2 ? B TYR 302 CE2 
18 1 Y 1 B TYR 331 ? CZ  ? B TYR 302 CZ  
19 1 Y 1 B TYR 331 ? OH  ? B TYR 302 OH  
20 1 Y 1 B ARG 351 ? CG  ? B ARG 322 CG  
21 1 Y 1 B ARG 351 ? CD  ? B ARG 322 CD  
22 1 Y 1 B ARG 351 ? NE  ? B ARG 322 NE  
23 1 Y 1 B ARG 351 ? CZ  ? B ARG 322 CZ  
24 1 Y 1 B ARG 351 ? NH1 ? B ARG 322 NH1 
25 1 Y 1 B ARG 351 ? NH2 ? B ARG 322 NH2 
26 1 Y 1 B LYS 352 ? CG  ? B LYS 323 CG  
27 1 Y 1 B LYS 352 ? CD  ? B LYS 323 CD  
28 1 Y 1 B LYS 352 ? CE  ? B LYS 323 CE  
29 1 Y 1 B LYS 352 ? NZ  ? B LYS 323 NZ  
30 1 Y 1 B LYS 395 ? CG  ? B LYS 366 CG  
31 1 Y 1 B LYS 395 ? CD  ? B LYS 366 CD  
32 1 Y 1 B LYS 395 ? CE  ? B LYS 366 CE  
33 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                  101.58 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   98.87 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  116.40 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8ZVR 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     57.924 
_cell.length_a_esd                 ? 
_cell.length_b                     59.732 
_cell.length_b_esd                 ? 
_cell.length_c                     73.280 
_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                         8ZVR 
_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                   8ZVR 
_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          44.03 
_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                                       8ZVR 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.80 
_reflns.d_resolution_low                               68.97 
_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                                     67914 
_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                           88.3 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          5.3 
_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                                0.180 
_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                                   0.895 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.140 
_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                                    1.80 
_reflns_shell.d_res_low                                     1.90 
_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                             9328 
_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                               1.508 
_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                                  0.501 
_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                                  1.163 
_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]                            -0.81 
_refine.aniso_B[1][2]                            0.79 
_refine.aniso_B[1][3]                            -0.70 
_refine.aniso_B[2][2]                            1.03 
_refine.aniso_B[2][3]                            0.19 
_refine.aniso_B[3][3]                            -0.94 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               39.303 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.919 
_refine.correlation_coeff_Fo_to_Fc_free          0.894 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8ZVR 
_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                            1.80 
_refine.ls_d_res_low                             68.97 
_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                     61068 
_refine.ls_number_reflns_R_free                  3223 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    83.57 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.22301 
_refine.ls_R_factor_R_free                       0.27385 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.22036 
_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                       0.204 
_refine.pdbx_overall_ESU_R_Free                  0.183 
_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                             5.689 
_refine.overall_SU_ML                            0.160 
_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                       1.80 
_refine_hist.d_res_low                        68.97 
_refine_hist.number_atoms_solvent             357 
_refine_hist.number_atoms_total               7228 
_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        6871 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.008  0.012  7062  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  6653  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.727  1.829  9595  ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.575  1.747  15328 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.893  5.000  870   ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 7.079  5.000  40    ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 16.042 10.000 1180  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.081  0.200  1057  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.008  0.020  8281  ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  1604  ? 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' ? 3.956  3.865  3475  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 3.953  3.866  3475  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 5.970  6.942  4340  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 5.970  6.943  4341  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 4.369  4.367  3587  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 4.368  4.368  3588  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 6.804  7.836  5254  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 10.301 43.86  8431  ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 10.304 43.59  8383  ? 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                       1.800 
_refine_ls_shell.d_res_low                        1.846 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             254 
_refine_ls_shell.number_reflns_R_work             4695 
_refine_ls_shell.percent_reflns_obs               86.72 
_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                  0.304 
_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   ? 
_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                     8ZVR 
_struct.title                        'Human citrate synthase intermediate 2' 
_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        8ZVR 
_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 8ZVR A 1 ? 434 ? O75390 30 ? 463 ? 30 463 
2 1 8ZVR 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)' 11030 ? 
1 MORE         -59   ? 
1 'SSA (A^2)'  30490 ? 
# 
_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]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
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 ASP A 296 ? GLY A 310 ? ASP A 325 GLY A 339 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 ? GLU A 361 ? ASP A 371 GLU A 390 1 ? 20 
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 ? ASP A 433 ? SER A 453 ASP A 462 1 ? 10 
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 ? ALA B 116 ? THR B 130 ALA B 145 1 ? 16 
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 ? ASN B 147 ? HIS B 163 ASN B 176 1 ? 14 
HELX_P HELX_P32 AD5 SER B 150 ? GLN B 158 ? SER B 179 GLN B 187 1 ? 9  
HELX_P HELX_P33 AD6 SER B 161 ? THR B 163 ? SER B 190 THR B 192 5 ? 3  
HELX_P HELX_P34 AD7 LYS B 164 ? ARG B 193 ? LYS B 193 ARG B 222 1 ? 30 
HELX_P HELX_P35 AD8 ASP B 206 ? GLY B 216 ? ASP B 235 GLY B 245 1 ? 11 
HELX_P HELX_P36 AD9 ASP B 219 ? HIS B 233 ? ASP B 248 HIS B 262 1 ? 15 
HELX_P HELX_P37 AE1 ASN B 240 ? ALA B 252 ? ASN B 269 ALA B 281 1 ? 13 
HELX_P HELX_P38 AE2 ASP B 255 ? ALA B 268 ? ASP B 284 ALA B 297 1 ? 14 
HELX_P HELX_P39 AE3 GLY B 269 ? LEU B 274 ? GLY B 298 LEU B 303 1 ? 6  
HELX_P HELX_P40 AE4 LEU B 274 ? GLN B 287 ? LEU B 303 GLN B 316 1 ? 14 
HELX_P HELX_P41 AE5 SER B 295 ? ASN B 308 ? SER B 324 ASN B 337 1 ? 14 
HELX_P HELX_P42 AE6 ASP B 325 ? LEU B 339 ? ASP B 354 LEU B 368 1 ? 15 
HELX_P HELX_P43 AE7 ASP B 342 ? VAL B 355 ? ASP B 371 VAL B 384 1 ? 14 
HELX_P HELX_P44 AE8 VAL B 358 ? GLN B 362 ? VAL B 387 GLN B 391 5 ? 5  
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 ASP B 57  ? N ASP B 86  O GLY B 61  ? O GLY B 90  
AA5 2 3 N PHE B 64  ? N PHE B 93  O PHE B 67  ? O PHE B 96  
# 
_pdbx_entry_details.entry_id                   8ZVR 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O   A ACE 502 ? ? O3 A OAA 503 ? ? 1.38 
2 1 CH3 A ACE 502 ? ? O  A HOH 602 ? ? 1.94 
3 1 O   A ASP 322 ? ? O  A HOH 601 ? ? 2.03 
4 1 OD2 A ASP 402 ? ? O  A HOH 602 ? ? 2.04 
5 1 O   B HOH 621 ? ? O  B HOH 645 ? ? 2.09 
6 1 C   A ACE 502 ? ? O3 A OAA 503 ? ? 2.12 
7 1 O   A HOH 649 ? ? O  A HOH 755 ? ? 2.12 
8 1 O   B ASN 334 ? ? OG B SER 338 ? ? 2.12 
9 1 NH2 B ARG 222 ? ? O  B HOH 501 ? ? 2.14 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 OG1 A THR 247 ? ? 1_555 OE1 B GLU 326 ? ? 1_444 1.85 
2 1 OG1 A THR 247 ? ? 1_555 CD  B GLU 326 ? ? 1_444 2.05 
# 
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 A VAL 349 ? ? N A LEU 350 ? ? 1.530 1.336 0.194 0.023 Y 
2 1 C B ASP 330 ? ? N B TYR 331 ? ? 1.490 1.336 0.154 0.023 Y 
3 1 C B HIS 347 ? ? N B ALA 348 ? ? 1.547 1.336 0.211 0.023 Y 
4 1 C B ALA 348 ? ? N B VAL 349 ? ? 1.593 1.336 0.257 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 C  A ASN 337 ? ? N  A SER 338 ? ? CA A SER 338 ? ? 105.82 121.70 -15.88 2.50 Y 
2 1 CG A MET 414 ? ? SD A MET 414 ? ? CE A MET 414 ? ? 113.57 100.20 13.37  1.60 N 
3 1 CG B MET 75  ? ? SD B MET 75  ? ? CE B MET 75  ? ? 86.97  100.20 -13.23 1.60 N 
4 1 CB B LYS 109 ? ? CA B LYS 109 ? ? C  B LYS 109 ? ? 126.02 110.40 15.62  2.00 N 
5 1 CG B MET 154 ? ? SD B MET 154 ? ? CE B MET 154 ? ? 88.06  100.20 -12.14 1.60 N 
6 1 C  B ALA 348 ? ? N  B VAL 349 ? ? CA B VAL 349 ? ? 105.75 121.70 -15.95 2.50 Y 
7 1 N  B LYS 352 ? ? CA B LYS 352 ? ? CB B LYS 352 ? ? 121.52 110.60 10.92  1.80 N 
8 1 CG B MET 414 ? ? SD B MET 414 ? ? CE B MET 414 ? ? 117.57 100.20 17.37  1.60 N 
9 1 CG B MET 452 ? ? SD B MET 452 ? ? CE B MET 452 ? ? 85.28  100.20 -14.92 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 ARG A 222 ? ? -140.89 33.02   
2  1 GLU A 223 ? ? 39.39   46.01   
3  1 HIS A 265 ? ? -144.50 53.82   
4  1 GLU A 266 ? ? 75.72   -179.72 
5  1 VAL A 349 ? ? -136.77 -39.57  
6  1 LEU A 368 ? ? -145.50 51.89   
7  1 ALA A 394 ? ? 165.41  -61.03  
8  1 LYS A 395 ? ? 72.73   -48.33  
9  1 ARG A 448 ? ? -152.30 79.35   
10 1 ARG B 222 ? ? -144.44 38.12   
11 1 ASP B 248 ? ? -162.58 108.79  
12 1 HIS B 265 ? ? -148.89 56.86   
13 1 GLU B 266 ? ? 70.57   -174.29 
14 1 GLN B 316 ? ? -83.69  45.18   
15 1 LYS B 317 ? ? -93.71  -62.38  
16 1 ASP B 322 ? ? 140.64  126.28  
17 1 VAL B 323 ? ? -159.16 -150.42 
18 1 THR B 335 ? ? -126.88 -55.07  
19 1 ARG B 340 ? ? -86.10  -133.34 
20 1 TYR B 345 ? ? -144.40 50.42   
21 1 LEU B 350 ? ? -69.78  -176.75 
22 1 ARG B 351 ? ? -178.40 62.23   
23 1 LYS B 352 ? ? 159.28  159.17  
24 1 THR B 353 ? ? -49.14  107.80  
25 1 LEU B 368 ? ? -146.18 56.31   
26 1 ASN B 386 ? ? -89.09  35.39   
27 1 VAL B 387 ? ? 46.15   82.00   
28 1 ALA B 394 ? ? 166.36  -45.70  
29 1 ASN B 396 ? ? -165.84 92.99   
30 1 ARG B 448 ? ? -156.16 79.61   
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG A 73  ? ? 0.075 'SIDE CHAIN' 
2 1 ARG B 92  ? ? 0.073 'SIDE CHAIN' 
3 1 ARG B 222 ? ? 0.089 'SIDE CHAIN' 
4 1 ARG B 340 ? ? 0.233 'SIDE CHAIN' 
# 
loop_
_pdbx_validate_main_chain_plane.id 
_pdbx_validate_main_chain_plane.PDB_model_num 
_pdbx_validate_main_chain_plane.auth_comp_id 
_pdbx_validate_main_chain_plane.auth_asym_id 
_pdbx_validate_main_chain_plane.auth_seq_id 
_pdbx_validate_main_chain_plane.PDB_ins_code 
_pdbx_validate_main_chain_plane.label_alt_id 
_pdbx_validate_main_chain_plane.improper_torsion_angle 
1 1 GLY B 346 ? ? 16.46  
2 1 VAL B 349 ? ? -10.26 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 782 ? 5.95 . 
2 1 O ? A HOH 783 ? 6.28 . 
3 1 O ? B HOH 674 ? 5.90 . 
# 
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 
ACE C    C N N 1   
ACE O    O N N 2   
ACE CH3  C N N 3   
ACE H    H N N 4   
ACE H1   H N N 5   
ACE H2   H N N 6   
ACE H3   H N N 7   
ALA N    N N N 8   
ALA CA   C N S 9   
ALA C    C N N 10  
ALA O    O N N 11  
ALA CB   C N N 12  
ALA OXT  O N N 13  
ALA H    H N N 14  
ALA H2   H N N 15  
ALA HA   H N N 16  
ALA HB1  H N N 17  
ALA HB2  H N N 18  
ALA HB3  H N N 19  
ALA HXT  H N N 20  
ARG N    N N N 21  
ARG CA   C N S 22  
ARG C    C N N 23  
ARG O    O N N 24  
ARG CB   C N N 25  
ARG CG   C N N 26  
ARG CD   C N N 27  
ARG NE   N N N 28  
ARG CZ   C N N 29  
ARG NH1  N N N 30  
ARG NH2  N N N 31  
ARG OXT  O N N 32  
ARG H    H N N 33  
ARG H2   H N N 34  
ARG HA   H N N 35  
ARG HB2  H N N 36  
ARG HB3  H N N 37  
ARG HG2  H N N 38  
ARG HG3  H N N 39  
ARG HD2  H N N 40  
ARG HD3  H N N 41  
ARG HE   H N N 42  
ARG HH11 H N N 43  
ARG HH12 H N N 44  
ARG HH21 H N N 45  
ARG HH22 H N N 46  
ARG HXT  H N N 47  
ASN N    N N N 48  
ASN CA   C N S 49  
ASN C    C N N 50  
ASN O    O N N 51  
ASN CB   C N N 52  
ASN CG   C N N 53  
ASN OD1  O N N 54  
ASN ND2  N N N 55  
ASN OXT  O N N 56  
ASN H    H N N 57  
ASN H2   H N N 58  
ASN HA   H N N 59  
ASN HB2  H N N 60  
ASN HB3  H N N 61  
ASN HD21 H N N 62  
ASN HD22 H N N 63  
ASN HXT  H N N 64  
ASP N    N N N 65  
ASP CA   C N S 66  
ASP C    C N N 67  
ASP O    O N N 68  
ASP CB   C N N 69  
ASP CG   C N N 70  
ASP OD1  O N N 71  
ASP OD2  O N N 72  
ASP OXT  O N N 73  
ASP H    H N N 74  
ASP H2   H N N 75  
ASP HA   H N N 76  
ASP HB2  H N N 77  
ASP HB3  H N N 78  
ASP HD2  H N N 79  
ASP HXT  H N N 80  
COA N1A  N Y N 81  
COA C2A  C Y N 82  
COA N3A  N Y N 83  
COA C4A  C Y N 84  
COA C5A  C Y N 85  
COA C6A  C Y N 86  
COA N6A  N N N 87  
COA N7A  N Y N 88  
COA C8A  C Y N 89  
COA N9A  N Y N 90  
COA C1B  C N R 91  
COA C2B  C N R 92  
COA O2B  O N N 93  
COA C3B  C N S 94  
COA O3B  O N N 95  
COA P3B  P N N 96  
COA O7A  O N N 97  
COA O8A  O N N 98  
COA O9A  O N N 99  
COA C4B  C N R 100 
COA O4B  O N N 101 
COA C5B  C N N 102 
COA O5B  O N N 103 
COA P1A  P N S 104 
COA O1A  O N N 105 
COA O2A  O N N 106 
COA O3A  O N N 107 
COA P2A  P N S 108 
COA O4A  O N N 109 
COA O5A  O N N 110 
COA O6A  O N N 111 
COA CBP  C N N 112 
COA CCP  C N N 113 
COA CDP  C N N 114 
COA CEP  C N N 115 
COA CAP  C N R 116 
COA OAP  O N N 117 
COA C9P  C N N 118 
COA O9P  O N N 119 
COA N8P  N N N 120 
COA C7P  C N N 121 
COA C6P  C N N 122 
COA C5P  C N N 123 
COA O5P  O N N 124 
COA N4P  N N N 125 
COA C3P  C N N 126 
COA C2P  C N N 127 
COA S1P  S N N 128 
COA H2A  H N N 129 
COA H61A H N N 130 
COA H62A H N N 131 
COA H8A  H N N 132 
COA H1B  H N N 133 
COA H2B  H N N 134 
COA HO2A H N N 135 
COA H3B  H N N 136 
COA HOA8 H N N 137 
COA HOA9 H N N 138 
COA H4B  H N N 139 
COA H51A H N N 140 
COA H52A H N N 141 
COA HOA2 H N N 142 
COA HOA5 H N N 143 
COA H121 H N N 144 
COA H122 H N N 145 
COA H131 H N N 146 
COA H132 H N N 147 
COA H133 H N N 148 
COA H141 H N N 149 
COA H142 H N N 150 
COA H143 H N N 151 
COA H10  H N N 152 
COA HO1  H N N 153 
COA HN8  H N N 154 
COA H71  H N N 155 
COA H72  H N N 156 
COA H61  H N N 157 
COA H62  H N N 158 
COA HN4  H N N 159 
COA H31  H N N 160 
COA H32  H N N 161 
COA H21  H N N 162 
COA H22  H N N 163 
COA HS1  H N N 164 
CYS N    N N N 165 
CYS CA   C N R 166 
CYS C    C N N 167 
CYS O    O N N 168 
CYS CB   C N N 169 
CYS SG   S N N 170 
CYS OXT  O N N 171 
CYS H    H N N 172 
CYS H2   H N N 173 
CYS HA   H N N 174 
CYS HB2  H N N 175 
CYS HB3  H N N 176 
CYS HG   H N N 177 
CYS HXT  H N N 178 
GLN N    N N N 179 
GLN CA   C N S 180 
GLN C    C N N 181 
GLN O    O N N 182 
GLN CB   C N N 183 
GLN CG   C N N 184 
GLN CD   C N N 185 
GLN OE1  O N N 186 
GLN NE2  N N N 187 
GLN OXT  O N N 188 
GLN H    H N N 189 
GLN H2   H N N 190 
GLN HA   H N N 191 
GLN HB2  H N N 192 
GLN HB3  H N N 193 
GLN HG2  H N N 194 
GLN HG3  H N N 195 
GLN HE21 H N N 196 
GLN HE22 H N N 197 
GLN HXT  H N N 198 
GLU N    N N N 199 
GLU CA   C N S 200 
GLU C    C N N 201 
GLU O    O N N 202 
GLU CB   C N N 203 
GLU CG   C N N 204 
GLU CD   C N N 205 
GLU OE1  O N N 206 
GLU OE2  O N N 207 
GLU OXT  O N N 208 
GLU H    H N N 209 
GLU H2   H N N 210 
GLU HA   H N N 211 
GLU HB2  H N N 212 
GLU HB3  H N N 213 
GLU HG2  H N N 214 
GLU HG3  H N N 215 
GLU HE2  H N N 216 
GLU HXT  H N N 217 
GLY N    N N N 218 
GLY CA   C N N 219 
GLY C    C N N 220 
GLY O    O N N 221 
GLY OXT  O N N 222 
GLY H    H N N 223 
GLY H2   H N N 224 
GLY HA2  H N N 225 
GLY HA3  H N N 226 
GLY HXT  H N N 227 
HIS N    N N N 228 
HIS CA   C N S 229 
HIS C    C N N 230 
HIS O    O N N 231 
HIS CB   C N N 232 
HIS CG   C Y N 233 
HIS ND1  N Y N 234 
HIS CD2  C Y N 235 
HIS CE1  C Y N 236 
HIS NE2  N Y N 237 
HIS OXT  O N N 238 
HIS H    H N N 239 
HIS H2   H N N 240 
HIS HA   H N N 241 
HIS HB2  H N N 242 
HIS HB3  H N N 243 
HIS HD1  H N N 244 
HIS HD2  H N N 245 
HIS HE1  H N N 246 
HIS HE2  H N N 247 
HIS HXT  H N N 248 
HOH O    O N N 249 
HOH H1   H N N 250 
HOH H2   H N N 251 
ILE N    N N N 252 
ILE CA   C N S 253 
ILE C    C N N 254 
ILE O    O N N 255 
ILE CB   C N S 256 
ILE CG1  C N N 257 
ILE CG2  C N N 258 
ILE CD1  C N N 259 
ILE OXT  O N N 260 
ILE H    H N N 261 
ILE H2   H N N 262 
ILE HA   H N N 263 
ILE HB   H N N 264 
ILE HG12 H N N 265 
ILE HG13 H N N 266 
ILE HG21 H N N 267 
ILE HG22 H N N 268 
ILE HG23 H N N 269 
ILE HD11 H N N 270 
ILE HD12 H N N 271 
ILE HD13 H N N 272 
ILE HXT  H N N 273 
LEU N    N N N 274 
LEU CA   C N S 275 
LEU C    C N N 276 
LEU O    O N N 277 
LEU CB   C N N 278 
LEU CG   C N N 279 
LEU CD1  C N N 280 
LEU CD2  C N N 281 
LEU OXT  O N N 282 
LEU H    H N N 283 
LEU H2   H N N 284 
LEU HA   H N N 285 
LEU HB2  H N N 286 
LEU HB3  H N N 287 
LEU HG   H N N 288 
LEU HD11 H N N 289 
LEU HD12 H N N 290 
LEU HD13 H N N 291 
LEU HD21 H N N 292 
LEU HD22 H N N 293 
LEU HD23 H N N 294 
LEU HXT  H N N 295 
LYS N    N N N 296 
LYS CA   C N S 297 
LYS C    C N N 298 
LYS O    O N N 299 
LYS CB   C N N 300 
LYS CG   C N N 301 
LYS CD   C N N 302 
LYS CE   C N N 303 
LYS NZ   N N N 304 
LYS OXT  O N N 305 
LYS H    H N N 306 
LYS H2   H N N 307 
LYS HA   H N N 308 
LYS HB2  H N N 309 
LYS HB3  H N N 310 
LYS HG2  H N N 311 
LYS HG3  H N N 312 
LYS HD2  H N N 313 
LYS HD3  H N N 314 
LYS HE2  H N N 315 
LYS HE3  H N N 316 
LYS HZ1  H N N 317 
LYS HZ2  H N N 318 
LYS HZ3  H N N 319 
LYS HXT  H N N 320 
MET N    N N N 321 
MET CA   C N S 322 
MET C    C N N 323 
MET O    O N N 324 
MET CB   C N N 325 
MET CG   C N N 326 
MET SD   S N N 327 
MET CE   C N N 328 
MET OXT  O N N 329 
MET H    H N N 330 
MET H2   H N N 331 
MET HA   H N N 332 
MET HB2  H N N 333 
MET HB3  H N N 334 
MET HG2  H N N 335 
MET HG3  H N N 336 
MET HE1  H N N 337 
MET HE2  H N N 338 
MET HE3  H N N 339 
MET HXT  H N N 340 
OAA O1   O N N 341 
OAA O2   O N N 342 
OAA O4   O N N 343 
OAA O5   O N N 344 
OAA O3   O N N 345 
OAA C1   C N N 346 
OAA C2   C N N 347 
OAA C3   C N N 348 
OAA C4   C N N 349 
OAA HO5  H N N 350 
OAA H21  H N N 351 
OAA H22  H N N 352 
PHE N    N N N 353 
PHE CA   C N S 354 
PHE C    C N N 355 
PHE O    O N N 356 
PHE CB   C N N 357 
PHE CG   C Y N 358 
PHE CD1  C Y N 359 
PHE CD2  C Y N 360 
PHE CE1  C Y N 361 
PHE CE2  C Y N 362 
PHE CZ   C Y N 363 
PHE OXT  O N N 364 
PHE H    H N N 365 
PHE H2   H N N 366 
PHE HA   H N N 367 
PHE HB2  H N N 368 
PHE HB3  H N N 369 
PHE HD1  H N N 370 
PHE HD2  H N N 371 
PHE HE1  H N N 372 
PHE HE2  H N N 373 
PHE HZ   H N N 374 
PHE HXT  H N N 375 
PRO N    N N N 376 
PRO CA   C N S 377 
PRO C    C N N 378 
PRO O    O N N 379 
PRO CB   C N N 380 
PRO CG   C N N 381 
PRO CD   C N N 382 
PRO OXT  O N N 383 
PRO H    H N N 384 
PRO HA   H N N 385 
PRO HB2  H N N 386 
PRO HB3  H N N 387 
PRO HG2  H N N 388 
PRO HG3  H N N 389 
PRO HD2  H N N 390 
PRO HD3  H N N 391 
PRO HXT  H N N 392 
SER N    N N N 393 
SER CA   C N S 394 
SER C    C N N 395 
SER O    O N N 396 
SER CB   C N N 397 
SER OG   O N N 398 
SER OXT  O N N 399 
SER H    H N N 400 
SER H2   H N N 401 
SER HA   H N N 402 
SER HB2  H N N 403 
SER HB3  H N N 404 
SER HG   H N N 405 
SER HXT  H N N 406 
THR N    N N N 407 
THR CA   C N S 408 
THR C    C N N 409 
THR O    O N N 410 
THR CB   C N R 411 
THR OG1  O N N 412 
THR CG2  C N N 413 
THR OXT  O N N 414 
THR H    H N N 415 
THR H2   H N N 416 
THR HA   H N N 417 
THR HB   H N N 418 
THR HG1  H N N 419 
THR HG21 H N N 420 
THR HG22 H N N 421 
THR HG23 H N N 422 
THR HXT  H N N 423 
TRP N    N N N 424 
TRP CA   C N S 425 
TRP C    C N N 426 
TRP O    O N N 427 
TRP CB   C N N 428 
TRP CG   C Y N 429 
TRP CD1  C Y N 430 
TRP CD2  C Y N 431 
TRP NE1  N Y N 432 
TRP CE2  C Y N 433 
TRP CE3  C Y N 434 
TRP CZ2  C Y N 435 
TRP CZ3  C Y N 436 
TRP CH2  C Y N 437 
TRP OXT  O N N 438 
TRP H    H N N 439 
TRP H2   H N N 440 
TRP HA   H N N 441 
TRP HB2  H N N 442 
TRP HB3  H N N 443 
TRP HD1  H N N 444 
TRP HE1  H N N 445 
TRP HE3  H N N 446 
TRP HZ2  H N N 447 
TRP HZ3  H N N 448 
TRP HH2  H N N 449 
TRP HXT  H N N 450 
TYR N    N N N 451 
TYR CA   C N S 452 
TYR C    C N N 453 
TYR O    O N N 454 
TYR CB   C N N 455 
TYR CG   C Y N 456 
TYR CD1  C Y N 457 
TYR CD2  C Y N 458 
TYR CE1  C Y N 459 
TYR CE2  C Y N 460 
TYR CZ   C Y N 461 
TYR OH   O N N 462 
TYR OXT  O N N 463 
TYR H    H N N 464 
TYR H2   H N N 465 
TYR HA   H N N 466 
TYR HB2  H N N 467 
TYR HB3  H N N 468 
TYR HD1  H N N 469 
TYR HD2  H N N 470 
TYR HE1  H N N 471 
TYR HE2  H N N 472 
TYR HH   H N N 473 
TYR HXT  H N N 474 
VAL N    N N N 475 
VAL CA   C N S 476 
VAL C    C N N 477 
VAL O    O N N 478 
VAL CB   C N N 479 
VAL CG1  C N N 480 
VAL CG2  C N N 481 
VAL OXT  O N N 482 
VAL H    H N N 483 
VAL H2   H N N 484 
VAL HA   H N N 485 
VAL HB   H N N 486 
VAL HG11 H N N 487 
VAL HG12 H N N 488 
VAL HG13 H N N 489 
VAL HG21 H N N 490 
VAL HG22 H N N 491 
VAL HG23 H N N 492 
VAL HXT  H N N 493 
# 
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 
ACE C   O    doub N N 1   
ACE C   CH3  sing N N 2   
ACE C   H    sing N N 3   
ACE CH3 H1   sing N N 4   
ACE CH3 H2   sing N N 5   
ACE CH3 H3   sing N N 6   
ALA N   CA   sing N N 7   
ALA N   H    sing N N 8   
ALA N   H2   sing N N 9   
ALA CA  C    sing N N 10  
ALA CA  CB   sing N N 11  
ALA CA  HA   sing N N 12  
ALA C   O    doub N N 13  
ALA C   OXT  sing N N 14  
ALA CB  HB1  sing N N 15  
ALA CB  HB2  sing N N 16  
ALA CB  HB3  sing N N 17  
ALA OXT HXT  sing N N 18  
ARG N   CA   sing N N 19  
ARG N   H    sing N N 20  
ARG N   H2   sing N N 21  
ARG CA  C    sing N N 22  
ARG CA  CB   sing N N 23  
ARG CA  HA   sing N N 24  
ARG C   O    doub N N 25  
ARG C   OXT  sing N N 26  
ARG CB  CG   sing N N 27  
ARG CB  HB2  sing N N 28  
ARG CB  HB3  sing N N 29  
ARG CG  CD   sing N N 30  
ARG CG  HG2  sing N N 31  
ARG CG  HG3  sing N N 32  
ARG CD  NE   sing N N 33  
ARG CD  HD2  sing N N 34  
ARG CD  HD3  sing N N 35  
ARG NE  CZ   sing N N 36  
ARG NE  HE   sing N N 37  
ARG CZ  NH1  sing N N 38  
ARG CZ  NH2  doub N N 39  
ARG NH1 HH11 sing N N 40  
ARG NH1 HH12 sing N N 41  
ARG NH2 HH21 sing N N 42  
ARG NH2 HH22 sing N N 43  
ARG OXT HXT  sing N N 44  
ASN N   CA   sing N N 45  
ASN N   H    sing N N 46  
ASN N   H2   sing N N 47  
ASN CA  C    sing N N 48  
ASN CA  CB   sing N N 49  
ASN CA  HA   sing N N 50  
ASN C   O    doub N N 51  
ASN C   OXT  sing N N 52  
ASN CB  CG   sing N N 53  
ASN CB  HB2  sing N N 54  
ASN CB  HB3  sing N N 55  
ASN CG  OD1  doub N N 56  
ASN CG  ND2  sing N N 57  
ASN ND2 HD21 sing N N 58  
ASN ND2 HD22 sing N N 59  
ASN OXT HXT  sing N N 60  
ASP N   CA   sing N N 61  
ASP N   H    sing N N 62  
ASP N   H2   sing N N 63  
ASP CA  C    sing N N 64  
ASP CA  CB   sing N N 65  
ASP CA  HA   sing N N 66  
ASP C   O    doub N N 67  
ASP C   OXT  sing N N 68  
ASP CB  CG   sing N N 69  
ASP CB  HB2  sing N N 70  
ASP CB  HB3  sing N N 71  
ASP CG  OD1  doub N N 72  
ASP CG  OD2  sing N N 73  
ASP OD2 HD2  sing N N 74  
ASP OXT HXT  sing N N 75  
COA N1A C2A  sing Y N 76  
COA N1A C6A  doub Y N 77  
COA C2A N3A  doub Y N 78  
COA C2A H2A  sing N N 79  
COA N3A C4A  sing Y N 80  
COA C4A C5A  doub Y N 81  
COA C4A N9A  sing Y N 82  
COA C5A C6A  sing Y N 83  
COA C5A N7A  sing Y N 84  
COA C6A N6A  sing N N 85  
COA N6A H61A sing N N 86  
COA N6A H62A sing N N 87  
COA N7A C8A  doub Y N 88  
COA C8A N9A  sing Y N 89  
COA C8A H8A  sing N N 90  
COA N9A C1B  sing N N 91  
COA C1B C2B  sing N N 92  
COA C1B O4B  sing N N 93  
COA C1B H1B  sing N N 94  
COA C2B O2B  sing N N 95  
COA C2B C3B  sing N N 96  
COA C2B H2B  sing N N 97  
COA O2B HO2A sing N N 98  
COA C3B O3B  sing N N 99  
COA C3B C4B  sing N N 100 
COA C3B H3B  sing N N 101 
COA O3B P3B  sing N N 102 
COA P3B O7A  doub N N 103 
COA P3B O8A  sing N N 104 
COA P3B O9A  sing N N 105 
COA O8A HOA8 sing N N 106 
COA O9A HOA9 sing N N 107 
COA C4B O4B  sing N N 108 
COA C4B C5B  sing N N 109 
COA C4B H4B  sing N N 110 
COA C5B O5B  sing N N 111 
COA C5B H51A sing N N 112 
COA C5B H52A sing N N 113 
COA O5B P1A  sing N N 114 
COA P1A O1A  doub N N 115 
COA P1A O2A  sing N N 116 
COA P1A O3A  sing N N 117 
COA O2A HOA2 sing N N 118 
COA O3A P2A  sing N N 119 
COA P2A O4A  doub N N 120 
COA P2A O5A  sing N N 121 
COA P2A O6A  sing N N 122 
COA O5A HOA5 sing N N 123 
COA O6A CCP  sing N N 124 
COA CBP CCP  sing N N 125 
COA CBP CDP  sing N N 126 
COA CBP CEP  sing N N 127 
COA CBP CAP  sing N N 128 
COA CCP H121 sing N N 129 
COA CCP H122 sing N N 130 
COA CDP H131 sing N N 131 
COA CDP H132 sing N N 132 
COA CDP H133 sing N N 133 
COA CEP H141 sing N N 134 
COA CEP H142 sing N N 135 
COA CEP H143 sing N N 136 
COA CAP OAP  sing N N 137 
COA CAP C9P  sing N N 138 
COA CAP H10  sing N N 139 
COA OAP HO1  sing N N 140 
COA C9P O9P  doub N N 141 
COA C9P N8P  sing N N 142 
COA N8P C7P  sing N N 143 
COA N8P HN8  sing N N 144 
COA C7P C6P  sing N N 145 
COA C7P H71  sing N N 146 
COA C7P H72  sing N N 147 
COA C6P C5P  sing N N 148 
COA C6P H61  sing N N 149 
COA C6P H62  sing N N 150 
COA C5P O5P  doub N N 151 
COA C5P N4P  sing N N 152 
COA N4P C3P  sing N N 153 
COA N4P HN4  sing N N 154 
COA C3P C2P  sing N N 155 
COA C3P H31  sing N N 156 
COA C3P H32  sing N N 157 
COA C2P S1P  sing N N 158 
COA C2P H21  sing N N 159 
COA C2P H22  sing N N 160 
COA S1P HS1  sing N N 161 
CYS N   CA   sing N N 162 
CYS N   H    sing N N 163 
CYS N   H2   sing N N 164 
CYS CA  C    sing N N 165 
CYS CA  CB   sing N N 166 
CYS CA  HA   sing N N 167 
CYS C   O    doub N N 168 
CYS C   OXT  sing N N 169 
CYS CB  SG   sing N N 170 
CYS CB  HB2  sing N N 171 
CYS CB  HB3  sing N N 172 
CYS SG  HG   sing N N 173 
CYS OXT HXT  sing N N 174 
GLN N   CA   sing N N 175 
GLN N   H    sing N N 176 
GLN N   H2   sing N N 177 
GLN CA  C    sing N N 178 
GLN CA  CB   sing N N 179 
GLN CA  HA   sing N N 180 
GLN C   O    doub N N 181 
GLN C   OXT  sing N N 182 
GLN CB  CG   sing N N 183 
GLN CB  HB2  sing N N 184 
GLN CB  HB3  sing N N 185 
GLN CG  CD   sing N N 186 
GLN CG  HG2  sing N N 187 
GLN CG  HG3  sing N N 188 
GLN CD  OE1  doub N N 189 
GLN CD  NE2  sing N N 190 
GLN NE2 HE21 sing N N 191 
GLN NE2 HE22 sing N N 192 
GLN OXT HXT  sing N N 193 
GLU N   CA   sing N N 194 
GLU N   H    sing N N 195 
GLU N   H2   sing N N 196 
GLU CA  C    sing N N 197 
GLU CA  CB   sing N N 198 
GLU CA  HA   sing N N 199 
GLU C   O    doub N N 200 
GLU C   OXT  sing N N 201 
GLU CB  CG   sing N N 202 
GLU CB  HB2  sing N N 203 
GLU CB  HB3  sing N N 204 
GLU CG  CD   sing N N 205 
GLU CG  HG2  sing N N 206 
GLU CG  HG3  sing N N 207 
GLU CD  OE1  doub N N 208 
GLU CD  OE2  sing N N 209 
GLU OE2 HE2  sing N N 210 
GLU OXT HXT  sing N N 211 
GLY N   CA   sing N N 212 
GLY N   H    sing N N 213 
GLY N   H2   sing N N 214 
GLY CA  C    sing N N 215 
GLY CA  HA2  sing N N 216 
GLY CA  HA3  sing N N 217 
GLY C   O    doub N N 218 
GLY C   OXT  sing N N 219 
GLY OXT HXT  sing N N 220 
HIS N   CA   sing N N 221 
HIS N   H    sing N N 222 
HIS N   H2   sing N N 223 
HIS CA  C    sing N N 224 
HIS CA  CB   sing N N 225 
HIS CA  HA   sing N N 226 
HIS C   O    doub N N 227 
HIS C   OXT  sing N N 228 
HIS CB  CG   sing N N 229 
HIS CB  HB2  sing N N 230 
HIS CB  HB3  sing N N 231 
HIS CG  ND1  sing Y N 232 
HIS CG  CD2  doub Y N 233 
HIS ND1 CE1  doub Y N 234 
HIS ND1 HD1  sing N N 235 
HIS CD2 NE2  sing Y N 236 
HIS CD2 HD2  sing N N 237 
HIS CE1 NE2  sing Y N 238 
HIS CE1 HE1  sing N N 239 
HIS NE2 HE2  sing N N 240 
HIS OXT HXT  sing N N 241 
HOH O   H1   sing N N 242 
HOH O   H2   sing N N 243 
ILE N   CA   sing N N 244 
ILE N   H    sing N N 245 
ILE N   H2   sing N N 246 
ILE CA  C    sing N N 247 
ILE CA  CB   sing N N 248 
ILE CA  HA   sing N N 249 
ILE C   O    doub N N 250 
ILE C   OXT  sing N N 251 
ILE CB  CG1  sing N N 252 
ILE CB  CG2  sing N N 253 
ILE CB  HB   sing N N 254 
ILE CG1 CD1  sing N N 255 
ILE CG1 HG12 sing N N 256 
ILE CG1 HG13 sing N N 257 
ILE CG2 HG21 sing N N 258 
ILE CG2 HG22 sing N N 259 
ILE CG2 HG23 sing N N 260 
ILE CD1 HD11 sing N N 261 
ILE CD1 HD12 sing N N 262 
ILE CD1 HD13 sing N N 263 
ILE OXT HXT  sing N N 264 
LEU N   CA   sing N N 265 
LEU N   H    sing N N 266 
LEU N   H2   sing N N 267 
LEU CA  C    sing N N 268 
LEU CA  CB   sing N N 269 
LEU CA  HA   sing N N 270 
LEU C   O    doub N N 271 
LEU C   OXT  sing N N 272 
LEU CB  CG   sing N N 273 
LEU CB  HB2  sing N N 274 
LEU CB  HB3  sing N N 275 
LEU CG  CD1  sing N N 276 
LEU CG  CD2  sing N N 277 
LEU CG  HG   sing N N 278 
LEU CD1 HD11 sing N N 279 
LEU CD1 HD12 sing N N 280 
LEU CD1 HD13 sing N N 281 
LEU CD2 HD21 sing N N 282 
LEU CD2 HD22 sing N N 283 
LEU CD2 HD23 sing N N 284 
LEU OXT HXT  sing N N 285 
LYS N   CA   sing N N 286 
LYS N   H    sing N N 287 
LYS N   H2   sing N N 288 
LYS CA  C    sing N N 289 
LYS CA  CB   sing N N 290 
LYS CA  HA   sing N N 291 
LYS C   O    doub N N 292 
LYS C   OXT  sing N N 293 
LYS CB  CG   sing N N 294 
LYS CB  HB2  sing N N 295 
LYS CB  HB3  sing N N 296 
LYS CG  CD   sing N N 297 
LYS CG  HG2  sing N N 298 
LYS CG  HG3  sing N N 299 
LYS CD  CE   sing N N 300 
LYS CD  HD2  sing N N 301 
LYS CD  HD3  sing N N 302 
LYS CE  NZ   sing N N 303 
LYS CE  HE2  sing N N 304 
LYS CE  HE3  sing N N 305 
LYS NZ  HZ1  sing N N 306 
LYS NZ  HZ2  sing N N 307 
LYS NZ  HZ3  sing N N 308 
LYS OXT HXT  sing N N 309 
MET N   CA   sing N N 310 
MET N   H    sing N N 311 
MET N   H2   sing N N 312 
MET CA  C    sing N N 313 
MET CA  CB   sing N N 314 
MET CA  HA   sing N N 315 
MET C   O    doub N N 316 
MET C   OXT  sing N N 317 
MET CB  CG   sing N N 318 
MET CB  HB2  sing N N 319 
MET CB  HB3  sing N N 320 
MET CG  SD   sing N N 321 
MET CG  HG2  sing N N 322 
MET CG  HG3  sing N N 323 
MET SD  CE   sing N N 324 
MET CE  HE1  sing N N 325 
MET CE  HE2  sing N N 326 
MET CE  HE3  sing N N 327 
MET OXT HXT  sing N N 328 
OAA O1  C1   doub N N 329 
OAA O2  C1   sing N N 330 
OAA O4  C4   doub N N 331 
OAA O5  C4   sing N N 332 
OAA O5  HO5  sing N N 333 
OAA O3  C3   doub N N 334 
OAA C1  C2   sing N N 335 
OAA C2  C3   sing N N 336 
OAA C2  H21  sing N N 337 
OAA C2  H22  sing N N 338 
OAA C3  C4   sing N N 339 
PHE N   CA   sing N N 340 
PHE N   H    sing N N 341 
PHE N   H2   sing N N 342 
PHE CA  C    sing N N 343 
PHE CA  CB   sing N N 344 
PHE CA  HA   sing N N 345 
PHE C   O    doub N N 346 
PHE C   OXT  sing N N 347 
PHE CB  CG   sing N N 348 
PHE CB  HB2  sing N N 349 
PHE CB  HB3  sing N N 350 
PHE CG  CD1  doub Y N 351 
PHE CG  CD2  sing Y N 352 
PHE CD1 CE1  sing Y N 353 
PHE CD1 HD1  sing N N 354 
PHE CD2 CE2  doub Y N 355 
PHE CD2 HD2  sing N N 356 
PHE CE1 CZ   doub Y N 357 
PHE CE1 HE1  sing N N 358 
PHE CE2 CZ   sing Y N 359 
PHE CE2 HE2  sing N N 360 
PHE CZ  HZ   sing N N 361 
PHE OXT HXT  sing N N 362 
PRO N   CA   sing N N 363 
PRO N   CD   sing N N 364 
PRO N   H    sing N N 365 
PRO CA  C    sing N N 366 
PRO CA  CB   sing N N 367 
PRO CA  HA   sing N N 368 
PRO C   O    doub N N 369 
PRO C   OXT  sing N N 370 
PRO CB  CG   sing N N 371 
PRO CB  HB2  sing N N 372 
PRO CB  HB3  sing N N 373 
PRO CG  CD   sing N N 374 
PRO CG  HG2  sing N N 375 
PRO CG  HG3  sing N N 376 
PRO CD  HD2  sing N N 377 
PRO CD  HD3  sing N N 378 
PRO OXT HXT  sing N N 379 
SER N   CA   sing N N 380 
SER N   H    sing N N 381 
SER N   H2   sing N N 382 
SER CA  C    sing N N 383 
SER CA  CB   sing N N 384 
SER CA  HA   sing N N 385 
SER C   O    doub N N 386 
SER C   OXT  sing N N 387 
SER CB  OG   sing N N 388 
SER CB  HB2  sing N N 389 
SER CB  HB3  sing N N 390 
SER OG  HG   sing N N 391 
SER OXT HXT  sing N N 392 
THR N   CA   sing N N 393 
THR N   H    sing N N 394 
THR N   H2   sing N N 395 
THR CA  C    sing N N 396 
THR CA  CB   sing N N 397 
THR CA  HA   sing N N 398 
THR C   O    doub N N 399 
THR C   OXT  sing N N 400 
THR CB  OG1  sing N N 401 
THR CB  CG2  sing N N 402 
THR CB  HB   sing N N 403 
THR OG1 HG1  sing N N 404 
THR CG2 HG21 sing N N 405 
THR CG2 HG22 sing N N 406 
THR CG2 HG23 sing N N 407 
THR OXT HXT  sing N N 408 
TRP N   CA   sing N N 409 
TRP N   H    sing N N 410 
TRP N   H2   sing N N 411 
TRP CA  C    sing N N 412 
TRP CA  CB   sing N N 413 
TRP CA  HA   sing N N 414 
TRP C   O    doub N N 415 
TRP C   OXT  sing N N 416 
TRP CB  CG   sing N N 417 
TRP CB  HB2  sing N N 418 
TRP CB  HB3  sing N N 419 
TRP CG  CD1  doub Y N 420 
TRP CG  CD2  sing Y N 421 
TRP CD1 NE1  sing Y N 422 
TRP CD1 HD1  sing N N 423 
TRP CD2 CE2  doub Y N 424 
TRP CD2 CE3  sing Y N 425 
TRP NE1 CE2  sing Y N 426 
TRP NE1 HE1  sing N N 427 
TRP CE2 CZ2  sing Y N 428 
TRP CE3 CZ3  doub Y N 429 
TRP CE3 HE3  sing N N 430 
TRP CZ2 CH2  doub Y N 431 
TRP CZ2 HZ2  sing N N 432 
TRP CZ3 CH2  sing Y N 433 
TRP CZ3 HZ3  sing N N 434 
TRP CH2 HH2  sing N N 435 
TRP OXT HXT  sing N N 436 
TYR N   CA   sing N N 437 
TYR N   H    sing N N 438 
TYR N   H2   sing N N 439 
TYR CA  C    sing N N 440 
TYR CA  CB   sing N N 441 
TYR CA  HA   sing N N 442 
TYR C   O    doub N N 443 
TYR C   OXT  sing N N 444 
TYR CB  CG   sing N N 445 
TYR CB  HB2  sing N N 446 
TYR CB  HB3  sing N N 447 
TYR CG  CD1  doub Y N 448 
TYR CG  CD2  sing Y N 449 
TYR CD1 CE1  sing Y N 450 
TYR CD1 HD1  sing N N 451 
TYR CD2 CE2  doub Y N 452 
TYR CD2 HD2  sing N N 453 
TYR CE1 CZ   doub Y N 454 
TYR CE1 HE1  sing N N 455 
TYR CE2 CZ   sing Y N 456 
TYR CE2 HE2  sing N N 457 
TYR CZ  OH   sing N N 458 
TYR OH  HH   sing N N 459 
TYR OXT HXT  sing N N 460 
VAL N   CA   sing N N 461 
VAL N   H    sing N N 462 
VAL N   H2   sing N N 463 
VAL CA  C    sing N N 464 
VAL CA  CB   sing N N 465 
VAL CA  HA   sing N N 466 
VAL C   O    doub N N 467 
VAL C   OXT  sing N N 468 
VAL CB  CG1  sing N N 469 
VAL CB  CG2  sing N N 470 
VAL CB  HB   sing N N 471 
VAL CG1 HG11 sing N N 472 
VAL CG1 HG12 sing N N 473 
VAL CG1 HG13 sing N N 474 
VAL CG2 HG21 sing N N 475 
VAL CG2 HG22 sing N N 476 
VAL CG2 HG23 sing N N 477 
VAL OXT HXT  sing N N 478 
# 
_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                    8ZVR 
_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]   0.017264 
_atom_sites.fract_transf_matrix[1][2]   0.008569 
_atom_sites.fract_transf_matrix[1][3]   0.005563 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.018690 
_atom_sites.fract_transf_matrix[2][3]   0.005968 
_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]   0.014498 
_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   ? 48.733  4.451   -13.938 1.00 68.31  ? 30  SER A N   1 
ATOM   2    C CA  . SER A 1 1   ? 48.747  4.121   -15.397 1.00 75.77  ? 30  SER A CA  1 
ATOM   3    C C   . SER A 1 1   ? 47.473  3.377   -15.814 1.00 75.45  ? 30  SER A C   1 
ATOM   4    O O   . SER A 1 1   ? 46.696  3.809   -16.688 1.00 47.93  ? 30  SER A O   1 
ATOM   5    C CB  . SER A 1 1   ? 49.966  3.295   -15.768 1.00 77.66  ? 30  SER A CB  1 
ATOM   6    O OG  . SER A 1 1   ? 49.909  2.888   -17.132 1.00 79.68  ? 30  SER A OG  1 
ATOM   7    N N   . THR A 1 2   ? 47.302  2.199   -15.208 1.00 72.58  ? 31  THR A N   1 
ATOM   8    C CA  . THR A 1 2   ? 46.085  1.438   -15.408 1.00 67.11  ? 31  THR A CA  1 
ATOM   9    C C   . THR A 1 2   ? 45.390  1.184   -14.073 1.00 56.49  ? 31  THR A C   1 
ATOM   10   O O   . THR A 1 2   ? 44.201  0.874   -14.134 1.00 55.40  ? 31  THR A O   1 
ATOM   11   C CB  . THR A 1 2   ? 46.348  0.147   -16.187 1.00 66.29  ? 31  THR A CB  1 
ATOM   12   O OG1 . THR A 1 2   ? 47.727  -0.139  -15.971 1.00 70.07  ? 31  THR A OG1 1 
ATOM   13   C CG2 . THR A 1 2   ? 46.053  0.299   -17.670 1.00 61.70  ? 31  THR A CG2 1 
ATOM   14   N N   . ASN A 1 3   ? 46.072  1.309   -12.903 1.00 44.06  ? 32  ASN A N   1 
ATOM   15   C CA  . ASN A 1 3   ? 45.378  0.997   -11.657 1.00 33.80  ? 32  ASN A CA  1 
ATOM   16   C C   . ASN A 1 3   ? 44.562  2.208   -11.241 1.00 27.44  ? 32  ASN A C   1 
ATOM   17   O O   . ASN A 1 3   ? 45.083  3.215   -10.765 1.00 23.24  ? 32  ASN A O   1 
ATOM   18   C CB  . ASN A 1 3   ? 46.204  0.490   -10.483 1.00 31.62  ? 32  ASN A CB  1 
ATOM   19   C CG  . ASN A 1 3   ? 45.309  -0.175  -9.446  1.00 34.33  ? 32  ASN A CG  1 
ATOM   20   O OD1 . ASN A 1 3   ? 44.167  0.243   -9.187  1.00 29.83  ? 32  ASN A OD1 1 
ATOM   21   N ND2 . ASN A 1 3   ? 45.765  -1.282  -8.901  1.00 38.17  ? 32  ASN A ND2 1 
ATOM   22   N N   . LEU A 1 4   ? 43.248  2.060   -11.429 1.00 29.31  ? 33  LEU A N   1 
ATOM   23   C CA  . LEU A 1 4   ? 42.302  3.130   -11.178 1.00 26.03  ? 33  LEU A CA  1 
ATOM   24   C C   . LEU A 1 4   ? 42.467  3.656   -9.764  1.00 23.49  ? 33  LEU A C   1 
ATOM   25   O O   . LEU A 1 4   ? 42.205  4.843   -9.526  1.00 24.50  ? 33  LEU A O   1 
ATOM   26   C CB  . LEU A 1 4   ? 40.902  2.565   -11.422 1.00 26.23  ? 33  LEU A CB  1 
ATOM   27   C CG  . LEU A 1 4   ? 39.718  3.468   -11.060 1.00 26.96  ? 33  LEU A CG  1 
ATOM   28   C CD1 . LEU A 1 4   ? 39.663  4.775   -11.845 1.00 25.24  ? 33  LEU A CD1 1 
ATOM   29   C CD2 . LEU A 1 4   ? 38.451  2.647   -11.270 1.00 26.98  ? 33  LEU A CD2 1 
ATOM   30   N N   . LYS A 1 5   ? 42.873  2.780   -8.828  1.00 22.99  ? 34  LYS A N   1 
ATOM   31   C CA  . LYS A 1 5   ? 42.930  3.181   -7.425  1.00 24.02  ? 34  LYS A CA  1 
ATOM   32   C C   . LYS A 1 5   ? 44.061  4.192   -7.186  1.00 23.55  ? 34  LYS A C   1 
ATOM   33   O O   . LYS A 1 5   ? 43.968  5.085   -6.352  1.00 23.06  ? 34  LYS A O   1 
ATOM   34   C CB  . LYS A 1 5   ? 43.065  1.922   -6.559  1.00 25.50  ? 34  LYS A CB  1 
ATOM   35   C CG  . LYS A 1 5   ? 42.764  2.137   -5.093  1.00 28.07  ? 34  LYS A CG  1 
ATOM   36   C CD  . LYS A 1 5   ? 42.901  0.866   -4.268  1.00 33.10  ? 34  LYS A CD  1 
ATOM   37   C CE  . LYS A 1 5   ? 42.415  1.029   -2.858  1.00 30.85  ? 34  LYS A CE  1 
ATOM   38   N NZ  . LYS A 1 5   ? 42.676  -0.255  -2.194  1.00 30.10  ? 34  LYS A NZ  1 
ATOM   39   N N   . ASP A 1 6   ? 45.181  3.993   -7.885  1.00 26.21  ? 35  ASP A N   1 
ATOM   40   C CA  . ASP A 1 6   ? 46.339  4.865   -7.790  1.00 27.10  ? 35  ASP A CA  1 
ATOM   41   C C   . ASP A 1 6   ? 46.052  6.186   -8.498  1.00 24.36  ? 35  ASP A C   1 
ATOM   42   O O   . ASP A 1 6   ? 46.462  7.225   -8.005  1.00 24.01  ? 35  ASP A O   1 
ATOM   43   C CB  . ASP A 1 6   ? 47.568  4.176   -8.346  1.00 29.91  ? 35  ASP A CB  1 
ATOM   44   C CG  . ASP A 1 6   ? 48.006  2.969   -7.531  1.00 36.53  ? 35  ASP A CG  1 
ATOM   45   O OD1 . ASP A 1 6   ? 48.105  3.112   -6.291  1.00 29.96  ? 35  ASP A OD1 1 
ATOM   46   O OD2 . ASP A 1 6   ? 48.242  1.897   -8.148  1.00 42.95  ? 35  ASP A OD2 1 
ATOM   47   N N   . ILE A 1 7   ? 45.311  6.142   -9.621  1.00 25.36  ? 36  ILE A N   1 
ATOM   48   C CA  . ILE A 1 7   ? 44.949  7.336   -10.362 1.00 26.56  ? 36  ILE A CA  1 
ATOM   49   C C   . ILE A 1 7   ? 44.021  8.183   -9.491  1.00 29.35  ? 36  ILE A C   1 
ATOM   50   O O   . ILE A 1 7   ? 44.155  9.410   -9.412  1.00 30.71  ? 36  ILE A O   1 
ATOM   51   C CB  . ILE A 1 7   ? 44.351  6.953   -11.741 1.00 31.37  ? 36  ILE A CB  1 
ATOM   52   C CG1 . ILE A 1 7   ? 45.439  6.354   -12.669 1.00 31.04  ? 36  ILE A CG1 1 
ATOM   53   C CG2 . ILE A 1 7   ? 43.697  8.154   -12.415 1.00 31.55  ? 36  ILE A CG2 1 
ATOM   54   C CD1 . ILE A 1 7   ? 44.965  5.226   -13.565 1.00 34.63  ? 36  ILE A CD1 1 
ATOM   55   N N   . LEU A 1 8   ? 43.119  7.509   -8.776  1.00 27.26  ? 37  LEU A N   1 
ATOM   56   C CA  . LEU A 1 8   ? 42.177  8.177   -7.898  1.00 26.68  ? 37  LEU A CA  1 
ATOM   57   C C   . LEU A 1 8   ? 42.910  8.745   -6.679  1.00 27.28  ? 37  LEU A C   1 
ATOM   58   O O   . LEU A 1 8   ? 42.717  9.910   -6.327  1.00 29.83  ? 37  LEU A O   1 
ATOM   59   C CB  . LEU A 1 8   ? 41.132  7.096   -7.629  1.00 25.73  ? 37  LEU A CB  1 
ATOM   60   C CG  . LEU A 1 8   ? 39.929  7.460   -6.770  1.00 32.38  ? 37  LEU A CG  1 
ATOM   61   C CD1 . LEU A 1 8   ? 39.301  8.781   -7.179  1.00 32.53  ? 37  LEU A CD1 1 
ATOM   62   C CD2 . LEU A 1 8   ? 38.931  6.291   -6.833  1.00 33.73  ? 37  LEU A CD2 1 
ATOM   63   N N   . ALA A 1 9   ? 43.840  7.986   -6.089  1.00 23.63  ? 38  ALA A N   1 
ATOM   64   C CA  . ALA A 1 9   ? 44.616  8.495   -4.966  1.00 25.83  ? 38  ALA A CA  1 
ATOM   65   C C   . ALA A 1 9   ? 45.336  9.797   -5.317  1.00 27.76  ? 38  ALA A C   1 
ATOM   66   O O   . ALA A 1 9   ? 45.470  10.680  -4.459  1.00 24.12  ? 38  ALA A O   1 
ATOM   67   C CB  . ALA A 1 9   ? 45.619  7.444   -4.490  1.00 26.44  ? 38  ALA A CB  1 
ATOM   68   N N   . ASP A 1 10  ? 45.746  9.965   -6.578  1.00 26.63  ? 39  ASP A N   1 
ATOM   69   C CA  . ASP A 1 10  ? 46.485  11.171  -6.955  1.00 27.24  ? 39  ASP A CA  1 
ATOM   70   C C   . ASP A 1 10  ? 45.577  12.384  -7.165  1.00 29.21  ? 39  ASP A C   1 
ATOM   71   O O   . ASP A 1 10  ? 46.022  13.511  -6.948  1.00 31.69  ? 39  ASP A O   1 
ATOM   72   C CB  . ASP A 1 10  ? 47.383  10.927  -8.151  1.00 28.11  ? 39  ASP A CB  1 
ATOM   73   C CG  . ASP A 1 10  ? 48.579  10.007  -7.860  1.00 29.23  ? 39  ASP A CG  1 
ATOM   74   O OD1 . ASP A 1 10  ? 48.961  9.835   -6.682  1.00 35.29  ? 39  ASP A OD1 1 
ATOM   75   O OD2 . ASP A 1 10  ? 49.146  9.482   -8.813  1.00 34.98  ? 39  ASP A OD2 1 
ATOM   76   N N   . LEU A 1 11  ? 44.331  12.148  -7.593  1.00 24.86  ? 40  LEU A N   1 
ATOM   77   C CA  . LEU A 1 11  ? 43.356  13.195  -7.893  1.00 26.44  ? 40  LEU A CA  1 
ATOM   78   C C   . LEU A 1 11  ? 42.745  13.759  -6.615  1.00 24.90  ? 40  LEU A C   1 
ATOM   79   O O   . LEU A 1 11  ? 42.385  14.926  -6.573  1.00 26.62  ? 40  LEU A O   1 
ATOM   80   C CB  . LEU A 1 11  ? 42.235  12.649  -8.768  1.00 27.45  ? 40  LEU A CB  1 
ATOM   81   C CG  . LEU A 1 11  ? 42.569  12.298  -10.223 1.00 31.17  ? 40  LEU A CG  1 
ATOM   82   C CD1 . LEU A 1 11  ? 41.432  11.447  -10.795 1.00 31.78  ? 40  LEU A CD1 1 
ATOM   83   C CD2 . LEU A 1 11  ? 42.755  13.549  -11.055 1.00 31.56  ? 40  LEU A CD2 1 
ATOM   84   N N   . ILE A 1 12  ? 42.629  12.940  -5.570  1.00 26.01  ? 41  ILE A N   1 
ATOM   85   C CA  . ILE A 1 12  ? 41.835  13.316  -4.416  1.00 24.26  ? 41  ILE A CA  1 
ATOM   86   C C   . ILE A 1 12  ? 42.382  14.541  -3.687  1.00 28.34  ? 41  ILE A C   1 
ATOM   87   O O   . ILE A 1 12  ? 41.631  15.473  -3.401  1.00 29.13  ? 41  ILE A O   1 
ATOM   88   C CB  . ILE A 1 12  ? 41.658  12.117  -3.484  1.00 21.48  ? 41  ILE A CB  1 
ATOM   89   C CG1 . ILE A 1 12  ? 40.642  11.135  -4.055  1.00 19.61  ? 41  ILE A CG1 1 
ATOM   90   C CG2 . ILE A 1 12  ? 41.234  12.602  -2.113  1.00 21.89  ? 41  ILE A CG2 1 
ATOM   91   C CD1 . ILE A 1 12  ? 40.732  9.756   -3.437  1.00 20.37  ? 41  ILE A CD1 1 
ATOM   92   N N   . PRO A 1 13  ? 43.695  14.614  -3.364  1.00 30.11  ? 42  PRO A N   1 
ATOM   93   C CA  . PRO A 1 13  ? 44.250  15.815  -2.715  1.00 29.45  ? 42  PRO A CA  1 
ATOM   94   C C   . PRO A 1 13  ? 43.951  17.136  -3.419  1.00 30.51  ? 42  PRO A C   1 
ATOM   95   O O   . PRO A 1 13  ? 43.654  18.152  -2.787  1.00 28.04  ? 42  PRO A O   1 
ATOM   96   C CB  . PRO A 1 13  ? 45.758  15.549  -2.690  1.00 29.31  ? 42  PRO A CB  1 
ATOM   97   C CG  . PRO A 1 13  ? 45.923  14.048  -2.842  1.00 30.46  ? 42  PRO A CG  1 
ATOM   98   C CD  . PRO A 1 13  ? 44.658  13.510  -3.479  1.00 28.86  ? 42  PRO A CD  1 
ATOM   99   N N   . LYS A 1 14  ? 44.096  17.105  -4.744  1.00 32.05  ? 43  LYS A N   1 
ATOM   100  C CA  . LYS A 1 14  ? 43.922  18.273  -5.576  1.00 34.80  ? 43  LYS A CA  1 
ATOM   101  C C   . LYS A 1 14  ? 42.539  18.850  -5.307  1.00 30.96  ? 43  LYS A C   1 
ATOM   102  O O   . LYS A 1 14  ? 42.377  20.048  -5.183  1.00 32.57  ? 43  LYS A O   1 
ATOM   103  C CB  . LYS A 1 14  ? 43.979  17.871  -7.056  1.00 40.57  ? 43  LYS A CB  1 
ATOM   104  C CG  . LYS A 1 14  ? 45.278  17.312  -7.630  1.00 51.65  ? 43  LYS A CG  1 
ATOM   105  C CD  . LYS A 1 14  ? 45.183  17.119  -9.144  1.00 55.64  ? 43  LYS A CD  1 
ATOM   106  C CE  . LYS A 1 14  ? 46.434  17.466  -9.911  1.00 63.53  ? 43  LYS A CE  1 
ATOM   107  N NZ  . LYS A 1 14  ? 47.477  16.438  -9.836  1.00 60.18  ? 43  LYS A NZ  1 
ATOM   108  N N   . GLU A 1 15  ? 41.554  17.960  -5.256  1.00 31.83  ? 44  GLU A N   1 
ATOM   109  C CA  . GLU A 1 15  ? 40.153  18.329  -5.181  1.00 33.72  ? 44  GLU A CA  1 
ATOM   110  C C   . GLU A 1 15  ? 39.753  18.686  -3.752  1.00 27.08  ? 44  GLU A C   1 
ATOM   111  O O   . GLU A 1 15  ? 38.962  19.613  -3.546  1.00 28.60  ? 44  GLU A O   1 
ATOM   112  C CB  . GLU A 1 15  ? 39.304  17.172  -5.696  1.00 32.57  ? 44  GLU A CB  1 
ATOM   113  C CG  . GLU A 1 15  ? 37.882  17.612  -5.986  1.00 44.24  ? 44  GLU A CG  1 
ATOM   114  C CD  . GLU A 1 15  ? 37.757  18.452  -7.243  1.00 48.07  ? 44  GLU A CD  1 
ATOM   115  O OE1 . GLU A 1 15  ? 38.703  18.470  -8.077  1.00 54.20  ? 44  GLU A OE1 1 
ATOM   116  O OE2 . GLU A 1 15  ? 36.686  19.081  -7.366  1.00 53.86  ? 44  GLU A OE2 1 
ATOM   117  N N   . GLN A 1 16  ? 40.323  17.990  -2.778  1.00 25.84  ? 45  GLN A N   1 
ATOM   118  C CA  . GLN A 1 16  ? 40.168  18.384  -1.385  1.00 31.03  ? 45  GLN A CA  1 
ATOM   119  C C   . GLN A 1 16  ? 40.577  19.840  -1.169  1.00 33.19  ? 45  GLN A C   1 
ATOM   120  O O   . GLN A 1 16  ? 39.851  20.622  -0.538  1.00 29.71  ? 45  GLN A O   1 
ATOM   121  C CB  . GLN A 1 16  ? 41.010  17.538  -0.436  1.00 29.94  ? 45  GLN A CB  1 
ATOM   122  C CG  . GLN A 1 16  ? 40.467  16.121  -0.270  1.00 33.88  ? 45  GLN A CG  1 
ATOM   123  C CD  . GLN A 1 16  ? 41.419  15.192  0.464   1.00 33.63  ? 45  GLN A CD  1 
ATOM   124  O OE1 . GLN A 1 16  ? 42.642  15.340  0.412   1.00 33.73  ? 45  GLN A OE1 1 
ATOM   125  N NE2 . GLN A 1 16  ? 40.868  14.202  1.144   1.00 30.45  ? 45  GLN A NE2 1 
ATOM   126  N N   . ALA A 1 17  ? 41.756  20.190  -1.694  1.00 35.32  ? 46  ALA A N   1 
ATOM   127  C CA  . ALA A 1 17  ? 42.311  21.510  -1.454  1.00 36.64  ? 46  ALA A CA  1 
ATOM   128  C C   . ALA A 1 17  ? 41.454  22.555  -2.169  1.00 36.89  ? 46  ALA A C   1 
ATOM   129  O O   . ALA A 1 17  ? 41.234  23.640  -1.624  1.00 35.11  ? 46  ALA A O   1 
ATOM   130  C CB  . ALA A 1 17  ? 43.774  21.536  -1.881  1.00 38.06  ? 46  ALA A CB  1 
ATOM   131  N N   . ARG A 1 18  ? 40.930  22.187  -3.349  1.00 30.56  ? 47  ARG A N   1 
ATOM   132  C CA  . ARG A 1 18  ? 40.072  23.064  -4.136  1.00 33.99  ? 47  ARG A CA  1 
ATOM   133  C C   . ARG A 1 18  ? 38.766  23.381  -3.408  1.00 34.10  ? 47  ARG A C   1 
ATOM   134  O O   . ARG A 1 18  ? 38.290  24.508  -3.427  1.00 36.95  ? 47  ARG A O   1 
ATOM   135  C CB  . ARG A 1 18  ? 39.836  22.392  -5.488  1.00 34.59  ? 47  ARG A CB  1 
ATOM   136  C CG  . ARG A 1 18  ? 38.808  23.022  -6.409  1.00 41.76  ? 47  ARG A CG  1 
ATOM   137  C CD  . ARG A 1 18  ? 38.936  22.387  -7.791  1.00 50.68  ? 47  ARG A CD  1 
ATOM   138  N NE  . ARG A 1 18  ? 37.758  22.615  -8.633  1.00 58.40  ? 47  ARG A NE  1 
ATOM   139  C CZ  . ARG A 1 18  ? 37.546  22.010  -9.806  1.00 69.16  ? 47  ARG A CZ  1 
ATOM   140  N NH1 . ARG A 1 18  ? 38.470  21.196  -10.301 1.00 67.98  ? 47  ARG A NH1 1 
ATOM   141  N NH2 . ARG A 1 18  ? 36.420  22.218  -10.480 1.00 65.13  ? 47  ARG A NH2 1 
ATOM   142  N N   . ILE A 1 19  ? 38.151  22.377  -2.795  1.00 29.75  ? 48  ILE A N   1 
ATOM   143  C CA  . ILE A 1 19  ? 36.951  22.599  -2.025  1.00 29.36  ? 48  ILE A CA  1 
ATOM   144  C C   . ILE A 1 19  ? 37.271  23.378  -0.750  1.00 29.18  ? 48  ILE A C   1 
ATOM   145  O O   . ILE A 1 19  ? 36.475  24.195  -0.331  1.00 27.87  ? 48  ILE A O   1 
ATOM   146  C CB  . ILE A 1 19  ? 36.255  21.256  -1.748  1.00 27.08  ? 48  ILE A CB  1 
ATOM   147  C CG1 . ILE A 1 19  ? 35.789  20.652  -3.073  1.00 26.32  ? 48  ILE A CG1 1 
ATOM   148  C CG2 . ILE A 1 19  ? 35.115  21.432  -0.748  1.00 24.33  ? 48  ILE A CG2 1 
ATOM   149  C CD1 . ILE A 1 19  ? 35.440  19.180  -2.994  1.00 28.55  ? 48  ILE A CD1 1 
ATOM   150  N N   . LYS A 1 20  ? 38.414  23.119  -0.119  1.00 31.17  ? 49  LYS A N   1 
ATOM   151  C CA  . LYS A 1 20  ? 38.749  23.787  1.131   1.00 34.26  ? 49  LYS A CA  1 
ATOM   152  C C   . LYS A 1 20  ? 38.807  25.294  0.888   1.00 36.96  ? 49  LYS A C   1 
ATOM   153  O O   . LYS A 1 20  ? 38.253  26.061  1.667   1.00 37.44  ? 49  LYS A O   1 
ATOM   154  C CB  . LYS A 1 20  ? 40.062  23.214  1.669   1.00 35.57  ? 49  LYS A CB  1 
ATOM   155  C CG  . LYS A 1 20  ? 40.524  23.669  3.037   1.00 39.88  ? 49  LYS A CG  1 
ATOM   156  C CD  . LYS A 1 20  ? 41.875  23.058  3.401   1.00 41.74  ? 49  LYS A CD  1 
ATOM   157  C CE  . LYS A 1 20  ? 42.641  23.815  4.426   1.00 47.51  ? 49  LYS A CE  1 
ATOM   158  N NZ  . LYS A 1 20  ? 41.993  23.724  5.731   1.00 48.86  ? 49  LYS A NZ  1 
ATOM   159  N N   . THR A 1 21  ? 39.470  25.684  -0.203  1.00 34.67  ? 50  THR A N   1 
ATOM   160  C CA  . THR A 1 21  ? 39.645  27.078  -0.559  1.00 42.66  ? 50  THR A CA  1 
ATOM   161  C C   . THR A 1 21  ? 38.273  27.693  -0.831  1.00 43.61  ? 50  THR A C   1 
ATOM   162  O O   . THR A 1 21  ? 37.913  28.717  -0.242  1.00 42.61  ? 50  THR A O   1 
ATOM   163  C CB  . THR A 1 21  ? 40.590  27.136  -1.763  1.00 43.00  ? 50  THR A CB  1 
ATOM   164  O OG1 . THR A 1 21  ? 41.789  26.561  -1.261  1.00 42.90  ? 50  THR A OG1 1 
ATOM   165  C CG2 . THR A 1 21  ? 40.902  28.542  -2.247  1.00 44.64  ? 50  THR A CG2 1 
ATOM   166  N N   . PHE A 1 22  ? 37.502  27.028  -1.705  1.00 41.14  ? 51  PHE A N   1 
ATOM   167  C CA  . PHE A 1 22  ? 36.173  27.492  -2.086  1.00 38.68  ? 51  PHE A CA  1 
ATOM   168  C C   . PHE A 1 22  ? 35.284  27.735  -0.853  1.00 33.09  ? 51  PHE A C   1 
ATOM   169  O O   . PHE A 1 22  ? 34.577  28.727  -0.776  1.00 36.35  ? 51  PHE A O   1 
ATOM   170  C CB  . PHE A 1 22  ? 35.632  26.491  -3.108  1.00 34.04  ? 51  PHE A CB  1 
ATOM   171  C CG  . PHE A 1 22  ? 34.224  26.812  -3.587  1.00 34.35  ? 51  PHE A CG  1 
ATOM   172  C CD1 . PHE A 1 22  ? 33.930  28.060  -4.117  1.00 37.10  ? 51  PHE A CD1 1 
ATOM   173  C CD2 . PHE A 1 22  ? 33.189  25.889  -3.440  1.00 34.39  ? 51  PHE A CD2 1 
ATOM   174  C CE1 . PHE A 1 22  ? 32.638  28.370  -4.522  1.00 38.86  ? 51  PHE A CE1 1 
ATOM   175  C CE2 . PHE A 1 22  ? 31.904  26.196  -3.856  1.00 39.29  ? 51  PHE A CE2 1 
ATOM   176  C CZ  . PHE A 1 22  ? 31.625  27.443  -4.380  1.00 39.60  ? 51  PHE A CZ  1 
ATOM   177  N N   . ARG A 1 23  ? 35.307  26.854  0.128   1.00 31.64  ? 52  ARG A N   1 
ATOM   178  C CA  . ARG A 1 23  ? 34.447  26.992  1.290   1.00 35.15  ? 52  ARG A CA  1 
ATOM   179  C C   . ARG A 1 23  ? 34.947  28.078  2.244   1.00 37.64  ? 52  ARG A C   1 
ATOM   180  O O   . ARG A 1 23  ? 34.134  28.741  2.876   1.00 31.17  ? 52  ARG A O   1 
ATOM   181  C CB  . ARG A 1 23  ? 34.313  25.702  2.097   1.00 31.15  ? 52  ARG A CB  1 
ATOM   182  C CG  . ARG A 1 23  ? 33.672  24.619  1.239   1.00 33.60  ? 52  ARG A CG  1 
ATOM   183  C CD  . ARG A 1 23  ? 33.562  23.351  2.021   1.00 32.71  ? 52  ARG A CD  1 
ATOM   184  N NE  . ARG A 1 23  ? 32.641  23.573  3.134   1.00 39.45  ? 52  ARG A NE  1 
ATOM   185  C CZ  . ARG A 1 23  ? 32.447  22.701  4.097   1.00 43.10  ? 52  ARG A CZ  1 
ATOM   186  N NH1 . ARG A 1 23  ? 33.098  21.552  4.049   1.00 41.59  ? 52  ARG A NH1 1 
ATOM   187  N NH2 . ARG A 1 23  ? 31.590  22.979  5.075   1.00 40.91  ? 52  ARG A NH2 1 
ATOM   188  N N   . GLN A 1 24  ? 36.264  28.260  2.366   1.00 38.90  ? 53  GLN A N   1 
ATOM   189  C CA  . GLN A 1 24  ? 36.781  29.385  3.145   1.00 44.81  ? 53  GLN A CA  1 
ATOM   190  C C   . GLN A 1 24  ? 36.265  30.704  2.573   1.00 38.91  ? 53  GLN A C   1 
ATOM   191  O O   . GLN A 1 24  ? 35.761  31.536  3.311   1.00 49.72  ? 53  GLN A O   1 
ATOM   192  C CB  . GLN A 1 24  ? 38.306  29.450  3.202   1.00 47.84  ? 53  GLN A CB  1 
ATOM   193  C CG  . GLN A 1 24  ? 38.967  28.345  4.020   1.00 47.96  ? 53  GLN A CG  1 
ATOM   194  C CD  . GLN A 1 24  ? 40.415  28.134  3.621   1.00 48.32  ? 53  GLN A CD  1 
ATOM   195  O OE1 . GLN A 1 24  ? 40.911  28.683  2.629   1.00 49.03  ? 53  GLN A OE1 1 
ATOM   196  N NE2 . GLN A 1 24  ? 41.103  27.303  4.379   1.00 47.64  ? 53  GLN A NE2 1 
ATOM   197  N N   . GLN A 1 25  ? 36.383  30.894  1.264   1.00 46.08  ? 54  GLN A N   1 
ATOM   198  C CA  . GLN A 1 25  ? 36.016  32.159  0.651   1.00 49.29  ? 54  GLN A CA  1 
ATOM   199  C C   . GLN A 1 25  ? 34.500  32.307  0.496   1.00 49.20  ? 54  GLN A C   1 
ATOM   200  O O   . GLN A 1 25  ? 33.961  33.372  0.778   1.00 50.95  ? 54  GLN A O   1 
ATOM   201  C CB  . GLN A 1 25  ? 36.787  32.246  -0.658  1.00 52.38  ? 54  GLN A CB  1 
ATOM   202  C CG  . GLN A 1 25  ? 38.296  32.240  -0.445  1.00 56.01  ? 54  GLN A CG  1 
ATOM   203  C CD  . GLN A 1 25  ? 39.084  32.400  -1.726  1.00 69.61  ? 54  GLN A CD  1 
ATOM   204  O OE1 . GLN A 1 25  ? 40.324  32.419  -1.719  1.00 71.99  ? 54  GLN A OE1 1 
ATOM   205  N NE2 . GLN A 1 25  ? 38.374  32.517  -2.843  1.00 72.31  ? 54  GLN A NE2 1 
ATOM   206  N N   . HIS A 1 26  ? 33.799  31.247  0.077   1.00 44.07  ? 55  HIS A N   1 
ATOM   207  C CA  . HIS A 1 26  ? 32.432  31.392  -0.406  1.00 42.65  ? 55  HIS A CA  1 
ATOM   208  C C   . HIS A 1 26  ? 31.455  30.535  0.380   1.00 41.50  ? 55  HIS A C   1 
ATOM   209  O O   . HIS A 1 26  ? 30.297  30.403  -0.019  1.00 42.01  ? 55  HIS A O   1 
ATOM   210  C CB  . HIS A 1 26  ? 32.333  31.071  -1.904  1.00 46.03  ? 55  HIS A CB  1 
ATOM   211  C CG  . HIS A 1 26  ? 33.280  31.850  -2.751  1.00 57.69  ? 55  HIS A CG  1 
ATOM   212  N ND1 . HIS A 1 26  ? 32.968  33.055  -3.342  1.00 66.55  ? 55  HIS A ND1 1 
ATOM   213  C CD2 . HIS A 1 26  ? 34.542  31.585  -3.116  1.00 70.36  ? 55  HIS A CD2 1 
ATOM   214  C CE1 . HIS A 1 26  ? 34.017  33.489  -4.035  1.00 71.25  ? 55  HIS A CE1 1 
ATOM   215  N NE2 . HIS A 1 26  ? 34.988  32.618  -3.902  1.00 68.52  ? 55  HIS A NE2 1 
ATOM   216  N N   . GLY A 1 27  ? 31.907  29.989  1.507   1.00 36.22  ? 56  GLY A N   1 
ATOM   217  C CA  . GLY A 1 27  ? 31.093  29.067  2.276   1.00 36.44  ? 56  GLY A CA  1 
ATOM   218  C C   . GLY A 1 27  ? 29.791  29.709  2.753   1.00 36.22  ? 56  GLY A C   1 
ATOM   219  O O   . GLY A 1 27  ? 28.763  29.030  2.882   1.00 30.15  ? 56  GLY A O   1 
ATOM   220  N N   . LYS A 1 28  ? 29.845  31.016  3.037   1.00 35.37  ? 57  LYS A N   1 
ATOM   221  C CA  . LYS A 1 28  ? 28.667  31.714  3.522   1.00 37.72  ? 57  LYS A CA  1 
ATOM   222  C C   . LYS A 1 28  ? 27.867  32.343  2.377   1.00 31.41  ? 57  LYS A C   1 
ATOM   223  O O   . LYS A 1 28  ? 26.879  33.007  2.625   1.00 33.13  ? 57  LYS A O   1 
ATOM   224  C CB  . LYS A 1 28  ? 29.081  32.727  4.599   1.00 46.13  ? 57  LYS A CB  1 
ATOM   225  C CG  . LYS A 1 28  ? 29.635  32.102  5.871   1.00 49.13  ? 57  LYS A CG  1 
ATOM   226  C CD  . LYS A 1 28  ? 30.386  33.055  6.796   1.00 56.75  ? 57  LYS A CD  1 
ATOM   227  C CE  . LYS A 1 28  ? 30.776  32.389  8.089   1.00 61.91  ? 57  LYS A CE  1 
ATOM   228  N NZ  . LYS A 1 28  ? 31.202  33.332  9.133   1.00 63.68  ? 57  LYS A NZ  1 
ATOM   229  N N   . THR A 1 29  ? 28.264  32.157  1.120   1.00 35.85  ? 58  THR A N   1 
ATOM   230  C CA  . THR A 1 29  ? 27.462  32.671  0.019   1.00 34.57  ? 58  THR A CA  1 
ATOM   231  C C   . THR A 1 29  ? 26.096  31.974  0.025   1.00 35.19  ? 58  THR A C   1 
ATOM   232  O O   . THR A 1 29  ? 26.000  30.761  0.162   1.00 30.86  ? 58  THR A O   1 
ATOM   233  C CB  . THR A 1 29  ? 28.195  32.461  -1.300  1.00 37.48  ? 58  THR A CB  1 
ATOM   234  O OG1 . THR A 1 29  ? 29.450  33.104  -1.163  1.00 43.22  ? 58  THR A OG1 1 
ATOM   235  C CG2 . THR A 1 29  ? 27.475  33.047  -2.502  1.00 38.97  ? 58  THR A CG2 1 
ATOM   236  N N   . VAL A 1 30  ? 25.035  32.759  -0.152  1.00 32.32  ? 59  VAL A N   1 
ATOM   237  C CA  . VAL A 1 30  ? 23.686  32.233  -0.181  1.00 31.90  ? 59  VAL A CA  1 
ATOM   238  C C   . VAL A 1 30  ? 23.352  31.879  -1.630  1.00 35.34  ? 59  VAL A C   1 
ATOM   239  O O   . VAL A 1 30  ? 23.451  32.719  -2.521  1.00 35.11  ? 59  VAL A O   1 
ATOM   240  C CB  . VAL A 1 30  ? 22.707  33.247  0.459   1.00 32.80  ? 59  VAL A CB  1 
ATOM   241  C CG1 . VAL A 1 30  ? 21.251  32.938  0.163   1.00 34.44  ? 59  VAL A CG1 1 
ATOM   242  C CG2 . VAL A 1 30  ? 22.860  33.307  1.971   1.00 31.91  ? 59  VAL A CG2 1 
ATOM   243  N N   . VAL A 1 31  ? 22.967  30.613  -1.870  1.00 33.80  ? 60  VAL A N   1 
ATOM   244  C CA  . VAL A 1 31  ? 22.722  30.150  -3.225  1.00 31.54  ? 60  VAL A CA  1 
ATOM   245  C C   . VAL A 1 31  ? 21.233  29.940  -3.493  1.00 28.93  ? 60  VAL A C   1 
ATOM   246  O O   . VAL A 1 31  ? 20.867  29.675  -4.632  1.00 28.66  ? 60  VAL A O   1 
ATOM   247  C CB  . VAL A 1 31  ? 23.491  28.857  -3.492  1.00 30.64  ? 60  VAL A CB  1 
ATOM   248  C CG1 . VAL A 1 31  ? 24.989  29.100  -3.473  1.00 34.76  ? 60  VAL A CG1 1 
ATOM   249  C CG2 . VAL A 1 31  ? 23.057  27.747  -2.546  1.00 32.11  ? 60  VAL A CG2 1 
ATOM   250  N N   . GLY A 1 32  ? 20.387  30.015  -2.461  1.00 33.39  ? 61  GLY A N   1 
ATOM   251  C CA  . GLY A 1 32  ? 18.946  29.911  -2.664  1.00 32.12  ? 61  GLY A CA  1 
ATOM   252  C C   . GLY A 1 32  ? 18.194  30.166  -1.364  1.00 29.05  ? 61  GLY A C   1 
ATOM   253  O O   . GLY A 1 32  ? 18.808  30.324  -0.313  1.00 29.11  ? 61  GLY A O   1 
ATOM   254  N N   . GLN A 1 33  ? 16.865  30.183  -1.450  1.00 28.11  ? 62  GLN A N   1 
ATOM   255  C CA  . GLN A 1 33  ? 16.009  30.385  -0.291  1.00 30.57  ? 62  GLN A CA  1 
ATOM   256  C C   . GLN A 1 33  ? 15.157  29.133  -0.077  1.00 32.16  ? 62  GLN A C   1 
ATOM   257  O O   . GLN A 1 33  ? 14.856  28.417  -1.035  1.00 32.36  ? 62  GLN A O   1 
ATOM   258  C CB  . GLN A 1 33  ? 15.129  31.616  -0.485  1.00 34.67  ? 62  GLN A CB  1 
ATOM   259  C CG  . GLN A 1 33  ? 15.784  32.759  -1.259  1.00 45.19  ? 62  GLN A CG  1 
ATOM   260  C CD  . GLN A 1 33  ? 16.526  33.738  -0.379  1.00 53.16  ? 62  GLN A CD  1 
ATOM   261  O OE1 . GLN A 1 33  ? 17.735  33.950  -0.530  1.00 50.77  ? 62  GLN A OE1 1 
ATOM   262  N NE2 . GLN A 1 33  ? 15.798  34.361  0.537   1.00 50.70  ? 62  GLN A NE2 1 
ATOM   263  N N   . ILE A 1 34  ? 14.807  28.838  1.185   1.00 29.79  ? 63  ILE A N   1 
ATOM   264  C CA  . ILE A 1 34  ? 13.795  27.823  1.474   1.00 29.61  ? 63  ILE A CA  1 
ATOM   265  C C   . ILE A 1 34  ? 12.459  28.511  1.762   1.00 29.00  ? 63  ILE A C   1 
ATOM   266  O O   . ILE A 1 34  ? 12.403  29.353  2.651   1.00 31.75  ? 63  ILE A O   1 
ATOM   267  C CB  . ILE A 1 34  ? 14.178  26.960  2.695   1.00 29.13  ? 63  ILE A CB  1 
ATOM   268  C CG1 . ILE A 1 34  ? 15.533  26.295  2.535   1.00 34.07  ? 63  ILE A CG1 1 
ATOM   269  C CG2 . ILE A 1 34  ? 13.094  25.915  2.958   1.00 26.39  ? 63  ILE A CG2 1 
ATOM   270  C CD1 . ILE A 1 34  ? 16.190  25.951  3.862   1.00 40.33  ? 63  ILE A CD1 1 
ATOM   271  N N   . THR A 1 35  ? 11.385  28.084  1.090   1.00 26.40  ? 64  THR A N   1 
ATOM   272  C CA  . THR A 1 35  ? 10.029  28.535  1.385   1.00 26.25  ? 64  THR A CA  1 
ATOM   273  C C   . THR A 1 35  ? 9.229   27.431  2.076   1.00 28.70  ? 64  THR A C   1 
ATOM   274  O O   . THR A 1 35  ? 9.644   26.273  2.088   1.00 25.33  ? 64  THR A O   1 
ATOM   275  C CB  . THR A 1 35  ? 9.302   28.975  0.113   1.00 26.64  ? 64  THR A CB  1 
ATOM   276  O OG1 . THR A 1 35  ? 9.119   27.784  -0.643  1.00 25.08  ? 64  THR A OG1 1 
ATOM   277  C CG2 . THR A 1 35  ? 10.028  30.060  -0.673  1.00 26.45  ? 64  THR A CG2 1 
ATOM   278  N N   . VAL A 1 36  ? 8.072   27.804  2.639   1.00 25.36  ? 65  VAL A N   1 
ATOM   279  C CA  . VAL A 1 36  ? 7.183   26.835  3.262   1.00 24.76  ? 65  VAL A CA  1 
ATOM   280  C C   . VAL A 1 36  ? 6.747   25.791  2.217   1.00 24.69  ? 65  VAL A C   1 
ATOM   281  O O   . VAL A 1 36  ? 6.770   24.564  2.448   1.00 21.65  ? 65  VAL A O   1 
ATOM   282  C CB  . VAL A 1 36  ? 5.997   27.614  3.853   1.00 24.25  ? 65  VAL A CB  1 
ATOM   283  C CG1 . VAL A 1 36  ? 4.786   26.740  4.131   1.00 24.35  ? 65  VAL A CG1 1 
ATOM   284  C CG2 . VAL A 1 36  ? 6.416   28.373  5.108   1.00 24.30  ? 65  VAL A CG2 1 
ATOM   285  N N   . ASP A 1 37  ? 6.397   26.288  1.029   1.00 25.45  ? 66  ASP A N   1 
ATOM   286  C CA  . ASP A 1 37  ? 5.995   25.408  -0.056  1.00 25.55  ? 66  ASP A CA  1 
ATOM   287  C C   . ASP A 1 37  ? 7.062   24.359  -0.370  1.00 25.98  ? 66  ASP A C   1 
ATOM   288  O O   . ASP A 1 37  ? 6.699   23.225  -0.708  1.00 23.57  ? 66  ASP A O   1 
ATOM   289  C CB  . ASP A 1 37  ? 5.598   26.166  -1.305  1.00 27.80  ? 66  ASP A CB  1 
ATOM   290  C CG  . ASP A 1 37  ? 4.150   26.649  -1.299  1.00 31.16  ? 66  ASP A CG  1 
ATOM   291  O OD1 . ASP A 1 37  ? 3.414   26.238  -0.396  1.00 32.45  ? 66  ASP A OD1 1 
ATOM   292  O OD2 . ASP A 1 37  ? 3.796   27.473  -2.177  1.00 41.23  ? 66  ASP A OD2 1 
ATOM   293  N N   . MET A 1 38  ? 8.351   24.741  -0.320  1.00 25.58  ? 67  MET A N   1 
ATOM   294  C CA  . MET A 1 38  ? 9.414   23.800  -0.654  1.00 25.25  ? 67  MET A CA  1 
ATOM   295  C C   . MET A 1 38  ? 9.459   22.665  0.358   1.00 24.37  ? 67  MET A C   1 
ATOM   296  O O   . MET A 1 38  ? 9.754   21.525  -0.005  1.00 25.97  ? 67  MET A O   1 
ATOM   297  C CB  . MET A 1 38  ? 10.798  24.457  -0.689  1.00 25.71  ? 67  MET A CB  1 
ATOM   298  C CG  . MET A 1 38  ? 10.988  25.452  -1.826  1.00 29.30  ? 67  MET A CG  1 
ATOM   299  S SD  . MET A 1 38  ? 12.637  26.218  -1.779  1.00 38.20  ? 67  MET A SD  1 
ATOM   300  C CE  . MET A 1 38  ? 12.243  27.515  -2.962  1.00 36.07  ? 67  MET A CE  1 
ATOM   301  N N   . MET A 1 39  ? 9.263   23.011  1.639   1.00 22.95  ? 68  MET A N   1 
ATOM   302  C CA  . MET A 1 39  ? 9.256   22.037  2.719   1.00 24.15  ? 68  MET A CA  1 
ATOM   303  C C   . MET A 1 39  ? 8.088   21.066  2.546   1.00 25.15  ? 68  MET A C   1 
ATOM   304  O O   . MET A 1 39  ? 8.244   19.856  2.767   1.00 24.02  ? 68  MET A O   1 
ATOM   305  C CB  . MET A 1 39  ? 9.206   22.737  4.078   1.00 28.23  ? 68  MET A CB  1 
ATOM   306  C CG  . MET A 1 39  ? 10.519  23.386  4.472   1.00 29.07  ? 68  MET A CG  1 
ATOM   307  S SD  . MET A 1 39  ? 10.317  24.310  5.997   1.00 29.93  ? 68  MET A SD  1 
ATOM   308  C CE  . MET A 1 39  ? 10.357  22.947  7.166   1.00 28.94  ? 68  MET A CE  1 
ATOM   309  N N   . TYR A 1 40  ? 6.919   21.578  2.142   1.00 24.47  ? 69  TYR A N   1 
ATOM   310  C CA  . TYR A 1 40  ? 5.773   20.708  1.956   1.00 25.94  ? 69  TYR A CA  1 
ATOM   311  C C   . TYR A 1 40  ? 5.937   19.916  0.667   1.00 26.00  ? 69  TYR A C   1 
ATOM   312  O O   . TYR A 1 40  ? 5.366   18.831  0.546   1.00 29.53  ? 69  TYR A O   1 
ATOM   313  C CB  . TYR A 1 40  ? 4.426   21.444  1.925   1.00 27.25  ? 69  TYR A CB  1 
ATOM   314  C CG  . TYR A 1 40  ? 3.918   21.749  3.324   1.00 24.29  ? 69  TYR A CG  1 
ATOM   315  C CD1 . TYR A 1 40  ? 3.360   20.754  4.115   1.00 25.83  ? 69  TYR A CD1 1 
ATOM   316  C CD2 . TYR A 1 40  ? 4.073   23.015  3.873   1.00 23.69  ? 69  TYR A CD2 1 
ATOM   317  C CE1 . TYR A 1 40  ? 2.966   20.993  5.423   1.00 22.41  ? 69  TYR A CE1 1 
ATOM   318  C CE2 . TYR A 1 40  ? 3.660   23.275  5.166   1.00 28.20  ? 69  TYR A CE2 1 
ATOM   319  C CZ  . TYR A 1 40  ? 3.107   22.266  5.937   1.00 25.73  ? 69  TYR A CZ  1 
ATOM   320  O OH  . TYR A 1 40  ? 2.702   22.568  7.180   1.00 26.00  ? 69  TYR A OH  1 
ATOM   321  N N   . GLY A 1 41  ? 6.665   20.508  -0.291  1.00 24.29  ? 70  GLY A N   1 
ATOM   322  C CA  . GLY A 1 41  ? 6.738   20.064  -1.664  1.00 25.15  ? 70  GLY A CA  1 
ATOM   323  C C   . GLY A 1 41  ? 7.979   19.217  -1.953  1.00 23.32  ? 70  GLY A C   1 
ATOM   324  O O   . GLY A 1 41  ? 8.482   19.206  -3.072  1.00 24.02  ? 70  GLY A O   1 
ATOM   325  N N   . GLY A 1 42  ? 8.440   18.456  -0.964  1.00 22.67  ? 71  GLY A N   1 
ATOM   326  C CA  . GLY A 1 42  ? 9.546   17.519  -1.185  1.00 23.59  ? 71  GLY A CA  1 
ATOM   327  C C   . GLY A 1 42  ? 10.853  18.199  -1.605  1.00 22.30  ? 71  GLY A C   1 
ATOM   328  O O   . GLY A 1 42  ? 11.620  17.639  -2.364  1.00 25.25  ? 71  GLY A O   1 
ATOM   329  N N   . MET A 1 43  ? 11.133  19.417  -1.135  1.00 21.53  ? 72  MET A N   1 
ATOM   330  C CA  . MET A 1 43  ? 12.396  20.101  -1.410  1.00 23.20  ? 72  MET A CA  1 
ATOM   331  C C   . MET A 1 43  ? 12.541  20.517  -2.880  1.00 22.98  ? 72  MET A C   1 
ATOM   332  O O   . MET A 1 43  ? 13.665  20.720  -3.366  1.00 22.78  ? 72  MET A O   1 
ATOM   333  C CB  . MET A 1 43  ? 13.596  19.216  -1.053  1.00 24.00  ? 72  MET A CB  1 
ATOM   334  C CG  . MET A 1 43  ? 13.650  18.729  0.388   1.00 26.56  ? 72  MET A CG  1 
ATOM   335  S SD  . MET A 1 43  ? 15.199  17.829  0.639   1.00 31.55  ? 72  MET A SD  1 
ATOM   336  C CE  . MET A 1 43  ? 14.967  17.322  2.349   1.00 27.30  ? 72  MET A CE  1 
ATOM   337  N N   . ARG A 1 44  ? 11.423  20.578  -3.611  1.00 23.68  ? 73  ARG A N   1 
ATOM   338  C CA  . ARG A 1 44  ? 11.431  20.870  -5.031  1.00 30.72  ? 73  ARG A CA  1 
ATOM   339  C C   . ARG A 1 44  ? 12.080  22.232  -5.246  1.00 28.04  ? 73  ARG A C   1 
ATOM   340  O O   . ARG A 1 44  ? 11.647  23.203  -4.625  1.00 30.90  ? 73  ARG A O   1 
ATOM   341  C CB  . ARG A 1 44  ? 10.006  20.924  -5.597  1.00 37.65  ? 73  ARG A CB  1 
ATOM   342  C CG  . ARG A 1 44  ? 9.915   21.419  -7.037  1.00 48.28  ? 73  ARG A CG  1 
ATOM   343  C CD  . ARG A 1 44  ? 8.546   22.000  -7.393  1.00 57.78  ? 73  ARG A CD  1 
ATOM   344  N NE  . ARG A 1 44  ? 7.511   21.101  -6.873  1.00 67.83  ? 73  ARG A NE  1 
ATOM   345  C CZ  . ARG A 1 44  ? 6.690   21.370  -5.843  1.00 83.76  ? 73  ARG A CZ  1 
ATOM   346  N NH1 . ARG A 1 44  ? 6.523   22.617  -5.406  1.00 83.88  ? 73  ARG A NH1 1 
ATOM   347  N NH2 . ARG A 1 44  ? 6.006   20.385  -5.273  1.00 79.27  ? 73  ARG A NH2 1 
ATOM   348  N N   . GLY A 1 45  ? 13.053  22.288  -6.166  1.00 32.65  ? 74  GLY A N   1 
ATOM   349  C CA  . GLY A 1 45  ? 13.792  23.506  -6.478  1.00 34.86  ? 74  GLY A CA  1 
ATOM   350  C C   . GLY A 1 45  ? 14.762  23.937  -5.370  1.00 40.20  ? 74  GLY A C   1 
ATOM   351  O O   . GLY A 1 45  ? 15.241  25.073  -5.355  1.00 41.72  ? 74  GLY A O   1 
ATOM   352  N N   . MET A 1 46  ? 15.085  23.038  -4.439  1.00 33.59  ? 75  MET A N   1 
ATOM   353  C CA  . MET A 1 46  ? 15.949  23.402  -3.335  1.00 33.07  ? 75  MET A CA  1 
ATOM   354  C C   . MET A 1 46  ? 17.317  22.810  -3.611  1.00 32.15  ? 75  MET A C   1 
ATOM   355  O O   . MET A 1 46  ? 17.405  21.606  -3.829  1.00 31.21  ? 75  MET A O   1 
ATOM   356  C CB  . MET A 1 46  ? 15.382  22.828  -2.034  1.00 36.48  ? 75  MET A CB  1 
ATOM   357  C CG  . MET A 1 46  ? 16.047  23.281  -0.752  1.00 41.71  ? 75  MET A CG  1 
ATOM   358  S SD  . MET A 1 46  ? 15.377  22.526  0.758   1.00 45.42  ? 75  MET A SD  1 
ATOM   359  C CE  . MET A 1 46  ? 13.752  23.247  0.524   1.00 39.63  ? 75  MET A CE  1 
ATOM   360  N N   . LYS A 1 47  ? 18.346  23.675  -3.583  1.00 30.63  ? 76  LYS A N   1 
ATOM   361  C CA  . LYS A 1 47  ? 19.739  23.286  -3.734  1.00 30.68  ? 76  LYS A CA  1 
ATOM   362  C C   . LYS A 1 47  ? 20.242  22.645  -2.447  1.00 30.07  ? 76  LYS A C   1 
ATOM   363  O O   . LYS A 1 47  ? 20.584  23.329  -1.480  1.00 38.99  ? 76  LYS A O   1 
ATOM   364  C CB  . LYS A 1 47  ? 20.596  24.493  -4.139  1.00 35.16  ? 76  LYS A CB  1 
ATOM   365  C CG  . LYS A 1 47  ? 20.463  24.834  -5.611  1.00 39.41  ? 76  LYS A CG  1 
ATOM   366  C CD  . LYS A 1 47  ? 21.361  25.973  -6.071  1.00 44.90  ? 76  LYS A CD  1 
ATOM   367  C CE  . LYS A 1 47  ? 21.308  26.154  -7.572  1.00 44.96  ? 76  LYS A CE  1 
ATOM   368  N NZ  . LYS A 1 47  ? 20.032  26.727  -8.004  1.00 47.47  ? 76  LYS A NZ  1 
ATOM   369  N N   . GLY A 1 48  ? 20.283  21.317  -2.422  1.00 28.07  ? 77  GLY A N   1 
ATOM   370  C CA  . GLY A 1 48  ? 20.360  20.620  -1.137  1.00 27.36  ? 77  GLY A CA  1 
ATOM   371  C C   . GLY A 1 48  ? 21.657  19.841  -0.926  1.00 23.09  ? 77  GLY A C   1 
ATOM   372  O O   . GLY A 1 48  ? 22.008  19.539  0.210   1.00 23.56  ? 77  GLY A O   1 
ATOM   373  N N   . LEU A 1 49  ? 22.347  19.463  -2.005  1.00 21.29  ? 78  LEU A N   1 
ATOM   374  C CA  . LEU A 1 49  ? 23.515  18.629  -1.814  1.00 22.69  ? 78  LEU A CA  1 
ATOM   375  C C   . LEU A 1 49  ? 24.524  18.810  -2.952  1.00 21.39  ? 78  LEU A C   1 
ATOM   376  O O   . LEU A 1 49  ? 24.215  19.290  -4.035  1.00 23.84  ? 78  LEU A O   1 
ATOM   377  C CB  . LEU A 1 49  ? 23.105  17.177  -1.609  1.00 25.96  ? 78  LEU A CB  1 
ATOM   378  C CG  . LEU A 1 49  ? 22.596  16.423  -2.842  1.00 24.08  ? 78  LEU A CG  1 
ATOM   379  C CD1 . LEU A 1 49  ? 22.569  14.913  -2.573  1.00 29.96  ? 78  LEU A CD1 1 
ATOM   380  C CD2 . LEU A 1 49  ? 21.202  16.850  -3.175  1.00 26.90  ? 78  LEU A CD2 1 
ATOM   381  N N   . VAL A 1 50  ? 25.771  18.493  -2.639  1.00 24.05  ? 79  VAL A N   1 
ATOM   382  C CA  . VAL A 1 50  ? 26.819  18.437  -3.634  1.00 22.94  ? 79  VAL A CA  1 
ATOM   383  C C   . VAL A 1 50  ? 26.966  16.996  -4.098  1.00 22.24  ? 79  VAL A C   1 
ATOM   384  O O   . VAL A 1 50  ? 27.074  16.090  -3.290  1.00 19.99  ? 79  VAL A O   1 
ATOM   385  C CB  . VAL A 1 50  ? 28.157  18.985  -3.102  1.00 23.06  ? 79  VAL A CB  1 
ATOM   386  C CG1 . VAL A 1 50  ? 29.238  18.900  -4.166  1.00 24.79  ? 79  VAL A CG1 1 
ATOM   387  C CG2 . VAL A 1 50  ? 27.993  20.406  -2.567  1.00 23.01  ? 79  VAL A CG2 1 
ATOM   388  N N   . TYR A 1 51  ? 27.045  16.858  -5.427  1.00 23.55  ? 80  TYR A N   1 
ATOM   389  C CA  . TYR A 1 51  ? 27.087  15.592  -6.106  1.00 25.62  ? 80  TYR A CA  1 
ATOM   390  C C   . TYR A 1 51  ? 27.912  15.833  -7.354  1.00 22.65  ? 80  TYR A C   1 
ATOM   391  O O   . TYR A 1 51  ? 27.517  16.641  -8.194  1.00 25.67  ? 80  TYR A O   1 
ATOM   392  C CB  . TYR A 1 51  ? 25.666  15.117  -6.394  1.00 23.94  ? 80  TYR A CB  1 
ATOM   393  C CG  . TYR A 1 51  ? 25.545  13.646  -6.756  1.00 23.91  ? 80  TYR A CG  1 
ATOM   394  C CD1 . TYR A 1 51  ? 25.324  12.682  -5.781  1.00 20.51  ? 80  TYR A CD1 1 
ATOM   395  C CD2 . TYR A 1 51  ? 25.542  13.252  -8.088  1.00 22.15  ? 80  TYR A CD2 1 
ATOM   396  C CE1 . TYR A 1 51  ? 25.182  11.342  -6.122  1.00 22.35  ? 80  TYR A CE1 1 
ATOM   397  C CE2 . TYR A 1 51  ? 25.369  11.926  -8.432  1.00 24.44  ? 80  TYR A CE2 1 
ATOM   398  C CZ  . TYR A 1 51  ? 25.174  10.975  -7.455  1.00 24.40  ? 80  TYR A CZ  1 
ATOM   399  O OH  . TYR A 1 51  ? 25.059  9.683   -7.861  1.00 25.97  ? 80  TYR A OH  1 
ATOM   400  N N   . GLU A 1 52  ? 29.080  15.190  -7.386  1.00 24.61  ? 81  GLU A N   1 
ATOM   401  C CA  . GLU A 1 52  ? 30.158  15.566  -8.283  1.00 24.44  ? 81  GLU A CA  1 
ATOM   402  C C   . GLU A 1 52  ? 30.098  14.838  -9.620  1.00 25.47  ? 81  GLU A C   1 
ATOM   403  O O   . GLU A 1 52  ? 30.566  15.375  -10.626 1.00 21.61  ? 81  GLU A O   1 
ATOM   404  C CB  . GLU A 1 52  ? 31.522  15.284  -7.650  1.00 24.74  ? 81  GLU A CB  1 
ATOM   405  C CG  . GLU A 1 52  ? 31.761  15.945  -6.298  1.00 26.98  ? 81  GLU A CG  1 
ATOM   406  C CD  . GLU A 1 52  ? 32.034  17.428  -6.389  1.00 28.09  ? 81  GLU A CD  1 
ATOM   407  O OE1 . GLU A 1 52  ? 31.731  18.061  -7.415  1.00 28.52  ? 81  GLU A OE1 1 
ATOM   408  O OE2 . GLU A 1 52  ? 32.588  17.915  -5.405  1.00 31.56  ? 81  GLU A OE2 1 
ATOM   409  N N   . THR A 1 53  ? 29.481  13.646  -9.664  1.00 25.45  ? 82  THR A N   1 
ATOM   410  C CA  . THR A 1 53  ? 29.663  12.761  -10.811 1.00 24.83  ? 82  THR A CA  1 
ATOM   411  C C   . THR A 1 53  ? 28.851  13.199  -12.026 1.00 23.62  ? 82  THR A C   1 
ATOM   412  O O   . THR A 1 53  ? 29.316  13.032  -13.163 1.00 24.04  ? 82  THR A O   1 
ATOM   413  C CB  . THR A 1 53  ? 29.399  11.309  -10.392 1.00 23.96  ? 82  THR A CB  1 
ATOM   414  O OG1 . THR A 1 53  ? 28.112  11.293  -9.767  1.00 23.54  ? 82  THR A OG1 1 
ATOM   415  C CG2 . THR A 1 53  ? 30.500  10.820  -9.468  1.00 24.23  ? 82  THR A CG2 1 
ATOM   416  N N   . SER A 1 54  ? 27.708  13.863  -11.820 1.00 22.70  ? 83  SER A N   1 
ATOM   417  C CA  . SER A 1 54  ? 26.856  14.240  -12.923 1.00 25.14  ? 83  SER A CA  1 
ATOM   418  C C   . SER A 1 54  ? 26.010  15.450  -12.564 1.00 23.86  ? 83  SER A C   1 
ATOM   419  O O   . SER A 1 54  ? 25.669  15.663  -11.408 1.00 22.76  ? 83  SER A O   1 
ATOM   420  C CB  . SER A 1 54  ? 25.968  13.087  -13.420 1.00 28.75  ? 83  SER A CB  1 
ATOM   421  O OG  . SER A 1 54  ? 24.918  12.762  -12.519 1.00 28.75  ? 83  SER A OG  1 
ATOM   422  N N   . VAL A 1 55  ? 25.682  16.228  -13.585 1.00 25.39  ? 84  VAL A N   1 
ATOM   423  C CA  . VAL A 1 55  ? 24.880  17.428  -13.413 1.00 29.14  ? 84  VAL A CA  1 
ATOM   424  C C   . VAL A 1 55  ? 23.868  17.500  -14.550 1.00 29.50  ? 84  VAL A C   1 
ATOM   425  O O   . VAL A 1 55  ? 24.168  17.223  -15.705 1.00 27.77  ? 84  VAL A O   1 
ATOM   426  C CB  . VAL A 1 55  ? 25.705  18.727  -13.341 1.00 31.85  ? 84  VAL A CB  1 
ATOM   427  C CG1 . VAL A 1 55  ? 24.821  19.917  -13.009 1.00 36.80  ? 84  VAL A CG1 1 
ATOM   428  C CG2 . VAL A 1 55  ? 26.819  18.659  -12.308 1.00 33.48  ? 84  VAL A CG2 1 
ATOM   429  N N   . LEU A 1 56  ? 22.632  17.787  -14.178 1.00 36.80  ? 85  LEU A N   1 
ATOM   430  C CA  . LEU A 1 56  ? 21.521  17.725  -15.102 1.00 44.83  ? 85  LEU A CA  1 
ATOM   431  C C   . LEU A 1 56  ? 21.071  19.150  -15.345 1.00 56.14  ? 85  LEU A C   1 
ATOM   432  O O   . LEU A 1 56  ? 20.359  19.705  -14.512 1.00 60.75  ? 85  LEU A O   1 
ATOM   433  C CB  . LEU A 1 56  ? 20.392  16.902  -14.490 1.00 49.58  ? 85  LEU A CB  1 
ATOM   434  C CG  . LEU A 1 56  ? 19.068  16.936  -15.247 1.00 51.85  ? 85  LEU A CG  1 
ATOM   435  C CD1 . LEU A 1 56  ? 19.280  16.409  -16.649 1.00 51.11  ? 85  LEU A CD1 1 
ATOM   436  C CD2 . LEU A 1 56  ? 18.015  16.144  -14.482 1.00 58.46  ? 85  LEU A CD2 1 
ATOM   437  N N   . ASP A 1 57  ? 21.547  19.752  -16.434 1.00 63.81  ? 86  ASP A N   1 
ATOM   438  C CA  . ASP A 1 57  ? 20.946  20.997  -16.873 1.00 82.10  ? 86  ASP A CA  1 
ATOM   439  C C   . ASP A 1 57  ? 19.545  20.652  -17.400 1.00 83.78  ? 86  ASP A C   1 
ATOM   440  O O   . ASP A 1 57  ? 19.382  19.655  -18.115 1.00 65.49  ? 86  ASP A O   1 
ATOM   441  C CB  . ASP A 1 57  ? 21.900  21.818  -17.739 1.00 86.88  ? 86  ASP A CB  1 
ATOM   442  C CG  . ASP A 1 57  ? 22.511  21.120  -18.945 1.00 90.11  ? 86  ASP A CG  1 
ATOM   443  O OD1 . ASP A 1 57  ? 22.972  19.975  -18.783 1.00 85.91  ? 86  ASP A OD1 1 
ATOM   444  O OD2 . ASP A 1 57  ? 22.560  21.746  -20.024 1.00 100.49 ? 86  ASP A OD2 1 
ATOM   445  N N   . PRO A 1 58  ? 18.481  21.405  -16.997 1.00 94.64  ? 87  PRO A N   1 
ATOM   446  C CA  . PRO A 1 58  ? 17.160  21.288  -17.632 1.00 90.96  ? 87  PRO A CA  1 
ATOM   447  C C   . PRO A 1 58  ? 17.178  21.404  -19.159 1.00 86.29  ? 87  PRO A C   1 
ATOM   448  O O   . PRO A 1 58  ? 16.334  20.816  -19.833 1.00 75.70  ? 87  PRO A O   1 
ATOM   449  C CB  . PRO A 1 58  ? 16.342  22.425  -16.969 1.00 89.75  ? 87  PRO A CB  1 
ATOM   450  C CG  . PRO A 1 58  ? 17.000  22.627  -15.618 1.00 89.50  ? 87  PRO A CG  1 
ATOM   451  C CD  . PRO A 1 58  ? 18.478  22.362  -15.869 1.00 88.85  ? 87  PRO A CD  1 
ATOM   452  N N   . ASP A 1 59  ? 18.188  22.116  -19.686 1.00 91.60  ? 88  ASP A N   1 
ATOM   453  C CA  . ASP A 1 59  ? 18.263  22.514  -21.086 1.00 93.26  ? 88  ASP A CA  1 
ATOM   454  C C   . ASP A 1 59  ? 18.789  21.392  -21.988 1.00 79.80  ? 88  ASP A C   1 
ATOM   455  O O   . ASP A 1 59  ? 18.065  20.956  -22.880 1.00 66.72  ? 88  ASP A O   1 
ATOM   456  C CB  . ASP A 1 59  ? 19.048  23.809  -21.234 1.00 104.13 ? 88  ASP A CB  1 
ATOM   457  C CG  . ASP A 1 59  ? 20.239  23.992  -20.298 1.00 111.82 ? 88  ASP A CG  1 
ATOM   458  O OD1 . ASP A 1 59  ? 20.058  23.822  -19.067 1.00 97.44  ? 88  ASP A OD1 1 
ATOM   459  O OD2 . ASP A 1 59  ? 21.330  24.330  -20.802 1.00 118.65 ? 88  ASP A OD2 1 
ATOM   460  N N   . GLU A 1 60  ? 20.045  20.953  -21.787 1.00 76.13  ? 89  GLU A N   1 
ATOM   461  C CA  . GLU A 1 60  ? 20.720  20.056  -22.725 1.00 76.49  ? 89  GLU A CA  1 
ATOM   462  C C   . GLU A 1 60  ? 20.791  18.614  -22.212 1.00 69.11  ? 89  GLU A C   1 
ATOM   463  O O   . GLU A 1 60  ? 21.264  17.716  -22.916 1.00 56.83  ? 89  GLU A O   1 
ATOM   464  C CB  . GLU A 1 60  ? 22.133  20.553  -23.024 1.00 85.72  ? 89  GLU A CB  1 
ATOM   465  C CG  . GLU A 1 60  ? 22.182  22.052  -23.315 1.00 96.71  ? 89  GLU A CG  1 
ATOM   466  C CD  . GLU A 1 60  ? 23.410  22.522  -24.075 1.00 106.37 ? 89  GLU A CD  1 
ATOM   467  O OE1 . GLU A 1 60  ? 23.688  23.744  -24.057 1.00 113.72 ? 89  GLU A OE1 1 
ATOM   468  O OE2 . GLU A 1 60  ? 24.075  21.673  -24.708 1.00 105.25 ? 89  GLU A OE2 1 
ATOM   469  N N   . GLY A 1 61  ? 20.329  18.396  -20.976 1.00 61.79  ? 90  GLY A N   1 
ATOM   470  C CA  . GLY A 1 61  ? 20.204  17.055  -20.430 1.00 52.38  ? 90  GLY A CA  1 
ATOM   471  C C   . GLY A 1 61  ? 21.377  16.712  -19.522 1.00 43.78  ? 90  GLY A C   1 
ATOM   472  O O   . GLY A 1 61  ? 22.092  17.589  -19.057 1.00 33.96  ? 90  GLY A O   1 
ATOM   473  N N   . ILE A 1 62  ? 21.527  15.423  -19.227 1.00 36.55  ? 91  ILE A N   1 
ATOM   474  C CA  . ILE A 1 62  ? 22.513  15.001  -18.245 1.00 31.83  ? 91  ILE A CA  1 
ATOM   475  C C   . ILE A 1 62  ? 23.915  15.191  -18.823 1.00 31.22  ? 91  ILE A C   1 
ATOM   476  O O   . ILE A 1 62  ? 24.147  14.906  -19.995 1.00 31.89  ? 91  ILE A O   1 
ATOM   477  C CB  . ILE A 1 62  ? 22.246  13.547  -17.823 1.00 29.71  ? 91  ILE A CB  1 
ATOM   478  C CG1 . ILE A 1 62  ? 23.059  13.189  -16.563 1.00 28.96  ? 91  ILE A CG1 1 
ATOM   479  C CG2 . ILE A 1 62  ? 22.490  12.566  -18.978 1.00 31.30  ? 91  ILE A CG2 1 
ATOM   480  C CD1 . ILE A 1 62  ? 22.595  13.933  -15.311 1.00 28.73  ? 91  ILE A CD1 1 
ATOM   481  N N   . ARG A 1 63  ? 24.841  15.681  -17.994 1.00 30.71  ? 92  ARG A N   1 
ATOM   482  C CA  . ARG A 1 63  ? 26.253  15.636  -18.344 1.00 31.96  ? 92  ARG A CA  1 
ATOM   483  C C   . ARG A 1 63  ? 27.002  14.791  -17.325 1.00 27.51  ? 92  ARG A C   1 
ATOM   484  O O   . ARG A 1 63  ? 26.892  15.023  -16.131 1.00 27.47  ? 92  ARG A O   1 
ATOM   485  C CB  . ARG A 1 63  ? 26.866  17.044  -18.441 1.00 33.23  ? 92  ARG A CB  1 
ATOM   486  C CG  . ARG A 1 63  ? 26.415  17.854  -19.657 1.00 36.71  ? 92  ARG A CG  1 
ATOM   487  C CD  . ARG A 1 63  ? 27.107  19.198  -19.680 1.00 42.39  ? 92  ARG A CD  1 
ATOM   488  N NE  . ARG A 1 63  ? 26.712  20.052  -20.808 1.00 55.67  ? 92  ARG A NE  1 
ATOM   489  C CZ  . ARG A 1 63  ? 27.211  20.011  -22.049 1.00 57.16  ? 92  ARG A CZ  1 
ATOM   490  N NH1 . ARG A 1 63  ? 28.178  19.166  -22.397 1.00 55.46  ? 92  ARG A NH1 1 
ATOM   491  N NH2 . ARG A 1 63  ? 26.737  20.853  -22.947 1.00 59.63  ? 92  ARG A NH2 1 
ATOM   492  N N   . PHE A 1 64  ? 27.851  13.892  -17.818 1.00 25.00  ? 93  PHE A N   1 
ATOM   493  C CA  . PHE A 1 64  ? 28.684  13.055  -16.993 1.00 24.24  ? 93  PHE A CA  1 
ATOM   494  C C   . PHE A 1 64  ? 30.067  13.683  -16.933 1.00 25.28  ? 93  PHE A C   1 
ATOM   495  O O   . PHE A 1 64  ? 30.778  13.626  -17.929 1.00 24.32  ? 93  PHE A O   1 
ATOM   496  C CB  . PHE A 1 64  ? 28.806  11.656  -17.605 1.00 24.44  ? 93  PHE A CB  1 
ATOM   497  C CG  . PHE A 1 64  ? 27.496  10.925  -17.819 1.00 22.12  ? 93  PHE A CG  1 
ATOM   498  C CD1 . PHE A 1 64  ? 26.516  10.892  -16.837 1.00 26.14  ? 93  PHE A CD1 1 
ATOM   499  C CD2 . PHE A 1 64  ? 27.271  10.215  -18.973 1.00 24.17  ? 93  PHE A CD2 1 
ATOM   500  C CE1 . PHE A 1 64  ? 25.323  10.225  -17.055 1.00 25.30  ? 93  PHE A CE1 1 
ATOM   501  C CE2 . PHE A 1 64  ? 26.090  9.515   -19.171 1.00 25.25  ? 93  PHE A CE2 1 
ATOM   502  C CZ  . PHE A 1 64  ? 25.100  9.548   -18.218 1.00 25.05  ? 93  PHE A CZ  1 
ATOM   503  N N   . ARG A 1 65  ? 30.412  14.288  -15.788 1.00 23.85  ? 94  ARG A N   1 
ATOM   504  C CA  . ARG A 1 65  ? 31.674  14.990  -15.597 1.00 25.37  ? 94  ARG A CA  1 
ATOM   505  C C   . ARG A 1 65  ? 31.926  15.896  -16.793 1.00 30.16  ? 94  ARG A C   1 
ATOM   506  O O   . ARG A 1 65  ? 32.951  15.801  -17.457 1.00 30.82  ? 94  ARG A O   1 
ATOM   507  C CB  . ARG A 1 65  ? 32.877  14.064  -15.427 1.00 24.69  ? 94  ARG A CB  1 
ATOM   508  C CG  . ARG A 1 65  ? 32.808  13.251  -14.142 1.00 26.68  ? 94  ARG A CG  1 
ATOM   509  C CD  . ARG A 1 65  ? 33.250  14.054  -12.921 1.00 26.57  ? 94  ARG A CD  1 
ATOM   510  N NE  . ARG A 1 65  ? 33.506  13.169  -11.774 1.00 27.69  ? 94  ARG A NE  1 
ATOM   511  C CZ  . ARG A 1 65  ? 33.956  13.523  -10.569 1.00 30.07  ? 94  ARG A CZ  1 
ATOM   512  N NH1 . ARG A 1 65  ? 34.186  14.789  -10.299 1.00 27.27  ? 94  ARG A NH1 1 
ATOM   513  N NH2 . ARG A 1 65  ? 34.223  12.616  -9.634  1.00 30.61  ? 94  ARG A NH2 1 
ATOM   514  N N   . GLY A 1 66  ? 30.924  16.708  -17.109 1.00 33.10  ? 95  GLY A N   1 
ATOM   515  C CA  . GLY A 1 66  ? 31.055  17.706  -18.151 1.00 31.21  ? 95  GLY A CA  1 
ATOM   516  C C   . GLY A 1 66  ? 30.811  17.185  -19.568 1.00 29.05  ? 95  GLY A C   1 
ATOM   517  O O   . GLY A 1 66  ? 30.750  17.998  -20.475 1.00 28.92  ? 95  GLY A O   1 
ATOM   518  N N   . PHE A 1 67  ? 30.603  15.879  -19.773 1.00 31.33  ? 96  PHE A N   1 
ATOM   519  C CA  . PHE A 1 67  ? 30.359  15.359  -21.115 1.00 29.17  ? 96  PHE A CA  1 
ATOM   520  C C   . PHE A 1 67  ? 28.899  14.975  -21.340 1.00 34.08  ? 96  PHE A C   1 
ATOM   521  O O   . PHE A 1 67  ? 28.316  14.274  -20.522 1.00 33.27  ? 96  PHE A O   1 
ATOM   522  C CB  . PHE A 1 67  ? 31.262  14.135  -21.265 1.00 28.16  ? 96  PHE A CB  1 
ATOM   523  C CG  . PHE A 1 67  ? 32.743  14.446  -21.332 1.00 27.81  ? 96  PHE A CG  1 
ATOM   524  C CD1 . PHE A 1 67  ? 33.330  14.852  -22.528 1.00 30.38  ? 96  PHE A CD1 1 
ATOM   525  C CD2 . PHE A 1 67  ? 33.548  14.382  -20.208 1.00 25.13  ? 96  PHE A CD2 1 
ATOM   526  C CE1 . PHE A 1 67  ? 34.693  15.118  -22.590 1.00 29.45  ? 96  PHE A CE1 1 
ATOM   527  C CE2 . PHE A 1 67  ? 34.903  14.654  -20.280 1.00 27.29  ? 96  PHE A CE2 1 
ATOM   528  C CZ  . PHE A 1 67  ? 35.471  15.041  -21.460 1.00 28.81  ? 96  PHE A CZ  1 
ATOM   529  N N   . SER A 1 68  ? 28.310  15.353  -22.489 1.00 30.63  ? 97  SER A N   1 
ATOM   530  C CA  . SER A 1 68  ? 26.946  14.926  -22.781 1.00 29.99  ? 97  SER A CA  1 
ATOM   531  C C   . SER A 1 68  ? 26.950  13.468  -23.234 1.00 27.11  ? 97  SER A C   1 
ATOM   532  O O   . SER A 1 68  ? 27.997  12.904  -23.490 1.00 26.21  ? 97  SER A O   1 
ATOM   533  C CB  . SER A 1 68  ? 26.262  15.811  -23.814 1.00 33.82  ? 97  SER A CB  1 
ATOM   534  O OG  . SER A 1 68  ? 26.710  15.432  -25.104 1.00 36.53  ? 97  SER A OG  1 
ATOM   535  N N   . ILE A 1 69  ? 25.771  12.850  -23.317 1.00 24.45  ? 98  ILE A N   1 
ATOM   536  C CA  . ILE A 1 69  ? 25.655  11.482  -23.744 1.00 31.31  ? 98  ILE A CA  1 
ATOM   537  C C   . ILE A 1 69  ? 26.137  11.344  -25.193 1.00 36.02  ? 98  ILE A C   1 
ATOM   538  O O   . ILE A 1 69  ? 26.807  10.361  -25.508 1.00 30.75  ? 98  ILE A O   1 
ATOM   539  C CB  . ILE A 1 69  ? 24.203  11.004  -23.600 1.00 37.59  ? 98  ILE A CB  1 
ATOM   540  C CG1 . ILE A 1 69  ? 23.807  10.844  -22.135 1.00 39.52  ? 98  ILE A CG1 1 
ATOM   541  C CG2 . ILE A 1 69  ? 23.980  9.731   -24.414 1.00 35.77  ? 98  ILE A CG2 1 
ATOM   542  C CD1 . ILE A 1 69  ? 23.686  9.414   -21.679 1.00 43.91  ? 98  ILE A CD1 1 
ATOM   543  N N   . PRO A 1 70  ? 25.753  12.229  -26.146 1.00 36.75  ? 99  PRO A N   1 
ATOM   544  C CA  . PRO A 1 70  ? 26.363  12.193  -27.487 1.00 39.14  ? 99  PRO A CA  1 
ATOM   545  C C   . PRO A 1 70  ? 27.888  12.333  -27.479 1.00 34.38  ? 99  PRO A C   1 
ATOM   546  O O   . PRO A 1 70  ? 28.584  11.629  -28.191 1.00 36.17  ? 99  PRO A O   1 
ATOM   547  C CB  . PRO A 1 70  ? 25.675  13.373  -28.201 1.00 41.78  ? 99  PRO A CB  1 
ATOM   548  C CG  . PRO A 1 70  ? 24.338  13.515  -27.491 1.00 39.52  ? 99  PRO A CG  1 
ATOM   549  C CD  . PRO A 1 70  ? 24.645  13.201  -26.046 1.00 37.11  ? 99  PRO A CD  1 
ATOM   550  N N   . GLU A 1 71  ? 28.438  13.234  -26.657 1.00 37.15  ? 100 GLU A N   1 
ATOM   551  C CA  . GLU A 1 71  ? 29.889  13.316  -26.557 1.00 33.83  ? 100 GLU A CA  1 
ATOM   552  C C   . GLU A 1 71  ? 30.450  11.987  -26.043 1.00 34.22  ? 100 GLU A C   1 
ATOM   553  O O   . GLU A 1 71  ? 31.500  11.563  -26.506 1.00 38.78  ? 100 GLU A O   1 
ATOM   554  C CB  . GLU A 1 71  ? 30.366  14.481  -25.706 1.00 37.96  ? 100 GLU A CB  1 
ATOM   555  C CG  . GLU A 1 71  ? 30.148  15.852  -26.335 1.00 39.11  ? 100 GLU A CG  1 
ATOM   556  C CD  . GLU A 1 71  ? 30.504  16.975  -25.371 1.00 43.55  ? 100 GLU A CD  1 
ATOM   557  O OE1 . GLU A 1 71  ? 31.427  17.776  -25.679 1.00 42.97  ? 100 GLU A OE1 1 
ATOM   558  O OE2 . GLU A 1 71  ? 29.845  17.051  -24.291 1.00 43.08  ? 100 GLU A OE2 1 
ATOM   559  N N   . CYS A 1 72  ? 29.750  11.306  -25.111 1.00 30.34  ? 101 CYS A N   1 
ATOM   560  C CA  . CYS A 1 72  ? 30.230  10.044  -24.542 1.00 26.50  ? 101 CYS A CA  1 
ATOM   561  C C   . CYS A 1 72  ? 30.113  8.882   -25.535 1.00 27.01  ? 101 CYS A C   1 
ATOM   562  O O   . CYS A 1 72  ? 30.963  7.986   -25.551 1.00 25.57  ? 101 CYS A O   1 
ATOM   563  C CB  . CYS A 1 72  ? 29.492  9.663   -23.254 1.00 27.85  ? 101 CYS A CB  1 
ATOM   564  S SG  . CYS A 1 72  ? 29.876  10.737  -21.843 1.00 30.23  ? 101 CYS A SG  1 
ATOM   565  N N   . GLN A 1 73  ? 29.008  8.826   -26.286 1.00 26.83  ? 102 GLN A N   1 
ATOM   566  C CA  . GLN A 1 73  ? 28.819  7.797   -27.300 1.00 33.39  ? 102 GLN A CA  1 
ATOM   567  C C   . GLN A 1 73  ? 29.996  7.769   -28.275 1.00 31.95  ? 102 GLN A C   1 
ATOM   568  O O   . GLN A 1 73  ? 30.461  6.695   -28.655 1.00 34.01  ? 102 GLN A O   1 
ATOM   569  C CB  . GLN A 1 73  ? 27.546  7.992   -28.125 1.00 37.59  ? 102 GLN A CB  1 
ATOM   570  C CG  . GLN A 1 73  ? 26.286  7.544   -27.389 1.00 42.75  ? 102 GLN A CG  1 
ATOM   571  C CD  . GLN A 1 73  ? 25.020  8.018   -28.070 1.00 44.79  ? 102 GLN A CD  1 
ATOM   572  O OE1 . GLN A 1 73  ? 24.663  9.194   -28.022 1.00 48.12  ? 102 GLN A OE1 1 
ATOM   573  N NE2 . GLN A 1 73  ? 24.327  7.105   -28.726 1.00 52.78  ? 102 GLN A NE2 1 
ATOM   574  N N   . LYS A 1 74  ? 30.463  8.953   -28.646 1.00 33.28  ? 103 LYS A N   1 
ATOM   575  C CA  . LYS A 1 74  ? 31.666  9.105   -29.444 1.00 39.80  ? 103 LYS A CA  1 
ATOM   576  C C   . LYS A 1 74  ? 32.958  8.743   -28.705 1.00 38.17  ? 103 LYS A C   1 
ATOM   577  O O   . LYS A 1 74  ? 33.752  7.941   -29.208 1.00 40.15  ? 103 LYS A O   1 
ATOM   578  C CB  . LYS A 1 74  ? 31.724  10.545  -29.967 1.00 41.00  ? 103 LYS A CB  1 
ATOM   579  C CG  . LYS A 1 74  ? 30.948  10.675  -31.266 1.00 48.09  ? 103 LYS A CG  1 
ATOM   580  C CD  . LYS A 1 74  ? 30.790  12.094  -31.790 1.00 50.58  ? 103 LYS A CD  1 
ATOM   581  C CE  . LYS A 1 74  ? 30.297  12.104  -33.205 1.00 55.37  ? 103 LYS A CE  1 
ATOM   582  N NZ  . LYS A 1 74  ? 28.986  11.478  -33.366 1.00 53.98  ? 103 LYS A NZ  1 
ATOM   583  N N   . LEU A 1 75  ? 33.224  9.387   -27.565 1.00 34.54  ? 104 LEU A N   1 
ATOM   584  C CA  . LEU A 1 75  ? 34.545  9.339   -26.950 1.00 33.95  ? 104 LEU A CA  1 
ATOM   585  C C   . LEU A 1 75  ? 34.818  8.025   -26.213 1.00 34.22  ? 104 LEU A C   1 
ATOM   586  O O   . LEU A 1 75  ? 35.963  7.596   -26.114 1.00 30.58  ? 104 LEU A O   1 
ATOM   587  C CB  . LEU A 1 75  ? 34.682  10.528  -26.019 1.00 35.41  ? 104 LEU A CB  1 
ATOM   588  C CG  . LEU A 1 75  ? 34.874  11.890  -26.691 1.00 37.64  ? 104 LEU A CG  1 
ATOM   589  C CD1 . LEU A 1 75  ? 34.536  12.987  -25.709 1.00 32.75  ? 104 LEU A CD1 1 
ATOM   590  C CD2 . LEU A 1 75  ? 36.295  12.072  -27.220 1.00 41.14  ? 104 LEU A CD2 1 
ATOM   591  N N   . LEU A 1 76  ? 33.787  7.374   -25.672 1.00 34.18  ? 105 LEU A N   1 
ATOM   592  C CA  . LEU A 1 76  ? 34.007  6.216   -24.825 1.00 30.97  ? 105 LEU A CA  1 
ATOM   593  C C   . LEU A 1 76  ? 34.337  4.960   -25.640 1.00 34.04  ? 105 LEU A C   1 
ATOM   594  O O   . LEU A 1 76  ? 33.656  4.636   -26.616 1.00 35.95  ? 105 LEU A O   1 
ATOM   595  C CB  . LEU A 1 76  ? 32.786  5.968   -23.940 1.00 30.64  ? 105 LEU A CB  1 
ATOM   596  C CG  . LEU A 1 76  ? 32.498  7.012   -22.854 1.00 30.78  ? 105 LEU A CG  1 
ATOM   597  C CD1 . LEU A 1 76  ? 31.191  6.661   -22.116 1.00 30.09  ? 105 LEU A CD1 1 
ATOM   598  C CD2 . LEU A 1 76  ? 33.663  7.186   -21.888 1.00 31.46  ? 105 LEU A CD2 1 
ATOM   599  N N   . PRO A 1 77  ? 35.348  4.158   -25.211 1.00 31.99  ? 106 PRO A N   1 
ATOM   600  C CA  . PRO A 1 77  ? 35.615  2.857   -25.808 1.00 31.02  ? 106 PRO A CA  1 
ATOM   601  C C   . PRO A 1 77  ? 34.408  1.960   -26.008 1.00 38.30  ? 106 PRO A C   1 
ATOM   602  O O   . PRO A 1 77  ? 33.477  1.959   -25.203 1.00 38.14  ? 106 PRO A O   1 
ATOM   603  C CB  . PRO A 1 77  ? 36.637  2.223   -24.853 1.00 30.08  ? 106 PRO A CB  1 
ATOM   604  C CG  . PRO A 1 77  ? 37.413  3.406   -24.336 1.00 31.67  ? 106 PRO A CG  1 
ATOM   605  C CD  . PRO A 1 77  ? 36.355  4.504   -24.196 1.00 29.41  ? 106 PRO A CD  1 
ATOM   606  N N   . LYS A 1 78  ? 34.502  1.173   -27.091 1.00 34.27  ? 107 LYS A N   1 
ATOM   607  C CA  . LYS A 1 78  ? 33.495  0.215   -27.492 1.00 34.86  ? 107 LYS A CA  1 
ATOM   608  C C   . LYS A 1 78  ? 34.129  -1.163  -27.388 1.00 30.86  ? 107 LYS A C   1 
ATOM   609  O O   . LYS A 1 78  ? 35.335  -1.254  -27.294 1.00 30.35  ? 107 LYS A O   1 
ATOM   610  C CB  . LYS A 1 78  ? 33.140  0.658   -28.916 1.00 39.04  ? 107 LYS A CB  1 
ATOM   611  C CG  . LYS A 1 78  ? 32.686  2.111   -28.983 1.00 42.14  ? 107 LYS A CG  1 
ATOM   612  C CD  . LYS A 1 78  ? 32.816  2.778   -30.342 1.00 53.16  ? 107 LYS A CD  1 
ATOM   613  C CE  . LYS A 1 78  ? 32.056  4.081   -30.393 1.00 60.42  ? 107 LYS A CE  1 
ATOM   614  N NZ  . LYS A 1 78  ? 32.611  5.088   -29.480 1.00 60.61  ? 107 LYS A NZ  1 
ATOM   615  N N   . ALA A 1 79  ? 33.334  -2.230  -27.407 1.00 28.89  ? 108 ALA A N   1 
ATOM   616  C CA  . ALA A 1 79  ? 33.899  -3.556  -27.588 1.00 33.09  ? 108 ALA A CA  1 
ATOM   617  C C   . ALA A 1 79  ? 34.368  -3.737  -29.041 1.00 43.02  ? 108 ALA A C   1 
ATOM   618  O O   . ALA A 1 79  ? 33.872  -3.061  -29.961 1.00 41.26  ? 108 ALA A O   1 
ATOM   619  C CB  . ALA A 1 79  ? 32.874  -4.585  -27.216 1.00 30.31  ? 108 ALA A CB  1 
ATOM   620  N N   . LYS A 1 80  ? 35.294  -4.682  -29.252 1.00 40.84  ? 109 LYS A N   1 
ATOM   621  C CA  . LYS A 1 80  ? 35.721  -5.036  -30.598 1.00 45.91  ? 109 LYS A CA  1 
ATOM   622  C C   . LYS A 1 80  ? 34.508  -5.544  -31.383 1.00 44.46  ? 109 LYS A C   1 
ATOM   623  O O   . LYS A 1 80  ? 33.770  -6.406  -30.905 1.00 41.43  ? 109 LYS A O   1 
ATOM   624  C CB  . LYS A 1 80  ? 36.901  -6.014  -30.481 1.00 47.56  ? 109 LYS A CB  1 
ATOM   625  C CG  . LYS A 1 80  ? 37.476  -6.602  -31.761 1.00 53.85  ? 109 LYS A CG  1 
ATOM   626  C CD  . LYS A 1 80  ? 38.736  -7.434  -31.516 1.00 61.50  ? 109 LYS A CD  1 
ATOM   627  C CE  . LYS A 1 80  ? 38.930  -8.616  -32.429 1.00 64.66  ? 109 LYS A CE  1 
ATOM   628  N NZ  . LYS A 1 80  ? 38.955  -8.233  -33.843 1.00 67.02  ? 109 LYS A NZ  1 
ATOM   629  N N   . GLY A 1 81  ? 34.296  -4.959  -32.573 1.00 45.21  ? 110 GLY A N   1 
ATOM   630  C CA  . GLY A 1 81  ? 33.156  -5.250  -33.424 1.00 45.62  ? 110 GLY A CA  1 
ATOM   631  C C   . GLY A 1 81  ? 31.883  -4.562  -32.920 1.00 49.91  ? 110 GLY A C   1 
ATOM   632  O O   . GLY A 1 81  ? 30.783  -5.102  -33.061 1.00 45.70  ? 110 GLY A O   1 
ATOM   633  N N   . GLY A 1 82  ? 32.048  -3.358  -32.351 1.00 47.76  ? 111 GLY A N   1 
ATOM   634  C CA  . GLY A 1 82  ? 31.036  -2.766  -31.483 1.00 46.59  ? 111 GLY A CA  1 
ATOM   635  C C   . GLY A 1 82  ? 30.848  -1.281  -31.766 1.00 41.79  ? 111 GLY A C   1 
ATOM   636  O O   . GLY A 1 82  ? 31.758  -0.611  -32.258 1.00 41.90  ? 111 GLY A O   1 
ATOM   637  N N   . GLU A 1 83  ? 29.641  -0.788  -31.468 1.00 40.55  ? 112 GLU A N   1 
ATOM   638  C CA  . GLU A 1 83  ? 29.290  0.599   -31.739 1.00 51.35  ? 112 GLU A CA  1 
ATOM   639  C C   . GLU A 1 83  ? 28.947  1.355   -30.446 1.00 45.44  ? 112 GLU A C   1 
ATOM   640  O O   . GLU A 1 83  ? 29.103  2.566   -30.393 1.00 45.09  ? 112 GLU A O   1 
ATOM   641  C CB  . GLU A 1 83  ? 28.145  0.643   -32.755 1.00 61.39  ? 112 GLU A CB  1 
ATOM   642  C CG  . GLU A 1 83  ? 28.569  0.311   -34.187 1.00 75.40  ? 112 GLU A CG  1 
ATOM   643  C CD  . GLU A 1 83  ? 27.461  0.182   -35.237 1.00 85.58  ? 112 GLU A CD  1 
ATOM   644  O OE1 . GLU A 1 83  ? 26.775  1.192   -35.529 1.00 85.21  ? 112 GLU A OE1 1 
ATOM   645  O OE2 . GLU A 1 83  ? 27.287  -0.934  -35.790 1.00 93.24  ? 112 GLU A OE2 1 
ATOM   646  N N   . GLU A 1 84  ? 28.494  0.656   -29.400 1.00 42.68  ? 113 GLU A N   1 
ATOM   647  C CA  . GLU A 1 84  ? 27.944  1.307   -28.209 1.00 41.83  ? 113 GLU A CA  1 
ATOM   648  C C   . GLU A 1 84  ? 28.999  1.498   -27.115 1.00 33.78  ? 113 GLU A C   1 
ATOM   649  O O   . GLU A 1 84  ? 29.890  0.678   -26.963 1.00 30.12  ? 113 GLU A O   1 
ATOM   650  C CB  . GLU A 1 84  ? 26.781  0.461   -27.703 1.00 36.92  ? 113 GLU A CB  1 
ATOM   651  C CG  . GLU A 1 84  ? 25.669  0.317   -28.731 1.00 40.13  ? 113 GLU A CG  1 
ATOM   652  C CD  . GLU A 1 84  ? 25.012  1.616   -29.164 1.00 39.08  ? 113 GLU A CD  1 
ATOM   653  O OE1 . GLU A 1 84  ? 25.312  2.683   -28.589 1.00 33.10  ? 113 GLU A OE1 1 
ATOM   654  O OE2 . GLU A 1 84  ? 24.217  1.539   -30.134 1.00 41.03  ? 113 GLU A OE2 1 
ATOM   655  N N   . PRO A 1 85  ? 28.927  2.603   -26.328 1.00 36.72  ? 114 PRO A N   1 
ATOM   656  C CA  . PRO A 1 85  ? 29.883  2.874   -25.231 1.00 32.88  ? 114 PRO A CA  1 
ATOM   657  C C   . PRO A 1 85  ? 29.815  1.766   -24.175 1.00 29.09  ? 114 PRO A C   1 
ATOM   658  O O   . PRO A 1 85  ? 28.749  1.206   -23.953 1.00 24.18  ? 114 PRO A O   1 
ATOM   659  C CB  . PRO A 1 85  ? 29.413  4.244   -24.699 1.00 34.91  ? 114 PRO A CB  1 
ATOM   660  C CG  . PRO A 1 85  ? 27.937  4.286   -25.034 1.00 34.43  ? 114 PRO A CG  1 
ATOM   661  C CD  . PRO A 1 85  ? 27.840  3.594   -26.389 1.00 35.47  ? 114 PRO A CD  1 
ATOM   662  N N   . LEU A 1 86  ? 30.968  1.339   -23.628 1.00 29.81  ? 115 LEU A N   1 
ATOM   663  C CA  . LEU A 1 86  ? 30.969  0.293   -22.611 1.00 28.68  ? 115 LEU A CA  1 
ATOM   664  C C   . LEU A 1 86  ? 30.754  0.965   -21.256 1.00 26.64  ? 115 LEU A C   1 
ATOM   665  O O   . LEU A 1 86  ? 31.362  1.993   -20.988 1.00 27.08  ? 115 LEU A O   1 
ATOM   666  C CB  . LEU A 1 86  ? 32.256  -0.531  -22.590 1.00 29.86  ? 115 LEU A CB  1 
ATOM   667  C CG  . LEU A 1 86  ? 32.587  -1.345  -23.844 1.00 33.01  ? 115 LEU A CG  1 
ATOM   668  C CD1 . LEU A 1 86  ? 33.869  -2.145  -23.663 1.00 40.79  ? 115 LEU A CD1 1 
ATOM   669  C CD2 . LEU A 1 86  ? 31.472  -2.277  -24.203 1.00 35.31  ? 115 LEU A CD2 1 
ATOM   670  N N   . PRO A 1 87  ? 29.874  0.448   -20.378 1.00 27.94  ? 116 PRO A N   1 
ATOM   671  C CA  . PRO A 1 87  ? 29.691  1.062   -19.077 1.00 26.40  ? 116 PRO A CA  1 
ATOM   672  C C   . PRO A 1 87  ? 30.953  1.215   -18.237 1.00 25.30  ? 116 PRO A C   1 
ATOM   673  O O   . PRO A 1 87  ? 31.035  2.159   -17.469 1.00 27.83  ? 116 PRO A O   1 
ATOM   674  C CB  . PRO A 1 87  ? 28.631  0.179   -18.415 1.00 28.10  ? 116 PRO A CB  1 
ATOM   675  C CG  . PRO A 1 87  ? 28.488  -1.029  -19.304 1.00 28.95  ? 116 PRO A CG  1 
ATOM   676  C CD  . PRO A 1 87  ? 28.882  -0.588  -20.661 1.00 25.68  ? 116 PRO A CD  1 
ATOM   677  N N   . GLU A 1 88  ? 31.910  0.296   -18.391 1.00 21.28  ? 117 GLU A N   1 
ATOM   678  C CA  . GLU A 1 88  ? 33.215  0.407   -17.781 1.00 23.57  ? 117 GLU A CA  1 
ATOM   679  C C   . GLU A 1 88  ? 33.798  1.791   -18.018 1.00 23.00  ? 117 GLU A C   1 
ATOM   680  O O   . GLU A 1 88  ? 34.333  2.409   -17.115 1.00 20.38  ? 117 GLU A O   1 
ATOM   681  C CB  . GLU A 1 88  ? 34.225  -0.583  -18.344 1.00 27.07  ? 117 GLU A CB  1 
ATOM   682  C CG  . GLU A 1 88  ? 33.960  -2.033  -17.949 1.00 26.70  ? 117 GLU A CG  1 
ATOM   683  C CD  . GLU A 1 88  ? 33.090  -2.838  -18.881 1.00 22.91  ? 117 GLU A CD  1 
ATOM   684  O OE1 . GLU A 1 88  ? 32.084  -2.266  -19.318 1.00 21.96  ? 117 GLU A OE1 1 
ATOM   685  O OE2 . GLU A 1 88  ? 33.375  -4.066  -19.072 1.00 19.68  ? 117 GLU A OE2 1 
ATOM   686  N N   . GLY A 1 89  ? 33.742  2.262   -19.266 1.00 21.36  ? 118 GLY A N   1 
ATOM   687  C CA  . GLY A 1 89  ? 34.324  3.555   -19.561 1.00 22.27  ? 118 GLY A CA  1 
ATOM   688  C C   . GLY A 1 89  ? 33.566  4.694   -18.897 1.00 20.48  ? 118 GLY A C   1 
ATOM   689  O O   . GLY A 1 89  ? 34.148  5.695   -18.471 1.00 22.17  ? 118 GLY A O   1 
ATOM   690  N N   . LEU A 1 90  ? 32.247  4.541   -18.860 1.00 23.21  ? 119 LEU A N   1 
ATOM   691  C CA  . LEU A 1 90  ? 31.389  5.464   -18.165 1.00 24.11  ? 119 LEU A CA  1 
ATOM   692  C C   . LEU A 1 90  ? 31.852  5.565   -16.715 1.00 22.54  ? 119 LEU A C   1 
ATOM   693  O O   . LEU A 1 90  ? 32.067  6.665   -16.228 1.00 19.30  ? 119 LEU A O   1 
ATOM   694  C CB  . LEU A 1 90  ? 29.924  5.046   -18.286 1.00 26.27  ? 119 LEU A CB  1 
ATOM   695  C CG  . LEU A 1 90  ? 28.910  5.992   -17.629 1.00 29.42  ? 119 LEU A CG  1 
ATOM   696  C CD1 . LEU A 1 90  ? 28.831  5.671   -16.154 1.00 29.63  ? 119 LEU A CD1 1 
ATOM   697  C CD2 . LEU A 1 90  ? 29.179  7.477   -17.833 1.00 27.08  ? 119 LEU A CD2 1 
ATOM   698  N N   . PHE A 1 91  ? 32.064  4.416   -16.065 1.00 20.83  ? 120 PHE A N   1 
ATOM   699  C CA  . PHE A 1 91  ? 32.426  4.417   -14.657 1.00 21.81  ? 120 PHE A CA  1 
ATOM   700  C C   . PHE A 1 91  ? 33.791  5.076   -14.444 1.00 21.99  ? 120 PHE A C   1 
ATOM   701  O O   . PHE A 1 91  ? 33.942  5.857   -13.518 1.00 17.44  ? 120 PHE A O   1 
ATOM   702  C CB  . PHE A 1 91  ? 32.394  3.005   -14.084 1.00 21.90  ? 120 PHE A CB  1 
ATOM   703  C CG  . PHE A 1 91  ? 32.795  2.929   -12.626 1.00 18.77  ? 120 PHE A CG  1 
ATOM   704  C CD1 . PHE A 1 91  ? 31.875  3.213   -11.640 1.00 19.06  ? 120 PHE A CD1 1 
ATOM   705  C CD2 . PHE A 1 91  ? 34.070  2.541   -12.232 1.00 18.43  ? 120 PHE A CD2 1 
ATOM   706  C CE1 . PHE A 1 91  ? 32.219  3.107   -10.292 1.00 18.72  ? 120 PHE A CE1 1 
ATOM   707  C CE2 . PHE A 1 91  ? 34.395  2.403   -10.896 1.00 21.51  ? 120 PHE A CE2 1 
ATOM   708  C CZ  . PHE A 1 91  ? 33.490  2.743   -9.921  1.00 18.99  ? 120 PHE A CZ  1 
ATOM   709  N N   . TRP A 1 92  ? 34.756  4.808   -15.348 1.00 22.88  ? 121 TRP A N   1 
ATOM   710  C CA  . TRP A 1 92  ? 36.070  5.404   -15.259 1.00 23.01  ? 121 TRP A CA  1 
ATOM   711  C C   . TRP A 1 92  ? 35.928  6.918   -15.342 1.00 21.44  ? 121 TRP A C   1 
ATOM   712  O O   . TRP A 1 92  ? 36.529  7.637   -14.563 1.00 26.07  ? 121 TRP A O   1 
ATOM   713  C CB  . TRP A 1 92  ? 36.978  4.869   -16.377 1.00 26.95  ? 121 TRP A CB  1 
ATOM   714  C CG  . TRP A 1 92  ? 38.420  5.284   -16.223 1.00 26.55  ? 121 TRP A CG  1 
ATOM   715  C CD1 . TRP A 1 92  ? 38.961  6.511   -16.465 1.00 29.18  ? 121 TRP A CD1 1 
ATOM   716  C CD2 . TRP A 1 92  ? 39.505  4.443   -15.803 1.00 24.94  ? 121 TRP A CD2 1 
ATOM   717  N NE1 . TRP A 1 92  ? 40.305  6.500   -16.205 1.00 25.58  ? 121 TRP A NE1 1 
ATOM   718  C CE2 . TRP A 1 92  ? 40.669  5.243   -15.812 1.00 27.11  ? 121 TRP A CE2 1 
ATOM   719  C CE3 . TRP A 1 92  ? 39.606  3.101   -15.447 1.00 23.78  ? 121 TRP A CE3 1 
ATOM   720  C CZ2 . TRP A 1 92  ? 41.914  4.746   -15.441 1.00 24.67  ? 121 TRP A CZ2 1 
ATOM   721  C CZ3 . TRP A 1 92  ? 40.851  2.590   -15.158 1.00 22.30  ? 121 TRP A CZ3 1 
ATOM   722  C CH2 . TRP A 1 92  ? 41.977  3.405   -15.140 1.00 24.75  ? 121 TRP A CH2 1 
ATOM   723  N N   . LEU A 1 93  ? 35.124  7.406   -16.288 1.00 22.53  ? 122 LEU A N   1 
ATOM   724  C CA  . LEU A 1 93  ? 34.890  8.846   -16.408 1.00 22.07  ? 122 LEU A CA  1 
ATOM   725  C C   . LEU A 1 93  ? 34.332  9.430   -15.105 1.00 22.35  ? 122 LEU A C   1 
ATOM   726  O O   . LEU A 1 93  ? 34.697  10.523  -14.652 1.00 22.06  ? 122 LEU A O   1 
ATOM   727  C CB  . LEU A 1 93  ? 33.958  9.089   -17.601 1.00 20.70  ? 122 LEU A CB  1 
ATOM   728  C CG  . LEU A 1 93  ? 33.380  10.493  -17.753 1.00 23.07  ? 122 LEU A CG  1 
ATOM   729  C CD1 . LEU A 1 93  ? 34.459  11.498  -17.975 1.00 22.75  ? 122 LEU A CD1 1 
ATOM   730  C CD2 . LEU A 1 93  ? 32.429  10.481  -18.909 1.00 25.60  ? 122 LEU A CD2 1 
ATOM   731  N N   . LEU A 1 94  ? 33.329  8.781   -14.554 1.00 26.37  ? 123 LEU A N   1 
ATOM   732  C CA  . LEU A 1 94  ? 32.662  9.350   -13.387 1.00 24.28  ? 123 LEU A CA  1 
ATOM   733  C C   . LEU A 1 94  ? 33.648  9.411   -12.224 1.00 23.39  ? 123 LEU A C   1 
ATOM   734  O O   . LEU A 1 94  ? 33.647  10.374  -11.474 1.00 26.03  ? 123 LEU A O   1 
ATOM   735  C CB  . LEU A 1 94  ? 31.429  8.506   -13.066 1.00 23.89  ? 123 LEU A CB  1 
ATOM   736  C CG  . LEU A 1 94  ? 30.254  8.557   -14.044 1.00 25.88  ? 123 LEU A CG  1 
ATOM   737  C CD1 . LEU A 1 94  ? 29.038  7.841   -13.412 1.00 28.39  ? 123 LEU A CD1 1 
ATOM   738  C CD2 . LEU A 1 94  ? 29.863  9.977   -14.441 1.00 28.00  ? 123 LEU A CD2 1 
ATOM   739  N N   . VAL A 1 95  ? 34.489  8.377   -12.078 1.00 24.77  ? 124 VAL A N   1 
ATOM   740  C CA  . VAL A 1 95  ? 35.443  8.290   -10.982 1.00 27.72  ? 124 VAL A CA  1 
ATOM   741  C C   . VAL A 1 95  ? 36.571  9.312   -11.152 1.00 27.46  ? 124 VAL A C   1 
ATOM   742  O O   . VAL A 1 95  ? 37.035  9.904   -10.173 1.00 24.08  ? 124 VAL A O   1 
ATOM   743  C CB  . VAL A 1 95  ? 36.003  6.866   -10.885 1.00 25.41  ? 124 VAL A CB  1 
ATOM   744  C CG1 . VAL A 1 95  ? 37.221  6.801   -9.988  1.00 30.66  ? 124 VAL A CG1 1 
ATOM   745  C CG2 . VAL A 1 95  ? 34.922  5.953   -10.347 1.00 25.79  ? 124 VAL A CG2 1 
ATOM   746  N N   . THR A 1 96  ? 37.039  9.503   -12.385 1.00 25.03  ? 125 THR A N   1 
ATOM   747  C CA  . THR A 1 96  ? 38.307  10.185  -12.577 1.00 26.05  ? 125 THR A CA  1 
ATOM   748  C C   . THR A 1 96  ? 38.062  11.554  -13.182 1.00 26.18  ? 125 THR A C   1 
ATOM   749  O O   . THR A 1 96  ? 38.868  12.469  -12.999 1.00 25.97  ? 125 THR A O   1 
ATOM   750  C CB  . THR A 1 96  ? 39.275  9.382   -13.459 1.00 28.49  ? 125 THR A CB  1 
ATOM   751  O OG1 . THR A 1 96  ? 38.757  9.351   -14.786 1.00 25.28  ? 125 THR A OG1 1 
ATOM   752  C CG2 . THR A 1 96  ? 39.577  8.004   -12.903 1.00 30.26  ? 125 THR A CG2 1 
ATOM   753  N N   . GLY A 1 97  ? 36.943  11.686  -13.890 1.00 27.27  ? 126 GLY A N   1 
ATOM   754  C CA  . GLY A 1 97  ? 36.646  12.912  -14.607 1.00 26.91  ? 126 GLY A CA  1 
ATOM   755  C C   . GLY A 1 97  ? 37.365  12.933  -15.946 1.00 27.02  ? 126 GLY A C   1 
ATOM   756  O O   . GLY A 1 97  ? 37.282  13.926  -16.646 1.00 27.12  ? 126 GLY A O   1 
ATOM   757  N N   . HIS A 1 98  ? 38.025  11.819  -16.287 1.00 26.06  ? 127 HIS A N   1 
ATOM   758  C CA  . HIS A 1 98  ? 38.789  11.714  -17.515 1.00 28.17  ? 127 HIS A CA  1 
ATOM   759  C C   . HIS A 1 98  ? 38.170  10.625  -18.380 1.00 30.01  ? 127 HIS A C   1 
ATOM   760  O O   . HIS A 1 98  ? 37.744  9.583   -17.872 1.00 27.59  ? 127 HIS A O   1 
ATOM   761  C CB  . HIS A 1 98  ? 40.256  11.350  -17.264 1.00 31.60  ? 127 HIS A CB  1 
ATOM   762  C CG  . HIS A 1 98  ? 40.981  12.370  -16.473 1.00 40.74  ? 127 HIS A CG  1 
ATOM   763  N ND1 . HIS A 1 98  ? 40.733  13.715  -16.628 1.00 46.49  ? 127 HIS A ND1 1 
ATOM   764  C CD2 . HIS A 1 98  ? 41.930  12.263  -15.543 1.00 47.66  ? 127 HIS A CD2 1 
ATOM   765  C CE1 . HIS A 1 98  ? 41.513  14.396  -15.811 1.00 48.93  ? 127 HIS A CE1 1 
ATOM   766  N NE2 . HIS A 1 98  ? 42.241  13.537  -15.133 1.00 52.42  ? 127 HIS A NE2 1 
ATOM   767  N N   . ILE A 1 99  ? 38.181  10.853  -19.701 1.00 29.09  ? 128 ILE A N   1 
ATOM   768  C CA  . ILE A 1 99  ? 37.845  9.815   -20.658 1.00 27.89  ? 128 ILE A CA  1 
ATOM   769  C C   . ILE A 1 99  ? 38.929  8.750   -20.591 1.00 28.39  ? 128 ILE A C   1 
ATOM   770  O O   . ILE A 1 99  ? 40.093  9.078   -20.753 1.00 31.25  ? 128 ILE A O   1 
ATOM   771  C CB  . ILE A 1 99  ? 37.751  10.402  -22.083 1.00 30.71  ? 128 ILE A CB  1 
ATOM   772  C CG1 . ILE A 1 99  ? 36.638  11.452  -22.182 1.00 32.09  ? 128 ILE A CG1 1 
ATOM   773  C CG2 . ILE A 1 99  ? 37.569  9.280   -23.118 1.00 33.25  ? 128 ILE A CG2 1 
ATOM   774  C CD1 . ILE A 1 99  ? 35.220  10.899  -22.088 1.00 33.61  ? 128 ILE A CD1 1 
ATOM   775  N N   . PRO A 1 100 ? 38.597  7.455   -20.401 1.00 24.92  ? 129 PRO A N   1 
ATOM   776  C CA  . PRO A 1 100 ? 39.598  6.390   -20.333 1.00 25.85  ? 129 PRO A CA  1 
ATOM   777  C C   . PRO A 1 100 ? 40.130  6.005   -21.712 1.00 27.59  ? 129 PRO A C   1 
ATOM   778  O O   . PRO A 1 100 ? 39.398  6.168   -22.674 1.00 24.17  ? 129 PRO A O   1 
ATOM   779  C CB  . PRO A 1 100 ? 38.806  5.224   -19.748 1.00 25.45  ? 129 PRO A CB  1 
ATOM   780  C CG  . PRO A 1 100 ? 37.425  5.431   -20.259 1.00 25.04  ? 129 PRO A CG  1 
ATOM   781  C CD  . PRO A 1 100 ? 37.234  6.941   -20.282 1.00 24.84  ? 129 PRO A CD  1 
ATOM   782  N N   . THR A 1 101 ? 41.360  5.464   -21.764 1.00 28.63  ? 130 THR A N   1 
ATOM   783  C CA  . THR A 1 101 ? 41.902  4.792   -22.934 1.00 30.27  ? 130 THR A CA  1 
ATOM   784  C C   . THR A 1 101 ? 41.247  3.422   -23.079 1.00 34.36  ? 130 THR A C   1 
ATOM   785  O O   . THR A 1 101 ? 40.653  2.889   -22.134 1.00 31.24  ? 130 THR A O   1 
ATOM   786  C CB  . THR A 1 101 ? 43.418  4.605   -22.800 1.00 32.18  ? 130 THR A CB  1 
ATOM   787  O OG1 . THR A 1 101 ? 43.528  3.689   -21.722 1.00 35.07  ? 130 THR A OG1 1 
ATOM   788  C CG2 . THR A 1 101 ? 44.184  5.875   -22.478 1.00 29.20  ? 130 THR A CG2 1 
ATOM   789  N N   . GLU A 1 102 ? 41.431  2.833   -24.265 1.00 32.42  ? 131 GLU A N   1 
ATOM   790  C CA  . GLU A 1 102 ? 41.088  1.452   -24.536 1.00 35.41  ? 131 GLU A CA  1 
ATOM   791  C C   . GLU A 1 102 ? 41.655  0.532   -23.453 1.00 33.05  ? 131 GLU A C   1 
ATOM   792  O O   . GLU A 1 102 ? 40.996  -0.398  -23.012 1.00 33.05  ? 131 GLU A O   1 
ATOM   793  C CB  . GLU A 1 102 ? 41.678  1.048   -25.889 1.00 43.30  ? 131 GLU A CB  1 
ATOM   794  C CG  . GLU A 1 102 ? 41.062  1.739   -27.104 1.00 49.36  ? 131 GLU A CG  1 
ATOM   795  C CD  . GLU A 1 102 ? 39.732  1.189   -27.595 1.00 61.09  ? 131 GLU A CD  1 
ATOM   796  O OE1 . GLU A 1 102 ? 39.165  0.274   -26.958 1.00 72.49  ? 131 GLU A OE1 1 
ATOM   797  O OE2 . GLU A 1 102 ? 39.248  1.679   -28.635 1.00 66.58  ? 131 GLU A OE2 1 
ATOM   798  N N   . GLU A 1 103 ? 42.905  0.771   -23.064 1.00 33.32  ? 132 GLU A N   1 
ATOM   799  C CA  . GLU A 1 103 ? 43.625  -0.101  -22.148 1.00 38.12  ? 132 GLU A CA  1 
ATOM   800  C C   . GLU A 1 103 ? 43.012  -0.052  -20.741 1.00 31.42  ? 132 GLU A C   1 
ATOM   801  O O   . GLU A 1 103 ? 42.962  -1.048  -20.028 1.00 26.83  ? 132 GLU A O   1 
ATOM   802  C CB  . GLU A 1 103 ? 45.099  0.319   -22.069 1.00 44.55  ? 132 GLU A CB  1 
ATOM   803  C CG  . GLU A 1 103 ? 45.919  0.051   -23.339 1.00 55.07  ? 132 GLU A CG  1 
ATOM   804  C CD  . GLU A 1 103 ? 45.508  0.802   -24.615 1.00 58.46  ? 132 GLU A CD  1 
ATOM   805  O OE1 . GLU A 1 103 ? 45.297  2.051   -24.595 1.00 46.75  ? 132 GLU A OE1 1 
ATOM   806  O OE2 . GLU A 1 103 ? 45.389  0.117   -25.662 1.00 57.96  ? 132 GLU A OE2 1 
ATOM   807  N N   . GLN A 1 104 ? 42.605  1.131   -20.301 1.00 31.84  ? 133 GLN A N   1 
ATOM   808  C CA  . GLN A 1 104 ? 42.025  1.275   -18.977 1.00 29.14  ? 133 GLN A CA  1 
ATOM   809  C C   . GLN A 1 104 ? 40.669  0.580   -18.911 1.00 30.09  ? 133 GLN A C   1 
ATOM   810  O O   . GLN A 1 104 ? 40.328  -0.059  -17.924 1.00 34.15  ? 133 GLN A O   1 
ATOM   811  C CB  . GLN A 1 104 ? 41.979  2.760   -18.654 1.00 29.45  ? 133 GLN A CB  1 
ATOM   812  C CG  . GLN A 1 104 ? 43.364  3.384   -18.570 1.00 29.38  ? 133 GLN A CG  1 
ATOM   813  C CD  . GLN A 1 104 ? 43.326  4.893   -18.525 1.00 30.31  ? 133 GLN A CD  1 
ATOM   814  O OE1 . GLN A 1 104 ? 42.497  5.549   -19.162 1.00 33.83  ? 133 GLN A OE1 1 
ATOM   815  N NE2 . GLN A 1 104 ? 44.171  5.464   -17.688 1.00 31.54  ? 133 GLN A NE2 1 
ATOM   816  N N   . VAL A 1 105 ? 39.909  0.659   -19.998 1.00 31.62  ? 134 VAL A N   1 
ATOM   817  C CA  . VAL A 1 105 ? 38.626  -0.011  -20.067 1.00 29.40  ? 134 VAL A CA  1 
ATOM   818  C C   . VAL A 1 105 ? 38.840  -1.514  -20.009 1.00 32.53  ? 134 VAL A C   1 
ATOM   819  O O   . VAL A 1 105 ? 38.141  -2.171  -19.238 1.00 30.97  ? 134 VAL A O   1 
ATOM   820  C CB  . VAL A 1 105 ? 37.876  0.462   -21.318 1.00 30.46  ? 134 VAL A CB  1 
ATOM   821  C CG1 . VAL A 1 105 ? 36.719  -0.452  -21.673 1.00 30.44  ? 134 VAL A CG1 1 
ATOM   822  C CG2 . VAL A 1 105 ? 37.403  1.890   -21.093 1.00 30.16  ? 134 VAL A CG2 1 
ATOM   823  N N   . SER A 1 106 ? 39.818  -2.011  -20.805 1.00 33.10  ? 135 SER A N   1 
ATOM   824  C CA  A SER A 1 106 ? 40.204  -3.418  -20.819 0.50 33.92  ? 135 SER A CA  1 
ATOM   825  C CA  B SER A 1 106 ? 40.215  -3.416  -20.823 0.50 33.67  ? 135 SER A CA  1 
ATOM   826  C C   . SER A 1 106 ? 40.619  -3.881  -19.421 1.00 29.42  ? 135 SER A C   1 
ATOM   827  O O   . SER A 1 106 ? 40.231  -4.943  -18.984 1.00 30.10  ? 135 SER A O   1 
ATOM   828  C CB  A SER A 1 106 ? 41.321  -3.674  -21.812 0.50 34.34  ? 135 SER A CB  1 
ATOM   829  C CB  B SER A 1 106 ? 41.349  -3.654  -21.816 0.50 33.69  ? 135 SER A CB  1 
ATOM   830  O OG  A SER A 1 106 ? 41.615  -5.062  -21.878 0.50 34.10  ? 135 SER A OG  1 
ATOM   831  O OG  B SER A 1 106 ? 40.933  -3.403  -23.154 0.50 33.08  ? 135 SER A OG  1 
ATOM   832  N N   . TRP A 1 107 ? 41.417  -3.077  -18.730 1.00 26.95  ? 136 TRP A N   1 
ATOM   833  C CA  . TRP A 1 107 ? 41.824  -3.388  -17.365 1.00 29.99  ? 136 TRP A CA  1 
ATOM   834  C C   . TRP A 1 107 ? 40.615  -3.404  -16.406 1.00 26.33  ? 136 TRP A C   1 
ATOM   835  O O   . TRP A 1 107 ? 40.442  -4.296  -15.604 1.00 24.14  ? 136 TRP A O   1 
ATOM   836  C CB  . TRP A 1 107 ? 42.893  -2.382  -16.915 1.00 31.87  ? 136 TRP A CB  1 
ATOM   837  C CG  . TRP A 1 107 ? 43.304  -2.574  -15.481 1.00 33.32  ? 136 TRP A CG  1 
ATOM   838  C CD1 . TRP A 1 107 ? 44.267  -3.398  -14.978 1.00 33.60  ? 136 TRP A CD1 1 
ATOM   839  C CD2 . TRP A 1 107 ? 42.653  -1.972  -14.346 1.00 32.39  ? 136 TRP A CD2 1 
ATOM   840  N NE1 . TRP A 1 107 ? 44.294  -3.301  -13.610 1.00 35.15  ? 136 TRP A NE1 1 
ATOM   841  C CE2 . TRP A 1 107 ? 43.299  -2.461  -13.191 1.00 35.54  ? 136 TRP A CE2 1 
ATOM   842  C CE3 . TRP A 1 107 ? 41.581  -1.087  -14.196 1.00 35.22  ? 136 TRP A CE3 1 
ATOM   843  C CZ2 . TRP A 1 107 ? 42.913  -2.079  -11.908 1.00 36.44  ? 136 TRP A CZ2 1 
ATOM   844  C CZ3 . TRP A 1 107 ? 41.185  -0.732  -12.924 1.00 33.86  ? 136 TRP A CZ3 1 
ATOM   845  C CH2 . TRP A 1 107 ? 41.832  -1.233  -11.795 1.00 34.63  ? 136 TRP A CH2 1 
ATOM   846  N N   . LEU A 1 108 ? 39.692  -2.461  -16.526 1.00 29.80  ? 137 LEU A N   1 
ATOM   847  C CA  . LEU A 1 108 ? 38.536  -2.464  -15.646 1.00 28.45  ? 137 LEU A CA  1 
ATOM   848  C C   . LEU A 1 108 ? 37.597  -3.635  -15.939 1.00 28.42  ? 137 LEU A C   1 
ATOM   849  O O   . LEU A 1 108 ? 36.981  -4.199  -15.032 1.00 26.70  ? 137 LEU A O   1 
ATOM   850  C CB  . LEU A 1 108 ? 37.867  -1.111  -15.783 1.00 29.03  ? 137 LEU A CB  1 
ATOM   851  C CG  . LEU A 1 108 ? 36.673  -0.909  -14.860 1.00 28.66  ? 137 LEU A CG  1 
ATOM   852  C CD1 . LEU A 1 108 ? 37.067  -1.070  -13.395 1.00 28.91  ? 137 LEU A CD1 1 
ATOM   853  C CD2 . LEU A 1 108 ? 36.161  0.464   -15.167 1.00 27.52  ? 137 LEU A CD2 1 
ATOM   854  N N   . SER A 1 109 ? 37.539  -4.089  -17.190 1.00 26.73  ? 138 SER A N   1 
ATOM   855  C CA  . SER A 1 109 ? 36.686  -5.233  -17.503 1.00 27.97  ? 138 SER A CA  1 
ATOM   856  C C   . SER A 1 109 ? 37.206  -6.489  -16.807 1.00 25.47  ? 138 SER A C   1 
ATOM   857  O O   . SER A 1 109 ? 36.414  -7.321  -16.382 1.00 23.30  ? 138 SER A O   1 
ATOM   858  C CB  . SER A 1 109 ? 36.545  -5.489  -19.006 1.00 28.76  ? 138 SER A CB  1 
ATOM   859  O OG  . SER A 1 109 ? 35.766  -4.490  -19.646 1.00 31.16  ? 138 SER A OG  1 
ATOM   860  N N   . LYS A 1 110 ? 38.537  -6.658  -16.797 1.00 23.14  ? 139 LYS A N   1 
ATOM   861  C CA  . LYS A 1 110 ? 39.177  -7.814  -16.180 1.00 28.12  ? 139 LYS A CA  1 
ATOM   862  C C   . LYS A 1 110 ? 39.072  -7.728  -14.655 1.00 27.51  ? 139 LYS A C   1 
ATOM   863  O O   . LYS A 1 110 ? 38.853  -8.729  -13.985 1.00 25.21  ? 139 LYS A O   1 
ATOM   864  C CB  . LYS A 1 110 ? 40.637  -7.879  -16.649 1.00 32.96  ? 139 LYS A CB  1 
ATOM   865  C CG  . LYS A 1 110 ? 40.813  -8.469  -18.025 1.00 36.90  ? 139 LYS A CG  1 
ATOM   866  C CD  . LYS A 1 110 ? 42.190  -8.252  -18.653 1.00 44.97  ? 139 LYS A CD  1 
ATOM   867  C CE  . LYS A 1 110 ? 42.120  -8.299  -20.170 1.00 47.90  ? 139 LYS A CE  1 
ATOM   868  N NZ  . LYS A 1 110 ? 43.004  -7.283  -20.751 1.00 55.40  ? 139 LYS A NZ  1 
ATOM   869  N N   . GLU A 1 111 ? 39.161  -6.519  -14.109 1.00 25.84  ? 140 GLU A N   1 
ATOM   870  C CA  . GLU A 1 111 ? 38.986  -6.334  -12.665 1.00 29.97  ? 140 GLU A CA  1 
ATOM   871  C C   . GLU A 1 111 ? 37.595  -6.773  -12.203 1.00 29.64  ? 140 GLU A C   1 
ATOM   872  O O   . GLU A 1 111 ? 37.466  -7.423  -11.157 1.00 30.48  ? 140 GLU A O   1 
ATOM   873  C CB  . GLU A 1 111 ? 39.211  -4.888  -12.242 1.00 31.30  ? 140 GLU A CB  1 
ATOM   874  C CG  . GLU A 1 111 ? 40.672  -4.508  -12.066 1.00 38.23  ? 140 GLU A CG  1 
ATOM   875  C CD  . GLU A 1 111 ? 41.326  -5.354  -10.985 1.00 43.28  ? 140 GLU A CD  1 
ATOM   876  O OE1 . GLU A 1 111 ? 40.943  -5.273  -9.781  1.00 52.28  ? 140 GLU A OE1 1 
ATOM   877  O OE2 . GLU A 1 111 ? 42.169  -6.158  -11.389 1.00 44.05  ? 140 GLU A OE2 1 
ATOM   878  N N   . TRP A 1 112 ? 36.557  -6.431  -12.985 1.00 27.92  ? 141 TRP A N   1 
ATOM   879  C CA  . TRP A 1 112 ? 35.198  -6.769  -12.625 1.00 24.45  ? 141 TRP A CA  1 
ATOM   880  C C   . TRP A 1 112 ? 34.927  -8.255  -12.866 1.00 29.29  ? 141 TRP A C   1 
ATOM   881  O O   . TRP A 1 112 ? 34.274  -8.895  -12.061 1.00 28.70  ? 141 TRP A O   1 
ATOM   882  C CB  . TRP A 1 112 ? 34.174  -5.871  -13.345 1.00 26.30  ? 141 TRP A CB  1 
ATOM   883  C CG  . TRP A 1 112 ? 34.141  -4.465  -12.804 1.00 21.40  ? 141 TRP A CG  1 
ATOM   884  C CD1 . TRP A 1 112 ? 34.767  -4.017  -11.696 1.00 23.64  ? 141 TRP A CD1 1 
ATOM   885  C CD2 . TRP A 1 112 ? 33.467  -3.320  -13.352 1.00 22.79  ? 141 TRP A CD2 1 
ATOM   886  N NE1 . TRP A 1 112 ? 34.547  -2.688  -11.521 1.00 23.64  ? 141 TRP A NE1 1 
ATOM   887  C CE2 . TRP A 1 112 ? 33.746  -2.230  -12.511 1.00 23.31  ? 141 TRP A CE2 1 
ATOM   888  C CE3 . TRP A 1 112 ? 32.677  -3.107  -14.476 1.00 23.59  ? 141 TRP A CE3 1 
ATOM   889  C CZ2 . TRP A 1 112 ? 33.259  -0.949  -12.745 1.00 23.24  ? 141 TRP A CZ2 1 
ATOM   890  C CZ3 . TRP A 1 112 ? 32.176  -1.846  -14.707 1.00 25.23  ? 141 TRP A CZ3 1 
ATOM   891  C CH2 . TRP A 1 112 ? 32.477  -0.780  -13.858 1.00 23.75  ? 141 TRP A CH2 1 
ATOM   892  N N   . ALA A 1 113 ? 35.510  -8.856  -13.904 1.00 33.45  ? 142 ALA A N   1 
ATOM   893  C CA  . ALA A 1 113 ? 35.434  -10.315 -14.049 1.00 32.58  ? 142 ALA A CA  1 
ATOM   894  C C   . ALA A 1 113 ? 36.014  -11.051 -12.846 1.00 27.72  ? 142 ALA A C   1 
ATOM   895  O O   . ALA A 1 113 ? 35.433  -12.011 -12.362 1.00 33.39  ? 142 ALA A O   1 
ATOM   896  C CB  . ALA A 1 113 ? 36.172  -10.760 -15.280 1.00 31.90  ? 142 ALA A CB  1 
ATOM   897  N N   . LYS A 1 114 ? 37.148  -10.586 -12.340 1.00 31.73  ? 143 LYS A N   1 
ATOM   898  C CA  . LYS A 1 114 ? 37.850  -11.292 -11.280 1.00 34.75  ? 143 LYS A CA  1 
ATOM   899  C C   . LYS A 1 114 ? 37.098  -11.208 -9.943  1.00 34.12  ? 143 LYS A C   1 
ATOM   900  O O   . LYS A 1 114 ? 37.293  -12.072 -9.097  1.00 27.65  ? 143 LYS A O   1 
ATOM   901  C CB  . LYS A 1 114 ? 39.226  -10.694 -10.970 1.00 38.60  ? 143 LYS A CB  1 
ATOM   902  C CG  . LYS A 1 114 ? 40.292  -10.686 -12.046 1.00 45.26  ? 143 LYS A CG  1 
ATOM   903  C CD  . LYS A 1 114 ? 41.501  -9.881  -11.565 1.00 52.20  ? 143 LYS A CD  1 
ATOM   904  C CE  . LYS A 1 114 ? 42.762  -10.111 -12.324 1.00 54.39  ? 143 LYS A CE  1 
ATOM   905  N NZ  . LYS A 1 114 ? 43.770  -9.154  -11.862 1.00 54.88  ? 143 LYS A NZ  1 
ATOM   906  N N   . ARG A 1 115 ? 36.249  -10.176 -9.745  1.00 29.34  ? 144 ARG A N   1 
ATOM   907  C CA  . ARG A 1 115 ? 35.631  -9.929  -8.440  1.00 26.57  ? 144 ARG A CA  1 
ATOM   908  C C   . ARG A 1 115 ? 34.184  -10.417 -8.358  1.00 26.44  ? 144 ARG A C   1 
ATOM   909  O O   . ARG A 1 115 ? 33.504  -10.140 -7.377  1.00 26.73  ? 144 ARG A O   1 
ATOM   910  C CB  . ARG A 1 115 ? 35.644  -8.419  -8.144  1.00 26.22  ? 144 ARG A CB  1 
ATOM   911  C CG  . ARG A 1 115 ? 36.994  -7.783  -7.849  1.00 25.03  ? 144 ARG A CG  1 
ATOM   912  C CD  . ARG A 1 115 ? 36.964  -6.286  -8.002  1.00 25.90  ? 144 ARG A CD  1 
ATOM   913  N NE  . ARG A 1 115 ? 38.259  -5.652  -7.761  1.00 26.26  ? 144 ARG A NE  1 
ATOM   914  C CZ  . ARG A 1 115 ? 38.641  -4.943  -6.707  1.00 28.77  ? 144 ARG A CZ  1 
ATOM   915  N NH1 . ARG A 1 115 ? 37.918  -4.949  -5.616  1.00 27.52  ? 144 ARG A NH1 1 
ATOM   916  N NH2 . ARG A 1 115 ? 39.818  -4.337  -6.692  1.00 26.61  ? 144 ARG A NH2 1 
ATOM   917  N N   . ALA A 1 116 ? 33.729  -11.213 -9.333  1.00 25.65  ? 145 ALA A N   1 
ATOM   918  C CA  . ALA A 1 116 ? 32.325  -11.488 -9.583  1.00 28.01  ? 145 ALA A CA  1 
ATOM   919  C C   . ALA A 1 116 ? 31.713  -12.641 -8.778  1.00 29.99  ? 145 ALA A C   1 
ATOM   920  O O   . ALA A 1 116 ? 30.521  -12.900 -8.933  1.00 36.95  ? 145 ALA A O   1 
ATOM   921  C CB  . ALA A 1 116 ? 32.181  -11.810 -11.045 1.00 31.31  ? 145 ALA A CB  1 
ATOM   922  N N   . ALA A 1 117 ? 32.486  -13.343 -7.945  1.00 32.23  ? 146 ALA A N   1 
ATOM   923  C CA  . ALA A 1 117 ? 31.989  -14.517 -7.237  1.00 31.70  ? 146 ALA A CA  1 
ATOM   924  C C   . ALA A 1 117 ? 30.977  -14.107 -6.173  1.00 30.39  ? 146 ALA A C   1 
ATOM   925  O O   . ALA A 1 117 ? 31.200  -13.125 -5.492  1.00 30.35  ? 146 ALA A O   1 
ATOM   926  C CB  . ALA A 1 117 ? 33.136  -15.231 -6.578  1.00 35.59  ? 146 ALA A CB  1 
ATOM   927  N N   . LEU A 1 118 ? 29.908  -14.893 -6.013  1.00 28.03  ? 147 LEU A N   1 
ATOM   928  C CA  . LEU A 1 118 ? 28.957  -14.713 -4.928  1.00 28.46  ? 147 LEU A CA  1 
ATOM   929  C C   . LEU A 1 118 ? 29.225  -15.699 -3.788  1.00 28.67  ? 147 LEU A C   1 
ATOM   930  O O   . LEU A 1 118 ? 29.439  -16.880 -4.038  1.00 29.35  ? 147 LEU A O   1 
ATOM   931  C CB  . LEU A 1 118 ? 27.546  -14.920 -5.477  1.00 27.07  ? 147 LEU A CB  1 
ATOM   932  C CG  . LEU A 1 118 ? 27.114  -14.063 -6.673  1.00 30.80  ? 147 LEU A CG  1 
ATOM   933  C CD1 . LEU A 1 118 ? 25.675  -14.374 -6.998  1.00 33.64  ? 147 LEU A CD1 1 
ATOM   934  C CD2 . LEU A 1 118 ? 27.265  -12.560 -6.391  1.00 28.60  ? 147 LEU A CD2 1 
ATOM   935  N N   . PRO A 1 119 ? 29.036  -15.331 -2.500  1.00 29.15  ? 148 PRO A N   1 
ATOM   936  C CA  . PRO A 1 119 ? 29.166  -16.305 -1.405  1.00 26.96  ? 148 PRO A CA  1 
ATOM   937  C C   . PRO A 1 119 ? 27.981  -17.271 -1.372  1.00 24.76  ? 148 PRO A C   1 
ATOM   938  O O   . PRO A 1 119 ? 26.874  -16.893 -1.759  1.00 22.61  ? 148 PRO A O   1 
ATOM   939  C CB  . PRO A 1 119 ? 29.241  -15.439 -0.131  1.00 26.82  ? 148 PRO A CB  1 
ATOM   940  C CG  . PRO A 1 119 ? 28.749  -14.089 -0.539  1.00 29.50  ? 148 PRO A CG  1 
ATOM   941  C CD  . PRO A 1 119 ? 28.572  -14.007 -2.043  1.00 27.90  ? 148 PRO A CD  1 
ATOM   942  N N   . SER A 1 120 ? 28.184  -18.495 -0.868  1.00 22.29  ? 149 SER A N   1 
ATOM   943  C CA  . SER A 1 120 ? 27.155  -19.528 -0.977  1.00 22.80  ? 149 SER A CA  1 
ATOM   944  C C   . SER A 1 120 ? 25.816  -19.059 -0.365  1.00 23.72  ? 149 SER A C   1 
ATOM   945  O O   . SER A 1 120 ? 24.739  -19.425 -0.834  1.00 20.76  ? 149 SER A O   1 
ATOM   946  C CB  . SER A 1 120 ? 27.598  -20.814 -0.333  1.00 24.89  ? 149 SER A CB  1 
ATOM   947  O OG  . SER A 1 120 ? 28.908  -21.192 -0.718  1.00 27.98  ? 149 SER A OG  1 
ATOM   948  N N   . HIS A 1 121 ? 25.848  -18.260 0.711   1.00 20.42  ? 150 HIS A N   1 
ATOM   949  C CA  . HIS A 1 121 ? 24.591  -17.904 1.362   1.00 21.37  ? 150 HIS A CA  1 
ATOM   950  C C   . HIS A 1 121 ? 23.750  -17.018 0.441   1.00 22.77  ? 150 HIS A C   1 
ATOM   951  O O   . HIS A 1 121 ? 22.516  -17.090 0.491   1.00 23.15  ? 150 HIS A O   1 
ATOM   952  C CB  . HIS A 1 121 ? 24.774  -17.269 2.747   1.00 20.92  ? 150 HIS A CB  1 
ATOM   953  C CG  . HIS A 1 121 ? 25.293  -15.860 2.755   1.00 22.68  ? 150 HIS A CG  1 
ATOM   954  N ND1 . HIS A 1 121 ? 26.626  -15.565 2.604   1.00 23.87  ? 150 HIS A ND1 1 
ATOM   955  C CD2 . HIS A 1 121 ? 24.682  -14.695 2.905   1.00 21.23  ? 150 HIS A CD2 1 
ATOM   956  C CE1 . HIS A 1 121 ? 26.798  -14.252 2.670   1.00 24.28  ? 150 HIS A CE1 1 
ATOM   957  N NE2 . HIS A 1 121 ? 25.638  -13.719 2.872   1.00 21.49  ? 150 HIS A NE2 1 
ATOM   958  N N   . VAL A 1 122 ? 24.397  -16.242 -0.451  1.00 23.03  ? 151 VAL A N   1 
ATOM   959  C CA  . VAL A 1 122 ? 23.639  -15.360 -1.333  1.00 23.21  ? 151 VAL A CA  1 
ATOM   960  C C   . VAL A 1 122 ? 23.010  -16.127 -2.498  1.00 26.38  ? 151 VAL A C   1 
ATOM   961  O O   . VAL A 1 122 ? 21.841  -15.984 -2.787  1.00 24.30  ? 151 VAL A O   1 
ATOM   962  C CB  . VAL A 1 122 ? 24.463  -14.140 -1.758  1.00 23.63  ? 151 VAL A CB  1 
ATOM   963  C CG1 . VAL A 1 122 ? 23.710  -13.250 -2.763  1.00 22.84  ? 151 VAL A CG1 1 
ATOM   964  C CG2 . VAL A 1 122 ? 24.820  -13.358 -0.494  1.00 22.69  ? 151 VAL A CG2 1 
ATOM   965  N N   . VAL A 1 123 ? 23.764  -17.038 -3.087  1.00 27.85  ? 152 VAL A N   1 
ATOM   966  C CA  . VAL A 1 123 ? 23.228  -18.013 -4.013  1.00 25.27  ? 152 VAL A CA  1 
ATOM   967  C C   . VAL A 1 123 ? 22.002  -18.729 -3.443  1.00 24.68  ? 152 VAL A C   1 
ATOM   968  O O   . VAL A 1 123 ? 20.947  -18.729 -4.081  1.00 26.85  ? 152 VAL A O   1 
ATOM   969  C CB  . VAL A 1 123 ? 24.331  -19.029 -4.350  1.00 24.84  ? 152 VAL A CB  1 
ATOM   970  C CG1 . VAL A 1 123 ? 23.784  -20.132 -5.259  1.00 30.49  ? 152 VAL A CG1 1 
ATOM   971  C CG2 . VAL A 1 123 ? 25.547  -18.337 -4.973  1.00 27.19  ? 152 VAL A CG2 1 
ATOM   972  N N   . THR A 1 124 ? 22.142  -19.369 -2.278  1.00 22.01  ? 153 THR A N   1 
ATOM   973  C CA  . THR A 1 124 ? 21.065  -20.107 -1.639  1.00 26.39  ? 153 THR A CA  1 
ATOM   974  C C   . THR A 1 124 ? 19.816  -19.256 -1.455  1.00 23.41  ? 153 THR A C   1 
ATOM   975  O O   . THR A 1 124 ? 18.697  -19.728 -1.625  1.00 25.35  ? 153 THR A O   1 
ATOM   976  C CB  . THR A 1 124 ? 21.528  -20.608 -0.271  1.00 30.07  ? 153 THR A CB  1 
ATOM   977  O OG1 . THR A 1 124 ? 22.524  -21.538 -0.661  1.00 34.11  ? 153 THR A OG1 1 
ATOM   978  C CG2 . THR A 1 124 ? 20.423  -21.269 0.537   1.00 32.39  ? 153 THR A CG2 1 
ATOM   979  N N   . MET A 1 125 ? 20.014  -18.045 -0.959  1.00 23.76  ? 154 MET A N   1 
ATOM   980  C CA  . MET A 1 125 ? 18.923  -17.124 -0.678  1.00 26.20  ? 154 MET A CA  1 
ATOM   981  C C   . MET A 1 125 ? 18.145  -16.830 -1.955  1.00 23.80  ? 154 MET A C   1 
ATOM   982  O O   . MET A 1 125 ? 16.907  -16.887 -1.969  1.00 22.73  ? 154 MET A O   1 
ATOM   983  C CB  . MET A 1 125 ? 19.527  -15.866 -0.056  1.00 27.86  ? 154 MET A CB  1 
ATOM   984  C CG  . MET A 1 125 ? 18.567  -14.765 0.228   1.00 39.73  ? 154 MET A CG  1 
ATOM   985  S SD  . MET A 1 125 ? 19.617  -13.322 0.492   1.00 40.58  ? 154 MET A SD  1 
ATOM   986  C CE  . MET A 1 125 ? 18.442  -11.996 0.292   1.00 40.03  ? 154 MET A CE  1 
ATOM   987  N N   . LEU A 1 126 ? 18.865  -16.549 -3.051  1.00 25.55  ? 155 LEU A N   1 
ATOM   988  C CA  . LEU A 1 126 ? 18.199  -16.244 -4.297  1.00 26.12  ? 155 LEU A CA  1 
ATOM   989  C C   . LEU A 1 126 ? 17.434  -17.473 -4.762  1.00 29.99  ? 155 LEU A C   1 
ATOM   990  O O   . LEU A 1 126 ? 16.278  -17.349 -5.101  1.00 31.10  ? 155 LEU A O   1 
ATOM   991  C CB  . LEU A 1 126 ? 19.150  -15.783 -5.390  1.00 27.71  ? 155 LEU A CB  1 
ATOM   992  C CG  . LEU A 1 126 ? 19.777  -14.399 -5.200  1.00 26.71  ? 155 LEU A CG  1 
ATOM   993  C CD1 . LEU A 1 126 ? 20.984  -14.219 -6.061  1.00 27.77  ? 155 LEU A CD1 1 
ATOM   994  C CD2 . LEU A 1 126 ? 18.712  -13.358 -5.505  1.00 34.07  ? 155 LEU A CD2 1 
ATOM   995  N N   . ASP A 1 127 ? 18.071  -18.651 -4.748  1.00 28.53  ? 156 ASP A N   1 
ATOM   996  C CA  . ASP A 1 127 ? 17.431  -19.867 -5.225  1.00 31.08  ? 156 ASP A CA  1 
ATOM   997  C C   . ASP A 1 127 ? 16.221  -20.292 -4.388  1.00 32.46  ? 156 ASP A C   1 
ATOM   998  O O   . ASP A 1 127 ? 15.400  -21.072 -4.868  1.00 34.21  ? 156 ASP A O   1 
ATOM   999  C CB  . ASP A 1 127 ? 18.400  -21.042 -5.283  1.00 33.18  ? 156 ASP A CB  1 
ATOM   1000 C CG  . ASP A 1 127 ? 19.595  -20.934 -6.219  1.00 32.77  ? 156 ASP A CG  1 
ATOM   1001 O OD1 . ASP A 1 127 ? 19.544  -20.177 -7.204  1.00 32.32  ? 156 ASP A OD1 1 
ATOM   1002 O OD2 . ASP A 1 127 ? 20.577  -21.646 -5.960  1.00 39.01  ? 156 ASP A OD2 1 
ATOM   1003 N N   . ASN A 1 128 ? 16.076  -19.799 -3.150  1.00 32.39  ? 157 ASN A N   1 
ATOM   1004 C CA  . ASN A 1 128 ? 14.925  -20.164 -2.347  1.00 34.88  ? 157 ASN A CA  1 
ATOM   1005 C C   . ASN A 1 128 ? 13.833  -19.092 -2.430  1.00 34.68  ? 157 ASN A C   1 
ATOM   1006 O O   . ASN A 1 128 ? 12.713  -19.333 -2.001  1.00 35.88  ? 157 ASN A O   1 
ATOM   1007 C CB  . ASN A 1 128 ? 15.305  -20.455 -0.899  1.00 37.18  ? 157 ASN A CB  1 
ATOM   1008 C CG  . ASN A 1 128 ? 16.068  -21.750 -0.708  1.00 43.94  ? 157 ASN A CG  1 
ATOM   1009 O OD1 . ASN A 1 128 ? 16.077  -22.635 -1.573  1.00 45.63  ? 157 ASN A OD1 1 
ATOM   1010 N ND2 . ASN A 1 128 ? 16.747  -21.867 0.420   1.00 47.11  ? 157 ASN A ND2 1 
ATOM   1011 N N   . PHE A 1 129 ? 14.135  -17.915 -2.975  1.00 31.13  ? 158 PHE A N   1 
ATOM   1012 C CA  . PHE A 1 129 ? 13.119  -16.885 -3.076  1.00 33.07  ? 158 PHE A CA  1 
ATOM   1013 C C   . PHE A 1 129 ? 11.922  -17.394 -3.888  1.00 35.10  ? 158 PHE A C   1 
ATOM   1014 O O   . PHE A 1 129 ? 12.081  -17.851 -5.020  1.00 31.87  ? 158 PHE A O   1 
ATOM   1015 C CB  . PHE A 1 129 ? 13.621  -15.622 -3.773  1.00 30.47  ? 158 PHE A CB  1 
ATOM   1016 C CG  . PHE A 1 129 ? 14.412  -14.652 -2.910  1.00 28.67  ? 158 PHE A CG  1 
ATOM   1017 C CD1 . PHE A 1 129 ? 14.167  -14.544 -1.542  1.00 26.56  ? 158 PHE A CD1 1 
ATOM   1018 C CD2 . PHE A 1 129 ? 15.367  -13.827 -3.485  1.00 26.50  ? 158 PHE A CD2 1 
ATOM   1019 C CE1 . PHE A 1 129 ? 14.864  -13.610 -0.783  1.00 28.12  ? 158 PHE A CE1 1 
ATOM   1020 C CE2 . PHE A 1 129 ? 16.090  -12.926 -2.710  1.00 23.85  ? 158 PHE A CE2 1 
ATOM   1021 C CZ  . PHE A 1 129 ? 15.817  -12.823 -1.364  1.00 23.69  ? 158 PHE A CZ  1 
ATOM   1022 N N   . PRO A 1 130 ? 10.684  -17.166 -3.396  1.00 35.04  ? 159 PRO A N   1 
ATOM   1023 C CA  . PRO A 1 130 ? 9.464   -17.562 -4.111  1.00 32.80  ? 159 PRO A CA  1 
ATOM   1024 C C   . PRO A 1 130 ? 9.220   -16.698 -5.342  1.00 33.86  ? 159 PRO A C   1 
ATOM   1025 O O   . PRO A 1 130 ? 9.754   -15.595 -5.433  1.00 30.35  ? 159 PRO A O   1 
ATOM   1026 C CB  . PRO A 1 130 ? 8.373   -17.330 -3.049  1.00 31.41  ? 159 PRO A CB  1 
ATOM   1027 C CG  . PRO A 1 130 ? 8.890   -16.132 -2.264  1.00 30.55  ? 159 PRO A CG  1 
ATOM   1028 C CD  . PRO A 1 130 ? 10.398  -16.391 -2.178  1.00 31.58  ? 159 PRO A CD  1 
ATOM   1029 N N   . THR A 1 131 ? 8.326   -17.155 -6.237  1.00 31.28  ? 160 THR A N   1 
ATOM   1030 C CA  . THR A 1 131 ? 8.146   -16.482 -7.509  1.00 31.52  ? 160 THR A CA  1 
ATOM   1031 C C   . THR A 1 131 ? 7.229   -15.265 -7.355  1.00 30.17  ? 160 THR A C   1 
ATOM   1032 O O   . THR A 1 131 ? 7.160   -14.438 -8.248  1.00 31.99  ? 160 THR A O   1 
ATOM   1033 C CB  . THR A 1 131 ? 7.660   -17.491 -8.551  1.00 37.61  ? 160 THR A CB  1 
ATOM   1034 O OG1 . THR A 1 131 ? 6.412   -17.981 -8.077  1.00 36.03  ? 160 THR A OG1 1 
ATOM   1035 C CG2 . THR A 1 131 ? 8.627   -18.645 -8.747  1.00 40.65  ? 160 THR A CG2 1 
ATOM   1036 N N   . ASN A 1 132 ? 6.568   -15.094 -6.204  1.00 30.91  ? 161 ASN A N   1 
ATOM   1037 C CA  . ASN A 1 132 ? 5.760   -13.908 -5.967  1.00 33.29  ? 161 ASN A CA  1 
ATOM   1038 C C   . ASN A 1 132 ? 6.573   -12.804 -5.263  1.00 35.03  ? 161 ASN A C   1 
ATOM   1039 O O   . ASN A 1 132 ? 6.004   -11.799 -4.840  1.00 35.58  ? 161 ASN A O   1 
ATOM   1040 C CB  . ASN A 1 132 ? 4.525   -14.265 -5.137  1.00 36.13  ? 161 ASN A CB  1 
ATOM   1041 C CG  . ASN A 1 132 ? 4.874   -14.766 -3.754  1.00 39.25  ? 161 ASN A CG  1 
ATOM   1042 O OD1 . ASN A 1 132 ? 5.870   -15.475 -3.581  1.00 47.46  ? 161 ASN A OD1 1 
ATOM   1043 N ND2 . ASN A 1 132 ? 4.116   -14.387 -2.741  1.00 40.63  ? 161 ASN A ND2 1 
ATOM   1044 N N   . LEU A 1 133 ? 7.878   -13.007 -5.038  1.00 27.64  ? 162 LEU A N   1 
ATOM   1045 C CA  . LEU A 1 133 ? 8.699   -11.923 -4.510  1.00 26.05  ? 162 LEU A CA  1 
ATOM   1046 C C   . LEU A 1 133 ? 9.282   -11.180 -5.705  1.00 23.86  ? 162 LEU A C   1 
ATOM   1047 O O   . LEU A 1 133 ? 10.063  -11.728 -6.462  1.00 24.15  ? 162 LEU A O   1 
ATOM   1048 C CB  . LEU A 1 133 ? 9.772   -12.449 -3.567  1.00 25.88  ? 162 LEU A CB  1 
ATOM   1049 C CG  . LEU A 1 133 ? 10.713  -11.409 -2.957  1.00 27.83  ? 162 LEU A CG  1 
ATOM   1050 C CD1 . LEU A 1 133 ? 9.923   -10.421 -2.132  1.00 27.94  ? 162 LEU A CD1 1 
ATOM   1051 C CD2 . LEU A 1 133 ? 11.759  -12.099 -2.099  1.00 27.72  ? 162 LEU A CD2 1 
ATOM   1052 N N   . HIS A 1 134 ? 8.839   -9.937  -5.855  1.00 25.58  ? 163 HIS A N   1 
ATOM   1053 C CA  . HIS A 1 134 ? 9.240   -9.047  -6.924  1.00 25.57  ? 163 HIS A CA  1 
ATOM   1054 C C   . HIS A 1 134 ? 10.762  -9.039  -7.083  1.00 24.15  ? 163 HIS A C   1 
ATOM   1055 O O   . HIS A 1 134 ? 11.500  -9.023  -6.080  1.00 22.08  ? 163 HIS A O   1 
ATOM   1056 C CB  . HIS A 1 134 ? 8.649   -7.666  -6.622  1.00 27.73  ? 163 HIS A CB  1 
ATOM   1057 C CG  . HIS A 1 134 ? 8.852   -6.618  -7.673  1.00 35.73  ? 163 HIS A CG  1 
ATOM   1058 N ND1 . HIS A 1 134 ? 10.079  -6.202  -8.154  1.00 34.78  ? 163 HIS A ND1 1 
ATOM   1059 C CD2 . HIS A 1 134 ? 7.937   -5.825  -8.269  1.00 38.05  ? 163 HIS A CD2 1 
ATOM   1060 C CE1 . HIS A 1 134 ? 9.907   -5.259  -9.064  1.00 37.42  ? 163 HIS A CE1 1 
ATOM   1061 N NE2 . HIS A 1 134 ? 8.612   -4.993  -9.121  1.00 40.65  ? 163 HIS A NE2 1 
ATOM   1062 N N   . PRO A 1 135 ? 11.247  -8.989  -8.340  1.00 22.76  ? 164 PRO A N   1 
ATOM   1063 C CA  . PRO A 1 135 ? 12.672  -8.947  -8.651  1.00 26.42  ? 164 PRO A CA  1 
ATOM   1064 C C   . PRO A 1 135 ? 13.477  -7.840  -7.963  1.00 24.13  ? 164 PRO A C   1 
ATOM   1065 O O   . PRO A 1 135 ? 14.588  -8.101  -7.553  1.00 23.37  ? 164 PRO A O   1 
ATOM   1066 C CB  . PRO A 1 135 ? 12.723  -8.779  -10.185 1.00 26.94  ? 164 PRO A CB  1 
ATOM   1067 C CG  . PRO A 1 135 ? 11.379  -9.158  -10.673 1.00 26.30  ? 164 PRO A CG  1 
ATOM   1068 C CD  . PRO A 1 135 ? 10.411  -9.024  -9.550  1.00 25.20  ? 164 PRO A CD  1 
ATOM   1069 N N   . MET A 1 136 ? 12.924  -6.629  -7.811  1.00 22.15  ? 165 MET A N   1 
ATOM   1070 C CA  . MET A 1 136 ? 13.610  -5.547  -7.101  1.00 24.49  ? 165 MET A CA  1 
ATOM   1071 C C   . MET A 1 136 ? 13.785  -5.854  -5.604  1.00 23.38  ? 165 MET A C   1 
ATOM   1072 O O   . MET A 1 136 ? 14.744  -5.383  -4.992  1.00 24.96  ? 165 MET A O   1 
ATOM   1073 C CB  . MET A 1 136 ? 12.878  -4.207  -7.297  1.00 24.33  ? 165 MET A CB  1 
ATOM   1074 C CG  . MET A 1 136 ? 13.134  -3.603  -8.666  1.00 24.34  ? 165 MET A CG  1 
ATOM   1075 S SD  . MET A 1 136 ? 14.849  -3.163  -9.028  1.00 25.75  ? 165 MET A SD  1 
ATOM   1076 C CE  . MET A 1 136 ? 15.103  -1.776  -7.923  1.00 27.56  ? 165 MET A CE  1 
ATOM   1077 N N   . SER A 1 137 ? 12.839  -6.598  -5.020  1.00 20.49  ? 166 SER A N   1 
ATOM   1078 C CA  . SER A 1 137 ? 12.903  -7.034  -3.635  1.00 23.43  ? 166 SER A CA  1 
ATOM   1079 C C   . SER A 1 137 ? 13.992  -8.081  -3.444  1.00 22.19  ? 166 SER A C   1 
ATOM   1080 O O   . SER A 1 137 ? 14.804  -7.951  -2.518  1.00 22.11  ? 166 SER A O   1 
ATOM   1081 C CB  . SER A 1 137 ? 11.588  -7.522  -3.123  1.00 22.38  ? 166 SER A CB  1 
ATOM   1082 O OG  . SER A 1 137 ? 10.591  -6.506  -3.238  1.00 26.05  ? 166 SER A OG  1 
ATOM   1083 N N   . GLN A 1 138 ? 14.043  -9.061  -4.358  1.00 20.57  ? 167 GLN A N   1 
ATOM   1084 C CA  . GLN A 1 138 ? 15.154  -10.003 -4.410  1.00 20.98  ? 167 GLN A CA  1 
ATOM   1085 C C   . GLN A 1 138 ? 16.481  -9.251  -4.547  1.00 19.36  ? 167 GLN A C   1 
ATOM   1086 O O   . GLN A 1 138 ? 17.453  -9.591  -3.898  1.00 19.60  ? 167 GLN A O   1 
ATOM   1087 C CB  . GLN A 1 138 ? 14.938  -10.992 -5.550  1.00 19.83  ? 167 GLN A CB  1 
ATOM   1088 C CG  . GLN A 1 138 ? 13.575  -11.679 -5.506  1.00 23.64  ? 167 GLN A CG  1 
ATOM   1089 C CD  . GLN A 1 138 ? 13.543  -12.947 -6.342  1.00 26.39  ? 167 GLN A CD  1 
ATOM   1090 O OE1 . GLN A 1 138 ? 14.601  -13.497 -6.647  1.00 23.02  ? 167 GLN A OE1 1 
ATOM   1091 N NE2 . GLN A 1 138 ? 12.356  -13.441 -6.677  1.00 26.08  ? 167 GLN A NE2 1 
ATOM   1092 N N   . LEU A 1 139 ? 16.539  -8.257  -5.434  1.00 21.21  ? 168 LEU A N   1 
ATOM   1093 C CA  . LEU A 1 139 ? 17.786  -7.558  -5.703  1.00 19.21  ? 168 LEU A CA  1 
ATOM   1094 C C   . LEU A 1 139 ? 18.281  -6.861  -4.431  1.00 20.30  ? 168 LEU A C   1 
ATOM   1095 O O   . LEU A 1 139 ? 19.427  -7.062  -4.042  1.00 21.33  ? 168 LEU A O   1 
ATOM   1096 C CB  . LEU A 1 139 ? 17.657  -6.562  -6.837  1.00 19.23  ? 168 LEU A CB  1 
ATOM   1097 C CG  . LEU A 1 139 ? 18.877  -5.682  -7.073  1.00 20.23  ? 168 LEU A CG  1 
ATOM   1098 C CD1 . LEU A 1 139 ? 19.947  -6.483  -7.707  1.00 19.51  ? 168 LEU A CD1 1 
ATOM   1099 C CD2 . LEU A 1 139 ? 18.484  -4.517  -7.926  1.00 22.52  ? 168 LEU A CD2 1 
ATOM   1100 N N   . SER A 1 140 ? 17.383  -6.153  -3.745  1.00 20.86  ? 169 SER A N   1 
ATOM   1101 C CA  . SER A 1 140 ? 17.720  -5.373  -2.571  1.00 19.77  ? 169 SER A CA  1 
ATOM   1102 C C   . SER A 1 140 ? 18.145  -6.287  -1.437  1.00 17.94  ? 169 SER A C   1 
ATOM   1103 O O   . SER A 1 140 ? 19.157  -6.028  -0.789  1.00 19.52  ? 169 SER A O   1 
ATOM   1104 C CB  . SER A 1 140 ? 16.611  -4.407  -2.138  1.00 19.01  ? 169 SER A CB  1 
ATOM   1105 O OG  . SER A 1 140 ? 17.005  -3.772  -0.910  1.00 24.06  ? 169 SER A OG  1 
ATOM   1106 N N   . ALA A 1 141 ? 17.372  -7.345  -1.212  1.00 18.47  ? 170 ALA A N   1 
ATOM   1107 C CA  . ALA A 1 141 ? 17.637  -8.301  -0.157  1.00 18.32  ? 170 ALA A CA  1 
ATOM   1108 C C   . ALA A 1 141 ? 18.973  -9.008  -0.382  1.00 19.42  ? 170 ALA A C   1 
ATOM   1109 O O   . ALA A 1 141 ? 19.683  -9.231  0.595   1.00 19.22  ? 170 ALA A O   1 
ATOM   1110 C CB  . ALA A 1 141 ? 16.526  -9.313  -0.030  1.00 20.57  ? 170 ALA A CB  1 
ATOM   1111 N N   . ALA A 1 142 ? 19.258  -9.418  -1.626  1.00 18.90  ? 171 ALA A N   1 
ATOM   1112 C CA  . ALA A 1 142 ? 20.510  -10.091 -1.955  1.00 20.91  ? 171 ALA A CA  1 
ATOM   1113 C C   . ALA A 1 142 ? 21.683  -9.148  -1.746  1.00 21.55  ? 171 ALA A C   1 
ATOM   1114 O O   . ALA A 1 142 ? 22.708  -9.551  -1.199  1.00 22.76  ? 171 ALA A O   1 
ATOM   1115 C CB  . ALA A 1 142 ? 20.475  -10.651 -3.352  1.00 23.75  ? 171 ALA A CB  1 
ATOM   1116 N N   . VAL A 1 143 ? 21.521  -7.868  -2.116  1.00 20.54  ? 172 VAL A N   1 
ATOM   1117 C CA  . VAL A 1 143 ? 22.608  -6.917  -1.952  1.00 19.42  ? 172 VAL A CA  1 
ATOM   1118 C C   . VAL A 1 143 ? 22.838  -6.631  -0.462  1.00 19.75  ? 172 VAL A C   1 
ATOM   1119 O O   . VAL A 1 143 ? 23.977  -6.573  -0.016  1.00 23.93  ? 172 VAL A O   1 
ATOM   1120 C CB  . VAL A 1 143 ? 22.388  -5.633  -2.764  1.00 21.40  ? 172 VAL A CB  1 
ATOM   1121 C CG1 . VAL A 1 143 ? 23.386  -4.564  -2.343  1.00 19.84  ? 172 VAL A CG1 1 
ATOM   1122 C CG2 . VAL A 1 143 ? 22.462  -5.868  -4.283  1.00 21.48  ? 172 VAL A CG2 1 
ATOM   1123 N N   . THR A 1 144 ? 21.776  -6.474  0.336   1.00 20.86  ? 173 THR A N   1 
ATOM   1124 C CA  . THR A 1 144 ? 21.923  -6.379  1.780   1.00 20.12  ? 173 THR A CA  1 
ATOM   1125 C C   . THR A 1 144 ? 22.707  -7.575  2.318   1.00 20.94  ? 173 THR A C   1 
ATOM   1126 O O   . THR A 1 144 ? 23.637  -7.356  3.089   1.00 18.74  ? 173 THR A O   1 
ATOM   1127 C CB  . THR A 1 144 ? 20.592  -6.223  2.501   1.00 20.49  ? 173 THR A CB  1 
ATOM   1128 O OG1 . THR A 1 144 ? 20.016  -5.047  1.929   1.00 20.45  ? 173 THR A OG1 1 
ATOM   1129 C CG2 . THR A 1 144 ? 20.756  -6.029  4.001   1.00 20.28  ? 173 THR A CG2 1 
ATOM   1130 N N   . ALA A 1 145 ? 22.373  -8.805  1.888   1.00 19.61  ? 174 ALA A N   1 
ATOM   1131 C CA  . ALA A 1 145 ? 23.039  -9.998  2.402   1.00 21.70  ? 174 ALA A CA  1 
ATOM   1132 C C   . ALA A 1 145 ? 24.520  -10.125 2.021   1.00 23.41  ? 174 ALA A C   1 
ATOM   1133 O O   . ALA A 1 145 ? 25.287  -10.880 2.663   1.00 23.04  ? 174 ALA A O   1 
ATOM   1134 C CB  . ALA A 1 145 ? 22.292  -11.244 1.952   1.00 23.61  ? 174 ALA A CB  1 
ATOM   1135 N N   . LEU A 1 146 ? 24.902  -9.484  0.917   1.00 22.42  ? 175 LEU A N   1 
ATOM   1136 C CA  . LEU A 1 146 ? 26.287  -9.454  0.478   1.00 22.96  ? 175 LEU A CA  1 
ATOM   1137 C C   . LEU A 1 146 ? 27.134  -8.605  1.435   1.00 23.23  ? 175 LEU A C   1 
ATOM   1138 O O   . LEU A 1 146 ? 28.356  -8.616  1.372   1.00 23.56  ? 175 LEU A O   1 
ATOM   1139 C CB  . LEU A 1 146 ? 26.359  -8.901  -0.943  1.00 23.82  ? 175 LEU A CB  1 
ATOM   1140 C CG  . LEU A 1 146 ? 26.109  -9.873  -2.100  1.00 22.36  ? 175 LEU A CG  1 
ATOM   1141 C CD1 . LEU A 1 146 ? 25.957  -9.101  -3.390  1.00 24.41  ? 175 LEU A CD1 1 
ATOM   1142 C CD2 . LEU A 1 146 ? 27.307  -10.795 -2.183  1.00 23.98  ? 175 LEU A CD2 1 
ATOM   1143 N N   . ASN A 1 147 ? 26.522  -7.850  2.343   1.00 21.51  ? 176 ASN A N   1 
ATOM   1144 C CA  . ASN A 1 147 ? 27.333  -6.911  3.109   1.00 23.60  ? 176 ASN A CA  1 
ATOM   1145 C C   . ASN A 1 147 ? 28.179  -7.683  4.117   1.00 25.32  ? 176 ASN A C   1 
ATOM   1146 O O   . ASN A 1 147 ? 29.029  -7.103  4.793   1.00 21.47  ? 176 ASN A O   1 
ATOM   1147 C CB  . ASN A 1 147 ? 26.539  -5.785  3.774   1.00 24.93  ? 176 ASN A CB  1 
ATOM   1148 C CG  . ASN A 1 147 ? 26.534  -5.888  5.276   1.00 28.82  ? 176 ASN A CG  1 
ATOM   1149 O OD1 . ASN A 1 147 ? 26.190  -6.948  5.796   1.00 29.12  ? 176 ASN A OD1 1 
ATOM   1150 N ND2 . ASN A 1 147 ? 26.919  -4.824  5.980   1.00 24.04  ? 176 ASN A ND2 1 
ATOM   1151 N N   . SER A 1 148 ? 27.970  -9.010  4.172   1.00 28.21  ? 177 SER A N   1 
ATOM   1152 C CA  . SER A 1 148 ? 28.869  -9.898  4.874   1.00 24.43  ? 177 SER A CA  1 
ATOM   1153 C C   . SER A 1 148 ? 30.254  -9.845  4.238   1.00 25.78  ? 177 SER A C   1 
ATOM   1154 O O   . SER A 1 148 ? 31.237  -10.161 4.902   1.00 28.58  ? 177 SER A O   1 
ATOM   1155 C CB  . SER A 1 148 ? 28.333  -11.289 4.845   1.00 22.94  ? 177 SER A CB  1 
ATOM   1156 O OG  . SER A 1 148 ? 28.231  -11.701 3.502   1.00 26.40  ? 177 SER A OG  1 
ATOM   1157 N N   . GLU A 1 149 ? 30.332  -9.483  2.952   1.00 23.85  ? 178 GLU A N   1 
ATOM   1158 C CA  . GLU A 1 149 ? 31.620  -9.357  2.285   1.00 27.58  ? 178 GLU A CA  1 
ATOM   1159 C C   . GLU A 1 149 ? 32.263  -7.982  2.513   1.00 24.75  ? 178 GLU A C   1 
ATOM   1160 O O   . GLU A 1 149 ? 33.299  -7.701  1.916   1.00 25.58  ? 178 GLU A O   1 
ATOM   1161 C CB  . GLU A 1 149 ? 31.496  -9.536  0.768   1.00 32.53  ? 178 GLU A CB  1 
ATOM   1162 C CG  . GLU A 1 149 ? 30.646  -10.748 0.375   1.00 39.71  ? 178 GLU A CG  1 
ATOM   1163 C CD  . GLU A 1 149 ? 31.356  -12.080 0.561   1.00 46.58  ? 178 GLU A CD  1 
ATOM   1164 O OE1 . GLU A 1 149 ? 31.693  -12.673 -0.491  1.00 47.82  ? 178 GLU A OE1 1 
ATOM   1165 O OE2 . GLU A 1 149 ? 31.561  -12.529 1.719   1.00 47.65  ? 178 GLU A OE2 1 
ATOM   1166 N N   . SER A 1 150 ? 31.623  -7.081  3.264   1.00 23.98  ? 179 SER A N   1 
ATOM   1167 C CA  . SER A 1 150 ? 32.054  -5.682  3.293   1.00 24.31  ? 179 SER A CA  1 
ATOM   1168 C C   . SER A 1 150 ? 33.417  -5.520  3.954   1.00 25.95  ? 179 SER A C   1 
ATOM   1169 O O   . SER A 1 150 ? 33.521  -5.650  5.164   1.00 27.24  ? 179 SER A O   1 
ATOM   1170 C CB  . SER A 1 150 ? 31.083  -4.731  3.965   1.00 20.96  ? 179 SER A CB  1 
ATOM   1171 O OG  . SER A 1 150 ? 31.658  -3.428  3.896   1.00 21.73  ? 179 SER A OG  1 
ATOM   1172 N N   . ASN A 1 151 ? 34.420  -5.116  3.161   1.00 25.94  ? 180 ASN A N   1 
ATOM   1173 C CA  . ASN A 1 151 ? 35.724  -4.714  3.672   1.00 32.05  ? 180 ASN A CA  1 
ATOM   1174 C C   . ASN A 1 151 ? 35.616  -3.440  4.512   1.00 29.18  ? 180 ASN A C   1 
ATOM   1175 O O   . ASN A 1 151 ? 36.354  -3.252  5.470   1.00 28.15  ? 180 ASN A O   1 
ATOM   1176 C CB  . ASN A 1 151 ? 36.732  -4.421  2.554   1.00 38.34  ? 180 ASN A CB  1 
ATOM   1177 C CG  . ASN A 1 151 ? 36.884  -5.552  1.560   1.00 43.06  ? 180 ASN A CG  1 
ATOM   1178 O OD1 . ASN A 1 151 ? 36.722  -5.352  0.345   1.00 51.48  ? 180 ASN A OD1 1 
ATOM   1179 N ND2 . ASN A 1 151 ? 37.171  -6.746  2.053   1.00 42.13  ? 180 ASN A ND2 1 
ATOM   1180 N N   . PHE A 1 152 ? 34.757  -2.514  4.086   1.00 26.05  ? 181 PHE A N   1 
ATOM   1181 C CA  . PHE A 1 152 ? 34.641  -1.228  4.747   1.00 25.81  ? 181 PHE A CA  1 
ATOM   1182 C C   . PHE A 1 152 ? 34.055  -1.422  6.141   1.00 26.64  ? 181 PHE A C   1 
ATOM   1183 O O   . PHE A 1 152 ? 34.531  -0.837  7.107   1.00 24.35  ? 181 PHE A O   1 
ATOM   1184 C CB  . PHE A 1 152 ? 33.772  -0.217  4.013   1.00 22.15  ? 181 PHE A CB  1 
ATOM   1185 C CG  . PHE A 1 152 ? 33.644  1.056   4.828   1.00 23.00  ? 181 PHE A CG  1 
ATOM   1186 C CD1 . PHE A 1 152 ? 34.664  1.985   4.864   1.00 25.05  ? 181 PHE A CD1 1 
ATOM   1187 C CD2 . PHE A 1 152 ? 32.493  1.351   5.519   1.00 24.04  ? 181 PHE A CD2 1 
ATOM   1188 C CE1 . PHE A 1 152 ? 34.520  3.167   5.538   1.00 21.80  ? 181 PHE A CE1 1 
ATOM   1189 C CE2 . PHE A 1 152 ? 32.370  2.516   6.225   1.00 24.93  ? 181 PHE A CE2 1 
ATOM   1190 C CZ  . PHE A 1 152 ? 33.394  3.427   6.240   1.00 24.37  ? 181 PHE A CZ  1 
ATOM   1191 N N   . ALA A 1 153 ? 33.021  -2.254  6.248   1.00 29.86  ? 182 ALA A N   1 
ATOM   1192 C CA  . ALA A 1 153 ? 32.390  -2.476  7.545   1.00 27.91  ? 182 ALA A CA  1 
ATOM   1193 C C   . ALA A 1 153 ? 33.412  -3.031  8.563   1.00 32.23  ? 182 ALA A C   1 
ATOM   1194 O O   . ALA A 1 153 ? 33.429  -2.625  9.727   1.00 30.56  ? 182 ALA A O   1 
ATOM   1195 C CB  . ALA A 1 153 ? 31.161  -3.369  7.371   1.00 25.76  ? 182 ALA A CB  1 
ATOM   1196 N N   . ARG A 1 154 ? 34.297  -3.935  8.123   1.00 34.96  ? 183 ARG A N   1 
ATOM   1197 C CA  . ARG A 1 154 ? 35.246  -4.569  9.032   1.00 36.46  ? 183 ARG A CA  1 
ATOM   1198 C C   . ARG A 1 154 ? 36.378  -3.592  9.353   1.00 34.09  ? 183 ARG A C   1 
ATOM   1199 O O   . ARG A 1 154 ? 36.804  -3.472  10.497  1.00 31.33  ? 183 ARG A O   1 
ATOM   1200 C CB  . ARG A 1 154 ? 35.776  -5.908  8.501   1.00 44.71  ? 183 ARG A CB  1 
ATOM   1201 C CG  . ARG A 1 154 ? 34.841  -7.084  8.765   1.00 53.03  ? 183 ARG A CG  1 
ATOM   1202 C CD  . ARG A 1 154 ? 35.428  -8.472  8.422   1.00 61.03  ? 183 ARG A CD  1 
ATOM   1203 N NE  . ARG A 1 154 ? 35.766  -8.720  7.011   1.00 65.28  ? 183 ARG A NE  1 
ATOM   1204 C CZ  . ARG A 1 154 ? 34.892  -8.908  6.017   1.00 69.01  ? 183 ARG A CZ  1 
ATOM   1205 N NH1 . ARG A 1 154 ? 35.300  -9.196  4.785   1.00 64.97  ? 183 ARG A NH1 1 
ATOM   1206 N NH2 . ARG A 1 154 ? 33.598  -8.820  6.271   1.00 68.19  ? 183 ARG A NH2 1 
ATOM   1207 N N   . ALA A 1 155 ? 36.841  -2.839  8.358   1.00 31.90  ? 184 ALA A N   1 
ATOM   1208 C CA  . ALA A 1 155 ? 37.845  -1.815  8.633   1.00 28.07  ? 184 ALA A CA  1 
ATOM   1209 C C   . ALA A 1 155 ? 37.339  -0.813  9.662   1.00 29.12  ? 184 ALA A C   1 
ATOM   1210 O O   . ALA A 1 155 ? 38.110  -0.308  10.485  1.00 32.24  ? 184 ALA A O   1 
ATOM   1211 C CB  . ALA A 1 155 ? 38.244  -1.096  7.362   1.00 25.23  ? 184 ALA A CB  1 
ATOM   1212 N N   . TYR A 1 156 ? 36.051  -0.452  9.603   1.00 29.54  ? 185 TYR A N   1 
ATOM   1213 C CA  . TYR A 1 156 ? 35.619  0.683   10.401  1.00 28.05  ? 185 TYR A CA  1 
ATOM   1214 C C   . TYR A 1 156 ? 35.590  0.282   11.874  1.00 30.48  ? 185 TYR A C   1 
ATOM   1215 O O   . TYR A 1 156 ? 36.028  1.033   12.746  1.00 32.57  ? 185 TYR A O   1 
ATOM   1216 C CB  . TYR A 1 156 ? 34.272  1.217   9.934   1.00 28.61  ? 185 TYR A CB  1 
ATOM   1217 C CG  . TYR A 1 156 ? 33.829  2.432   10.712  1.00 27.56  ? 185 TYR A CG  1 
ATOM   1218 C CD1 . TYR A 1 156 ? 33.167  2.303   11.931  1.00 28.19  ? 185 TYR A CD1 1 
ATOM   1219 C CD2 . TYR A 1 156 ? 34.090  3.708   10.230  1.00 28.79  ? 185 TYR A CD2 1 
ATOM   1220 C CE1 . TYR A 1 156 ? 32.812  3.428   12.657  1.00 32.51  ? 185 TYR A CE1 1 
ATOM   1221 C CE2 . TYR A 1 156 ? 33.733  4.837   10.943  1.00 27.97  ? 185 TYR A CE2 1 
ATOM   1222 C CZ  . TYR A 1 156 ? 33.069  4.692   12.144  1.00 29.83  ? 185 TYR A CZ  1 
ATOM   1223 O OH  . TYR A 1 156 ? 32.692  5.819   12.803  1.00 41.15  ? 185 TYR A OH  1 
ATOM   1224 N N   . ALA A 1 157 ? 35.105  -0.929  12.134  1.00 35.21  ? 186 ALA A N   1 
ATOM   1225 C CA  . ALA A 1 157 ? 35.098  -1.487  13.477  1.00 38.21  ? 186 ALA A CA  1 
ATOM   1226 C C   . ALA A 1 157 ? 36.506  -1.547  14.090  1.00 39.80  ? 186 ALA A C   1 
ATOM   1227 O O   . ALA A 1 157 ? 36.642  -1.419  15.304  1.00 36.80  ? 186 ALA A O   1 
ATOM   1228 C CB  . ALA A 1 157 ? 34.446  -2.861  13.436  1.00 39.85  ? 186 ALA A CB  1 
ATOM   1229 N N   . GLN A 1 158 ? 37.564  -1.749  13.283  1.00 37.89  ? 187 GLN A N   1 
ATOM   1230 C CA  . GLN A 1 158 ? 38.920  -1.798  13.825  1.00 37.49  ? 187 GLN A CA  1 
ATOM   1231 C C   . GLN A 1 158 ? 39.618  -0.431  13.841  1.00 38.63  ? 187 GLN A C   1 
ATOM   1232 O O   . GLN A 1 158 ? 40.795  -0.348  14.138  1.00 38.43  ? 187 GLN A O   1 
ATOM   1233 C CB  . GLN A 1 158 ? 39.810  -2.728  13.014  1.00 42.52  ? 187 GLN A CB  1 
ATOM   1234 C CG  . GLN A 1 158 ? 39.273  -4.143  12.847  1.00 41.59  ? 187 GLN A CG  1 
ATOM   1235 C CD  . GLN A 1 158 ? 40.060  -4.886  11.795  1.00 49.01  ? 187 GLN A CD  1 
ATOM   1236 O OE1 . GLN A 1 158 ? 40.564  -4.290  10.838  1.00 53.98  ? 187 GLN A OE1 1 
ATOM   1237 N NE2 . GLN A 1 158 ? 40.205  -6.190  11.974  1.00 56.36  ? 187 GLN A NE2 1 
ATOM   1238 N N   . GLY A 1 159 ? 38.930  0.653   13.493  1.00 35.75  ? 188 GLY A N   1 
ATOM   1239 C CA  . GLY A 1 159 ? 39.389  1.987   13.841  1.00 38.35  ? 188 GLY A CA  1 
ATOM   1240 C C   . GLY A 1 159 ? 40.283  2.621   12.777  1.00 39.24  ? 188 GLY A C   1 
ATOM   1241 O O   . GLY A 1 159 ? 41.151  3.429   13.110  1.00 44.30  ? 188 GLY A O   1 
ATOM   1242 N N   . ILE A 1 160 ? 39.994  2.360   11.501  1.00 32.80  ? 189 ILE A N   1 
ATOM   1243 C CA  . ILE A 1 160 ? 40.780  2.916   10.417  1.00 33.95  ? 189 ILE A CA  1 
ATOM   1244 C C   . ILE A 1 160 ? 40.675  4.451   10.384  1.00 33.45  ? 189 ILE A C   1 
ATOM   1245 O O   . ILE A 1 160 ? 39.662  5.048   10.761  1.00 28.36  ? 189 ILE A O   1 
ATOM   1246 C CB  . ILE A 1 160 ? 40.355  2.235   9.107   1.00 39.17  ? 189 ILE A CB  1 
ATOM   1247 C CG1 . ILE A 1 160 ? 41.378  2.436   7.952   1.00 49.10  ? 189 ILE A CG1 1 
ATOM   1248 C CG2 . ILE A 1 160 ? 38.945  2.657   8.695   1.00 37.03  ? 189 ILE A CG2 1 
ATOM   1249 C CD1 . ILE A 1 160 ? 42.463  1.372   7.852   1.00 53.70  ? 189 ILE A CD1 1 
ATOM   1250 N N   . SER A 1 161 ? 41.765  5.098   9.950   1.00 28.21  ? 190 SER A N   1 
ATOM   1251 C CA  . SER A 1 161 ? 41.814  6.541   9.764   1.00 30.30  ? 190 SER A CA  1 
ATOM   1252 C C   . SER A 1 161 ? 40.759  6.998   8.756   1.00 27.56  ? 190 SER A C   1 
ATOM   1253 O O   . SER A 1 161 ? 40.610  6.394   7.702   1.00 26.17  ? 190 SER A O   1 
ATOM   1254 C CB  . SER A 1 161 ? 43.209  6.971   9.325   1.00 31.02  ? 190 SER A CB  1 
ATOM   1255 O OG  . SER A 1 161 ? 43.194  8.249   8.700   1.00 29.85  ? 190 SER A OG  1 
ATOM   1256 N N   . ARG A 1 162 ? 40.050  8.089   9.073   1.00 27.50  ? 191 ARG A N   1 
ATOM   1257 C CA  . ARG A 1 162 ? 39.141  8.763   8.156   1.00 31.29  ? 191 ARG A CA  1 
ATOM   1258 C C   . ARG A 1 162 ? 39.757  9.023   6.773   1.00 32.65  ? 191 ARG A C   1 
ATOM   1259 O O   . ARG A 1 162 ? 39.043  9.100   5.773   1.00 29.40  ? 191 ARG A O   1 
ATOM   1260 C CB  . ARG A 1 162 ? 38.791  10.148  8.710   1.00 42.05  ? 191 ARG A CB  1 
ATOM   1261 C CG  . ARG A 1 162 ? 37.799  10.207  9.858   1.00 53.34  ? 191 ARG A CG  1 
ATOM   1262 C CD  . ARG A 1 162 ? 37.916  11.535  10.592  1.00 67.00  ? 191 ARG A CD  1 
ATOM   1263 N NE  . ARG A 1 162 ? 37.010  11.580  11.749  1.00 83.38  ? 191 ARG A NE  1 
ATOM   1264 C CZ  . ARG A 1 162 ? 37.026  12.453  12.765  1.00 85.65  ? 191 ARG A CZ  1 
ATOM   1265 N NH1 . ARG A 1 162 ? 38.042  13.284  12.933  1.00 79.10  ? 191 ARG A NH1 1 
ATOM   1266 N NH2 . ARG A 1 162 ? 36.028  12.461  13.639  1.00 89.46  ? 191 ARG A NH2 1 
ATOM   1267 N N   . THR A 1 163 ? 41.086  9.217   6.725   1.00 28.61  ? 192 THR A N   1 
ATOM   1268 C CA  . THR A 1 163 ? 41.783  9.509   5.488   1.00 27.94  ? 192 THR A CA  1 
ATOM   1269 C C   . THR A 1 163 ? 41.763  8.285   4.575   1.00 26.70  ? 192 THR A C   1 
ATOM   1270 O O   . THR A 1 163 ? 42.065  8.395   3.394   1.00 28.85  ? 192 THR A O   1 
ATOM   1271 C CB  . THR A 1 163 ? 43.210  9.991   5.784   1.00 26.39  ? 192 THR A CB  1 
ATOM   1272 O OG1 . THR A 1 163 ? 43.948  8.845   6.184   1.00 22.95  ? 192 THR A OG1 1 
ATOM   1273 C CG2 . THR A 1 163 ? 43.194  11.094  6.823   1.00 25.42  ? 192 THR A CG2 1 
ATOM   1274 N N   . LYS A 1 164 ? 41.420  7.122   5.110   1.00 26.60  ? 193 LYS A N   1 
ATOM   1275 C CA  . LYS A 1 164 ? 41.414  5.914   4.296   1.00 29.63  ? 193 LYS A CA  1 
ATOM   1276 C C   . LYS A 1 164 ? 40.004  5.409   3.985   1.00 23.93  ? 193 LYS A C   1 
ATOM   1277 O O   . LYS A 1 164 ? 39.851  4.387   3.330   1.00 22.51  ? 193 LYS A O   1 
ATOM   1278 C CB  . LYS A 1 164 ? 42.168  4.810   5.031   1.00 33.47  ? 193 LYS A CB  1 
ATOM   1279 C CG  . LYS A 1 164 ? 43.621  5.165   5.273   1.00 42.70  ? 193 LYS A CG  1 
ATOM   1280 C CD  . LYS A 1 164 ? 44.592  4.247   4.552   1.00 51.06  ? 193 LYS A CD  1 
ATOM   1281 C CE  . LYS A 1 164 ? 44.477  2.833   5.021   1.00 51.84  ? 193 LYS A CE  1 
ATOM   1282 N NZ  . LYS A 1 164 ? 45.550  2.085   4.377   1.00 56.48  ? 193 LYS A NZ  1 
ATOM   1283 N N   . TYR A 1 165 ? 38.959  6.126   4.374   1.00 21.77  ? 194 TYR A N   1 
ATOM   1284 C CA  . TYR A 1 165 ? 37.627  5.588   4.154   1.00 23.40  ? 194 TYR A CA  1 
ATOM   1285 C C   . TYR A 1 165 ? 37.449  5.255   2.678   1.00 24.02  ? 194 TYR A C   1 
ATOM   1286 O O   . TYR A 1 165 ? 37.008  4.161   2.339   1.00 23.60  ? 194 TYR A O   1 
ATOM   1287 C CB  . TYR A 1 165 ? 36.499  6.471   4.698   1.00 22.11  ? 194 TYR A CB  1 
ATOM   1288 C CG  . TYR A 1 165 ? 36.358  6.600   6.203   1.00 22.06  ? 194 TYR A CG  1 
ATOM   1289 C CD1 . TYR A 1 165 ? 36.957  5.727   7.106   1.00 26.13  ? 194 TYR A CD1 1 
ATOM   1290 C CD2 . TYR A 1 165 ? 35.592  7.632   6.726   1.00 22.29  ? 194 TYR A CD2 1 
ATOM   1291 C CE1 . TYR A 1 165 ? 36.816  5.895   8.478   1.00 27.93  ? 194 TYR A CE1 1 
ATOM   1292 C CE2 . TYR A 1 165 ? 35.438  7.807   8.082   1.00 24.32  ? 194 TYR A CE2 1 
ATOM   1293 C CZ  . TYR A 1 165 ? 36.020  6.927   8.959   1.00 27.78  ? 194 TYR A CZ  1 
ATOM   1294 O OH  . TYR A 1 165 ? 35.838  7.222   10.263  1.00 35.63  ? 194 TYR A OH  1 
ATOM   1295 N N   . TRP A 1 166 ? 37.844  6.177   1.798   1.00 23.46  ? 195 TRP A N   1 
ATOM   1296 C CA  . TRP A 1 166 ? 37.568  6.076   0.378   1.00 22.89  ? 195 TRP A CA  1 
ATOM   1297 C C   . TRP A 1 166 ? 38.123  4.769   -0.203  1.00 22.60  ? 195 TRP A C   1 
ATOM   1298 O O   . TRP A 1 166 ? 37.484  4.169   -1.065  1.00 21.79  ? 195 TRP A O   1 
ATOM   1299 C CB  . TRP A 1 166 ? 38.065  7.334   -0.363  1.00 22.52  ? 195 TRP A CB  1 
ATOM   1300 C CG  . TRP A 1 166 ? 39.558  7.418   -0.539  1.00 25.58  ? 195 TRP A CG  1 
ATOM   1301 C CD1 . TRP A 1 166 ? 40.463  8.080   0.246   1.00 26.70  ? 195 TRP A CD1 1 
ATOM   1302 C CD2 . TRP A 1 166 ? 40.320  6.827   -1.618  1.00 27.63  ? 195 TRP A CD2 1 
ATOM   1303 N NE1 . TRP A 1 166 ? 41.731  7.955   -0.277  1.00 30.65  ? 195 TRP A NE1 1 
ATOM   1304 C CE2 . TRP A 1 166 ? 41.679  7.166   -1.398  1.00 25.76  ? 195 TRP A CE2 1 
ATOM   1305 C CE3 . TRP A 1 166 ? 39.980  6.033   -2.726  1.00 25.74  ? 195 TRP A CE3 1 
ATOM   1306 C CZ2 . TRP A 1 166 ? 42.694  6.759   -2.262  1.00 27.46  ? 195 TRP A CZ2 1 
ATOM   1307 C CZ3 . TRP A 1 166 ? 40.989  5.610   -3.561  1.00 28.84  ? 195 TRP A CZ3 1 
ATOM   1308 C CH2 . TRP A 1 166 ? 42.324  5.972   -3.334  1.00 26.02  ? 195 TRP A CH2 1 
ATOM   1309 N N   . GLU A 1 167 ? 39.282  4.299   0.290   1.00 19.91  ? 196 GLU A N   1 
ATOM   1310 C CA  . GLU A 1 167 ? 39.920  3.105   -0.247  1.00 21.32  ? 196 GLU A CA  1 
ATOM   1311 C C   . GLU A 1 167 ? 39.054  1.879   0.003   1.00 20.29  ? 196 GLU A C   1 
ATOM   1312 O O   . GLU A 1 167 ? 38.906  1.034   -0.853  1.00 18.68  ? 196 GLU A O   1 
ATOM   1313 C CB  . GLU A 1 167 ? 41.351  2.870   0.254   1.00 25.74  ? 196 GLU A CB  1 
ATOM   1314 C CG  . GLU A 1 167 ? 42.256  4.077   0.059   1.00 28.41  ? 196 GLU A CG  1 
ATOM   1315 C CD  . GLU A 1 167 ? 43.628  3.947   0.692   1.00 36.52  ? 196 GLU A CD  1 
ATOM   1316 O OE1 . GLU A 1 167 ? 44.205  4.993   0.994   1.00 40.21  ? 196 GLU A OE1 1 
ATOM   1317 O OE2 . GLU A 1 167 ? 44.101  2.822   0.906   1.00 41.57  ? 196 GLU A OE2 1 
ATOM   1318 N N   . LEU A 1 168 ? 38.430  1.769   1.156   1.00 22.79  ? 197 LEU A N   1 
ATOM   1319 C CA  . LEU A 1 168 ? 37.630  0.578   1.405   1.00 24.77  ? 197 LEU A CA  1 
ATOM   1320 C C   . LEU A 1 168 ? 36.279  0.688   0.689   1.00 20.69  ? 197 LEU A C   1 
ATOM   1321 O O   . LEU A 1 168 ? 35.703  -0.292  0.267   1.00 18.62  ? 197 LEU A O   1 
ATOM   1322 C CB  . LEU A 1 168 ? 37.473  0.411   2.916   1.00 28.45  ? 197 LEU A CB  1 
ATOM   1323 C CG  . LEU A 1 168 ? 38.652  -0.179  3.689   1.00 34.04  ? 197 LEU A CG  1 
ATOM   1324 C CD1 . LEU A 1 168 ? 39.168  -1.457  3.084   1.00 37.65  ? 197 LEU A CD1 1 
ATOM   1325 C CD2 . LEU A 1 168 ? 39.763  0.848   3.828   1.00 42.84  ? 197 LEU A CD2 1 
ATOM   1326 N N   . ILE A 1 169 ? 35.702  1.876   0.651   1.00 19.77  ? 198 ILE A N   1 
ATOM   1327 C CA  . ILE A 1 169 ? 34.521  2.137   -0.161  1.00 20.68  ? 198 ILE A CA  1 
ATOM   1328 C C   . ILE A 1 169 ? 34.742  1.749   -1.630  1.00 20.20  ? 198 ILE A C   1 
ATOM   1329 O O   . ILE A 1 169 ? 33.902  1.070   -2.216  1.00 18.59  ? 198 ILE A O   1 
ATOM   1330 C CB  . ILE A 1 169 ? 34.160  3.621   -0.022  1.00 20.83  ? 198 ILE A CB  1 
ATOM   1331 C CG1 . ILE A 1 169 ? 33.763  4.000   1.428   1.00 21.55  ? 198 ILE A CG1 1 
ATOM   1332 C CG2 . ILE A 1 169 ? 33.076  4.030   -1.006  1.00 22.74  ? 198 ILE A CG2 1 
ATOM   1333 C CD1 . ILE A 1 169 ? 32.509  3.316   1.949   1.00 21.97  ? 198 ILE A CD1 1 
ATOM   1334 N N   . TYR A 1 170 ? 35.886  2.175   -2.197  1.00 20.60  ? 199 TYR A N   1 
ATOM   1335 C CA  . TYR A 1 170 ? 36.292  1.850   -3.560  1.00 20.35  ? 199 TYR A CA  1 
ATOM   1336 C C   . TYR A 1 170 ? 36.303  0.327   -3.733  1.00 20.66  ? 199 TYR A C   1 
ATOM   1337 O O   . TYR A 1 170 ? 35.740  -0.184  -4.694  1.00 20.35  ? 199 TYR A O   1 
ATOM   1338 C CB  . TYR A 1 170 ? 37.634  2.499   -3.926  1.00 21.22  ? 199 TYR A CB  1 
ATOM   1339 C CG  . TYR A 1 170 ? 38.328  1.911   -5.161  1.00 21.34  ? 199 TYR A CG  1 
ATOM   1340 C CD1 . TYR A 1 170 ? 39.163  0.803   -5.060  1.00 20.43  ? 199 TYR A CD1 1 
ATOM   1341 C CD2 . TYR A 1 170 ? 38.167  2.486   -6.417  1.00 22.19  ? 199 TYR A CD2 1 
ATOM   1342 C CE1 . TYR A 1 170 ? 39.709  0.220   -6.194  1.00 22.97  ? 199 TYR A CE1 1 
ATOM   1343 C CE2 . TYR A 1 170 ? 38.767  1.962   -7.541  1.00 19.67  ? 199 TYR A CE2 1 
ATOM   1344 C CZ  . TYR A 1 170 ? 39.516  0.803   -7.433  1.00 22.48  ? 199 TYR A CZ  1 
ATOM   1345 O OH  . TYR A 1 170 ? 40.132  0.304   -8.544  1.00 20.79  ? 199 TYR A OH  1 
ATOM   1346 N N   . GLU A 1 171 ? 36.964  -0.396  -2.834  1.00 22.96  ? 200 GLU A N   1 
ATOM   1347 C CA  . GLU A 1 171 ? 37.087  -1.850  -2.989  1.00 21.63  ? 200 GLU A CA  1 
ATOM   1348 C C   . GLU A 1 171 ? 35.711  -2.513  -2.956  1.00 21.87  ? 200 GLU A C   1 
ATOM   1349 O O   . GLU A 1 171 ? 35.399  -3.372  -3.784  1.00 18.87  ? 200 GLU A O   1 
ATOM   1350 C CB  . GLU A 1 171 ? 37.928  -2.561  -1.924  1.00 23.84  ? 200 GLU A CB  1 
ATOM   1351 C CG  . GLU A 1 171 ? 39.432  -2.286  -1.983  1.00 25.57  ? 200 GLU A CG  1 
ATOM   1352 C CD  . GLU A 1 171 ? 40.122  -2.637  -3.294  1.00 25.07  ? 200 GLU A CD  1 
ATOM   1353 O OE1 . GLU A 1 171 ? 41.106  -1.961  -3.702  1.00 24.91  ? 200 GLU A OE1 1 
ATOM   1354 O OE2 . GLU A 1 171 ? 39.660  -3.609  -3.925  1.00 24.82  ? 200 GLU A OE2 1 
ATOM   1355 N N   . ASP A 1 172 ? 34.945  -2.191  -1.922  1.00 20.54  ? 201 ASP A N   1 
ATOM   1356 C CA  . ASP A 1 172 ? 33.588  -2.711  -1.778  1.00 21.74  ? 201 ASP A CA  1 
ATOM   1357 C C   . ASP A 1 172 ? 32.752  -2.328  -2.990  1.00 18.66  ? 201 ASP A C   1 
ATOM   1358 O O   . ASP A 1 172 ? 31.947  -3.130  -3.443  1.00 19.33  ? 201 ASP A O   1 
ATOM   1359 C CB  . ASP A 1 172 ? 32.895  -2.197  -0.534  1.00 21.12  ? 201 ASP A CB  1 
ATOM   1360 C CG  . ASP A 1 172 ? 33.315  -2.888  0.752   1.00 24.94  ? 201 ASP A CG  1 
ATOM   1361 O OD1 . ASP A 1 172 ? 34.091  -3.871  0.681   1.00 28.53  ? 201 ASP A OD1 1 
ATOM   1362 O OD2 . ASP A 1 172 ? 32.884  -2.457  1.816   1.00 22.82  ? 201 ASP A OD2 1 
ATOM   1363 N N   . SER A 1 173 ? 32.922  -1.122  -3.529  1.00 19.69  ? 202 SER A N   1 
ATOM   1364 C CA  . SER A 1 173 ? 32.140  -0.731  -4.701  1.00 21.05  ? 202 SER A CA  1 
ATOM   1365 C C   . SER A 1 173 ? 32.547  -1.564  -5.921  1.00 22.75  ? 202 SER A C   1 
ATOM   1366 O O   . SER A 1 173 ? 31.719  -1.896  -6.766  1.00 21.50  ? 202 SER A O   1 
ATOM   1367 C CB  . SER A 1 173 ? 32.289  0.735   -5.029  1.00 22.52  ? 202 SER A CB  1 
ATOM   1368 O OG  . SER A 1 173 ? 31.703  1.559   -4.029  1.00 24.21  ? 202 SER A OG  1 
ATOM   1369 N N   . MET A 1 174 ? 33.847  -1.799  -6.081  1.00 21.48  ? 203 MET A N   1 
ATOM   1370 C CA  . MET A 1 174 ? 34.308  -2.592  -7.207  1.00 22.05  ? 203 MET A CA  1 
ATOM   1371 C C   . MET A 1 174 ? 33.792  -4.029  -7.095  1.00 24.26  ? 203 MET A C   1 
ATOM   1372 O O   . MET A 1 174 ? 33.384  -4.609  -8.092  1.00 25.42  ? 203 MET A O   1 
ATOM   1373 C CB  . MET A 1 174 ? 35.828  -2.549  -7.318  1.00 20.36  ? 203 MET A CB  1 
ATOM   1374 C CG  . MET A 1 174 ? 36.384  -1.157  -7.636  1.00 21.87  ? 203 MET A CG  1 
ATOM   1375 S SD  . MET A 1 174 ? 36.370  -0.802  -9.406  1.00 23.01  ? 203 MET A SD  1 
ATOM   1376 C CE  . MET A 1 174 ? 37.789  -1.802  -9.860  1.00 25.41  ? 203 MET A CE  1 
ATOM   1377 N N   . ASP A 1 175 ? 33.734  -4.569  -5.875  1.00 21.87  ? 204 ASP A N   1 
ATOM   1378 C CA  . ASP A 1 175 ? 33.224  -5.908  -5.652  1.00 22.47  ? 204 ASP A CA  1 
ATOM   1379 C C   . ASP A 1 175 ? 31.727  -5.959  -5.959  1.00 23.56  ? 204 ASP A C   1 
ATOM   1380 O O   . ASP A 1 175 ? 31.263  -6.902  -6.609  1.00 24.35  ? 204 ASP A O   1 
ATOM   1381 C CB  . ASP A 1 175 ? 33.472  -6.375  -4.223  1.00 24.64  ? 204 ASP A CB  1 
ATOM   1382 C CG  . ASP A 1 175 ? 34.924  -6.679  -3.863  1.00 26.89  ? 204 ASP A CG  1 
ATOM   1383 O OD1 . ASP A 1 175 ? 35.743  -6.858  -4.763  1.00 26.81  ? 204 ASP A OD1 1 
ATOM   1384 O OD2 . ASP A 1 175 ? 35.262  -6.617  -2.685  1.00 27.00  ? 204 ASP A OD2 1 
ATOM   1385 N N   . LEU A 1 176 ? 30.954  -4.968  -5.463  1.00 21.33  ? 205 LEU A N   1 
ATOM   1386 C CA  . LEU A 1 176 ? 29.511  -4.974  -5.722  1.00 20.83  ? 205 LEU A CA  1 
ATOM   1387 C C   . LEU A 1 176 ? 29.198  -4.868  -7.219  1.00 18.12  ? 205 LEU A C   1 
ATOM   1388 O O   . LEU A 1 176 ? 28.356  -5.608  -7.733  1.00 19.69  ? 205 LEU A O   1 
ATOM   1389 C CB  . LEU A 1 176 ? 28.873  -3.828  -4.944  1.00 18.70  ? 205 LEU A CB  1 
ATOM   1390 C CG  . LEU A 1 176 ? 27.361  -3.632  -5.101  1.00 20.72  ? 205 LEU A CG  1 
ATOM   1391 C CD1 . LEU A 1 176 ? 26.507  -4.879  -4.901  1.00 23.65  ? 205 LEU A CD1 1 
ATOM   1392 C CD2 . LEU A 1 176 ? 26.961  -2.570  -4.092  1.00 21.43  ? 205 LEU A CD2 1 
ATOM   1393 N N   . ILE A 1 177 ? 29.753  -3.864  -7.904  1.00 18.79  ? 206 ILE A N   1 
ATOM   1394 C CA  . ILE A 1 177 ? 29.532  -3.740  -9.339  1.00 20.14  ? 206 ILE A CA  1 
ATOM   1395 C C   . ILE A 1 177 ? 29.819  -5.068  -10.056 1.00 19.85  ? 206 ILE A C   1 
ATOM   1396 O O   . ILE A 1 177 ? 28.989  -5.568  -10.812 1.00 18.22  ? 206 ILE A O   1 
ATOM   1397 C CB  . ILE A 1 177 ? 30.344  -2.562  -9.875  1.00 22.67  ? 206 ILE A CB  1 
ATOM   1398 C CG1 . ILE A 1 177 ? 29.738  -1.244  -9.380  1.00 22.74  ? 206 ILE A CG1 1 
ATOM   1399 C CG2 . ILE A 1 177 ? 30.423  -2.598  -11.414 1.00 27.64  ? 206 ILE A CG2 1 
ATOM   1400 C CD1 . ILE A 1 177 ? 30.715  -0.081  -9.484  1.00 24.61  ? 206 ILE A CD1 1 
ATOM   1401 N N   . ALA A 1 178 ? 30.970  -5.683  -9.782  1.00 19.23  ? 207 ALA A N   1 
ATOM   1402 C CA  . ALA A 1 178 ? 31.304  -6.967  -10.395 1.00 18.99  ? 207 ALA A CA  1 
ATOM   1403 C C   . ALA A 1 178 ? 30.248  -8.049  -10.135 1.00 21.97  ? 207 ALA A C   1 
ATOM   1404 O O   . ALA A 1 178 ? 30.032  -8.880  -11.003 1.00 21.19  ? 207 ALA A O   1 
ATOM   1405 C CB  . ALA A 1 178 ? 32.633  -7.414  -9.916  1.00 18.72  ? 207 ALA A CB  1 
ATOM   1406 N N   . LYS A 1 179 ? 29.607  -8.049  -8.941  1.00 24.96  ? 208 LYS A N   1 
ATOM   1407 C CA  . LYS A 1 179 ? 28.709  -9.109  -8.514  1.00 25.16  ? 208 LYS A CA  1 
ATOM   1408 C C   . LYS A 1 179 ? 27.278  -8.880  -8.994  1.00 25.62  ? 208 LYS A C   1 
ATOM   1409 O O   . LYS A 1 179 ? 26.510  -9.822  -9.193  1.00 21.25  ? 208 LYS A O   1 
ATOM   1410 C CB  . LYS A 1 179 ? 28.669  -9.177  -6.987  1.00 27.52  ? 208 LYS A CB  1 
ATOM   1411 C CG  . LYS A 1 179 ? 29.921  -9.748  -6.378  1.00 29.90  ? 208 LYS A CG  1 
ATOM   1412 C CD  . LYS A 1 179 ? 29.963  -9.783  -4.860  1.00 28.38  ? 208 LYS A CD  1 
ATOM   1413 C CE  . LYS A 1 179 ? 31.422  -9.884  -4.475  1.00 31.94  ? 208 LYS A CE  1 
ATOM   1414 N NZ  . LYS A 1 179 ? 31.571  -9.532  -3.059  1.00 42.73  ? 208 LYS A NZ  1 
ATOM   1415 N N   . LEU A 1 180 ? 26.919  -7.623  -9.198  1.00 22.86  ? 209 LEU A N   1 
ATOM   1416 C CA  . LEU A 1 180 ? 25.553  -7.278  -9.543  1.00 23.42  ? 209 LEU A CA  1 
ATOM   1417 C C   . LEU A 1 180 ? 24.997  -8.080  -10.725 1.00 22.42  ? 209 LEU A C   1 
ATOM   1418 O O   . LEU A 1 180 ? 23.873  -8.559  -10.625 1.00 19.58  ? 209 LEU A O   1 
ATOM   1419 C CB  . LEU A 1 180 ? 25.492  -5.774  -9.798  1.00 22.91  ? 209 LEU A CB  1 
ATOM   1420 C CG  . LEU A 1 180 ? 25.260  -4.935  -8.555  1.00 25.83  ? 209 LEU A CG  1 
ATOM   1421 C CD1 . LEU A 1 180 ? 25.299  -3.474  -8.953  1.00 30.03  ? 209 LEU A CD1 1 
ATOM   1422 C CD2 . LEU A 1 180 ? 23.951  -5.297  -7.873  1.00 25.02  ? 209 LEU A CD2 1 
ATOM   1423 N N   . PRO A 1 181 ? 25.678  -8.192  -11.886 1.00 21.66  ? 210 PRO A N   1 
ATOM   1424 C CA  . PRO A 1 181 ? 25.160  -8.984  -12.989 1.00 25.46  ? 210 PRO A CA  1 
ATOM   1425 C C   . PRO A 1 181 ? 24.874  -10.438 -12.635 1.00 26.68  ? 210 PRO A C   1 
ATOM   1426 O O   . PRO A 1 181 ? 23.954  -11.016 -13.214 1.00 27.30  ? 210 PRO A O   1 
ATOM   1427 C CB  . PRO A 1 181 ? 26.226  -8.870  -14.082 1.00 24.75  ? 210 PRO A CB  1 
ATOM   1428 C CG  . PRO A 1 181 ? 26.985  -7.625  -13.719 1.00 27.13  ? 210 PRO A CG  1 
ATOM   1429 C CD  . PRO A 1 181 ? 26.945  -7.532  -12.235 1.00 23.47  ? 210 PRO A CD  1 
ATOM   1430 N N   . CYS A 1 182 ? 25.703  -11.009 -11.747 1.00 26.04  ? 211 CYS A N   1 
ATOM   1431 C CA  . CYS A 1 182 ? 25.506  -12.353 -11.250 1.00 26.64  ? 211 CYS A CA  1 
ATOM   1432 C C   . CYS A 1 182 ? 24.219  -12.411 -10.435 1.00 25.90  ? 211 CYS A C   1 
ATOM   1433 O O   . CYS A 1 182 ? 23.362  -13.234 -10.710 1.00 25.63  ? 211 CYS A O   1 
ATOM   1434 C CB  . CYS A 1 182 ? 26.665  -12.797 -10.374 1.00 29.68  ? 211 CYS A CB  1 
ATOM   1435 S SG  . CYS A 1 182 ? 28.191  -12.927 -11.321 1.00 39.13  ? 211 CYS A SG  1 
ATOM   1436 N N   . VAL A 1 183 ? 24.053  -11.475 -9.485  1.00 22.19  ? 212 VAL A N   1 
ATOM   1437 C CA  . VAL A 1 183 ? 22.810  -11.412 -8.732  1.00 22.20  ? 212 VAL A CA  1 
ATOM   1438 C C   . VAL A 1 183 ? 21.616  -11.267 -9.687  1.00 22.75  ? 212 VAL A C   1 
ATOM   1439 O O   . VAL A 1 183 ? 20.610  -12.001 -9.575  1.00 23.46  ? 212 VAL A O   1 
ATOM   1440 C CB  . VAL A 1 183 ? 22.823  -10.269 -7.683  1.00 20.16  ? 212 VAL A CB  1 
ATOM   1441 C CG1 . VAL A 1 183 ? 21.480  -10.130 -6.963  1.00 20.73  ? 212 VAL A CG1 1 
ATOM   1442 C CG2 . VAL A 1 183 ? 23.948  -10.437 -6.711  1.00 23.08  ? 212 VAL A CG2 1 
ATOM   1443 N N   . ALA A 1 184 ? 21.714  -10.285 -10.594 1.00 21.43  ? 213 ALA A N   1 
ATOM   1444 C CA  . ALA A 1 184 ? 20.624  -9.896  -11.459 1.00 22.45  ? 213 ALA A CA  1 
ATOM   1445 C C   . ALA A 1 184 ? 20.242  -11.069 -12.375 1.00 24.46  ? 213 ALA A C   1 
ATOM   1446 O O   . ALA A 1 184 ? 19.056  -11.350 -12.547 1.00 23.48  ? 213 ALA A O   1 
ATOM   1447 C CB  . ALA A 1 184 ? 20.974  -8.654  -12.255 1.00 22.79  ? 213 ALA A CB  1 
ATOM   1448 N N   . ALA A 1 185 ? 21.231  -11.779 -12.930 1.00 22.21  ? 214 ALA A N   1 
ATOM   1449 C CA  . ALA A 1 185 ? 20.942  -12.876 -13.838 1.00 23.18  ? 214 ALA A CA  1 
ATOM   1450 C C   . ALA A 1 185 ? 20.424  -14.098 -13.087 1.00 25.93  ? 214 ALA A C   1 
ATOM   1451 O O   . ALA A 1 185 ? 19.632  -14.843 -13.648 1.00 33.55  ? 214 ALA A O   1 
ATOM   1452 C CB  . ALA A 1 185 ? 22.169  -13.196 -14.647 1.00 24.36  ? 214 ALA A CB  1 
ATOM   1453 N N   . LYS A 1 186 ? 20.784  -14.294 -11.813 1.00 28.04  ? 215 LYS A N   1 
ATOM   1454 C CA  . LYS A 1 186 ? 20.206  -15.369 -11.011 1.00 28.86  ? 215 LYS A CA  1 
ATOM   1455 C C   . LYS A 1 186 ? 18.712  -15.145 -10.782 1.00 27.18  ? 215 LYS A C   1 
ATOM   1456 O O   . LYS A 1 186 ? 17.901  -16.103 -10.809 1.00 24.94  ? 215 LYS A O   1 
ATOM   1457 C CB  . LYS A 1 186 ? 20.928  -15.571 -9.668  1.00 34.10  ? 215 LYS A CB  1 
ATOM   1458 C CG  . LYS A 1 186 ? 20.801  -16.959 -9.021  1.00 40.39  ? 215 LYS A CG  1 
ATOM   1459 C CD  . LYS A 1 186 ? 22.097  -17.682 -8.651  1.00 38.14  ? 215 LYS A CD  1 
ATOM   1460 C CE  . LYS A 1 186 ? 22.148  -19.094 -9.154  1.00 34.93  ? 215 LYS A CE  1 
ATOM   1461 N N   . ILE A 1 187 ? 18.357  -13.872 -10.514 1.00 25.52  ? 216 ILE A N   1 
ATOM   1462 C CA  . ILE A 1 187 ? 16.975  -13.490 -10.321 1.00 24.45  ? 216 ILE A CA  1 
ATOM   1463 C C   . ILE A 1 187 ? 16.242  -13.795 -11.623 1.00 24.19  ? 216 ILE A C   1 
ATOM   1464 O O   . ILE A 1 187 ? 15.191  -14.434 -11.608 1.00 24.11  ? 216 ILE A O   1 
ATOM   1465 C CB  . ILE A 1 187 ? 16.813  -12.001 -9.935  1.00 25.05  ? 216 ILE A CB  1 
ATOM   1466 C CG1 . ILE A 1 187 ? 17.377  -11.708 -8.539  1.00 30.05  ? 216 ILE A CG1 1 
ATOM   1467 C CG2 . ILE A 1 187 ? 15.345  -11.590 -10.029 1.00 22.53  ? 216 ILE A CG2 1 
ATOM   1468 C CD1 . ILE A 1 187 ? 17.752  -10.259 -8.279  1.00 32.85  ? 216 ILE A CD1 1 
ATOM   1469 N N   . TYR A 1 188 ? 16.799  -13.302 -12.740 1.00 24.02  ? 217 TYR A N   1 
ATOM   1470 C CA  . TYR A 1 188 ? 16.134  -13.420 -14.027 1.00 25.31  ? 217 TYR A CA  1 
ATOM   1471 C C   . TYR A 1 188 ? 15.804  -14.883 -14.299 1.00 23.96  ? 217 TYR A C   1 
ATOM   1472 O O   . TYR A 1 188 ? 14.664  -15.217 -14.664 1.00 28.08  ? 217 TYR A O   1 
ATOM   1473 C CB  . TYR A 1 188 ? 16.966  -12.852 -15.173 1.00 26.21  ? 217 TYR A CB  1 
ATOM   1474 C CG  . TYR A 1 188 ? 16.179  -12.845 -16.472 1.00 29.88  ? 217 TYR A CG  1 
ATOM   1475 C CD1 . TYR A 1 188 ? 15.137  -11.940 -16.646 1.00 32.24  ? 217 TYR A CD1 1 
ATOM   1476 C CD2 . TYR A 1 188 ? 16.438  -13.749 -17.498 1.00 31.84  ? 217 TYR A CD2 1 
ATOM   1477 C CE1 . TYR A 1 188 ? 14.383  -11.906 -17.803 1.00 31.87  ? 217 TYR A CE1 1 
ATOM   1478 C CE2 . TYR A 1 188 ? 15.712  -13.700 -18.682 1.00 35.13  ? 217 TYR A CE2 1 
ATOM   1479 C CZ  . TYR A 1 188 ? 14.681  -12.778 -18.831 1.00 36.60  ? 217 TYR A CZ  1 
ATOM   1480 O OH  . TYR A 1 188 ? 13.891  -12.697 -19.939 1.00 35.74  ? 217 TYR A OH  1 
ATOM   1481 N N   . ARG A 1 189 ? 16.805  -15.741 -14.101 1.00 24.83  ? 218 ARG A N   1 
ATOM   1482 C CA  . ARG A 1 189 ? 16.697  -17.149 -14.436 1.00 28.93  ? 218 ARG A CA  1 
ATOM   1483 C C   . ARG A 1 189 ? 15.786  -17.896 -13.462 1.00 32.60  ? 218 ARG A C   1 
ATOM   1484 O O   . ARG A 1 189 ? 15.045  -18.787 -13.885 1.00 31.19  ? 218 ARG A O   1 
ATOM   1485 C CB  . ARG A 1 189 ? 18.038  -17.879 -14.492 1.00 32.38  ? 218 ARG A CB  1 
ATOM   1486 C CG  . ARG A 1 189 ? 18.958  -17.337 -15.568 1.00 40.44  ? 218 ARG A CG  1 
ATOM   1487 C CD  . ARG A 1 189 ? 20.036  -18.324 -15.966 1.00 49.60  ? 218 ARG A CD  1 
ATOM   1488 N NE  . ARG A 1 189 ? 19.418  -19.244 -16.925 1.00 59.94  ? 218 ARG A NE  1 
ATOM   1489 C CZ  . ARG A 1 189 ? 19.628  -19.239 -18.230 1.00 59.39  ? 218 ARG A CZ  1 
ATOM   1490 N NH1 . ARG A 1 189 ? 20.616  -18.521 -18.736 1.00 59.11  ? 218 ARG A NH1 1 
ATOM   1491 N NH2 . ARG A 1 189 ? 18.862  -19.986 -19.010 1.00 58.06  ? 218 ARG A NH2 1 
ATOM   1492 N N   . ASN A 1 190 ? 15.864  -17.575 -12.167 1.00 30.20  ? 219 ASN A N   1 
ATOM   1493 C CA  . ASN A 1 190 ? 15.057  -18.248 -11.163 1.00 29.91  ? 219 ASN A CA  1 
ATOM   1494 C C   . ASN A 1 190 ? 13.583  -17.940 -11.387 1.00 30.33  ? 219 ASN A C   1 
ATOM   1495 O O   . ASN A 1 190 ? 12.734  -18.806 -11.166 1.00 30.70  ? 219 ASN A O   1 
ATOM   1496 C CB  . ASN A 1 190 ? 15.460  -17.858 -9.739  1.00 34.59  ? 219 ASN A CB  1 
ATOM   1497 C CG  . ASN A 1 190 ? 16.753  -18.500 -9.298  1.00 37.48  ? 219 ASN A CG  1 
ATOM   1498 O OD1 . ASN A 1 190 ? 17.331  -19.308 -10.034 1.00 41.63  ? 219 ASN A OD1 1 
ATOM   1499 N ND2 . ASN A 1 190 ? 17.219  -18.174 -8.099  1.00 34.38  ? 219 ASN A ND2 1 
ATOM   1500 N N   . LEU A 1 191 ? 13.272  -16.701 -11.805 1.00 28.31  ? 220 LEU A N   1 
ATOM   1501 C CA  . LEU A 1 191 ? 11.891  -16.302 -12.018 1.00 29.80  ? 220 LEU A CA  1 
ATOM   1502 C C   . LEU A 1 191 ? 11.381  -16.736 -13.399 1.00 31.36  ? 220 LEU A C   1 
ATOM   1503 O O   . LEU A 1 191 ? 10.208  -17.076 -13.509 1.00 27.36  ? 220 LEU A O   1 
ATOM   1504 C CB  . LEU A 1 191 ? 11.678  -14.797 -11.839 1.00 29.33  ? 220 LEU A CB  1 
ATOM   1505 C CG  . LEU A 1 191 ? 11.751  -14.259 -10.394 1.00 32.24  ? 220 LEU A CG  1 
ATOM   1506 C CD1 . LEU A 1 191 ? 11.850  -12.716 -10.428 1.00 33.18  ? 220 LEU A CD1 1 
ATOM   1507 C CD2 . LEU A 1 191 ? 10.583  -14.715 -9.558  1.00 33.88  ? 220 LEU A CD2 1 
ATOM   1508 N N   . TYR A 1 192 ? 12.204  -16.606 -14.456 1.00 31.13  ? 221 TYR A N   1 
ATOM   1509 C CA  . TYR A 1 192 ? 11.672  -16.557 -15.811 1.00 32.48  ? 221 TYR A CA  1 
ATOM   1510 C C   . TYR A 1 192 ? 12.232  -17.670 -16.685 1.00 37.02  ? 221 TYR A C   1 
ATOM   1511 O O   . TYR A 1 192 ? 11.907  -17.713 -17.869 1.00 39.58  ? 221 TYR A O   1 
ATOM   1512 C CB  . TYR A 1 192 ? 11.960  -15.211 -16.467 1.00 36.13  ? 221 TYR A CB  1 
ATOM   1513 C CG  . TYR A 1 192 ? 11.434  -14.046 -15.639 1.00 36.79  ? 221 TYR A CG  1 
ATOM   1514 C CD1 . TYR A 1 192 ? 10.090  -13.971 -15.293 1.00 35.09  ? 221 TYR A CD1 1 
ATOM   1515 C CD2 . TYR A 1 192 ? 12.296  -13.080 -15.132 1.00 36.10  ? 221 TYR A CD2 1 
ATOM   1516 C CE1 . TYR A 1 192 ? 9.611   -12.931 -14.528 1.00 33.29  ? 221 TYR A CE1 1 
ATOM   1517 C CE2 . TYR A 1 192 ? 11.828  -12.041 -14.348 1.00 32.37  ? 221 TYR A CE2 1 
ATOM   1518 C CZ  . TYR A 1 192 ? 10.485  -11.974 -14.048 1.00 32.81  ? 221 TYR A CZ  1 
ATOM   1519 O OH  . TYR A 1 192 ? 9.986   -10.965 -13.292 1.00 32.39  ? 221 TYR A OH  1 
ATOM   1520 N N   . ARG A 1 193 ? 13.084  -18.536 -16.123 1.00 39.99  ? 222 ARG A N   1 
ATOM   1521 C CA  . ARG A 1 193 ? 13.680  -19.644 -16.860 1.00 37.12  ? 222 ARG A CA  1 
ATOM   1522 C C   . ARG A 1 193 ? 13.750  -20.885 -15.975 1.00 34.52  ? 222 ARG A C   1 
ATOM   1523 O O   . ARG A 1 193 ? 14.730  -21.622 -16.053 1.00 34.09  ? 222 ARG A O   1 
ATOM   1524 C CB  . ARG A 1 193 ? 15.113  -19.283 -17.263 1.00 37.69  ? 222 ARG A CB  1 
ATOM   1525 C CG  . ARG A 1 193 ? 15.217  -18.107 -18.212 1.00 36.43  ? 222 ARG A CG  1 
ATOM   1526 C CD  . ARG A 1 193 ? 14.686  -18.509 -19.567 1.00 39.87  ? 222 ARG A CD  1 
ATOM   1527 N NE  . ARG A 1 193 ? 14.782  -17.439 -20.565 1.00 41.30  ? 222 ARG A NE  1 
ATOM   1528 C CZ  . ARG A 1 193 ? 13.984  -16.377 -20.701 1.00 41.73  ? 222 ARG A CZ  1 
ATOM   1529 N NH1 . ARG A 1 193 ? 12.863  -16.248 -19.999 1.00 43.96  ? 222 ARG A NH1 1 
ATOM   1530 N NH2 . ARG A 1 193 ? 14.316  -15.450 -21.578 1.00 39.92  ? 222 ARG A NH2 1 
ATOM   1531 N N   . GLU A 1 194 ? 12.757  -21.033 -15.079 1.00 38.42  ? 223 GLU A N   1 
ATOM   1532 C CA  . GLU A 1 194 ? 12.659  -22.121 -14.109 1.00 45.38  ? 223 GLU A CA  1 
ATOM   1533 C C   . GLU A 1 194 ? 14.001  -22.528 -13.477 1.00 46.33  ? 223 GLU A C   1 
ATOM   1534 O O   . GLU A 1 194 ? 14.291  -23.730 -13.339 1.00 41.12  ? 223 GLU A O   1 
ATOM   1535 C CB  . GLU A 1 194 ? 12.032  -23.339 -14.791 1.00 58.35  ? 223 GLU A CB  1 
ATOM   1536 C CG  . GLU A 1 194 ? 10.683  -23.065 -15.451 1.00 63.99  ? 223 GLU A CG  1 
ATOM   1537 C CD  . GLU A 1 194 ? 10.001  -24.336 -15.936 1.00 82.89  ? 223 GLU A CD  1 
ATOM   1538 O OE1 . GLU A 1 194 ? 10.657  -25.164 -16.625 1.00 81.16  ? 223 GLU A OE1 1 
ATOM   1539 O OE2 . GLU A 1 194 ? 8.799   -24.489 -15.625 1.00 97.08  ? 223 GLU A OE2 1 
ATOM   1540 N N   . GLY A 1 195 ? 14.810  -21.544 -13.042 1.00 36.37  ? 224 GLY A N   1 
ATOM   1541 C CA  . GLY A 1 195 ? 15.929  -21.858 -12.166 1.00 35.54  ? 224 GLY A CA  1 
ATOM   1542 C C   . GLY A 1 195 ? 17.121  -22.479 -12.880 1.00 32.31  ? 224 GLY A C   1 
ATOM   1543 O O   . GLY A 1 195 ? 18.023  -23.009 -12.248 1.00 37.88  ? 224 GLY A O   1 
ATOM   1544 N N   . SER A 1 196 ? 17.170  -22.393 -14.204 1.00 37.68  ? 225 SER A N   1 
ATOM   1545 C CA  . SER A 1 196 ? 18.356  -22.830 -14.919 1.00 38.56  ? 225 SER A CA  1 
ATOM   1546 C C   . SER A 1 196 ? 19.558  -21.985 -14.484 1.00 41.66  ? 225 SER A C   1 
ATOM   1547 O O   . SER A 1 196 ? 19.384  -20.853 -14.034 1.00 38.88  ? 225 SER A O   1 
ATOM   1548 C CB  . SER A 1 196 ? 18.134  -22.763 -16.393 1.00 43.66  ? 225 SER A CB  1 
ATOM   1549 O OG  . SER A 1 196 ? 17.682  -21.477 -16.801 1.00 50.50  ? 225 SER A OG  1 
ATOM   1550 N N   . GLY A 1 197 ? 20.766  -22.548 -14.634 1.00 34.51  ? 226 GLY A N   1 
ATOM   1551 C CA  . GLY A 1 197 ? 21.992  -21.990 -14.096 1.00 35.07  ? 226 GLY A CA  1 
ATOM   1552 C C   . GLY A 1 197 ? 22.548  -20.865 -14.966 1.00 36.46  ? 226 GLY A C   1 
ATOM   1553 O O   . GLY A 1 197 ? 22.312  -20.818 -16.171 1.00 41.17  ? 226 GLY A O   1 
ATOM   1554 N N   . ILE A 1 198 ? 23.322  -19.968 -14.346 1.00 30.99  ? 227 ILE A N   1 
ATOM   1555 C CA  . ILE A 1 198 ? 23.735  -18.744 -15.015 1.00 34.43  ? 227 ILE A CA  1 
ATOM   1556 C C   . ILE A 1 198 ? 25.010  -18.941 -15.828 1.00 37.90  ? 227 ILE A C   1 
ATOM   1557 O O   . ILE A 1 198 ? 25.394  -18.032 -16.575 1.00 37.73  ? 227 ILE A O   1 
ATOM   1558 C CB  . ILE A 1 198 ? 23.898  -17.562 -14.046 1.00 31.32  ? 227 ILE A CB  1 
ATOM   1559 C CG1 . ILE A 1 198 ? 24.672  -17.911 -12.792 1.00 30.65  ? 227 ILE A CG1 1 
ATOM   1560 C CG2 . ILE A 1 198 ? 22.528  -16.961 -13.729 1.00 32.78  ? 227 ILE A CG2 1 
ATOM   1561 C CD1 . ILE A 1 198 ? 24.994  -16.683 -11.942 1.00 34.62  ? 227 ILE A CD1 1 
ATOM   1562 N N   . GLY A 1 199 ? 25.664  -20.096 -15.646 1.00 35.79  ? 228 GLY A N   1 
ATOM   1563 C CA  . GLY A 1 199 ? 26.910  -20.381 -16.322 1.00 37.69  ? 228 GLY A CA  1 
ATOM   1564 C C   . GLY A 1 199 ? 28.047  -19.592 -15.691 1.00 39.40  ? 228 GLY A C   1 
ATOM   1565 O O   . GLY A 1 199 ? 27.938  -19.111 -14.570 1.00 44.78  ? 228 GLY A O   1 
ATOM   1566 N N   . ALA A 1 200 ? 29.143  -19.469 -16.430 1.00 44.52  ? 229 ALA A N   1 
ATOM   1567 C CA  . ALA A 1 200 ? 30.379  -18.978 -15.862 1.00 43.70  ? 229 ALA A CA  1 
ATOM   1568 C C   . ALA A 1 200 ? 30.605  -17.567 -16.373 1.00 38.20  ? 229 ALA A C   1 
ATOM   1569 O O   . ALA A 1 200 ? 29.942  -17.133 -17.310 1.00 41.13  ? 229 ALA A O   1 
ATOM   1570 C CB  . ALA A 1 200 ? 31.519  -19.901 -16.221 1.00 45.88  ? 229 ALA A CB  1 
ATOM   1571 N N   . ILE A 1 201 ? 31.494  -16.864 -15.671 1.00 40.42  ? 230 ILE A N   1 
ATOM   1572 C CA  . ILE A 1 201 ? 32.033  -15.596 -16.108 1.00 39.51  ? 230 ILE A CA  1 
ATOM   1573 C C   . ILE A 1 201 ? 33.200  -15.899 -17.020 1.00 40.31  ? 230 ILE A C   1 
ATOM   1574 O O   . ILE A 1 201 ? 33.973  -16.794 -16.693 1.00 44.36  ? 230 ILE A O   1 
ATOM   1575 C CB  . ILE A 1 201 ? 32.495  -14.767 -14.902 1.00 37.87  ? 230 ILE A CB  1 
ATOM   1576 C CG1 . ILE A 1 201 ? 31.305  -14.276 -14.082 1.00 41.76  ? 230 ILE A CG1 1 
ATOM   1577 C CG2 . ILE A 1 201 ? 33.390  -13.620 -15.355 1.00 36.23  ? 230 ILE A CG2 1 
ATOM   1578 C CD1 . ILE A 1 201 ? 30.514  -13.145 -14.722 1.00 39.55  ? 230 ILE A CD1 1 
ATOM   1579 N N   . ASP A 1 202 ? 33.293  -15.160 -18.134 1.00 38.54  ? 231 ASP A N   1 
ATOM   1580 C CA  . ASP A 1 202 ? 34.434  -15.237 -19.028 1.00 42.45  ? 231 ASP A CA  1 
ATOM   1581 C C   . ASP A 1 202 ? 35.344  -14.065 -18.699 1.00 44.88  ? 231 ASP A C   1 
ATOM   1582 O O   . ASP A 1 202 ? 34.923  -12.916 -18.785 1.00 37.53  ? 231 ASP A O   1 
ATOM   1583 C CB  . ASP A 1 202 ? 34.048  -15.186 -20.494 1.00 44.29  ? 231 ASP A CB  1 
ATOM   1584 C CG  . ASP A 1 202 ? 35.194  -15.404 -21.483 1.00 47.79  ? 231 ASP A CG  1 
ATOM   1585 O OD1 . ASP A 1 202 ? 36.275  -14.746 -21.355 1.00 39.44  ? 231 ASP A OD1 1 
ATOM   1586 O OD2 . ASP A 1 202 ? 34.993  -16.232 -22.396 1.00 48.91  ? 231 ASP A OD2 1 
ATOM   1587 N N   . SER A 1 203 ? 36.590  -14.371 -18.339 1.00 40.18  ? 232 SER A N   1 
ATOM   1588 C CA  . SER A 1 203 ? 37.476  -13.379 -17.757 1.00 44.05  ? 232 SER A CA  1 
ATOM   1589 C C   . SER A 1 203 ? 37.927  -12.364 -18.807 1.00 39.73  ? 232 SER A C   1 
ATOM   1590 O O   . SER A 1 203 ? 38.533  -11.347 -18.475 1.00 41.68  ? 232 SER A O   1 
ATOM   1591 C CB  . SER A 1 203 ? 38.663  -14.072 -17.126 1.00 52.01  ? 232 SER A CB  1 
ATOM   1592 O OG  . SER A 1 203 ? 39.323  -13.214 -16.203 1.00 62.82  ? 232 SER A OG  1 
ATOM   1593 N N   . ASN A 1 204 ? 37.676  -12.664 -20.089 1.00 38.49  ? 233 ASN A N   1 
ATOM   1594 C CA  . ASN A 1 204 ? 38.098  -11.785 -21.165 1.00 39.59  ? 233 ASN A CA  1 
ATOM   1595 C C   . ASN A 1 204 ? 36.918  -11.045 -21.785 1.00 36.32  ? 233 ASN A C   1 
ATOM   1596 O O   . ASN A 1 204 ? 37.124  -10.335 -22.754 1.00 37.05  ? 233 ASN A O   1 
ATOM   1597 C CB  . ASN A 1 204 ? 38.840  -12.554 -22.257 1.00 45.64  ? 233 ASN A CB  1 
ATOM   1598 C CG  . ASN A 1 204 ? 40.272  -12.798 -21.863 1.00 52.74  ? 233 ASN A CG  1 
ATOM   1599 O OD1 . ASN A 1 204 ? 41.004  -11.847 -21.567 1.00 61.44  ? 233 ASN A OD1 1 
ATOM   1600 N ND2 . ASN A 1 204 ? 40.672  -14.058 -21.806 1.00 61.56  ? 233 ASN A ND2 1 
ATOM   1601 N N   . LEU A 1 205 ? 35.688  -11.207 -21.281 1.00 34.19  ? 234 LEU A N   1 
ATOM   1602 C CA  . LEU A 1 205 ? 34.580  -10.413 -21.816 1.00 33.88  ? 234 LEU A CA  1 
ATOM   1603 C C   . LEU A 1 205 ? 34.388  -9.114  -21.042 1.00 32.09  ? 234 LEU A C   1 
ATOM   1604 O O   . LEU A 1 205 ? 34.837  -8.971  -19.907 1.00 31.84  ? 234 LEU A O   1 
ATOM   1605 C CB  . LEU A 1 205 ? 33.319  -11.264 -21.820 1.00 32.64  ? 234 LEU A CB  1 
ATOM   1606 C CG  . LEU A 1 205 ? 33.402  -12.525 -22.675 1.00 33.71  ? 234 LEU A CG  1 
ATOM   1607 C CD1 . LEU A 1 205 ? 32.051  -13.186 -22.595 1.00 34.29  ? 234 LEU A CD1 1 
ATOM   1608 C CD2 . LEU A 1 205 ? 33.842  -12.268 -24.101 1.00 34.90  ? 234 LEU A CD2 1 
ATOM   1609 N N   . ASP A 1 206 ? 33.698  -8.146  -21.647 1.00 32.50  ? 235 ASP A N   1 
ATOM   1610 C CA  . ASP A 1 206 ? 33.279  -6.979  -20.880 1.00 33.73  ? 235 ASP A CA  1 
ATOM   1611 C C   . ASP A 1 206 ? 32.112  -7.333  -19.953 1.00 29.42  ? 235 ASP A C   1 
ATOM   1612 O O   . ASP A 1 206 ? 31.436  -8.336  -20.094 1.00 29.98  ? 235 ASP A O   1 
ATOM   1613 C CB  . ASP A 1 206 ? 32.952  -5.777  -21.761 1.00 33.81  ? 235 ASP A CB  1 
ATOM   1614 C CG  . ASP A 1 206 ? 31.819  -5.993  -22.757 1.00 36.01  ? 235 ASP A CG  1 
ATOM   1615 O OD1 . ASP A 1 206 ? 31.979  -6.877  -23.607 1.00 43.93  ? 235 ASP A OD1 1 
ATOM   1616 O OD2 . ASP A 1 206 ? 30.760  -5.320  -22.663 1.00 33.31  ? 235 ASP A OD2 1 
ATOM   1617 N N   . TRP A 1 207 ? 31.813  -6.425  -19.031 1.00 26.86  ? 236 TRP A N   1 
ATOM   1618 C CA  . TRP A 1 207 ? 30.787  -6.628  -18.018 1.00 25.86  ? 236 TRP A CA  1 
ATOM   1619 C C   . TRP A 1 207 ? 29.391  -6.882  -18.622 1.00 26.89  ? 236 TRP A C   1 
ATOM   1620 O O   . TRP A 1 207 ? 28.678  -7.797  -18.184 1.00 24.00  ? 236 TRP A O   1 
ATOM   1621 C CB  . TRP A 1 207 ? 30.844  -5.349  -17.164 1.00 24.77  ? 236 TRP A CB  1 
ATOM   1622 C CG  . TRP A 1 207 ? 30.064  -5.315  -15.892 1.00 23.18  ? 236 TRP A CG  1 
ATOM   1623 C CD1 . TRP A 1 207 ? 30.249  -6.030  -14.747 1.00 25.70  ? 236 TRP A CD1 1 
ATOM   1624 C CD2 . TRP A 1 207 ? 29.049  -4.340  -15.598 1.00 23.66  ? 236 TRP A CD2 1 
ATOM   1625 N NE1 . TRP A 1 207 ? 29.385  -5.591  -13.778 1.00 25.71  ? 236 TRP A NE1 1 
ATOM   1626 C CE2 . TRP A 1 207 ? 28.627  -4.569  -14.278 1.00 23.25  ? 236 TRP A CE2 1 
ATOM   1627 C CE3 . TRP A 1 207 ? 28.441  -3.327  -16.343 1.00 24.58  ? 236 TRP A CE3 1 
ATOM   1628 C CZ2 . TRP A 1 207 ? 27.642  -3.796  -13.677 1.00 22.79  ? 236 TRP A CZ2 1 
ATOM   1629 C CZ3 . TRP A 1 207 ? 27.461  -2.567  -15.746 1.00 22.99  ? 236 TRP A CZ3 1 
ATOM   1630 C CH2 . TRP A 1 207 ? 27.107  -2.774  -14.420 1.00 21.89  ? 236 TRP A CH2 1 
ATOM   1631 N N   . SER A 1 208 ? 28.995  -6.049  -19.602 1.00 27.28  ? 237 SER A N   1 
ATOM   1632 C CA  . SER A 1 208 ? 27.694  -6.147  -20.256 1.00 29.14  ? 237 SER A CA  1 
ATOM   1633 C C   . SER A 1 208 ? 27.515  -7.476  -20.993 1.00 26.51  ? 237 SER A C   1 
ATOM   1634 O O   . SER A 1 208 ? 26.412  -8.002  -21.017 1.00 25.80  ? 237 SER A O   1 
ATOM   1635 C CB  . SER A 1 208 ? 27.419  -5.017  -21.213 1.00 26.18  ? 237 SER A CB  1 
ATOM   1636 O OG  . SER A 1 208 ? 27.513  -3.742  -20.626 1.00 25.29  ? 237 SER A OG  1 
ATOM   1637 N N   . HIS A 1 209 ? 28.587  -8.035  -21.543 1.00 27.34  ? 238 HIS A N   1 
ATOM   1638 C CA  . HIS A 1 209 ? 28.484  -9.289  -22.289 1.00 27.09  ? 238 HIS A CA  1 
ATOM   1639 C C   . HIS A 1 209 ? 28.428  -10.493 -21.355 1.00 27.27  ? 238 HIS A C   1 
ATOM   1640 O O   . HIS A 1 209 ? 27.663  -11.434 -21.570 1.00 30.56  ? 238 HIS A O   1 
ATOM   1641 C CB  . HIS A 1 209 ? 29.662  -9.407  -23.259 1.00 31.32  ? 238 HIS A CB  1 
ATOM   1642 C CG  . HIS A 1 209 ? 29.541  -10.456 -24.305 1.00 33.21  ? 238 HIS A CG  1 
ATOM   1643 N ND1 . HIS A 1 209 ? 30.488  -10.485 -25.306 1.00 37.14  ? 238 HIS A ND1 1 
ATOM   1644 C CD2 . HIS A 1 209 ? 28.717  -11.505 -24.523 1.00 33.85  ? 238 HIS A CD2 1 
ATOM   1645 C CE1 . HIS A 1 209 ? 30.189  -11.481 -26.143 1.00 37.33  ? 238 HIS A CE1 1 
ATOM   1646 N NE2 . HIS A 1 209 ? 29.130  -12.117 -25.684 1.00 32.89  ? 238 HIS A NE2 1 
ATOM   1647 N N   . ASN A 1 210 ? 29.244  -10.482 -20.294 1.00 27.22  ? 239 ASN A N   1 
ATOM   1648 C CA  . ASN A 1 210 ? 29.108  -11.501 -19.257 1.00 25.80  ? 239 ASN A CA  1 
ATOM   1649 C C   . ASN A 1 210 ? 27.666  -11.549 -18.784 1.00 23.96  ? 239 ASN A C   1 
ATOM   1650 O O   . ASN A 1 210 ? 27.110  -12.626 -18.589 1.00 25.72  ? 239 ASN A O   1 
ATOM   1651 C CB  . ASN A 1 210 ? 30.092  -11.305 -18.107 1.00 25.07  ? 239 ASN A CB  1 
ATOM   1652 C CG  . ASN A 1 210 ? 31.427  -11.962 -18.381 1.00 30.43  ? 239 ASN A CG  1 
ATOM   1653 O OD1 . ASN A 1 210 ? 31.479  -13.098 -18.870 1.00 32.71  ? 239 ASN A OD1 1 
ATOM   1654 N ND2 . ASN A 1 210 ? 32.525  -11.293 -18.065 1.00 28.53  ? 239 ASN A ND2 1 
ATOM   1655 N N   . PHE A 1 211 ? 27.066  -10.360 -18.628 1.00 27.18  ? 240 PHE A N   1 
ATOM   1656 C CA  . PHE A 1 211 ? 25.723  -10.219 -18.081 1.00 26.11  ? 240 PHE A CA  1 
ATOM   1657 C C   . PHE A 1 211 ? 24.694  -10.836 -19.026 1.00 22.52  ? 240 PHE A C   1 
ATOM   1658 O O   . PHE A 1 211 ? 23.848  -11.590 -18.591 1.00 24.51  ? 240 PHE A O   1 
ATOM   1659 C CB  . PHE A 1 211 ? 25.437  -8.732  -17.834 1.00 24.78  ? 240 PHE A CB  1 
ATOM   1660 C CG  . PHE A 1 211 ? 24.110  -8.399  -17.167 1.00 26.44  ? 240 PHE A CG  1 
ATOM   1661 C CD1 . PHE A 1 211 ? 23.477  -9.300  -16.312 1.00 25.50  ? 240 PHE A CD1 1 
ATOM   1662 C CD2 . PHE A 1 211 ? 23.507  -7.176  -17.403 1.00 28.15  ? 240 PHE A CD2 1 
ATOM   1663 C CE1 . PHE A 1 211 ? 22.282  -8.982  -15.706 1.00 25.55  ? 240 PHE A CE1 1 
ATOM   1664 C CE2 . PHE A 1 211 ? 22.316  -6.852  -16.775 1.00 30.20  ? 240 PHE A CE2 1 
ATOM   1665 C CZ  . PHE A 1 211 ? 21.707  -7.759  -15.936 1.00 29.28  ? 240 PHE A CZ  1 
ATOM   1666 N N   . THR A 1 212 ? 24.753  -10.486 -20.307 1.00 25.80  ? 241 THR A N   1 
ATOM   1667 C CA  . THR A 1 212 ? 23.802  -10.996 -21.273 1.00 26.77  ? 241 THR A CA  1 
ATOM   1668 C C   . THR A 1 212 ? 24.008  -12.508 -21.442 1.00 26.16  ? 241 THR A C   1 
ATOM   1669 O O   . THR A 1 212 ? 23.025  -13.218 -21.599 1.00 27.78  ? 241 THR A O   1 
ATOM   1670 C CB  . THR A 1 212 ? 23.845  -10.248 -22.605 1.00 26.24  ? 241 THR A CB  1 
ATOM   1671 O OG1 . THR A 1 212 ? 25.174  -10.325 -23.088 1.00 23.50  ? 241 THR A OG1 1 
ATOM   1672 C CG2 . THR A 1 212 ? 23.455  -8.783  -22.495 1.00 27.10  ? 241 THR A CG2 1 
ATOM   1673 N N   . ASN A 1 213 ? 25.248  -13.001 -21.391 1.00 26.14  ? 242 ASN A N   1 
ATOM   1674 C CA  . ASN A 1 213 ? 25.494  -14.441 -21.352 1.00 30.89  ? 242 ASN A CA  1 
ATOM   1675 C C   . ASN A 1 213 ? 24.751  -15.106 -20.186 1.00 33.99  ? 242 ASN A C   1 
ATOM   1676 O O   . ASN A 1 213 ? 23.991  -16.067 -20.368 1.00 39.36  ? 242 ASN A O   1 
ATOM   1677 C CB  . ASN A 1 213 ? 26.996  -14.732 -21.299 1.00 36.87  ? 242 ASN A CB  1 
ATOM   1678 C CG  . ASN A 1 213 ? 27.684  -14.607 -22.639 1.00 34.00  ? 242 ASN A CG  1 
ATOM   1679 O OD1 . ASN A 1 213 ? 27.034  -14.387 -23.667 1.00 35.86  ? 242 ASN A OD1 1 
ATOM   1680 N ND2 . ASN A 1 213 ? 28.993  -14.766 -22.654 1.00 35.84  ? 242 ASN A ND2 1 
ATOM   1681 N N   . MET A 1 214 ? 24.945  -14.573 -18.973 1.00 31.04  ? 243 MET A N   1 
ATOM   1682 C CA  . MET A 1 214 ? 24.361  -15.142 -17.772 1.00 26.82  ? 243 MET A CA  1 
ATOM   1683 C C   . MET A 1 214 ? 22.844  -15.073 -17.824 1.00 32.17  ? 243 MET A C   1 
ATOM   1684 O O   . MET A 1 214 ? 22.210  -15.942 -17.251 1.00 29.36  ? 243 MET A O   1 
ATOM   1685 C CB  . MET A 1 214 ? 24.864  -14.428 -16.510 1.00 29.73  ? 243 MET A CB  1 
ATOM   1686 C CG  . MET A 1 214 ? 26.320  -14.710 -16.190 1.00 29.86  ? 243 MET A CG  1 
ATOM   1687 S SD  . MET A 1 214 ? 26.808  -14.085 -14.569 1.00 32.66  ? 243 MET A SD  1 
ATOM   1688 C CE  . MET A 1 214 ? 27.040  -12.324 -14.818 1.00 31.16  ? 243 MET A CE  1 
ATOM   1689 N N   . LEU A 1 215 ? 22.284  -14.066 -18.526 1.00 30.98  ? 244 LEU A N   1 
ATOM   1690 C CA  . LEU A 1 215 ? 20.847  -13.918 -18.654 1.00 30.41  ? 244 LEU A CA  1 
ATOM   1691 C C   . LEU A 1 215 ? 20.285  -14.968 -19.614 1.00 35.24  ? 244 LEU A C   1 
ATOM   1692 O O   . LEU A 1 215 ? 19.119  -15.327 -19.520 1.00 35.42  ? 244 LEU A O   1 
ATOM   1693 C CB  . LEU A 1 215 ? 20.503  -12.521 -19.154 1.00 31.37  ? 244 LEU A CB  1 
ATOM   1694 C CG  . LEU A 1 215 ? 20.584  -11.369 -18.146 1.00 31.63  ? 244 LEU A CG  1 
ATOM   1695 C CD1 . LEU A 1 215 ? 20.511  -10.022 -18.868 1.00 34.83  ? 244 LEU A CD1 1 
ATOM   1696 C CD2 . LEU A 1 215 ? 19.475  -11.414 -17.103 1.00 32.19  ? 244 LEU A CD2 1 
ATOM   1697 N N   . GLY A 1 216 ? 21.097  -15.438 -20.555 1.00 43.88  ? 245 GLY A N   1 
ATOM   1698 C CA  . GLY A 1 216 ? 20.625  -16.421 -21.526 1.00 43.82  ? 245 GLY A CA  1 
ATOM   1699 C C   . GLY A 1 216 ? 20.362  -15.815 -22.906 1.00 42.44  ? 245 GLY A C   1 
ATOM   1700 O O   . GLY A 1 216 ? 19.834  -16.491 -23.779 1.00 45.85  ? 245 GLY A O   1 
ATOM   1701 N N   . TYR A 1 217 ? 20.744  -14.551 -23.104 1.00 38.69  ? 246 TYR A N   1 
ATOM   1702 C CA  . TYR A 1 217 ? 20.693  -13.908 -24.408 1.00 42.44  ? 246 TYR A CA  1 
ATOM   1703 C C   . TYR A 1 217 ? 22.061  -14.071 -25.068 1.00 48.99  ? 246 TYR A C   1 
ATOM   1704 O O   . TYR A 1 217 ? 23.092  -13.928 -24.421 1.00 71.69  ? 246 TYR A O   1 
ATOM   1705 C CB  . TYR A 1 217 ? 20.270  -12.440 -24.257 1.00 34.05  ? 246 TYR A CB  1 
ATOM   1706 C CG  . TYR A 1 217 ? 18.843  -12.287 -23.747 1.00 35.26  ? 246 TYR A CG  1 
ATOM   1707 C CD1 . TYR A 1 217 ? 18.497  -12.670 -22.446 1.00 31.12  ? 246 TYR A CD1 1 
ATOM   1708 C CD2 . TYR A 1 217 ? 17.853  -11.701 -24.534 1.00 32.16  ? 246 TYR A CD2 1 
ATOM   1709 C CE1 . TYR A 1 217 ? 17.205  -12.530 -21.978 1.00 33.77  ? 246 TYR A CE1 1 
ATOM   1710 C CE2 . TYR A 1 217 ? 16.551  -11.564 -24.069 1.00 34.65  ? 246 TYR A CE2 1 
ATOM   1711 C CZ  . TYR A 1 217 ? 16.236  -11.972 -22.786 1.00 30.83  ? 246 TYR A CZ  1 
ATOM   1712 O OH  . TYR A 1 217 ? 14.976  -11.873 -22.282 1.00 36.65  ? 246 TYR A OH  1 
ATOM   1713 N N   . THR A 1 218 ? 22.080  -14.393 -26.358 1.00 55.04  ? 247 THR A N   1 
ATOM   1714 C CA  . THR A 1 218 ? 23.330  -14.429 -27.093 1.00 56.60  ? 247 THR A CA  1 
ATOM   1715 C C   . THR A 1 218 ? 23.146  -13.716 -28.430 1.00 51.46  ? 247 THR A C   1 
ATOM   1716 O O   . THR A 1 218 ? 23.777  -14.055 -29.420 1.00 59.63  ? 247 THR A O   1 
ATOM   1717 C CB  . THR A 1 218 ? 23.757  -15.890 -27.238 1.00 64.19  ? 247 THR A CB  1 
ATOM   1718 O OG1 . THR A 1 218 ? 22.625  -16.565 -27.765 1.00 61.20  ? 247 THR A OG1 1 
ATOM   1719 C CG2 . THR A 1 218 ? 24.048  -16.573 -25.914 1.00 65.95  ? 247 THR A CG2 1 
ATOM   1720 N N   . ASP A 1 219 ? 22.275  -12.718 -28.452 1.00 47.09  ? 248 ASP A N   1 
ATOM   1721 C CA  . ASP A 1 219 ? 22.094  -11.876 -29.617 1.00 46.99  ? 248 ASP A CA  1 
ATOM   1722 C C   . ASP A 1 219 ? 23.037  -10.685 -29.464 1.00 47.59  ? 248 ASP A C   1 
ATOM   1723 O O   . ASP A 1 219 ? 22.911  -9.912  -28.516 1.00 51.43  ? 248 ASP A O   1 
ATOM   1724 C CB  . ASP A 1 219 ? 20.616  -11.525 -29.710 1.00 56.30  ? 248 ASP A CB  1 
ATOM   1725 C CG  . ASP A 1 219 ? 20.154  -10.761 -30.942 1.00 61.17  ? 248 ASP A CG  1 
ATOM   1726 O OD1 . ASP A 1 219 ? 20.886  -9.837  -31.357 1.00 63.17  ? 248 ASP A OD1 1 
ATOM   1727 O OD2 . ASP A 1 219 ? 19.038  -11.067 -31.444 1.00 67.89  ? 248 ASP A OD2 1 
ATOM   1728 N N   . HIS A 1 220 ? 24.000  -10.534 -30.381 1.00 43.01  ? 249 HIS A N   1 
ATOM   1729 C CA  . HIS A 1 220 ? 24.970  -9.452  -30.314 1.00 41.25  ? 249 HIS A CA  1 
ATOM   1730 C C   . HIS A 1 220 ? 24.296  -8.079  -30.195 1.00 43.26  ? 249 HIS A C   1 
ATOM   1731 O O   . HIS A 1 220 ? 24.854  -7.165  -29.579 1.00 41.53  ? 249 HIS A O   1 
ATOM   1732 C CB  . HIS A 1 220 ? 25.902  -9.506  -31.533 1.00 48.30  ? 249 HIS A CB  1 
ATOM   1733 C CG  . HIS A 1 220 ? 26.741  -8.278  -31.755 1.00 48.60  ? 249 HIS A CG  1 
ATOM   1734 N ND1 . HIS A 1 220 ? 27.914  -8.009  -31.072 1.00 46.51  ? 249 HIS A ND1 1 
ATOM   1735 C CD2 . HIS A 1 220 ? 26.558  -7.254  -32.602 1.00 41.87  ? 249 HIS A CD2 1 
ATOM   1736 C CE1 . HIS A 1 220 ? 28.429  -6.870  -31.515 1.00 43.45  ? 249 HIS A CE1 1 
ATOM   1737 N NE2 . HIS A 1 220 ? 27.622  -6.391  -32.451 1.00 44.97  ? 249 HIS A NE2 1 
ATOM   1738 N N   . GLN A 1 221 ? 23.108  -7.918  -30.793 1.00 37.45  ? 250 GLN A N   1 
ATOM   1739 C CA  . GLN A 1 221 ? 22.433  -6.629  -30.812 1.00 43.31  ? 250 GLN A CA  1 
ATOM   1740 C C   . GLN A 1 221 ? 21.881  -6.309  -29.430 1.00 33.12  ? 250 GLN A C   1 
ATOM   1741 O O   . GLN A 1 221 ? 21.787  -5.148  -29.073 1.00 37.41  ? 250 GLN A O   1 
ATOM   1742 C CB  . GLN A 1 221 ? 21.256  -6.502  -31.791 1.00 47.17  ? 250 GLN A CB  1 
ATOM   1743 C CG  . GLN A 1 221 ? 21.684  -6.244  -33.232 1.00 56.66  ? 250 GLN A CG  1 
ATOM   1744 C CD  . GLN A 1 221 ? 22.819  -5.248  -33.351 1.00 64.54  ? 250 GLN A CD  1 
ATOM   1745 O OE1 . GLN A 1 221 ? 22.768  -4.135  -32.811 1.00 67.53  ? 250 GLN A OE1 1 
ATOM   1746 N NE2 . GLN A 1 221 ? 23.874  -5.647  -34.049 1.00 70.07  ? 250 GLN A NE2 1 
ATOM   1747 N N   . PHE A 1 222 ? 21.464  -7.350  -28.721 1.00 35.85  ? 251 PHE A N   1 
ATOM   1748 C CA  . PHE A 1 222 ? 20.919  -7.201  -27.390 1.00 32.76  ? 251 PHE A CA  1 
ATOM   1749 C C   . PHE A 1 222 ? 22.055  -6.866  -26.423 1.00 33.15  ? 251 PHE A C   1 
ATOM   1750 O O   . PHE A 1 222 ? 21.860  -6.098  -25.488 1.00 33.53  ? 251 PHE A O   1 
ATOM   1751 C CB  . PHE A 1 222 ? 20.153  -8.439  -26.952 1.00 31.53  ? 251 PHE A CB  1 
ATOM   1752 C CG  . PHE A 1 222 ? 19.569  -8.247  -25.554 1.00 35.05  ? 251 PHE A CG  1 
ATOM   1753 C CD1 . PHE A 1 222 ? 18.506  -7.361  -25.339 1.00 34.64  ? 251 PHE A CD1 1 
ATOM   1754 C CD2 . PHE A 1 222 ? 20.086  -8.938  -24.463 1.00 33.98  ? 251 PHE A CD2 1 
ATOM   1755 C CE1 . PHE A 1 222 ? 17.984  -7.174  -24.065 1.00 35.24  ? 251 PHE A CE1 1 
ATOM   1756 C CE2 . PHE A 1 222 ? 19.569  -8.738  -23.186 1.00 35.45  ? 251 PHE A CE2 1 
ATOM   1757 C CZ  . PHE A 1 222 ? 18.520  -7.857  -22.990 1.00 34.95  ? 251 PHE A CZ  1 
ATOM   1758 N N   . THR A 1 223 ? 23.242  -7.422  -26.667 1.00 29.18  ? 252 THR A N   1 
ATOM   1759 C CA  . THR A 1 223 ? 24.415  -7.039  -25.902 1.00 31.04  ? 252 THR A CA  1 
ATOM   1760 C C   . THR A 1 223 ? 24.718  -5.562  -26.146 1.00 30.27  ? 252 THR A C   1 
ATOM   1761 O O   . THR A 1 223 ? 25.040  -4.850  -25.210 1.00 30.59  ? 252 THR A O   1 
ATOM   1762 C CB  . THR A 1 223 ? 25.599  -7.961  -26.208 1.00 27.89  ? 252 THR A CB  1 
ATOM   1763 O OG1 . THR A 1 223 ? 25.130  -9.238  -25.790 1.00 26.09  ? 252 THR A OG1 1 
ATOM   1764 C CG2 . THR A 1 223 ? 26.838  -7.560  -25.422 1.00 30.50  ? 252 THR A CG2 1 
ATOM   1765 N N   . GLU A 1 224 ? 24.647  -5.103  -27.395 1.00 31.15  ? 253 GLU A N   1 
ATOM   1766 C CA  . GLU A 1 224 ? 24.968  -3.721  -27.724 1.00 31.33  ? 253 GLU A CA  1 
ATOM   1767 C C   . GLU A 1 224 ? 23.955  -2.768  -27.087 1.00 30.21  ? 253 GLU A C   1 
ATOM   1768 O O   . GLU A 1 224 ? 24.328  -1.675  -26.638 1.00 31.46  ? 253 GLU A O   1 
ATOM   1769 C CB  . GLU A 1 224 ? 25.007  -3.563  -29.241 1.00 32.77  ? 253 GLU A CB  1 
ATOM   1770 C CG  . GLU A 1 224 ? 26.290  -4.126  -29.827 1.00 34.36  ? 253 GLU A CG  1 
ATOM   1771 C CD  . GLU A 1 224 ? 27.404  -3.130  -29.571 1.00 35.44  ? 253 GLU A CD  1 
ATOM   1772 O OE1 . GLU A 1 224 ? 28.272  -3.330  -28.682 1.00 34.37  ? 253 GLU A OE1 1 
ATOM   1773 O OE2 . GLU A 1 224 ? 27.370  -2.123  -30.299 1.00 44.86  ? 253 GLU A OE2 1 
ATOM   1774 N N   . LEU A 1 225 ? 22.682  -3.190  -27.061 1.00 27.65  ? 254 LEU A N   1 
ATOM   1775 C CA  . LEU A 1 225 ? 21.622  -2.479  -26.356 1.00 27.43  ? 254 LEU A CA  1 
ATOM   1776 C C   . LEU A 1 225 ? 21.967  -2.379  -24.860 1.00 26.78  ? 254 LEU A C   1 
ATOM   1777 O O   . LEU A 1 225 ? 21.802  -1.314  -24.277 1.00 25.56  ? 254 LEU A O   1 
ATOM   1778 C CB  . LEU A 1 225 ? 20.260  -3.151  -26.498 1.00 28.55  ? 254 LEU A CB  1 
ATOM   1779 C CG  . LEU A 1 225 ? 19.101  -2.463  -25.753 1.00 26.75  ? 254 LEU A CG  1 
ATOM   1780 C CD1 . LEU A 1 225 ? 18.979  -1.005  -26.132 1.00 29.44  ? 254 LEU A CD1 1 
ATOM   1781 C CD2 . LEU A 1 225 ? 17.774  -3.147  -26.001 1.00 26.76  ? 254 LEU A CD2 1 
ATOM   1782 N N   . THR A 1 226 ? 22.386  -3.493  -24.252 1.00 26.71  ? 255 THR A N   1 
ATOM   1783 C CA  . THR A 1 226 ? 22.679  -3.546  -22.825 1.00 28.93  ? 255 THR A CA  1 
ATOM   1784 C C   . THR A 1 226 ? 23.813  -2.575  -22.493 1.00 32.46  ? 255 THR A C   1 
ATOM   1785 O O   . THR A 1 226 ? 23.742  -1.834  -21.516 1.00 33.09  ? 255 THR A O   1 
ATOM   1786 C CB  . THR A 1 226 ? 23.028  -4.963  -22.405 1.00 28.53  ? 255 THR A CB  1 
ATOM   1787 O OG1 . THR A 1 226 ? 21.844  -5.717  -22.597 1.00 27.13  ? 255 THR A OG1 1 
ATOM   1788 C CG2 . THR A 1 226 ? 23.467  -5.044  -20.956 1.00 29.00  ? 255 THR A CG2 1 
ATOM   1789 N N   . ARG A 1 227 ? 24.854  -2.570  -23.328 1.00 24.65  ? 256 ARG A N   1 
ATOM   1790 C CA  . ARG A 1 227 ? 25.970  -1.671  -23.127 1.00 24.23  ? 256 ARG A CA  1 
ATOM   1791 C C   . ARG A 1 227 ? 25.491  -0.218  -23.136 1.00 26.12  ? 256 ARG A C   1 
ATOM   1792 O O   . ARG A 1 227 ? 25.900  0.594   -22.300 1.00 26.80  ? 256 ARG A O   1 
ATOM   1793 C CB  . ARG A 1 227 ? 26.985  -1.906  -24.251 1.00 22.62  ? 256 ARG A CB  1 
ATOM   1794 C CG  . ARG A 1 227 ? 27.684  -3.247  -24.208 1.00 24.64  ? 256 ARG A CG  1 
ATOM   1795 C CD  . ARG A 1 227 ? 28.615  -3.466  -25.417 1.00 26.52  ? 256 ARG A CD  1 
ATOM   1796 N NE  . ARG A 1 227 ? 29.438  -4.669  -25.215 1.00 31.54  ? 256 ARG A NE  1 
ATOM   1797 C CZ  . ARG A 1 227 ? 29.623  -5.661  -26.110 1.00 35.07  ? 256 ARG A CZ  1 
ATOM   1798 N NH1 . ARG A 1 227 ? 29.160  -5.576  -27.355 1.00 35.81  ? 256 ARG A NH1 1 
ATOM   1799 N NH2 . ARG A 1 227 ? 30.303  -6.727  -25.763 1.00 29.31  ? 256 ARG A NH2 1 
ATOM   1800 N N   . LEU A 1 228 ? 24.640  0.114   -24.109 1.00 24.45  ? 257 LEU A N   1 
ATOM   1801 C CA  . LEU A 1 228 ? 24.077  1.446   -24.234 1.00 29.01  ? 257 LEU A CA  1 
ATOM   1802 C C   . LEU A 1 228 ? 23.166  1.742   -23.036 1.00 28.92  ? 257 LEU A C   1 
ATOM   1803 O O   . LEU A 1 228 ? 23.239  2.824   -22.457 1.00 29.32  ? 257 LEU A O   1 
ATOM   1804 C CB  . LEU A 1 228 ? 23.328  1.558   -25.563 1.00 30.16  ? 257 LEU A CB  1 
ATOM   1805 C CG  . LEU A 1 228 ? 22.628  2.900   -25.793 1.00 32.91  ? 257 LEU A CG  1 
ATOM   1806 C CD1 . LEU A 1 228 ? 23.681  3.976   -25.913 1.00 32.34  ? 257 LEU A CD1 1 
ATOM   1807 C CD2 . LEU A 1 228 ? 21.712  2.922   -27.004 1.00 32.89  ? 257 LEU A CD2 1 
ATOM   1808 N N   . TYR A 1 229 ? 22.293  0.790   -22.682 1.00 24.69  ? 258 TYR A N   1 
ATOM   1809 C CA  . TYR A 1 229 ? 21.333  0.994   -21.610 1.00 26.02  ? 258 TYR A CA  1 
ATOM   1810 C C   . TYR A 1 229 ? 22.049  1.196   -20.259 1.00 27.08  ? 258 TYR A C   1 
ATOM   1811 O O   . TYR A 1 229 ? 21.700  2.082   -19.492 1.00 24.28  ? 258 TYR A O   1 
ATOM   1812 C CB  . TYR A 1 229 ? 20.362  -0.187  -21.600 1.00 26.44  ? 258 TYR A CB  1 
ATOM   1813 C CG  . TYR A 1 229 ? 19.317  -0.115  -20.499 1.00 28.72  ? 258 TYR A CG  1 
ATOM   1814 C CD1 . TYR A 1 229 ? 19.693  -0.302  -19.181 1.00 29.63  ? 258 TYR A CD1 1 
ATOM   1815 C CD2 . TYR A 1 229 ? 17.979  0.145   -20.765 1.00 29.99  ? 258 TYR A CD2 1 
ATOM   1816 C CE1 . TYR A 1 229 ? 18.787  -0.267  -18.153 1.00 30.50  ? 258 TYR A CE1 1 
ATOM   1817 C CE2 . TYR A 1 229 ? 17.047  0.165   -19.742 1.00 32.37  ? 258 TYR A CE2 1 
ATOM   1818 C CZ  . TYR A 1 229 ? 17.456  -0.042  -18.434 1.00 31.37  ? 258 TYR A CZ  1 
ATOM   1819 O OH  . TYR A 1 229 ? 16.602  -0.020  -17.367 1.00 36.69  ? 258 TYR A OH  1 
ATOM   1820 N N   . LEU A 1 230 ? 23.039  0.348   -19.955 1.00 26.69  ? 259 LEU A N   1 
ATOM   1821 C CA  . LEU A 1 230 ? 23.772  0.456   -18.709 1.00 25.04  ? 259 LEU A CA  1 
ATOM   1822 C C   . LEU A 1 230 ? 24.577  1.750   -18.665 1.00 25.18  ? 259 LEU A C   1 
ATOM   1823 O O   . LEU A 1 230 ? 24.786  2.351   -17.616 1.00 23.56  ? 259 LEU A O   1 
ATOM   1824 C CB  . LEU A 1 230 ? 24.634  -0.784  -18.504 1.00 23.93  ? 259 LEU A CB  1 
ATOM   1825 C CG  . LEU A 1 230 ? 23.868  -2.098  -18.349 1.00 22.64  ? 259 LEU A CG  1 
ATOM   1826 C CD1 . LEU A 1 230 ? 24.805  -3.245  -18.109 1.00 22.96  ? 259 LEU A CD1 1 
ATOM   1827 C CD2 . LEU A 1 230 ? 22.799  -2.054  -17.251 1.00 23.60  ? 259 LEU A CD2 1 
ATOM   1828 N N   . THR A 1 231 ? 25.021  2.234   -19.803 1.00 23.00  ? 260 THR A N   1 
ATOM   1829 C CA  . THR A 1 231 ? 25.762  3.473   -19.795 1.00 23.49  ? 260 THR A CA  1 
ATOM   1830 C C   . THR A 1 231 ? 24.842  4.654   -19.469 1.00 25.93  ? 260 THR A C   1 
ATOM   1831 O O   . THR A 1 231 ? 25.230  5.542   -18.726 1.00 25.85  ? 260 THR A O   1 
ATOM   1832 C CB  . THR A 1 231 ? 26.505  3.644   -21.115 1.00 25.75  ? 260 THR A CB  1 
ATOM   1833 O OG1 . THR A 1 231 ? 27.516  2.627   -21.067 1.00 29.70  ? 260 THR A OG1 1 
ATOM   1834 C CG2 . THR A 1 231 ? 27.105  5.042   -21.208 1.00 22.29  ? 260 THR A CG2 1 
ATOM   1835 N N   . ILE A 1 232 ? 23.635  4.692   -20.027 1.00 27.36  ? 261 ILE A N   1 
ATOM   1836 C CA  . ILE A 1 232 ? 22.856  5.934   -20.021 1.00 28.62  ? 261 ILE A CA  1 
ATOM   1837 C C   . ILE A 1 232 ? 21.993  6.077   -18.764 1.00 26.62  ? 261 ILE A C   1 
ATOM   1838 O O   . ILE A 1 232 ? 21.533  7.172   -18.471 1.00 23.91  ? 261 ILE A O   1 
ATOM   1839 C CB  . ILE A 1 232 ? 21.971  6.124   -21.272 1.00 27.80  ? 261 ILE A CB  1 
ATOM   1840 C CG1 . ILE A 1 232 ? 20.820  5.132   -21.379 1.00 30.31  ? 261 ILE A CG1 1 
ATOM   1841 C CG2 . ILE A 1 232 ? 22.809  6.156   -22.557 1.00 27.72  ? 261 ILE A CG2 1 
ATOM   1842 C CD1 . ILE A 1 232 ? 19.848  5.449   -22.513 1.00 31.89  ? 261 ILE A CD1 1 
ATOM   1843 N N   . HIS A 1 233 ? 21.700  4.971   -18.078 1.00 25.56  ? 262 HIS A N   1 
ATOM   1844 C CA  . HIS A 1 233 ? 20.922  5.017   -16.850 1.00 24.22  ? 262 HIS A CA  1 
ATOM   1845 C C   . HIS A 1 233 ? 21.832  5.188   -15.634 1.00 21.27  ? 262 HIS A C   1 
ATOM   1846 O O   . HIS A 1 233 ? 21.349  5.208   -14.480 1.00 23.33  ? 262 HIS A O   1 
ATOM   1847 C CB  . HIS A 1 233 ? 20.052  3.753   -16.743 1.00 24.56  ? 262 HIS A CB  1 
ATOM   1848 C CG  . HIS A 1 233 ? 18.897  3.682   -17.681 1.00 28.79  ? 262 HIS A CG  1 
ATOM   1849 N ND1 . HIS A 1 233 ? 19.027  3.526   -19.047 1.00 30.92  ? 262 HIS A ND1 1 
ATOM   1850 C CD2 . HIS A 1 233 ? 17.580  3.715   -17.435 1.00 33.70  ? 262 HIS A CD2 1 
ATOM   1851 C CE1 . HIS A 1 233 ? 17.822  3.484   -19.593 1.00 33.00  ? 262 HIS A CE1 1 
ATOM   1852 N NE2 . HIS A 1 233 ? 16.929  3.614   -18.628 1.00 33.22  ? 262 HIS A NE2 1 
ATOM   1853 N N   . SER A 1 234 ? 23.137  5.334   -15.885 1.00 24.23  ? 263 SER A N   1 
ATOM   1854 C CA  . SER A 1 234 ? 24.172  5.205   -14.860 1.00 21.82  ? 263 SER A CA  1 
ATOM   1855 C C   . SER A 1 234 ? 24.055  6.232   -13.746 1.00 23.31  ? 263 SER A C   1 
ATOM   1856 O O   . SER A 1 234 ? 24.316  5.910   -12.594 1.00 19.35  ? 263 SER A O   1 
ATOM   1857 C CB  . SER A 1 234 ? 25.534  5.274   -15.476 1.00 23.05  ? 263 SER A CB  1 
ATOM   1858 O OG  . SER A 1 234 ? 25.722  6.561   -16.048 1.00 28.08  ? 263 SER A OG  1 
ATOM   1859 N N   . ASP A 1 235 ? 23.678  7.477   -14.087 1.00 20.64  ? 264 ASP A N   1 
ATOM   1860 C CA  . ASP A 1 235 ? 23.667  8.548   -13.114 1.00 21.86  ? 264 ASP A CA  1 
ATOM   1861 C C   . ASP A 1 235 ? 22.751  9.646   -13.622 1.00 21.73  ? 264 ASP A C   1 
ATOM   1862 O O   . ASP A 1 235 ? 22.620  9.804   -14.839 1.00 20.20  ? 264 ASP A O   1 
ATOM   1863 C CB  . ASP A 1 235 ? 25.084  9.041   -12.872 1.00 23.55  ? 264 ASP A CB  1 
ATOM   1864 C CG  . ASP A 1 235 ? 25.355  9.628   -11.500 1.00 24.03  ? 264 ASP A CG  1 
ATOM   1865 O OD1 . ASP A 1 235 ? 24.828  9.081   -10.525 1.00 27.17  ? 264 ASP A OD1 1 
ATOM   1866 O OD2 . ASP A 1 235 ? 26.091  10.623  -11.439 1.00 30.87  ? 264 ASP A OD2 1 
ATOM   1867 N N   . HIS A 1 236 ? 22.019  10.287  -12.706 1.00 20.30  ? 265 HIS A N   1 
ATOM   1868 C CA  . HIS A 1 236 ? 21.168  11.396  -13.110 1.00 22.93  ? 265 HIS A CA  1 
ATOM   1869 C C   . HIS A 1 236 ? 21.133  12.472  -12.027 1.00 21.51  ? 265 HIS A C   1 
ATOM   1870 O O   . HIS A 1 236 ? 20.061  12.855  -11.569 1.00 22.60  ? 265 HIS A O   1 
ATOM   1871 C CB  . HIS A 1 236 ? 19.747  10.909  -13.433 1.00 23.91  ? 265 HIS A CB  1 
ATOM   1872 C CG  . HIS A 1 236 ? 19.150  11.665  -14.561 1.00 29.42  ? 265 HIS A CG  1 
ATOM   1873 N ND1 . HIS A 1 236 ? 17.961  12.372  -14.481 1.00 35.05  ? 265 HIS A ND1 1 
ATOM   1874 C CD2 . HIS A 1 236 ? 19.613  11.854  -15.817 1.00 30.00  ? 265 HIS A CD2 1 
ATOM   1875 C CE1 . HIS A 1 236 ? 17.711  12.939  -15.659 1.00 35.43  ? 265 HIS A CE1 1 
ATOM   1876 N NE2 . HIS A 1 236 ? 18.702  12.631  -16.489 1.00 34.38  ? 265 HIS A NE2 1 
ATOM   1877 N N   . GLU A 1 237 ? 22.310  12.947  -11.605 1.00 21.19  ? 266 GLU A N   1 
ATOM   1878 C CA  . GLU A 1 237 ? 22.427  13.905  -10.507 1.00 25.38  ? 266 GLU A CA  1 
ATOM   1879 C C   . GLU A 1 237 ? 22.221  13.234  -9.137  1.00 21.92  ? 266 GLU A C   1 
ATOM   1880 O O   . GLU A 1 237 ? 21.972  12.023  -9.025  1.00 18.85  ? 266 GLU A O   1 
ATOM   1881 C CB  . GLU A 1 237 ? 21.461  15.084  -10.657 1.00 28.91  ? 266 GLU A CB  1 
ATOM   1882 C CG  . GLU A 1 237 ? 22.092  16.311  -11.259 1.00 36.25  ? 266 GLU A CG  1 
ATOM   1883 C CD  . GLU A 1 237 ? 21.088  17.442  -11.201 1.00 43.14  ? 266 GLU A CD  1 
ATOM   1884 O OE1 . GLU A 1 237 ? 20.008  17.327  -10.545 1.00 44.54  ? 266 GLU A OE1 1 
ATOM   1885 O OE2 . GLU A 1 237 ? 21.450  18.453  -11.836 1.00 44.86  ? 266 GLU A OE2 1 
ATOM   1886 N N   . GLY A 1 238 ? 22.305  14.039  -8.071  1.00 18.52  ? 267 GLY A N   1 
ATOM   1887 C CA  . GLY A 1 238 ? 22.204  13.500  -6.734  1.00 19.54  ? 267 GLY A CA  1 
ATOM   1888 C C   . GLY A 1 238 ? 20.794  13.580  -6.159  1.00 18.59  ? 267 GLY A C   1 
ATOM   1889 O O   . GLY A 1 238 ? 20.529  12.945  -5.151  1.00 18.72  ? 267 GLY A O   1 
ATOM   1890 N N   . GLY A 1 239 ? 19.899  14.314  -6.817  1.00 17.49  ? 268 GLY A N   1 
ATOM   1891 C CA  . GLY A 1 239 ? 18.577  14.611  -6.280  1.00 17.35  ? 268 GLY A CA  1 
ATOM   1892 C C   . GLY A 1 239 ? 17.494  13.564  -6.571  1.00 17.84  ? 268 GLY A C   1 
ATOM   1893 O O   . GLY A 1 239 ? 16.438  13.593  -5.946  1.00 21.33  ? 268 GLY A O   1 
ATOM   1894 N N   . ASN A 1 240 ? 17.731  12.640  -7.497  1.00 21.75  ? 269 ASN A N   1 
ATOM   1895 C CA  . ASN A 1 240 ? 16.765  11.571  -7.732  1.00 22.34  ? 269 ASN A CA  1 
ATOM   1896 C C   . ASN A 1 240 ? 16.809  10.648  -6.516  1.00 21.01  ? 269 ASN A C   1 
ATOM   1897 O O   . ASN A 1 240 ? 17.820  10.604  -5.819  1.00 17.19  ? 269 ASN A O   1 
ATOM   1898 C CB  . ASN A 1 240 ? 17.049  10.799  -9.013  1.00 24.23  ? 269 ASN A CB  1 
ATOM   1899 C CG  . ASN A 1 240 ? 18.321  9.998   -8.981  1.00 24.39  ? 269 ASN A CG  1 
ATOM   1900 O OD1 . ASN A 1 240 ? 18.384  8.923   -8.366  1.00 23.42  ? 269 ASN A OD1 1 
ATOM   1901 N ND2 . ASN A 1 240 ? 19.354  10.526  -9.616  1.00 25.71  ? 269 ASN A ND2 1 
ATOM   1902 N N   . VAL A 1 241 ? 15.721  9.918   -6.277  1.00 17.73  ? 270 VAL A N   1 
ATOM   1903 C CA  . VAL A 1 241 ? 15.542  9.228   -5.014  1.00 18.68  ? 270 VAL A CA  1 
ATOM   1904 C C   . VAL A 1 241 ? 16.600  8.144   -4.847  1.00 17.29  ? 270 VAL A C   1 
ATOM   1905 O O   . VAL A 1 241 ? 17.102  7.990   -3.744  1.00 17.79  ? 270 VAL A O   1 
ATOM   1906 C CB  . VAL A 1 241 ? 14.124  8.632   -4.960  1.00 20.93  ? 270 VAL A CB  1 
ATOM   1907 C CG1 . VAL A 1 241 ? 13.965  7.594   -3.855  1.00 22.40  ? 270 VAL A CG1 1 
ATOM   1908 C CG2 . VAL A 1 241 ? 13.128  9.739   -4.783  1.00 25.55  ? 270 VAL A CG2 1 
ATOM   1909 N N   . SER A 1 242 ? 16.949  7.439   -5.926  1.00 17.75  ? 271 SER A N   1 
ATOM   1910 C CA  . SER A 1 242 ? 17.966  6.389   -5.828  1.00 19.67  ? 271 SER A CA  1 
ATOM   1911 C C   . SER A 1 242 ? 19.339  6.942   -5.452  1.00 19.01  ? 271 SER A C   1 
ATOM   1912 O O   . SER A 1 242 ? 19.984  6.454   -4.503  1.00 16.67  ? 271 SER A O   1 
ATOM   1913 C CB  . SER A 1 242 ? 17.979  5.430   -7.016  1.00 21.00  ? 271 SER A CB  1 
ATOM   1914 O OG  . SER A 1 242 ? 18.331  6.018   -8.243  1.00 22.47  ? 271 SER A OG  1 
ATOM   1915 N N   . ALA A 1 243 ? 19.768  8.034   -6.084  1.00 19.65  ? 272 ALA A N   1 
ATOM   1916 C CA  . ALA A 1 243 ? 21.094  8.569   -5.768  1.00 18.40  ? 272 ALA A CA  1 
ATOM   1917 C C   . ALA A 1 243 ? 21.063  9.199   -4.388  1.00 17.34  ? 272 ALA A C   1 
ATOM   1918 O O   . ALA A 1 243 ? 21.959  9.022   -3.583  1.00 16.18  ? 272 ALA A O   1 
ATOM   1919 C CB  . ALA A 1 243 ? 21.525  9.609   -6.741  1.00 20.67  ? 272 ALA A CB  1 
ATOM   1920 N N   . HIS A 1 244 ? 20.032  9.983   -4.148  1.00 16.84  ? 273 HIS A N   1 
ATOM   1921 C CA  . HIS A 1 244 ? 19.879  10.601  -2.849  1.00 18.05  ? 273 HIS A CA  1 
ATOM   1922 C C   . HIS A 1 244 ? 19.836  9.572   -1.713  1.00 15.34  ? 273 HIS A C   1 
ATOM   1923 O O   . HIS A 1 244 ? 20.394  9.830   -0.673  1.00 15.60  ? 273 HIS A O   1 
ATOM   1924 C CB  . HIS A 1 244 ? 18.731  11.592  -2.876  1.00 18.37  ? 273 HIS A CB  1 
ATOM   1925 C CG  . HIS A 1 244 ? 18.576  12.426  -1.638  1.00 19.68  ? 273 HIS A CG  1 
ATOM   1926 N ND1 . HIS A 1 244 ? 17.378  13.055  -1.368  1.00 19.77  ? 273 HIS A ND1 1 
ATOM   1927 C CD2 . HIS A 1 244 ? 19.414  12.838  -0.692  1.00 21.02  ? 273 HIS A CD2 1 
ATOM   1928 C CE1 . HIS A 1 244 ? 17.473  13.694  -0.214  1.00 21.34  ? 273 HIS A CE1 1 
ATOM   1929 N NE2 . HIS A 1 244 ? 18.697  13.596  0.207   1.00 21.24  ? 273 HIS A NE2 1 
ATOM   1930 N N   . THR A 1 245 ? 19.056  8.492   -1.825  1.00 13.91  ? 274 THR A N   1 
ATOM   1931 C CA  . THR A 1 245 ? 19.023  7.481   -0.786  1.00 15.02  ? 274 THR A CA  1 
ATOM   1932 C C   . THR A 1 245 ? 20.423  6.943   -0.532  1.00 14.13  ? 274 THR A C   1 
ATOM   1933 O O   . THR A 1 245 ? 20.859  6.833   0.591   1.00 13.86  ? 274 THR A O   1 
ATOM   1934 C CB  . THR A 1 245 ? 18.027  6.390   -1.198  1.00 14.92  ? 274 THR A CB  1 
ATOM   1935 O OG1 . THR A 1 245 ? 16.730  6.975   -1.291  1.00 15.91  ? 274 THR A OG1 1 
ATOM   1936 C CG2 . THR A 1 245 ? 17.820  5.321   -0.142  1.00 16.82  ? 274 THR A CG2 1 
ATOM   1937 N N   . SER A 1 246 ? 21.170  6.684   -1.591  1.00 17.18  ? 275 SER A N   1 
ATOM   1938 C CA  . SER A 1 246 ? 22.516  6.145   -1.474  1.00 18.37  ? 275 SER A CA  1 
ATOM   1939 C C   . SER A 1 246 ? 23.419  7.147   -0.781  1.00 16.57  ? 275 SER A C   1 
ATOM   1940 O O   . SER A 1 246 ? 24.243  6.752   0.009   1.00 18.54  ? 275 SER A O   1 
ATOM   1941 C CB  . SER A 1 246 ? 23.091  5.726   -2.847  1.00 18.76  ? 275 SER A CB  1 
ATOM   1942 O OG  . SER A 1 246 ? 23.548  6.862   -3.571  1.00 21.70  ? 275 SER A OG  1 
ATOM   1943 N N   . HIS A 1 247 ? 23.233  8.435   -1.082  1.00 17.09  ? 276 HIS A N   1 
ATOM   1944 C CA  . HIS A 1 247 ? 24.058  9.493   -0.518  1.00 18.13  ? 276 HIS A CA  1 
ATOM   1945 C C   . HIS A 1 247 ? 23.750  9.597   0.979   1.00 18.37  ? 276 HIS A C   1 
ATOM   1946 O O   . HIS A 1 247 ? 24.638  9.805   1.827   1.00 17.08  ? 276 HIS A O   1 
ATOM   1947 C CB  . HIS A 1 247 ? 23.729  10.780  -1.280  1.00 20.81  ? 276 HIS A CB  1 
ATOM   1948 C CG  . HIS A 1 247 ? 24.565  11.967  -1.017  1.00 22.52  ? 276 HIS A CG  1 
ATOM   1949 N ND1 . HIS A 1 247 ? 25.888  12.090  -1.426  1.00 22.66  ? 276 HIS A ND1 1 
ATOM   1950 C CD2 . HIS A 1 247 ? 24.279  13.055  -0.268  1.00 22.17  ? 276 HIS A CD2 1 
ATOM   1951 C CE1 . HIS A 1 247 ? 26.349  13.263  -0.972  1.00 21.52  ? 276 HIS A CE1 1 
ATOM   1952 N NE2 . HIS A 1 247 ? 25.369  13.877  -0.310  1.00 20.21  ? 276 HIS A NE2 1 
ATOM   1953 N N   . LEU A 1 248 ? 22.448  9.574   1.287   1.00 18.69  ? 277 LEU A N   1 
ATOM   1954 C CA  . LEU A 1 248 ? 21.966  9.722   2.646   1.00 17.95  ? 277 LEU A CA  1 
ATOM   1955 C C   . LEU A 1 248 ? 22.432  8.559   3.536   1.00 17.09  ? 277 LEU A C   1 
ATOM   1956 O O   . LEU A 1 248 ? 23.027  8.791   4.589   1.00 16.71  ? 277 LEU A O   1 
ATOM   1957 C CB  . LEU A 1 248 ? 20.447  9.898   2.672   1.00 17.49  ? 277 LEU A CB  1 
ATOM   1958 C CG  . LEU A 1 248 ? 19.767  9.759   4.036   1.00 18.75  ? 277 LEU A CG  1 
ATOM   1959 C CD1 . LEU A 1 248 ? 20.349  10.799  4.973   1.00 20.17  ? 277 LEU A CD1 1 
ATOM   1960 C CD2 . LEU A 1 248 ? 18.258  9.923   3.933   1.00 19.86  ? 277 LEU A CD2 1 
ATOM   1961 N N   . VAL A 1 249 ? 22.187  7.321   3.116   1.00 17.16  ? 278 VAL A N   1 
ATOM   1962 C CA  . VAL A 1 249 ? 22.598  6.150   3.866   1.00 15.71  ? 278 VAL A CA  1 
ATOM   1963 C C   . VAL A 1 249 ? 24.114  6.057   3.911   1.00 16.81  ? 278 VAL A C   1 
ATOM   1964 O O   . VAL A 1 249 ? 24.694  5.820   4.968   1.00 17.01  ? 278 VAL A O   1 
ATOM   1965 C CB  . VAL A 1 249 ? 21.941  4.858   3.340   1.00 16.85  ? 278 VAL A CB  1 
ATOM   1966 C CG1 . VAL A 1 249 ? 22.562  3.592   3.961   1.00 16.28  ? 278 VAL A CG1 1 
ATOM   1967 C CG2 . VAL A 1 249 ? 20.429  4.908   3.578   1.00 18.32  ? 278 VAL A CG2 1 
ATOM   1968 N N   . GLY A 1 250 ? 24.790  6.410   2.805   1.00 16.97  ? 279 GLY A N   1 
ATOM   1969 C CA  . GLY A 1 250 ? 26.239  6.431   2.854   1.00 16.57  ? 279 GLY A CA  1 
ATOM   1970 C C   . GLY A 1 250 ? 26.853  7.384   3.891   1.00 15.92  ? 279 GLY A C   1 
ATOM   1971 O O   . GLY A 1 250 ? 27.952  7.137   4.349   1.00 14.77  ? 279 GLY A O   1 
ATOM   1972 N N   . SER A 1 251 ? 26.215  8.519   4.100   1.00 14.94  ? 280 SER A N   1 
ATOM   1973 C CA  . SER A 1 251 ? 26.738  9.605   4.910   1.00 16.73  ? 280 SER A CA  1 
ATOM   1974 C C   . SER A 1 251 ? 26.752  9.193   6.398   1.00 17.65  ? 280 SER A C   1 
ATOM   1975 O O   . SER A 1 251 ? 27.490  9.780   7.187   1.00 15.68  ? 280 SER A O   1 
ATOM   1976 C CB  . SER A 1 251 ? 25.901  10.856  4.713   1.00 18.60  ? 280 SER A CB  1 
ATOM   1977 O OG  . SER A 1 251 ? 24.623  10.679  5.339   1.00 17.94  ? 280 SER A OG  1 
ATOM   1978 N N   . ALA A 1 252 ? 26.021  8.128   6.751   1.00 16.22  ? 281 ALA A N   1 
ATOM   1979 C CA  . ALA A 1 252 ? 26.133  7.523   8.077   1.00 18.80  ? 281 ALA A CA  1 
ATOM   1980 C C   . ALA A 1 252 ? 27.202  6.437   8.129   1.00 19.77  ? 281 ALA A C   1 
ATOM   1981 O O   . ALA A 1 252 ? 27.314  5.706   9.116   1.00 19.39  ? 281 ALA A O   1 
ATOM   1982 C CB  . ALA A 1 252 ? 24.803  6.967   8.489   1.00 20.48  ? 281 ALA A CB  1 
ATOM   1983 N N   . LEU A 1 253 ? 27.956  6.302   7.034   1.00 21.21  ? 282 LEU A N   1 
ATOM   1984 C CA  . LEU A 1 253 ? 29.084  5.391   6.916   1.00 19.28  ? 282 LEU A CA  1 
ATOM   1985 C C   . LEU A 1 253 ? 28.613  3.945   6.825   1.00 21.58  ? 282 LEU A C   1 
ATOM   1986 O O   . LEU A 1 253 ? 29.387  3.017   7.077   1.00 20.43  ? 282 LEU A O   1 
ATOM   1987 C CB  . LEU A 1 253 ? 30.129  5.628   7.999   1.00 20.77  ? 282 LEU A CB  1 
ATOM   1988 C CG  . LEU A 1 253 ? 30.685  7.046   8.038   1.00 22.53  ? 282 LEU A CG  1 
ATOM   1989 C CD1 . LEU A 1 253 ? 31.783  7.169   9.094   1.00 23.71  ? 282 LEU A CD1 1 
ATOM   1990 C CD2 . LEU A 1 253 ? 31.212  7.427   6.666   1.00 25.54  ? 282 LEU A CD2 1 
ATOM   1991 N N   . SER A 1 254 ? 27.383  3.785   6.339   1.00 22.34  ? 283 SER A N   1 
ATOM   1992 C CA  . SER A 1 254 ? 26.913  2.486   5.922   1.00 25.05  ? 283 SER A CA  1 
ATOM   1993 C C   . SER A 1 254 ? 27.717  2.102   4.694   1.00 23.93  ? 283 SER A C   1 
ATOM   1994 O O   . SER A 1 254 ? 27.945  2.946   3.842   1.00 20.91  ? 283 SER A O   1 
ATOM   1995 C CB  . SER A 1 254 ? 25.447  2.523   5.577   1.00 24.92  ? 283 SER A CB  1 
ATOM   1996 O OG  . SER A 1 254 ? 24.631  2.698   6.720   1.00 21.90  ? 283 SER A OG  1 
ATOM   1997 N N   . ASP A 1 255 ? 28.082  0.818   4.598   1.00 24.27  ? 284 ASP A N   1 
ATOM   1998 C CA  . ASP A 1 255 ? 28.954  0.360   3.537   1.00 23.02  ? 284 ASP A CA  1 
ATOM   1999 C C   . ASP A 1 255 ? 28.208  0.427   2.208   1.00 19.01  ? 284 ASP A C   1 
ATOM   2000 O O   . ASP A 1 255 ? 27.020  0.734   2.129   1.00 19.46  ? 284 ASP A O   1 
ATOM   2001 C CB  . ASP A 1 255 ? 29.576  -0.988  3.898   1.00 22.77  ? 284 ASP A CB  1 
ATOM   2002 C CG  . ASP A 1 255 ? 28.572  -2.126  3.954   1.00 26.94  ? 284 ASP A CG  1 
ATOM   2003 O OD1 . ASP A 1 255 ? 27.966  -2.345  2.892   1.00 26.22  ? 284 ASP A OD1 1 
ATOM   2004 O OD2 . ASP A 1 255 ? 28.311  -2.654  5.054   1.00 23.39  ? 284 ASP A OD2 1 
ATOM   2005 N N   . PRO A 1 256 ? 28.919  0.269   1.069   1.00 18.78  ? 285 PRO A N   1 
ATOM   2006 C CA  . PRO A 1 256 ? 28.275  0.353   -0.238  1.00 17.99  ? 285 PRO A CA  1 
ATOM   2007 C C   . PRO A 1 256 ? 27.144  -0.632  -0.470  1.00 18.02  ? 285 PRO A C   1 
ATOM   2008 O O   . PRO A 1 256 ? 26.209  -0.349  -1.204  1.00 17.50  ? 285 PRO A O   1 
ATOM   2009 C CB  . PRO A 1 256 ? 29.428  0.080   -1.135  1.00 18.20  ? 285 PRO A CB  1 
ATOM   2010 C CG  . PRO A 1 256 ? 30.595  0.670   -0.377  1.00 19.25  ? 285 PRO A CG  1 
ATOM   2011 C CD  . PRO A 1 256 ? 30.373  0.075   0.987   1.00 18.97  ? 285 PRO A CD  1 
ATOM   2012 N N   . TYR A 1 257 ? 27.261  -1.830  0.085   1.00 17.40  ? 286 TYR A N   1 
ATOM   2013 C CA  . TYR A 1 257 ? 26.171  -2.783  -0.065  1.00 20.41  ? 286 TYR A CA  1 
ATOM   2014 C C   . TYR A 1 257 ? 24.881  -2.244  0.581   1.00 21.57  ? 286 TYR A C   1 
ATOM   2015 O O   . TYR A 1 257 ? 23.820  -2.257  -0.013  1.00 21.76  ? 286 TYR A O   1 
ATOM   2016 C CB  . TYR A 1 257 ? 26.593  -4.123  0.557   1.00 20.59  ? 286 TYR A CB  1 
ATOM   2017 C CG  . TYR A 1 257 ? 27.777  -4.775  -0.122  1.00 19.70  ? 286 TYR A CG  1 
ATOM   2018 C CD1 . TYR A 1 257 ? 27.585  -5.664  -1.162  1.00 23.82  ? 286 TYR A CD1 1 
ATOM   2019 C CD2 . TYR A 1 257 ? 29.088  -4.541  0.276   1.00 23.73  ? 286 TYR A CD2 1 
ATOM   2020 C CE1 . TYR A 1 257 ? 28.654  -6.264  -1.813  1.00 23.44  ? 286 TYR A CE1 1 
ATOM   2021 C CE2 . TYR A 1 257 ? 30.169  -5.149  -0.362  1.00 20.45  ? 286 TYR A CE2 1 
ATOM   2022 C CZ  . TYR A 1 257 ? 29.949  -6.019  -1.416  1.00 22.59  ? 286 TYR A CZ  1 
ATOM   2023 O OH  . TYR A 1 257 ? 30.990  -6.671  -2.075  1.00 23.50  ? 286 TYR A OH  1 
ATOM   2024 N N   . LEU A 1 258 ? 24.944  -1.774  1.836   1.00 18.34  ? 287 LEU A N   1 
ATOM   2025 C CA  . LEU A 1 258 ? 23.766  -1.235  2.489   1.00 19.42  ? 287 LEU A CA  1 
ATOM   2026 C C   . LEU A 1 258 ? 23.232  0.040   1.824   1.00 20.51  ? 287 LEU A C   1 
ATOM   2027 O O   . LEU A 1 258 ? 22.022  0.209   1.702   1.00 16.83  ? 287 LEU A O   1 
ATOM   2028 C CB  . LEU A 1 258 ? 24.132  -0.968  3.936   1.00 20.81  ? 287 LEU A CB  1 
ATOM   2029 C CG  . LEU A 1 258 ? 24.555  -2.198  4.728   1.00 21.60  ? 287 LEU A CG  1 
ATOM   2030 C CD1 . LEU A 1 258 ? 24.668  -1.718  6.165   1.00 23.45  ? 287 LEU A CD1 1 
ATOM   2031 C CD2 . LEU A 1 258 ? 23.613  -3.347  4.555   1.00 22.91  ? 287 LEU A CD2 1 
ATOM   2032 N N   . SER A 1 259 ? 24.131  0.899   1.334   1.00 17.02  ? 288 SER A N   1 
ATOM   2033 C CA  . SER A 1 259 ? 23.750  2.145   0.700   1.00 17.80  ? 288 SER A CA  1 
ATOM   2034 C C   . SER A 1 259 ? 23.045  1.844   -0.610  1.00 18.35  ? 288 SER A C   1 
ATOM   2035 O O   . SER A 1 259 ? 22.081  2.495   -0.956  1.00 18.52  ? 288 SER A O   1 
ATOM   2036 C CB  . SER A 1 259 ? 24.969  2.982   0.457   1.00 19.56  ? 288 SER A CB  1 
ATOM   2037 O OG  . SER A 1 259 ? 25.647  3.150   1.689   1.00 25.09  ? 288 SER A OG  1 
ATOM   2038 N N   . PHE A 1 260 ? 23.549  0.846   -1.331  1.00 17.90  ? 289 PHE A N   1 
ATOM   2039 C CA  . PHE A 1 260 ? 23.016  0.511   -2.635  1.00 19.64  ? 289 PHE A CA  1 
ATOM   2040 C C   . PHE A 1 260 ? 21.679  -0.217  -2.466  1.00 20.22  ? 289 PHE A C   1 
ATOM   2041 O O   . PHE A 1 260 ? 20.703  0.148   -3.122  1.00 17.61  ? 289 PHE A O   1 
ATOM   2042 C CB  . PHE A 1 260 ? 24.016  -0.238  -3.507  1.00 19.76  ? 289 PHE A CB  1 
ATOM   2043 C CG  . PHE A 1 260 ? 23.455  -0.584  -4.877  1.00 21.00  ? 289 PHE A CG  1 
ATOM   2044 C CD1 . PHE A 1 260 ? 23.380  0.360   -5.879  1.00 20.21  ? 289 PHE A CD1 1 
ATOM   2045 C CD2 . PHE A 1 260 ? 23.014  -1.870  -5.159  1.00 22.86  ? 289 PHE A CD2 1 
ATOM   2046 C CE1 . PHE A 1 260 ? 22.833  0.037   -7.115  1.00 20.68  ? 289 PHE A CE1 1 
ATOM   2047 C CE2 . PHE A 1 260 ? 22.476  -2.169  -6.392  1.00 23.95  ? 289 PHE A CE2 1 
ATOM   2048 C CZ  . PHE A 1 260 ? 22.414  -1.223  -7.375  1.00 18.75  ? 289 PHE A CZ  1 
ATOM   2049 N N   . ALA A 1 261 ? 21.576  -1.131  -1.500  1.00 19.25  ? 290 ALA A N   1 
ATOM   2050 C CA  . ALA A 1 261 ? 20.301  -1.812  -1.310  1.00 19.23  ? 290 ALA A CA  1 
ATOM   2051 C C   . ALA A 1 261 ? 19.207  -0.846  -0.890  1.00 18.85  ? 290 ALA A C   1 
ATOM   2052 O O   . ALA A 1 261 ? 18.038  -0.998  -1.272  1.00 21.27  ? 290 ALA A O   1 
ATOM   2053 C CB  . ALA A 1 261 ? 20.453  -2.936  -0.319  1.00 19.13  ? 290 ALA A CB  1 
ATOM   2054 N N   . ALA A 1 262 ? 19.589  0.175   -0.141  1.00 19.12  ? 291 ALA A N   1 
ATOM   2055 C CA  . ALA A 1 262 ? 18.650  1.213   0.248   1.00 20.27  ? 291 ALA A CA  1 
ATOM   2056 C C   . ALA A 1 262 ? 18.189  1.950   -0.989  1.00 18.67  ? 291 ALA A C   1 
ATOM   2057 O O   . ALA A 1 262 ? 16.999  2.210   -1.118  1.00 17.32  ? 291 ALA A O   1 
ATOM   2058 C CB  . ALA A 1 262 ? 19.232  2.203   1.263   1.00 21.14  ? 291 ALA A CB  1 
ATOM   2059 N N   . ALA A 1 263 ? 19.135  2.295   -1.868  1.00 18.15  ? 292 ALA A N   1 
ATOM   2060 C CA  . ALA A 1 263 ? 18.809  3.020   -3.088  1.00 18.26  ? 292 ALA A CA  1 
ATOM   2061 C C   . ALA A 1 263 ? 17.843  2.237   -3.974  1.00 18.42  ? 292 ALA A C   1 
ATOM   2062 O O   . ALA A 1 263 ? 16.946  2.815   -4.562  1.00 18.22  ? 292 ALA A O   1 
ATOM   2063 C CB  . ALA A 1 263 ? 20.055  3.356   -3.846  1.00 17.43  ? 292 ALA A CB  1 
ATOM   2064 N N   . MET A 1 264 ? 18.021  0.921   -4.057  1.00 20.33  ? 293 MET A N   1 
ATOM   2065 C CA  . MET A 1 264 ? 17.123  0.074   -4.862  1.00 18.71  ? 293 MET A CA  1 
ATOM   2066 C C   . MET A 1 264 ? 15.702  0.023   -4.303  1.00 20.99  ? 293 MET A C   1 
ATOM   2067 O O   . MET A 1 264 ? 14.716  -0.093  -5.056  1.00 19.01  ? 293 MET A O   1 
ATOM   2068 C CB  . MET A 1 264 ? 17.693  -1.340  -4.884  1.00 19.38  ? 293 MET A CB  1 
ATOM   2069 C CG  . MET A 1 264 ? 19.007  -1.434  -5.623  1.00 18.56  ? 293 MET A CG  1 
ATOM   2070 S SD  . MET A 1 264 ? 18.956  -0.851  -7.332  1.00 20.66  ? 293 MET A SD  1 
ATOM   2071 C CE  . MET A 1 264 ? 19.306  0.902   -7.218  1.00 19.46  ? 293 MET A CE  1 
ATOM   2072 N N   . ASN A 1 265 ? 15.593  0.108   -2.970  1.00 18.06  ? 294 ASN A N   1 
ATOM   2073 C CA  . ASN A 1 265 ? 14.286  0.207   -2.350  1.00 19.42  ? 294 ASN A CA  1 
ATOM   2074 C C   . ASN A 1 265 ? 13.619  1.505   -2.771  1.00 18.46  ? 294 ASN A C   1 
ATOM   2075 O O   . ASN A 1 265 ? 12.415  1.531   -2.913  1.00 16.01  ? 294 ASN A O   1 
ATOM   2076 C CB  . ASN A 1 265 ? 14.369  0.035   -0.841  1.00 19.86  ? 294 ASN A CB  1 
ATOM   2077 C CG  . ASN A 1 265 ? 14.487  -1.421  -0.480  1.00 23.59  ? 294 ASN A CG  1 
ATOM   2078 O OD1 . ASN A 1 265 ? 14.706  -2.245  -1.358  1.00 25.53  ? 294 ASN A OD1 1 
ATOM   2079 N ND2 . ASN A 1 265 ? 14.282  -1.772  0.773   1.00 26.09  ? 294 ASN A ND2 1 
ATOM   2080 N N   . GLY A 1 266 ? 14.399  2.592   -2.903  1.00 19.52  ? 295 GLY A N   1 
ATOM   2081 C CA  . GLY A 1 266 ? 13.910  3.848   -3.447  1.00 19.14  ? 295 GLY A CA  1 
ATOM   2082 C C   . GLY A 1 266 ? 13.522  3.665   -4.911  1.00 21.83  ? 295 GLY A C   1 
ATOM   2083 O O   . GLY A 1 266 ? 12.467  4.128   -5.364  1.00 18.15  ? 295 GLY A O   1 
ATOM   2084 N N   . LEU A 1 267 ? 14.393  2.987   -5.653  1.00 20.03  ? 296 LEU A N   1 
ATOM   2085 C CA  . LEU A 1 267 ? 14.222  2.861   -7.091  1.00 22.37  ? 296 LEU A CA  1 
ATOM   2086 C C   . LEU A 1 267 ? 12.970  2.046   -7.393  1.00 22.40  ? 296 LEU A C   1 
ATOM   2087 O O   . LEU A 1 267 ? 12.311  2.316   -8.392  1.00 23.32  ? 296 LEU A O   1 
ATOM   2088 C CB  . LEU A 1 267 ? 15.441  2.234   -7.773  1.00 24.82  ? 296 LEU A CB  1 
ATOM   2089 C CG  . LEU A 1 267 ? 15.457  2.306   -9.306  1.00 23.69  ? 296 LEU A CG  1 
ATOM   2090 C CD1 . LEU A 1 267 ? 15.425  3.695   -9.937  1.00 23.75  ? 296 LEU A CD1 1 
ATOM   2091 C CD2 . LEU A 1 267 ? 16.660  1.532   -9.808  1.00 21.86  ? 296 LEU A CD2 1 
ATOM   2092 N N   . ALA A 1 268 ? 12.612  1.132   -6.494  1.00 23.25  ? 297 ALA A N   1 
ATOM   2093 C CA  . ALA A 1 268 ? 11.499  0.221   -6.707  1.00 21.97  ? 297 ALA A CA  1 
ATOM   2094 C C   . ALA A 1 268 ? 10.169  0.967   -6.535  1.00 23.18  ? 297 ALA A C   1 
ATOM   2095 O O   . ALA A 1 268 ? 9.126   0.440   -6.884  1.00 27.02  ? 297 ALA A O   1 
ATOM   2096 C CB  . ALA A 1 268 ? 11.605  -0.963  -5.756  1.00 21.27  ? 297 ALA A CB  1 
ATOM   2097 N N   . GLY A 1 269 ? 10.187  2.192   -5.994  1.00 22.60  ? 298 GLY A N   1 
ATOM   2098 C CA  . GLY A 1 269 ? 8.961   2.948   -5.818  1.00 23.21  ? 298 GLY A CA  1 
ATOM   2099 C C   . GLY A 1 269 ? 8.349   3.288   -7.176  1.00 24.85  ? 298 GLY A C   1 
ATOM   2100 O O   . GLY A 1 269 ? 9.063   3.637   -8.109  1.00 23.92  ? 298 GLY A O   1 
ATOM   2101 N N   . PRO A 1 270 ? 7.022   3.194   -7.353  1.00 24.58  ? 299 PRO A N   1 
ATOM   2102 C CA  . PRO A 1 270 ? 6.384   3.616   -8.601  1.00 28.02  ? 299 PRO A CA  1 
ATOM   2103 C C   . PRO A 1 270 ? 6.726   4.997   -9.197  1.00 29.10  ? 299 PRO A C   1 
ATOM   2104 O O   . PRO A 1 270 ? 6.765   5.159   -10.425 1.00 28.46  ? 299 PRO A O   1 
ATOM   2105 C CB  . PRO A 1 270 ? 4.887   3.512   -8.320  1.00 27.95  ? 299 PRO A CB  1 
ATOM   2106 C CG  . PRO A 1 270 ? 4.731   2.689   -7.050  1.00 27.05  ? 299 PRO A CG  1 
ATOM   2107 C CD  . PRO A 1 270 ? 6.083   2.630   -6.371  1.00 28.62  ? 299 PRO A CD  1 
ATOM   2108 N N   . LEU A 1 271 ? 7.024   5.990   -8.364  1.00 26.68  ? 300 LEU A N   1 
ATOM   2109 C CA  . LEU A 1 271 ? 7.323   7.319   -8.878  1.00 30.12  ? 300 LEU A CA  1 
ATOM   2110 C C   . LEU A 1 271 ? 8.794   7.470   -9.257  1.00 32.80  ? 300 LEU A C   1 
ATOM   2111 O O   . LEU A 1 271 ? 9.210   8.553   -9.679  1.00 38.83  ? 300 LEU A O   1 
ATOM   2112 C CB  . LEU A 1 271 ? 6.903   8.395   -7.877  1.00 27.69  ? 300 LEU A CB  1 
ATOM   2113 C CG  . LEU A 1 271 ? 5.406   8.469   -7.572  1.00 28.96  ? 300 LEU A CG  1 
ATOM   2114 C CD1 . LEU A 1 271 ? 5.157   9.638   -6.625  1.00 31.01  ? 300 LEU A CD1 1 
ATOM   2115 C CD2 . LEU A 1 271 ? 4.586   8.578   -8.877  1.00 32.72  ? 300 LEU A CD2 1 
ATOM   2116 N N   . HIS A 1 272 ? 9.584   6.409   -9.080  1.00 33.10  ? 301 HIS A N   1 
ATOM   2117 C CA  . HIS A 1 272 ? 11.002  6.480   -9.391  1.00 36.19  ? 301 HIS A CA  1 
ATOM   2118 C C   . HIS A 1 272 ? 11.345  5.563   -10.563 1.00 37.77  ? 301 HIS A C   1 
ATOM   2119 O O   . HIS A 1 272 ? 11.950  6.031   -11.527 1.00 39.21  ? 301 HIS A O   1 
ATOM   2120 C CB  . HIS A 1 272 ? 11.900  6.229   -8.170  1.00 35.58  ? 301 HIS A CB  1 
ATOM   2121 C CG  . HIS A 1 272 ? 13.321  6.561   -8.491  1.00 37.93  ? 301 HIS A CG  1 
ATOM   2122 N ND1 . HIS A 1 272 ? 13.640  7.216   -9.668  1.00 33.16  ? 301 HIS A ND1 1 
ATOM   2123 C CD2 . HIS A 1 272 ? 14.505  6.301   -7.877  1.00 36.12  ? 301 HIS A CD2 1 
ATOM   2124 C CE1 . HIS A 1 272 ? 14.964  7.409   -9.721  1.00 41.16  ? 301 HIS A CE1 1 
ATOM   2125 N NE2 . HIS A 1 272 ? 15.531  6.827   -8.673  1.00 38.49  ? 301 HIS A NE2 1 
ATOM   2126 N N   . GLY A 1 273 ? 10.965  4.280   -10.497 1.00 34.16  ? 302 GLY A N   1 
ATOM   2127 C CA  . GLY A 1 273 ? 11.568  3.311   -11.401 1.00 38.35  ? 302 GLY A CA  1 
ATOM   2128 C C   . GLY A 1 273 ? 10.591  2.352   -12.074 1.00 37.90  ? 302 GLY A C   1 
ATOM   2129 O O   . GLY A 1 273 ? 11.047  1.325   -12.564 1.00 47.59  ? 302 GLY A O   1 
ATOM   2130 N N   . LEU A 1 274 ? 9.285   2.669   -12.123 1.00 35.57  ? 303 LEU A N   1 
ATOM   2131 C CA  . LEU A 1 274 ? 8.301   1.827   -12.792 1.00 37.59  ? 303 LEU A CA  1 
ATOM   2132 C C   . LEU A 1 274 ? 7.678   2.521   -14.010 1.00 38.79  ? 303 LEU A C   1 
ATOM   2133 O O   . LEU A 1 274 ? 6.745   1.976   -14.592 1.00 38.80  ? 303 LEU A O   1 
ATOM   2134 C CB  . LEU A 1 274 ? 7.182   1.373   -11.857 1.00 44.00  ? 303 LEU A CB  1 
ATOM   2135 C CG  . LEU A 1 274 ? 7.537   0.233   -10.886 1.00 47.56  ? 303 LEU A CG  1 
ATOM   2136 C CD1 . LEU A 1 274 ? 8.905   0.362   -10.235 1.00 47.76  ? 303 LEU A CD1 1 
ATOM   2137 C CD2 . LEU A 1 274 ? 6.486   0.125   -9.795  1.00 51.28  ? 303 LEU A CD2 1 
ATOM   2138 N N   . ALA A 1 275 ? 8.183   3.690   -14.424 1.00 37.43  ? 304 ALA A N   1 
ATOM   2139 C CA  . ALA A 1 275 ? 7.614   4.384   -15.568 1.00 37.32  ? 304 ALA A CA  1 
ATOM   2140 C C   . ALA A 1 275 ? 7.804   3.567   -16.853 1.00 39.14  ? 304 ALA A C   1 
ATOM   2141 O O   . ALA A 1 275 ? 6.941   3.611   -17.720 1.00 36.44  ? 304 ALA A O   1 
ATOM   2142 C CB  . ALA A 1 275 ? 8.228   5.763   -15.708 1.00 37.45  ? 304 ALA A CB  1 
ATOM   2143 N N   . ASN A 1 276 ? 8.941   2.855   -16.977 1.00 35.70  ? 305 ASN A N   1 
ATOM   2144 C CA  . ASN A 1 276 ? 9.204   1.962   -18.102 1.00 39.21  ? 305 ASN A CA  1 
ATOM   2145 C C   . ASN A 1 276 ? 8.000   1.045   -18.339 1.00 33.98  ? 305 ASN A C   1 
ATOM   2146 O O   . ASN A 1 276 ? 7.340   1.137   -19.364 1.00 38.80  ? 305 ASN A O   1 
ATOM   2147 C CB  . ASN A 1 276 ? 10.511  1.193   -17.908 1.00 38.24  ? 305 ASN A CB  1 
ATOM   2148 C CG  . ASN A 1 276 ? 10.897  0.376   -19.121 1.00 44.27  ? 305 ASN A CG  1 
ATOM   2149 O OD1 . ASN A 1 276 ? 10.043  -0.029  -19.927 1.00 43.21  ? 305 ASN A OD1 1 
ATOM   2150 N ND2 . ASN A 1 276 ? 12.182  0.095   -19.261 1.00 46.45  ? 305 ASN A ND2 1 
ATOM   2151 N N   . GLN A 1 277 ? 7.731   0.165   -17.377 1.00 37.99  ? 306 GLN A N   1 
ATOM   2152 C CA  . GLN A 1 277 ? 6.571   -0.714  -17.356 1.00 40.80  ? 306 GLN A CA  1 
ATOM   2153 C C   . GLN A 1 277 ? 5.289   0.072   -17.644 1.00 43.27  ? 306 GLN A C   1 
ATOM   2154 O O   . GLN A 1 277 ? 4.468   -0.359  -18.440 1.00 42.68  ? 306 GLN A O   1 
ATOM   2155 C CB  . GLN A 1 277 ? 6.435   -1.425  -16.001 1.00 42.18  ? 306 GLN A CB  1 
ATOM   2156 C CG  . GLN A 1 277 ? 7.633   -2.298  -15.626 1.00 49.86  ? 306 GLN A CG  1 
ATOM   2157 C CD  . GLN A 1 277 ? 8.799   -1.603  -14.921 1.00 53.19  ? 306 GLN A CD  1 
ATOM   2158 O OE1 . GLN A 1 277 ? 9.211   -0.473  -15.233 1.00 46.69  ? 306 GLN A OE1 1 
ATOM   2159 N NE2 . GLN A 1 277 ? 9.397   -2.311  -13.970 1.00 48.90  ? 306 GLN A NE2 1 
ATOM   2160 N N   . GLU A 1 278 ? 5.087   1.206   -16.963 1.00 46.78  ? 307 GLU A N   1 
ATOM   2161 C CA  . GLU A 1 278 ? 3.838   1.940   -17.090 1.00 50.19  ? 307 GLU A CA  1 
ATOM   2162 C C   . GLU A 1 278 ? 3.615   2.402   -18.531 1.00 45.36  ? 307 GLU A C   1 
ATOM   2163 O O   . GLU A 1 278 ? 2.476   2.434   -18.993 1.00 41.99  ? 307 GLU A O   1 
ATOM   2164 C CB  . GLU A 1 278 ? 3.773   3.159   -16.176 1.00 52.43  ? 307 GLU A CB  1 
ATOM   2165 C CG  . GLU A 1 278 ? 3.021   2.858   -14.885 1.00 62.46  ? 307 GLU A CG  1 
ATOM   2166 C CD  . GLU A 1 278 ? 2.867   4.077   -13.997 1.00 73.47  ? 307 GLU A CD  1 
ATOM   2167 O OE1 . GLU A 1 278 ? 2.501   5.150   -14.533 1.00 70.62  ? 307 GLU A OE1 1 
ATOM   2168 O OE2 . GLU A 1 278 ? 3.094   3.944   -12.774 1.00 81.40  ? 307 GLU A OE2 1 
ATOM   2169 N N   . VAL A 1 279 ? 4.703   2.817   -19.186 1.00 34.38  ? 308 VAL A N   1 
ATOM   2170 C CA  . VAL A 1 279 ? 4.677   3.257   -20.570 1.00 36.11  ? 308 VAL A CA  1 
ATOM   2171 C C   . VAL A 1 279 ? 4.257   2.080   -21.436 1.00 35.31  ? 308 VAL A C   1 
ATOM   2172 O O   . VAL A 1 279 ? 3.335   2.193   -22.210 1.00 39.08  ? 308 VAL A O   1 
ATOM   2173 C CB  . VAL A 1 279 ? 6.038   3.837   -21.011 1.00 31.52  ? 308 VAL A CB  1 
ATOM   2174 C CG1 . VAL A 1 279 ? 6.187   3.922   -22.534 1.00 31.47  ? 308 VAL A CG1 1 
ATOM   2175 C CG2 . VAL A 1 279 ? 6.286   5.195   -20.362 1.00 31.78  ? 308 VAL A CG2 1 
ATOM   2176 N N   . LEU A 1 280 ? 4.926   0.948   -21.271 1.00 39.60  ? 309 LEU A N   1 
ATOM   2177 C CA  . LEU A 1 280 ? 4.691   -0.221  -22.100 1.00 40.80  ? 309 LEU A CA  1 
ATOM   2178 C C   . LEU A 1 280 ? 3.272   -0.797  -21.955 1.00 38.41  ? 309 LEU A C   1 
ATOM   2179 O O   . LEU A 1 280 ? 2.737   -1.352  -22.908 1.00 43.02  ? 309 LEU A O   1 
ATOM   2180 C CB  . LEU A 1 280 ? 5.760   -1.243  -21.728 1.00 40.35  ? 309 LEU A CB  1 
ATOM   2181 C CG  . LEU A 1 280 ? 5.910   -2.415  -22.706 1.00 46.75  ? 309 LEU A CG  1 
ATOM   2182 C CD1 . LEU A 1 280 ? 6.202   -1.894  -24.122 1.00 42.76  ? 309 LEU A CD1 1 
ATOM   2183 C CD2 . LEU A 1 280 ? 6.984   -3.390  -22.228 1.00 45.19  ? 309 LEU A CD2 1 
ATOM   2184 N N   . VAL A 1 281 ? 2.675   -0.714  -20.770 1.00 36.60  ? 310 VAL A N   1 
ATOM   2185 C CA  . VAL A 1 281 ? 1.310   -1.162  -20.552 1.00 43.66  ? 310 VAL A CA  1 
ATOM   2186 C C   . VAL A 1 281 ? 0.343   -0.246  -21.306 1.00 42.08  ? 310 VAL A C   1 
ATOM   2187 O O   . VAL A 1 281 ? -0.623  -0.701  -21.915 1.00 43.22  ? 310 VAL A O   1 
ATOM   2188 C CB  . VAL A 1 281 ? 1.025   -1.213  -19.035 1.00 45.94  ? 310 VAL A CB  1 
ATOM   2189 C CG1 . VAL A 1 281 ? -0.463  -1.308  -18.720 1.00 44.62  ? 310 VAL A CG1 1 
ATOM   2190 C CG2 . VAL A 1 281 ? 1.787   -2.351  -18.356 1.00 41.75  ? 310 VAL A CG2 1 
ATOM   2191 N N   . TRP A 1 282 ? 0.626   1.052   -21.285 1.00 36.11  ? 311 TRP A N   1 
ATOM   2192 C CA  . TRP A 1 282 ? -0.204  2.008   -22.000 1.00 42.81  ? 311 TRP A CA  1 
ATOM   2193 C C   . TRP A 1 282 ? -0.074  1.859   -23.523 1.00 47.87  ? 311 TRP A C   1 
ATOM   2194 O O   . TRP A 1 282 ? -1.073  1.915   -24.232 1.00 43.81  ? 311 TRP A O   1 
ATOM   2195 C CB  . TRP A 1 282 ? 0.212   3.399   -21.527 1.00 44.36  ? 311 TRP A CB  1 
ATOM   2196 C CG  . TRP A 1 282 ? -0.572  4.562   -22.061 1.00 45.88  ? 311 TRP A CG  1 
ATOM   2197 C CD1 . TRP A 1 282 ? -1.698  5.117   -21.528 1.00 42.91  ? 311 TRP A CD1 1 
ATOM   2198 C CD2 . TRP A 1 282 ? -0.184  5.400   -23.162 1.00 44.31  ? 311 TRP A CD2 1 
ATOM   2199 N NE1 . TRP A 1 282 ? -2.044  6.235   -22.235 1.00 44.42  ? 311 TRP A NE1 1 
ATOM   2200 C CE2 . TRP A 1 282 ? -1.138  6.433   -23.242 1.00 47.17  ? 311 TRP A CE2 1 
ATOM   2201 C CE3 . TRP A 1 282 ? 0.870   5.376   -24.076 1.00 48.42  ? 311 TRP A CE3 1 
ATOM   2202 C CZ2 . TRP A 1 282 ? -1.074  7.430   -24.212 1.00 51.87  ? 311 TRP A CZ2 1 
ATOM   2203 C CZ3 . TRP A 1 282 ? 0.938   6.369   -25.025 1.00 51.83  ? 311 TRP A CZ3 1 
ATOM   2204 C CH2 . TRP A 1 282 ? -0.006  7.397   -25.076 1.00 49.79  ? 311 TRP A CH2 1 
ATOM   2205 N N   . LEU A 1 283 ? 1.154   1.686   -24.035 1.00 44.55  ? 312 LEU A N   1 
ATOM   2206 C CA  . LEU A 1 283 ? 1.365   1.534   -25.466 1.00 48.07  ? 312 LEU A CA  1 
ATOM   2207 C C   . LEU A 1 283 ? 0.668   0.266   -25.949 1.00 57.69  ? 312 LEU A C   1 
ATOM   2208 O O   . LEU A 1 283 ? 0.189   0.252   -27.079 1.00 56.35  ? 312 LEU A O   1 
ATOM   2209 C CB  . LEU A 1 283 ? 2.825   1.448   -25.900 1.00 45.53  ? 312 LEU A CB  1 
ATOM   2210 C CG  . LEU A 1 283 ? 3.683   2.710   -25.770 1.00 46.87  ? 312 LEU A CG  1 
ATOM   2211 C CD1 . LEU A 1 283 ? 5.138   2.277   -25.920 1.00 42.79  ? 312 LEU A CD1 1 
ATOM   2212 C CD2 . LEU A 1 283 ? 3.339   3.809   -26.755 1.00 44.82  ? 312 LEU A CD2 1 
ATOM   2213 N N   . THR A 1 284 ? 0.707   -0.817  -25.149 1.00 58.53  ? 313 THR A N   1 
ATOM   2214 C CA  . THR A 1 284 ? 0.159   -2.096  -25.592 1.00 57.74  ? 313 THR A CA  1 
ATOM   2215 C C   . THR A 1 284 ? -1.365  -1.970  -25.633 1.00 67.29  ? 313 THR A C   1 
ATOM   2216 O O   . THR A 1 284 ? -1.988  -2.353  -26.624 1.00 62.29  ? 313 THR A O   1 
ATOM   2217 C CB  . THR A 1 284 ? 0.652   -3.261  -24.725 1.00 51.68  ? 313 THR A CB  1 
ATOM   2218 O OG1 . THR A 1 284 ? 2.065   -3.261  -24.913 1.00 51.72  ? 313 THR A OG1 1 
ATOM   2219 C CG2 . THR A 1 284 ? 0.171   -4.627  -25.185 1.00 47.17  ? 313 THR A CG2 1 
ATOM   2220 N N   . GLN A 1 285 ? -1.950  -1.377  -24.579 1.00 69.83  ? 314 GLN A N   1 
ATOM   2221 C CA  . GLN A 1 285 ? -3.377  -1.084  -24.551 1.00 78.22  ? 314 GLN A CA  1 
ATOM   2222 C C   . GLN A 1 285 ? -3.791  -0.258  -25.774 1.00 84.50  ? 314 GLN A C   1 
ATOM   2223 O O   . GLN A 1 285 ? -4.718  -0.637  -26.490 1.00 97.58  ? 314 GLN A O   1 
ATOM   2224 C CB  . GLN A 1 285 ? -3.764  -0.416  -23.231 1.00 80.61  ? 314 GLN A CB  1 
ATOM   2225 C CG  . GLN A 1 285 ? -4.860  0.633   -23.368 1.00 86.22  ? 314 GLN A CG  1 
ATOM   2226 C CD  . GLN A 1 285 ? -5.995  0.415   -22.400 1.00 94.33  ? 314 GLN A CD  1 
ATOM   2227 O OE1 . GLN A 1 285 ? -6.278  1.254   -21.539 1.00 104.40 ? 314 GLN A OE1 1 
ATOM   2228 N NE2 . GLN A 1 285 ? -6.663  -0.720  -22.550 1.00 96.48  ? 314 GLN A NE2 1 
ATOM   2229 N N   . LEU A 1 286 ? -3.110  0.878   -25.996 1.00 79.46  ? 315 LEU A N   1 
ATOM   2230 C CA  . LEU A 1 286 ? -3.372  1.756   -27.131 1.00 70.32  ? 315 LEU A CA  1 
ATOM   2231 C C   . LEU A 1 286 ? -3.370  0.970   -28.446 1.00 67.69  ? 315 LEU A C   1 
ATOM   2232 O O   . LEU A 1 286 ? -4.207  1.209   -29.310 1.00 61.43  ? 315 LEU A O   1 
ATOM   2233 C CB  . LEU A 1 286 ? -2.336  2.884   -27.140 1.00 65.80  ? 315 LEU A CB  1 
ATOM   2234 C CG  . LEU A 1 286 ? -2.313  3.811   -28.365 1.00 64.39  ? 315 LEU A CG  1 
ATOM   2235 C CD1 . LEU A 1 286 ? -3.643  4.487   -28.593 1.00 65.36  ? 315 LEU A CD1 1 
ATOM   2236 C CD2 . LEU A 1 286 ? -1.235  4.867   -28.241 1.00 60.31  ? 315 LEU A CD2 1 
ATOM   2237 N N   . GLN A 1 287 ? -2.417  0.047   -28.608 1.00 65.45  ? 316 GLN A N   1 
ATOM   2238 C CA  . GLN A 1 287 ? -2.261  -0.688  -29.853 1.00 68.28  ? 316 GLN A CA  1 
ATOM   2239 C C   . GLN A 1 287 ? -3.464  -1.578  -30.136 1.00 76.60  ? 316 GLN A C   1 
ATOM   2240 O O   . GLN A 1 287 ? -3.713  -1.888  -31.298 1.00 86.51  ? 316 GLN A O   1 
ATOM   2241 C CB  . GLN A 1 287 ? -0.990  -1.529  -29.848 1.00 65.29  ? 316 GLN A CB  1 
ATOM   2242 C CG  . GLN A 1 287 ? 0.220   -0.740  -30.330 1.00 68.94  ? 316 GLN A CG  1 
ATOM   2243 C CD  . GLN A 1 287 ? 0.744   -1.198  -31.672 1.00 67.19  ? 316 GLN A CD  1 
ATOM   2244 O OE1 . GLN A 1 287 ? 0.681   -0.482  -32.680 1.00 73.12  ? 316 GLN A OE1 1 
ATOM   2245 N NE2 . GLN A 1 287 ? 1.298   -2.402  -31.682 1.00 67.13  ? 316 GLN A NE2 1 
ATOM   2246 N N   . LYS A 1 288 ? -4.193  -1.993  -29.092 1.00 74.02  ? 317 LYS A N   1 
ATOM   2247 C CA  . LYS A 1 288 ? -5.435  -2.715  -29.295 1.00 76.74  ? 317 LYS A CA  1 
ATOM   2248 C C   . LYS A 1 288 ? -6.519  -1.708  -29.667 1.00 75.38  ? 317 LYS A C   1 
ATOM   2249 O O   . LYS A 1 288 ? -7.127  -1.833  -30.726 1.00 79.77  ? 317 LYS A O   1 
ATOM   2250 C CB  . LYS A 1 288 ? -5.809  -3.562  -28.076 1.00 84.76  ? 317 LYS A CB  1 
ATOM   2251 C CG  . LYS A 1 288 ? -4.764  -4.612  -27.715 1.00 97.78  ? 317 LYS A CG  1 
ATOM   2252 C CD  . LYS A 1 288 ? -5.020  -5.404  -26.436 1.00 106.10 ? 317 LYS A CD  1 
ATOM   2253 C CE  . LYS A 1 288 ? -5.402  -4.530  -25.277 1.00 117.34 ? 317 LYS A CE  1 
ATOM   2254 N NZ  . LYS A 1 288 ? -4.983  -5.090  -23.988 1.00 123.40 ? 317 LYS A NZ  1 
ATOM   2255 N N   . GLU A 1 289 ? -6.716  -0.695  -28.811 1.00 73.23  ? 318 GLU A N   1 
ATOM   2256 C CA  . GLU A 1 289 ? -7.820  0.246   -28.946 1.00 75.91  ? 318 GLU A CA  1 
ATOM   2257 C C   . GLU A 1 289 ? -7.801  1.013   -30.273 1.00 79.97  ? 318 GLU A C   1 
ATOM   2258 O O   . GLU A 1 289 ? -8.851  1.509   -30.676 1.00 90.69  ? 318 GLU A O   1 
ATOM   2259 C CB  . GLU A 1 289 ? -7.887  1.227   -27.774 1.00 73.53  ? 318 GLU A CB  1 
ATOM   2260 C CG  . GLU A 1 289 ? -8.606  0.632   -26.568 1.00 75.68  ? 318 GLU A CG  1 
ATOM   2261 C CD  . GLU A 1 289 ? -8.401  1.365   -25.260 1.00 76.62  ? 318 GLU A CD  1 
ATOM   2262 O OE1 . GLU A 1 289 ? -8.026  2.549   -25.318 1.00 82.65  ? 318 GLU A OE1 1 
ATOM   2263 O OE2 . GLU A 1 289 ? -8.587  0.743   -24.190 1.00 75.11  ? 318 GLU A OE2 1 
ATOM   2264 N N   . VAL A 1 290 ? -6.649  1.145   -30.950 1.00 73.90  ? 319 VAL A N   1 
ATOM   2265 C CA  . VAL A 1 290 ? -6.617  1.869   -32.218 1.00 72.46  ? 319 VAL A CA  1 
ATOM   2266 C C   . VAL A 1 290 ? -5.972  1.033   -33.328 1.00 72.90  ? 319 VAL A C   1 
ATOM   2267 O O   . VAL A 1 290 ? -5.657  1.586   -34.385 1.00 67.84  ? 319 VAL A O   1 
ATOM   2268 C CB  . VAL A 1 290 ? -5.920  3.243   -32.124 1.00 71.51  ? 319 VAL A CB  1 
ATOM   2269 C CG1 . VAL A 1 290 ? -6.440  4.074   -30.956 1.00 74.75  ? 319 VAL A CG1 1 
ATOM   2270 C CG2 . VAL A 1 290 ? -4.401  3.130   -32.063 1.00 77.59  ? 319 VAL A CG2 1 
ATOM   2271 N N   . GLY A 1 291 ? -5.781  -0.278  -33.105 1.00 66.03  ? 320 GLY A N   1 
ATOM   2272 C CA  . GLY A 1 291 ? -5.117  -1.141  -34.078 1.00 69.28  ? 320 GLY A CA  1 
ATOM   2273 C C   . GLY A 1 291 ? -3.629  -0.810  -34.229 1.00 74.98  ? 320 GLY A C   1 
ATOM   2274 O O   . GLY A 1 291 ? -3.180  0.251   -33.812 1.00 78.35  ? 320 GLY A O   1 
ATOM   2275 N N   . LYS A 1 292 ? -2.858  -1.720  -34.836 1.00 89.82  ? 321 LYS A N   1 
ATOM   2276 C CA  . LYS A 1 292 ? -1.421  -1.517  -34.998 1.00 101.72 ? 321 LYS A CA  1 
ATOM   2277 C C   . LYS A 1 292 ? -1.189  -0.590  -36.197 1.00 102.43 ? 321 LYS A C   1 
ATOM   2278 O O   . LYS A 1 292 ? -0.363  0.322   -36.136 1.00 99.60  ? 321 LYS A O   1 
ATOM   2279 C CB  . LYS A 1 292 ? -0.676  -2.863  -35.071 1.00 106.96 ? 321 LYS A CB  1 
ATOM   2280 C CG  . LYS A 1 292 ? -0.051  -3.246  -36.414 1.00 116.70 ? 321 LYS A CG  1 
ATOM   2281 C CD  . LYS A 1 292 ? 1.320   -2.619  -36.655 1.00 128.25 ? 321 LYS A CD  1 
ATOM   2282 C CE  . LYS A 1 292 ? 1.517   -1.955  -37.993 1.00 140.63 ? 321 LYS A CE  1 
ATOM   2283 N NZ  . LYS A 1 292 ? 1.293   -2.823  -39.155 1.00 144.57 ? 321 LYS A NZ  1 
ATOM   2284 N N   . ASP A 1 293 ? -1.937  -0.845  -37.282 1.00 107.55 ? 322 ASP A N   1 
ATOM   2285 C CA  . ASP A 1 293 ? -1.952  -0.010  -38.474 1.00 103.78 ? 322 ASP A CA  1 
ATOM   2286 C C   . ASP A 1 293 ? -2.783  1.238   -38.173 1.00 97.27  ? 322 ASP A C   1 
ATOM   2287 O O   . ASP A 1 293 ? -4.006  1.210   -38.295 1.00 95.11  ? 322 ASP A O   1 
ATOM   2288 C CB  . ASP A 1 293 ? -2.524  -0.772  -39.666 1.00 112.62 ? 322 ASP A CB  1 
ATOM   2289 C CG  . ASP A 1 293 ? -1.885  -2.114  -40.019 1.00 112.06 ? 322 ASP A CG  1 
ATOM   2290 O OD1 . ASP A 1 293 ? -1.902  -3.029  -39.169 1.00 99.23  ? 322 ASP A OD1 1 
ATOM   2291 O OD2 . ASP A 1 293 ? -1.402  -2.256  -41.164 1.00 112.62 ? 322 ASP A OD2 1 
ATOM   2292 N N   . VAL A 1 294 ? -2.115  2.332   -37.786 1.00 85.81  ? 323 VAL A N   1 
ATOM   2293 C CA  . VAL A 1 294 ? -2.789  3.451   -37.149 1.00 86.04  ? 323 VAL A CA  1 
ATOM   2294 C C   . VAL A 1 294 ? -2.560  4.714   -37.970 1.00 84.59  ? 323 VAL A C   1 
ATOM   2295 O O   . VAL A 1 294 ? -1.555  4.817   -38.664 1.00 92.01  ? 323 VAL A O   1 
ATOM   2296 C CB  . VAL A 1 294 ? -2.284  3.606   -35.700 1.00 95.35  ? 323 VAL A CB  1 
ATOM   2297 C CG1 . VAL A 1 294 ? -0.766  3.749   -35.628 1.00 94.51  ? 323 VAL A CG1 1 
ATOM   2298 C CG2 . VAL A 1 294 ? -2.974  4.753   -34.966 1.00 99.90  ? 323 VAL A CG2 1 
ATOM   2299 N N   . SER A 1 295 ? -3.499  5.665   -37.876 1.00 89.76  ? 324 SER A N   1 
ATOM   2300 C CA  . SER A 1 295 ? -3.428  6.927   -38.602 1.00 89.82  ? 324 SER A CA  1 
ATOM   2301 C C   . SER A 1 295 ? -2.620  7.935   -37.782 1.00 83.56  ? 324 SER A C   1 
ATOM   2302 O O   . SER A 1 295 ? -1.911  7.536   -36.865 1.00 92.22  ? 324 SER A O   1 
ATOM   2303 C CB  . SER A 1 295 ? -4.825  7.438   -38.943 1.00 87.52  ? 324 SER A CB  1 
ATOM   2304 O OG  . SER A 1 295 ? -5.553  7.820   -37.781 1.00 82.05  ? 324 SER A OG  1 
ATOM   2305 N N   . ASP A 1 296 ? -2.713  9.226   -38.135 1.00 84.03  ? 325 ASP A N   1 
ATOM   2306 C CA  . ASP A 1 296 ? -2.075  10.310  -37.399 1.00 79.52  ? 325 ASP A CA  1 
ATOM   2307 C C   . ASP A 1 296 ? -3.116  11.062  -36.564 1.00 79.12  ? 325 ASP A C   1 
ATOM   2308 O O   . ASP A 1 296 ? -2.752  11.721  -35.588 1.00 63.08  ? 325 ASP A O   1 
ATOM   2309 C CB  . ASP A 1 296 ? -1.314  11.243  -38.339 1.00 80.23  ? 325 ASP A CB  1 
ATOM   2310 C CG  . ASP A 1 296 ? 0.213   11.168  -38.327 1.00 85.39  ? 325 ASP A CG  1 
ATOM   2311 O OD1 . ASP A 1 296 ? 0.774   10.058  -38.495 1.00 75.59  ? 325 ASP A OD1 1 
ATOM   2312 O OD2 . ASP A 1 296 ? 0.849   12.236  -38.171 1.00 82.30  ? 325 ASP A OD2 1 
ATOM   2313 N N   . GLU A 1 297 ? -4.400  10.981  -36.962 1.00 81.78  ? 326 GLU A N   1 
ATOM   2314 C CA  . GLU A 1 297 ? -5.465  11.729  -36.305 1.00 77.75  ? 326 GLU A CA  1 
ATOM   2315 C C   . GLU A 1 297 ? -6.019  10.898  -35.159 1.00 68.29  ? 326 GLU A C   1 
ATOM   2316 O O   . GLU A 1 297 ? -6.193  11.403  -34.050 1.00 62.27  ? 326 GLU A O   1 
ATOM   2317 C CB  . GLU A 1 297 ? -6.693  12.041  -37.164 1.00 88.70  ? 326 GLU A CB  1 
ATOM   2318 C CG  . GLU A 1 297 ? -6.414  12.217  -38.653 1.00 93.51  ? 326 GLU A CG  1 
ATOM   2319 C CD  . GLU A 1 297 ? -7.633  12.734  -39.397 1.00 96.11  ? 326 GLU A CD  1 
ATOM   2320 O OE1 . GLU A 1 297 ? -8.135  13.815  -39.017 1.00 100.46 ? 326 GLU A OE1 1 
ATOM   2321 O OE2 . GLU A 1 297 ? -8.086  12.062  -40.349 1.00 93.59  ? 326 GLU A OE2 1 
ATOM   2322 N N   . LYS A 1 298 ? -6.311  9.629   -35.477 1.00 73.68  ? 327 LYS A N   1 
ATOM   2323 C CA  . LYS A 1 298 ? -6.860  8.687   -34.518 1.00 77.90  ? 327 LYS A CA  1 
ATOM   2324 C C   . LYS A 1 298 ? -5.894  8.600   -33.341 1.00 75.06  ? 327 LYS A C   1 
ATOM   2325 O O   . LYS A 1 298 ? -6.324  8.375   -32.213 1.00 85.35  ? 327 LYS A O   1 
ATOM   2326 C CB  . LYS A 1 298 ? -7.138  7.310   -35.141 1.00 81.04  ? 327 LYS A CB  1 
ATOM   2327 C CG  . LYS A 1 298 ? -8.176  6.470   -34.385 1.00 80.96  ? 327 LYS A CG  1 
ATOM   2328 C CD  . LYS A 1 298 ? -8.345  5.017   -34.824 1.00 80.25  ? 327 LYS A CD  1 
ATOM   2329 C CE  . LYS A 1 298 ? -9.399  4.327   -34.003 1.00 83.33  ? 327 LYS A CE  1 
ATOM   2330 N NZ  . LYS A 1 298 ? -9.692  2.957   -34.441 1.00 82.94  ? 327 LYS A NZ  1 
ATOM   2331 N N   . LEU A 1 299 ? -4.599  8.813   -33.620 1.00 72.42  ? 328 LEU A N   1 
ATOM   2332 C CA  . LEU A 1 299 ? -3.590  8.880   -32.576 1.00 68.76  ? 328 LEU A CA  1 
ATOM   2333 C C   . LEU A 1 299 ? -3.709  10.207  -31.832 1.00 58.47  ? 328 LEU A C   1 
ATOM   2334 O O   . LEU A 1 299 ? -3.562  10.240  -30.617 1.00 56.90  ? 328 LEU A O   1 
ATOM   2335 C CB  . LEU A 1 299 ? -2.190  8.660   -33.150 1.00 73.41  ? 328 LEU A CB  1 
ATOM   2336 C CG  . LEU A 1 299 ? -1.120  8.191   -32.157 1.00 76.54  ? 328 LEU A CG  1 
ATOM   2337 C CD1 . LEU A 1 299 ? -1.623  7.120   -31.206 1.00 74.87  ? 328 LEU A CD1 1 
ATOM   2338 C CD2 . LEU A 1 299 ? 0.083   7.661   -32.908 1.00 78.96  ? 328 LEU A CD2 1 
ATOM   2339 N N   . ARG A 1 300 ? -3.984  11.299  -32.548 1.00 61.83  ? 329 ARG A N   1 
ATOM   2340 C CA  . ARG A 1 300 ? -4.122  12.597  -31.896 1.00 70.88  ? 329 ARG A CA  1 
ATOM   2341 C C   . ARG A 1 300 ? -5.436  12.656  -31.115 1.00 71.12  ? 329 ARG A C   1 
ATOM   2342 O O   . ARG A 1 300 ? -5.507  13.310  -30.073 1.00 74.35  ? 329 ARG A O   1 
ATOM   2343 C CB  . ARG A 1 300 ? -4.022  13.767  -32.881 1.00 73.80  ? 329 ARG A CB  1 
ATOM   2344 C CG  . ARG A 1 300 ? -3.583  15.080  -32.242 1.00 79.36  ? 329 ARG A CG  1 
ATOM   2345 C CD  . ARG A 1 300 ? -3.761  16.277  -33.166 1.00 87.64  ? 329 ARG A CD  1 
ATOM   2346 N NE  . ARG A 1 300 ? -3.435  15.930  -34.554 1.00 95.33  ? 329 ARG A NE  1 
ATOM   2347 C CZ  . ARG A 1 300 ? -4.328  15.656  -35.507 1.00 118.57 ? 329 ARG A CZ  1 
ATOM   2348 N NH1 . ARG A 1 300 ? -5.627  15.724  -35.253 1.00 127.95 ? 329 ARG A NH1 1 
ATOM   2349 N NH2 . ARG A 1 300 ? -3.923  15.302  -36.717 1.00 123.35 ? 329 ARG A NH2 1 
ATOM   2350 N N   . ASP A 1 301 ? -6.466  11.963  -31.622 1.00 74.35  ? 330 ASP A N   1 
ATOM   2351 C CA  . ASP A 1 301 ? -7.741  11.853  -30.923 1.00 79.42  ? 330 ASP A CA  1 
ATOM   2352 C C   . ASP A 1 301 ? -7.531  11.191  -29.559 1.00 73.94  ? 330 ASP A C   1 
ATOM   2353 O O   . ASP A 1 301 ? -7.896  11.767  -28.536 1.00 72.94  ? 330 ASP A O   1 
ATOM   2354 C CB  . ASP A 1 301 ? -8.785  11.161  -31.790 1.00 83.31  ? 330 ASP A CB  1 
ATOM   2355 C CG  . ASP A 1 301 ? -9.436  12.044  -32.848 1.00 84.35  ? 330 ASP A CG  1 
ATOM   2356 O OD1 . ASP A 1 301 ? -9.377  13.286  -32.685 1.00 89.60  ? 330 ASP A OD1 1 
ATOM   2357 O OD2 . ASP A 1 301 ? -9.986  11.491  -33.831 1.00 67.90  ? 330 ASP A OD2 1 
ATOM   2358 N N   . TYR A 1 302 ? -6.912  10.000  -29.566 1.00 72.59  ? 331 TYR A N   1 
ATOM   2359 C CA  . TYR A 1 302 ? -6.674  9.211   -28.365 1.00 64.61  ? 331 TYR A CA  1 
ATOM   2360 C C   . TYR A 1 302 ? -5.893  10.027  -27.340 1.00 66.52  ? 331 TYR A C   1 
ATOM   2361 O O   . TYR A 1 302 ? -6.241  10.020  -26.159 1.00 68.66  ? 331 TYR A O   1 
ATOM   2362 C CB  . TYR A 1 302 ? -5.923  7.926   -28.719 1.00 64.53  ? 331 TYR A CB  1 
ATOM   2363 C CG  . TYR A 1 302 ? -5.722  6.966   -27.554 1.00 64.91  ? 331 TYR A CG  1 
ATOM   2364 C CD1 . TYR A 1 302 ? -4.780  7.224   -26.562 1.00 66.43  ? 331 TYR A CD1 1 
ATOM   2365 C CD2 . TYR A 1 302 ? -6.446  5.782   -27.464 1.00 66.31  ? 331 TYR A CD2 1 
ATOM   2366 C CE1 . TYR A 1 302 ? -4.581  6.350   -25.506 1.00 64.95  ? 331 TYR A CE1 1 
ATOM   2367 C CE2 . TYR A 1 302 ? -6.255  4.900   -26.411 1.00 69.89  ? 331 TYR A CE2 1 
ATOM   2368 C CZ  . TYR A 1 302 ? -5.321  5.184   -25.428 1.00 66.96  ? 331 TYR A CZ  1 
ATOM   2369 O OH  . TYR A 1 302 ? -5.114  4.315   -24.396 1.00 80.39  ? 331 TYR A OH  1 
ATOM   2370 N N   . ILE A 1 303 ? -4.839  10.722  -27.796 1.00 67.17  ? 332 ILE A N   1 
ATOM   2371 C CA  . ILE A 1 303 ? -4.048  11.555  -26.904 1.00 66.00  ? 332 ILE A CA  1 
ATOM   2372 C C   . ILE A 1 303 ? -4.916  12.708  -26.416 1.00 61.23  ? 332 ILE A C   1 
ATOM   2373 O O   . ILE A 1 303 ? -4.857  13.056  -25.237 1.00 61.95  ? 332 ILE A O   1 
ATOM   2374 C CB  . ILE A 1 303 ? -2.736  12.040  -27.549 1.00 71.55  ? 332 ILE A CB  1 
ATOM   2375 C CG1 . ILE A 1 303 ? -1.566  11.107  -27.256 1.00 73.36  ? 332 ILE A CG1 1 
ATOM   2376 C CG2 . ILE A 1 303 ? -2.388  13.446  -27.073 1.00 77.10  ? 332 ILE A CG2 1 
ATOM   2377 C CD1 . ILE A 1 303 ? -1.767  9.678   -27.708 1.00 73.06  ? 332 ILE A CD1 1 
ATOM   2378 N N   . TRP A 1 304 ? -5.739  13.276  -27.308 1.00 59.81  ? 333 TRP A N   1 
ATOM   2379 C CA  . TRP A 1 304 ? -6.705  14.269  -26.863 1.00 64.63  ? 333 TRP A CA  1 
ATOM   2380 C C   . TRP A 1 304 ? -7.667  13.663  -25.842 1.00 61.45  ? 333 TRP A C   1 
ATOM   2381 O O   . TRP A 1 304 ? -7.908  14.269  -24.804 1.00 54.53  ? 333 TRP A O   1 
ATOM   2382 C CB  . TRP A 1 304 ? -7.448  14.938  -28.033 1.00 65.31  ? 333 TRP A CB  1 
ATOM   2383 C CG  . TRP A 1 304 ? -6.813  16.243  -28.445 1.00 68.69  ? 333 TRP A CG  1 
ATOM   2384 C CD1 . TRP A 1 304 ? -6.511  16.645  -29.714 1.00 66.42  ? 333 TRP A CD1 1 
ATOM   2385 C CD2 . TRP A 1 304 ? -6.384  17.317  -27.568 1.00 66.74  ? 333 TRP A CD2 1 
ATOM   2386 N NE1 . TRP A 1 304 ? -5.920  17.883  -29.692 1.00 69.19  ? 333 TRP A NE1 1 
ATOM   2387 C CE2 . TRP A 1 304 ? -5.829  18.323  -28.392 1.00 64.38  ? 333 TRP A CE2 1 
ATOM   2388 C CE3 . TRP A 1 304 ? -6.416  17.532  -26.181 1.00 69.89  ? 333 TRP A CE3 1 
ATOM   2389 C CZ2 . TRP A 1 304 ? -5.316  19.512  -27.874 1.00 60.90  ? 333 TRP A CZ2 1 
ATOM   2390 C CZ3 . TRP A 1 304 ? -5.913  18.712  -25.670 1.00 68.02  ? 333 TRP A CZ3 1 
ATOM   2391 C CH2 . TRP A 1 304 ? -5.375  19.690  -26.510 1.00 66.83  ? 333 TRP A CH2 1 
ATOM   2392 N N   . ASN A 1 305 ? -8.174  12.453  -26.108 1.00 61.87  ? 334 ASN A N   1 
ATOM   2393 C CA  . ASN A 1 305 ? -9.174  11.844  -25.240 1.00 67.87  ? 334 ASN A CA  1 
ATOM   2394 C C   . ASN A 1 305 ? -8.539  11.413  -23.912 1.00 68.84  ? 334 ASN A C   1 
ATOM   2395 O O   . ASN A 1 305 ? -9.232  11.351  -22.901 1.00 75.26  ? 334 ASN A O   1 
ATOM   2396 C CB  . ASN A 1 305 ? -9.931  10.717  -25.951 1.00 71.49  ? 334 ASN A CB  1 
ATOM   2397 C CG  . ASN A 1 305 ? -10.728 11.172  -27.161 1.00 73.54  ? 334 ASN A CG  1 
ATOM   2398 O OD1 . ASN A 1 305 ? -11.119 12.341  -27.277 1.00 65.05  ? 334 ASN A OD1 1 
ATOM   2399 N ND2 . ASN A 1 305 ? -11.003 10.258  -28.081 1.00 75.44  ? 334 ASN A ND2 1 
ATOM   2400 N N   . THR A 1 306 ? -7.227  11.120  -23.907 1.00 75.30  ? 335 THR A N   1 
ATOM   2401 C CA  . THR A 1 306 ? -6.502  10.775  -22.687 1.00 72.48  ? 335 THR A CA  1 
ATOM   2402 C C   . THR A 1 306 ? -6.420  11.988  -21.757 1.00 71.55  ? 335 THR A C   1 
ATOM   2403 O O   . THR A 1 306 ? -6.544  11.859  -20.533 1.00 60.45  ? 335 THR A O   1 
ATOM   2404 C CB  . THR A 1 306 ? -5.095  10.277  -23.034 1.00 74.69  ? 335 THR A CB  1 
ATOM   2405 O OG1 . THR A 1 306 ? -5.207  9.186   -23.945 1.00 68.98  ? 335 THR A OG1 1 
ATOM   2406 C CG2 . THR A 1 306 ? -4.323  9.817   -21.807 1.00 75.56  ? 335 THR A CG2 1 
ATOM   2407 N N   . LEU A 1 307 ? -6.148  13.156  -22.357 1.00 76.54  ? 336 LEU A N   1 
ATOM   2408 C CA  . LEU A 1 307 ? -5.875  14.381  -21.616 1.00 84.48  ? 336 LEU A CA  1 
ATOM   2409 C C   . LEU A 1 307 ? -7.127  14.880  -20.894 1.00 84.19  ? 336 LEU A C   1 
ATOM   2410 O O   . LEU A 1 307 ? -7.040  15.415  -19.789 1.00 76.30  ? 336 LEU A O   1 
ATOM   2411 C CB  . LEU A 1 307 ? -5.329  15.439  -22.577 1.00 81.76  ? 336 LEU A CB  1 
ATOM   2412 C CG  . LEU A 1 307 ? -3.937  15.167  -23.162 1.00 77.15  ? 336 LEU A CG  1 
ATOM   2413 C CD1 . LEU A 1 307 ? -3.502  16.346  -24.032 1.00 75.90  ? 336 LEU A CD1 1 
ATOM   2414 C CD2 . LEU A 1 307 ? -2.898  14.868  -22.086 1.00 74.03  ? 336 LEU A CD2 1 
ATOM   2415 N N   . ASN A 1 308 ? -8.287  14.694  -21.529 1.00 88.44  ? 337 ASN A N   1 
ATOM   2416 C CA  . ASN A 1 308 ? -9.549  15.136  -20.959 1.00 92.98  ? 337 ASN A CA  1 
ATOM   2417 C C   . ASN A 1 308 ? -9.891  14.249  -19.764 1.00 89.87  ? 337 ASN A C   1 
ATOM   2418 O O   . ASN A 1 308 ? -10.017 14.751  -18.650 1.00 86.67  ? 337 ASN A O   1 
ATOM   2419 C CB  . ASN A 1 308 ? -10.596 15.250  -22.057 1.00 89.14  ? 337 ASN A CB  1 
ATOM   2420 C CG  . ASN A 1 308 ? -10.139 16.260  -23.086 1.00 84.79  ? 337 ASN A CG  1 
ATOM   2421 O OD1 . ASN A 1 308 ? -9.675  17.342  -22.707 1.00 68.65  ? 337 ASN A OD1 1 
ATOM   2422 N ND2 . ASN A 1 308 ? -10.193 15.917  -24.367 1.00 80.91  ? 337 ASN A ND2 1 
ATOM   2423 N N   . SER A 1 309 ? -9.826  12.827  -20.027 1.00 87.15  ? 338 SER A N   1 
ATOM   2424 C CA  . SER A 1 309 ? -10.358 12.163  -18.804 1.00 81.97  ? 338 SER A CA  1 
ATOM   2425 C C   . SER A 1 309 ? -9.598  12.646  -17.560 1.00 80.46  ? 338 SER A C   1 
ATOM   2426 O O   . SER A 1 309 ? -10.122 12.452  -16.442 1.00 76.44  ? 338 SER A O   1 
ATOM   2427 C CB  . SER A 1 309 ? -10.283 10.665  -18.934 1.00 82.07  ? 338 SER A CB  1 
ATOM   2428 O OG  . SER A 1 309 ? -8.933  10.224  -18.906 1.00 77.94  ? 338 SER A OG  1 
ATOM   2429 N N   . GLY A 1 310 ? -8.422  13.279  -17.753 1.00 77.94  ? 339 GLY A N   1 
ATOM   2430 C CA  . GLY A 1 310 ? -7.642  13.772  -16.630 1.00 72.54  ? 339 GLY A CA  1 
ATOM   2431 C C   . GLY A 1 310 ? -6.471  12.838  -16.321 1.00 80.99  ? 339 GLY A C   1 
ATOM   2432 O O   . GLY A 1 310 ? -5.976  12.830  -15.195 1.00 78.51  ? 339 GLY A O   1 
ATOM   2433 N N   . ARG A 1 311 ? -6.038  12.055  -17.326 1.00 87.13  ? 340 ARG A N   1 
ATOM   2434 C CA  . ARG A 1 311 ? -5.068  10.986  -17.120 1.00 91.49  ? 340 ARG A CA  1 
ATOM   2435 C C   . ARG A 1 311 ? -3.766  11.328  -17.846 1.00 92.20  ? 340 ARG A C   1 
ATOM   2436 O O   . ARG A 1 311 ? -3.777  11.964  -18.901 1.00 93.49  ? 340 ARG A O   1 
ATOM   2437 C CB  . ARG A 1 311 ? -5.661  9.647   -17.580 1.00 95.14  ? 340 ARG A CB  1 
ATOM   2438 C CG  . ARG A 1 311 ? -5.229  8.450   -16.742 1.00 100.16 ? 340 ARG A CG  1 
ATOM   2439 C CD  . ARG A 1 311 ? -5.896  7.138   -17.170 1.00 103.23 ? 340 ARG A CD  1 
ATOM   2440 N NE  . ARG A 1 311 ? -7.363  7.178   -17.100 1.00 107.38 ? 340 ARG A NE  1 
ATOM   2441 C CZ  . ARG A 1 311 ? -8.192  7.236   -18.138 1.00 105.24 ? 340 ARG A CZ  1 
ATOM   2442 N NH1 . ARG A 1 311 ? -9.500  7.263   -17.943 1.00 99.29  ? 340 ARG A NH1 1 
ATOM   2443 N NH2 . ARG A 1 311 ? -7.713  7.275   -19.368 1.00 108.15 ? 340 ARG A NH2 1 
ATOM   2444 N N   . VAL A 1 312 ? -2.641  10.889  -17.269 1.00 87.60  ? 341 VAL A N   1 
ATOM   2445 C CA  . VAL A 1 312 ? -1.325  11.281  -17.748 1.00 83.55  ? 341 VAL A CA  1 
ATOM   2446 C C   . VAL A 1 312 ? -0.970  10.502  -19.015 1.00 74.30  ? 341 VAL A C   1 
ATOM   2447 O O   . VAL A 1 312 ? -1.414  9.373   -19.236 1.00 64.24  ? 341 VAL A O   1 
ATOM   2448 C CB  . VAL A 1 312 ? -0.255  11.073  -16.658 1.00 89.39  ? 341 VAL A CB  1 
ATOM   2449 C CG1 . VAL A 1 312 ? 0.223   9.625   -16.582 1.00 85.57  ? 341 VAL A CG1 1 
ATOM   2450 C CG2 . VAL A 1 312 ? 0.935   12.004  -16.850 1.00 96.08  ? 341 VAL A CG2 1 
ATOM   2451 N N   . VAL A 1 313 ? -0.135  11.124  -19.845 1.00 70.93  ? 342 VAL A N   1 
ATOM   2452 C CA  . VAL A 1 313 ? 0.555   10.407  -20.903 1.00 65.79  ? 342 VAL A CA  1 
ATOM   2453 C C   . VAL A 1 313 ? 1.880   9.921   -20.311 1.00 60.06  ? 342 VAL A C   1 
ATOM   2454 O O   . VAL A 1 313 ? 2.775   10.721  -20.016 1.00 57.50  ? 342 VAL A O   1 
ATOM   2455 C CB  . VAL A 1 313 ? 0.750   11.290  -22.150 1.00 68.21  ? 342 VAL A CB  1 
ATOM   2456 C CG1 . VAL A 1 313 ? 1.169   10.476  -23.369 1.00 65.62  ? 342 VAL A CG1 1 
ATOM   2457 C CG2 . VAL A 1 313 ? -0.504  12.101  -22.457 1.00 70.22  ? 342 VAL A CG2 1 
ATOM   2458 N N   . PRO A 1 314 ? 2.033   8.602   -20.045 1.00 51.18  ? 343 PRO A N   1 
ATOM   2459 C CA  . PRO A 1 314 ? 3.222   8.113   -19.361 1.00 49.39  ? 343 PRO A CA  1 
ATOM   2460 C C   . PRO A 1 314 ? 4.392   8.355   -20.303 1.00 43.01  ? 343 PRO A C   1 
ATOM   2461 O O   . PRO A 1 314 ? 4.244   8.243   -21.514 1.00 46.88  ? 343 PRO A O   1 
ATOM   2462 C CB  . PRO A 1 314 ? 2.937   6.623   -19.094 1.00 48.73  ? 343 PRO A CB  1 
ATOM   2463 C CG  . PRO A 1 314 ? 1.958   6.256   -20.194 1.00 53.39  ? 343 PRO A CG  1 
ATOM   2464 C CD  . PRO A 1 314 ? 1.125   7.508   -20.438 1.00 51.87  ? 343 PRO A CD  1 
ATOM   2465 N N   . GLY A 1 315 ? 5.530   8.736   -19.727 1.00 42.81  ? 344 GLY A N   1 
ATOM   2466 C CA  . GLY A 1 315 ? 6.796   8.799   -20.429 1.00 42.42  ? 344 GLY A CA  1 
ATOM   2467 C C   . GLY A 1 315 ? 7.118   10.212  -20.887 1.00 43.61  ? 344 GLY A C   1 
ATOM   2468 O O   . GLY A 1 315 ? 8.167   10.428  -21.497 1.00 46.22  ? 344 GLY A O   1 
ATOM   2469 N N   . TYR A 1 316 ? 6.208   11.149  -20.586 1.00 47.00  ? 345 TYR A N   1 
ATOM   2470 C CA  . TYR A 1 316 ? 6.372   12.559  -20.921 1.00 48.75  ? 345 TYR A CA  1 
ATOM   2471 C C   . TYR A 1 316 ? 6.460   13.344  -19.613 1.00 49.85  ? 345 TYR A C   1 
ATOM   2472 O O   . TYR A 1 316 ? 5.787   13.001  -18.631 1.00 50.13  ? 345 TYR A O   1 
ATOM   2473 C CB  . TYR A 1 316 ? 5.264   12.968  -21.899 1.00 46.26  ? 345 TYR A CB  1 
ATOM   2474 C CG  . TYR A 1 316 ? 5.528   12.442  -23.306 1.00 49.20  ? 345 TYR A CG  1 
ATOM   2475 C CD1 . TYR A 1 316 ? 5.291   11.106  -23.632 1.00 45.55  ? 345 TYR A CD1 1 
ATOM   2476 C CD2 . TYR A 1 316 ? 6.058   13.266  -24.296 1.00 49.64  ? 345 TYR A CD2 1 
ATOM   2477 C CE1 . TYR A 1 316 ? 5.558   10.606  -24.893 1.00 41.55  ? 345 TYR A CE1 1 
ATOM   2478 C CE2 . TYR A 1 316 ? 6.330   12.774  -25.565 1.00 49.16  ? 345 TYR A CE2 1 
ATOM   2479 C CZ  . TYR A 1 316 ? 6.084   11.443  -25.865 1.00 44.98  ? 345 TYR A CZ  1 
ATOM   2480 O OH  . TYR A 1 316 ? 6.386   10.949  -27.114 1.00 46.35  ? 345 TYR A OH  1 
ATOM   2481 N N   . GLY A 1 317 ? 7.351   14.352  -19.593 1.00 48.65  ? 346 GLY A N   1 
ATOM   2482 C CA  . GLY A 1 317 ? 7.534   15.218  -18.433 1.00 47.27  ? 346 GLY A CA  1 
ATOM   2483 C C   . GLY A 1 317 ? 8.713   14.790  -17.553 1.00 51.58  ? 346 GLY A C   1 
ATOM   2484 O O   . GLY A 1 317 ? 9.239   13.688  -17.716 1.00 53.84  ? 346 GLY A O   1 
ATOM   2485 N N   . HIS A 1 318 ? 9.140   15.688  -16.647 1.00 43.70  ? 347 HIS A N   1 
ATOM   2486 C CA  . HIS A 1 318 ? 10.153  15.366  -15.657 1.00 52.76  ? 347 HIS A CA  1 
ATOM   2487 C C   . HIS A 1 318 ? 10.101  16.382  -14.514 1.00 51.83  ? 347 HIS A C   1 
ATOM   2488 O O   . HIS A 1 318 ? 9.714   17.539  -14.715 1.00 49.00  ? 347 HIS A O   1 
ATOM   2489 C CB  . HIS A 1 318 ? 11.559  15.306  -16.285 1.00 57.92  ? 347 HIS A CB  1 
ATOM   2490 C CG  . HIS A 1 318 ? 12.605  14.596  -15.455 1.00 61.56  ? 347 HIS A CG  1 
ATOM   2491 N ND1 . HIS A 1 318 ? 12.824  13.239  -15.565 1.00 63.30  ? 347 HIS A ND1 1 
ATOM   2492 C CD2 . HIS A 1 318 ? 13.491  15.020  -14.529 1.00 61.59  ? 347 HIS A CD2 1 
ATOM   2493 C CE1 . HIS A 1 318 ? 13.795  12.875  -14.730 1.00 62.29  ? 347 HIS A CE1 1 
ATOM   2494 N NE2 . HIS A 1 318 ? 14.220  13.940  -14.097 1.00 62.55  ? 347 HIS A NE2 1 
ATOM   2495 N N   . ALA A 1 319 ? 10.591  15.951  -13.344 1.00 49.16  ? 348 ALA A N   1 
ATOM   2496 C CA  . ALA A 1 319 ? 10.758  16.822  -12.189 1.00 60.72  ? 348 ALA A CA  1 
ATOM   2497 C C   . ALA A 1 319 ? 11.754  17.976  -12.410 1.00 64.01  ? 348 ALA A C   1 
ATOM   2498 O O   . ALA A 1 319 ? 11.722  18.937  -11.640 1.00 61.79  ? 348 ALA A O   1 
ATOM   2499 C CB  . ALA A 1 319 ? 11.160  15.983  -10.992 1.00 61.13  ? 348 ALA A CB  1 
ATOM   2500 N N   . VAL A 1 320 ? 12.802  17.877  -13.387 1.00 62.55  ? 349 VAL A N   1 
ATOM   2501 C CA  . VAL A 1 320 ? 13.604  19.130  -13.570 1.00 60.38  ? 349 VAL A CA  1 
ATOM   2502 C C   . VAL A 1 320 ? 13.840  19.379  -15.071 1.00 53.77  ? 349 VAL A C   1 
ATOM   2503 O O   . VAL A 1 320 ? 13.569  20.514  -15.520 1.00 49.04  ? 349 VAL A O   1 
ATOM   2504 C CB  . VAL A 1 320 ? 14.921  19.138  -12.763 1.00 62.98  ? 349 VAL A CB  1 
ATOM   2505 C CG1 . VAL A 1 320 ? 15.387  17.740  -12.376 1.00 63.85  ? 349 VAL A CG1 1 
ATOM   2506 C CG2 . VAL A 1 320 ? 16.031  19.931  -13.444 1.00 67.42  ? 349 VAL A CG2 1 
ATOM   2507 N N   . LEU A 1 321 ? 14.135  18.117  -15.884 1.00 54.73  ? 350 LEU A N   1 
ATOM   2508 C CA  . LEU A 1 321 ? 14.294  18.294  -17.325 1.00 59.45  ? 350 LEU A CA  1 
ATOM   2509 C C   . LEU A 1 321 ? 13.130  19.112  -17.886 1.00 61.50  ? 350 LEU A C   1 
ATOM   2510 O O   . LEU A 1 321 ? 11.979  18.924  -17.480 1.00 56.26  ? 350 LEU A O   1 
ATOM   2511 C CB  . LEU A 1 321 ? 14.401  16.957  -18.059 1.00 61.80  ? 350 LEU A CB  1 
ATOM   2512 C CG  . LEU A 1 321 ? 15.789  16.305  -18.076 1.00 55.70  ? 350 LEU A CG  1 
ATOM   2513 C CD1 . LEU A 1 321 ? 15.653  14.795  -17.997 1.00 58.57  ? 350 LEU A CD1 1 
ATOM   2514 C CD2 . LEU A 1 321 ? 16.581  16.694  -19.308 1.00 55.11  ? 350 LEU A CD2 1 
ATOM   2515 N N   . ARG A 1 322 ? 13.459  19.997  -18.841 1.00 60.49  ? 351 ARG A N   1 
ATOM   2516 C CA  . ARG A 1 322 ? 12.488  20.831  -19.531 1.00 60.80  ? 351 ARG A CA  1 
ATOM   2517 C C   . ARG A 1 322 ? 12.759  20.821  -21.037 1.00 57.54  ? 351 ARG A C   1 
ATOM   2518 O O   . ARG A 1 322 ? 12.560  21.829  -21.703 1.00 63.06  ? 351 ARG A O   1 
ATOM   2519 C CB  . ARG A 1 322 ? 12.544  22.269  -18.990 1.00 61.42  ? 351 ARG A CB  1 
ATOM   2520 C CG  . ARG A 1 322 ? 12.355  22.454  -17.489 1.00 59.73  ? 351 ARG A CG  1 
ATOM   2521 C CD  . ARG A 1 322 ? 10.892  22.404  -17.095 1.00 61.14  ? 351 ARG A CD  1 
ATOM   2522 N NE  . ARG A 1 322 ? 10.659  22.297  -15.647 1.00 62.29  ? 351 ARG A NE  1 
ATOM   2523 C CZ  . ARG A 1 322 ? 10.218  21.211  -15.017 1.00 61.91  ? 351 ARG A CZ  1 
ATOM   2524 N NH1 . ARG A 1 322 ? 9.828   21.308  -13.759 1.00 63.72  ? 351 ARG A NH1 1 
ATOM   2525 N NH2 . ARG A 1 322 ? 10.119  20.046  -15.648 1.00 57.98  ? 351 ARG A NH2 1 
ATOM   2526 N N   . LYS A 1 323 ? 13.213  19.683  -21.574 1.00 59.04  ? 352 LYS A N   1 
ATOM   2527 C CA  . LYS A 1 323 ? 13.351  19.496  -23.015 1.00 55.14  ? 352 LYS A CA  1 
ATOM   2528 C C   . LYS A 1 323 ? 13.530  17.999  -23.286 1.00 49.12  ? 352 LYS A C   1 
ATOM   2529 O O   . LYS A 1 323 ? 13.472  17.200  -22.349 1.00 52.19  ? 352 LYS A O   1 
ATOM   2530 C CB  . LYS A 1 323 ? 14.517  20.331  -23.560 1.00 59.21  ? 352 LYS A CB  1 
ATOM   2531 C CG  . LYS A 1 323 ? 14.293  20.902  -24.953 1.00 72.89  ? 352 LYS A CG  1 
ATOM   2532 C CD  . LYS A 1 323 ? 15.474  20.749  -25.917 1.00 83.68  ? 352 LYS A CD  1 
ATOM   2533 C CE  . LYS A 1 323 ? 16.611  21.741  -25.793 1.00 85.73  ? 352 LYS A CE  1 
ATOM   2534 N NZ  . LYS A 1 323 ? 16.408  22.974  -26.565 1.00 81.15  ? 352 LYS A NZ  1 
ATOM   2535 N N   . THR A 1 324 ? 13.745  17.601  -24.552 1.00 41.49  ? 353 THR A N   1 
ATOM   2536 C CA  . THR A 1 324 ? 13.836  16.181  -24.872 1.00 45.94  ? 353 THR A CA  1 
ATOM   2537 C C   . THR A 1 324 ? 15.035  15.568  -24.136 1.00 44.72  ? 353 THR A C   1 
ATOM   2538 O O   . THR A 1 324 ? 16.131  16.126  -24.134 1.00 40.27  ? 353 THR A O   1 
ATOM   2539 C CB  . THR A 1 324 ? 13.901  15.930  -26.380 1.00 43.59  ? 353 THR A CB  1 
ATOM   2540 O OG1 . THR A 1 324 ? 12.636  16.357  -26.856 1.00 42.18  ? 353 THR A OG1 1 
ATOM   2541 C CG2 . THR A 1 324 ? 14.025  14.459  -26.751 1.00 41.01  ? 353 THR A CG2 1 
ATOM   2542 N N   . ASP A 1 325 ? 14.789  14.420  -23.487 1.00 44.59  ? 354 ASP A N   1 
ATOM   2543 C CA  . ASP A 1 325 ? 15.792  13.757  -22.673 1.00 39.29  ? 354 ASP A CA  1 
ATOM   2544 C C   . ASP A 1 325 ? 16.793  13.111  -23.619 1.00 36.82  ? 354 ASP A C   1 
ATOM   2545 O O   . ASP A 1 325 ? 16.434  12.292  -24.465 1.00 34.34  ? 354 ASP A O   1 
ATOM   2546 C CB  . ASP A 1 325 ? 15.153  12.791  -21.688 1.00 39.59  ? 354 ASP A CB  1 
ATOM   2547 C CG  . ASP A 1 325 ? 16.059  11.940  -20.798 1.00 39.93  ? 354 ASP A CG  1 
ATOM   2548 O OD1 . ASP A 1 325 ? 17.325  12.086  -20.843 1.00 37.87  ? 354 ASP A OD1 1 
ATOM   2549 O OD2 . ASP A 1 325 ? 15.480  11.101  -20.072 1.00 39.34  ? 354 ASP A OD2 1 
ATOM   2550 N N   . PRO A 1 326 ? 18.082  13.474  -23.535 1.00 33.71  ? 355 PRO A N   1 
ATOM   2551 C CA  . PRO A 1 326 ? 19.051  12.873  -24.452 1.00 37.54  ? 355 PRO A CA  1 
ATOM   2552 C C   . PRO A 1 326 ? 19.149  11.347  -24.315 1.00 36.44  ? 355 PRO A C   1 
ATOM   2553 O O   . PRO A 1 326 ? 19.617  10.678  -25.231 1.00 39.10  ? 355 PRO A O   1 
ATOM   2554 C CB  . PRO A 1 326 ? 20.345  13.648  -24.103 1.00 36.41  ? 355 PRO A CB  1 
ATOM   2555 C CG  . PRO A 1 326 ? 20.129  14.119  -22.676 1.00 38.96  ? 355 PRO A CG  1 
ATOM   2556 C CD  . PRO A 1 326 ? 18.661  14.483  -22.621 1.00 37.17  ? 355 PRO A CD  1 
ATOM   2557 N N   . ARG A 1 327 ? 18.665  10.785  -23.193 1.00 34.31  ? 356 ARG A N   1 
ATOM   2558 C CA  . ARG A 1 327 ? 18.617  9.340   -22.997 1.00 32.10  ? 356 ARG A CA  1 
ATOM   2559 C C   . ARG A 1 327 ? 17.492  8.694   -23.819 1.00 32.48  ? 356 ARG A C   1 
ATOM   2560 O O   . ARG A 1 327 ? 17.565  7.526   -24.191 1.00 31.93  ? 356 ARG A O   1 
ATOM   2561 C CB  . ARG A 1 327 ? 18.466  9.059   -21.497 1.00 30.91  ? 356 ARG A CB  1 
ATOM   2562 C CG  . ARG A 1 327 ? 19.609  9.513   -20.593 1.00 28.54  ? 356 ARG A CG  1 
ATOM   2563 C CD  . ARG A 1 327 ? 19.314  9.256   -19.136 1.00 28.45  ? 356 ARG A CD  1 
ATOM   2564 N NE  . ARG A 1 327 ? 18.120  9.990   -18.714 1.00 28.67  ? 356 ARG A NE  1 
ATOM   2565 C CZ  . ARG A 1 327 ? 17.452  9.795   -17.582 1.00 33.48  ? 356 ARG A CZ  1 
ATOM   2566 N NH1 . ARG A 1 327 ? 17.873  8.928   -16.666 1.00 32.06  ? 356 ARG A NH1 1 
ATOM   2567 N NH2 . ARG A 1 327 ? 16.339  10.474  -17.360 1.00 33.70  ? 356 ARG A NH2 1 
ATOM   2568 N N   . TYR A 1 328 ? 16.423  9.458   -24.082 1.00 35.47  ? 357 TYR A N   1 
ATOM   2569 C CA  . TYR A 1 328 ? 15.451  9.123   -25.120 1.00 33.84  ? 357 TYR A CA  1 
ATOM   2570 C C   . TYR A 1 328 ? 16.063  9.088   -26.534 1.00 32.79  ? 357 TYR A C   1 
ATOM   2571 O O   . TYR A 1 328 ? 15.958  8.077   -27.237 1.00 32.49  ? 357 TYR A O   1 
ATOM   2572 C CB  . TYR A 1 328 ? 14.323  10.158  -25.026 1.00 34.27  ? 357 TYR A CB  1 
ATOM   2573 C CG  . TYR A 1 328 ? 13.185  9.884   -25.997 1.00 35.89  ? 357 TYR A CG  1 
ATOM   2574 C CD1 . TYR A 1 328 ? 12.133  9.040   -25.650 1.00 33.25  ? 357 TYR A CD1 1 
ATOM   2575 C CD2 . TYR A 1 328 ? 13.176  10.455  -27.273 1.00 37.64  ? 357 TYR A CD2 1 
ATOM   2576 C CE1 . TYR A 1 328 ? 11.103  8.778   -26.541 1.00 39.55  ? 357 TYR A CE1 1 
ATOM   2577 C CE2 . TYR A 1 328 ? 12.154  10.186  -28.176 1.00 34.06  ? 357 TYR A CE2 1 
ATOM   2578 C CZ  . TYR A 1 328 ? 11.111  9.359   -27.806 1.00 42.21  ? 357 TYR A CZ  1 
ATOM   2579 O OH  . TYR A 1 328 ? 10.100  9.087   -28.693 1.00 47.62  ? 357 TYR A OH  1 
ATOM   2580 N N   . THR A 1 329 ? 16.620  10.215  -26.997 1.00 35.44  ? 358 THR A N   1 
ATOM   2581 C CA  . THR A 1 329 ? 17.228  10.319  -28.323 1.00 36.97  ? 358 THR A CA  1 
ATOM   2582 C C   . THR A 1 329 ? 18.156  9.122   -28.578 1.00 37.60  ? 358 THR A C   1 
ATOM   2583 O O   . THR A 1 329 ? 18.080  8.468   -29.611 1.00 36.95  ? 358 THR A O   1 
ATOM   2584 C CB  . THR A 1 329 ? 17.965  11.658  -28.382 1.00 38.49  ? 358 THR A CB  1 
ATOM   2585 O OG1 . THR A 1 329 ? 17.015  12.657  -28.045 1.00 39.48  ? 358 THR A OG1 1 
ATOM   2586 C CG2 . THR A 1 329 ? 18.579  12.005  -29.725 1.00 44.52  ? 358 THR A CG2 1 
ATOM   2587 N N   . CYS A 1 330 ? 19.029  8.823   -27.608 1.00 39.57  ? 359 CYS A N   1 
ATOM   2588 C CA  . CYS A 1 330 ? 19.918  7.674   -27.629 1.00 40.53  ? 359 CYS A CA  1 
ATOM   2589 C C   . CYS A 1 330 ? 19.205  6.382   -28.018 1.00 35.90  ? 359 CYS A C   1 
ATOM   2590 O O   . CYS A 1 330 ? 19.686  5.594   -28.826 1.00 31.49  ? 359 CYS A O   1 
ATOM   2591 C CB  . CYS A 1 330 ? 20.457  7.439   -26.219 1.00 49.00  ? 359 CYS A CB  1 
ATOM   2592 S SG  . CYS A 1 330 ? 22.130  6.792   -26.240 1.00 71.56  ? 359 CYS A SG  1 
ATOM   2593 N N   . GLN A 1 331 ? 18.064  6.130   -27.381 1.00 31.38  ? 360 GLN A N   1 
ATOM   2594 C CA  . GLN A 1 331 ? 17.299  4.934   -27.652 1.00 33.34  ? 360 GLN A CA  1 
ATOM   2595 C C   . GLN A 1 331 ? 16.641  5.029   -29.025 1.00 35.87  ? 360 GLN A C   1 
ATOM   2596 O O   . GLN A 1 331 ? 16.560  4.041   -29.736 1.00 36.77  ? 360 GLN A O   1 
ATOM   2597 C CB  . GLN A 1 331 ? 16.346  4.724   -26.478 1.00 41.04  ? 360 GLN A CB  1 
ATOM   2598 C CG  . GLN A 1 331 ? 17.093  4.286   -25.223 1.00 41.01  ? 360 GLN A CG  1 
ATOM   2599 C CD  . GLN A 1 331 ? 16.214  4.157   -24.002 1.00 40.95  ? 360 GLN A CD  1 
ATOM   2600 O OE1 . GLN A 1 331 ? 16.031  3.066   -23.464 1.00 47.31  ? 360 GLN A OE1 1 
ATOM   2601 N NE2 . GLN A 1 331 ? 15.683  5.275   -23.534 1.00 43.12  ? 360 GLN A NE2 1 
ATOM   2602 N N   . ARG A 1 332 ? 16.154  6.215   -29.382 1.00 38.39  ? 361 ARG A N   1 
ATOM   2603 C CA  . ARG A 1 332 ? 15.591  6.450   -30.702 1.00 39.66  ? 361 ARG A CA  1 
ATOM   2604 C C   . ARG A 1 332 ? 16.633  6.063   -31.754 1.00 36.52  ? 361 ARG A C   1 
ATOM   2605 O O   . ARG A 1 332 ? 16.395  5.127   -32.519 1.00 40.90  ? 361 ARG A O   1 
ATOM   2606 C CB  . ARG A 1 332 ? 15.078  7.894   -30.702 1.00 39.58  ? 361 ARG A CB  1 
ATOM   2607 C CG  . ARG A 1 332 ? 14.435  8.304   -32.013 1.00 46.09  ? 361 ARG A CG  1 
ATOM   2608 C CD  . ARG A 1 332 ? 13.828  9.675   -31.875 1.00 49.13  ? 361 ARG A CD  1 
ATOM   2609 N NE  . ARG A 1 332 ? 13.598  10.227  -33.211 1.00 50.77  ? 361 ARG A NE  1 
ATOM   2610 C CZ  . ARG A 1 332 ? 12.853  9.672   -34.151 1.00 52.02  ? 361 ARG A CZ  1 
ATOM   2611 N NH1 . ARG A 1 332 ? 12.095  8.614   -33.890 1.00 51.97  ? 361 ARG A NH1 1 
ATOM   2612 N NH2 . ARG A 1 332 ? 12.825  10.233  -35.344 1.00 51.92  ? 361 ARG A NH2 1 
ATOM   2613 N N   . GLU A 1 333 ? 17.804  6.722   -31.718 1.00 33.01  ? 362 GLU A N   1 
ATOM   2614 C CA  . GLU A 1 333 ? 18.904  6.475   -32.655 1.00 37.39  ? 362 GLU A CA  1 
ATOM   2615 C C   . GLU A 1 333 ? 19.194  4.980   -32.780 1.00 36.96  ? 362 GLU A C   1 
ATOM   2616 O O   . GLU A 1 333 ? 19.443  4.472   -33.870 1.00 40.77  ? 362 GLU A O   1 
ATOM   2617 C CB  . GLU A 1 333 ? 20.215  7.170   -32.257 1.00 38.90  ? 362 GLU A CB  1 
ATOM   2618 C CG  . GLU A 1 333 ? 20.246  8.681   -32.514 1.00 42.10  ? 362 GLU A CG  1 
ATOM   2619 C CD  . GLU A 1 333 ? 21.399  9.459   -31.880 1.00 44.49  ? 362 GLU A CD  1 
ATOM   2620 O OE1 . GLU A 1 333 ? 22.270  8.830   -31.232 1.00 48.25  ? 362 GLU A OE1 1 
ATOM   2621 O OE2 . GLU A 1 333 ? 21.397  10.716  -31.958 1.00 40.39  ? 362 GLU A OE2 1 
ATOM   2622 N N   . PHE A 1 334 ? 19.176  4.268   -31.656 1.00 35.91  ? 363 PHE A N   1 
ATOM   2623 C CA  . PHE A 1 334 ? 19.437  2.840   -31.651 1.00 37.51  ? 363 PHE A CA  1 
ATOM   2624 C C   . PHE A 1 334 ? 18.316  2.084   -32.349 1.00 41.96  ? 363 PHE A C   1 
ATOM   2625 O O   . PHE A 1 334 ? 18.585  1.059   -32.979 1.00 37.07  ? 363 PHE A O   1 
ATOM   2626 C CB  . PHE A 1 334 ? 19.577  2.288   -30.232 1.00 40.21  ? 363 PHE A CB  1 
ATOM   2627 C CG  . PHE A 1 334 ? 19.968  0.823   -30.171 1.00 36.57  ? 363 PHE A CG  1 
ATOM   2628 C CD1 . PHE A 1 334 ? 19.011  -0.184  -30.226 1.00 33.98  ? 363 PHE A CD1 1 
ATOM   2629 C CD2 . PHE A 1 334 ? 21.292  0.458   -30.022 1.00 30.85  ? 363 PHE A CD2 1 
ATOM   2630 C CE1 . PHE A 1 334 ? 19.385  -1.517  -30.139 1.00 35.20  ? 363 PHE A CE1 1 
ATOM   2631 C CE2 . PHE A 1 334 ? 21.654  -0.880  -29.961 1.00 33.83  ? 363 PHE A CE2 1 
ATOM   2632 C CZ  . PHE A 1 334 ? 20.708  -1.860  -30.022 1.00 32.91  ? 363 PHE A CZ  1 
ATOM   2633 N N   . ALA A 1 335 ? 17.072  2.548   -32.168 1.00 38.80  ? 364 ALA A N   1 
ATOM   2634 C CA  . ALA A 1 335 ? 15.918  1.902   -32.786 1.00 43.47  ? 364 ALA A CA  1 
ATOM   2635 C C   . ALA A 1 335 ? 15.896  2.114   -34.310 1.00 41.87  ? 364 ALA A C   1 
ATOM   2636 O O   . ALA A 1 335 ? 15.694  1.157   -35.040 1.00 40.26  ? 364 ALA A O   1 
ATOM   2637 C CB  . ALA A 1 335 ? 14.652  2.412   -32.147 1.00 41.92  ? 364 ALA A CB  1 
ATOM   2638 N N   . LEU A 1 336 ? 16.042  3.368   -34.772 1.00 41.45  ? 365 LEU A N   1 
ATOM   2639 C CA  . LEU A 1 336 ? 16.142  3.699   -36.193 1.00 43.68  ? 365 LEU A CA  1 
ATOM   2640 C C   . LEU A 1 336 ? 17.160  2.791   -36.896 1.00 50.12  ? 365 LEU A C   1 
ATOM   2641 O O   . LEU A 1 336 ? 16.907  2.289   -37.993 1.00 49.13  ? 365 LEU A O   1 
ATOM   2642 C CB  . LEU A 1 336 ? 16.499  5.179   -36.347 1.00 42.39  ? 365 LEU A CB  1 
ATOM   2643 C CG  . LEU A 1 336 ? 15.398  6.184   -35.980 1.00 46.07  ? 365 LEU A CG  1 
ATOM   2644 C CD1 . LEU A 1 336 ? 15.911  7.623   -35.912 1.00 47.77  ? 365 LEU A CD1 1 
ATOM   2645 C CD2 . LEU A 1 336 ? 14.235  6.097   -36.949 1.00 48.63  ? 365 LEU A CD2 1 
ATOM   2646 N N   . LYS A 1 337 ? 18.298  2.543   -36.237 1.00 49.51  ? 366 LYS A N   1 
ATOM   2647 C CA  . LYS A 1 337 ? 19.339  1.680   -36.771 1.00 52.29  ? 366 LYS A CA  1 
ATOM   2648 C C   . LYS A 1 337 ? 18.933  0.209   -36.788 1.00 47.88  ? 366 LYS A C   1 
ATOM   2649 O O   . LYS A 1 337 ? 19.234  -0.477  -37.759 1.00 47.81  ? 366 LYS A O   1 
ATOM   2650 C CB  . LYS A 1 337 ? 20.658  1.717   -35.990 1.00 53.44  ? 366 LYS A CB  1 
ATOM   2651 C CG  . LYS A 1 337 ? 21.727  2.598   -36.588 1.00 60.25  ? 366 LYS A CG  1 
ATOM   2652 C CD  . LYS A 1 337 ? 23.114  2.489   -35.965 1.00 65.07  ? 366 LYS A CD  1 
ATOM   2653 C CE  . LYS A 1 337 ? 23.251  3.247   -34.676 1.00 70.27  ? 366 LYS A CE  1 
ATOM   2654 N NZ  . LYS A 1 337 ? 22.769  2.488   -33.519 1.00 78.09  ? 366 LYS A NZ  1 
ATOM   2655 N N   . HIS A 1 338 ? 18.325  -0.301  -35.711 1.00 41.66  ? 367 HIS A N   1 
ATOM   2656 C CA  . HIS A 1 338 ? 18.312  -1.744  -35.505 1.00 44.53  ? 367 HIS A CA  1 
ATOM   2657 C C   . HIS A 1 338 ? 16.920  -2.357  -35.634 1.00 40.14  ? 367 HIS A C   1 
ATOM   2658 O O   . HIS A 1 338 ? 16.830  -3.544  -35.912 1.00 39.07  ? 367 HIS A O   1 
ATOM   2659 C CB  . HIS A 1 338 ? 18.989  -2.136  -34.183 1.00 48.84  ? 367 HIS A CB  1 
ATOM   2660 C CG  . HIS A 1 338 ? 20.445  -1.777  -34.132 1.00 50.73  ? 367 HIS A CG  1 
ATOM   2661 N ND1 . HIS A 1 338 ? 21.397  -2.410  -34.906 1.00 50.05  ? 367 HIS A ND1 1 
ATOM   2662 C CD2 . HIS A 1 338 ? 21.100  -0.826  -33.450 1.00 51.72  ? 367 HIS A CD2 1 
ATOM   2663 C CE1 . HIS A 1 338 ? 22.577  -1.851  -34.698 1.00 52.46  ? 367 HIS A CE1 1 
ATOM   2664 N NE2 . HIS A 1 338 ? 22.428  -0.900  -33.801 1.00 52.84  ? 367 HIS A NE2 1 
ATOM   2665 N N   . LEU A 1 339 ? 15.838  -1.603  -35.402 1.00 45.86  ? 368 LEU A N   1 
ATOM   2666 C CA  . LEU A 1 339 ? 14.504  -2.189  -35.489 1.00 45.78  ? 368 LEU A CA  1 
ATOM   2667 C C   . LEU A 1 339 ? 13.508  -1.166  -36.030 1.00 52.83  ? 368 LEU A C   1 
ATOM   2668 O O   . LEU A 1 339 ? 12.449  -0.964  -35.436 1.00 50.82  ? 368 LEU A O   1 
ATOM   2669 C CB  . LEU A 1 339 ? 14.059  -2.696  -34.118 1.00 47.98  ? 368 LEU A CB  1 
ATOM   2670 C CG  . LEU A 1 339 ? 14.185  -1.692  -32.963 1.00 51.17  ? 368 LEU A CG  1 
ATOM   2671 C CD1 . LEU A 1 339 ? 12.915  -1.532  -32.139 1.00 46.88  ? 368 LEU A CD1 1 
ATOM   2672 C CD2 . LEU A 1 339 ? 15.322  -2.180  -32.087 1.00 49.63  ? 368 LEU A CD2 1 
ATOM   2673 N N   . PRO A 1 340 ? 13.786  -0.509  -37.180 1.00 54.51  ? 369 PRO A N   1 
ATOM   2674 C CA  . PRO A 1 340 ? 12.940  0.594   -37.635 1.00 57.41  ? 369 PRO A CA  1 
ATOM   2675 C C   . PRO A 1 340 ? 11.497  0.212   -37.974 1.00 51.53  ? 369 PRO A C   1 
ATOM   2676 O O   . PRO A 1 340 ? 10.620  1.076   -37.958 1.00 52.47  ? 369 PRO A O   1 
ATOM   2677 C CB  . PRO A 1 340 ? 13.716  1.170   -38.852 1.00 60.00  ? 369 PRO A CB  1 
ATOM   2678 C CG  . PRO A 1 340 ? 14.602  0.040   -39.332 1.00 58.53  ? 369 PRO A CG  1 
ATOM   2679 C CD  . PRO A 1 340 ? 14.917  -0.780  -38.085 1.00 59.29  ? 369 PRO A CD  1 
ATOM   2680 N N   . ASN A 1 341 ? 11.257  -1.081  -38.239 1.00 49.73  ? 370 ASN A N   1 
ATOM   2681 C CA  . ASN A 1 341 ? 9.975   -1.549  -38.752 1.00 58.35  ? 370 ASN A CA  1 
ATOM   2682 C C   . ASN A 1 341 ? 9.168   -2.254  -37.668 1.00 57.08  ? 370 ASN A C   1 
ATOM   2683 O O   . ASN A 1 341 ? 8.091   -2.786  -37.945 1.00 51.23  ? 370 ASN A O   1 
ATOM   2684 C CB  . ASN A 1 341 ? 10.145  -2.470  -39.959 1.00 59.43  ? 370 ASN A CB  1 
ATOM   2685 C CG  . ASN A 1 341 ? 10.740  -1.734  -41.138 1.00 59.68  ? 370 ASN A CG  1 
ATOM   2686 O OD1 . ASN A 1 341 ? 10.245  -0.664  -41.512 1.00 61.16  ? 370 ASN A OD1 1 
ATOM   2687 N ND2 . ASN A 1 341 ? 11.820  -2.255  -41.704 1.00 61.51  ? 370 ASN A ND2 1 
ATOM   2688 N N   . ASP A 1 342 ? 9.696   -2.245  -36.440 1.00 55.35  ? 371 ASP A N   1 
ATOM   2689 C CA  . ASP A 1 342 ? 8.984   -2.787  -35.299 1.00 53.41  ? 371 ASP A CA  1 
ATOM   2690 C C   . ASP A 1 342 ? 7.710   -1.983  -35.062 1.00 51.80  ? 371 ASP A C   1 
ATOM   2691 O O   . ASP A 1 342 ? 7.759   -0.759  -34.939 1.00 59.71  ? 371 ASP A O   1 
ATOM   2692 C CB  . ASP A 1 342 ? 9.860   -2.832  -34.060 1.00 54.32  ? 371 ASP A CB  1 
ATOM   2693 C CG  . ASP A 1 342 ? 9.120   -3.333  -32.835 1.00 53.66  ? 371 ASP A CG  1 
ATOM   2694 O OD1 . ASP A 1 342 ? 8.681   -4.506  -32.854 1.00 59.67  ? 371 ASP A OD1 1 
ATOM   2695 O OD2 . ASP A 1 342 ? 8.939   -2.524  -31.917 1.00 60.69  ? 371 ASP A OD2 1 
ATOM   2696 N N   . PRO A 1 343 ? 6.528   -2.644  -35.052 1.00 56.02  ? 372 PRO A N   1 
ATOM   2697 C CA  . PRO A 1 343 ? 5.250   -1.959  -34.828 1.00 57.32  ? 372 PRO A CA  1 
ATOM   2698 C C   . PRO A 1 343 ? 5.237   -1.059  -33.599 1.00 53.49  ? 372 PRO A C   1 
ATOM   2699 O O   . PRO A 1 343 ? 4.705   0.054   -33.629 1.00 51.92  ? 372 PRO A O   1 
ATOM   2700 C CB  . PRO A 1 343 ? 4.275   -3.139  -34.656 1.00 55.59  ? 372 PRO A CB  1 
ATOM   2701 C CG  . PRO A 1 343 ? 4.867   -4.220  -35.518 1.00 54.63  ? 372 PRO A CG  1 
ATOM   2702 C CD  . PRO A 1 343 ? 6.359   -4.081  -35.324 1.00 53.03  ? 372 PRO A CD  1 
ATOM   2703 N N   . MET A 1 344 ? 5.804   -1.572  -32.500 1.00 50.82  ? 373 MET A N   1 
ATOM   2704 C CA  . MET A 1 344 ? 5.756   -0.832  -31.250 1.00 48.28  ? 373 MET A CA  1 
ATOM   2705 C C   . MET A 1 344 ? 6.649   0.395   -31.384 1.00 42.87  ? 373 MET A C   1 
ATOM   2706 O O   . MET A 1 344 ? 6.247   1.487   -30.982 1.00 43.54  ? 373 MET A O   1 
ATOM   2707 C CB  . MET A 1 344 ? 6.133   -1.712  -30.053 1.00 55.53  ? 373 MET A CB  1 
ATOM   2708 C CG  . MET A 1 344 ? 5.065   -2.728  -29.682 1.00 61.38  ? 373 MET A CG  1 
ATOM   2709 S SD  . MET A 1 344 ? 3.581   -1.987  -28.967 1.00 64.70  ? 373 MET A SD  1 
ATOM   2710 C CE  . MET A 1 344 ? 4.210   -1.479  -27.361 1.00 66.59  ? 373 MET A CE  1 
ATOM   2711 N N   . PHE A 1 345 ? 7.819   0.246   -32.030 1.00 42.40  ? 374 PHE A N   1 
ATOM   2712 C CA  . PHE A 1 345 ? 8.718   1.385   -32.157 1.00 42.27  ? 374 PHE A CA  1 
ATOM   2713 C C   . PHE A 1 345 ? 8.028   2.470   -32.986 1.00 46.64  ? 374 PHE A C   1 
ATOM   2714 O O   . PHE A 1 345 ? 8.001   3.636   -32.593 1.00 49.70  ? 374 PHE A O   1 
ATOM   2715 C CB  . PHE A 1 345 ? 10.096  1.009   -32.708 1.00 42.18  ? 374 PHE A CB  1 
ATOM   2716 C CG  . PHE A 1 345 ? 10.846  2.236   -33.202 1.00 42.61  ? 374 PHE A CG  1 
ATOM   2717 C CD1 . PHE A 1 345 ? 11.297  3.197   -32.304 1.00 38.59  ? 374 PHE A CD1 1 
ATOM   2718 C CD2 . PHE A 1 345 ? 11.068  2.438   -34.564 1.00 41.84  ? 374 PHE A CD2 1 
ATOM   2719 C CE1 . PHE A 1 345 ? 11.955  4.332   -32.752 1.00 44.82  ? 374 PHE A CE1 1 
ATOM   2720 C CE2 . PHE A 1 345 ? 11.734  3.565   -35.016 1.00 41.10  ? 374 PHE A CE2 1 
ATOM   2721 C CZ  . PHE A 1 345 ? 12.189  4.510   -34.112 1.00 46.73  ? 374 PHE A CZ  1 
ATOM   2722 N N   . LYS A 1 346 ? 7.444   2.066   -34.123 1.00 53.93  ? 375 LYS A N   1 
ATOM   2723 C CA  . LYS A 1 346 ? 6.781   3.000   -35.018 1.00 50.79  ? 375 LYS A CA  1 
ATOM   2724 C C   . LYS A 1 346 ? 5.818   3.878   -34.222 1.00 43.70  ? 375 LYS A C   1 
ATOM   2725 O O   . LYS A 1 346 ? 5.821   5.109   -34.356 1.00 46.71  ? 375 LYS A O   1 
ATOM   2726 C CB  . LYS A 1 346 ? 6.090   2.199   -36.130 1.00 60.86  ? 375 LYS A CB  1 
ATOM   2727 C CG  . LYS A 1 346 ? 6.965   1.859   -37.334 1.00 65.25  ? 375 LYS A CG  1 
ATOM   2728 C CD  . LYS A 1 346 ? 6.461   0.650   -38.117 1.00 72.42  ? 375 LYS A CD  1 
ATOM   2729 C CE  . LYS A 1 346 ? 6.961   0.524   -39.535 1.00 75.25  ? 375 LYS A CE  1 
ATOM   2730 N NZ  . LYS A 1 346 ? 5.967   0.888   -40.552 1.00 71.21  ? 375 LYS A NZ  1 
ATOM   2731 N N   . LEU A 1 347 ? 5.028   3.227   -33.368 1.00 37.75  ? 376 LEU A N   1 
ATOM   2732 C CA  . LEU A 1 347 ? 4.056   3.894   -32.527 1.00 40.17  ? 376 LEU A CA  1 
ATOM   2733 C C   . LEU A 1 347 ? 4.733   4.900   -31.598 1.00 40.61  ? 376 LEU A C   1 
ATOM   2734 O O   . LEU A 1 347 ? 4.314   6.057   -31.511 1.00 41.49  ? 376 LEU A O   1 
ATOM   2735 C CB  . LEU A 1 347 ? 3.285   2.847   -31.744 1.00 40.11  ? 376 LEU A CB  1 
ATOM   2736 C CG  . LEU A 1 347 ? 2.100   3.415   -30.968 1.00 48.80  ? 376 LEU A CG  1 
ATOM   2737 C CD1 . LEU A 1 347 ? 0.997   3.957   -31.874 1.00 49.65  ? 376 LEU A CD1 1 
ATOM   2738 C CD2 . LEU A 1 347 ? 1.580   2.321   -30.080 1.00 59.23  ? 376 LEU A CD2 1 
ATOM   2739 N N   . VAL A 1 348 ? 5.773   4.443   -30.889 1.00 43.44  ? 377 VAL A N   1 
ATOM   2740 C CA  . VAL A 1 348 ? 6.544   5.325   -30.022 1.00 43.74  ? 377 VAL A CA  1 
ATOM   2741 C C   . VAL A 1 348 ? 6.996   6.521   -30.850 1.00 42.12  ? 377 VAL A C   1 
ATOM   2742 O O   . VAL A 1 348 ? 6.883   7.659   -30.399 1.00 41.24  ? 377 VAL A O   1 
ATOM   2743 C CB  . VAL A 1 348 ? 7.738   4.605   -29.353 1.00 43.78  ? 377 VAL A CB  1 
ATOM   2744 C CG1 . VAL A 1 348 ? 8.843   5.552   -28.890 1.00 39.32  ? 377 VAL A CG1 1 
ATOM   2745 C CG2 . VAL A 1 348 ? 7.270   3.740   -28.192 1.00 45.98  ? 377 VAL A CG2 1 
ATOM   2746 N N   . ALA A 1 349 ? 7.502   6.241   -32.065 1.00 45.30  ? 378 ALA A N   1 
ATOM   2747 C CA  . ALA A 1 349 ? 8.068   7.271   -32.925 1.00 45.05  ? 378 ALA A CA  1 
ATOM   2748 C C   . ALA A 1 349 ? 6.988   8.265   -33.361 1.00 49.67  ? 378 ALA A C   1 
ATOM   2749 O O   . ALA A 1 349 ? 7.204   9.476   -33.277 1.00 51.57  ? 378 ALA A O   1 
ATOM   2750 C CB  . ALA A 1 349 ? 8.777   6.631   -34.099 1.00 45.14  ? 378 ALA A CB  1 
ATOM   2751 N N   . GLN A 1 350 ? 5.842   7.732   -33.820 1.00 51.45  ? 379 GLN A N   1 
ATOM   2752 C CA  . GLN A 1 350 ? 4.632   8.508   -34.081 1.00 54.24  ? 379 GLN A CA  1 
ATOM   2753 C C   . GLN A 1 350 ? 4.262   9.403   -32.897 1.00 52.73  ? 379 GLN A C   1 
ATOM   2754 O O   . GLN A 1 350 ? 3.895   10.560  -33.098 1.00 49.06  ? 379 GLN A O   1 
ATOM   2755 C CB  . GLN A 1 350 ? 3.392   7.635   -34.307 1.00 59.99  ? 379 GLN A CB  1 
ATOM   2756 C CG  . GLN A 1 350 ? 3.406   6.779   -35.571 1.00 71.98  ? 379 GLN A CG  1 
ATOM   2757 C CD  . GLN A 1 350 ? 2.096   6.058   -35.834 1.00 76.14  ? 379 GLN A CD  1 
ATOM   2758 O OE1 . GLN A 1 350 ? 1.990   4.824   -35.759 1.00 74.00  ? 379 GLN A OE1 1 
ATOM   2759 N NE2 . GLN A 1 350 ? 1.071   6.837   -36.148 1.00 82.62  ? 379 GLN A NE2 1 
ATOM   2760 N N   . LEU A 1 351 ? 4.335   8.869   -31.662 1.00 51.89  ? 380 LEU A N   1 
ATOM   2761 C CA  . LEU A 1 351 ? 3.940   9.633   -30.477 1.00 50.10  ? 380 LEU A CA  1 
ATOM   2762 C C   . LEU A 1 351 ? 4.864   10.823  -30.231 1.00 47.70  ? 380 LEU A C   1 
ATOM   2763 O O   . LEU A 1 351 ? 4.425   11.826  -29.664 1.00 39.87  ? 380 LEU A O   1 
ATOM   2764 C CB  . LEU A 1 351 ? 3.860   8.763   -29.222 1.00 52.38  ? 380 LEU A CB  1 
ATOM   2765 C CG  . LEU A 1 351 ? 2.695   7.770   -29.152 1.00 50.13  ? 380 LEU A CG  1 
ATOM   2766 C CD1 . LEU A 1 351 ? 2.939   6.700   -28.094 1.00 50.78  ? 380 LEU A CD1 1 
ATOM   2767 C CD2 . LEU A 1 351 ? 1.399   8.516   -28.873 1.00 53.51  ? 380 LEU A CD2 1 
ATOM   2768 N N   . TYR A 1 352 ? 6.148   10.694  -30.596 1.00 50.70  ? 381 TYR A N   1 
ATOM   2769 C CA  . TYR A 1 352 ? 7.090   11.803  -30.505 1.00 48.66  ? 381 TYR A CA  1 
ATOM   2770 C C   . TYR A 1 352 ? 6.641   12.927  -31.443 1.00 49.56  ? 381 TYR A C   1 
ATOM   2771 O O   . TYR A 1 352 ? 6.768   14.111  -31.117 1.00 41.71  ? 381 TYR A O   1 
ATOM   2772 C CB  . TYR A 1 352 ? 8.494   11.282  -30.839 1.00 50.39  ? 381 TYR A CB  1 
ATOM   2773 C CG  . TYR A 1 352 ? 9.638   12.265  -30.623 1.00 54.91  ? 381 TYR A CG  1 
ATOM   2774 C CD1 . TYR A 1 352 ? 9.614   13.178  -29.569 1.00 56.66  ? 381 TYR A CD1 1 
ATOM   2775 C CD2 . TYR A 1 352 ? 10.755  12.275  -31.460 1.00 56.86  ? 381 TYR A CD2 1 
ATOM   2776 C CE1 . TYR A 1 352 ? 10.654  14.067  -29.359 1.00 50.68  ? 381 TYR A CE1 1 
ATOM   2777 C CE2 . TYR A 1 352 ? 11.797  13.172  -31.261 1.00 55.70  ? 381 TYR A CE2 1 
ATOM   2778 C CZ  . TYR A 1 352 ? 11.742  14.069  -30.209 1.00 49.86  ? 381 TYR A CZ  1 
ATOM   2779 O OH  . TYR A 1 352 ? 12.742  14.963  -29.969 1.00 57.78  ? 381 TYR A OH  1 
ATOM   2780 N N   . LYS A 1 353 ? 6.114   12.532  -32.615 1.00 58.88  ? 382 LYS A N   1 
ATOM   2781 C CA  . LYS A 1 353 ? 5.579   13.469  -33.598 1.00 64.29  ? 382 LYS A CA  1 
ATOM   2782 C C   . LYS A 1 353 ? 4.393   14.226  -33.005 1.00 60.08  ? 382 LYS A C   1 
ATOM   2783 O O   . LYS A 1 353 ? 4.350   15.455  -33.045 1.00 55.10  ? 382 LYS A O   1 
ATOM   2784 C CB  . LYS A 1 353 ? 5.149   12.774  -34.899 1.00 72.52  ? 382 LYS A CB  1 
ATOM   2785 C CG  . LYS A 1 353 ? 6.256   12.075  -35.711 1.00 83.16  ? 382 LYS A CG  1 
ATOM   2786 C CD  . LYS A 1 353 ? 5.789   11.078  -36.778 1.00 83.92  ? 382 LYS A CD  1 
ATOM   2787 C CE  . LYS A 1 353 ? 4.751   11.609  -37.736 1.00 86.19  ? 382 LYS A CE  1 
ATOM   2788 N NZ  . LYS A 1 353 ? 4.088   10.553  -38.512 1.00 78.52  ? 382 LYS A NZ  1 
ATOM   2789 N N   . ILE A 1 354 ? 3.467   13.463  -32.413 1.00 65.24  ? 383 ILE A N   1 
ATOM   2790 C CA  . ILE A 1 354 ? 2.161   13.950  -31.993 1.00 64.46  ? 383 ILE A CA  1 
ATOM   2791 C C   . ILE A 1 354 ? 2.224   14.592  -30.604 1.00 55.54  ? 383 ILE A C   1 
ATOM   2792 O O   . ILE A 1 354 ? 1.942   15.770  -30.470 1.00 55.51  ? 383 ILE A O   1 
ATOM   2793 C CB  . ILE A 1 354 ? 1.150   12.786  -32.032 1.00 76.00  ? 383 ILE A CB  1 
ATOM   2794 C CG1 . ILE A 1 354 ? 0.874   12.322  -33.470 1.00 83.99  ? 383 ILE A CG1 1 
ATOM   2795 C CG2 . ILE A 1 354 ? -0.142  13.123  -31.282 1.00 74.82  ? 383 ILE A CG2 1 
ATOM   2796 C CD1 . ILE A 1 354 ? 0.200   13.356  -34.355 1.00 89.83  ? 383 ILE A CD1 1 
ATOM   2797 N N   . VAL A 1 355 ? 2.590   13.808  -29.582 1.00 52.57  ? 384 VAL A N   1 
ATOM   2798 C CA  . VAL A 1 355 ? 2.289   14.101  -28.185 1.00 48.78  ? 384 VAL A CA  1 
ATOM   2799 C C   . VAL A 1 355 ? 2.800   15.484  -27.794 1.00 51.54  ? 384 VAL A C   1 
ATOM   2800 O O   . VAL A 1 355 ? 2.095   16.189  -27.075 1.00 58.87  ? 384 VAL A O   1 
ATOM   2801 C CB  . VAL A 1 355 ? 2.805   13.034  -27.185 1.00 44.24  ? 384 VAL A CB  1 
ATOM   2802 C CG1 . VAL A 1 355 ? 2.667   13.474  -25.733 1.00 43.55  ? 384 VAL A CG1 1 
ATOM   2803 C CG2 . VAL A 1 355 ? 2.109   11.687  -27.366 1.00 46.19  ? 384 VAL A CG2 1 
ATOM   2804 N N   . PRO A 1 356 ? 4.030   15.916  -28.172 1.00 52.44  ? 385 PRO A N   1 
ATOM   2805 C CA  . PRO A 1 356 ? 4.560   17.194  -27.684 1.00 56.19  ? 385 PRO A CA  1 
ATOM   2806 C C   . PRO A 1 356 ? 3.689   18.386  -28.071 1.00 61.83  ? 385 PRO A C   1 
ATOM   2807 O O   . PRO A 1 356 ? 3.562   19.354  -27.319 1.00 61.75  ? 385 PRO A O   1 
ATOM   2808 C CB  . PRO A 1 356 ? 5.957   17.261  -28.321 1.00 58.44  ? 385 PRO A CB  1 
ATOM   2809 C CG  . PRO A 1 356 ? 6.297   15.822  -28.586 1.00 52.71  ? 385 PRO A CG  1 
ATOM   2810 C CD  . PRO A 1 356 ? 4.985   15.211  -29.037 1.00 49.53  ? 385 PRO A CD  1 
ATOM   2811 N N   . ASN A 1 357 ? 3.086   18.287  -29.258 1.00 68.14  ? 386 ASN A N   1 
ATOM   2812 C CA  . ASN A 1 357 ? 2.118   19.266  -29.728 1.00 82.71  ? 386 ASN A CA  1 
ATOM   2813 C C   . ASN A 1 357 ? 1.097   19.537  -28.616 1.00 76.41  ? 386 ASN A C   1 
ATOM   2814 O O   . ASN A 1 357 ? 1.056   20.630  -28.049 1.00 77.70  ? 386 ASN A O   1 
ATOM   2815 C CB  . ASN A 1 357 ? 1.506   18.786  -31.046 1.00 87.24  ? 386 ASN A CB  1 
ATOM   2816 C CG  . ASN A 1 357 ? 1.106   19.900  -31.987 1.00 93.28  ? 386 ASN A CG  1 
ATOM   2817 O OD1 . ASN A 1 357 ? 0.597   19.624  -33.081 1.00 83.18  ? 386 ASN A OD1 1 
ATOM   2818 N ND2 . ASN A 1 357 ? 1.334   21.150  -31.606 1.00 98.96  ? 386 ASN A ND2 1 
ATOM   2819 N N   . VAL A 1 358 ? 0.344   18.493  -28.247 1.00 73.84  ? 387 VAL A N   1 
ATOM   2820 C CA  . VAL A 1 358 ? -0.906  18.636  -27.519 1.00 78.19  ? 387 VAL A CA  1 
ATOM   2821 C C   . VAL A 1 358 ? -0.659  19.199  -26.122 1.00 90.40  ? 387 VAL A C   1 
ATOM   2822 O O   . VAL A 1 358 ? -1.497  19.945  -25.621 1.00 100.95 ? 387 VAL A O   1 
ATOM   2823 C CB  . VAL A 1 358 ? -1.701  17.316  -27.438 1.00 78.01  ? 387 VAL A CB  1 
ATOM   2824 C CG1 . VAL A 1 358 ? -1.882  16.669  -28.810 1.00 68.82  ? 387 VAL A CG1 1 
ATOM   2825 C CG2 . VAL A 1 358 ? -1.073  16.331  -26.461 1.00 85.78  ? 387 VAL A CG2 1 
ATOM   2826 N N   . LEU A 1 359 ? 0.469   18.826  -25.494 1.00 96.25  ? 388 LEU A N   1 
ATOM   2827 C CA  . LEU A 1 359 ? 0.775   19.257  -24.136 1.00 96.83  ? 388 LEU A CA  1 
ATOM   2828 C C   . LEU A 1 359 ? 1.164   20.735  -24.119 1.00 97.04  ? 388 LEU A C   1 
ATOM   2829 O O   . LEU A 1 359 ? 1.213   21.335  -23.042 1.00 89.53  ? 388 LEU A O   1 
ATOM   2830 C CB  . LEU A 1 359 ? 1.878   18.400  -23.515 1.00 100.08 ? 388 LEU A CB  1 
ATOM   2831 C CG  . LEU A 1 359 ? 1.521   16.946  -23.191 1.00 99.45  ? 388 LEU A CG  1 
ATOM   2832 C CD1 . LEU A 1 359 ? 2.737   16.251  -22.602 1.00 98.41  ? 388 LEU A CD1 1 
ATOM   2833 C CD2 . LEU A 1 359 ? 0.335   16.847  -22.242 1.00 101.55 ? 388 LEU A CD2 1 
ATOM   2834 N N   . LEU A 1 360 ? 1.465   21.289  -25.309 1.00 102.92 ? 389 LEU A N   1 
ATOM   2835 C CA  . LEU A 1 360 ? 1.716   22.715  -25.484 1.00 111.08 ? 389 LEU A CA  1 
ATOM   2836 C C   . LEU A 1 360 ? 0.407   23.499  -25.377 1.00 111.29 ? 389 LEU A C   1 
ATOM   2837 O O   . LEU A 1 360 ? 0.348   24.514  -24.684 1.00 113.95 ? 389 LEU A O   1 
ATOM   2838 C CB  . LEU A 1 360 ? 2.447   22.977  -26.807 1.00 107.75 ? 389 LEU A CB  1 
ATOM   2839 C CG  . LEU A 1 360 ? 3.901   23.471  -26.730 1.00 100.69 ? 389 LEU A CG  1 
ATOM   2840 C CD1 . LEU A 1 360 ? 3.961   24.968  -27.018 1.00 101.60 ? 389 LEU A CD1 1 
ATOM   2841 C CD2 . LEU A 1 360 ? 4.597   23.177  -25.407 1.00 93.60  ? 389 LEU A CD2 1 
ATOM   2842 N N   . GLU A 1 361 ? -0.653  23.000  -26.023 1.00 107.11 ? 390 GLU A N   1 
ATOM   2843 C CA  . GLU A 1 361 ? -1.959  23.643  -25.968 1.00 98.93  ? 390 GLU A CA  1 
ATOM   2844 C C   . GLU A 1 361 ? -2.629  23.454  -24.605 1.00 95.16  ? 390 GLU A C   1 
ATOM   2845 O O   . GLU A 1 361 ? -3.721  23.968  -24.387 1.00 88.51  ? 390 GLU A O   1 
ATOM   2846 C CB  . GLU A 1 361 ? -2.801  23.079  -27.107 1.00 89.03  ? 390 GLU A CB  1 
ATOM   2847 C CG  . GLU A 1 361 ? -2.306  23.567  -28.462 1.00 91.46  ? 390 GLU A CG  1 
ATOM   2848 C CD  . GLU A 1 361 ? -2.517  22.600  -29.603 1.00 96.22  ? 390 GLU A CD  1 
ATOM   2849 O OE1 . GLU A 1 361 ? -2.750  21.408  -29.316 1.00 98.60  ? 390 GLU A OE1 1 
ATOM   2850 O OE2 . GLU A 1 361 ? -2.458  23.048  -30.770 1.00 94.05  ? 390 GLU A OE2 1 
ATOM   2851 N N   . GLN A 1 362 ? -1.978  22.722  -23.693 1.00 94.82  ? 391 GLN A N   1 
ATOM   2852 C CA  . GLN A 1 362 ? -2.518  22.477  -22.367 1.00 98.41  ? 391 GLN A CA  1 
ATOM   2853 C C   . GLN A 1 362 ? -2.110  23.619  -21.442 1.00 98.17  ? 391 GLN A C   1 
ATOM   2854 O O   . GLN A 1 362 ? -2.940  24.123  -20.690 1.00 103.47 ? 391 GLN A O   1 
ATOM   2855 C CB  . GLN A 1 362 ? -2.036  21.125  -21.833 1.00 106.12 ? 391 GLN A CB  1 
ATOM   2856 C CG  . GLN A 1 362 ? -2.838  20.578  -20.652 1.00 100.87 ? 391 GLN A CG  1 
ATOM   2857 C CD  . GLN A 1 362 ? -2.779  19.068  -20.551 1.00 94.70  ? 391 GLN A CD  1 
ATOM   2858 O OE1 . GLN A 1 362 ? -3.287  18.352  -21.418 1.00 81.51  ? 391 GLN A OE1 1 
ATOM   2859 N NE2 . GLN A 1 362 ? -2.151  18.559  -19.500 1.00 97.83  ? 391 GLN A NE2 1 
ATOM   2860 N N   . GLY A 1 363 ? -0.828  24.009  -21.492 1.00 84.63  ? 392 GLY A N   1 
ATOM   2861 C CA  . GLY A 1 363 ? -0.282  24.968  -20.544 1.00 84.69  ? 392 GLY A CA  1 
ATOM   2862 C C   . GLY A 1 363 ? 0.078   24.304  -19.212 1.00 88.20  ? 392 GLY A C   1 
ATOM   2863 O O   . GLY A 1 363 ? 0.860   24.847  -18.431 1.00 85.34  ? 392 GLY A O   1 
ATOM   2864 N N   . LYS A 1 364 ? -0.542  23.149  -18.938 1.00 92.13  ? 393 LYS A N   1 
ATOM   2865 C CA  . LYS A 1 364 ? -0.095  22.252  -17.887 1.00 96.51  ? 393 LYS A CA  1 
ATOM   2866 C C   . LYS A 1 364 ? 0.800   21.202  -18.536 1.00 91.97  ? 393 LYS A C   1 
ATOM   2867 O O   . LYS A 1 364 ? 0.384   20.514  -19.467 1.00 88.53  ? 393 LYS A O   1 
ATOM   2868 C CB  . LYS A 1 364 ? -1.283  21.658  -17.117 1.00 100.73 ? 393 LYS A CB  1 
ATOM   2869 C CG  . LYS A 1 364 ? -1.800  22.521  -15.964 1.00 103.58 ? 393 LYS A CG  1 
ATOM   2870 C CD  . LYS A 1 364 ? -3.202  22.164  -15.470 1.00 105.48 ? 393 LYS A CD  1 
ATOM   2871 C CE  . LYS A 1 364 ? -4.329  22.755  -16.276 1.00 104.45 ? 393 LYS A CE  1 
ATOM   2872 N NZ  . LYS A 1 364 ? -4.433  24.214  -16.146 1.00 99.00  ? 393 LYS A NZ  1 
ATOM   2873 N N   . ALA A 1 365 ? 2.051   21.164  -18.068 1.00 84.30  ? 394 ALA A N   1 
ATOM   2874 C CA  . ALA A 1 365 ? 3.050   20.188  -18.470 1.00 79.30  ? 394 ALA A CA  1 
ATOM   2875 C C   . ALA A 1 365 ? 4.416   20.688  -18.009 1.00 77.27  ? 394 ALA A C   1 
ATOM   2876 O O   . ALA A 1 365 ? 5.059   20.027  -17.198 1.00 79.22  ? 394 ALA A O   1 
ATOM   2877 C CB  . ALA A 1 365 ? 3.032   19.928  -19.961 1.00 74.65  ? 394 ALA A CB  1 
ATOM   2878 N N   . LYS A 1 366 ? 4.832   21.862  -18.512 1.00 72.85  ? 395 LYS A N   1 
ATOM   2879 C CA  . LYS A 1 366 ? 6.170   22.401  -18.279 1.00 86.80  ? 395 LYS A CA  1 
ATOM   2880 C C   . LYS A 1 366 ? 7.213   21.613  -19.083 1.00 84.90  ? 395 LYS A C   1 
ATOM   2881 O O   . LYS A 1 366 ? 8.071   22.208  -19.733 1.00 84.72  ? 395 LYS A O   1 
ATOM   2882 C CB  . LYS A 1 366 ? 6.607   22.448  -16.806 1.00 95.83  ? 395 LYS A CB  1 
ATOM   2883 C CG  . LYS A 1 366 ? 5.928   23.492  -15.919 1.00 105.11 ? 395 LYS A CG  1 
ATOM   2884 C CD  . LYS A 1 366 ? 6.788   23.954  -14.745 1.00 115.07 ? 395 LYS A CD  1 
ATOM   2885 C CE  . LYS A 1 366 ? 7.967   24.792  -15.170 1.00 122.98 ? 395 LYS A CE  1 
ATOM   2886 N NZ  . LYS A 1 366 ? 8.962   24.982  -14.109 1.00 126.62 ? 395 LYS A NZ  1 
ATOM   2887 N N   . ASN A 1 367 ? 7.161   20.273  -19.008 1.00 80.14  ? 396 ASN A N   1 
ATOM   2888 C CA  . ASN A 1 367 ? 7.988   19.415  -19.845 1.00 73.34  ? 396 ASN A CA  1 
ATOM   2889 C C   . ASN A 1 367 ? 7.088   18.584  -20.769 1.00 66.90  ? 396 ASN A C   1 
ATOM   2890 O O   . ASN A 1 367 ? 6.630   17.504  -20.394 1.00 73.62  ? 396 ASN A O   1 
ATOM   2891 C CB  . ASN A 1 367 ? 8.936   18.584  -18.983 1.00 67.37  ? 396 ASN A CB  1 
ATOM   2892 C CG  . ASN A 1 367 ? 9.831   17.675  -19.795 1.00 67.10  ? 396 ASN A CG  1 
ATOM   2893 O OD1 . ASN A 1 367 ? 10.188  16.577  -19.350 1.00 71.71  ? 396 ASN A OD1 1 
ATOM   2894 N ND2 . ASN A 1 367 ? 10.251  18.134  -20.963 1.00 64.17  ? 396 ASN A ND2 1 
ATOM   2895 N N   . PRO A 1 368 ? 6.818   19.050  -22.015 1.00 60.03  ? 397 PRO A N   1 
ATOM   2896 C CA  . PRO A 1 368 ? 5.988   18.304  -22.972 1.00 56.87  ? 397 PRO A CA  1 
ATOM   2897 C C   . PRO A 1 368 ? 6.709   17.235  -23.797 1.00 49.79  ? 397 PRO A C   1 
ATOM   2898 O O   . PRO A 1 368 ? 6.122   16.623  -24.681 1.00 54.69  ? 397 PRO A O   1 
ATOM   2899 C CB  . PRO A 1 368 ? 5.502   19.462  -23.865 1.00 59.31  ? 397 PRO A CB  1 
ATOM   2900 C CG  . PRO A 1 368 ? 6.705   20.372  -23.959 1.00 55.97  ? 397 PRO A CG  1 
ATOM   2901 C CD  . PRO A 1 368 ? 7.310   20.324  -22.567 1.00 55.16  ? 397 PRO A CD  1 
ATOM   2902 N N   . TRP A 1 369 ? 7.987   17.009  -23.489 1.00 44.63  ? 398 TRP A N   1 
ATOM   2903 C CA  . TRP A 1 369 ? 8.848   16.121  -24.251 1.00 47.97  ? 398 TRP A CA  1 
ATOM   2904 C C   . TRP A 1 369 ? 9.094   14.829  -23.478 1.00 39.09  ? 398 TRP A C   1 
ATOM   2905 O O   . TRP A 1 369 ? 8.915   14.758  -22.265 1.00 39.39  ? 398 TRP A O   1 
ATOM   2906 C CB  . TRP A 1 369 ? 10.166  16.844  -24.576 1.00 49.58  ? 398 TRP A CB  1 
ATOM   2907 C CG  . TRP A 1 369 ? 9.962   18.161  -25.275 1.00 46.65  ? 398 TRP A CG  1 
ATOM   2908 C CD1 . TRP A 1 369 ? 10.002  19.408  -24.724 1.00 47.09  ? 398 TRP A CD1 1 
ATOM   2909 C CD2 . TRP A 1 369 ? 9.658   18.342  -26.673 1.00 47.71  ? 398 TRP A CD2 1 
ATOM   2910 N NE1 . TRP A 1 369 ? 9.746   20.354  -25.679 1.00 41.43  ? 398 TRP A NE1 1 
ATOM   2911 C CE2 . TRP A 1 369 ? 9.528   19.735  -26.881 1.00 45.44  ? 398 TRP A CE2 1 
ATOM   2912 C CE3 . TRP A 1 369 ? 9.487   17.472  -27.762 1.00 51.60  ? 398 TRP A CE3 1 
ATOM   2913 C CZ2 . TRP A 1 369 ? 9.241   20.269  -28.136 1.00 47.77  ? 398 TRP A CZ2 1 
ATOM   2914 C CZ3 . TRP A 1 369 ? 9.194   18.008  -29.001 1.00 53.23  ? 398 TRP A CZ3 1 
ATOM   2915 C CH2 . TRP A 1 369 ? 9.076   19.385  -29.180 1.00 50.12  ? 398 TRP A CH2 1 
ATOM   2916 N N   . PRO A 1 370 ? 9.533   13.756  -24.158 1.00 39.64  ? 399 PRO A N   1 
ATOM   2917 C CA  . PRO A 1 370 ? 9.615   12.451  -23.510 1.00 38.85  ? 399 PRO A CA  1 
ATOM   2918 C C   . PRO A 1 370 ? 10.839  12.354  -22.609 1.00 35.71  ? 399 PRO A C   1 
ATOM   2919 O O   . PRO A 1 370 ? 11.836  13.032  -22.828 1.00 36.26  ? 399 PRO A O   1 
ATOM   2920 C CB  . PRO A 1 370 ? 9.654   11.502  -24.702 1.00 39.40  ? 399 PRO A CB  1 
ATOM   2921 C CG  . PRO A 1 370 ? 10.395  12.295  -25.767 1.00 40.25  ? 399 PRO A CG  1 
ATOM   2922 C CD  . PRO A 1 370 ? 9.939   13.724  -25.575 1.00 38.45  ? 399 PRO A CD  1 
ATOM   2923 N N   . ASN A 1 371 ? 10.730  11.517  -21.578 1.00 34.16  ? 400 ASN A N   1 
ATOM   2924 C CA  . ASN A 1 371 ? 11.878  11.114  -20.784 1.00 37.60  ? 400 ASN A CA  1 
ATOM   2925 C C   . ASN A 1 371 ? 12.387  9.765   -21.316 1.00 34.98  ? 400 ASN A C   1 
ATOM   2926 O O   . ASN A 1 371 ? 11.848  9.229   -22.272 1.00 34.16  ? 400 ASN A O   1 
ATOM   2927 C CB  . ASN A 1 371 ? 11.509  11.144  -19.300 1.00 39.88  ? 400 ASN A CB  1 
ATOM   2928 C CG  . ASN A 1 371 ? 10.374  10.203  -18.993 1.00 42.58  ? 400 ASN A CG  1 
ATOM   2929 O OD1 . ASN A 1 371 ? 10.446  9.022   -19.348 1.00 39.46  ? 400 ASN A OD1 1 
ATOM   2930 N ND2 . ASN A 1 371 ? 9.305   10.712  -18.393 1.00 45.20  ? 400 ASN A ND2 1 
ATOM   2931 N N   . VAL A 1 372 ? 13.431  9.222   -20.670 1.00 38.93  ? 401 VAL A N   1 
ATOM   2932 C CA  . VAL A 1 372 ? 14.082  7.973   -21.048 1.00 34.85  ? 401 VAL A CA  1 
ATOM   2933 C C   . VAL A 1 372 ? 13.064  6.837   -21.085 1.00 35.88  ? 401 VAL A C   1 
ATOM   2934 O O   . VAL A 1 372 ? 13.088  6.049   -22.011 1.00 40.12  ? 401 VAL A O   1 
ATOM   2935 C CB  . VAL A 1 372 ? 15.255  7.638   -20.099 1.00 36.44  ? 401 VAL A CB  1 
ATOM   2936 C CG1 . VAL A 1 372 ? 14.821  7.430   -18.651 1.00 34.48  ? 401 VAL A CG1 1 
ATOM   2937 C CG2 . VAL A 1 372 ? 16.059  6.423   -20.571 1.00 38.44  ? 401 VAL A CG2 1 
ATOM   2938 N N   . ASP A 1 373 ? 12.136  6.809   -20.119 1.00 35.22  ? 402 ASP A N   1 
ATOM   2939 C CA  . ASP A 1 373 ? 11.260  5.677   -19.901 1.00 31.46  ? 402 ASP A CA  1 
ATOM   2940 C C   . ASP A 1 373 ? 10.213  5.546   -21.004 1.00 33.03  ? 402 ASP A C   1 
ATOM   2941 O O   . ASP A 1 373 ? 9.592   4.500   -21.113 1.00 32.84  ? 402 ASP A O   1 
ATOM   2942 C CB  . ASP A 1 373 ? 10.536  5.762   -18.567 1.00 33.66  ? 402 ASP A CB  1 
ATOM   2943 C CG  . ASP A 1 373 ? 11.419  5.783   -17.327 1.00 37.33  ? 402 ASP A CG  1 
ATOM   2944 O OD1 . ASP A 1 373 ? 12.132  4.783   -17.060 1.00 37.18  ? 402 ASP A OD1 1 
ATOM   2945 O OD2 . ASP A 1 373 ? 11.380  6.813   -16.629 1.00 39.39  ? 402 ASP A OD2 1 
ATOM   2946 N N   . ALA A 1 374 ? 10.021  6.592   -21.818 1.00 35.97  ? 403 ALA A N   1 
ATOM   2947 C CA  . ALA A 1 374 ? 9.114   6.510   -22.957 1.00 37.47  ? 403 ALA A CA  1 
ATOM   2948 C C   . ALA A 1 374 ? 9.608   5.502   -24.006 1.00 36.75  ? 403 ALA A C   1 
ATOM   2949 O O   . ALA A 1 374 ? 8.814   4.912   -24.734 1.00 40.92  ? 403 ALA A O   1 
ATOM   2950 C CB  . ALA A 1 374 ? 8.922   7.902   -23.545 1.00 37.33  ? 403 ALA A CB  1 
ATOM   2951 N N   . HIS A 1 375 ? 10.921  5.254   -24.061 1.00 36.26  ? 404 HIS A N   1 
ATOM   2952 C CA  . HIS A 1 375 ? 11.504  4.529   -25.183 1.00 35.04  ? 404 HIS A CA  1 
ATOM   2953 C C   . HIS A 1 375 ? 12.050  3.155   -24.802 1.00 38.97  ? 404 HIS A C   1 
ATOM   2954 O O   . HIS A 1 375 ? 12.359  2.353   -25.684 1.00 40.54  ? 404 HIS A O   1 
ATOM   2955 C CB  . HIS A 1 375 ? 12.622  5.369   -25.794 1.00 32.45  ? 404 HIS A CB  1 
ATOM   2956 C CG  . HIS A 1 375 ? 12.682  5.247   -27.282 1.00 37.35  ? 404 HIS A CG  1 
ATOM   2957 N ND1 . HIS A 1 375 ? 12.690  4.037   -27.929 1.00 38.24  ? 404 HIS A ND1 1 
ATOM   2958 C CD2 . HIS A 1 375 ? 12.734  6.183   -28.240 1.00 35.90  ? 404 HIS A CD2 1 
ATOM   2959 C CE1 . HIS A 1 375 ? 12.706  4.258   -29.239 1.00 42.98  ? 404 HIS A CE1 1 
ATOM   2960 N NE2 . HIS A 1 375 ? 12.749  5.555   -29.448 1.00 37.68  ? 404 HIS A NE2 1 
ATOM   2961 N N   . SER A 1 376 ? 12.198  2.864   -23.503 1.00 37.61  ? 405 SER A N   1 
ATOM   2962 C CA  . SER A 1 376 ? 13.017  1.716   -23.101 1.00 37.51  ? 405 SER A CA  1 
ATOM   2963 C C   . SER A 1 376 ? 12.275  0.383   -23.255 1.00 32.92  ? 405 SER A C   1 
ATOM   2964 O O   . SER A 1 376 ? 12.793  -0.576  -23.839 1.00 34.39  ? 405 SER A O   1 
ATOM   2965 C CB  . SER A 1 376 ? 13.570  1.923   -21.700 1.00 37.30  ? 405 SER A CB  1 
ATOM   2966 O OG  . SER A 1 376 ? 12.700  2.779   -20.976 1.00 38.19  ? 405 SER A OG  1 
ATOM   2967 N N   . GLY A 1 377 ? 11.033  0.329   -22.784 1.00 35.12  ? 406 GLY A N   1 
ATOM   2968 C CA  . GLY A 1 377 ? 10.255  -0.902  -22.817 1.00 37.83  ? 406 GLY A CA  1 
ATOM   2969 C C   . GLY A 1 377 ? 10.303  -1.603  -24.176 1.00 37.45  ? 406 GLY A C   1 
ATOM   2970 O O   . GLY A 1 377 ? 10.490  -2.821  -24.245 1.00 38.19  ? 406 GLY A O   1 
ATOM   2971 N N   . VAL A 1 378 ? 10.105  -0.845  -25.257 1.00 37.30  ? 407 VAL A N   1 
ATOM   2972 C CA  . VAL A 1 378 ? 9.892   -1.469  -26.555 1.00 41.54  ? 407 VAL A CA  1 
ATOM   2973 C C   . VAL A 1 378 ? 11.205  -2.047  -27.072 1.00 39.72  ? 407 VAL A C   1 
ATOM   2974 O O   . VAL A 1 378 ? 11.200  -3.087  -27.707 1.00 40.19  ? 407 VAL A O   1 
ATOM   2975 C CB  . VAL A 1 378 ? 9.245   -0.521  -27.579 1.00 39.70  ? 407 VAL A CB  1 
ATOM   2976 C CG1 . VAL A 1 378 ? 7.913   -0.004  -27.054 1.00 38.16  ? 407 VAL A CG1 1 
ATOM   2977 C CG2 . VAL A 1 378 ? 10.167  0.622   -27.961 1.00 39.46  ? 407 VAL A CG2 1 
ATOM   2978 N N   . LEU A 1 379 ? 12.337  -1.431  -26.718 1.00 42.22  ? 408 LEU A N   1 
ATOM   2979 C CA  . LEU A 1 379 ? 13.631  -1.980  -27.072 1.00 38.00  ? 408 LEU A CA  1 
ATOM   2980 C C   . LEU A 1 379 ? 13.849  -3.321  -26.378 1.00 43.26  ? 408 LEU A C   1 
ATOM   2981 O O   . LEU A 1 379 ? 14.384  -4.244  -26.992 1.00 41.86  ? 408 LEU A O   1 
ATOM   2982 C CB  . LEU A 1 379 ? 14.754  -1.005  -26.741 1.00 39.84  ? 408 LEU A CB  1 
ATOM   2983 C CG  . LEU A 1 379 ? 14.838  0.247   -27.607 1.00 38.99  ? 408 LEU A CG  1 
ATOM   2984 C CD1 . LEU A 1 379 ? 15.804  1.211   -26.994 1.00 37.87  ? 408 LEU A CD1 1 
ATOM   2985 C CD2 . LEU A 1 379 ? 15.280  -0.083  -29.011 1.00 47.43  ? 408 LEU A CD2 1 
ATOM   2986 N N   . LEU A 1 380 ? 13.450  -3.430  -25.098 1.00 40.25  ? 409 LEU A N   1 
ATOM   2987 C CA  . LEU A 1 380 ? 13.612  -4.686  -24.378 1.00 35.87  ? 409 LEU A CA  1 
ATOM   2988 C C   . LEU A 1 380 ? 12.650  -5.759  -24.910 1.00 34.85  ? 409 LEU A C   1 
ATOM   2989 O O   . LEU A 1 380 ? 13.054  -6.899  -25.145 1.00 32.08  ? 409 LEU A O   1 
ATOM   2990 C CB  . LEU A 1 380 ? 13.428  -4.439  -22.881 1.00 33.99  ? 409 LEU A CB  1 
ATOM   2991 C CG  . LEU A 1 380 ? 14.466  -3.529  -22.211 1.00 34.20  ? 409 LEU A CG  1 
ATOM   2992 C CD1 . LEU A 1 380 ? 13.926  -3.006  -20.899 1.00 33.93  ? 409 LEU A CD1 1 
ATOM   2993 C CD2 . LEU A 1 380 ? 15.802  -4.235  -22.007 1.00 32.00  ? 409 LEU A CD2 1 
ATOM   2994 N N   . GLN A 1 381 ? 11.359  -5.432  -25.044 1.00 34.04  ? 410 GLN A N   1 
ATOM   2995 C CA  . GLN A 1 381 ? 10.380  -6.395  -25.538 1.00 40.15  ? 410 GLN A CA  1 
ATOM   2996 C C   . GLN A 1 381 ? 10.825  -6.967  -26.895 1.00 36.44  ? 410 GLN A C   1 
ATOM   2997 O O   . GLN A 1 381 ? 10.765  -8.172  -27.120 1.00 42.89  ? 410 GLN A O   1 
ATOM   2998 C CB  . GLN A 1 381 ? 9.022   -5.691  -25.591 1.00 46.34  ? 410 GLN A CB  1 
ATOM   2999 C CG  . GLN A 1 381 ? 7.881   -6.535  -26.149 1.00 53.26  ? 410 GLN A CG  1 
ATOM   3000 C CD  . GLN A 1 381 ? 6.528   -5.876  -25.996 1.00 57.95  ? 410 GLN A CD  1 
ATOM   3001 O OE1 . GLN A 1 381 ? 6.044   -5.204  -26.909 1.00 68.08  ? 410 GLN A OE1 1 
ATOM   3002 N NE2 . GLN A 1 381 ? 5.908   -6.039  -24.836 1.00 59.74  ? 410 GLN A NE2 1 
ATOM   3003 N N   . TYR A 1 382 ? 11.341  -6.101  -27.764 1.00 38.46  ? 411 TYR A N   1 
ATOM   3004 C CA  . TYR A 1 382 ? 11.792  -6.488  -29.094 1.00 43.66  ? 411 TYR A CA  1 
ATOM   3005 C C   . TYR A 1 382 ? 12.793  -7.645  -29.015 1.00 52.22  ? 411 TYR A C   1 
ATOM   3006 O O   . TYR A 1 382 ? 12.692  -8.594  -29.802 1.00 48.37  ? 411 TYR A O   1 
ATOM   3007 C CB  . TYR A 1 382 ? 12.395  -5.263  -29.799 1.00 41.85  ? 411 TYR A CB  1 
ATOM   3008 C CG  . TYR A 1 382 ? 12.852  -5.563  -31.220 1.00 42.04  ? 411 TYR A CG  1 
ATOM   3009 C CD1 . TYR A 1 382 ? 11.961  -5.493  -32.284 1.00 44.27  ? 411 TYR A CD1 1 
ATOM   3010 C CD2 . TYR A 1 382 ? 14.146  -5.990  -31.477 1.00 41.60  ? 411 TYR A CD2 1 
ATOM   3011 C CE1 . TYR A 1 382 ? 12.359  -5.789  -33.575 1.00 45.47  ? 411 TYR A CE1 1 
ATOM   3012 C CE2 . TYR A 1 382 ? 14.562  -6.287  -32.762 1.00 45.49  ? 411 TYR A CE2 1 
ATOM   3013 C CZ  . TYR A 1 382 ? 13.656  -6.209  -33.808 1.00 48.59  ? 411 TYR A CZ  1 
ATOM   3014 O OH  . TYR A 1 382 ? 14.062  -6.510  -35.068 1.00 53.75  ? 411 TYR A OH  1 
ATOM   3015 N N   . TYR A 1 383 ? 13.762  -7.576  -28.075 1.00 40.26  ? 412 TYR A N   1 
ATOM   3016 C CA  . TYR A 1 383 ? 14.827  -8.562  -28.046 1.00 35.47  ? 412 TYR A CA  1 
ATOM   3017 C C   . TYR A 1 383 ? 14.415  -9.799  -27.252 1.00 34.50  ? 412 TYR A C   1 
ATOM   3018 O O   . TYR A 1 383 ? 15.225  -10.711 -27.090 1.00 38.47  ? 412 TYR A O   1 
ATOM   3019 C CB  . TYR A 1 383 ? 16.121  -7.897  -27.569 1.00 37.80  ? 412 TYR A CB  1 
ATOM   3020 C CG  . TYR A 1 383 ? 16.761  -7.044  -28.655 1.00 34.76  ? 412 TYR A CG  1 
ATOM   3021 C CD1 . TYR A 1 383 ? 17.363  -7.631  -29.761 1.00 38.81  ? 412 TYR A CD1 1 
ATOM   3022 C CD2 . TYR A 1 383 ? 16.754  -5.656  -28.592 1.00 33.76  ? 412 TYR A CD2 1 
ATOM   3023 C CE1 . TYR A 1 383 ? 17.933  -6.860  -30.766 1.00 39.52  ? 412 TYR A CE1 1 
ATOM   3024 C CE2 . TYR A 1 383 ? 17.318  -4.875  -29.588 1.00 32.14  ? 412 TYR A CE2 1 
ATOM   3025 C CZ  . TYR A 1 383 ? 17.907  -5.476  -30.687 1.00 33.35  ? 412 TYR A CZ  1 
ATOM   3026 O OH  . TYR A 1 383 ? 18.475  -4.698  -31.658 1.00 35.18  ? 412 TYR A OH  1 
ATOM   3027 N N   . GLY A 1 384 ? 13.156  -9.876  -26.797 1.00 33.91  ? 413 GLY A N   1 
ATOM   3028 C CA  . GLY A 1 384 ? 12.657  -11.104 -26.194 1.00 32.99  ? 413 GLY A CA  1 
ATOM   3029 C C   . GLY A 1 384 ? 12.551  -11.023 -24.672 1.00 34.92  ? 413 GLY A C   1 
ATOM   3030 O O   . GLY A 1 384 ? 12.086  -11.969 -24.021 1.00 35.28  ? 413 GLY A O   1 
ATOM   3031 N N   . MET A 1 385 ? 12.967  -9.880  -24.115 1.00 35.30  ? 414 MET A N   1 
ATOM   3032 C CA  . MET A 1 385 ? 12.825  -9.639  -22.685 1.00 35.14  ? 414 MET A CA  1 
ATOM   3033 C C   . MET A 1 385 ? 11.494  -8.946  -22.427 1.00 36.52  ? 414 MET A C   1 
ATOM   3034 O O   . MET A 1 385 ? 11.392  -7.725  -22.509 1.00 38.00  ? 414 MET A O   1 
ATOM   3035 C CB  . MET A 1 385 ? 13.979  -8.781  -22.155 1.00 37.53  ? 414 MET A CB  1 
ATOM   3036 C CG  . MET A 1 385 ? 13.724  -8.271  -20.746 1.00 42.83  ? 414 MET A CG  1 
ATOM   3037 S SD  . MET A 1 385 ? 15.208  -8.122  -19.741 1.00 38.88  ? 414 MET A SD  1 
ATOM   3038 C CE  . MET A 1 385 ? 16.419  -9.413  -20.052 1.00 32.43  ? 414 MET A CE  1 
ATOM   3039 N N   . THR A 1 386 ? 10.491  -9.750  -22.067 1.00 39.51  ? 415 THR A N   1 
ATOM   3040 C CA  . THR A 1 386 ? 9.120   -9.289  -21.999 1.00 39.05  ? 415 THR A CA  1 
ATOM   3041 C C   . THR A 1 386 ? 8.616   -9.252  -20.557 1.00 39.60  ? 415 THR A C   1 
ATOM   3042 O O   . THR A 1 386 ? 7.471   -8.880  -20.315 1.00 37.86  ? 415 THR A O   1 
ATOM   3043 C CB  . THR A 1 386 ? 8.308   -10.250 -22.871 1.00 45.25  ? 415 THR A CB  1 
ATOM   3044 O OG1 . THR A 1 386 ? 8.384   -11.504 -22.205 1.00 45.98  ? 415 THR A OG1 1 
ATOM   3045 C CG2 . THR A 1 386 ? 8.862   -10.363 -24.283 1.00 42.31  ? 415 THR A CG2 1 
ATOM   3046 N N   . GLU A 1 387 ? 9.462   -9.648  -19.595 1.00 39.69  ? 416 GLU A N   1 
ATOM   3047 C CA  . GLU A 1 387 ? 9.035   -9.737  -18.211 1.00 35.51  ? 416 GLU A CA  1 
ATOM   3048 C C   . GLU A 1 387 ? 9.205   -8.358  -17.565 1.00 32.69  ? 416 GLU A C   1 
ATOM   3049 O O   . GLU A 1 387 ? 10.225  -8.080  -16.947 1.00 30.45  ? 416 GLU A O   1 
ATOM   3050 C CB  . GLU A 1 387 ? 9.801   -10.844 -17.478 1.00 39.36  ? 416 GLU A CB  1 
ATOM   3051 C CG  . GLU A 1 387 ? 9.737   -12.216 -18.150 1.00 38.80  ? 416 GLU A CG  1 
ATOM   3052 C CD  . GLU A 1 387 ? 10.817  -12.533 -19.177 1.00 39.86  ? 416 GLU A CD  1 
ATOM   3053 O OE1 . GLU A 1 387 ? 10.960  -13.737 -19.568 1.00 44.38  ? 416 GLU A OE1 1 
ATOM   3054 O OE2 . GLU A 1 387 ? 11.516  -11.582 -19.586 1.00 30.15  ? 416 GLU A OE2 1 
ATOM   3055 N N   . MET A 1 388 ? 8.169   -7.530  -17.682 1.00 29.60  ? 417 MET A N   1 
ATOM   3056 C CA  . MET A 1 388 ? 8.165   -6.134  -17.295 1.00 30.27  ? 417 MET A CA  1 
ATOM   3057 C C   . MET A 1 388 ? 8.524   -5.926  -15.827 1.00 30.49  ? 417 MET A C   1 
ATOM   3058 O O   . MET A 1 388 ? 8.996   -4.865  -15.477 1.00 30.53  ? 417 MET A O   1 
ATOM   3059 C CB  . MET A 1 388 ? 6.781   -5.516  -17.516 1.00 35.73  ? 417 MET A CB  1 
ATOM   3060 C CG  . MET A 1 388 ? 6.374   -5.478  -18.981 1.00 42.78  ? 417 MET A CG  1 
ATOM   3061 S SD  . MET A 1 388 ? 4.895   -4.471  -19.151 1.00 48.28  ? 417 MET A SD  1 
ATOM   3062 C CE  . MET A 1 388 ? 4.024   -5.595  -20.251 1.00 58.47  ? 417 MET A CE  1 
ATOM   3063 N N   . ASN A 1 389 ? 8.298   -6.905  -14.964 1.00 31.87  ? 418 ASN A N   1 
ATOM   3064 C CA  . ASN A 1 389 ? 8.603   -6.714  -13.558 1.00 34.86  ? 418 ASN A CA  1 
ATOM   3065 C C   . ASN A 1 389 ? 10.107  -6.646  -13.328 1.00 32.69  ? 418 ASN A C   1 
ATOM   3066 O O   . ASN A 1 389 ? 10.502  -6.233  -12.251 1.00 33.93  ? 418 ASN A O   1 
ATOM   3067 C CB  . ASN A 1 389 ? 7.995   -7.828  -12.724 1.00 36.20  ? 418 ASN A CB  1 
ATOM   3068 C CG  . ASN A 1 389 ? 6.515   -7.629  -12.533 1.00 41.75  ? 418 ASN A CG  1 
ATOM   3069 O OD1 . ASN A 1 389 ? 5.955   -6.637  -13.007 1.00 41.88  ? 418 ASN A OD1 1 
ATOM   3070 N ND2 . ASN A 1 389 ? 5.883   -8.557  -11.832 1.00 47.49  ? 418 ASN A ND2 1 
ATOM   3071 N N   . TYR A 1 390 ? 10.909  -7.037  -14.338 1.00 26.26  ? 419 TYR A N   1 
ATOM   3072 C CA  . TYR A 1 390 ? 12.351  -7.165  -14.226 1.00 26.35  ? 419 TYR A CA  1 
ATOM   3073 C C   . TYR A 1 390 ? 13.062  -5.917  -14.730 1.00 25.80  ? 419 TYR A C   1 
ATOM   3074 O O   . TYR A 1 390 ? 14.250  -5.708  -14.519 1.00 22.50  ? 419 TYR A O   1 
ATOM   3075 C CB  . TYR A 1 390 ? 12.769  -8.400  -15.029 1.00 26.29  ? 419 TYR A CB  1 
ATOM   3076 C CG  . TYR A 1 390 ? 14.228  -8.759  -14.836 1.00 25.00  ? 419 TYR A CG  1 
ATOM   3077 C CD1 . TYR A 1 390 ? 14.658  -9.436  -13.700 1.00 27.23  ? 419 TYR A CD1 1 
ATOM   3078 C CD2 . TYR A 1 390 ? 15.194  -8.283  -15.709 1.00 23.65  ? 419 TYR A CD2 1 
ATOM   3079 C CE1 . TYR A 1 390 ? 15.997  -9.721  -13.508 1.00 24.09  ? 419 TYR A CE1 1 
ATOM   3080 C CE2 . TYR A 1 390 ? 16.539  -8.572  -15.528 1.00 23.69  ? 419 TYR A CE2 1 
ATOM   3081 C CZ  . TYR A 1 390 ? 16.943  -9.254  -14.407 1.00 22.16  ? 419 TYR A CZ  1 
ATOM   3082 O OH  . TYR A 1 390 ? 18.268  -9.551  -14.293 1.00 24.48  ? 419 TYR A OH  1 
ATOM   3083 N N   . TYR A 1 391 ? 12.355  -5.094  -15.499 1.00 28.67  ? 420 TYR A N   1 
ATOM   3084 C CA  . TYR A 1 391 ? 12.979  -3.950  -16.143 1.00 29.00  ? 420 TYR A CA  1 
ATOM   3085 C C   . TYR A 1 391 ? 13.752  -3.077  -15.146 1.00 28.44  ? 420 TYR A C   1 
ATOM   3086 O O   . TYR A 1 391 ? 14.840  -2.577  -15.440 1.00 25.07  ? 420 TYR A O   1 
ATOM   3087 C CB  . TYR A 1 391 ? 11.829  -3.214  -16.847 1.00 36.04  ? 420 TYR A CB  1 
ATOM   3088 C CG  . TYR A 1 391 ? 11.299  -3.863  -18.127 1.00 34.67  ? 420 TYR A CG  1 
ATOM   3089 C CD1 . TYR A 1 391 ? 11.611  -5.167  -18.477 1.00 32.46  ? 420 TYR A CD1 1 
ATOM   3090 C CD2 . TYR A 1 391 ? 10.467  -3.158  -18.979 1.00 36.47  ? 420 TYR A CD2 1 
ATOM   3091 C CE1 . TYR A 1 391 ? 11.144  -5.722  -19.656 1.00 37.76  ? 420 TYR A CE1 1 
ATOM   3092 C CE2 . TYR A 1 391 ? 10.004  -3.699  -20.161 1.00 36.00  ? 420 TYR A CE2 1 
ATOM   3093 C CZ  . TYR A 1 391 ? 10.336  -4.991  -20.499 1.00 38.96  ? 420 TYR A CZ  1 
ATOM   3094 O OH  . TYR A 1 391 ? 9.909   -5.496  -21.678 1.00 37.26  ? 420 TYR A OH  1 
ATOM   3095 N N   . THR A 1 392 ? 13.203  -2.878  -13.950 1.00 25.11  ? 421 THR A N   1 
ATOM   3096 C CA  . THR A 1 392 ? 13.833  -1.940  -13.033 1.00 26.30  ? 421 THR A CA  1 
ATOM   3097 C C   . THR A 1 392 ? 15.130  -2.530  -12.454 1.00 22.50  ? 421 THR A C   1 
ATOM   3098 O O   . THR A 1 392 ? 16.012  -1.798  -11.974 1.00 21.19  ? 421 THR A O   1 
ATOM   3099 C CB  . THR A 1 392 ? 12.815  -1.571  -11.953 1.00 25.03  ? 421 THR A CB  1 
ATOM   3100 O OG1 . THR A 1 392 ? 11.656  -1.086  -12.606 1.00 25.45  ? 421 THR A OG1 1 
ATOM   3101 C CG2 . THR A 1 392 ? 13.311  -0.487  -11.019 1.00 29.49  ? 421 THR A CG2 1 
ATOM   3102 N N   . VAL A 1 393 ? 15.267  -3.860  -12.498 1.00 20.89  ? 422 VAL A N   1 
ATOM   3103 C CA  . VAL A 1 393 ? 16.524  -4.499  -12.150 1.00 21.08  ? 422 VAL A CA  1 
ATOM   3104 C C   . VAL A 1 393 ? 17.649  -4.018  -13.053 1.00 23.01  ? 422 VAL A C   1 
ATOM   3105 O O   . VAL A 1 393 ? 18.685  -3.587  -12.534 1.00 23.27  ? 422 VAL A O   1 
ATOM   3106 C CB  . VAL A 1 393 ? 16.434  -6.035  -12.159 1.00 23.61  ? 422 VAL A CB  1 
ATOM   3107 C CG1 . VAL A 1 393 ? 17.802  -6.705  -11.982 1.00 21.98  ? 422 VAL A CG1 1 
ATOM   3108 C CG2 . VAL A 1 393 ? 15.497  -6.500  -11.052 1.00 24.45  ? 422 VAL A CG2 1 
ATOM   3109 N N   . LEU A 1 394 ? 17.426  -4.008  -14.377 1.00 22.88  ? 423 LEU A N   1 
ATOM   3110 C CA  . LEU A 1 394 ? 18.381  -3.412  -15.294 1.00 25.54  ? 423 LEU A CA  1 
ATOM   3111 C C   . LEU A 1 394 ? 18.737  -1.979  -14.904 1.00 22.67  ? 423 LEU A C   1 
ATOM   3112 O O   . LEU A 1 394 ? 19.913  -1.642  -14.876 1.00 25.11  ? 423 LEU A O   1 
ATOM   3113 C CB  . LEU A 1 394 ? 17.932  -3.464  -16.760 1.00 29.57  ? 423 LEU A CB  1 
ATOM   3114 C CG  . LEU A 1 394 ? 17.606  -4.854  -17.305 1.00 32.92  ? 423 LEU A CG  1 
ATOM   3115 C CD1 . LEU A 1 394 ? 17.006  -4.799  -18.726 1.00 31.11  ? 423 LEU A CD1 1 
ATOM   3116 C CD2 . LEU A 1 394 ? 18.860  -5.687  -17.253 1.00 30.57  ? 423 LEU A CD2 1 
ATOM   3117 N N   . PHE A 1 395 ? 17.744  -1.116  -14.655 1.00 22.15  ? 424 PHE A N   1 
ATOM   3118 C CA  . PHE A 1 395 ? 17.992  0.272   -14.248 1.00 20.05  ? 424 PHE A CA  1 
ATOM   3119 C C   . PHE A 1 395 ? 18.875  0.309   -12.992 1.00 20.73  ? 424 PHE A C   1 
ATOM   3120 O O   . PHE A 1 395 ? 19.798  1.099   -12.878 1.00 22.34  ? 424 PHE A O   1 
ATOM   3121 C CB  . PHE A 1 395 ? 16.601  0.896   -14.046 1.00 22.17  ? 424 PHE A CB  1 
ATOM   3122 C CG  . PHE A 1 395 ? 16.509  2.408   -13.960 1.00 25.93  ? 424 PHE A CG  1 
ATOM   3123 C CD1 . PHE A 1 395 ? 17.579  3.199   -13.561 1.00 23.52  ? 424 PHE A CD1 1 
ATOM   3124 C CD2 . PHE A 1 395 ? 15.301  3.046   -14.250 1.00 29.37  ? 424 PHE A CD2 1 
ATOM   3125 C CE1 . PHE A 1 395 ? 17.466  4.584   -13.504 1.00 25.48  ? 424 PHE A CE1 1 
ATOM   3126 C CE2 . PHE A 1 395 ? 15.196  4.435   -14.173 1.00 27.93  ? 424 PHE A CE2 1 
ATOM   3127 C CZ  . PHE A 1 395 ? 16.273  5.202   -13.774 1.00 25.43  ? 424 PHE A CZ  1 
ATOM   3128 N N   . GLY A 1 396 ? 18.580  -0.535  -12.015 1.00 21.12  ? 425 GLY A N   1 
ATOM   3129 C CA  . GLY A 1 396 ? 19.367  -0.589  -10.809 1.00 20.39  ? 425 GLY A CA  1 
ATOM   3130 C C   . GLY A 1 396 ? 20.831  -0.938  -11.073 1.00 18.97  ? 425 GLY A C   1 
ATOM   3131 O O   . GLY A 1 396 ? 21.725  -0.369  -10.484 1.00 21.11  ? 425 GLY A O   1 
ATOM   3132 N N   . VAL A 1 397 ? 21.077  -1.936  -11.900 1.00 18.70  ? 426 VAL A N   1 
ATOM   3133 C CA  . VAL A 1 397 ? 22.434  -2.365  -12.148 1.00 21.23  ? 426 VAL A CA  1 
ATOM   3134 C C   . VAL A 1 397 ? 23.197  -1.231  -12.817 1.00 21.34  ? 426 VAL A C   1 
ATOM   3135 O O   . VAL A 1 397 ? 24.368  -0.997  -12.519 1.00 20.94  ? 426 VAL A O   1 
ATOM   3136 C CB  . VAL A 1 397 ? 22.382  -3.628  -13.011 1.00 19.57  ? 426 VAL A CB  1 
ATOM   3137 C CG1 . VAL A 1 397 ? 23.756  -3.952  -13.572 1.00 22.07  ? 426 VAL A CG1 1 
ATOM   3138 C CG2 . VAL A 1 397 ? 21.784  -4.780  -12.224 1.00 21.81  ? 426 VAL A CG2 1 
ATOM   3139 N N   . SER A 1 398 ? 22.526  -0.508  -13.715 1.00 23.00  ? 427 SER A N   1 
ATOM   3140 C CA  . SER A 1 398 ? 23.126  0.689   -14.313 1.00 21.05  ? 427 SER A CA  1 
ATOM   3141 C C   . SER A 1 398 ? 23.428  1.763   -13.267 1.00 20.39  ? 427 SER A C   1 
ATOM   3142 O O   . SER A 1 398 ? 24.516  2.349   -13.247 1.00 19.70  ? 427 SER A O   1 
ATOM   3143 C CB  . SER A 1 398 ? 22.276  1.248   -15.376 1.00 18.73  ? 427 SER A CB  1 
ATOM   3144 O OG  . SER A 1 398 ? 22.834  2.455   -15.880 1.00 19.63  ? 427 SER A OG  1 
ATOM   3145 N N   . ARG A 1 399 ? 22.414  2.105   -12.485 1.00 21.00  ? 428 ARG A N   1 
ATOM   3146 C CA  . ARG A 1 399 ? 22.542  3.172   -11.498 1.00 20.50  ? 428 ARG A CA  1 
ATOM   3147 C C   . ARG A 1 399 ? 23.646  2.895   -10.475 1.00 18.98  ? 428 ARG A C   1 
ATOM   3148 O O   . ARG A 1 399 ? 24.224  3.834   -9.944  1.00 21.47  ? 428 ARG A O   1 
ATOM   3149 C CB  . ARG A 1 399 ? 21.144  3.351   -10.897 1.00 20.96  ? 428 ARG A CB  1 
ATOM   3150 C CG  . ARG A 1 399 ? 20.946  4.538   -9.982  1.00 20.99  ? 428 ARG A CG  1 
ATOM   3151 C CD  . ARG A 1 399 ? 21.526  5.796   -10.546 1.00 20.51  ? 428 ARG A CD  1 
ATOM   3152 N NE  . ARG A 1 399 ? 21.005  6.231   -11.833 1.00 20.88  ? 428 ARG A NE  1 
ATOM   3153 C CZ  . ARG A 1 399 ? 19.862  6.935   -12.027 1.00 24.64  ? 428 ARG A CZ  1 
ATOM   3154 N NH1 . ARG A 1 399 ? 19.137  7.397   -11.010 1.00 21.63  ? 428 ARG A NH1 1 
ATOM   3155 N NH2 . ARG A 1 399 ? 19.483  7.258   -13.262 1.00 25.50  ? 428 ARG A NH2 1 
ATOM   3156 N N   . ALA A 1 400 ? 24.016  1.630   -10.242 1.00 17.49  ? 429 ALA A N   1 
ATOM   3157 C CA  . ALA A 1 400 ? 25.140  1.309   -9.378  1.00 18.57  ? 429 ALA A CA  1 
ATOM   3158 C C   . ALA A 1 400 ? 26.396  2.093   -9.775  1.00 19.86  ? 429 ALA A C   1 
ATOM   3159 O O   . ALA A 1 400 ? 27.136  2.599   -8.932  1.00 19.95  ? 429 ALA A O   1 
ATOM   3160 C CB  . ALA A 1 400 ? 25.370  -0.188  -9.351  1.00 18.85  ? 429 ALA A CB  1 
ATOM   3161 N N   . LEU A 1 401 ? 26.680  2.175   -11.073 1.00 19.18  ? 430 LEU A N   1 
ATOM   3162 C CA  . LEU A 1 401 ? 27.859  2.858   -11.526 1.00 21.32  ? 430 LEU A CA  1 
ATOM   3163 C C   . LEU A 1 401 ? 27.897  4.293   -11.013 1.00 21.81  ? 430 LEU A C   1 
ATOM   3164 O O   . LEU A 1 401 ? 28.935  4.756   -10.522 1.00 21.83  ? 430 LEU A O   1 
ATOM   3165 C CB  . LEU A 1 401 ? 27.931  2.808   -13.046 1.00 21.18  ? 430 LEU A CB  1 
ATOM   3166 C CG  . LEU A 1 401 ? 27.880  1.417   -13.671 1.00 27.30  ? 430 LEU A CG  1 
ATOM   3167 C CD1 . LEU A 1 401 ? 27.956  1.591   -15.195 1.00 29.25  ? 430 LEU A CD1 1 
ATOM   3168 C CD2 . LEU A 1 401 ? 28.973  0.509   -13.193 1.00 29.17  ? 430 LEU A CD2 1 
ATOM   3169 N N   . GLY A 1 402 ? 26.796  5.021   -11.179 1.00 19.81  ? 431 GLY A N   1 
ATOM   3170 C CA  . GLY A 1 402 ? 26.809  6.427   -10.797 1.00 19.25  ? 431 GLY A CA  1 
ATOM   3171 C C   . GLY A 1 402 ? 26.889  6.643   -9.286  1.00 18.62  ? 431 GLY A C   1 
ATOM   3172 O O   . GLY A 1 402 ? 27.743  7.389   -8.781  1.00 18.54  ? 431 GLY A O   1 
ATOM   3173 N N   . VAL A 1 403 ? 25.989  6.000   -8.540  1.00 18.35  ? 432 VAL A N   1 
ATOM   3174 C CA  . VAL A 1 403 ? 25.891  6.294   -7.113  1.00 18.98  ? 432 VAL A CA  1 
ATOM   3175 C C   . VAL A 1 403 ? 27.143  5.822   -6.363  1.00 18.85  ? 432 VAL A C   1 
ATOM   3176 O O   . VAL A 1 403 ? 27.563  6.445   -5.391  1.00 18.19  ? 432 VAL A O   1 
ATOM   3177 C CB  . VAL A 1 403 ? 24.590  5.714   -6.532  1.00 19.99  ? 432 VAL A CB  1 
ATOM   3178 C CG1 . VAL A 1 403 ? 23.402  6.156   -7.349  1.00 19.46  ? 432 VAL A CG1 1 
ATOM   3179 C CG2 . VAL A 1 403 ? 24.588  4.194   -6.403  1.00 21.13  ? 432 VAL A CG2 1 
ATOM   3180 N N   . LEU A 1 404 ? 27.756  4.717   -6.814  1.00 20.17  ? 433 LEU A N   1 
ATOM   3181 C CA  . LEU A 1 404 ? 28.982  4.221   -6.202  1.00 18.83  ? 433 LEU A CA  1 
ATOM   3182 C C   . LEU A 1 404 ? 30.184  5.088   -6.586  1.00 19.36  ? 433 LEU A C   1 
ATOM   3183 O O   . LEU A 1 404 ? 31.019  5.369   -5.722  1.00 17.65  ? 433 LEU A O   1 
ATOM   3184 C CB  . LEU A 1 404 ? 29.195  2.746   -6.516  1.00 19.62  ? 433 LEU A CB  1 
ATOM   3185 C CG  . LEU A 1 404 ? 28.098  1.828   -5.981  1.00 21.36  ? 433 LEU A CG  1 
ATOM   3186 C CD1 . LEU A 1 404 ? 28.342  0.403   -6.382  1.00 21.54  ? 433 LEU A CD1 1 
ATOM   3187 C CD2 . LEU A 1 404 ? 28.010  1.923   -4.470  1.00 23.09  ? 433 LEU A CD2 1 
ATOM   3188 N N   . ALA A 1 405 ? 30.264  5.551   -7.845  1.00 19.14  ? 434 ALA A N   1 
ATOM   3189 C CA  . ALA A 1 405 ? 31.301  6.511   -8.187  1.00 20.41  ? 434 ALA A CA  1 
ATOM   3190 C C   . ALA A 1 405 ? 31.245  7.689   -7.232  1.00 20.31  ? 434 ALA A C   1 
ATOM   3191 O O   . ALA A 1 405 ? 32.262  8.139   -6.728  1.00 19.85  ? 434 ALA A O   1 
ATOM   3192 C CB  . ALA A 1 405 ? 31.215  6.983   -9.629  1.00 22.97  ? 434 ALA A CB  1 
ATOM   3193 N N   . GLN A 1 406 ? 30.049  8.218   -6.979  1.00 20.08  ? 435 GLN A N   1 
ATOM   3194 C CA  . GLN A 1 406 ? 29.941  9.373   -6.114  1.00 21.34  ? 435 GLN A CA  1 
ATOM   3195 C C   . GLN A 1 406 ? 30.242  8.963   -4.660  1.00 19.77  ? 435 GLN A C   1 
ATOM   3196 O O   . GLN A 1 406 ? 30.812  9.729   -3.899  1.00 20.49  ? 435 GLN A O   1 
ATOM   3197 C CB  . GLN A 1 406 ? 28.573  10.041  -6.250  1.00 23.14  ? 435 GLN A CB  1 
ATOM   3198 C CG  . GLN A 1 406 ? 28.302  11.163  -5.251  1.00 24.32  ? 435 GLN A CG  1 
ATOM   3199 C CD  . GLN A 1 406 ? 29.322  12.282  -5.329  1.00 26.75  ? 435 GLN A CD  1 
ATOM   3200 O OE1 . GLN A 1 406 ? 29.692  12.709  -6.421  1.00 23.51  ? 435 GLN A OE1 1 
ATOM   3201 N NE2 . GLN A 1 406 ? 29.818  12.752  -4.186  1.00 25.13  ? 435 GLN A NE2 1 
ATOM   3202 N N   . LEU A 1 407 ? 29.816  7.780   -4.238  1.00 17.91  ? 436 LEU A N   1 
ATOM   3203 C CA  . LEU A 1 407 ? 30.011  7.356   -2.865  1.00 18.48  ? 436 LEU A CA  1 
ATOM   3204 C C   . LEU A 1 407 ? 31.503  7.344   -2.499  1.00 18.53  ? 436 LEU A C   1 
ATOM   3205 O O   . LEU A 1 407 ? 31.868  7.761   -1.419  1.00 21.67  ? 436 LEU A O   1 
ATOM   3206 C CB  . LEU A 1 407 ? 29.372  5.983   -2.682  1.00 18.41  ? 436 LEU A CB  1 
ATOM   3207 C CG  . LEU A 1 407 ? 29.372  5.508   -1.223  1.00 19.83  ? 436 LEU A CG  1 
ATOM   3208 C CD1 . LEU A 1 407 ? 28.601  6.522   -0.382  1.00 19.82  ? 436 LEU A CD1 1 
ATOM   3209 C CD2 . LEU A 1 407 ? 28.769  4.145   -1.023  1.00 19.17  ? 436 LEU A CD2 1 
ATOM   3210 N N   . ILE A 1 408 ? 32.349  6.925   -3.435  1.00 17.29  ? 437 ILE A N   1 
ATOM   3211 C CA  . ILE A 1 408 ? 33.788  6.974   -3.293  1.00 19.14  ? 437 ILE A CA  1 
ATOM   3212 C C   . ILE A 1 408 ? 34.255  8.409   -3.025  1.00 20.68  ? 437 ILE A C   1 
ATOM   3213 O O   . ILE A 1 408 ? 34.959  8.658   -2.057  1.00 24.59  ? 437 ILE A O   1 
ATOM   3214 C CB  . ILE A 1 408 ? 34.427  6.335   -4.534  1.00 21.69  ? 437 ILE A CB  1 
ATOM   3215 C CG1 . ILE A 1 408 ? 34.201  4.811   -4.576  1.00 21.79  ? 437 ILE A CG1 1 
ATOM   3216 C CG2 . ILE A 1 408 ? 35.911  6.657   -4.641  1.00 22.70  ? 437 ILE A CG2 1 
ATOM   3217 C CD1 . ILE A 1 408 ? 34.518  4.200   -5.932  1.00 23.99  ? 437 ILE A CD1 1 
ATOM   3218 N N   . TRP A 1 409 ? 33.805  9.351   -3.840  1.00 21.54  ? 438 TRP A N   1 
ATOM   3219 C CA  . TRP A 1 409 ? 34.117  10.754  -3.679  1.00 20.72  ? 438 TRP A CA  1 
ATOM   3220 C C   . TRP A 1 409 ? 33.537  11.379  -2.420  1.00 19.26  ? 438 TRP A C   1 
ATOM   3221 O O   . TRP A 1 409 ? 34.194  12.182  -1.786  1.00 18.71  ? 438 TRP A O   1 
ATOM   3222 C CB  . TRP A 1 409 ? 33.673  11.491  -4.939  1.00 21.81  ? 438 TRP A CB  1 
ATOM   3223 C CG  . TRP A 1 409 ? 34.720  11.384  -6.005  1.00 23.74  ? 438 TRP A CG  1 
ATOM   3224 C CD1 . TRP A 1 409 ? 34.732  10.575  -7.107  1.00 25.08  ? 438 TRP A CD1 1 
ATOM   3225 C CD2 . TRP A 1 409 ? 35.983  12.069  -5.991  1.00 24.54  ? 438 TRP A CD2 1 
ATOM   3226 N NE1 . TRP A 1 409 ? 35.913  10.729  -7.793  1.00 22.26  ? 438 TRP A NE1 1 
ATOM   3227 C CE2 . TRP A 1 409 ? 36.693  11.648  -7.138  1.00 24.38  ? 438 TRP A CE2 1 
ATOM   3228 C CE3 . TRP A 1 409 ? 36.569  13.018  -5.137  1.00 27.70  ? 438 TRP A CE3 1 
ATOM   3229 C CZ2 . TRP A 1 409 ? 37.953  12.163  -7.450  1.00 24.21  ? 438 TRP A CZ2 1 
ATOM   3230 C CZ3 . TRP A 1 409 ? 37.816  13.528  -5.453  1.00 26.34  ? 438 TRP A CZ3 1 
ATOM   3231 C CH2 . TRP A 1 409 ? 38.497  13.086  -6.590  1.00 25.93  ? 438 TRP A CH2 1 
ATOM   3232 N N   . SER A 1 410 ? 32.296  11.090  -2.065  1.00 17.27  ? 439 SER A N   1 
ATOM   3233 C CA  . SER A 1 410 ? 31.726  11.581  -0.812  1.00 19.15  ? 439 SER A CA  1 
ATOM   3234 C C   . SER A 1 410 ? 32.582  11.179  0.390   1.00 19.23  ? 439 SER A C   1 
ATOM   3235 O O   . SER A 1 410 ? 32.824  11.994  1.260   1.00 21.40  ? 439 SER A O   1 
ATOM   3236 C CB  . SER A 1 410 ? 30.319  11.082  -0.623  1.00 21.76  ? 439 SER A CB  1 
ATOM   3237 O OG  . SER A 1 410 ? 29.523  11.483  -1.714  1.00 22.93  ? 439 SER A OG  1 
ATOM   3238 N N   . ARG A 1 411 ? 33.154  9.970   0.399   1.00 18.02  ? 440 ARG A N   1 
ATOM   3239 C CA  . ARG A 1 411 ? 34.041  9.576   1.479   1.00 19.36  ? 440 ARG A CA  1 
ATOM   3240 C C   . ARG A 1 411 ? 35.431  10.206  1.321   1.00 20.89  ? 440 ARG A C   1 
ATOM   3241 O O   . ARG A 1 411 ? 36.005  10.662  2.298   1.00 19.98  ? 440 ARG A O   1 
ATOM   3242 C CB  . ARG A 1 411 ? 34.090  8.055   1.578   1.00 19.02  ? 440 ARG A CB  1 
ATOM   3243 C CG  . ARG A 1 411 ? 32.714  7.507   1.917   1.00 19.51  ? 440 ARG A CG  1 
ATOM   3244 C CD  . ARG A 1 411 ? 32.172  7.758   3.317   1.00 19.88  ? 440 ARG A CD  1 
ATOM   3245 N NE  . ARG A 1 411 ? 31.519  9.057   3.552   1.00 20.18  ? 440 ARG A NE  1 
ATOM   3246 C CZ  . ARG A 1 411 ? 30.362  9.472   3.040   1.00 22.16  ? 440 ARG A CZ  1 
ATOM   3247 N NH1 . ARG A 1 411 ? 29.730  8.717   2.182   1.00 21.31  ? 440 ARG A NH1 1 
ATOM   3248 N NH2 . ARG A 1 411 ? 29.867  10.663  3.333   1.00 22.05  ? 440 ARG A NH2 1 
ATOM   3249 N N   . ALA A 1 412 ? 35.931  10.303  0.091   1.00 18.52  ? 441 ALA A N   1 
ATOM   3250 C CA  . ALA A 1 412 ? 37.226  10.901  -0.159  1.00 19.39  ? 441 ALA A CA  1 
ATOM   3251 C C   . ALA A 1 412 ? 37.274  12.338  0.325   1.00 22.33  ? 441 ALA A C   1 
ATOM   3252 O O   . ALA A 1 412 ? 38.293  12.757  0.907   1.00 21.55  ? 441 ALA A O   1 
ATOM   3253 C CB  . ALA A 1 412 ? 37.534  10.816  -1.638  1.00 23.45  ? 441 ALA A CB  1 
ATOM   3254 N N   . LEU A 1 413 ? 36.179  13.066  0.055   1.00 21.04  ? 442 LEU A N   1 
ATOM   3255 C CA  . LEU A 1 413 ? 36.041  14.464  0.401   1.00 23.66  ? 442 LEU A CA  1 
ATOM   3256 C C   . LEU A 1 413 ? 35.492  14.696  1.797   1.00 25.31  ? 442 LEU A C   1 
ATOM   3257 O O   . LEU A 1 413 ? 35.283  15.845  2.177   1.00 26.68  ? 442 LEU A O   1 
ATOM   3258 C CB  . LEU A 1 413 ? 35.118  15.083  -0.630  1.00 24.83  ? 442 LEU A CB  1 
ATOM   3259 C CG  . LEU A 1 413 ? 35.627  14.990  -2.069  1.00 26.59  ? 442 LEU A CG  1 
ATOM   3260 C CD1 . LEU A 1 413 ? 34.595  15.510  -3.028  1.00 25.02  ? 442 LEU A CD1 1 
ATOM   3261 C CD2 . LEU A 1 413 ? 36.923  15.777  -2.185  1.00 25.30  ? 442 LEU A CD2 1 
ATOM   3262 N N   . GLY A 1 414 ? 35.206  13.637  2.556   1.00 26.00  ? 443 GLY A N   1 
ATOM   3263 C CA  . GLY A 1 414 ? 34.820  13.836  3.943   1.00 25.10  ? 443 GLY A CA  1 
ATOM   3264 C C   . GLY A 1 414 ? 33.432  14.453  4.130   1.00 26.25  ? 443 GLY A C   1 
ATOM   3265 O O   . GLY A 1 414 ? 33.222  15.123  5.136   1.00 27.09  ? 443 GLY A O   1 
ATOM   3266 N N   . PHE A 1 415 ? 32.462  14.143  3.244   1.00 23.30  ? 444 PHE A N   1 
ATOM   3267 C CA  . PHE A 1 415 ? 31.110  14.673  3.345   1.00 25.33  ? 444 PHE A CA  1 
ATOM   3268 C C   . PHE A 1 415 ? 30.499  14.126  4.636   1.00 22.60  ? 444 PHE A C   1 
ATOM   3269 O O   . PHE A 1 415 ? 30.708  12.954  4.980   1.00 22.14  ? 444 PHE A O   1 
ATOM   3270 C CB  . PHE A 1 415 ? 30.234  14.347  2.132   1.00 22.68  ? 444 PHE A CB  1 
ATOM   3271 C CG  . PHE A 1 415 ? 30.496  15.084  0.819   1.00 22.77  ? 444 PHE A CG  1 
ATOM   3272 C CD1 . PHE A 1 415 ? 31.526  15.994  0.659   1.00 19.72  ? 444 PHE A CD1 1 
ATOM   3273 C CD2 . PHE A 1 415 ? 29.701  14.826  -0.289  1.00 21.76  ? 444 PHE A CD2 1 
ATOM   3274 C CE1 . PHE A 1 415 ? 31.755  16.606  -0.539  1.00 19.84  ? 444 PHE A CE1 1 
ATOM   3275 C CE2 . PHE A 1 415 ? 29.929  15.456  -1.504  1.00 22.35  ? 444 PHE A CE2 1 
ATOM   3276 C CZ  . PHE A 1 415 ? 30.919  16.396  -1.602  1.00 22.08  ? 444 PHE A CZ  1 
ATOM   3277 N N   . PRO A 1 416 ? 29.881  15.001  5.455   1.00 21.69  ? 445 PRO A N   1 
ATOM   3278 C CA  . PRO A 1 416 ? 29.411  14.589  6.773   1.00 20.58  ? 445 PRO A CA  1 
ATOM   3279 C C   . PRO A 1 416 ? 28.054  13.894  6.678   1.00 21.58  ? 445 PRO A C   1 
ATOM   3280 O O   . PRO A 1 416 ? 27.479  13.757  5.614   1.00 20.41  ? 445 PRO A O   1 
ATOM   3281 C CB  . PRO A 1 416 ? 29.429  15.915  7.556   1.00 20.10  ? 445 PRO A CB  1 
ATOM   3282 C CG  . PRO A 1 416 ? 29.082  16.949  6.535   1.00 21.65  ? 445 PRO A CG  1 
ATOM   3283 C CD  . PRO A 1 416 ? 29.678  16.450  5.208   1.00 22.19  ? 445 PRO A CD  1 
ATOM   3284 N N   . LEU A 1 417 ? 27.510  13.520  7.831   1.00 21.46  ? 446 LEU A N   1 
ATOM   3285 C CA  . LEU A 1 417 ? 26.166  12.989  7.894   1.00 19.05  ? 446 LEU A CA  1 
ATOM   3286 C C   . LEU A 1 417 ? 25.187  13.999  7.318   1.00 21.85  ? 446 LEU A C   1 
ATOM   3287 O O   . LEU A 1 417 ? 25.263  15.169  7.679   1.00 20.73  ? 446 LEU A O   1 
ATOM   3288 C CB  . LEU A 1 417 ? 25.899  12.763  9.374   1.00 19.35  ? 446 LEU A CB  1 
ATOM   3289 C CG  . LEU A 1 417 ? 24.561  12.159  9.760   1.00 24.01  ? 446 LEU A CG  1 
ATOM   3290 C CD1 . LEU A 1 417 ? 24.538  10.703  9.385   1.00 24.41  ? 446 LEU A CD1 1 
ATOM   3291 C CD2 . LEU A 1 417 ? 24.355  12.352  11.275  1.00 26.69  ? 446 LEU A CD2 1 
ATOM   3292 N N   . GLU A 1 418 ? 24.254  13.520  6.475   1.00 19.45  ? 447 GLU A N   1 
ATOM   3293 C CA  . GLU A 1 418 ? 23.145  14.333  5.996   1.00 21.09  ? 447 GLU A CA  1 
ATOM   3294 C C   . GLU A 1 418 ? 22.090  14.393  7.104   1.00 22.15  ? 447 GLU A C   1 
ATOM   3295 O O   . GLU A 1 418 ? 21.577  13.376  7.509   1.00 21.62  ? 447 GLU A O   1 
ATOM   3296 C CB  . GLU A 1 418 ? 22.552  13.784  4.696   1.00 18.97  ? 447 GLU A CB  1 
ATOM   3297 C CG  . GLU A 1 418 ? 21.434  14.640  4.129   1.00 20.15  ? 447 GLU A CG  1 
ATOM   3298 C CD  . GLU A 1 418 ? 21.022  14.247  2.711   1.00 24.33  ? 447 GLU A CD  1 
ATOM   3299 O OE1 . GLU A 1 418 ? 19.800  14.085  2.512   1.00 25.44  ? 447 GLU A OE1 1 
ATOM   3300 O OE2 . GLU A 1 418 ? 21.887  14.108  1.811   1.00 21.40  ? 447 GLU A OE2 1 
ATOM   3301 N N   . ARG A 1 419 ? 21.791  15.595  7.591   1.00 23.03  ? 448 ARG A N   1 
ATOM   3302 C CA  . ARG A 1 419 ? 20.869  15.779  8.691   1.00 30.07  ? 448 ARG A CA  1 
ATOM   3303 C C   . ARG A 1 419 ? 20.231  17.166  8.550   1.00 28.15  ? 448 ARG A C   1 
ATOM   3304 O O   . ARG A 1 419 ? 20.608  18.102  9.244   1.00 30.85  ? 448 ARG A O   1 
ATOM   3305 C CB  . ARG A 1 419 ? 21.664  15.630  10.001  1.00 35.85  ? 448 ARG A CB  1 
ATOM   3306 C CG  . ARG A 1 419 ? 20.925  14.951  11.150  1.00 50.08  ? 448 ARG A CG  1 
ATOM   3307 C CD  . ARG A 1 419 ? 19.719  15.755  11.623  1.00 60.34  ? 448 ARG A CD  1 
ATOM   3308 N NE  . ARG A 1 419 ? 18.908  15.132  12.686  1.00 70.33  ? 448 ARG A NE  1 
ATOM   3309 C CZ  . ARG A 1 419 ? 17.692  15.556  13.092  1.00 72.48  ? 448 ARG A CZ  1 
ATOM   3310 N NH1 . ARG A 1 419 ? 17.065  14.936  14.092  1.00 60.55  ? 448 ARG A NH1 1 
ATOM   3311 N NH2 . ARG A 1 419 ? 17.110  16.601  12.495  1.00 74.38  ? 448 ARG A NH2 1 
ATOM   3312 N N   . PRO A 1 420 ? 19.223  17.360  7.679   1.00 25.60  ? 449 PRO A N   1 
ATOM   3313 C CA  . PRO A 1 420 ? 18.492  18.619  7.677   1.00 23.15  ? 449 PRO A CA  1 
ATOM   3314 C C   . PRO A 1 420 ? 17.669  18.626  8.964   1.00 26.25  ? 449 PRO A C   1 
ATOM   3315 O O   . PRO A 1 420 ? 17.532  17.613  9.656   1.00 24.14  ? 449 PRO A O   1 
ATOM   3316 C CB  . PRO A 1 420 ? 17.628  18.521  6.430   1.00 23.97  ? 449 PRO A CB  1 
ATOM   3317 C CG  . PRO A 1 420 ? 17.353  17.001  6.307   1.00 26.59  ? 449 PRO A CG  1 
ATOM   3318 C CD  . PRO A 1 420 ? 18.651  16.367  6.759   1.00 26.23  ? 449 PRO A CD  1 
ATOM   3319 N N   . LYS A 1 421 ? 17.087  19.786  9.245   1.00 24.93  ? 450 LYS A N   1 
ATOM   3320 C CA  . LYS A 1 421 ? 16.140  19.928  10.340  1.00 26.87  ? 450 LYS A CA  1 
ATOM   3321 C C   . LYS A 1 421 ? 14.719  19.747  9.808   1.00 22.16  ? 450 LYS A C   1 
ATOM   3322 O O   . LYS A 1 421 ? 14.382  20.260  8.748   1.00 28.15  ? 450 LYS A O   1 
ATOM   3323 C CB  . LYS A 1 421 ? 16.325  21.348  10.893  1.00 27.86  ? 450 LYS A CB  1 
ATOM   3324 C CG  . LYS A 1 421 ? 15.386  21.723  12.007  1.00 30.69  ? 450 LYS A CG  1 
ATOM   3325 C CD  . LYS A 1 421 ? 15.597  20.900  13.262  1.00 32.48  ? 450 LYS A CD  1 
ATOM   3326 C CE  . LYS A 1 421 ? 14.762  21.412  14.387  1.00 32.89  ? 450 LYS A CE  1 
ATOM   3327 N NZ  . LYS A 1 421 ? 14.981  20.497  15.517  1.00 34.28  ? 450 LYS A NZ  1 
ATOM   3328 N N   . SER A 1 422 ? 13.895  18.966  10.506  1.00 21.27  ? 451 SER A N   1 
ATOM   3329 C CA  . SER A 1 422 ? 12.486  18.867  10.179  1.00 21.09  ? 451 SER A CA  1 
ATOM   3330 C C   . SER A 1 422 ? 11.686  19.793  11.102  1.00 21.72  ? 451 SER A C   1 
ATOM   3331 O O   . SER A 1 422 ? 12.153  20.144  12.179  1.00 21.56  ? 451 SER A O   1 
ATOM   3332 C CB  . SER A 1 422 ? 11.982  17.465  10.275  1.00 20.15  ? 451 SER A CB  1 
ATOM   3333 O OG  . SER A 1 422 ? 11.759  17.069  11.628  1.00 18.60  ? 451 SER A OG  1 
ATOM   3334 N N   . MET A 1 423 ? 10.472  20.128  10.659  1.00 23.60  ? 452 MET A N   1 
ATOM   3335 C CA  . MET A 1 423 ? 9.483   20.837  11.454  1.00 24.16  ? 452 MET A CA  1 
ATOM   3336 C C   . MET A 1 423 ? 8.127   20.171  11.301  1.00 24.10  ? 452 MET A C   1 
ATOM   3337 O O   . MET A 1 423 ? 7.832   19.597  10.260  1.00 24.71  ? 452 MET A O   1 
ATOM   3338 C CB  . MET A 1 423 ? 9.289   22.263  10.946  1.00 25.70  ? 452 MET A CB  1 
ATOM   3339 C CG  . MET A 1 423 ? 10.554  23.043  10.793  1.00 29.01  ? 452 MET A CG  1 
ATOM   3340 S SD  . MET A 1 423 ? 11.198  23.407  12.416  1.00 36.24  ? 452 MET A SD  1 
ATOM   3341 C CE  . MET A 1 423 ? 10.344  24.976  12.701  1.00 38.30  ? 452 MET A CE  1 
ATOM   3342 N N   . SER A 1 424 ? 7.294   20.278  12.340  1.00 24.44  ? 453 SER A N   1 
ATOM   3343 C CA  . SER A 1 424 ? 5.890   19.965  12.189  1.00 27.37  ? 453 SER A CA  1 
ATOM   3344 C C   . SER A 1 424 ? 5.208   21.191  11.617  1.00 26.83  ? 453 SER A C   1 
ATOM   3345 O O   . SER A 1 424 ? 5.733   22.302  11.749  1.00 27.67  ? 453 SER A O   1 
ATOM   3346 C CB  . SER A 1 424 ? 5.237   19.609  13.485  1.00 28.18  ? 453 SER A CB  1 
ATOM   3347 O OG  . SER A 1 424 ? 5.275   20.758  14.319  1.00 28.91  ? 453 SER A OG  1 
ATOM   3348 N N   . THR A 1 425 ? 3.991   20.944  11.131  1.00 26.83  ? 454 THR A N   1 
ATOM   3349 C CA  . THR A 1 425 ? 3.087   21.975  10.648  1.00 29.55  ? 454 THR A CA  1 
ATOM   3350 C C   . THR A 1 425 ? 2.876   23.007  11.757  1.00 30.62  ? 454 THR A C   1 
ATOM   3351 O O   . THR A 1 425 ? 2.962   24.212  11.493  1.00 30.54  ? 454 THR A O   1 
ATOM   3352 C CB  . THR A 1 425 ? 1.763   21.346  10.215  1.00 26.57  ? 454 THR A CB  1 
ATOM   3353 O OG1 . THR A 1 425 ? 1.987   20.600  9.021   1.00 24.74  ? 454 THR A OG1 1 
ATOM   3354 C CG2 . THR A 1 425 ? 0.694   22.378  9.888   1.00 26.85  ? 454 THR A CG2 1 
ATOM   3355 N N   . GLU A 1 426 ? 2.579   22.509  12.970  1.00 32.49  ? 455 GLU A N   1 
ATOM   3356 C CA  . GLU A 1 426 ? 2.394   23.339  14.160  1.00 39.29  ? 455 GLU A CA  1 
ATOM   3357 C C   . GLU A 1 426 ? 3.638   24.180  14.424  1.00 33.01  ? 455 GLU A C   1 
ATOM   3358 O O   . GLU A 1 426 ? 3.561   25.379  14.688  1.00 32.06  ? 455 GLU A O   1 
ATOM   3359 C CB  . GLU A 1 426 ? 2.148   22.468  15.400  1.00 46.59  ? 455 GLU A CB  1 
ATOM   3360 C CG  . GLU A 1 426 ? 2.186   23.225  16.726  1.00 55.79  ? 455 GLU A CG  1 
ATOM   3361 C CD  . GLU A 1 426 ? 2.268   22.355  17.981  1.00 75.36  ? 455 GLU A CD  1 
ATOM   3362 O OE1 . GLU A 1 426 ? 2.486   22.995  19.035  1.00 89.86  ? 455 GLU A OE1 1 
ATOM   3363 O OE2 . GLU A 1 426 ? 2.121   21.097  17.955  1.00 65.99  ? 455 GLU A OE2 1 
ATOM   3364 N N   . GLY A 1 427 ? 4.775   23.502  14.448  1.00 30.09  ? 456 GLY A N   1 
ATOM   3365 C CA  . GLY A 1 427 ? 6.054   24.144  14.681  1.00 26.97  ? 456 GLY A CA  1 
ATOM   3366 C C   . GLY A 1 427 ? 6.361   25.139  13.575  1.00 27.48  ? 456 GLY A C   1 
ATOM   3367 O O   . GLY A 1 427 ? 6.893   26.212  13.830  1.00 30.39  ? 456 GLY A O   1 
ATOM   3368 N N   . LEU A 1 428 ? 6.063   24.773  12.324  1.00 26.54  ? 457 LEU A N   1 
ATOM   3369 C CA  . LEU A 1 428 ? 6.420   25.667  11.235  1.00 29.65  ? 457 LEU A CA  1 
ATOM   3370 C C   . LEU A 1 428 ? 5.599   26.949  11.360  1.00 28.72  ? 457 LEU A C   1 
ATOM   3371 O O   . LEU A 1 428 ? 6.129   28.041  11.174  1.00 30.89  ? 457 LEU A O   1 
ATOM   3372 C CB  . LEU A 1 428 ? 6.120   25.006  9.899   1.00 25.76  ? 457 LEU A CB  1 
ATOM   3373 C CG  . LEU A 1 428 ? 7.216   24.987  8.847   1.00 29.43  ? 457 LEU A CG  1 
ATOM   3374 C CD1 . LEU A 1 428 ? 6.517   24.652  7.556   1.00 26.94  ? 457 LEU A CD1 1 
ATOM   3375 C CD2 . LEU A 1 428 ? 8.168   26.144  8.716   1.00 26.35  ? 457 LEU A CD2 1 
ATOM   3376 N N   . MET A 1 429 ? 4.301   26.774  11.643  1.00 29.66  ? 458 MET A N   1 
ATOM   3377 C CA  . MET A 1 429 ? 3.365   27.888  11.787  1.00 32.52  ? 458 MET A CA  1 
ATOM   3378 C C   . MET A 1 429 ? 3.821   28.862  12.867  1.00 30.01  ? 458 MET A C   1 
ATOM   3379 O O   . MET A 1 429 ? 3.677   30.086  12.717  1.00 29.64  ? 458 MET A O   1 
ATOM   3380 C CB  . MET A 1 429 ? 1.979   27.392  12.170  1.00 31.69  ? 458 MET A CB  1 
ATOM   3381 C CG  . MET A 1 429 ? 1.179   26.847  11.013  1.00 33.14  ? 458 MET A CG  1 
ATOM   3382 S SD  . MET A 1 429 ? -0.294  26.172  11.795  1.00 42.08  ? 458 MET A SD  1 
ATOM   3383 C CE  . MET A 1 429 ? -1.200  25.458  10.428  1.00 33.88  ? 458 MET A CE  1 
ATOM   3384 N N   . LYS A 1 430 ? 4.417   28.314  13.925  1.00 30.85  ? 459 LYS A N   1 
ATOM   3385 C CA  . LYS A 1 430 ? 4.869   29.151  15.017  1.00 33.47  ? 459 LYS A CA  1 
ATOM   3386 C C   . LYS A 1 430 ? 6.172   29.824  14.622  1.00 33.99  ? 459 LYS A C   1 
ATOM   3387 O O   . LYS A 1 430 ? 6.423   30.967  15.001  1.00 30.58  ? 459 LYS A O   1 
ATOM   3388 C CB  . LYS A 1 430 ? 4.934   28.374  16.332  1.00 38.96  ? 459 LYS A CB  1 
ATOM   3389 C CG  . LYS A 1 430 ? 3.552   28.080  16.904  1.00 45.05  ? 459 LYS A CG  1 
ATOM   3390 C CD  . LYS A 1 430 ? 3.440   28.360  18.401  1.00 56.94  ? 459 LYS A CD  1 
ATOM   3391 C CE  . LYS A 1 430 ? 4.034   27.293  19.262  1.00 63.33  ? 459 LYS A CE  1 
ATOM   3392 N NZ  . LYS A 1 430 ? 3.188   26.094  19.304  1.00 67.34  ? 459 LYS A NZ  1 
ATOM   3393 N N   . PHE A 1 431 ? 6.978   29.145  13.810  1.00 29.84  ? 460 PHE A N   1 
ATOM   3394 C CA  . PHE A 1 431 ? 8.264   29.706  13.463  1.00 29.69  ? 460 PHE A CA  1 
ATOM   3395 C C   . PHE A 1 431 ? 8.031   30.895  12.544  1.00 29.98  ? 460 PHE A C   1 
ATOM   3396 O O   . PHE A 1 431 ? 8.684   31.929  12.704  1.00 33.61  ? 460 PHE A O   1 
ATOM   3397 C CB  . PHE A 1 431 ? 9.192   28.656  12.849  1.00 31.27  ? 460 PHE A CB  1 
ATOM   3398 C CG  . PHE A 1 431 ? 10.519  29.200  12.349  1.00 31.48  ? 460 PHE A CG  1 
ATOM   3399 C CD1 . PHE A 1 431 ? 11.580  29.400  13.224  1.00 36.27  ? 460 PHE A CD1 1 
ATOM   3400 C CD2 . PHE A 1 431 ? 10.692  29.535  11.016  1.00 30.73  ? 460 PHE A CD2 1 
ATOM   3401 C CE1 . PHE A 1 431 ? 12.780  29.925  12.777  1.00 39.99  ? 460 PHE A CE1 1 
ATOM   3402 C CE2 . PHE A 1 431 ? 11.891  30.064  10.578  1.00 35.62  ? 460 PHE A CE2 1 
ATOM   3403 C CZ  . PHE A 1 431 ? 12.941  30.250  11.455  1.00 36.71  ? 460 PHE A CZ  1 
ATOM   3404 N N   . VAL A 1 432 ? 7.159   30.729  11.560  1.00 30.52  ? 461 VAL A N   1 
ATOM   3405 C CA  . VAL A 1 432 ? 6.894   31.823  10.640  1.00 39.25  ? 461 VAL A CA  1 
ATOM   3406 C C   . VAL A 1 432 ? 6.301   33.017  11.399  1.00 41.98  ? 461 VAL A C   1 
ATOM   3407 O O   . VAL A 1 432 ? 6.695   34.151  11.160  1.00 41.25  ? 461 VAL A O   1 
ATOM   3408 C CB  . VAL A 1 432 ? 5.987   31.408  9.472   1.00 43.57  ? 461 VAL A CB  1 
ATOM   3409 C CG1 . VAL A 1 432 ? 6.631   30.310  8.636   1.00 41.70  ? 461 VAL A CG1 1 
ATOM   3410 C CG2 . VAL A 1 432 ? 4.614   30.989  9.953   1.00 56.30  ? 461 VAL A CG2 1 
ATOM   3411 N N   . ASP A 1 433 ? 5.420   32.719  12.348  1.00 40.89  ? 462 ASP A N   1 
ATOM   3412 C CA  . ASP A 1 433 ? 4.861   33.782  13.212  1.00 52.35  ? 462 ASP A CA  1 
ATOM   3413 C C   . ASP A 1 433 ? 5.934   34.081  14.259  1.00 59.38  ? 462 ASP A C   1 
ATOM   3414 O O   . ASP A 1 433 ? 5.682   33.835  15.444  1.00 69.60  ? 462 ASP A O   1 
ATOM   3415 C CB  . ASP A 1 433 ? 3.512   33.373  13.784  1.00 47.64  ? 462 ASP A CB  1 
ATOM   3416 C CG  . ASP A 1 433 ? 2.400   33.173  12.766  1.00 54.94  ? 462 ASP A CG  1 
ATOM   3417 O OD1 . ASP A 1 433 ? 2.599   33.561  11.598  1.00 66.79  ? 462 ASP A OD1 1 
ATOM   3418 O OD2 . ASP A 1 433 ? 1.339   32.648  13.154  1.00 51.72  ? 462 ASP A OD2 1 
ATOM   3419 N N   . SER A 1 434 ? 7.091   34.574  13.820  1.00 60.80  ? 463 SER A N   1 
ATOM   3420 C CA  . SER A 1 434 ? 8.216   34.861  14.738  1.00 57.00  ? 463 SER A CA  1 
ATOM   3421 C C   . SER A 1 434 ? 9.232   35.736  13.998  1.00 57.10  ? 463 SER A C   1 
ATOM   3422 O O   . SER A 1 434 ? 9.135   35.798  12.749  1.00 61.47  ? 463 SER A O   1 
ATOM   3423 C CB  . SER A 1 434 ? 8.842   33.580  15.258  1.00 61.24  ? 463 SER A CB  1 
ATOM   3424 O OG  . SER A 1 434 ? 10.016  33.223  14.544  1.00 54.71  ? 463 SER A OG  1 
ATOM   3425 N N   . SER B 1 1   ? -14.576 3.993   17.057  1.00 74.44  ? 30  SER B N   1 
ATOM   3426 C CA  . SER B 1 1   ? -14.492 4.020   18.542  1.00 84.16  ? 30  SER B CA  1 
ATOM   3427 C C   . SER B 1 1   ? -13.153 3.462   19.026  1.00 82.99  ? 30  SER B C   1 
ATOM   3428 O O   . SER B 1 1   ? -12.325 4.190   19.576  1.00 82.30  ? 30  SER B O   1 
ATOM   3429 C CB  . SER B 1 1   ? -15.647 3.267   19.165  1.00 84.89  ? 30  SER B CB  1 
ATOM   3430 O OG  . SER B 1 1   ? -15.447 3.115   20.565  1.00 84.25  ? 30  SER B OG  1 
ATOM   3431 N N   . THR B 1 2   ? -12.977 2.146   18.877  1.00 74.37  ? 31  THR B N   1 
ATOM   3432 C CA  . THR B 1 2   ? -11.716 1.507   19.208  1.00 67.08  ? 31  THR B CA  1 
ATOM   3433 C C   . THR B 1 2   ? -10.913 1.329   17.924  1.00 56.54  ? 31  THR B C   1 
ATOM   3434 O O   . THR B 1 2   ? -9.686  1.225   18.012  1.00 55.57  ? 31  THR B O   1 
ATOM   3435 C CB  . THR B 1 2   ? -11.923 0.178   19.944  1.00 68.44  ? 31  THR B CB  1 
ATOM   3436 O OG1 . THR B 1 2   ? -13.199 -0.313  19.539  1.00 76.23  ? 31  THR B OG1 1 
ATOM   3437 C CG2 . THR B 1 2   ? -11.880 0.310   21.459  1.00 62.07  ? 31  THR B CG2 1 
ATOM   3438 N N   . ASN B 1 3   ? -11.587 1.328   16.752  1.00 42.60  ? 32  ASN B N   1 
ATOM   3439 C CA  . ASN B 1 3   ? -10.882 1.058   15.505  1.00 39.84  ? 32  ASN B CA  1 
ATOM   3440 C C   . ASN B 1 3   ? -10.071 2.295   15.134  1.00 31.92  ? 32  ASN B C   1 
ATOM   3441 O O   . ASN B 1 3   ? -10.619 3.316   14.751  1.00 28.42  ? 32  ASN B O   1 
ATOM   3442 C CB  . ASN B 1 3   ? -11.732 0.592   14.329  1.00 37.37  ? 32  ASN B CB  1 
ATOM   3443 C CG  . ASN B 1 3   ? -10.871 -0.111  13.292  1.00 43.82  ? 32  ASN B CG  1 
ATOM   3444 O OD1 . ASN B 1 3   ? -9.740  0.302   12.982  1.00 39.29  ? 32  ASN B OD1 1 
ATOM   3445 N ND2 . ASN B 1 3   ? -11.341 -1.238  12.791  1.00 45.92  ? 32  ASN B ND2 1 
ATOM   3446 N N   . LEU B 1 4   ? -8.752  2.173   15.275  1.00 29.37  ? 33  LEU B N   1 
ATOM   3447 C CA  . LEU B 1 4   ? -7.833  3.275   15.042  1.00 27.77  ? 33  LEU B CA  1 
ATOM   3448 C C   . LEU B 1 4   ? -7.988  3.784   13.609  1.00 23.89  ? 33  LEU B C   1 
ATOM   3449 O O   . LEU B 1 4   ? -7.832  4.974   13.354  1.00 27.08  ? 33  LEU B O   1 
ATOM   3450 C CB  . LEU B 1 4   ? -6.423  2.757   15.341  1.00 27.21  ? 33  LEU B CB  1 
ATOM   3451 C CG  . LEU B 1 4   ? -5.266  3.727   15.070  1.00 28.84  ? 33  LEU B CG  1 
ATOM   3452 C CD1 . LEU B 1 4   ? -5.451  5.013   15.811  1.00 29.42  ? 33  LEU B CD1 1 
ATOM   3453 C CD2 . LEU B 1 4   ? -3.877  3.119   15.379  1.00 28.10  ? 33  LEU B CD2 1 
ATOM   3454 N N   . LYS B 1 5   ? -8.334  2.882   12.688  1.00 23.28  ? 34  LYS B N   1 
ATOM   3455 C CA  . LYS B 1 5   ? -8.438  3.240   11.296  1.00 24.01  ? 34  LYS B CA  1 
ATOM   3456 C C   . LYS B 1 5   ? -9.570  4.245   11.044  1.00 28.07  ? 34  LYS B C   1 
ATOM   3457 O O   . LYS B 1 5   ? -9.444  5.126   10.184  1.00 25.38  ? 34  LYS B O   1 
ATOM   3458 C CB  . LYS B 1 5   ? -8.630  2.026   10.404  1.00 25.63  ? 34  LYS B CB  1 
ATOM   3459 C CG  . LYS B 1 5   ? -8.426  2.396   8.956   1.00 25.46  ? 34  LYS B CG  1 
ATOM   3460 C CD  . LYS B 1 5   ? -8.267  1.151   8.104   1.00 28.71  ? 34  LYS B CD  1 
ATOM   3461 C CE  . LYS B 1 5   ? -7.868  1.410   6.693   1.00 27.24  ? 34  LYS B CE  1 
ATOM   3462 N NZ  . LYS B 1 5   ? -8.106  0.135   6.005   1.00 28.16  ? 34  LYS B NZ  1 
ATOM   3463 N N   . ASP B 1 6   ? -10.687 4.109   11.757  1.00 31.84  ? 35  ASP B N   1 
ATOM   3464 C CA  . ASP B 1 6   ? -11.818 4.999   11.547  1.00 29.75  ? 35  ASP B CA  1 
ATOM   3465 C C   . ASP B 1 6   ? -11.559 6.337   12.234  1.00 24.83  ? 35  ASP B C   1 
ATOM   3466 O O   . ASP B 1 6   ? -11.976 7.372   11.727  1.00 24.84  ? 35  ASP B O   1 
ATOM   3467 C CB  . ASP B 1 6   ? -13.118 4.356   11.998  1.00 33.42  ? 35  ASP B CB  1 
ATOM   3468 C CG  . ASP B 1 6   ? -13.526 3.104   11.229  1.00 38.78  ? 35  ASP B CG  1 
ATOM   3469 O OD1 . ASP B 1 6   ? -13.862 3.232   10.050  1.00 42.26  ? 35  ASP B OD1 1 
ATOM   3470 O OD2 . ASP B 1 6   ? -13.495 2.010   11.812  1.00 44.75  ? 35  ASP B OD2 1 
ATOM   3471 N N   . ILE B 1 7   ? -10.874 6.301   13.385  1.00 23.70  ? 36  ILE B N   1 
ATOM   3472 C CA  . ILE B 1 7   ? -10.503 7.512   14.109  1.00 27.54  ? 36  ILE B CA  1 
ATOM   3473 C C   . ILE B 1 7   ? -9.529  8.325   13.258  1.00 27.53  ? 36  ILE B C   1 
ATOM   3474 O O   . ILE B 1 7   ? -9.697  9.536   13.119  1.00 26.13  ? 36  ILE B O   1 
ATOM   3475 C CB  . ILE B 1 7   ? -9.963  7.161   15.511  1.00 31.94  ? 36  ILE B CB  1 
ATOM   3476 C CG1 . ILE B 1 7   ? -11.060 6.514   16.334  1.00 33.51  ? 36  ILE B CG1 1 
ATOM   3477 C CG2 . ILE B 1 7   ? -9.387  8.364   16.261  1.00 33.97  ? 36  ILE B CG2 1 
ATOM   3478 C CD1 . ILE B 1 7   ? -10.543 5.603   17.429  1.00 35.61  ? 36  ILE B CD1 1 
ATOM   3479 N N   . LEU B 1 8   ? -8.535  7.644   12.662  1.00 26.46  ? 37  LEU B N   1 
ATOM   3480 C CA  . LEU B 1 8   ? -7.643  8.280   11.708  1.00 27.35  ? 37  LEU B CA  1 
ATOM   3481 C C   . LEU B 1 8   ? -8.451  8.891   10.571  1.00 23.74  ? 37  LEU B C   1 
ATOM   3482 O O   . LEU B 1 8   ? -8.293  10.078  10.284  1.00 24.63  ? 37  LEU B O   1 
ATOM   3483 C CB  . LEU B 1 8   ? -6.612  7.256   11.251  1.00 28.71  ? 37  LEU B CB  1 
ATOM   3484 C CG  . LEU B 1 8   ? -5.422  7.773   10.449  1.00 31.77  ? 37  LEU B CG  1 
ATOM   3485 C CD1 . LEU B 1 8   ? -4.788  9.028   10.978  1.00 31.65  ? 37  LEU B CD1 1 
ATOM   3486 C CD2 . LEU B 1 8   ? -4.417  6.636   10.417  1.00 31.59  ? 37  LEU B CD2 1 
ATOM   3487 N N   . ALA B 1 9   ? -9.345  8.110   9.955   1.00 22.98  ? 38  ALA B N   1 
ATOM   3488 C CA  . ALA B 1 9   ? -10.127 8.601   8.832   1.00 26.55  ? 38  ALA B CA  1 
ATOM   3489 C C   . ALA B 1 9   ? -10.841 9.905   9.210   1.00 26.23  ? 38  ALA B C   1 
ATOM   3490 O O   . ALA B 1 9   ? -10.924 10.797  8.390   1.00 28.01  ? 38  ALA B O   1 
ATOM   3491 C CB  . ALA B 1 9   ? -11.082 7.534   8.338   1.00 24.51  ? 38  ALA B CB  1 
ATOM   3492 N N   . ASP B 1 10  ? -11.278 10.065  10.460  1.00 26.32  ? 39  ASP B N   1 
ATOM   3493 C CA  . ASP B 1 10  ? -11.962 11.304  10.855  1.00 30.28  ? 39  ASP B CA  1 
ATOM   3494 C C   . ASP B 1 10  ? -11.006 12.474  11.085  1.00 28.52  ? 39  ASP B C   1 
ATOM   3495 O O   . ASP B 1 10  ? -11.378 13.624  10.886  1.00 30.67  ? 39  ASP B O   1 
ATOM   3496 C CB  . ASP B 1 10  ? -12.911 11.084  12.014  1.00 33.41  ? 39  ASP B CB  1 
ATOM   3497 C CG  . ASP B 1 10  ? -14.114 10.241  11.624  1.00 37.26  ? 39  ASP B CG  1 
ATOM   3498 O OD1 . ASP B 1 10  ? -14.422 10.166  10.412  1.00 38.20  ? 39  ASP B OD1 1 
ATOM   3499 O OD2 . ASP B 1 10  ? -14.709 9.648   12.523  1.00 40.79  ? 39  ASP B OD2 1 
ATOM   3500 N N   . LEU B 1 11  ? -9.748  12.184  11.378  1.00 27.42  ? 40  LEU B N   1 
ATOM   3501 C CA  . LEU B 1 11  ? -8.784  13.223  11.689  1.00 26.28  ? 40  LEU B CA  1 
ATOM   3502 C C   . LEU B 1 11  ? -8.182  13.815  10.411  1.00 28.17  ? 40  LEU B C   1 
ATOM   3503 O O   . LEU B 1 11  ? -7.741  14.950  10.408  1.00 26.61  ? 40  LEU B O   1 
ATOM   3504 C CB  . LEU B 1 11  ? -7.665  12.630  12.530  1.00 30.85  ? 40  LEU B CB  1 
ATOM   3505 C CG  . LEU B 1 11  ? -7.958  12.303  13.991  1.00 35.02  ? 40  LEU B CG  1 
ATOM   3506 C CD1 . LEU B 1 11  ? -6.752  11.526  14.520  1.00 37.72  ? 40  LEU B CD1 1 
ATOM   3507 C CD2 . LEU B 1 11  ? -8.194  13.510  14.845  1.00 39.26  ? 40  LEU B CD2 1 
ATOM   3508 N N   . ILE B 1 12  ? -8.078  13.025  9.346   1.00 26.66  ? 41  ILE B N   1 
ATOM   3509 C CA  . ILE B 1 12  ? -7.238  13.379  8.214   1.00 26.25  ? 41  ILE B CA  1 
ATOM   3510 C C   . ILE B 1 12  ? -7.778  14.625  7.521   1.00 28.75  ? 41  ILE B C   1 
ATOM   3511 O O   . ILE B 1 12  ? -6.992  15.536  7.257   1.00 24.84  ? 41  ILE B O   1 
ATOM   3512 C CB  . ILE B 1 12  ? -7.065  12.177  7.288   1.00 24.18  ? 41  ILE B CB  1 
ATOM   3513 C CG1 . ILE B 1 12  ? -5.943  11.252  7.826   1.00 23.99  ? 41  ILE B CG1 1 
ATOM   3514 C CG2 . ILE B 1 12  ? -6.817  12.588  5.840   1.00 27.77  ? 41  ILE B CG2 1 
ATOM   3515 C CD1 . ILE B 1 12  ? -6.118  9.806   7.410   1.00 24.57  ? 41  ILE B CD1 1 
ATOM   3516 N N   . PRO B 1 13  ? -9.111  14.771  7.328   1.00 26.62  ? 42  PRO B N   1 
ATOM   3517 C CA  . PRO B 1 13  ? -9.652  15.960  6.645   1.00 32.76  ? 42  PRO B CA  1 
ATOM   3518 C C   . PRO B 1 13  ? -9.347  17.269  7.374   1.00 29.98  ? 42  PRO B C   1 
ATOM   3519 O O   . PRO B 1 13  ? -8.985  18.271  6.746   1.00 31.88  ? 42  PRO B O   1 
ATOM   3520 C CB  . PRO B 1 13  ? -11.161 15.628  6.556   1.00 32.43  ? 42  PRO B CB  1 
ATOM   3521 C CG  . PRO B 1 13  ? -11.182 14.089  6.597   1.00 28.96  ? 42  PRO B CG  1 
ATOM   3522 C CD  . PRO B 1 13  ? -10.161 13.789  7.670   1.00 27.99  ? 42  PRO B CD  1 
ATOM   3523 N N   . LYS B 1 14  ? -9.393  17.226  8.704   1.00 31.49  ? 43  LYS B N   1 
ATOM   3524 C CA  . LYS B 1 14  ? -9.106  18.402  9.512   1.00 33.92  ? 43  LYS B CA  1 
ATOM   3525 C C   . LYS B 1 14  ? -7.666  18.873  9.306   1.00 34.81  ? 43  LYS B C   1 
ATOM   3526 O O   . LYS B 1 14  ? -7.408  20.075  9.248   1.00 33.12  ? 43  LYS B O   1 
ATOM   3527 C CB  . LYS B 1 14  ? -9.242  18.117  11.005  1.00 39.77  ? 43  LYS B CB  1 
ATOM   3528 C CG  . LYS B 1 14  ? -10.625 17.697  11.467  1.00 52.21  ? 43  LYS B CG  1 
ATOM   3529 C CD  . LYS B 1 14  ? -10.794 17.855  12.978  1.00 56.83  ? 43  LYS B CD  1 
ATOM   3530 C CE  . LYS B 1 14  ? -12.182 17.606  13.457  1.00 65.31  ? 43  LYS B CE  1 
ATOM   3531 N NZ  . LYS B 1 14  ? -12.628 16.255  13.109  1.00 69.18  ? 43  LYS B NZ  1 
ATOM   3532 N N   . GLU B 1 15  ? -6.732  17.906  9.244   1.00 30.09  ? 44  GLU B N   1 
ATOM   3533 C CA  . GLU B 1 15  ? -5.312  18.184  9.103   1.00 31.75  ? 44  GLU B CA  1 
ATOM   3534 C C   . GLU B 1 15  ? -5.028  18.667  7.680   1.00 28.92  ? 44  GLU B C   1 
ATOM   3535 O O   . GLU B 1 15  ? -4.223  19.569  7.471   1.00 29.24  ? 44  GLU B O   1 
ATOM   3536 C CB  . GLU B 1 15  ? -4.567  16.903  9.487   1.00 34.63  ? 44  GLU B CB  1 
ATOM   3537 C CG  . GLU B 1 15  ? -3.124  17.102  9.943   1.00 44.77  ? 44  GLU B CG  1 
ATOM   3538 C CD  . GLU B 1 15  ? -3.015  18.122  11.063  1.00 49.32  ? 44  GLU B CD  1 
ATOM   3539 O OE1 . GLU B 1 15  ? -3.630  17.959  12.152  1.00 50.96  ? 44  GLU B OE1 1 
ATOM   3540 O OE2 . GLU B 1 15  ? -2.365  19.140  10.761  1.00 46.86  ? 44  GLU B OE2 1 
ATOM   3541 N N   . GLN B 1 16  ? -5.682  18.067  6.685   1.00 24.53  ? 45  GLN B N   1 
ATOM   3542 C CA  . GLN B 1 16  ? -5.475  18.490  5.305   1.00 25.62  ? 45  GLN B CA  1 
ATOM   3543 C C   . GLN B 1 16  ? -5.880  19.953  5.131   1.00 28.24  ? 45  GLN B C   1 
ATOM   3544 O O   . GLN B 1 16  ? -5.220  20.714  4.444   1.00 26.45  ? 45  GLN B O   1 
ATOM   3545 C CB  . GLN B 1 16  ? -6.327  17.639  4.382   1.00 25.99  ? 45  GLN B CB  1 
ATOM   3546 C CG  . GLN B 1 16  ? -5.955  16.167  4.428   1.00 27.56  ? 45  GLN B CG  1 
ATOM   3547 C CD  . GLN B 1 16  ? -6.784  15.330  3.485   1.00 30.74  ? 45  GLN B CD  1 
ATOM   3548 O OE1 . GLN B 1 16  ? -8.009  15.452  3.423   1.00 31.96  ? 45  GLN B OE1 1 
ATOM   3549 N NE2 . GLN B 1 16  ? -6.125  14.464  2.729   1.00 29.29  ? 45  GLN B NE2 1 
ATOM   3550 N N   . ALA B 1 17  ? -6.980  20.345  5.773   1.00 32.20  ? 46  ALA B N   1 
ATOM   3551 C CA  . ALA B 1 17  ? -7.482  21.707  5.643   1.00 33.23  ? 46  ALA B CA  1 
ATOM   3552 C C   . ALA B 1 17  ? -6.524  22.662  6.359   1.00 34.77  ? 46  ALA B C   1 
ATOM   3553 O O   . ALA B 1 17  ? -6.245  23.751  5.861   1.00 34.97  ? 46  ALA B O   1 
ATOM   3554 C CB  . ALA B 1 17  ? -8.905  21.777  6.180   1.00 29.64  ? 46  ALA B CB  1 
ATOM   3555 N N   . ARG B 1 18  ? -5.970  22.231  7.504   1.00 33.40  ? 47  ARG B N   1 
ATOM   3556 C CA  . ARG B 1 18  ? -5.098  23.082  8.296   1.00 37.30  ? 47  ARG B CA  1 
ATOM   3557 C C   . ARG B 1 18  ? -3.810  23.383  7.532   1.00 37.08  ? 47  ARG B C   1 
ATOM   3558 O O   . ARG B 1 18  ? -3.271  24.492  7.620   1.00 33.46  ? 47  ARG B O   1 
ATOM   3559 C CB  . ARG B 1 18  ? -4.831  22.425  9.651   1.00 40.98  ? 47  ARG B CB  1 
ATOM   3560 C CG  . ARG B 1 18  ? -3.793  23.097  10.536  1.00 47.95  ? 47  ARG B CG  1 
ATOM   3561 C CD  . ARG B 1 18  ? -3.665  22.368  11.891  1.00 58.76  ? 47  ARG B CD  1 
ATOM   3562 N NE  . ARG B 1 18  ? -2.329  22.500  12.485  1.00 65.53  ? 47  ARG B NE  1 
ATOM   3563 C CZ  . ARG B 1 18  ? -1.998  22.380  13.773  1.00 73.53  ? 47  ARG B CZ  1 
ATOM   3564 N NH1 . ARG B 1 18  ? -2.903  22.125  14.704  1.00 75.38  ? 47  ARG B NH1 1 
ATOM   3565 N NH2 . ARG B 1 18  ? -0.739  22.539  14.129  1.00 72.02  ? 47  ARG B NH2 1 
ATOM   3566 N N   . ILE B 1 19  ? -3.309  22.384  6.794   1.00 28.60  ? 48  ILE B N   1 
ATOM   3567 C CA  . ILE B 1 19  ? -2.130  22.570  5.967   1.00 29.03  ? 48  ILE B CA  1 
ATOM   3568 C C   . ILE B 1 19  ? -2.468  23.448  4.761   1.00 29.07  ? 48  ILE B C   1 
ATOM   3569 O O   . ILE B 1 19  ? -1.695  24.341  4.395   1.00 33.38  ? 48  ILE B O   1 
ATOM   3570 C CB  . ILE B 1 19  ? -1.569  21.196  5.570   1.00 26.76  ? 48  ILE B CB  1 
ATOM   3571 C CG1 . ILE B 1 19  ? -0.918  20.550  6.754   1.00 27.47  ? 48  ILE B CG1 1 
ATOM   3572 C CG2 . ILE B 1 19  ? -0.617  21.265  4.379   1.00 26.86  ? 48  ILE B CG2 1 
ATOM   3573 C CD1 . ILE B 1 19  ? -0.623  19.061  6.571   1.00 26.59  ? 48  ILE B CD1 1 
ATOM   3574 N N   . LYS B 1 20  ? -3.595  23.161  4.107   1.00 29.48  ? 49  LYS B N   1 
ATOM   3575 C CA  . LYS B 1 20  ? -4.035  23.956  2.974   1.00 36.53  ? 49  LYS B CA  1 
ATOM   3576 C C   . LYS B 1 20  ? -4.169  25.439  3.361   1.00 31.39  ? 49  LYS B C   1 
ATOM   3577 O O   . LYS B 1 20  ? -3.674  26.301  2.644   1.00 29.16  ? 49  LYS B O   1 
ATOM   3578 C CB  . LYS B 1 20  ? -5.329  23.346  2.435   1.00 40.30  ? 49  LYS B CB  1 
ATOM   3579 C CG  . LYS B 1 20  ? -5.821  23.795  1.075   1.00 43.07  ? 49  LYS B CG  1 
ATOM   3580 C CD  . LYS B 1 20  ? -7.234  23.243  0.853   1.00 51.18  ? 49  LYS B CD  1 
ATOM   3581 C CE  . LYS B 1 20  ? -8.092  24.038  -0.092  1.00 59.55  ? 49  LYS B CE  1 
ATOM   3582 N NZ  . LYS B 1 20  ? -7.683  23.835  -1.486  1.00 65.89  ? 49  LYS B NZ  1 
ATOM   3583 N N   . THR B 1 21  ? -4.764  25.734  4.513   1.00 33.11  ? 50  THR B N   1 
ATOM   3584 C CA  . THR B 1 21  ? -4.884  27.107  4.998   1.00 35.51  ? 50  THR B CA  1 
ATOM   3585 C C   . THR B 1 21  ? -3.496  27.707  5.201   1.00 30.36  ? 50  THR B C   1 
ATOM   3586 O O   . THR B 1 21  ? -3.232  28.821  4.802   1.00 31.86  ? 50  THR B O   1 
ATOM   3587 C CB  . THR B 1 21  ? -5.716  27.160  6.285   1.00 35.01  ? 50  THR B CB  1 
ATOM   3588 O OG1 . THR B 1 21  ? -6.997  26.785  5.780   1.00 34.33  ? 50  THR B OG1 1 
ATOM   3589 C CG2 . THR B 1 21  ? -5.729  28.521  6.960   1.00 34.24  ? 50  THR B CG2 1 
ATOM   3590 N N   . PHE B 1 22  ? -2.582  26.963  5.792   1.00 29.71  ? 51  PHE B N   1 
ATOM   3591 C CA  . PHE B 1 22  ? -1.262  27.515  6.065   1.00 29.44  ? 51  PHE B CA  1 
ATOM   3592 C C   . PHE B 1 22  ? -0.425  27.805  4.810   1.00 23.36  ? 51  PHE B C   1 
ATOM   3593 O O   . PHE B 1 22  ? 0.261   28.824  4.744   1.00 25.37  ? 51  PHE B O   1 
ATOM   3594 C CB  . PHE B 1 22  ? -0.585  26.492  6.964   1.00 28.70  ? 51  PHE B CB  1 
ATOM   3595 C CG  . PHE B 1 22  ? 0.811   26.929  7.363   1.00 29.06  ? 51  PHE B CG  1 
ATOM   3596 C CD1 . PHE B 1 22  ? 1.052   28.247  7.744   1.00 27.18  ? 51  PHE B CD1 1 
ATOM   3597 C CD2 . PHE B 1 22  ? 1.866   26.022  7.329   1.00 26.54  ? 51  PHE B CD2 1 
ATOM   3598 C CE1 . PHE B 1 22  ? 2.309   28.644  8.108   1.00 27.77  ? 51  PHE B CE1 1 
ATOM   3599 C CE2 . PHE B 1 22  ? 3.130   26.425  7.675   1.00 24.90  ? 51  PHE B CE2 1 
ATOM   3600 C CZ  . PHE B 1 22  ? 3.354   27.736  8.055   1.00 31.58  ? 51  PHE B CZ  1 
ATOM   3601 N N   . ARG B 1 23  ? -0.428  26.895  3.834   1.00 21.58  ? 52  ARG B N   1 
ATOM   3602 C CA  . ARG B 1 23  ? 0.246   27.074  2.560   1.00 22.50  ? 52  ARG B CA  1 
ATOM   3603 C C   . ARG B 1 23  ? -0.363  28.210  1.730   1.00 29.02  ? 52  ARG B C   1 
ATOM   3604 O O   . ARG B 1 23  ? 0.332   28.914  0.981   1.00 29.67  ? 52  ARG B O   1 
ATOM   3605 C CB  . ARG B 1 23  ? 0.263   25.747  1.793   1.00 22.93  ? 52  ARG B CB  1 
ATOM   3606 C CG  . ARG B 1 23  ? 1.082   24.663  2.505   1.00 25.50  ? 52  ARG B CG  1 
ATOM   3607 C CD  . ARG B 1 23  ? 1.050   23.378  1.726   1.00 25.37  ? 52  ARG B CD  1 
ATOM   3608 N NE  . ARG B 1 23  ? 1.805   23.587  0.485   1.00 30.16  ? 52  ARG B NE  1 
ATOM   3609 C CZ  . ARG B 1 23  ? 2.157   22.610  -0.343  1.00 36.86  ? 52  ARG B CZ  1 
ATOM   3610 N NH1 . ARG B 1 23  ? 1.659   21.408  -0.141  1.00 38.29  ? 52  ARG B NH1 1 
ATOM   3611 N NH2 . ARG B 1 23  ? 3.028   22.828  -1.331  1.00 32.93  ? 52  ARG B NH2 1 
ATOM   3612 N N   . GLN B 1 24  ? -1.678  28.384  1.816   1.00 28.62  ? 53  GLN B N   1 
ATOM   3613 C CA  . GLN B 1 24  ? -2.316  29.511  1.142   1.00 33.88  ? 53  GLN B CA  1 
ATOM   3614 C C   . GLN B 1 24  ? -1.965  30.848  1.810   1.00 31.06  ? 53  GLN B C   1 
ATOM   3615 O O   . GLN B 1 24  ? -1.948  31.877  1.140   1.00 33.51  ? 53  GLN B O   1 
ATOM   3616 C CB  . GLN B 1 24  ? -3.825  29.337  1.092   1.00 36.22  ? 53  GLN B CB  1 
ATOM   3617 C CG  . GLN B 1 24  ? -4.309  28.292  0.094   1.00 40.31  ? 53  GLN B CG  1 
ATOM   3618 C CD  . GLN B 1 24  ? -5.805  28.079  0.208   1.00 44.35  ? 53  GLN B CD  1 
ATOM   3619 O OE1 . GLN B 1 24  ? -6.450  28.438  1.209   1.00 43.61  ? 53  GLN B OE1 1 
ATOM   3620 N NE2 . GLN B 1 24  ? -6.365  27.503  -0.838  1.00 46.38  ? 53  GLN B NE2 1 
ATOM   3621 N N   . GLN B 1 25  ? -1.685  30.843  3.118   1.00 28.38  ? 54  GLN B N   1 
ATOM   3622 C CA  . GLN B 1 25  ? -1.287  32.065  3.794   1.00 31.23  ? 54  GLN B CA  1 
ATOM   3623 C C   . GLN B 1 25  ? 0.191   32.385  3.569   1.00 27.25  ? 54  GLN B C   1 
ATOM   3624 O O   . GLN B 1 25  ? 0.564   33.555  3.608   1.00 23.28  ? 54  GLN B O   1 
ATOM   3625 C CB  . GLN B 1 25  ? -1.400  32.038  5.322   1.00 35.14  ? 54  GLN B CB  1 
ATOM   3626 C CG  . GLN B 1 25  ? -2.803  32.025  5.906   1.00 41.98  ? 54  GLN B CG  1 
ATOM   3627 C CD  . GLN B 1 25  ? -2.813  32.284  7.397   1.00 42.37  ? 54  GLN B CD  1 
ATOM   3628 O OE1 . GLN B 1 25  ? -3.853  32.488  8.027   1.00 53.82  ? 54  GLN B OE1 1 
ATOM   3629 N NE2 . GLN B 1 25  ? -1.644  32.234  7.989   1.00 41.32  ? 54  GLN B NE2 1 
ATOM   3630 N N   . HIS B 1 26  ? 1.041   31.346  3.485   1.00 25.45  ? 55  HIS B N   1 
ATOM   3631 C CA  . HIS B 1 26  ? 2.476   31.498  3.718   1.00 28.17  ? 55  HIS B CA  1 
ATOM   3632 C C   . HIS B 1 26  ? 3.362   30.629  2.817   1.00 27.51  ? 55  HIS B C   1 
ATOM   3633 O O   . HIS B 1 26  ? 4.581   30.599  3.003   1.00 25.76  ? 55  HIS B O   1 
ATOM   3634 C CB  . HIS B 1 26  ? 2.836   31.159  5.171   1.00 29.01  ? 55  HIS B CB  1 
ATOM   3635 C CG  . HIS B 1 26  ? 2.576   32.227  6.181   1.00 31.35  ? 55  HIS B CG  1 
ATOM   3636 N ND1 . HIS B 1 26  ? 3.263   33.423  6.197   1.00 30.02  ? 55  HIS B ND1 1 
ATOM   3637 C CD2 . HIS B 1 26  ? 1.692   32.276  7.185   1.00 31.15  ? 55  HIS B CD2 1 
ATOM   3638 C CE1 . HIS B 1 26  ? 2.836   34.146  7.235   1.00 32.39  ? 55  HIS B CE1 1 
ATOM   3639 N NE2 . HIS B 1 26  ? 1.870   33.478  7.837   1.00 32.23  ? 55  HIS B NE2 1 
ATOM   3640 N N   . GLY B 1 27  ? 2.777   29.950  1.823   1.00 30.71  ? 56  GLY B N   1 
ATOM   3641 C CA  . GLY B 1 27  ? 3.557   29.111  0.917   1.00 32.27  ? 56  GLY B CA  1 
ATOM   3642 C C   . GLY B 1 27  ? 4.860   29.765  0.430   1.00 32.91  ? 56  GLY B C   1 
ATOM   3643 O O   . GLY B 1 27  ? 5.930   29.144  0.395   1.00 26.06  ? 56  GLY B O   1 
ATOM   3644 N N   . LYS B 1 28  ? 4.792   31.041  0.062   1.00 33.88  ? 57  LYS B N   1 
ATOM   3645 C CA  . LYS B 1 28  ? 5.956   31.717  -0.496  1.00 31.34  ? 57  LYS B CA  1 
ATOM   3646 C C   . LYS B 1 28  ? 6.831   32.342  0.594   1.00 30.39  ? 57  LYS B C   1 
ATOM   3647 O O   . LYS B 1 28  ? 7.860   32.911  0.276   1.00 35.20  ? 57  LYS B O   1 
ATOM   3648 C CB  . LYS B 1 28  ? 5.504   32.779  -1.505  1.00 32.78  ? 57  LYS B CB  1 
ATOM   3649 C CG  . LYS B 1 28  ? 4.916   32.213  -2.787  1.00 34.51  ? 57  LYS B CG  1 
ATOM   3650 C CD  . LYS B 1 28  ? 4.346   33.308  -3.690  1.00 38.94  ? 57  LYS B CD  1 
ATOM   3651 C CE  . LYS B 1 28  ? 3.983   32.801  -5.051  1.00 47.99  ? 57  LYS B CE  1 
ATOM   3652 N NZ  . LYS B 1 28  ? 4.001   33.874  -6.060  1.00 57.76  ? 57  LYS B NZ  1 
ATOM   3653 N N   . THR B 1 29  ? 6.465   32.226  1.870   1.00 27.21  ? 58  THR B N   1 
ATOM   3654 C CA  . THR B 1 29  ? 7.254   32.860  2.922   1.00 29.00  ? 58  THR B CA  1 
ATOM   3655 C C   . THR B 1 29  ? 8.614   32.160  3.056   1.00 31.23  ? 58  THR B C   1 
ATOM   3656 O O   . THR B 1 29  ? 8.710   30.929  3.110   1.00 27.57  ? 58  THR B O   1 
ATOM   3657 C CB  . THR B 1 29  ? 6.470   32.813  4.229   1.00 30.67  ? 58  THR B CB  1 
ATOM   3658 O OG1 . THR B 1 29  ? 5.317   33.595  3.958   1.00 30.28  ? 58  THR B OG1 1 
ATOM   3659 C CG2 . THR B 1 29  ? 7.219   33.411  5.404   1.00 31.00  ? 58  THR B CG2 1 
ATOM   3660 N N   . VAL B 1 30  ? 9.672   32.965  3.133   1.00 30.83  ? 59  VAL B N   1 
ATOM   3661 C CA  . VAL B 1 30  ? 11.013  32.429  3.279   1.00 34.62  ? 59  VAL B CA  1 
ATOM   3662 C C   . VAL B 1 30  ? 11.254  32.038  4.745   1.00 31.72  ? 59  VAL B C   1 
ATOM   3663 O O   . VAL B 1 30  ? 11.077  32.859  5.643   1.00 28.59  ? 59  VAL B O   1 
ATOM   3664 C CB  . VAL B 1 30  ? 12.047  33.450  2.752   1.00 34.69  ? 59  VAL B CB  1 
ATOM   3665 C CG1 . VAL B 1 30  ? 13.475  32.944  2.880   1.00 35.05  ? 59  VAL B CG1 1 
ATOM   3666 C CG2 . VAL B 1 30  ? 11.799  33.852  1.301   1.00 32.85  ? 59  VAL B CG2 1 
ATOM   3667 N N   . VAL B 1 31  ? 11.680  30.771  4.977   1.00 31.96  ? 60  VAL B N   1 
ATOM   3668 C CA  . VAL B 1 31  ? 11.960  30.258  6.315   1.00 28.79  ? 60  VAL B CA  1 
ATOM   3669 C C   . VAL B 1 31  ? 13.451  30.083  6.584   1.00 31.25  ? 60  VAL B C   1 
ATOM   3670 O O   . VAL B 1 31  ? 13.820  29.899  7.742   1.00 32.31  ? 60  VAL B O   1 
ATOM   3671 C CB  . VAL B 1 31  ? 11.261  28.939  6.652   1.00 34.45  ? 60  VAL B CB  1 
ATOM   3672 C CG1 . VAL B 1 31  ? 9.838   29.187  7.113   1.00 36.37  ? 60  VAL B CG1 1 
ATOM   3673 C CG2 . VAL B 1 31  ? 11.314  27.968  5.500   1.00 34.44  ? 60  VAL B CG2 1 
ATOM   3674 N N   . GLY B 1 32  ? 14.283  30.160  5.546   1.00 27.16  ? 61  GLY B N   1 
ATOM   3675 C CA  . GLY B 1 32  ? 15.709  29.935  5.682   1.00 31.04  ? 61  GLY B CA  1 
ATOM   3676 C C   . GLY B 1 32  ? 16.460  30.243  4.387   1.00 31.51  ? 61  GLY B C   1 
ATOM   3677 O O   . GLY B 1 32  ? 15.878  30.293  3.296   1.00 26.43  ? 61  GLY B O   1 
ATOM   3678 N N   . GLN B 1 33  ? 17.771  30.454  4.541   1.00 32.01  ? 62  GLN B N   1 
ATOM   3679 C CA  . GLN B 1 33  ? 18.690  30.639  3.430   1.00 36.67  ? 62  GLN B CA  1 
ATOM   3680 C C   . GLN B 1 33  ? 19.445  29.333  3.241   1.00 33.64  ? 62  GLN B C   1 
ATOM   3681 O O   . GLN B 1 33  ? 19.587  28.594  4.216   1.00 30.42  ? 62  GLN B O   1 
ATOM   3682 C CB  . GLN B 1 33  ? 19.736  31.710  3.736   1.00 42.75  ? 62  GLN B CB  1 
ATOM   3683 C CG  . GLN B 1 33  ? 19.183  32.959  4.415   1.00 47.57  ? 62  GLN B CG  1 
ATOM   3684 C CD  . GLN B 1 33  ? 18.068  33.609  3.630   1.00 49.48  ? 62  GLN B CD  1 
ATOM   3685 O OE1 . GLN B 1 33  ? 16.965  33.840  4.142   1.00 50.48  ? 62  GLN B OE1 1 
ATOM   3686 N NE2 . GLN B 1 33  ? 18.355  33.894  2.370   1.00 51.60  ? 62  GLN B NE2 1 
ATOM   3687 N N   . ILE B 1 34  ? 19.916  29.073  2.008   1.00 30.83  ? 63  ILE B N   1 
ATOM   3688 C CA  . ILE B 1 34  ? 20.835  27.966  1.778   1.00 31.15  ? 63  ILE B CA  1 
ATOM   3689 C C   . ILE B 1 34  ? 22.199  28.528  1.420   1.00 27.61  ? 63  ILE B C   1 
ATOM   3690 O O   . ILE B 1 34  ? 22.301  29.347  0.498   1.00 33.68  ? 63  ILE B O   1 
ATOM   3691 C CB  . ILE B 1 34  ? 20.370  26.996  0.677   1.00 32.65  ? 63  ILE B CB  1 
ATOM   3692 C CG1 . ILE B 1 34  ? 18.946  26.529  0.915   1.00 32.26  ? 63  ILE B CG1 1 
ATOM   3693 C CG2 . ILE B 1 34  ? 21.346  25.809  0.592   1.00 31.90  ? 63  ILE B CG2 1 
ATOM   3694 C CD1 . ILE B 1 34  ? 18.325  25.832  -0.282  1.00 34.89  ? 63  ILE B CD1 1 
ATOM   3695 N N   . THR B 1 35  ? 23.227  28.121  2.169   1.00 28.03  ? 64  THR B N   1 
ATOM   3696 C CA  . THR B 1 35  ? 24.592  28.529  1.855   1.00 29.55  ? 64  THR B CA  1 
ATOM   3697 C C   . THR B 1 35  ? 25.366  27.402  1.191   1.00 32.32  ? 64  THR B C   1 
ATOM   3698 O O   . THR B 1 35  ? 24.953  26.249  1.209   1.00 28.49  ? 64  THR B O   1 
ATOM   3699 C CB  . THR B 1 35  ? 25.344  29.000  3.088   1.00 34.04  ? 64  THR B CB  1 
ATOM   3700 O OG1 . THR B 1 35  ? 25.342  27.892  3.978   1.00 32.81  ? 64  THR B OG1 1 
ATOM   3701 C CG2 . THR B 1 35  ? 24.682  30.220  3.713   1.00 35.03  ? 64  THR B CG2 1 
ATOM   3702 N N   . VAL B 1 36  ? 26.503  27.775  0.595   1.00 30.48  ? 65  VAL B N   1 
ATOM   3703 C CA  . VAL B 1 36  ? 27.431  26.816  0.022   1.00 28.85  ? 65  VAL B CA  1 
ATOM   3704 C C   . VAL B 1 36  ? 27.803  25.801  1.096   1.00 30.23  ? 65  VAL B C   1 
ATOM   3705 O O   . VAL B 1 36  ? 27.876  24.608  0.806   1.00 35.60  ? 65  VAL B O   1 
ATOM   3706 C CB  . VAL B 1 36  ? 28.653  27.544  -0.569  1.00 27.71  ? 65  VAL B CB  1 
ATOM   3707 C CG1 . VAL B 1 36  ? 29.794  26.589  -0.930  1.00 28.19  ? 65  VAL B CG1 1 
ATOM   3708 C CG2 . VAL B 1 36  ? 28.252  28.368  -1.782  1.00 26.83  ? 65  VAL B CG2 1 
ATOM   3709 N N   . ASP B 1 37  ? 28.009  26.278  2.328   1.00 27.72  ? 66  ASP B N   1 
ATOM   3710 C CA  . ASP B 1 37  ? 28.466  25.438  3.418   1.00 29.41  ? 66  ASP B CA  1 
ATOM   3711 C C   . ASP B 1 37  ? 27.417  24.410  3.829   1.00 28.73  ? 66  ASP B C   1 
ATOM   3712 O O   . ASP B 1 37  ? 27.804  23.356  4.308   1.00 24.28  ? 66  ASP B O   1 
ATOM   3713 C CB  . ASP B 1 37  ? 28.866  26.217  4.664   1.00 31.95  ? 66  ASP B CB  1 
ATOM   3714 C CG  . ASP B 1 37  ? 30.323  26.687  4.724   1.00 40.93  ? 66  ASP B CG  1 
ATOM   3715 O OD1 . ASP B 1 37  ? 31.188  26.054  4.079   1.00 40.64  ? 66  ASP B OD1 1 
ATOM   3716 O OD2 . ASP B 1 37  ? 30.595  27.690  5.417   1.00 42.31  ? 66  ASP B OD2 1 
ATOM   3717 N N   . MET B 1 38  ? 26.117  24.731  3.698   1.00 27.51  ? 67  MET B N   1 
ATOM   3718 C CA  . MET B 1 38  ? 25.078  23.811  4.126   1.00 27.48  ? 67  MET B CA  1 
ATOM   3719 C C   . MET B 1 38  ? 24.999  22.643  3.142   1.00 28.83  ? 67  MET B C   1 
ATOM   3720 O O   . MET B 1 38  ? 24.669  21.524  3.556   1.00 25.27  ? 67  MET B O   1 
ATOM   3721 C CB  . MET B 1 38  ? 23.697  24.475  4.201   1.00 28.16  ? 67  MET B CB  1 
ATOM   3722 C CG  . MET B 1 38  ? 23.625  25.636  5.161   1.00 35.29  ? 67  MET B CG  1 
ATOM   3723 S SD  . MET B 1 38  ? 22.037  26.496  5.102   1.00 40.00  ? 67  MET B SD  1 
ATOM   3724 C CE  . MET B 1 38  ? 22.394  27.795  6.292   1.00 47.04  ? 67  MET B CE  1 
ATOM   3725 N N   . MET B 1 39  ? 25.246  22.940  1.841   1.00 29.05  ? 68  MET B N   1 
ATOM   3726 C CA  . MET B 1 39  ? 25.264  21.936  0.790   1.00 27.51  ? 68  MET B CA  1 
ATOM   3727 C C   . MET B 1 39  ? 26.430  20.946  0.985   1.00 27.29  ? 68  MET B C   1 
ATOM   3728 O O   . MET B 1 39  ? 26.267  19.715  0.803   1.00 26.71  ? 68  MET B O   1 
ATOM   3729 C CB  . MET B 1 39  ? 25.386  22.620  -0.573  1.00 27.99  ? 68  MET B CB  1 
ATOM   3730 C CG  . MET B 1 39  ? 24.167  23.442  -0.966  1.00 29.99  ? 68  MET B CG  1 
ATOM   3731 S SD  . MET B 1 39  ? 24.366  24.172  -2.597  1.00 31.92  ? 68  MET B SD  1 
ATOM   3732 C CE  . MET B 1 39  ? 24.507  22.706  -3.631  1.00 29.23  ? 68  MET B CE  1 
ATOM   3733 N N   . TYR B 1 40  ? 27.616  21.498  1.291   1.00 23.31  ? 69  TYR B N   1 
ATOM   3734 C CA  . TYR B 1 40  ? 28.794  20.699  1.599   1.00 24.84  ? 69  TYR B CA  1 
ATOM   3735 C C   . TYR B 1 40  ? 28.622  19.999  2.953   1.00 23.99  ? 69  TYR B C   1 
ATOM   3736 O O   . TYR B 1 40  ? 29.257  18.983  3.183   1.00 27.94  ? 69  TYR B O   1 
ATOM   3737 C CB  . TYR B 1 40  ? 30.104  21.497  1.597   1.00 25.13  ? 69  TYR B CB  1 
ATOM   3738 C CG  . TYR B 1 40  ? 30.643  21.737  0.190   1.00 23.06  ? 69  TYR B CG  1 
ATOM   3739 C CD1 . TYR B 1 40  ? 31.232  20.720  -0.543  1.00 24.51  ? 69  TYR B CD1 1 
ATOM   3740 C CD2 . TYR B 1 40  ? 30.538  22.974  -0.396  1.00 22.17  ? 69  TYR B CD2 1 
ATOM   3741 C CE1 . TYR B 1 40  ? 31.692  20.914  -1.831  1.00 23.78  ? 69  TYR B CE1 1 
ATOM   3742 C CE2 . TYR B 1 40  ? 30.991  23.196  -1.683  1.00 23.17  ? 69  TYR B CE2 1 
ATOM   3743 C CZ  . TYR B 1 40  ? 31.572  22.167  -2.404  1.00 25.31  ? 69  TYR B CZ  1 
ATOM   3744 O OH  . TYR B 1 40  ? 32.031  22.418  -3.666  1.00 25.76  ? 69  TYR B OH  1 
ATOM   3745 N N   . GLY B 1 41  ? 27.788  20.546  3.839   1.00 25.91  ? 70  GLY B N   1 
ATOM   3746 C CA  . GLY B 1 41  ? 27.750  20.152  5.247   1.00 24.42  ? 70  GLY B CA  1 
ATOM   3747 C C   . GLY B 1 41  ? 26.518  19.293  5.563   1.00 25.96  ? 70  GLY B C   1 
ATOM   3748 O O   . GLY B 1 41  ? 26.052  19.250  6.696   1.00 23.13  ? 70  GLY B O   1 
ATOM   3749 N N   . GLY B 1 42  ? 25.993  18.574  4.558   1.00 24.88  ? 71  GLY B N   1 
ATOM   3750 C CA  . GLY B 1 42  ? 24.941  17.600  4.833   1.00 23.15  ? 71  GLY B CA  1 
ATOM   3751 C C   . GLY B 1 42  ? 23.646  18.279  5.265   1.00 20.43  ? 71  GLY B C   1 
ATOM   3752 O O   . GLY B 1 42  ? 22.896  17.708  6.047   1.00 21.80  ? 71  GLY B O   1 
ATOM   3753 N N   . MET B 1 43  ? 23.397  19.492  4.744   1.00 21.36  ? 72  MET B N   1 
ATOM   3754 C CA  . MET B 1 43  ? 22.177  20.243  4.971   1.00 21.03  ? 72  MET B CA  1 
ATOM   3755 C C   . MET B 1 43  ? 22.024  20.681  6.431   1.00 25.62  ? 72  MET B C   1 
ATOM   3756 O O   . MET B 1 43  ? 20.909  20.971  6.873   1.00 24.55  ? 72  MET B O   1 
ATOM   3757 C CB  . MET B 1 43  ? 20.945  19.398  4.616   1.00 24.06  ? 72  MET B CB  1 
ATOM   3758 C CG  . MET B 1 43  ? 20.914  18.815  3.216   1.00 24.50  ? 72  MET B CG  1 
ATOM   3759 S SD  . MET B 1 43  ? 19.342  17.941  2.955   1.00 29.24  ? 72  MET B SD  1 
ATOM   3760 C CE  . MET B 1 43  ? 19.241  17.514  1.207   1.00 25.83  ? 72  MET B CE  1 
ATOM   3761 N N   . ARG B 1 44  ? 23.128  20.780  7.169   1.00 28.60  ? 73  ARG B N   1 
ATOM   3762 C CA  . ARG B 1 44  ? 23.075  21.122  8.580   1.00 37.71  ? 73  ARG B CA  1 
ATOM   3763 C C   . ARG B 1 44  ? 22.378  22.472  8.746   1.00 30.90  ? 73  ARG B C   1 
ATOM   3764 O O   . ARG B 1 44  ? 22.738  23.424  8.085   1.00 30.00  ? 73  ARG B O   1 
ATOM   3765 C CB  . ARG B 1 44  ? 24.485  21.170  9.185   1.00 50.25  ? 73  ARG B CB  1 
ATOM   3766 C CG  . ARG B 1 44  ? 24.549  21.175  10.712  1.00 66.35  ? 73  ARG B CG  1 
ATOM   3767 C CD  . ARG B 1 44  ? 25.941  21.575  11.259  1.00 79.30  ? 73  ARG B CD  1 
ATOM   3768 N NE  . ARG B 1 44  ? 27.001  20.792  10.610  1.00 91.22  ? 73  ARG B NE  1 
ATOM   3769 C CZ  . ARG B 1 44  ? 27.750  21.153  9.558   1.00 101.99 ? 73  ARG B CZ  1 
ATOM   3770 N NH1 . ARG B 1 44  ? 27.753  22.402  9.110   1.00 107.46 ? 73  ARG B NH1 1 
ATOM   3771 N NH2 . ARG B 1 44  ? 28.515  20.250  8.959   1.00 97.48  ? 73  ARG B NH2 1 
ATOM   3772 N N   . GLY B 1 45  ? 21.368  22.509  9.625   1.00 33.57  ? 74  GLY B N   1 
ATOM   3773 C CA  . GLY B 1 45  ? 20.658  23.725  9.969   1.00 36.01  ? 74  GLY B CA  1 
ATOM   3774 C C   . GLY B 1 45  ? 19.587  24.116  8.956   1.00 38.71  ? 74  GLY B C   1 
ATOM   3775 O O   . GLY B 1 45  ? 18.866  25.096  9.178   1.00 42.50  ? 74  GLY B O   1 
ATOM   3776 N N   . MET B 1 46  ? 19.480  23.364  7.857   1.00 31.96  ? 75  MET B N   1 
ATOM   3777 C CA  . MET B 1 46  ? 18.582  23.709  6.779   1.00 28.48  ? 75  MET B CA  1 
ATOM   3778 C C   . MET B 1 46  ? 17.249  23.034  7.083   1.00 26.27  ? 75  MET B C   1 
ATOM   3779 O O   . MET B 1 46  ? 17.203  21.848  7.413   1.00 24.50  ? 75  MET B O   1 
ATOM   3780 C CB  . MET B 1 46  ? 19.246  23.291  5.459   1.00 34.83  ? 75  MET B CB  1 
ATOM   3781 C CG  . MET B 1 46  ? 18.432  23.370  4.178   1.00 40.80  ? 75  MET B CG  1 
ATOM   3782 S SD  . MET B 1 46  ? 19.213  22.629  2.719   1.00 41.74  ? 75  MET B SD  1 
ATOM   3783 C CE  . MET B 1 46  ? 20.740  23.369  3.278   1.00 32.38  ? 75  MET B CE  1 
ATOM   3784 N N   . LYS B 1 47  ? 16.180  23.833  7.023   1.00 27.64  ? 76  LYS B N   1 
ATOM   3785 C CA  . LYS B 1 47  ? 14.827  23.390  7.334   1.00 29.06  ? 76  LYS B CA  1 
ATOM   3786 C C   . LYS B 1 47  ? 14.254  22.803  6.058   1.00 28.13  ? 76  LYS B C   1 
ATOM   3787 O O   . LYS B 1 47  ? 13.945  23.534  5.120   1.00 37.09  ? 76  LYS B O   1 
ATOM   3788 C CB  . LYS B 1 47  ? 13.939  24.534  7.835   1.00 29.76  ? 76  LYS B CB  1 
ATOM   3789 C CG  . LYS B 1 47  ? 14.265  24.944  9.259   1.00 30.23  ? 76  LYS B CG  1 
ATOM   3790 C CD  . LYS B 1 47  ? 13.383  26.075  9.782   1.00 33.11  ? 76  LYS B CD  1 
ATOM   3791 C CE  . LYS B 1 47  ? 13.467  26.250  11.292  1.00 32.07  ? 76  LYS B CE  1 
ATOM   3792 N NZ  . LYS B 1 47  ? 14.768  26.827  11.664  1.00 34.18  ? 76  LYS B NZ  1 
ATOM   3793 N N   . GLY B 1 48  ? 14.216  21.475  5.991   1.00 26.92  ? 77  GLY B N   1 
ATOM   3794 C CA  . GLY B 1 48  ? 14.100  20.833  4.704   1.00 27.49  ? 77  GLY B CA  1 
ATOM   3795 C C   . GLY B 1 48  ? 12.856  19.974  4.523   1.00 25.34  ? 77  GLY B C   1 
ATOM   3796 O O   . GLY B 1 48  ? 12.560  19.591  3.385   1.00 24.20  ? 77  GLY B O   1 
ATOM   3797 N N   . LEU B 1 49  ? 12.210  19.547  5.611   1.00 22.44  ? 78  LEU B N   1 
ATOM   3798 C CA  . LEU B 1 49  ? 11.063  18.677  5.420   1.00 25.39  ? 78  LEU B CA  1 
ATOM   3799 C C   . LEU B 1 49  ? 10.079  18.834  6.567   1.00 21.82  ? 78  LEU B C   1 
ATOM   3800 O O   . LEU B 1 49  ? 10.444  19.262  7.658   1.00 20.77  ? 78  LEU B O   1 
ATOM   3801 C CB  . LEU B 1 49  ? 11.463  17.217  5.243   1.00 31.33  ? 78  LEU B CB  1 
ATOM   3802 C CG  . LEU B 1 49  ? 12.064  16.548  6.479   1.00 32.57  ? 78  LEU B CG  1 
ATOM   3803 C CD1 . LEU B 1 49  ? 11.976  15.050  6.275   1.00 33.20  ? 78  LEU B CD1 1 
ATOM   3804 C CD2 . LEU B 1 49  ? 13.475  17.036  6.661   1.00 34.24  ? 78  LEU B CD2 1 
ATOM   3805 N N   . VAL B 1 50  ? 8.822   18.527  6.268   1.00 23.53  ? 79  VAL B N   1 
ATOM   3806 C CA  . VAL B 1 50  ? 7.781   18.500  7.288   1.00 25.41  ? 79  VAL B CA  1 
ATOM   3807 C C   . VAL B 1 50  ? 7.579   17.072  7.792   1.00 23.86  ? 79  VAL B C   1 
ATOM   3808 O O   . VAL B 1 50  ? 7.459   16.165  6.981   1.00 20.85  ? 79  VAL B O   1 
ATOM   3809 C CB  . VAL B 1 50  ? 6.469   19.056  6.735   1.00 27.66  ? 79  VAL B CB  1 
ATOM   3810 C CG1 . VAL B 1 50  ? 5.368   18.952  7.795   1.00 27.62  ? 79  VAL B CG1 1 
ATOM   3811 C CG2 . VAL B 1 50  ? 6.691   20.487  6.216   1.00 29.41  ? 79  VAL B CG2 1 
ATOM   3812 N N   . TYR B 1 51  ? 7.464   16.968  9.121   1.00 21.06  ? 80  TYR B N   1 
ATOM   3813 C CA  . TYR B 1 51  ? 7.484   15.734  9.865   1.00 24.48  ? 80  TYR B CA  1 
ATOM   3814 C C   . TYR B 1 51  ? 6.694   15.950  11.157  1.00 21.02  ? 80  TYR B C   1 
ATOM   3815 O O   . TYR B 1 51  ? 7.091   16.695  12.046  1.00 25.64  ? 80  TYR B O   1 
ATOM   3816 C CB  . TYR B 1 51  ? 8.930   15.313  10.091  1.00 24.73  ? 80  TYR B CB  1 
ATOM   3817 C CG  . TYR B 1 51  ? 9.098   13.865  10.515  1.00 23.89  ? 80  TYR B CG  1 
ATOM   3818 C CD1 . TYR B 1 51  ? 9.048   13.504  11.849  1.00 27.00  ? 80  TYR B CD1 1 
ATOM   3819 C CD2 . TYR B 1 51  ? 9.367   12.881  9.592   1.00 24.58  ? 80  TYR B CD2 1 
ATOM   3820 C CE1 . TYR B 1 51  ? 9.240   12.195  12.250  1.00 26.58  ? 80  TYR B CE1 1 
ATOM   3821 C CE2 . TYR B 1 51  ? 9.519   11.554  9.975   1.00 23.50  ? 80  TYR B CE2 1 
ATOM   3822 C CZ  . TYR B 1 51  ? 9.456   11.211  11.304  1.00 23.34  ? 80  TYR B CZ  1 
ATOM   3823 O OH  . TYR B 1 51  ? 9.624   9.923   11.708  1.00 23.78  ? 80  TYR B OH  1 
ATOM   3824 N N   . GLU B 1 52  ? 5.531   15.308  11.229  1.00 24.05  ? 81  GLU B N   1 
ATOM   3825 C CA  . GLU B 1 52  ? 4.494   15.744  12.158  1.00 26.40  ? 81  GLU B CA  1 
ATOM   3826 C C   . GLU B 1 52  ? 4.585   15.070  13.529  1.00 25.73  ? 81  GLU B C   1 
ATOM   3827 O O   . GLU B 1 52  ? 4.034   15.588  14.483  1.00 23.85  ? 81  GLU B O   1 
ATOM   3828 C CB  . GLU B 1 52  ? 3.107   15.464  11.571  1.00 26.68  ? 81  GLU B CB  1 
ATOM   3829 C CG  . GLU B 1 52  ? 2.859   16.122  10.218  1.00 28.72  ? 81  GLU B CG  1 
ATOM   3830 C CD  . GLU B 1 52  ? 2.609   17.619  10.263  1.00 31.03  ? 81  GLU B CD  1 
ATOM   3831 O OE1 . GLU B 1 52  ? 2.927   18.313  11.227  1.00 28.98  ? 81  GLU B OE1 1 
ATOM   3832 O OE2 . GLU B 1 52  ? 2.120   18.098  9.236   1.00 33.75  ? 81  GLU B OE2 1 
ATOM   3833 N N   . THR B 1 53  ? 5.270   13.928  13.639  1.00 23.77  ? 82  THR B N   1 
ATOM   3834 C CA  . THR B 1 53  ? 5.030   13.065  14.781  1.00 20.82  ? 82  THR B CA  1 
ATOM   3835 C C   . THR B 1 53  ? 5.801   13.547  16.010  1.00 21.60  ? 82  THR B C   1 
ATOM   3836 O O   . THR B 1 53  ? 5.315   13.409  17.120  1.00 22.69  ? 82  THR B O   1 
ATOM   3837 C CB  . THR B 1 53  ? 5.298   11.614  14.398  1.00 22.40  ? 82  THR B CB  1 
ATOM   3838 O OG1 . THR B 1 53  ? 6.541   11.644  13.717  1.00 24.28  ? 82  THR B OG1 1 
ATOM   3839 C CG2 . THR B 1 53  ? 4.240   11.025  13.470  1.00 21.64  ? 82  THR B CG2 1 
ATOM   3840 N N   . SER B 1 54  ? 6.989   14.121  15.826  1.00 22.71  ? 83  SER B N   1 
ATOM   3841 C CA  . SER B 1 54  ? 7.838   14.509  16.931  1.00 22.88  ? 83  SER B CA  1 
ATOM   3842 C C   . SER B 1 54  ? 8.677   15.716  16.556  1.00 26.07  ? 83  SER B C   1 
ATOM   3843 O O   . SER B 1 54  ? 8.894   15.993  15.373  1.00 25.56  ? 83  SER B O   1 
ATOM   3844 C CB  . SER B 1 54  ? 8.675   13.353  17.412  1.00 23.80  ? 83  SER B CB  1 
ATOM   3845 O OG  . SER B 1 54  ? 9.640   12.972  16.459  1.00 20.79  ? 83  SER B OG  1 
ATOM   3846 N N   . VAL B 1 55  ? 9.066   16.438  17.607  1.00 26.51  ? 84  VAL B N   1 
ATOM   3847 C CA  . VAL B 1 55  ? 9.751   17.713  17.536  1.00 28.77  ? 84  VAL B CA  1 
ATOM   3848 C C   . VAL B 1 55  ? 10.701  17.809  18.720  1.00 30.25  ? 84  VAL B C   1 
ATOM   3849 O O   . VAL B 1 55  ? 10.307  17.553  19.861  1.00 37.03  ? 84  VAL B O   1 
ATOM   3850 C CB  . VAL B 1 55  ? 8.727   18.868  17.541  1.00 27.56  ? 84  VAL B CB  1 
ATOM   3851 C CG1 . VAL B 1 55  ? 9.409   20.219  17.733  1.00 29.94  ? 84  VAL B CG1 1 
ATOM   3852 C CG2 . VAL B 1 55  ? 7.875   18.882  16.282  1.00 31.49  ? 84  VAL B CG2 1 
ATOM   3853 N N   . LEU B 1 56  ? 11.936  18.262  18.468  1.00 38.09  ? 85  LEU B N   1 
ATOM   3854 C CA  . LEU B 1 56  ? 12.917  18.495  19.523  1.00 39.31  ? 85  LEU B CA  1 
ATOM   3855 C C   . LEU B 1 56  ? 12.665  19.822  20.258  1.00 41.31  ? 85  LEU B C   1 
ATOM   3856 O O   . LEU B 1 56  ? 12.927  20.908  19.739  1.00 37.90  ? 85  LEU B O   1 
ATOM   3857 C CB  . LEU B 1 56  ? 14.343  18.464  18.978  1.00 43.33  ? 85  LEU B CB  1 
ATOM   3858 C CG  . LEU B 1 56  ? 15.436  18.591  20.046  1.00 48.86  ? 85  LEU B CG  1 
ATOM   3859 C CD1 . LEU B 1 56  ? 15.513  17.306  20.853  1.00 49.55  ? 85  LEU B CD1 1 
ATOM   3860 C CD2 . LEU B 1 56  ? 16.793  18.949  19.470  1.00 50.58  ? 85  LEU B CD2 1 
ATOM   3861 N N   . ASP B 1 57  ? 12.227  19.721  21.513  1.00 43.65  ? 86  ASP B N   1 
ATOM   3862 C CA  . ASP B 1 57  ? 12.086  20.880  22.375  1.00 48.02  ? 86  ASP B CA  1 
ATOM   3863 C C   . ASP B 1 57  ? 13.450  21.171  22.991  1.00 50.22  ? 86  ASP B C   1 
ATOM   3864 O O   . ASP B 1 57  ? 14.011  20.348  23.718  1.00 48.47  ? 86  ASP B O   1 
ATOM   3865 C CB  . ASP B 1 57  ? 10.990  20.657  23.404  1.00 48.06  ? 86  ASP B CB  1 
ATOM   3866 C CG  . ASP B 1 57  ? 10.712  21.826  24.338  1.00 48.44  ? 86  ASP B CG  1 
ATOM   3867 O OD1 . ASP B 1 57  ? 11.694  22.425  24.807  1.00 46.79  ? 86  ASP B OD1 1 
ATOM   3868 O OD2 . ASP B 1 57  ? 9.514   22.091  24.609  1.00 49.82  ? 86  ASP B OD2 1 
ATOM   3869 N N   . PRO B 1 58  ? 14.032  22.361  22.742  1.00 57.58  ? 87  PRO B N   1 
ATOM   3870 C CA  . PRO B 1 58  ? 15.433  22.592  23.113  1.00 57.75  ? 87  PRO B CA  1 
ATOM   3871 C C   . PRO B 1 58  ? 15.717  22.687  24.615  1.00 60.30  ? 87  PRO B C   1 
ATOM   3872 O O   . PRO B 1 58  ? 16.881  22.697  25.023  1.00 48.75  ? 87  PRO B O   1 
ATOM   3873 C CB  . PRO B 1 58  ? 15.750  23.889  22.340  1.00 56.63  ? 87  PRO B CB  1 
ATOM   3874 C CG  . PRO B 1 58  ? 14.412  24.608  22.279  1.00 59.89  ? 87  PRO B CG  1 
ATOM   3875 C CD  . PRO B 1 58  ? 13.382  23.511  22.093  1.00 52.95  ? 87  PRO B CD  1 
ATOM   3876 N N   . ASP B 1 59  ? 14.653  22.721  25.431  1.00 62.00  ? 88  ASP B N   1 
ATOM   3877 C CA  . ASP B 1 59  ? 14.799  22.848  26.875  1.00 72.12  ? 88  ASP B CA  1 
ATOM   3878 C C   . ASP B 1 59  ? 14.057  21.740  27.635  1.00 73.25  ? 88  ASP B C   1 
ATOM   3879 O O   . ASP B 1 59  ? 14.132  21.722  28.861  1.00 81.96  ? 88  ASP B O   1 
ATOM   3880 C CB  . ASP B 1 59  ? 14.440  24.261  27.326  1.00 85.64  ? 88  ASP B CB  1 
ATOM   3881 C CG  . ASP B 1 59  ? 13.141  24.839  26.777  1.00 93.17  ? 88  ASP B CG  1 
ATOM   3882 O OD1 . ASP B 1 59  ? 13.004  24.929  25.534  1.00 101.82 ? 88  ASP B OD1 1 
ATOM   3883 O OD2 . ASP B 1 59  ? 12.274  25.204  27.597  1.00 101.50 ? 88  ASP B OD2 1 
ATOM   3884 N N   . GLU B 1 60  ? 13.363  20.818  26.937  1.00 65.92  ? 89  GLU B N   1 
ATOM   3885 C CA  . GLU B 1 60  ? 12.635  19.726  27.582  1.00 61.84  ? 89  GLU B CA  1 
ATOM   3886 C C   . GLU B 1 60  ? 12.826  18.378  26.873  1.00 58.75  ? 89  GLU B C   1 
ATOM   3887 O O   . GLU B 1 60  ? 12.338  17.361  27.383  1.00 59.20  ? 89  GLU B O   1 
ATOM   3888 C CB  . GLU B 1 60  ? 11.128  20.000  27.666  1.00 68.38  ? 89  GLU B CB  1 
ATOM   3889 C CG  . GLU B 1 60  ? 10.625  20.410  29.051  1.00 77.16  ? 89  GLU B CG  1 
ATOM   3890 C CD  . GLU B 1 60  ? 10.319  21.886  29.274  1.00 85.43  ? 89  GLU B CD  1 
ATOM   3891 O OE1 . GLU B 1 60  ? 10.984  22.512  30.131  1.00 79.75  ? 89  GLU B OE1 1 
ATOM   3892 O OE2 . GLU B 1 60  ? 9.389   22.413  28.616  1.00 86.13  ? 89  GLU B OE2 1 
ATOM   3893 N N   . GLY B 1 61  ? 13.474  18.379  25.687  1.00 52.57  ? 90  GLY B N   1 
ATOM   3894 C CA  . GLY B 1 61  ? 13.798  17.176  24.920  1.00 45.62  ? 90  GLY B CA  1 
ATOM   3895 C C   . GLY B 1 61  ? 12.830  16.899  23.760  1.00 41.98  ? 90  GLY B C   1 
ATOM   3896 O O   . GLY B 1 61  ? 12.080  17.765  23.316  1.00 38.22  ? 90  GLY B O   1 
ATOM   3897 N N   . ILE B 1 62  ? 12.878  15.672  23.236  1.00 35.88  ? 91  ILE B N   1 
ATOM   3898 C CA  . ILE B 1 62  ? 11.922  15.238  22.237  1.00 31.60  ? 91  ILE B CA  1 
ATOM   3899 C C   . ILE B 1 62  ? 10.518  15.336  22.835  1.00 32.24  ? 91  ILE B C   1 
ATOM   3900 O O   . ILE B 1 62  ? 10.285  14.835  23.923  1.00 33.90  ? 91  ILE B O   1 
ATOM   3901 C CB  . ILE B 1 62  ? 12.208  13.793  21.806  1.00 31.98  ? 91  ILE B CB  1 
ATOM   3902 C CG1 . ILE B 1 62  ? 11.403  13.437  20.542  1.00 31.07  ? 91  ILE B CG1 1 
ATOM   3903 C CG2 . ILE B 1 62  ? 11.951  12.796  22.948  1.00 32.29  ? 91  ILE B CG2 1 
ATOM   3904 C CD1 . ILE B 1 62  ? 11.801  14.269  19.338  1.00 29.60  ? 91  ILE B CD1 1 
ATOM   3905 N N   . ARG B 1 63  ? 9.584   15.919  22.086  1.00 33.65  ? 92  ARG B N   1 
ATOM   3906 C CA  . ARG B 1 63  ? 8.162   15.783  22.353  1.00 32.10  ? 92  ARG B CA  1 
ATOM   3907 C C   . ARG B 1 63  ? 7.508   14.917  21.280  1.00 28.29  ? 92  ARG B C   1 
ATOM   3908 O O   . ARG B 1 63  ? 7.744   15.084  20.080  1.00 23.83  ? 92  ARG B O   1 
ATOM   3909 C CB  . ARG B 1 63  ? 7.510   17.174  22.352  1.00 37.68  ? 92  ARG B CB  1 
ATOM   3910 C CG  . ARG B 1 63  ? 8.072   18.095  23.425  1.00 46.57  ? 92  ARG B CG  1 
ATOM   3911 C CD  . ARG B 1 63  ? 7.360   19.463  23.530  1.00 50.61  ? 92  ARG B CD  1 
ATOM   3912 N NE  . ARG B 1 63  ? 7.733   20.144  24.777  1.00 54.40  ? 92  ARG B NE  1 
ATOM   3913 C CZ  . ARG B 1 63  ? 7.188   19.985  25.988  1.00 57.32  ? 92  ARG B CZ  1 
ATOM   3914 N NH1 . ARG B 1 63  ? 5.996   19.425  26.142  1.00 54.52  ? 92  ARG B NH1 1 
ATOM   3915 N NH2 . ARG B 1 63  ? 7.824   20.446  27.053  1.00 60.84  ? 92  ARG B NH2 1 
ATOM   3916 N N   . PHE B 1 64  ? 6.627   14.033  21.726  1.00 25.04  ? 93  PHE B N   1 
ATOM   3917 C CA  . PHE B 1 64  ? 5.800   13.218  20.859  1.00 26.09  ? 93  PHE B CA  1 
ATOM   3918 C C   . PHE B 1 64  ? 4.432   13.887  20.725  1.00 28.99  ? 93  PHE B C   1 
ATOM   3919 O O   . PHE B 1 64  ? 3.648   13.912  21.679  1.00 34.36  ? 93  PHE B O   1 
ATOM   3920 C CB  . PHE B 1 64  ? 5.691   11.815  21.487  1.00 25.46  ? 93  PHE B CB  1 
ATOM   3921 C CG  . PHE B 1 64  ? 7.028   11.102  21.662  1.00 26.89  ? 93  PHE B CG  1 
ATOM   3922 C CD1 . PHE B 1 64  ? 7.945   11.024  20.620  1.00 29.00  ? 93  PHE B CD1 1 
ATOM   3923 C CD2 . PHE B 1 64  ? 7.378   10.539  22.864  1.00 25.99  ? 93  PHE B CD2 1 
ATOM   3924 C CE1 . PHE B 1 64  ? 9.164   10.401  20.778  1.00 27.85  ? 93  PHE B CE1 1 
ATOM   3925 C CE2 . PHE B 1 64  ? 8.608   9.937   23.021  1.00 28.80  ? 93  PHE B CE2 1 
ATOM   3926 C CZ  . PHE B 1 64  ? 9.489   9.849   21.975  1.00 26.91  ? 93  PHE B CZ  1 
ATOM   3927 N N   . ARG B 1 65  ? 4.130   14.418  19.537  1.00 26.37  ? 94  ARG B N   1 
ATOM   3928 C CA  . ARG B 1 65  ? 2.877   15.133  19.329  1.00 26.28  ? 94  ARG B CA  1 
ATOM   3929 C C   . ARG B 1 65  ? 2.646   16.099  20.485  1.00 28.48  ? 94  ARG B C   1 
ATOM   3930 O O   . ARG B 1 65  ? 1.523   16.192  20.981  1.00 27.46  ? 94  ARG B O   1 
ATOM   3931 C CB  . ARG B 1 65  ? 1.635   14.242  19.184  1.00 24.75  ? 94  ARG B CB  1 
ATOM   3932 C CG  . ARG B 1 65  ? 1.622   13.393  17.918  1.00 26.02  ? 94  ARG B CG  1 
ATOM   3933 C CD  . ARG B 1 65  ? 1.373   14.201  16.631  1.00 25.93  ? 94  ARG B CD  1 
ATOM   3934 N NE  . ARG B 1 65  ? 1.220   13.283  15.494  1.00 27.74  ? 94  ARG B NE  1 
ATOM   3935 C CZ  . ARG B 1 65  ? 0.751   13.604  14.300  1.00 28.06  ? 94  ARG B CZ  1 
ATOM   3936 N NH1 . ARG B 1 65  ? 0.507   14.864  13.994  1.00 24.91  ? 94  ARG B NH1 1 
ATOM   3937 N NH2 . ARG B 1 65  ? 0.514   12.662  13.404  1.00 33.26  ? 94  ARG B NH2 1 
ATOM   3938 N N   . GLY B 1 66  ? 3.719   16.773  20.921  1.00 30.35  ? 95  GLY B N   1 
ATOM   3939 C CA  . GLY B 1 66  ? 3.625   17.814  21.935  1.00 32.72  ? 95  GLY B CA  1 
ATOM   3940 C C   . GLY B 1 66  ? 3.966   17.340  23.353  1.00 32.99  ? 95  GLY B C   1 
ATOM   3941 O O   . GLY B 1 66  ? 4.314   18.163  24.197  1.00 37.81  ? 95  GLY B O   1 
ATOM   3942 N N   . PHE B 1 67  ? 3.853   16.035  23.631  1.00 31.72  ? 96  PHE B N   1 
ATOM   3943 C CA  . PHE B 1 67  ? 4.055   15.501  24.971  1.00 31.53  ? 96  PHE B CA  1 
ATOM   3944 C C   . PHE B 1 67  ? 5.520   15.143  25.183  1.00 33.17  ? 96  PHE B C   1 
ATOM   3945 O O   . PHE B 1 67  ? 6.120   14.509  24.316  1.00 31.46  ? 96  PHE B O   1 
ATOM   3946 C CB  . PHE B 1 67  ? 3.126   14.319  25.220  1.00 34.56  ? 96  PHE B CB  1 
ATOM   3947 C CG  . PHE B 1 67  ? 1.644   14.669  25.257  1.00 35.56  ? 96  PHE B CG  1 
ATOM   3948 C CD1 . PHE B 1 67  ? 0.887   14.698  24.092  1.00 35.63  ? 96  PHE B CD1 1 
ATOM   3949 C CD2 . PHE B 1 67  ? 0.986   14.901  26.458  1.00 40.99  ? 96  PHE B CD2 1 
ATOM   3950 C CE1 . PHE B 1 67  ? -0.476  14.957  24.127  1.00 38.90  ? 96  PHE B CE1 1 
ATOM   3951 C CE2 . PHE B 1 67  ? -0.375  15.192  26.486  1.00 40.73  ? 96  PHE B CE2 1 
ATOM   3952 C CZ  . PHE B 1 67  ? -1.105  15.217  25.320  1.00 37.80  ? 96  PHE B CZ  1 
ATOM   3953 N N   . SER B 1 68  ? 6.090   15.606  26.317  1.00 29.75  ? 97  SER B N   1 
ATOM   3954 C CA  . SER B 1 68  ? 7.467   15.313  26.710  1.00 29.89  ? 97  SER B CA  1 
ATOM   3955 C C   . SER B 1 68  ? 7.541   13.871  27.167  1.00 27.02  ? 97  SER B C   1 
ATOM   3956 O O   . SER B 1 68  ? 6.511   13.268  27.393  1.00 28.20  ? 97  SER B O   1 
ATOM   3957 C CB  . SER B 1 68  ? 7.944   16.205  27.836  1.00 33.80  ? 97  SER B CB  1 
ATOM   3958 O OG  . SER B 1 68  ? 7.381   15.753  29.059  1.00 34.31  ? 97  SER B OG  1 
ATOM   3959 N N   . ILE B 1 69  ? 8.750   13.339  27.352  1.00 29.01  ? 98  ILE B N   1 
ATOM   3960 C CA  . ILE B 1 69  ? 8.899   11.981  27.832  1.00 29.39  ? 98  ILE B CA  1 
ATOM   3961 C C   . ILE B 1 69  ? 8.259   11.815  29.215  1.00 29.07  ? 98  ILE B C   1 
ATOM   3962 O O   . ILE B 1 69  ? 7.527   10.859  29.438  1.00 27.94  ? 98  ILE B O   1 
ATOM   3963 C CB  . ILE B 1 69  ? 10.377  11.560  27.843  1.00 35.32  ? 98  ILE B CB  1 
ATOM   3964 C CG1 . ILE B 1 69  ? 10.990  11.576  26.429  1.00 35.80  ? 98  ILE B CG1 1 
ATOM   3965 C CG2 . ILE B 1 69  ? 10.514  10.192  28.516  1.00 37.38  ? 98  ILE B CG2 1 
ATOM   3966 C CD1 . ILE B 1 69  ? 10.815  10.306  25.664  1.00 31.91  ? 98  ILE B CD1 1 
ATOM   3967 N N   . PRO B 1 70  ? 8.587   12.649  30.226  1.00 30.97  ? 99  PRO B N   1 
ATOM   3968 C CA  . PRO B 1 70  ? 7.909   12.558  31.527  1.00 33.03  ? 99  PRO B CA  1 
ATOM   3969 C C   . PRO B 1 70  ? 6.385   12.583  31.421  1.00 33.60  ? 99  PRO B C   1 
ATOM   3970 O O   . PRO B 1 70  ? 5.704   11.840  32.132  1.00 32.63  ? 99  PRO B O   1 
ATOM   3971 C CB  . PRO B 1 70  ? 8.483   13.764  32.283  1.00 33.29  ? 99  PRO B CB  1 
ATOM   3972 C CG  . PRO B 1 70  ? 9.855   13.938  31.675  1.00 33.62  ? 99  PRO B CG  1 
ATOM   3973 C CD  . PRO B 1 70  ? 9.660   13.667  30.202  1.00 31.19  ? 99  PRO B CD  1 
ATOM   3974 N N   . GLU B 1 71  ? 5.848   13.401  30.491  1.00 34.30  ? 100 GLU B N   1 
ATOM   3975 C CA  . GLU B 1 71  ? 4.412   13.454  30.278  1.00 31.86  ? 100 GLU B CA  1 
ATOM   3976 C C   . GLU B 1 71  ? 3.903   12.106  29.769  1.00 36.25  ? 100 GLU B C   1 
ATOM   3977 O O   . GLU B 1 71  ? 2.828   11.654  30.188  1.00 38.19  ? 100 GLU B O   1 
ATOM   3978 C CB  . GLU B 1 71  ? 4.001   14.615  29.379  1.00 33.61  ? 100 GLU B CB  1 
ATOM   3979 C CG  . GLU B 1 71  ? 4.142   15.972  30.070  1.00 35.06  ? 100 GLU B CG  1 
ATOM   3980 C CD  . GLU B 1 71  ? 4.056   17.189  29.165  1.00 40.86  ? 100 GLU B CD  1 
ATOM   3981 O OE1 . GLU B 1 71  ? 3.540   18.195  29.672  1.00 45.17  ? 100 GLU B OE1 1 
ATOM   3982 O OE2 . GLU B 1 71  ? 4.482   17.180  27.977  1.00 46.78  ? 100 GLU B OE2 1 
ATOM   3983 N N   . CYS B 1 72  ? 4.668   11.453  28.876  1.00 35.89  ? 101 CYS B N   1 
ATOM   3984 C CA  . CYS B 1 72  ? 4.258   10.163  28.328  1.00 32.01  ? 101 CYS B CA  1 
ATOM   3985 C C   . CYS B 1 72  ? 4.315   9.069   29.396  1.00 31.58  ? 101 CYS B C   1 
ATOM   3986 O O   . CYS B 1 72  ? 3.476   8.164   29.451  1.00 30.84  ? 101 CYS B O   1 
ATOM   3987 C CB  . CYS B 1 72  ? 5.071   9.806   27.084  1.00 30.91  ? 101 CYS B CB  1 
ATOM   3988 S SG  . CYS B 1 72  ? 4.724   10.941  25.715  1.00 36.13  ? 101 CYS B SG  1 
ATOM   3989 N N   . GLN B 1 73  ? 5.331   9.133   30.249  1.00 31.39  ? 102 GLN B N   1 
ATOM   3990 C CA  . GLN B 1 73  ? 5.410   8.210   31.367  1.00 34.49  ? 102 GLN B CA  1 
ATOM   3991 C C   . GLN B 1 73  ? 4.209   8.313   32.315  1.00 35.97  ? 102 GLN B C   1 
ATOM   3992 O O   . GLN B 1 73  ? 3.680   7.291   32.734  1.00 35.12  ? 102 GLN B O   1 
ATOM   3993 C CB  . GLN B 1 73  ? 6.741   8.452   32.060  1.00 36.83  ? 102 GLN B CB  1 
ATOM   3994 C CG  . GLN B 1 73  ? 7.915   7.852   31.297  1.00 41.86  ? 102 GLN B CG  1 
ATOM   3995 C CD  . GLN B 1 73  ? 9.136   7.812   32.180  1.00 51.48  ? 102 GLN B CD  1 
ATOM   3996 O OE1 . GLN B 1 73  ? 9.756   8.849   32.443  1.00 43.49  ? 102 GLN B OE1 1 
ATOM   3997 N NE2 . GLN B 1 73  ? 9.452   6.621   32.678  1.00 50.44  ? 102 GLN B NE2 1 
ATOM   3998 N N   . LYS B 1 74  ? 3.783   9.535   32.652  1.00 40.72  ? 103 LYS B N   1 
ATOM   3999 C CA  . LYS B 1 74  ? 2.557   9.748   33.406  1.00 40.63  ? 103 LYS B CA  1 
ATOM   4000 C C   . LYS B 1 74  ? 1.323   9.227   32.666  1.00 37.51  ? 103 LYS B C   1 
ATOM   4001 O O   . LYS B 1 74  ? 0.538   8.480   33.255  1.00 32.60  ? 103 LYS B O   1 
ATOM   4002 C CB  . LYS B 1 74  ? 2.260   11.224  33.712  1.00 51.16  ? 103 LYS B CB  1 
ATOM   4003 C CG  . LYS B 1 74  ? 3.044   11.800  34.890  1.00 61.29  ? 103 LYS B CG  1 
ATOM   4004 C CD  . LYS B 1 74  ? 2.481   13.086  35.489  1.00 65.89  ? 103 LYS B CD  1 
ATOM   4005 C CE  . LYS B 1 74  ? 3.269   13.535  36.696  1.00 72.52  ? 103 LYS B CE  1 
ATOM   4006 N NZ  . LYS B 1 74  ? 4.691   13.755  36.406  1.00 67.88  ? 103 LYS B NZ  1 
ATOM   4007 N N   . LEU B 1 75  ? 1.107   9.660   31.409  1.00 30.69  ? 104 LEU B N   1 
ATOM   4008 C CA  . LEU B 1 75  ? -0.228  9.627   30.819  1.00 32.37  ? 104 LEU B CA  1 
ATOM   4009 C C   . LEU B 1 75  ? -0.514  8.323   30.078  1.00 30.02  ? 104 LEU B C   1 
ATOM   4010 O O   . LEU B 1 75  ? -1.671  7.914   30.010  1.00 32.99  ? 104 LEU B O   1 
ATOM   4011 C CB  . LEU B 1 75  ? -0.426  10.840  29.912  1.00 34.94  ? 104 LEU B CB  1 
ATOM   4012 C CG  . LEU B 1 75  ? -0.399  12.192  30.635  1.00 41.03  ? 104 LEU B CG  1 
ATOM   4013 C CD1 . LEU B 1 75  ? -0.235  13.370  29.689  1.00 38.53  ? 104 LEU B CD1 1 
ATOM   4014 C CD2 . LEU B 1 75  ? -1.670  12.356  31.470  1.00 43.98  ? 104 LEU B CD2 1 
ATOM   4015 N N   . LEU B 1 76  ? 0.506   7.683   29.485  1.00 29.27  ? 105 LEU B N   1 
ATOM   4016 C CA  . LEU B 1 76  ? 0.257   6.569   28.580  1.00 31.21  ? 105 LEU B CA  1 
ATOM   4017 C C   . LEU B 1 76  ? -0.145  5.345   29.396  1.00 30.73  ? 105 LEU B C   1 
ATOM   4018 O O   . LEU B 1 76  ? 0.372   5.175   30.477  1.00 29.08  ? 105 LEU B O   1 
ATOM   4019 C CB  . LEU B 1 76  ? 1.492   6.291   27.736  1.00 29.44  ? 105 LEU B CB  1 
ATOM   4020 C CG  . LEU B 1 76  ? 1.888   7.374   26.731  1.00 32.88  ? 105 LEU B CG  1 
ATOM   4021 C CD1 . LEU B 1 76  ? 3.225   6.964   26.114  1.00 33.41  ? 105 LEU B CD1 1 
ATOM   4022 C CD2 . LEU B 1 76  ? 0.818   7.525   25.656  1.00 31.28  ? 105 LEU B CD2 1 
ATOM   4023 N N   . PRO B 1 77  ? -1.088  4.480   28.944  1.00 31.16  ? 106 PRO B N   1 
ATOM   4024 C CA  . PRO B 1 77  ? -1.369  3.240   29.649  1.00 33.20  ? 106 PRO B CA  1 
ATOM   4025 C C   . PRO B 1 77  ? -0.123  2.379   29.835  1.00 35.97  ? 106 PRO B C   1 
ATOM   4026 O O   . PRO B 1 77  ? 0.703   2.251   28.928  1.00 30.95  ? 106 PRO B O   1 
ATOM   4027 C CB  . PRO B 1 77  ? -2.420  2.527   28.803  1.00 32.89  ? 106 PRO B CB  1 
ATOM   4028 C CG  . PRO B 1 77  ? -3.059  3.635   28.015  1.00 31.95  ? 106 PRO B CG  1 
ATOM   4029 C CD  . PRO B 1 77  ? -1.998  4.701   27.815  1.00 30.89  ? 106 PRO B CD  1 
ATOM   4030 N N   . LYS B 1 78  ? -0.063  1.746   31.011  1.00 32.48  ? 107 LYS B N   1 
ATOM   4031 C CA  . LYS B 1 78  ? 0.941   0.751   31.331  1.00 34.76  ? 107 LYS B CA  1 
ATOM   4032 C C   . LYS B 1 78  ? 0.268   -0.609  31.226  1.00 31.40  ? 107 LYS B C   1 
ATOM   4033 O O   . LYS B 1 78  ? -0.941  -0.675  31.042  1.00 34.48  ? 107 LYS B O   1 
ATOM   4034 C CB  . LYS B 1 78  ? 1.478   1.156   32.707  1.00 37.18  ? 107 LYS B CB  1 
ATOM   4035 C CG  . LYS B 1 78  ? 1.961   2.606   32.722  1.00 45.46  ? 107 LYS B CG  1 
ATOM   4036 C CD  . LYS B 1 78  ? 2.364   3.155   34.083  1.00 60.87  ? 107 LYS B CD  1 
ATOM   4037 C CE  . LYS B 1 78  ? 2.913   4.560   34.016  1.00 60.53  ? 107 LYS B CE  1 
ATOM   4038 N NZ  . LYS B 1 78  ? 1.925   5.503   33.482  1.00 61.80  ? 107 LYS B NZ  1 
ATOM   4039 N N   . ALA B 1 79  ? 1.054   -1.691  31.233  1.00 32.23  ? 108 ALA B N   1 
ATOM   4040 C CA  . ALA B 1 79  ? 0.501   -3.020  31.439  1.00 33.30  ? 108 ALA B CA  1 
ATOM   4041 C C   . ALA B 1 79  ? -0.029  -3.105  32.873  1.00 42.55  ? 108 ALA B C   1 
ATOM   4042 O O   . ALA B 1 79  ? 0.455   -2.424  33.778  1.00 34.47  ? 108 ALA B O   1 
ATOM   4043 C CB  . ALA B 1 79  ? 1.531   -4.111  31.205  1.00 31.17  ? 108 ALA B CB  1 
ATOM   4044 N N   . LYS B 1 80  ? -1.010  -3.974  33.104  1.00 51.94  ? 109 LYS B N   1 
ATOM   4045 C CA  . LYS B 1 80  ? -1.656  -3.947  34.405  1.00 58.67  ? 109 LYS B CA  1 
ATOM   4046 C C   . LYS B 1 80  ? -0.658  -4.547  35.412  1.00 59.00  ? 109 LYS B C   1 
ATOM   4047 O O   . LYS B 1 80  ? -0.009  -5.568  35.151  1.00 56.19  ? 109 LYS B O   1 
ATOM   4048 C CB  . LYS B 1 80  ? -3.127  -4.365  34.230  1.00 66.95  ? 109 LYS B CB  1 
ATOM   4049 C CG  . LYS B 1 80  ? -3.459  -5.821  34.441  1.00 78.49  ? 109 LYS B CG  1 
ATOM   4050 C CD  . LYS B 1 80  ? -2.977  -6.794  33.369  1.00 93.39  ? 109 LYS B CD  1 
ATOM   4051 C CE  . LYS B 1 80  ? -2.026  -7.880  33.836  1.00 106.97 ? 109 LYS B CE  1 
ATOM   4052 N NZ  . LYS B 1 80  ? -2.166  -8.359  35.217  1.00 120.24 ? 109 LYS B NZ  1 
ATOM   4053 N N   . GLY B 1 81  ? -0.435  -3.797  36.504  1.00 58.98  ? 110 GLY B N   1 
ATOM   4054 C CA  . GLY B 1 81  ? 0.574   -4.110  37.503  1.00 63.70  ? 110 GLY B CA  1 
ATOM   4055 C C   . GLY B 1 81  ? 1.982   -3.717  37.054  1.00 64.72  ? 110 GLY B C   1 
ATOM   4056 O O   . GLY B 1 81  ? 2.952   -4.428  37.311  1.00 69.75  ? 110 GLY B O   1 
ATOM   4057 N N   . GLY B 1 82  ? 2.093   -2.566  36.386  1.00 62.85  ? 111 GLY B N   1 
ATOM   4058 C CA  . GLY B 1 82  ? 3.338   -2.182  35.745  1.00 51.08  ? 111 GLY B CA  1 
ATOM   4059 C C   . GLY B 1 82  ? 3.538   -0.677  35.831  1.00 47.76  ? 111 GLY B C   1 
ATOM   4060 O O   . GLY B 1 82  ? 2.624   0.039   36.234  1.00 45.05  ? 111 GLY B O   1 
ATOM   4061 N N   . GLU B 1 83  ? 4.745   -0.222  35.474  1.00 40.91  ? 112 GLU B N   1 
ATOM   4062 C CA  . GLU B 1 83  ? 5.131   1.164   35.667  1.00 43.91  ? 112 GLU B CA  1 
ATOM   4063 C C   . GLU B 1 83  ? 5.487   1.848   34.342  1.00 37.54  ? 112 GLU B C   1 
ATOM   4064 O O   . GLU B 1 83  ? 5.526   3.070   34.273  1.00 38.79  ? 112 GLU B O   1 
ATOM   4065 C CB  . GLU B 1 83  ? 6.385   1.297   36.525  1.00 49.58  ? 112 GLU B CB  1 
ATOM   4066 C CG  . GLU B 1 83  ? 6.246   0.889   37.990  1.00 62.54  ? 112 GLU B CG  1 
ATOM   4067 C CD  . GLU B 1 83  ? 7.603   0.957   38.681  1.00 64.22  ? 112 GLU B CD  1 
ATOM   4068 O OE1 . GLU B 1 83  ? 7.857   1.976   39.360  1.00 64.90  ? 112 GLU B OE1 1 
ATOM   4069 O OE2 . GLU B 1 83  ? 8.420   0.016   38.513  1.00 76.95  ? 112 GLU B OE2 1 
ATOM   4070 N N   . GLU B 1 84  ? 5.757   1.083   33.290  1.00 35.19  ? 113 GLU B N   1 
ATOM   4071 C CA  . GLU B 1 84  ? 6.385   1.673   32.121  1.00 39.52  ? 113 GLU B CA  1 
ATOM   4072 C C   . GLU B 1 84  ? 5.370   1.847   30.987  1.00 32.10  ? 113 GLU B C   1 
ATOM   4073 O O   . GLU B 1 84  ? 4.505   0.998   30.787  1.00 33.51  ? 113 GLU B O   1 
ATOM   4074 C CB  . GLU B 1 84  ? 7.640   0.858   31.797  1.00 42.26  ? 113 GLU B CB  1 
ATOM   4075 C CG  . GLU B 1 84  ? 8.748   0.990   32.845  1.00 41.61  ? 113 GLU B CG  1 
ATOM   4076 C CD  . GLU B 1 84  ? 9.302   2.378   33.149  1.00 42.98  ? 113 GLU B CD  1 
ATOM   4077 O OE1 . GLU B 1 84  ? 9.099   3.392   32.428  1.00 36.23  ? 113 GLU B OE1 1 
ATOM   4078 O OE2 . GLU B 1 84  ? 9.974   2.434   34.211  1.00 45.40  ? 113 GLU B OE2 1 
ATOM   4079 N N   . PRO B 1 85  ? 5.460   2.956   30.207  1.00 35.82  ? 114 PRO B N   1 
ATOM   4080 C CA  . PRO B 1 85  ? 4.567   3.202   29.071  1.00 31.63  ? 114 PRO B CA  1 
ATOM   4081 C C   . PRO B 1 85  ? 4.614   2.041   28.080  1.00 30.51  ? 114 PRO B C   1 
ATOM   4082 O O   . PRO B 1 85  ? 5.686   1.498   27.809  1.00 28.69  ? 114 PRO B O   1 
ATOM   4083 C CB  . PRO B 1 85  ? 4.994   4.520   28.425  1.00 34.62  ? 114 PRO B CB  1 
ATOM   4084 C CG  . PRO B 1 85  ? 6.254   4.940   29.157  1.00 39.19  ? 114 PRO B CG  1 
ATOM   4085 C CD  . PRO B 1 85  ? 6.449   4.032   30.378  1.00 37.40  ? 114 PRO B CD  1 
ATOM   4086 N N   . LEU B 1 86  ? 3.426   1.605   27.648  1.00 27.96  ? 115 LEU B N   1 
ATOM   4087 C CA  . LEU B 1 86  ? 3.308   0.617   26.596  1.00 31.47  ? 115 LEU B CA  1 
ATOM   4088 C C   . LEU B 1 86  ? 3.526   1.259   25.221  1.00 34.07  ? 115 LEU B C   1 
ATOM   4089 O O   . LEU B 1 86  ? 2.838   2.216   24.851  1.00 27.95  ? 115 LEU B O   1 
ATOM   4090 C CB  . LEU B 1 86  ? 1.956   -0.088  26.659  1.00 34.99  ? 115 LEU B CB  1 
ATOM   4091 C CG  . LEU B 1 86  ? 1.734   -1.060  27.822  1.00 38.90  ? 115 LEU B CG  1 
ATOM   4092 C CD1 . LEU B 1 86  ? 0.478   -1.886  27.612  1.00 42.99  ? 115 LEU B CD1 1 
ATOM   4093 C CD2 . LEU B 1 86  ? 2.915   -1.981  27.988  1.00 39.36  ? 115 LEU B CD2 1 
ATOM   4094 N N   . PRO B 1 87  ? 4.481   0.737   24.404  1.00 28.15  ? 116 PRO B N   1 
ATOM   4095 C CA  . PRO B 1 87  ? 4.738   1.282   23.071  1.00 29.28  ? 116 PRO B CA  1 
ATOM   4096 C C   . PRO B 1 87  ? 3.524   1.359   22.163  1.00 28.39  ? 116 PRO B C   1 
ATOM   4097 O O   . PRO B 1 87  ? 3.522   2.190   21.254  1.00 27.83  ? 116 PRO B O   1 
ATOM   4098 C CB  . PRO B 1 87  ? 5.817   0.390   22.450  1.00 26.96  ? 116 PRO B CB  1 
ATOM   4099 C CG  . PRO B 1 87  ? 5.938   -0.785  23.416  1.00 29.46  ? 116 PRO B CG  1 
ATOM   4100 C CD  . PRO B 1 87  ? 5.415   -0.327  24.762  1.00 26.82  ? 116 PRO B CD  1 
ATOM   4101 N N   . GLU B 1 88  ? 2.523   0.501   22.407  1.00 25.27  ? 117 GLU B N   1 
ATOM   4102 C CA  . GLU B 1 88  ? 1.259   0.597   21.708  1.00 26.58  ? 117 GLU B CA  1 
ATOM   4103 C C   . GLU B 1 88  ? 0.668   1.992   21.915  1.00 26.33  ? 117 GLU B C   1 
ATOM   4104 O O   . GLU B 1 88  ? 0.156   2.597   20.976  1.00 23.98  ? 117 GLU B O   1 
ATOM   4105 C CB  . GLU B 1 88  ? 0.169   -0.355  22.205  1.00 26.39  ? 117 GLU B CB  1 
ATOM   4106 C CG  . GLU B 1 88  ? 0.368   -1.843  21.939  1.00 26.72  ? 117 GLU B CG  1 
ATOM   4107 C CD  . GLU B 1 88  ? 1.324   -2.601  22.842  1.00 25.46  ? 117 GLU B CD  1 
ATOM   4108 O OE1 . GLU B 1 88  ? 2.220   -1.936  23.412  1.00 25.39  ? 117 GLU B OE1 1 
ATOM   4109 O OE2 . GLU B 1 88  ? 1.151   -3.852  22.946  1.00 26.70  ? 117 GLU B OE2 1 
ATOM   4110 N N   . GLY B 1 89  ? 0.694   2.499   23.155  1.00 25.75  ? 118 GLY B N   1 
ATOM   4111 C CA  . GLY B 1 89  ? 0.071   3.786   23.408  1.00 25.25  ? 118 GLY B CA  1 
ATOM   4112 C C   . GLY B 1 89  ? 0.807   4.914   22.696  1.00 24.48  ? 118 GLY B C   1 
ATOM   4113 O O   . GLY B 1 89  ? 0.196   5.897   22.282  1.00 25.95  ? 118 GLY B O   1 
ATOM   4114 N N   . LEU B 1 90  ? 2.135   4.807   22.687  1.00 24.41  ? 119 LEU B N   1 
ATOM   4115 C CA  . LEU B 1 90  ? 2.982   5.738   21.964  1.00 23.40  ? 119 LEU B CA  1 
ATOM   4116 C C   . LEU B 1 90  ? 2.551   5.787   20.495  1.00 24.40  ? 119 LEU B C   1 
ATOM   4117 O O   . LEU B 1 90  ? 2.282   6.852   19.941  1.00 28.14  ? 119 LEU B O   1 
ATOM   4118 C CB  . LEU B 1 90  ? 4.441   5.310   22.182  1.00 26.76  ? 119 LEU B CB  1 
ATOM   4119 C CG  . LEU B 1 90  ? 5.512   6.139   21.479  1.00 26.70  ? 119 LEU B CG  1 
ATOM   4120 C CD1 . LEU B 1 90  ? 5.510   5.732   19.997  1.00 26.34  ? 119 LEU B CD1 1 
ATOM   4121 C CD2 . LEU B 1 90  ? 5.289   7.630   21.572  1.00 28.28  ? 119 LEU B CD2 1 
ATOM   4122 N N   . PHE B 1 91  ? 2.429   4.629   19.854  1.00 20.61  ? 120 PHE B N   1 
ATOM   4123 C CA  . PHE B 1 91  ? 2.017   4.630   18.462  1.00 19.54  ? 120 PHE B CA  1 
ATOM   4124 C C   . PHE B 1 91  ? 0.671   5.331   18.308  1.00 20.11  ? 120 PHE B C   1 
ATOM   4125 O O   . PHE B 1 91  ? 0.505   6.195   17.433  1.00 18.86  ? 120 PHE B O   1 
ATOM   4126 C CB  . PHE B 1 91  ? 2.001   3.168   18.030  1.00 21.46  ? 120 PHE B CB  1 
ATOM   4127 C CG  . PHE B 1 91  ? 1.659   3.065   16.557  1.00 19.49  ? 120 PHE B CG  1 
ATOM   4128 C CD1 . PHE B 1 91  ? 2.612   3.429   15.612  1.00 19.65  ? 120 PHE B CD1 1 
ATOM   4129 C CD2 . PHE B 1 91  ? 0.424   2.617   16.127  1.00 19.20  ? 120 PHE B CD2 1 
ATOM   4130 C CE1 . PHE B 1 91  ? 2.321   3.356   14.279  1.00 20.77  ? 120 PHE B CE1 1 
ATOM   4131 C CE2 . PHE B 1 91  ? 0.130   2.572   14.769  1.00 20.80  ? 120 PHE B CE2 1 
ATOM   4132 C CZ  . PHE B 1 91  ? 1.078   2.936   13.859  1.00 19.28  ? 120 PHE B CZ  1 
ATOM   4133 N N   . TRP B 1 92  ? -0.280  5.026   19.207  1.00 19.63  ? 121 TRP B N   1 
ATOM   4134 C CA  . TRP B 1 92  ? -1.610  5.621   19.139  1.00 19.83  ? 121 TRP B CA  1 
ATOM   4135 C C   . TRP B 1 92  ? -1.468  7.127   19.130  1.00 20.08  ? 121 TRP B C   1 
ATOM   4136 O O   . TRP B 1 92  ? -2.087  7.805   18.306  1.00 27.59  ? 121 TRP B O   1 
ATOM   4137 C CB  . TRP B 1 92  ? -2.500  5.177   20.317  1.00 22.99  ? 121 TRP B CB  1 
ATOM   4138 C CG  . TRP B 1 92  ? -3.939  5.585   20.167  1.00 20.71  ? 121 TRP B CG  1 
ATOM   4139 C CD1 . TRP B 1 92  ? -4.465  6.822   20.367  1.00 22.56  ? 121 TRP B CD1 1 
ATOM   4140 C CD2 . TRP B 1 92  ? -5.032  4.747   19.748  1.00 23.85  ? 121 TRP B CD2 1 
ATOM   4141 N NE1 . TRP B 1 92  ? -5.809  6.826   20.115  1.00 22.45  ? 121 TRP B NE1 1 
ATOM   4142 C CE2 . TRP B 1 92  ? -6.190  5.561   19.743  1.00 26.35  ? 121 TRP B CE2 1 
ATOM   4143 C CE3 . TRP B 1 92  ? -5.143  3.394   19.412  1.00 24.15  ? 121 TRP B CE3 1 
ATOM   4144 C CZ2 . TRP B 1 92  ? -7.437  5.068   19.377  1.00 26.31  ? 121 TRP B CZ2 1 
ATOM   4145 C CZ3 . TRP B 1 92  ? -6.381  2.907   19.038  1.00 26.90  ? 121 TRP B CZ3 1 
ATOM   4146 C CH2 . TRP B 1 92  ? -7.503  3.733   19.017  1.00 26.51  ? 121 TRP B CH2 1 
ATOM   4147 N N   . LEU B 1 93  ? -0.691  7.646   20.074  1.00 22.42  ? 122 LEU B N   1 
ATOM   4148 C CA  . LEU B 1 93  ? -0.439  9.072   20.177  1.00 21.37  ? 122 LEU B CA  1 
ATOM   4149 C C   . LEU B 1 93  ? 0.182   9.692   18.920  1.00 21.14  ? 122 LEU B C   1 
ATOM   4150 O O   . LEU B 1 93  ? -0.170  10.821  18.529  1.00 21.02  ? 122 LEU B O   1 
ATOM   4151 C CB  . LEU B 1 93  ? 0.439   9.305   21.397  1.00 23.38  ? 122 LEU B CB  1 
ATOM   4152 C CG  . LEU B 1 93  ? 1.015   10.710  21.514  1.00 26.07  ? 122 LEU B CG  1 
ATOM   4153 C CD1 . LEU B 1 93  ? -0.059  11.795  21.619  1.00 27.54  ? 122 LEU B CD1 1 
ATOM   4154 C CD2 . LEU B 1 93  ? 1.926   10.675  22.718  1.00 27.88  ? 122 LEU B CD2 1 
ATOM   4155 N N   . LEU B 1 94  ? 1.154   8.994   18.318  1.00 22.38  ? 123 LEU B N   1 
ATOM   4156 C CA  . LEU B 1 94  ? 1.861   9.508   17.156  1.00 23.86  ? 123 LEU B CA  1 
ATOM   4157 C C   . LEU B 1 94  ? 0.878   9.589   15.986  1.00 24.20  ? 123 LEU B C   1 
ATOM   4158 O O   . LEU B 1 94  ? 0.871   10.568  15.254  1.00 25.48  ? 123 LEU B O   1 
ATOM   4159 C CB  . LEU B 1 94  ? 3.099   8.656   16.830  1.00 23.73  ? 123 LEU B CB  1 
ATOM   4160 C CG  . LEU B 1 94  ? 4.286   8.779   17.798  1.00 24.11  ? 123 LEU B CG  1 
ATOM   4161 C CD1 . LEU B 1 94  ? 5.570   8.217   17.191  1.00 26.05  ? 123 LEU B CD1 1 
ATOM   4162 C CD2 . LEU B 1 94  ? 4.511   10.212  18.204  1.00 27.96  ? 123 LEU B CD2 1 
ATOM   4163 N N   . VAL B 1 95  ? 0.056   8.552   15.831  1.00 21.26  ? 124 VAL B N   1 
ATOM   4164 C CA  . VAL B 1 95  ? -0.948  8.494   14.784  1.00 23.76  ? 124 VAL B CA  1 
ATOM   4165 C C   . VAL B 1 95  ? -2.067  9.504   15.020  1.00 26.82  ? 124 VAL B C   1 
ATOM   4166 O O   . VAL B 1 95  ? -2.482  10.158  14.065  1.00 26.21  ? 124 VAL B O   1 
ATOM   4167 C CB  . VAL B 1 95  ? -1.538  7.085   14.651  1.00 22.00  ? 124 VAL B CB  1 
ATOM   4168 C CG1 . VAL B 1 95  ? -2.697  7.072   13.667  1.00 24.25  ? 124 VAL B CG1 1 
ATOM   4169 C CG2 . VAL B 1 95  ? -0.486  6.086   14.213  1.00 24.44  ? 124 VAL B CG2 1 
ATOM   4170 N N   . THR B 1 96  ? -2.541  9.675   16.279  1.00 25.62  ? 125 THR B N   1 
ATOM   4171 C CA  . THR B 1 96  ? -3.781  10.403  16.450  1.00 24.52  ? 125 THR B CA  1 
ATOM   4172 C C   . THR B 1 96  ? -3.541  11.813  16.981  1.00 26.03  ? 125 THR B C   1 
ATOM   4173 O O   . THR B 1 96  ? -4.312  12.710  16.676  1.00 27.68  ? 125 THR B O   1 
ATOM   4174 C CB  . THR B 1 96  ? -4.753  9.639   17.348  1.00 23.53  ? 125 THR B CB  1 
ATOM   4175 O OG1 . THR B 1 96  ? -4.218  9.727   18.668  1.00 20.18  ? 125 THR B OG1 1 
ATOM   4176 C CG2 . THR B 1 96  ? -5.015  8.224   16.865  1.00 23.26  ? 125 THR B CG2 1 
ATOM   4177 N N   . GLY B 1 97  ? -2.499  12.008  17.779  1.00 25.66  ? 126 GLY B N   1 
ATOM   4178 C CA  . GLY B 1 97  ? -2.283  13.275  18.457  1.00 26.90  ? 126 GLY B CA  1 
ATOM   4179 C C   . GLY B 1 97  ? -2.923  13.239  19.837  1.00 25.59  ? 126 GLY B C   1 
ATOM   4180 O O   . GLY B 1 97  ? -2.733  14.160  20.611  1.00 24.08  ? 126 GLY B O   1 
ATOM   4181 N N   . HIS B 1 98  ? -3.566  12.102  20.140  1.00 28.67  ? 127 HIS B N   1 
ATOM   4182 C CA  . HIS B 1 98  ? -4.331  11.894  21.357  1.00 34.77  ? 127 HIS B CA  1 
ATOM   4183 C C   . HIS B 1 98  ? -3.658  10.818  22.206  1.00 32.53  ? 127 HIS B C   1 
ATOM   4184 O O   . HIS B 1 98  ? -3.158  9.822   21.682  1.00 35.90  ? 127 HIS B O   1 
ATOM   4185 C CB  . HIS B 1 98  ? -5.783  11.491  21.035  1.00 36.95  ? 127 HIS B CB  1 
ATOM   4186 C CG  . HIS B 1 98  ? -6.557  12.618  20.433  1.00 46.46  ? 127 HIS B CG  1 
ATOM   4187 N ND1 . HIS B 1 98  ? -6.846  13.771  21.136  1.00 49.30  ? 127 HIS B ND1 1 
ATOM   4188 C CD2 . HIS B 1 98  ? -7.027  12.806  19.191  1.00 48.21  ? 127 HIS B CD2 1 
ATOM   4189 C CE1 . HIS B 1 98  ? -7.491  14.612  20.336  1.00 54.08  ? 127 HIS B CE1 1 
ATOM   4190 N NE2 . HIS B 1 98  ? -7.627  14.035  19.152  1.00 51.39  ? 127 HIS B NE2 1 
ATOM   4191 N N   . ILE B 1 99  ? -3.684  11.023  23.523  1.00 33.85  ? 128 ILE B N   1 
ATOM   4192 C CA  . ILE B 1 99  ? -3.361  9.982   24.486  1.00 33.56  ? 128 ILE B CA  1 
ATOM   4193 C C   . ILE B 1 99  ? -4.472  8.944   24.451  1.00 33.59  ? 128 ILE B C   1 
ATOM   4194 O O   . ILE B 1 99  ? -5.645  9.274   24.616  1.00 34.52  ? 128 ILE B O   1 
ATOM   4195 C CB  . ILE B 1 99  ? -3.178  10.574  25.893  1.00 35.56  ? 128 ILE B CB  1 
ATOM   4196 C CG1 . ILE B 1 99  ? -1.966  11.486  25.944  1.00 34.02  ? 128 ILE B CG1 1 
ATOM   4197 C CG2 . ILE B 1 99  ? -3.097  9.463   26.952  1.00 39.62  ? 128 ILE B CG2 1 
ATOM   4198 C CD1 . ILE B 1 99  ? -0.631  10.763  25.894  1.00 36.33  ? 128 ILE B CD1 1 
ATOM   4199 N N   . PRO B 1 100 ? -4.149  7.662   24.200  1.00 27.05  ? 129 PRO B N   1 
ATOM   4200 C CA  . PRO B 1 100 ? -5.167  6.612   24.146  1.00 27.27  ? 129 PRO B CA  1 
ATOM   4201 C C   . PRO B 1 100 ? -5.745  6.338   25.524  1.00 31.39  ? 129 PRO B C   1 
ATOM   4202 O O   . PRO B 1 100 ? -5.110  6.673   26.517  1.00 27.92  ? 129 PRO B O   1 
ATOM   4203 C CB  . PRO B 1 100 ? -4.354  5.428   23.678  1.00 24.52  ? 129 PRO B CB  1 
ATOM   4204 C CG  . PRO B 1 100 ? -2.990  5.686   24.253  1.00 23.61  ? 129 PRO B CG  1 
ATOM   4205 C CD  . PRO B 1 100 ? -2.787  7.133   23.997  1.00 24.89  ? 129 PRO B CD  1 
ATOM   4206 N N   . THR B 1 101 ? -6.920  5.709   25.554  1.00 34.28  ? 130 THR B N   1 
ATOM   4207 C CA  . THR B 1 101 ? -7.472  5.151   26.780  1.00 38.29  ? 130 THR B CA  1 
ATOM   4208 C C   . THR B 1 101 ? -6.872  3.763   26.937  1.00 40.44  ? 130 THR B C   1 
ATOM   4209 O O   . THR B 1 101 ? -6.325  3.231   25.966  1.00 38.75  ? 130 THR B O   1 
ATOM   4210 C CB  . THR B 1 101 ? -8.989  5.020   26.673  1.00 37.18  ? 130 THR B CB  1 
ATOM   4211 O OG1 . THR B 1 101 ? -9.108  3.988   25.702  1.00 40.63  ? 130 THR B OG1 1 
ATOM   4212 C CG2 . THR B 1 101 ? -9.699  6.280   26.217  1.00 38.09  ? 130 THR B CG2 1 
ATOM   4213 N N   . GLU B 1 102 ? -7.082  3.149   28.108  1.00 38.52  ? 131 GLU B N   1 
ATOM   4214 C CA  . GLU B 1 102 ? -6.596  1.803   28.358  1.00 41.27  ? 131 GLU B CA  1 
ATOM   4215 C C   . GLU B 1 102 ? -7.199  0.864   27.316  1.00 37.12  ? 131 GLU B C   1 
ATOM   4216 O O   . GLU B 1 102 ? -6.513  -0.000  26.798  1.00 36.72  ? 131 GLU B O   1 
ATOM   4217 C CB  . GLU B 1 102 ? -6.907  1.241   29.753  1.00 53.05  ? 131 GLU B CB  1 
ATOM   4218 C CG  . GLU B 1 102 ? -6.523  2.139   30.933  1.00 67.12  ? 131 GLU B CG  1 
ATOM   4219 C CD  . GLU B 1 102 ? -5.229  1.874   31.698  1.00 71.84  ? 131 GLU B CD  1 
ATOM   4220 O OE1 . GLU B 1 102 ? -4.550  0.835   31.517  1.00 78.00  ? 131 GLU B OE1 1 
ATOM   4221 O OE2 . GLU B 1 102 ? -4.895  2.762   32.514  1.00 72.58  ? 131 GLU B OE2 1 
ATOM   4222 N N   . GLU B 1 103 ? -8.484  1.019   27.006  1.00 32.63  ? 132 GLU B N   1 
ATOM   4223 C CA  . GLU B 1 103 ? -9.140  0.085   26.106  1.00 39.65  ? 132 GLU B CA  1 
ATOM   4224 C C   . GLU B 1 103 ? -8.588  0.213   24.683  1.00 30.40  ? 132 GLU B C   1 
ATOM   4225 O O   . GLU B 1 103 ? -8.568  -0.769  23.956  1.00 28.83  ? 132 GLU B O   1 
ATOM   4226 C CB  . GLU B 1 103 ? -10.665 0.261   26.091  1.00 49.57  ? 132 GLU B CB  1 
ATOM   4227 C CG  . GLU B 1 103 ? -11.327 -0.045  27.436  1.00 61.74  ? 132 GLU B CG  1 
ATOM   4228 C CD  . GLU B 1 103 ? -11.211 1.046   28.502  1.00 68.57  ? 132 GLU B CD  1 
ATOM   4229 O OE1 . GLU B 1 103 ? -10.098 1.304   29.015  1.00 64.08  ? 132 GLU B OE1 1 
ATOM   4230 O OE2 . GLU B 1 103 ? -12.253 1.662   28.814  1.00 76.35  ? 132 GLU B OE2 1 
ATOM   4231 N N   . GLN B 1 104 ? -8.208  1.426   24.267  1.00 28.46  ? 133 GLN B N   1 
ATOM   4232 C CA  . GLN B 1 104 ? -7.632  1.637   22.944  1.00 32.19  ? 133 GLN B CA  1 
ATOM   4233 C C   . GLN B 1 104 ? -6.308  0.882   22.806  1.00 31.97  ? 133 GLN B C   1 
ATOM   4234 O O   . GLN B 1 104 ? -6.075  0.219   21.784  1.00 37.90  ? 133 GLN B O   1 
ATOM   4235 C CB  . GLN B 1 104 ? -7.506  3.133   22.668  1.00 30.12  ? 133 GLN B CB  1 
ATOM   4236 C CG  . GLN B 1 104 ? -8.852  3.755   22.315  1.00 27.78  ? 133 GLN B CG  1 
ATOM   4237 C CD  . GLN B 1 104 ? -8.894  5.258   22.379  1.00 26.71  ? 133 GLN B CD  1 
ATOM   4238 O OE1 . GLN B 1 104 ? -8.117  5.922   23.071  1.00 26.64  ? 133 GLN B OE1 1 
ATOM   4239 N NE2 . GLN B 1 104 ? -9.847  5.808   21.654  1.00 30.41  ? 133 GLN B NE2 1 
ATOM   4240 N N   . VAL B 1 105 ? -5.460  0.976   23.834  1.00 31.02  ? 134 VAL B N   1 
ATOM   4241 C CA  . VAL B 1 105 ? -4.181  0.281   23.842  1.00 30.53  ? 134 VAL B CA  1 
ATOM   4242 C C   . VAL B 1 105 ? -4.429  -1.223  23.796  1.00 30.96  ? 134 VAL B C   1 
ATOM   4243 O O   . VAL B 1 105 ? -3.753  -1.940  23.087  1.00 29.23  ? 134 VAL B O   1 
ATOM   4244 C CB  . VAL B 1 105 ? -3.382  0.763   25.074  1.00 31.36  ? 134 VAL B CB  1 
ATOM   4245 C CG1 . VAL B 1 105 ? -2.224  -0.146  25.466  1.00 33.06  ? 134 VAL B CG1 1 
ATOM   4246 C CG2 . VAL B 1 105 ? -2.885  2.188   24.866  1.00 31.08  ? 134 VAL B CG2 1 
ATOM   4247 N N   . SER B 1 106 ? -5.448  -1.689  24.520  1.00 32.62  ? 135 SER B N   1 
ATOM   4248 C CA  A SER B 1 106 ? -5.799  -3.097  24.606  0.50 33.32  ? 135 SER B CA  1 
ATOM   4249 C CA  B SER B 1 106 ? -5.777  -3.104  24.601  0.50 31.38  ? 135 SER B CA  1 
ATOM   4250 C C   . SER B 1 106 ? -6.228  -3.626  23.238  1.00 30.19  ? 135 SER B C   1 
ATOM   4251 O O   . SER B 1 106 ? -5.833  -4.708  22.812  1.00 30.97  ? 135 SER B O   1 
ATOM   4252 C CB  A SER B 1 106 ? -6.905  -3.292  25.639  0.50 35.84  ? 135 SER B CB  1 
ATOM   4253 C CB  B SER B 1 106 ? -6.843  -3.356  25.665  0.50 31.71  ? 135 SER B CB  1 
ATOM   4254 O OG  A SER B 1 106 ? -7.560  -4.540  25.461  0.50 38.39  ? 135 SER B OG  1 
ATOM   4255 O OG  B SER B 1 106 ? -6.257  -3.472  26.953  0.50 28.96  ? 135 SER B OG  1 
ATOM   4256 N N   . TRP B 1 107 ? -7.055  -2.850  22.552  1.00 29.83  ? 136 TRP B N   1 
ATOM   4257 C CA  . TRP B 1 107 ? -7.434  -3.151  21.188  1.00 31.03  ? 136 TRP B CA  1 
ATOM   4258 C C   . TRP B 1 107 ? -6.194  -3.208  20.283  1.00 26.94  ? 136 TRP B C   1 
ATOM   4259 O O   . TRP B 1 107 ? -6.104  -4.038  19.392  1.00 28.76  ? 136 TRP B O   1 
ATOM   4260 C CB  . TRP B 1 107 ? -8.450  -2.098  20.711  1.00 30.80  ? 136 TRP B CB  1 
ATOM   4261 C CG  . TRP B 1 107 ? -8.847  -2.267  19.270  1.00 31.13  ? 136 TRP B CG  1 
ATOM   4262 C CD1 . TRP B 1 107 ? -9.891  -2.994  18.772  1.00 33.70  ? 136 TRP B CD1 1 
ATOM   4263 C CD2 . TRP B 1 107 ? -8.153  -1.718  18.130  1.00 30.34  ? 136 TRP B CD2 1 
ATOM   4264 N NE1 . TRP B 1 107 ? -9.907  -2.924  17.404  1.00 33.15  ? 136 TRP B NE1 1 
ATOM   4265 C CE2 . TRP B 1 107 ? -8.849  -2.154  16.978  1.00 33.35  ? 136 TRP B CE2 1 
ATOM   4266 C CE3 . TRP B 1 107 ? -7.037  -0.892  17.980  1.00 30.37  ? 136 TRP B CE3 1 
ATOM   4267 C CZ2 . TRP B 1 107 ? -8.443  -1.802  15.693  1.00 31.86  ? 136 TRP B CZ2 1 
ATOM   4268 C CZ3 . TRP B 1 107 ? -6.631  -0.558  16.707  1.00 33.92  ? 136 TRP B CZ3 1 
ATOM   4269 C CH2 . TRP B 1 107 ? -7.313  -1.021  15.579  1.00 31.93  ? 136 TRP B CH2 1 
ATOM   4270 N N   . LEU B 1 108 ? -5.273  -2.270  20.462  1.00 28.54  ? 137 LEU B N   1 
ATOM   4271 C CA  . LEU B 1 108 ? -4.131  -2.171  19.564  1.00 27.60  ? 137 LEU B CA  1 
ATOM   4272 C C   . LEU B 1 108 ? -3.204  -3.355  19.803  1.00 27.33  ? 137 LEU B C   1 
ATOM   4273 O O   . LEU B 1 108 ? -2.765  -3.983  18.839  1.00 33.46  ? 137 LEU B O   1 
ATOM   4274 C CB  . LEU B 1 108 ? -3.437  -0.823  19.719  1.00 28.60  ? 137 LEU B CB  1 
ATOM   4275 C CG  . LEU B 1 108 ? -2.238  -0.575  18.805  1.00 28.15  ? 137 LEU B CG  1 
ATOM   4276 C CD1 . LEU B 1 108 ? -2.543  -0.991  17.388  1.00 28.73  ? 137 LEU B CD1 1 
ATOM   4277 C CD2 . LEU B 1 108 ? -1.883  0.892   18.904  1.00 26.68  ? 137 LEU B CD2 1 
ATOM   4278 N N   . SER B 1 109 ? -2.986  -3.711  21.074  1.00 27.12  ? 138 SER B N   1 
ATOM   4279 C CA  . SER B 1 109 ? -2.262  -4.920  21.460  1.00 29.18  ? 138 SER B CA  1 
ATOM   4280 C C   . SER B 1 109 ? -2.789  -6.156  20.730  1.00 31.38  ? 138 SER B C   1 
ATOM   4281 O O   . SER B 1 109 ? -2.033  -6.908  20.086  1.00 30.16  ? 138 SER B O   1 
ATOM   4282 C CB  . SER B 1 109 ? -2.297  -5.137  22.962  1.00 32.56  ? 138 SER B CB  1 
ATOM   4283 O OG  . SER B 1 109 ? -1.473  -4.204  23.638  1.00 31.35  ? 138 SER B OG  1 
ATOM   4284 N N   . LYS B 1 110 ? -4.104  -6.382  20.809  1.00 31.37  ? 139 LYS B N   1 
ATOM   4285 C CA  . LYS B 1 110 ? -4.675  -7.545  20.128  1.00 33.20  ? 139 LYS B CA  1 
ATOM   4286 C C   . LYS B 1 110 ? -4.595  -7.408  18.613  1.00 30.34  ? 139 LYS B C   1 
ATOM   4287 O O   . LYS B 1 110 ? -4.516  -8.421  17.931  1.00 37.22  ? 139 LYS B O   1 
ATOM   4288 C CB  . LYS B 1 110 ? -6.104  -7.882  20.564  1.00 39.40  ? 139 LYS B CB  1 
ATOM   4289 C CG  . LYS B 1 110 ? -6.168  -8.242  22.056  1.00 43.50  ? 139 LYS B CG  1 
ATOM   4290 C CD  . LYS B 1 110 ? -7.589  -8.281  22.592  1.00 53.84  ? 139 LYS B CD  1 
ATOM   4291 C CE  . LYS B 1 110 ? -7.617  -8.207  24.079  1.00 59.99  ? 139 LYS B CE  1 
ATOM   4292 N NZ  . LYS B 1 110 ? -8.878  -7.605  24.513  1.00 66.16  ? 139 LYS B NZ  1 
ATOM   4293 N N   . GLU B 1 111 ? -4.619  -6.185  18.055  1.00 33.69  ? 140 GLU B N   1 
ATOM   4294 C CA  . GLU B 1 111 ? -4.507  -6.046  16.604  1.00 31.65  ? 140 GLU B CA  1 
ATOM   4295 C C   . GLU B 1 111 ? -3.152  -6.569  16.128  1.00 30.87  ? 140 GLU B C   1 
ATOM   4296 O O   . GLU B 1 111 ? -3.077  -7.300  15.142  1.00 30.21  ? 140 GLU B O   1 
ATOM   4297 C CB  . GLU B 1 111 ? -4.743  -4.627  16.096  1.00 36.73  ? 140 GLU B CB  1 
ATOM   4298 C CG  . GLU B 1 111 ? -6.214  -4.247  15.937  1.00 41.51  ? 140 GLU B CG  1 
ATOM   4299 C CD  . GLU B 1 111 ? -7.008  -5.066  14.937  1.00 43.41  ? 140 GLU B CD  1 
ATOM   4300 O OE1 . GLU B 1 111 ? -6.773  -4.968  13.703  1.00 48.24  ? 140 GLU B OE1 1 
ATOM   4301 O OE2 . GLU B 1 111 ? -7.828  -5.852  15.439  1.00 47.55  ? 140 GLU B OE2 1 
ATOM   4302 N N   . TRP B 1 112 ? -2.082  -6.251  16.870  1.00 28.80  ? 141 TRP B N   1 
ATOM   4303 C CA  . TRP B 1 112 ? -0.738  -6.631  16.462  1.00 25.72  ? 141 TRP B CA  1 
ATOM   4304 C C   . TRP B 1 112 ? -0.487  -8.130  16.686  1.00 27.95  ? 141 TRP B C   1 
ATOM   4305 O O   . TRP B 1 112 ? 0.196   -8.756  15.898  1.00 30.18  ? 141 TRP B O   1 
ATOM   4306 C CB  . TRP B 1 112 ? 0.292   -5.738  17.190  1.00 23.41  ? 141 TRP B CB  1 
ATOM   4307 C CG  . TRP B 1 112 ? 0.301   -4.301  16.723  1.00 23.11  ? 141 TRP B CG  1 
ATOM   4308 C CD1 . TRP B 1 112 ? -0.322  -3.826  15.610  1.00 23.71  ? 141 TRP B CD1 1 
ATOM   4309 C CD2 . TRP B 1 112 ? 0.986   -3.156  17.286  1.00 22.38  ? 141 TRP B CD2 1 
ATOM   4310 N NE1 . TRP B 1 112 ? -0.073  -2.484  15.441  1.00 22.69  ? 141 TRP B NE1 1 
ATOM   4311 C CE2 . TRP B 1 112 ? 0.711   -2.045  16.457  1.00 22.85  ? 141 TRP B CE2 1 
ATOM   4312 C CE3 . TRP B 1 112 ? 1.768   -2.939  18.413  1.00 26.81  ? 141 TRP B CE3 1 
ATOM   4313 C CZ2 . TRP B 1 112 ? 1.180   -0.764  16.699  1.00 21.53  ? 141 TRP B CZ2 1 
ATOM   4314 C CZ3 . TRP B 1 112 ? 2.258   -1.668  18.659  1.00 24.89  ? 141 TRP B CZ3 1 
ATOM   4315 C CH2 . TRP B 1 112 ? 1.973   -0.603  17.806  1.00 24.67  ? 141 TRP B CH2 1 
ATOM   4316 N N   . ALA B 1 113 ? -1.049  -8.747  17.736  1.00 28.34  ? 142 ALA B N   1 
ATOM   4317 C CA  . ALA B 1 113 ? -0.968  -10.204 17.896  1.00 26.88  ? 142 ALA B CA  1 
ATOM   4318 C C   . ALA B 1 113 ? -1.592  -10.950 16.715  1.00 28.64  ? 142 ALA B C   1 
ATOM   4319 O O   . ALA B 1 113 ? -1.017  -11.922 16.226  1.00 30.44  ? 142 ALA B O   1 
ATOM   4320 C CB  . ALA B 1 113 ? -1.661  -10.625 19.174  1.00 27.32  ? 142 ALA B CB  1 
ATOM   4321 N N   . LYS B 1 114 ? -2.760  -10.484 16.246  1.00 30.05  ? 143 LYS B N   1 
ATOM   4322 C CA  . LYS B 1 114 ? -3.454  -11.108 15.123  1.00 34.66  ? 143 LYS B CA  1 
ATOM   4323 C C   . LYS B 1 114 ? -2.638  -11.041 13.829  1.00 31.35  ? 143 LYS B C   1 
ATOM   4324 O O   . LYS B 1 114 ? -2.783  -11.903 12.982  1.00 31.82  ? 143 LYS B O   1 
ATOM   4325 C CB  . LYS B 1 114 ? -4.744  -10.418 14.665  1.00 40.68  ? 143 LYS B CB  1 
ATOM   4326 C CG  . LYS B 1 114 ? -5.950  -10.393 15.589  1.00 46.33  ? 143 LYS B CG  1 
ATOM   4327 C CD  . LYS B 1 114 ? -7.070  -9.620  14.887  1.00 50.38  ? 143 LYS B CD  1 
ATOM   4328 C CE  . LYS B 1 114 ? -8.204  -9.271  15.810  1.00 58.78  ? 143 LYS B CE  1 
ATOM   4329 N NZ  . LYS B 1 114 ? -9.302  -8.545  15.162  1.00 58.72  ? 143 LYS B NZ  1 
ATOM   4330 N N   . ARG B 1 115 ? -1.792  -10.014 13.646  1.00 32.20  ? 144 ARG B N   1 
ATOM   4331 C CA  . ARG B 1 115 ? -1.148  -9.786  12.351  1.00 29.01  ? 144 ARG B CA  1 
ATOM   4332 C C   . ARG B 1 115 ? 0.302   -10.263 12.348  1.00 28.96  ? 144 ARG B C   1 
ATOM   4333 O O   . ARG B 1 115 ? 0.992   -10.106 11.340  1.00 30.62  ? 144 ARG B O   1 
ATOM   4334 C CB  . ARG B 1 115 ? -1.158  -8.291  12.001  1.00 29.99  ? 144 ARG B CB  1 
ATOM   4335 C CG  . ARG B 1 115 ? -2.522  -7.628  11.980  1.00 29.49  ? 144 ARG B CG  1 
ATOM   4336 C CD  . ARG B 1 115 ? -2.393  -6.137  11.873  1.00 29.79  ? 144 ARG B CD  1 
ATOM   4337 N NE  . ARG B 1 115 ? -3.700  -5.485  11.752  1.00 29.90  ? 144 ARG B NE  1 
ATOM   4338 C CZ  . ARG B 1 115 ? -4.180  -4.841  10.703  1.00 29.40  ? 144 ARG B CZ  1 
ATOM   4339 N NH1 . ARG B 1 115 ? -3.515  -4.838  9.573   1.00 31.09  ? 144 ARG B NH1 1 
ATOM   4340 N NH2 . ARG B 1 115 ? -5.347  -4.206  10.770  1.00 33.75  ? 144 ARG B NH2 1 
ATOM   4341 N N   . ALA B 1 116 ? 0.723   -10.923 13.436  1.00 28.00  ? 145 ALA B N   1 
ATOM   4342 C CA  . ALA B 1 116 ? 2.121   -11.242 13.710  1.00 33.56  ? 145 ALA B CA  1 
ATOM   4343 C C   . ALA B 1 116 ? 2.762   -12.319 12.815  1.00 37.74  ? 145 ALA B C   1 
ATOM   4344 O O   . ALA B 1 116 ? 3.984   -12.331 12.699  1.00 39.74  ? 145 ALA B O   1 
ATOM   4345 C CB  . ALA B 1 116 ? 2.232   -11.635 15.160  1.00 35.08  ? 145 ALA B CB  1 
ATOM   4346 N N   . ALA B 1 117 ? 1.985   -13.186 12.156  1.00 36.02  ? 146 ALA B N   1 
ATOM   4347 C CA  . ALA B 1 117 ? 2.500   -14.334 11.413  1.00 33.50  ? 146 ALA B CA  1 
ATOM   4348 C C   . ALA B 1 117 ? 3.476   -13.961 10.297  1.00 32.77  ? 146 ALA B C   1 
ATOM   4349 O O   . ALA B 1 117 ? 3.189   -13.098 9.473   1.00 31.99  ? 146 ALA B O   1 
ATOM   4350 C CB  . ALA B 1 117 ? 1.354   -15.133 10.800  1.00 35.85  ? 146 ALA B CB  1 
ATOM   4351 N N   . LEU B 1 118 ? 4.583   -14.711 10.228  1.00 31.11  ? 147 LEU B N   1 
ATOM   4352 C CA  . LEU B 1 118 ? 5.570   -14.564 9.176   1.00 35.17  ? 147 LEU B CA  1 
ATOM   4353 C C   . LEU B 1 118 ? 5.266   -15.528 8.031   1.00 37.24  ? 147 LEU B C   1 
ATOM   4354 O O   . LEU B 1 118 ? 4.967   -16.694 8.266   1.00 36.18  ? 147 LEU B O   1 
ATOM   4355 C CB  . LEU B 1 118 ? 6.971   -14.803 9.728   1.00 35.62  ? 147 LEU B CB  1 
ATOM   4356 C CG  . LEU B 1 118 ? 7.426   -13.901 10.875  1.00 34.36  ? 147 LEU B CG  1 
ATOM   4357 C CD1 . LEU B 1 118 ? 8.881   -14.204 11.227  1.00 31.07  ? 147 LEU B CD1 1 
ATOM   4358 C CD2 . LEU B 1 118 ? 7.236   -12.430 10.498  1.00 33.07  ? 147 LEU B CD2 1 
ATOM   4359 N N   . PRO B 1 119 ? 5.392   -15.086 6.758   1.00 35.54  ? 148 PRO B N   1 
ATOM   4360 C CA  . PRO B 1 119 ? 5.418   -16.020 5.637   1.00 35.72  ? 148 PRO B CA  1 
ATOM   4361 C C   . PRO B 1 119 ? 6.639   -16.926 5.714   1.00 35.56  ? 148 PRO B C   1 
ATOM   4362 O O   . PRO B 1 119 ? 7.750   -16.505 6.081   1.00 32.27  ? 148 PRO B O   1 
ATOM   4363 C CB  . PRO B 1 119 ? 5.399   -15.176 4.369   1.00 34.20  ? 148 PRO B CB  1 
ATOM   4364 C CG  . PRO B 1 119 ? 5.815   -13.774 4.829   1.00 33.35  ? 148 PRO B CG  1 
ATOM   4365 C CD  . PRO B 1 119 ? 5.549   -13.684 6.340   1.00 34.29  ? 148 PRO B CD  1 
ATOM   4366 N N   . SER B 1 120 ? 6.405   -18.193 5.344   1.00 39.37  ? 149 SER B N   1 
ATOM   4367 C CA  . SER B 1 120 ? 7.411   -19.233 5.490   1.00 37.67  ? 149 SER B CA  1 
ATOM   4368 C C   . SER B 1 120 ? 8.666   -18.831 4.714   1.00 28.89  ? 149 SER B C   1 
ATOM   4369 O O   . SER B 1 120 ? 9.769   -19.160 5.139   1.00 30.97  ? 149 SER B O   1 
ATOM   4370 C CB  . SER B 1 120 ? 6.882   -20.604 5.082   1.00 39.47  ? 149 SER B CB  1 
ATOM   4371 O OG  . SER B 1 120 ? 6.934   -20.776 3.672   1.00 47.19  ? 149 SER B OG  1 
ATOM   4372 N N   . HIS B 1 121 ? 8.529   -18.063 3.627   1.00 27.03  ? 150 HIS B N   1 
ATOM   4373 C CA  . HIS B 1 121 ? 9.728   -17.773 2.845   1.00 30.12  ? 150 HIS B CA  1 
ATOM   4374 C C   . HIS B 1 121 ? 10.679  -16.873 3.650   1.00 29.43  ? 150 HIS B C   1 
ATOM   4375 O O   . HIS B 1 121 ? 11.903  -16.961 3.509   1.00 27.35  ? 150 HIS B O   1 
ATOM   4376 C CB  . HIS B 1 121 ? 9.410   -17.238 1.442   1.00 27.15  ? 150 HIS B CB  1 
ATOM   4377 C CG  . HIS B 1 121 ? 9.077   -15.789 1.388   1.00 26.17  ? 150 HIS B CG  1 
ATOM   4378 N ND1 . HIS B 1 121 ? 7.792   -15.316 1.577   1.00 26.03  ? 150 HIS B ND1 1 
ATOM   4379 C CD2 . HIS B 1 121 ? 9.846   -14.716 1.186   1.00 26.15  ? 150 HIS B CD2 1 
ATOM   4380 C CE1 . HIS B 1 121 ? 7.786   -14.000 1.478   1.00 28.65  ? 150 HIS B CE1 1 
ATOM   4381 N NE2 . HIS B 1 121 ? 9.026   -13.607 1.224   1.00 30.63  ? 150 HIS B NE2 1 
ATOM   4382 N N   . VAL B 1 122 ? 10.120  -16.001 4.489   1.00 27.56  ? 151 VAL B N   1 
ATOM   4383 C CA  . VAL B 1 122 ? 10.955  -15.170 5.346   1.00 29.17  ? 151 VAL B CA  1 
ATOM   4384 C C   . VAL B 1 122 ? 11.592  -16.021 6.446   1.00 29.12  ? 151 VAL B C   1 
ATOM   4385 O O   . VAL B 1 122 ? 12.799  -15.953 6.666   1.00 30.32  ? 151 VAL B O   1 
ATOM   4386 C CB  . VAL B 1 122 ? 10.128  -13.989 5.878   1.00 25.59  ? 151 VAL B CB  1 
ATOM   4387 C CG1 . VAL B 1 122 ? 10.839  -13.254 7.008   1.00 24.62  ? 151 VAL B CG1 1 
ATOM   4388 C CG2 . VAL B 1 122 ? 9.765   -13.065 4.728   1.00 24.63  ? 151 VAL B CG2 1 
ATOM   4389 N N   . VAL B 1 123 ? 10.806  -16.890 7.074   1.00 31.90  ? 152 VAL B N   1 
ATOM   4390 C CA  . VAL B 1 123 ? 11.309  -17.841 8.059   1.00 30.67  ? 152 VAL B CA  1 
ATOM   4391 C C   . VAL B 1 123 ? 12.525  -18.617 7.512   1.00 29.47  ? 152 VAL B C   1 
ATOM   4392 O O   . VAL B 1 123 ? 13.588  -18.692 8.150   1.00 26.31  ? 152 VAL B O   1 
ATOM   4393 C CB  . VAL B 1 123 ? 10.161  -18.796 8.434   1.00 30.59  ? 152 VAL B CB  1 
ATOM   4394 C CG1 . VAL B 1 123 ? 10.658  -19.925 9.334   1.00 30.62  ? 152 VAL B CG1 1 
ATOM   4395 C CG2 . VAL B 1 123 ? 8.974   -18.060 9.049   1.00 28.44  ? 152 VAL B CG2 1 
ATOM   4396 N N   . THR B 1 124 ? 12.356  -19.170 6.310   1.00 28.33  ? 153 THR B N   1 
ATOM   4397 C CA  . THR B 1 124 ? 13.368  -19.965 5.626   1.00 32.48  ? 153 THR B CA  1 
ATOM   4398 C C   . THR B 1 124 ? 14.641  -19.154 5.400   1.00 32.08  ? 153 THR B C   1 
ATOM   4399 O O   . THR B 1 124 ? 15.763  -19.627 5.611   1.00 31.12  ? 153 THR B O   1 
ATOM   4400 C CB  . THR B 1 124 ? 12.796  -20.397 4.273   1.00 34.34  ? 153 THR B CB  1 
ATOM   4401 O OG1 . THR B 1 124 ? 11.874  -21.382 4.695   1.00 38.55  ? 153 THR B OG1 1 
ATOM   4402 C CG2 . THR B 1 124 ? 13.829  -20.946 3.299   1.00 37.38  ? 153 THR B CG2 1 
ATOM   4403 N N   . MET B 1 125 ? 14.439  -17.949 4.860   1.00 30.54  ? 154 MET B N   1 
ATOM   4404 C CA  . MET B 1 125 ? 15.522  -17.030 4.585   1.00 29.22  ? 154 MET B CA  1 
ATOM   4405 C C   . MET B 1 125 ? 16.306  -16.729 5.865   1.00 26.71  ? 154 MET B C   1 
ATOM   4406 O O   . MET B 1 125 ? 17.537  -16.736 5.859   1.00 30.03  ? 154 MET B O   1 
ATOM   4407 C CB  . MET B 1 125 ? 14.877  -15.770 4.015   1.00 32.45  ? 154 MET B CB  1 
ATOM   4408 C CG  . MET B 1 125 ? 15.813  -14.712 3.531   1.00 37.49  ? 154 MET B CG  1 
ATOM   4409 S SD  . MET B 1 125 ? 14.811  -13.205 3.498   1.00 44.66  ? 154 MET B SD  1 
ATOM   4410 C CE  . MET B 1 125 ? 16.042  -12.483 2.420   1.00 42.32  ? 154 MET B CE  1 
ATOM   4411 N N   . LEU B 1 126 ? 15.610  -16.448 6.975   1.00 25.11  ? 155 LEU B N   1 
ATOM   4412 C CA  . LEU B 1 126 ? 16.286  -16.130 8.226   1.00 23.52  ? 155 LEU B CA  1 
ATOM   4413 C C   . LEU B 1 126 ? 17.016  -17.345 8.780   1.00 28.05  ? 155 LEU B C   1 
ATOM   4414 O O   . LEU B 1 126 ? 18.147  -17.222 9.265   1.00 28.97  ? 155 LEU B O   1 
ATOM   4415 C CB  . LEU B 1 126 ? 15.315  -15.617 9.269   1.00 25.32  ? 155 LEU B CB  1 
ATOM   4416 C CG  . LEU B 1 126 ? 14.805  -14.193 9.084   1.00 27.51  ? 155 LEU B CG  1 
ATOM   4417 C CD1 . LEU B 1 126 ? 13.609  -14.000 9.999   1.00 25.92  ? 155 LEU B CD1 1 
ATOM   4418 C CD2 . LEU B 1 126 ? 15.970  -13.223 9.394   1.00 27.68  ? 155 LEU B CD2 1 
ATOM   4419 N N   . ASP B 1 127 ? 16.332  -18.498 8.743   1.00 28.75  ? 156 ASP B N   1 
ATOM   4420 C CA  . ASP B 1 127 ? 16.925  -19.763 9.159   1.00 31.42  ? 156 ASP B CA  1 
ATOM   4421 C C   . ASP B 1 127 ? 18.170  -20.076 8.322   1.00 28.41  ? 156 ASP B C   1 
ATOM   4422 O O   . ASP B 1 127 ? 19.077  -20.737 8.804   1.00 34.28  ? 156 ASP B O   1 
ATOM   4423 C CB  . ASP B 1 127 ? 15.902  -20.896 9.151   1.00 32.08  ? 156 ASP B CB  1 
ATOM   4424 C CG  . ASP B 1 127 ? 14.820  -20.880 10.233  1.00 38.99  ? 156 ASP B CG  1 
ATOM   4425 O OD1 . ASP B 1 127 ? 14.896  -20.065 11.198  1.00 38.63  ? 156 ASP B OD1 1 
ATOM   4426 O OD2 . ASP B 1 127 ? 13.893  -21.718 10.147  1.00 39.04  ? 156 ASP B OD2 1 
ATOM   4427 N N   . ASN B 1 128 ? 18.284  -19.558 7.103   1.00 30.29  ? 157 ASN B N   1 
ATOM   4428 C CA  . ASN B 1 128 ? 19.415  -19.919 6.265   1.00 31.70  ? 157 ASN B CA  1 
ATOM   4429 C C   . ASN B 1 128 ? 20.596  -18.944 6.365   1.00 30.76  ? 157 ASN B C   1 
ATOM   4430 O O   . ASN B 1 128 ? 21.689  -19.312 5.968   1.00 28.11  ? 157 ASN B O   1 
ATOM   4431 C CB  . ASN B 1 128 ? 19.018  -20.146 4.819   1.00 33.78  ? 157 ASN B CB  1 
ATOM   4432 C CG  . ASN B 1 128 ? 18.329  -21.482 4.595   1.00 40.58  ? 157 ASN B CG  1 
ATOM   4433 O OD1 . ASN B 1 128 ? 18.748  -22.510 5.136   1.00 37.49  ? 157 ASN B OD1 1 
ATOM   4434 N ND2 . ASN B 1 128 ? 17.254  -21.480 3.818   1.00 39.68  ? 157 ASN B ND2 1 
ATOM   4435 N N   . PHE B 1 129 ? 20.398  -17.719 6.883   1.00 28.38  ? 158 PHE B N   1 
ATOM   4436 C CA  . PHE B 1 129 ? 21.463  -16.746 7.035   1.00 27.88  ? 158 PHE B CA  1 
ATOM   4437 C C   . PHE B 1 129 ? 22.597  -17.271 7.922   1.00 28.67  ? 158 PHE B C   1 
ATOM   4438 O O   . PHE B 1 129 ? 22.375  -17.775 9.017   1.00 25.99  ? 158 PHE B O   1 
ATOM   4439 C CB  . PHE B 1 129 ? 20.941  -15.435 7.635   1.00 29.30  ? 158 PHE B CB  1 
ATOM   4440 C CG  . PHE B 1 129 ? 20.096  -14.535 6.738   1.00 26.71  ? 158 PHE B CG  1 
ATOM   4441 C CD1 . PHE B 1 129 ? 20.254  -14.523 5.356   1.00 30.13  ? 158 PHE B CD1 1 
ATOM   4442 C CD2 . PHE B 1 129 ? 19.213  -13.633 7.305   1.00 26.35  ? 158 PHE B CD2 1 
ATOM   4443 C CE1 . PHE B 1 129 ? 19.534  -13.635 4.566   1.00 29.38  ? 158 PHE B CE1 1 
ATOM   4444 C CE2 . PHE B 1 129 ? 18.500  -12.748 6.524   1.00 27.73  ? 158 PHE B CE2 1 
ATOM   4445 C CZ  . PHE B 1 129 ? 18.637  -12.769 5.156   1.00 28.71  ? 158 PHE B CZ  1 
ATOM   4446 N N   . PRO B 1 130 ? 23.868  -17.035 7.532   1.00 29.13  ? 159 PRO B N   1 
ATOM   4447 C CA  . PRO B 1 130 ? 25.021  -17.385 8.360   1.00 27.26  ? 159 PRO B CA  1 
ATOM   4448 C C   . PRO B 1 130 ? 25.227  -16.414 9.514   1.00 28.63  ? 159 PRO B C   1 
ATOM   4449 O O   . PRO B 1 130 ? 24.677  -15.302 9.482   1.00 27.21  ? 159 PRO B O   1 
ATOM   4450 C CB  . PRO B 1 130 ? 26.178  -17.296 7.342   1.00 24.95  ? 159 PRO B CB  1 
ATOM   4451 C CG  . PRO B 1 130 ? 25.793  -16.132 6.484   1.00 25.41  ? 159 PRO B CG  1 
ATOM   4452 C CD  . PRO B 1 130 ? 24.264  -16.268 6.337   1.00 26.89  ? 159 PRO B CD  1 
ATOM   4453 N N   . THR B 1 131 ? 26.066  -16.838 10.491  1.00 28.23  ? 160 THR B N   1 
ATOM   4454 C CA  . THR B 1 131 ? 26.319  -16.077 11.704  1.00 28.62  ? 160 THR B CA  1 
ATOM   4455 C C   . THR B 1 131 ? 27.211  -14.880 11.422  1.00 27.72  ? 160 THR B C   1 
ATOM   4456 O O   . THR B 1 131 ? 27.271  -14.002 12.273  1.00 25.62  ? 160 THR B O   1 
ATOM   4457 C CB  . THR B 1 131 ? 26.906  -16.937 12.839  1.00 32.25  ? 160 THR B CB  1 
ATOM   4458 O OG1 . THR B 1 131 ? 28.216  -17.390 12.512  1.00 34.37  ? 160 THR B OG1 1 
ATOM   4459 C CG2 . THR B 1 131 ? 25.996  -18.098 13.186  1.00 32.99  ? 160 THR B CG2 1 
ATOM   4460 N N   . ASN B 1 132 ? 27.886  -14.823 10.259  1.00 25.47  ? 161 ASN B N   1 
ATOM   4461 C CA  . ASN B 1 132 ? 28.737  -13.688 9.964   1.00 28.60  ? 161 ASN B CA  1 
ATOM   4462 C C   . ASN B 1 132 ? 27.914  -12.566 9.309   1.00 25.91  ? 161 ASN B C   1 
ATOM   4463 O O   . ASN B 1 132 ? 28.477  -11.574 8.892   1.00 33.16  ? 161 ASN B O   1 
ATOM   4464 C CB  . ASN B 1 132 ? 29.964  -14.135 9.163   1.00 31.71  ? 161 ASN B CB  1 
ATOM   4465 C CG  . ASN B 1 132 ? 29.636  -14.690 7.789   1.00 32.64  ? 161 ASN B CG  1 
ATOM   4466 O OD1 . ASN B 1 132 ? 28.705  -15.476 7.633   1.00 37.22  ? 161 ASN B OD1 1 
ATOM   4467 N ND2 . ASN B 1 132 ? 30.365  -14.299 6.762   1.00 40.80  ? 161 ASN B ND2 1 
ATOM   4468 N N   . LEU B 1 133 ? 26.636  -12.790 9.022   1.00 25.09  ? 162 LEU B N   1 
ATOM   4469 C CA  . LEU B 1 133 ? 25.796  -11.742 8.445   1.00 22.48  ? 162 LEU B CA  1 
ATOM   4470 C C   . LEU B 1 133 ? 25.189  -10.977 9.608   1.00 23.54  ? 162 LEU B C   1 
ATOM   4471 O O   . LEU B 1 133 ? 24.475  -11.567 10.398  1.00 22.19  ? 162 LEU B O   1 
ATOM   4472 C CB  . LEU B 1 133 ? 24.696  -12.294 7.553   1.00 22.50  ? 162 LEU B CB  1 
ATOM   4473 C CG  . LEU B 1 133 ? 23.799  -11.241 6.888   1.00 22.08  ? 162 LEU B CG  1 
ATOM   4474 C CD1 . LEU B 1 133 ? 24.576  -10.307 6.001   1.00 20.44  ? 162 LEU B CD1 1 
ATOM   4475 C CD2 . LEU B 1 133 ? 22.705  -11.896 6.115   1.00 24.27  ? 162 LEU B CD2 1 
ATOM   4476 N N   . HIS B 1 134 ? 25.577  -9.695  9.734   1.00 24.16  ? 163 HIS B N   1 
ATOM   4477 C CA  . HIS B 1 134 ? 25.211  -8.839  10.851  1.00 25.21  ? 163 HIS B CA  1 
ATOM   4478 C C   . HIS B 1 134 ? 23.698  -8.866  11.077  1.00 24.90  ? 163 HIS B C   1 
ATOM   4479 O O   . HIS B 1 134 ? 22.938  -8.767  10.116  1.00 21.23  ? 163 HIS B O   1 
ATOM   4480 C CB  . HIS B 1 134 ? 25.691  -7.410  10.547  1.00 25.47  ? 163 HIS B CB  1 
ATOM   4481 C CG  . HIS B 1 134 ? 25.651  -6.503  11.723  1.00 29.93  ? 163 HIS B CG  1 
ATOM   4482 N ND1 . HIS B 1 134 ? 24.499  -5.861  12.150  1.00 32.69  ? 163 HIS B ND1 1 
ATOM   4483 C CD2 . HIS B 1 134 ? 26.626  -6.147  12.582  1.00 32.29  ? 163 HIS B CD2 1 
ATOM   4484 C CE1 . HIS B 1 134 ? 24.760  -5.147  13.236  1.00 33.43  ? 163 HIS B CE1 1 
ATOM   4485 N NE2 . HIS B 1 134 ? 26.060  -5.288  13.517  1.00 33.22  ? 163 HIS B NE2 1 
ATOM   4486 N N   . PRO B 1 135 ? 23.255  -8.866  12.354  1.00 21.57  ? 164 PRO B N   1 
ATOM   4487 C CA  . PRO B 1 135 ? 21.841  -8.839  12.705  1.00 22.89  ? 164 PRO B CA  1 
ATOM   4488 C C   . PRO B 1 135 ? 21.026  -7.751  12.018  1.00 20.04  ? 164 PRO B C   1 
ATOM   4489 O O   . PRO B 1 135 ? 19.913  -8.038  11.663  1.00 19.98  ? 164 PRO B O   1 
ATOM   4490 C CB  . PRO B 1 135 ? 21.855  -8.656  14.243  1.00 21.48  ? 164 PRO B CB  1 
ATOM   4491 C CG  . PRO B 1 135 ? 23.187  -9.092  14.689  1.00 22.50  ? 164 PRO B CG  1 
ATOM   4492 C CD  . PRO B 1 135 ? 24.121  -8.808  13.555  1.00 22.78  ? 164 PRO B CD  1 
ATOM   4493 N N   . MET B 1 136 ? 21.584  -6.552  11.811  1.00 18.84  ? 165 MET B N   1 
ATOM   4494 C CA  . MET B 1 136 ? 20.882  -5.440  11.135  1.00 20.34  ? 165 MET B CA  1 
ATOM   4495 C C   . MET B 1 136 ? 20.708  -5.678  9.627   1.00 17.69  ? 165 MET B C   1 
ATOM   4496 O O   . MET B 1 136 ? 19.721  -5.278  9.038   1.00 16.33  ? 165 MET B O   1 
ATOM   4497 C CB  . MET B 1 136 ? 21.639  -4.126  11.388  1.00 21.32  ? 165 MET B CB  1 
ATOM   4498 C CG  . MET B 1 136 ? 21.356  -3.531  12.779  1.00 21.59  ? 165 MET B CG  1 
ATOM   4499 S SD  . MET B 1 136 ? 19.643  -3.012  13.003  1.00 24.41  ? 165 MET B SD  1 
ATOM   4500 C CE  . MET B 1 136 ? 19.678  -1.742  11.721  1.00 23.08  ? 165 MET B CE  1 
ATOM   4501 N N   . SER B 1 137 ? 21.645  -6.397  9.013   1.00 18.93  ? 166 SER B N   1 
ATOM   4502 C CA  . SER B 1 137 ? 21.558  -6.810  7.633   1.00 21.91  ? 166 SER B CA  1 
ATOM   4503 C C   . SER B 1 137 ? 20.476  -7.885  7.493   1.00 19.80  ? 166 SER B C   1 
ATOM   4504 O O   . SER B 1 137 ? 19.695  -7.853  6.547   1.00 20.37  ? 166 SER B O   1 
ATOM   4505 C CB  . SER B 1 137 ? 22.931  -7.288  7.106   1.00 22.59  ? 166 SER B CB  1 
ATOM   4506 O OG  . SER B 1 137 ? 23.978  -6.384  7.468   1.00 24.35  ? 166 SER B OG  1 
ATOM   4507 N N   . GLN B 1 138 ? 20.423  -8.824  8.442   1.00 19.58  ? 167 GLN B N   1 
ATOM   4508 C CA  . GLN B 1 138 ? 19.355  -9.802  8.470   1.00 19.75  ? 167 GLN B CA  1 
ATOM   4509 C C   . GLN B 1 138 ? 17.987  -9.133  8.588   1.00 18.04  ? 167 GLN B C   1 
ATOM   4510 O O   . GLN B 1 138 ? 17.066  -9.498  7.873   1.00 20.28  ? 167 GLN B O   1 
ATOM   4511 C CB  . GLN B 1 138 ? 19.562  -10.773 9.623   1.00 19.29  ? 167 GLN B CB  1 
ATOM   4512 C CG  . GLN B 1 138 ? 20.854  -11.552 9.504   1.00 21.48  ? 167 GLN B CG  1 
ATOM   4513 C CD  . GLN B 1 138 ? 20.827  -12.818 10.322  1.00 21.73  ? 167 GLN B CD  1 
ATOM   4514 O OE1 . GLN B 1 138 ? 19.757  -13.366 10.637  1.00 24.88  ? 167 GLN B OE1 1 
ATOM   4515 N NE2 . GLN B 1 138 ? 22.014  -13.328 10.580  1.00 23.96  ? 167 GLN B NE2 1 
ATOM   4516 N N   . LEU B 1 139 ? 17.873  -8.162  9.497   1.00 17.93  ? 168 LEU B N   1 
ATOM   4517 C CA  . LEU B 1 139 ? 16.640  -7.412  9.688   1.00 18.52  ? 168 LEU B CA  1 
ATOM   4518 C C   . LEU B 1 139 ? 16.185  -6.699  8.404   1.00 19.12  ? 168 LEU B C   1 
ATOM   4519 O O   . LEU B 1 139 ? 15.049  -6.836  7.973   1.00 18.07  ? 168 LEU B O   1 
ATOM   4520 C CB  . LEU B 1 139 ? 16.830  -6.445  10.844  1.00 22.51  ? 168 LEU B CB  1 
ATOM   4521 C CG  . LEU B 1 139 ? 15.596  -5.602  11.169  1.00 25.15  ? 168 LEU B CG  1 
ATOM   4522 C CD1 . LEU B 1 139 ? 14.512  -6.465  11.744  1.00 24.72  ? 168 LEU B CD1 1 
ATOM   4523 C CD2 . LEU B 1 139 ? 15.892  -4.436  12.081  1.00 26.80  ? 168 LEU B CD2 1 
ATOM   4524 N N   . SER B 1 140 ? 17.087  -5.985  7.754   1.00 18.98  ? 169 SER B N   1 
ATOM   4525 C CA  . SER B 1 140 ? 16.748  -5.217  6.574   1.00 19.53  ? 169 SER B CA  1 
ATOM   4526 C C   . SER B 1 140 ? 16.354  -6.145  5.414   1.00 20.07  ? 169 SER B C   1 
ATOM   4527 O O   . SER B 1 140 ? 15.375  -5.891  4.722   1.00 19.48  ? 169 SER B O   1 
ATOM   4528 C CB  . SER B 1 140 ? 17.890  -4.308  6.187   1.00 18.63  ? 169 SER B CB  1 
ATOM   4529 O OG  . SER B 1 140 ? 17.510  -3.601  5.008   1.00 23.77  ? 169 SER B OG  1 
ATOM   4530 N N   . ALA B 1 141 ? 17.104  -7.236  5.220   1.00 20.42  ? 170 ALA B N   1 
ATOM   4531 C CA  . ALA B 1 141 ? 16.813  -8.218  4.182   1.00 17.73  ? 170 ALA B CA  1 
ATOM   4532 C C   . ALA B 1 141 ? 15.467  -8.914  4.359   1.00 18.51  ? 170 ALA B C   1 
ATOM   4533 O O   . ALA B 1 141 ? 14.743  -9.078  3.381   1.00 19.37  ? 170 ALA B O   1 
ATOM   4534 C CB  . ALA B 1 141 ? 17.909  -9.258  4.098   1.00 17.51  ? 170 ALA B CB  1 
ATOM   4535 N N   . ALA B 1 142 ? 15.123  -9.292  5.595   1.00 19.28  ? 171 ALA B N   1 
ATOM   4536 C CA  . ALA B 1 142 ? 13.861  -9.929  5.917   1.00 19.49  ? 171 ALA B CA  1 
ATOM   4537 C C   . ALA B 1 142 ? 12.679  -8.978  5.735   1.00 22.64  ? 171 ALA B C   1 
ATOM   4538 O O   . ALA B 1 142 ? 11.638  -9.379  5.245   1.00 22.22  ? 171 ALA B O   1 
ATOM   4539 C CB  . ALA B 1 142 ? 13.909  -10.475 7.327   1.00 20.47  ? 171 ALA B CB  1 
ATOM   4540 N N   . VAL B 1 143 ? 12.807  -7.710  6.148   1.00 20.99  ? 172 VAL B N   1 
ATOM   4541 C CA  . VAL B 1 143 ? 11.709  -6.775  5.955   1.00 19.77  ? 172 VAL B CA  1 
ATOM   4542 C C   . VAL B 1 143 ? 11.467  -6.529  4.459   1.00 19.13  ? 172 VAL B C   1 
ATOM   4543 O O   . VAL B 1 143 ? 10.329  -6.515  3.988   1.00 21.59  ? 172 VAL B O   1 
ATOM   4544 C CB  . VAL B 1 143 ? 11.988  -5.503  6.768   1.00 21.61  ? 172 VAL B CB  1 
ATOM   4545 C CG1 . VAL B 1 143 ? 11.003  -4.399  6.433   1.00 22.27  ? 172 VAL B CG1 1 
ATOM   4546 C CG2 . VAL B 1 143 ? 11.964  -5.778  8.265   1.00 21.04  ? 172 VAL B CG2 1 
ATOM   4547 N N   . THR B 1 144 ? 12.535  -6.377  3.690   1.00 19.39  ? 173 THR B N   1 
ATOM   4548 C CA  . THR B 1 144 ? 12.411  -6.228  2.244   1.00 20.86  ? 173 THR B CA  1 
ATOM   4549 C C   . THR B 1 144 ? 11.651  -7.413  1.663   1.00 21.32  ? 173 THR B C   1 
ATOM   4550 O O   . THR B 1 144 ? 10.777  -7.206  0.814   1.00 21.63  ? 173 THR B O   1 
ATOM   4551 C CB  . THR B 1 144 ? 13.779  -6.149  1.585   1.00 19.50  ? 173 THR B CB  1 
ATOM   4552 O OG1 . THR B 1 144 ? 14.368  -4.946  2.085   1.00 21.97  ? 173 THR B OG1 1 
ATOM   4553 C CG2 . THR B 1 144 ? 13.686  -6.099  0.074   1.00 18.53  ? 173 THR B CG2 1 
ATOM   4554 N N   . ALA B 1 145 ? 12.046  -8.622  2.088   1.00 20.70  ? 174 ALA B N   1 
ATOM   4555 C CA  . ALA B 1 145 ? 11.425  -9.855  1.617   1.00 20.31  ? 174 ALA B CA  1 
ATOM   4556 C C   . ALA B 1 145 ? 9.950   -9.930  2.010   1.00 21.54  ? 174 ALA B C   1 
ATOM   4557 O O   . ALA B 1 145 ? 9.127   -10.561 1.324   1.00 23.83  ? 174 ALA B O   1 
ATOM   4558 C CB  . ALA B 1 145 ? 12.201  -11.056 2.137   1.00 21.14  ? 174 ALA B CB  1 
ATOM   4559 N N   . LEU B 1 146 ? 9.605   -9.311  3.135   1.00 21.83  ? 175 LEU B N   1 
ATOM   4560 C CA  . LEU B 1 146 ? 8.224   -9.276  3.579   1.00 24.73  ? 175 LEU B CA  1 
ATOM   4561 C C   . LEU B 1 146 ? 7.351   -8.467  2.623   1.00 22.88  ? 175 LEU B C   1 
ATOM   4562 O O   . LEU B 1 146 ? 6.137   -8.544  2.699   1.00 28.64  ? 175 LEU B O   1 
ATOM   4563 C CB  . LEU B 1 146 ? 8.093   -8.718  4.999   1.00 22.59  ? 175 LEU B CB  1 
ATOM   4564 C CG  . LEU B 1 146 ? 8.392   -9.651  6.166   1.00 25.15  ? 175 LEU B CG  1 
ATOM   4565 C CD1 . LEU B 1 146 ? 8.454   -8.837  7.426   1.00 25.78  ? 175 LEU B CD1 1 
ATOM   4566 C CD2 . LEU B 1 146 ? 7.348   -10.744 6.363   1.00 27.26  ? 175 LEU B CD2 1 
ATOM   4567 N N   . ASN B 1 147 ? 7.921   -7.660  1.741   1.00 23.27  ? 176 ASN B N   1 
ATOM   4568 C CA  . ASN B 1 147 ? 7.086   -6.815  0.912   1.00 22.72  ? 176 ASN B CA  1 
ATOM   4569 C C   . ASN B 1 147 ? 6.290   -7.676  -0.077  1.00 21.95  ? 176 ASN B C   1 
ATOM   4570 O O   . ASN B 1 147 ? 5.466   -7.146  -0.782  1.00 23.51  ? 176 ASN B O   1 
ATOM   4571 C CB  . ASN B 1 147 ? 7.867   -5.684  0.242   1.00 21.75  ? 176 ASN B CB  1 
ATOM   4572 C CG  . ASN B 1 147 ? 7.909   -5.788  -1.258  1.00 27.07  ? 176 ASN B CG  1 
ATOM   4573 O OD1 . ASN B 1 147 ? 8.240   -6.855  -1.793  1.00 29.84  ? 176 ASN B OD1 1 
ATOM   4574 N ND2 . ASN B 1 147 ? 7.559   -4.713  -1.968  1.00 29.64  ? 176 ASN B ND2 1 
ATOM   4575 N N   . SER B 1 148 ? 6.539   -8.992  -0.148  1.00 24.57  ? 177 SER B N   1 
ATOM   4576 C CA  . SER B 1 148 ? 5.642   -9.866  -0.887  1.00 25.68  ? 177 SER B CA  1 
ATOM   4577 C C   . SER B 1 148 ? 4.236   -9.776  -0.303  1.00 29.27  ? 177 SER B C   1 
ATOM   4578 O O   . SER B 1 148 ? 3.291   -10.134 -0.958  1.00 33.31  ? 177 SER B O   1 
ATOM   4579 C CB  . SER B 1 148 ? 6.114   -11.301 -0.880  1.00 26.23  ? 177 SER B CB  1 
ATOM   4580 O OG  . SER B 1 148 ? 6.265   -11.776 0.442   1.00 26.17  ? 177 SER B OG  1 
ATOM   4581 N N   . GLU B 1 149 ? 4.109   -9.288  0.930   1.00 27.85  ? 178 GLU B N   1 
ATOM   4582 C CA  . GLU B 1 149 ? 2.821   -9.229  1.583   1.00 32.97  ? 178 GLU B CA  1 
ATOM   4583 C C   . GLU B 1 149 ? 2.207   -7.843  1.451   1.00 31.51  ? 178 GLU B C   1 
ATOM   4584 O O   . GLU B 1 149 ? 1.233   -7.563  2.140   1.00 31.51  ? 178 GLU B O   1 
ATOM   4585 C CB  . GLU B 1 149 ? 3.131   -9.585  3.030   1.00 38.62  ? 178 GLU B CB  1 
ATOM   4586 C CG  . GLU B 1 149 ? 3.899   -10.905 3.136   1.00 46.58  ? 178 GLU B CG  1 
ATOM   4587 C CD  . GLU B 1 149 ? 3.375   -12.020 2.234   1.00 49.59  ? 178 GLU B CD  1 
ATOM   4588 O OE1 . GLU B 1 149 ? 2.192   -12.354 2.424   1.00 66.68  ? 178 GLU B OE1 1 
ATOM   4589 O OE2 . GLU B 1 149 ? 4.105   -12.562 1.366   1.00 55.06  ? 178 GLU B OE2 1 
ATOM   4590 N N   . SER B 1 150 ? 2.780   -6.958  0.613   1.00 26.79  ? 179 SER B N   1 
ATOM   4591 C CA  . SER B 1 150 ? 2.384   -5.557  0.675   1.00 26.32  ? 179 SER B CA  1 
ATOM   4592 C C   . SER B 1 150 ? 1.024   -5.387  -0.003  1.00 29.21  ? 179 SER B C   1 
ATOM   4593 O O   . SER B 1 150 ? 0.872   -5.709  -1.181  1.00 26.09  ? 179 SER B O   1 
ATOM   4594 C CB  . SER B 1 150 ? 3.397   -4.610  0.102   1.00 23.51  ? 179 SER B CB  1 
ATOM   4595 O OG  . SER B 1 150 ? 2.863   -3.297  0.126   1.00 22.98  ? 179 SER B OG  1 
ATOM   4596 N N   . ASN B 1 151 ? 0.046   -4.896  0.774   1.00 33.15  ? 180 ASN B N   1 
ATOM   4597 C CA  . ASN B 1 151 ? -1.275  -4.559  0.253   1.00 36.85  ? 180 ASN B CA  1 
ATOM   4598 C C   . ASN B 1 151 ? -1.179  -3.286  -0.582  1.00 36.18  ? 180 ASN B C   1 
ATOM   4599 O O   . ASN B 1 151 ? -1.942  -3.092  -1.522  1.00 31.00  ? 180 ASN B O   1 
ATOM   4600 C CB  . ASN B 1 151 ? -2.307  -4.305  1.351   1.00 39.48  ? 180 ASN B CB  1 
ATOM   4601 C CG  . ASN B 1 151 ? -2.418  -5.443  2.340   1.00 41.51  ? 180 ASN B CG  1 
ATOM   4602 O OD1 . ASN B 1 151 ? -2.254  -5.240  3.557   1.00 42.00  ? 180 ASN B OD1 1 
ATOM   4603 N ND2 . ASN B 1 151 ? -2.628  -6.647  1.834   1.00 37.30  ? 180 ASN B ND2 1 
ATOM   4604 N N   . PHE B 1 152 ? -0.274  -2.383  -0.182  1.00 30.59  ? 181 PHE B N   1 
ATOM   4605 C CA  . PHE B 1 152 ? -0.151  -1.114  -0.852  1.00 31.65  ? 181 PHE B CA  1 
ATOM   4606 C C   . PHE B 1 152 ? 0.395   -1.342  -2.253  1.00 28.42  ? 181 PHE B C   1 
ATOM   4607 O O   . PHE B 1 152 ? -0.153  -0.836  -3.230  1.00 26.34  ? 181 PHE B O   1 
ATOM   4608 C CB  . PHE B 1 152 ? 0.704   -0.114  -0.071  1.00 27.52  ? 181 PHE B CB  1 
ATOM   4609 C CG  . PHE B 1 152 ? 0.803   1.172   -0.871  1.00 25.61  ? 181 PHE B CG  1 
ATOM   4610 C CD1 . PHE B 1 152 ? -0.227  2.084   -0.877  1.00 26.60  ? 181 PHE B CD1 1 
ATOM   4611 C CD2 . PHE B 1 152 ? 1.932   1.470   -1.613  1.00 29.21  ? 181 PHE B CD2 1 
ATOM   4612 C CE1 . PHE B 1 152 ? -0.127  3.259   -1.607  1.00 27.61  ? 181 PHE B CE1 1 
ATOM   4613 C CE2 . PHE B 1 152 ? 2.021   2.633   -2.352  1.00 28.93  ? 181 PHE B CE2 1 
ATOM   4614 C CZ  . PHE B 1 152 ? 0.989   3.522   -2.355  1.00 27.41  ? 181 PHE B CZ  1 
ATOM   4615 N N   . ALA B 1 153 ? 1.437   -2.157  -2.370  1.00 28.63  ? 182 ALA B N   1 
ATOM   4616 C CA  . ALA B 1 153 ? 2.055   -2.385  -3.672  1.00 28.65  ? 182 ALA B CA  1 
ATOM   4617 C C   . ALA B 1 153 ? 1.045   -2.983  -4.677  1.00 31.60  ? 182 ALA B C   1 
ATOM   4618 O O   . ALA B 1 153 ? 1.043   -2.654  -5.849  1.00 31.95  ? 182 ALA B O   1 
ATOM   4619 C CB  . ALA B 1 153 ? 3.293   -3.261  -3.494  1.00 27.21  ? 182 ALA B CB  1 
ATOM   4620 N N   . ARG B 1 154 ? 0.151   -3.859  -4.242  1.00 38.56  ? 183 ARG B N   1 
ATOM   4621 C CA  . ARG B 1 154 ? -0.776  -4.500  -5.173  1.00 39.00  ? 183 ARG B CA  1 
ATOM   4622 C C   . ARG B 1 154 ? -1.863  -3.507  -5.581  1.00 34.84  ? 183 ARG B C   1 
ATOM   4623 O O   . ARG B 1 154 ? -2.285  -3.451  -6.733  1.00 30.05  ? 183 ARG B O   1 
ATOM   4624 C CB  . ARG B 1 154 ? -1.388  -5.788  -4.600  1.00 45.78  ? 183 ARG B CB  1 
ATOM   4625 C CG  . ARG B 1 154 ? -0.603  -7.039  -4.990  1.00 60.97  ? 183 ARG B CG  1 
ATOM   4626 C CD  . ARG B 1 154 ? -1.199  -8.364  -4.482  1.00 70.82  ? 183 ARG B CD  1 
ATOM   4627 N NE  . ARG B 1 154 ? -1.251  -8.466  -3.014  1.00 80.86  ? 183 ARG B NE  1 
ATOM   4628 C CZ  . ARG B 1 154 ? -0.251  -8.799  -2.175  1.00 80.90  ? 183 ARG B CZ  1 
ATOM   4629 N NH1 . ARG B 1 154 ? -0.417  -8.695  -0.859  1.00 70.17  ? 183 ARG B NH1 1 
ATOM   4630 N NH2 . ARG B 1 154 ? 0.919   -9.213  -2.645  1.00 79.22  ? 183 ARG B NH2 1 
ATOM   4631 N N   . ALA B 1 155 ? -2.326  -2.714  -4.622  1.00 32.93  ? 184 ALA B N   1 
ATOM   4632 C CA  . ALA B 1 155 ? -3.441  -1.824  -4.903  1.00 36.95  ? 184 ALA B CA  1 
ATOM   4633 C C   . ALA B 1 155 ? -2.970  -0.717  -5.847  1.00 34.97  ? 184 ALA B C   1 
ATOM   4634 O O   . ALA B 1 155 ? -3.723  -0.300  -6.742  1.00 30.68  ? 184 ALA B O   1 
ATOM   4635 C CB  . ALA B 1 155 ? -4.058  -1.310  -3.606  1.00 32.44  ? 184 ALA B CB  1 
ATOM   4636 N N   . TYR B 1 156 ? -1.695  -0.306  -5.702  1.00 32.59  ? 185 TYR B N   1 
ATOM   4637 C CA  . TYR B 1 156 ? -1.173  0.724   -6.598  1.00 33.90  ? 185 TYR B CA  1 
ATOM   4638 C C   . TYR B 1 156 ? -1.111  0.191   -8.031  1.00 33.43  ? 185 TYR B C   1 
ATOM   4639 O O   . TYR B 1 156 ? -1.469  0.887   -8.972  1.00 36.06  ? 185 TYR B O   1 
ATOM   4640 C CB  . TYR B 1 156 ? 0.168   1.320   -6.166  1.00 34.67  ? 185 TYR B CB  1 
ATOM   4641 C CG  . TYR B 1 156 ? 0.608   2.525   -6.997  1.00 34.97  ? 185 TYR B CG  1 
ATOM   4642 C CD1 . TYR B 1 156 ? 1.236   2.369   -8.235  1.00 38.81  ? 185 TYR B CD1 1 
ATOM   4643 C CD2 . TYR B 1 156 ? 0.432   3.823   -6.521  1.00 32.52  ? 185 TYR B CD2 1 
ATOM   4644 C CE1 . TYR B 1 156 ? 1.636   3.464   -8.994  1.00 38.04  ? 185 TYR B CE1 1 
ATOM   4645 C CE2 . TYR B 1 156 ? 0.847   4.917   -7.264  1.00 33.47  ? 185 TYR B CE2 1 
ATOM   4646 C CZ  . TYR B 1 156 ? 1.450   4.741   -8.495  1.00 33.32  ? 185 TYR B CZ  1 
ATOM   4647 O OH  . TYR B 1 156 ? 1.853   5.840   -9.193  1.00 37.56  ? 185 TYR B OH  1 
ATOM   4648 N N   . ALA B 1 157 ? -0.705  -1.066  -8.212  1.00 39.51  ? 186 ALA B N   1 
ATOM   4649 C CA  . ALA B 1 157 ? -0.673  -1.639  -9.549  1.00 43.55  ? 186 ALA B CA  1 
ATOM   4650 C C   . ALA B 1 157 ? -2.061  -1.596  -10.214 1.00 47.23  ? 186 ALA B C   1 
ATOM   4651 O O   . ALA B 1 157 ? -2.140  -1.424  -11.430 1.00 50.74  ? 186 ALA B O   1 
ATOM   4652 C CB  . ALA B 1 157 ? -0.116  -3.053  -9.489  1.00 49.29  ? 186 ALA B CB  1 
ATOM   4653 N N   . GLN B 1 158 ? -3.147  -1.706  -9.427  1.00 38.70  ? 187 GLN B N   1 
ATOM   4654 C CA  . GLN B 1 158 ? -4.504  -1.734  -9.952  1.00 36.81  ? 187 GLN B CA  1 
ATOM   4655 C C   . GLN B 1 158 ? -5.190  -0.369  -9.987  1.00 33.41  ? 187 GLN B C   1 
ATOM   4656 O O   . GLN B 1 158 ? -6.388  -0.312  -10.207 1.00 37.17  ? 187 GLN B O   1 
ATOM   4657 C CB  . GLN B 1 158 ? -5.384  -2.656  -9.116  1.00 40.96  ? 187 GLN B CB  1 
ATOM   4658 C CG  . GLN B 1 158 ? -4.902  -4.098  -9.057  1.00 44.37  ? 187 GLN B CG  1 
ATOM   4659 C CD  . GLN B 1 158 ? -5.576  -4.819  -7.916  1.00 56.68  ? 187 GLN B CD  1 
ATOM   4660 O OE1 . GLN B 1 158 ? -5.612  -4.324  -6.785  1.00 51.29  ? 187 GLN B OE1 1 
ATOM   4661 N NE2 . GLN B 1 158 ? -6.189  -5.954  -8.215  1.00 65.02  ? 187 GLN B NE2 1 
ATOM   4662 N N   . GLY B 1 159 ? -4.468  0.725   -9.749  1.00 28.61  ? 188 GLY B N   1 
ATOM   4663 C CA  . GLY B 1 159 ? -4.926  2.078   -10.036 1.00 30.01  ? 188 GLY B CA  1 
ATOM   4664 C C   . GLY B 1 159 ? -5.817  2.700   -8.960  1.00 34.63  ? 188 GLY B C   1 
ATOM   4665 O O   . GLY B 1 159 ? -6.643  3.571   -9.280  1.00 34.50  ? 188 GLY B O   1 
ATOM   4666 N N   . ILE B 1 160 ? -5.609  2.301   -7.697  1.00 28.68  ? 189 ILE B N   1 
ATOM   4667 C CA  . ILE B 1 160 ? -6.325  2.846   -6.550  1.00 30.66  ? 189 ILE B CA  1 
ATOM   4668 C C   . ILE B 1 160 ? -6.165  4.368   -6.491  1.00 29.76  ? 189 ILE B C   1 
ATOM   4669 O O   . ILE B 1 160 ? -5.090  4.897   -6.724  1.00 26.83  ? 189 ILE B O   1 
ATOM   4670 C CB  . ILE B 1 160 ? -5.859  2.164   -5.244  1.00 38.70  ? 189 ILE B CB  1 
ATOM   4671 C CG1 . ILE B 1 160 ? -6.899  2.293   -4.103  1.00 44.29  ? 189 ILE B CG1 1 
ATOM   4672 C CG2 . ILE B 1 160 ? -4.482  2.674   -4.792  1.00 37.07  ? 189 ILE B CG2 1 
ATOM   4673 C CD1 . ILE B 1 160 ? -7.948  1.205   -4.095  1.00 46.35  ? 189 ILE B CD1 1 
ATOM   4674 N N   . SER B 1 161 ? -7.248  5.070   -6.129  1.00 26.25  ? 190 SER B N   1 
ATOM   4675 C CA  . SER B 1 161 ? -7.262  6.511   -5.950  1.00 24.10  ? 190 SER B CA  1 
ATOM   4676 C C   . SER B 1 161 ? -6.220  6.945   -4.935  1.00 23.87  ? 190 SER B C   1 
ATOM   4677 O O   . SER B 1 161 ? -6.029  6.287   -3.921  1.00 27.60  ? 190 SER B O   1 
ATOM   4678 C CB  . SER B 1 161 ? -8.645  6.950   -5.488  1.00 25.19  ? 190 SER B CB  1 
ATOM   4679 O OG  . SER B 1 161 ? -8.626  8.304   -5.055  1.00 31.04  ? 190 SER B OG  1 
ATOM   4680 N N   . ARG B 1 162 ? -5.568  8.081   -5.201  1.00 24.73  ? 191 ARG B N   1 
ATOM   4681 C CA  . ARG B 1 162 ? -4.644  8.723   -4.273  1.00 29.49  ? 191 ARG B CA  1 
ATOM   4682 C C   . ARG B 1 162 ? -5.288  8.912   -2.885  1.00 31.12  ? 191 ARG B C   1 
ATOM   4683 O O   . ARG B 1 162 ? -4.611  8.842   -1.855  1.00 30.69  ? 191 ARG B O   1 
ATOM   4684 C CB  . ARG B 1 162 ? -4.222  10.070  -4.876  1.00 33.05  ? 191 ARG B CB  1 
ATOM   4685 C CG  . ARG B 1 162 ? -3.263  10.051  -6.061  1.00 44.44  ? 191 ARG B CG  1 
ATOM   4686 C CD  . ARG B 1 162 ? -2.901  11.499  -6.438  1.00 54.35  ? 191 ARG B CD  1 
ATOM   4687 N NE  . ARG B 1 162 ? -1.465  11.810  -6.433  1.00 60.03  ? 191 ARG B NE  1 
ATOM   4688 C CZ  . ARG B 1 162 ? -0.963  13.036  -6.638  1.00 76.40  ? 191 ARG B CZ  1 
ATOM   4689 N NH1 . ARG B 1 162 ? -1.760  14.046  -6.955  1.00 76.31  ? 191 ARG B NH1 1 
ATOM   4690 N NH2 . ARG B 1 162 ? 0.337   13.260  -6.540  1.00 79.80  ? 191 ARG B NH2 1 
ATOM   4691 N N   . THR B 1 163 ? -6.605  9.182   -2.855  1.00 28.94  ? 192 THR B N   1 
ATOM   4692 C CA  . THR B 1 163 ? -7.345  9.442   -1.633  1.00 31.80  ? 192 THR B CA  1 
ATOM   4693 C C   . THR B 1 163 ? -7.369  8.214   -0.719  1.00 30.81  ? 192 THR B C   1 
ATOM   4694 O O   . THR B 1 163 ? -7.809  8.317   0.424   1.00 34.97  ? 192 THR B O   1 
ATOM   4695 C CB  . THR B 1 163 ? -8.778  9.866   -1.985  1.00 27.85  ? 192 THR B CB  1 
ATOM   4696 O OG1 . THR B 1 163 ? -9.335  8.689   -2.565  1.00 24.46  ? 192 THR B OG1 1 
ATOM   4697 C CG2 . THR B 1 163 ? -8.812  11.079  -2.891  1.00 28.67  ? 192 THR B CG2 1 
ATOM   4698 N N   . LYS B 1 164 ? -6.942  7.054   -1.208  1.00 30.76  ? 193 LYS B N   1 
ATOM   4699 C CA  . LYS B 1 164 ? -6.925  5.857   -0.383  1.00 33.42  ? 193 LYS B CA  1 
ATOM   4700 C C   . LYS B 1 164 ? -5.517  5.346   -0.060  1.00 28.03  ? 193 LYS B C   1 
ATOM   4701 O O   . LYS B 1 164 ? -5.357  4.345   0.632   1.00 28.50  ? 193 LYS B O   1 
ATOM   4702 C CB  . LYS B 1 164 ? -7.790  4.777   -1.046  1.00 36.27  ? 193 LYS B CB  1 
ATOM   4703 C CG  . LYS B 1 164 ? -9.278  5.150   -1.079  1.00 42.73  ? 193 LYS B CG  1 
ATOM   4704 C CD  . LYS B 1 164 ? -10.227 3.968   -0.896  1.00 53.81  ? 193 LYS B CD  1 
ATOM   4705 C CE  . LYS B 1 164 ? -9.812  2.771   -1.696  1.00 54.01  ? 193 LYS B CE  1 
ATOM   4706 N NZ  . LYS B 1 164 ? -10.901 1.816   -1.915  1.00 64.94  ? 193 LYS B NZ  1 
ATOM   4707 N N   . TYR B 1 165 ? -4.473  6.024   -0.513  1.00 25.06  ? 194 TYR B N   1 
ATOM   4708 C CA  . TYR B 1 165 ? -3.130  5.545   -0.254  1.00 24.21  ? 194 TYR B CA  1 
ATOM   4709 C C   . TYR B 1 165 ? -2.929  5.283   1.245   1.00 24.02  ? 194 TYR B C   1 
ATOM   4710 O O   . TYR B 1 165 ? -2.548  4.184   1.645   1.00 30.92  ? 194 TYR B O   1 
ATOM   4711 C CB  . TYR B 1 165 ? -2.129  6.546   -0.846  1.00 24.09  ? 194 TYR B CB  1 
ATOM   4712 C CG  . TYR B 1 165 ? -1.926  6.546   -2.359  1.00 23.50  ? 194 TYR B CG  1 
ATOM   4713 C CD1 . TYR B 1 165 ? -2.556  5.627   -3.194  1.00 26.74  ? 194 TYR B CD1 1 
ATOM   4714 C CD2 . TYR B 1 165 ? -1.068  7.460   -2.951  1.00 25.95  ? 194 TYR B CD2 1 
ATOM   4715 C CE1 . TYR B 1 165 ? -2.426  5.685   -4.573  1.00 26.92  ? 194 TYR B CE1 1 
ATOM   4716 C CE2 . TYR B 1 165 ? -0.894  7.503   -4.328  1.00 27.25  ? 194 TYR B CE2 1 
ATOM   4717 C CZ  . TYR B 1 165 ? -1.565  6.605   -5.136  1.00 27.41  ? 194 TYR B CZ  1 
ATOM   4718 O OH  . TYR B 1 165 ? -1.419  6.638   -6.479  1.00 28.90  ? 194 TYR B OH  1 
ATOM   4719 N N   . TRP B 1 166 ? -3.203  6.280   2.077   1.00 24.72  ? 195 TRP B N   1 
ATOM   4720 C CA  . TRP B 1 166 ? -3.042  6.181   3.517   1.00 24.13  ? 195 TRP B CA  1 
ATOM   4721 C C   . TRP B 1 166 ? -3.657  4.894   4.063   1.00 23.51  ? 195 TRP B C   1 
ATOM   4722 O O   . TRP B 1 166 ? -3.122  4.335   5.001   1.00 23.42  ? 195 TRP B O   1 
ATOM   4723 C CB  . TRP B 1 166 ? -3.578  7.445   4.210   1.00 25.12  ? 195 TRP B CB  1 
ATOM   4724 C CG  . TRP B 1 166 ? -5.070  7.480   4.443   1.00 26.50  ? 195 TRP B CG  1 
ATOM   4725 C CD1 . TRP B 1 166 ? -6.023  8.111   3.689   1.00 26.20  ? 195 TRP B CD1 1 
ATOM   4726 C CD2 . TRP B 1 166 ? -5.782  6.869   5.542   1.00 25.58  ? 195 TRP B CD2 1 
ATOM   4727 N NE1 . TRP B 1 166 ? -7.273  7.915   4.220   1.00 27.13  ? 195 TRP B NE1 1 
ATOM   4728 C CE2 . TRP B 1 166 ? -7.159  7.158   5.360   1.00 29.65  ? 195 TRP B CE2 1 
ATOM   4729 C CE3 . TRP B 1 166 ? -5.394  6.095   6.635   1.00 24.68  ? 195 TRP B CE3 1 
ATOM   4730 C CZ2 . TRP B 1 166 ? -8.139  6.701   6.244   1.00 30.17  ? 195 TRP B CZ2 1 
ATOM   4731 C CZ3 . TRP B 1 166 ? -6.368  5.625   7.488   1.00 28.08  ? 195 TRP B CZ3 1 
ATOM   4732 C CH2 . TRP B 1 166 ? -7.719  5.934   7.306   1.00 28.31  ? 195 TRP B CH2 1 
ATOM   4733 N N   . GLU B 1 167 ? -4.763  4.393   3.500   1.00 25.07  ? 196 GLU B N   1 
ATOM   4734 C CA  . GLU B 1 167 ? -5.410  3.207   4.053   1.00 24.39  ? 196 GLU B CA  1 
ATOM   4735 C C   . GLU B 1 167 ? -4.554  1.949   3.916   1.00 25.16  ? 196 GLU B C   1 
ATOM   4736 O O   . GLU B 1 167 ? -4.420  1.154   4.833   1.00 22.43  ? 196 GLU B O   1 
ATOM   4737 C CB  . GLU B 1 167 ? -6.764  2.948   3.398   1.00 25.91  ? 196 GLU B CB  1 
ATOM   4738 C CG  . GLU B 1 167 ? -7.756  4.070   3.684   1.00 28.83  ? 196 GLU B CG  1 
ATOM   4739 C CD  . GLU B 1 167 ? -9.136  3.759   3.151   1.00 38.14  ? 196 GLU B CD  1 
ATOM   4740 O OE1 . GLU B 1 167 ? -9.929  4.704   3.021   1.00 41.29  ? 196 GLU B OE1 1 
ATOM   4741 O OE2 . GLU B 1 167 ? -9.387  2.573   2.838   1.00 45.67  ? 196 GLU B OE2 1 
ATOM   4742 N N   . LEU B 1 168 ? -3.979  1.753   2.750   1.00 25.56  ? 197 LEU B N   1 
ATOM   4743 C CA  . LEU B 1 168 ? -3.174  0.576   2.530   1.00 27.02  ? 197 LEU B CA  1 
ATOM   4744 C C   . LEU B 1 168 ? -1.841  0.723   3.255   1.00 25.80  ? 197 LEU B C   1 
ATOM   4745 O O   . LEU B 1 168 ? -1.306  -0.266  3.737   1.00 25.28  ? 197 LEU B O   1 
ATOM   4746 C CB  . LEU B 1 168 ? -2.953  0.372   1.037   1.00 30.72  ? 197 LEU B CB  1 
ATOM   4747 C CG  . LEU B 1 168 ? -4.169  0.079   0.153   1.00 38.82  ? 197 LEU B CG  1 
ATOM   4748 C CD1 . LEU B 1 168 ? -4.960  -1.146  0.561   1.00 34.32  ? 197 LEU B CD1 1 
ATOM   4749 C CD2 . LEU B 1 168 ? -5.069  1.325   0.043   1.00 42.24  ? 197 LEU B CD2 1 
ATOM   4750 N N   . ILE B 1 169 ? -1.294  1.947   3.300   1.00 23.26  ? 198 ILE B N   1 
ATOM   4751 C CA  . ILE B 1 169 ? -0.094  2.247   4.062   1.00 23.70  ? 198 ILE B CA  1 
ATOM   4752 C C   . ILE B 1 169 ? -0.335  1.891   5.533   1.00 23.93  ? 198 ILE B C   1 
ATOM   4753 O O   . ILE B 1 169 ? 0.484   1.243   6.165   1.00 22.83  ? 198 ILE B O   1 
ATOM   4754 C CB  . ILE B 1 169 ? 0.301   3.731   3.886   1.00 27.06  ? 198 ILE B CB  1 
ATOM   4755 C CG1 . ILE B 1 169 ? 0.722   4.052   2.462   1.00 29.67  ? 198 ILE B CG1 1 
ATOM   4756 C CG2 . ILE B 1 169 ? 1.357   4.168   4.887   1.00 24.92  ? 198 ILE B CG2 1 
ATOM   4757 C CD1 . ILE B 1 169 ? 2.055   3.455   2.066   1.00 28.41  ? 198 ILE B CD1 1 
ATOM   4758 N N   . TYR B 1 170 ? -1.490  2.300   6.064   1.00 23.59  ? 199 TYR B N   1 
ATOM   4759 C CA  . TYR B 1 170 ? -1.880  1.948   7.421   1.00 22.07  ? 199 TYR B CA  1 
ATOM   4760 C C   . TYR B 1 170 ? -1.871  0.427   7.596   1.00 21.17  ? 199 TYR B C   1 
ATOM   4761 O O   . TYR B 1 170 ? -1.356  -0.064  8.599   1.00 20.59  ? 199 TYR B O   1 
ATOM   4762 C CB  . TYR B 1 170 ? -3.258  2.546   7.721   1.00 22.78  ? 199 TYR B CB  1 
ATOM   4763 C CG  . TYR B 1 170 ? -3.880  2.011   8.998   1.00 24.27  ? 199 TYR B CG  1 
ATOM   4764 C CD1 . TYR B 1 170 ? -4.664  0.858   8.959   1.00 26.79  ? 199 TYR B CD1 1 
ATOM   4765 C CD2 . TYR B 1 170 ? -3.675  2.612   10.224  1.00 24.94  ? 199 TYR B CD2 1 
ATOM   4766 C CE1 . TYR B 1 170 ? -5.206  0.327   10.109  1.00 25.13  ? 199 TYR B CE1 1 
ATOM   4767 C CE2 . TYR B 1 170 ? -4.209  2.074   11.384  1.00 26.46  ? 199 TYR B CE2 1 
ATOM   4768 C CZ  . TYR B 1 170 ? -4.991  0.935   11.317  1.00 25.85  ? 199 TYR B CZ  1 
ATOM   4769 O OH  . TYR B 1 170 ? -5.585  0.355   12.411  1.00 28.60  ? 199 TYR B OH  1 
ATOM   4770 N N   . GLU B 1 171 ? -2.481  -0.314  6.656   1.00 23.58  ? 200 GLU B N   1 
ATOM   4771 C CA  . GLU B 1 171 ? -2.589  -1.770  6.804   1.00 22.95  ? 200 GLU B CA  1 
ATOM   4772 C C   . GLU B 1 171 ? -1.206  -2.418  6.784   1.00 19.80  ? 200 GLU B C   1 
ATOM   4773 O O   . GLU B 1 171 ? -0.917  -3.303  7.578   1.00 19.45  ? 200 GLU B O   1 
ATOM   4774 C CB  . GLU B 1 171 ? -3.511  -2.419  5.764   1.00 21.86  ? 200 GLU B CB  1 
ATOM   4775 C CG  . GLU B 1 171 ? -4.972  -2.006  5.949   1.00 24.74  ? 200 GLU B CG  1 
ATOM   4776 C CD  . GLU B 1 171 ? -5.614  -2.519  7.218   1.00 27.90  ? 200 GLU B CD  1 
ATOM   4777 O OE1 . GLU B 1 171 ? -6.608  -1.924  7.696   1.00 31.61  ? 200 GLU B OE1 1 
ATOM   4778 O OE2 . GLU B 1 171 ? -5.102  -3.509  7.748   1.00 33.12  ? 200 GLU B OE2 1 
ATOM   4779 N N   . ASP B 1 172 ? -0.379  -1.992  5.835   1.00 20.42  ? 201 ASP B N   1 
ATOM   4780 C CA  . ASP B 1 172 ? 0.957   -2.529  5.699   1.00 21.55  ? 201 ASP B CA  1 
ATOM   4781 C C   . ASP B 1 172 ? 1.754   -2.188  6.960   1.00 21.68  ? 201 ASP B C   1 
ATOM   4782 O O   . ASP B 1 172 ? 2.549   -3.004  7.426   1.00 22.55  ? 201 ASP B O   1 
ATOM   4783 C CB  . ASP B 1 172 ? 1.611   -2.071  4.403   1.00 21.12  ? 201 ASP B CB  1 
ATOM   4784 C CG  . ASP B 1 172 ? 1.157   -2.766  3.128   1.00 23.35  ? 201 ASP B CG  1 
ATOM   4785 O OD1 . ASP B 1 172 ? 0.371   -3.735  3.219   1.00 24.97  ? 201 ASP B OD1 1 
ATOM   4786 O OD2 . ASP B 1 172 ? 1.612   -2.362  2.047   1.00 21.79  ? 201 ASP B OD2 1 
ATOM   4787 N N   . SER B 1 173 ? 1.561   -0.983  7.497   1.00 24.49  ? 202 SER B N   1 
ATOM   4788 C CA  . SER B 1 173 ? 2.361   -0.520  8.625   1.00 23.78  ? 202 SER B CA  1 
ATOM   4789 C C   . SER B 1 173 ? 2.026   -1.297  9.899   1.00 26.52  ? 202 SER B C   1 
ATOM   4790 O O   . SER B 1 173 ? 2.916   -1.675  10.644  1.00 25.46  ? 202 SER B O   1 
ATOM   4791 C CB  . SER B 1 173 ? 2.189   0.936   8.873   1.00 24.32  ? 202 SER B CB  1 
ATOM   4792 O OG  . SER B 1 173 ? 2.811   1.698   7.855   1.00 22.48  ? 202 SER B OG  1 
ATOM   4793 N N   . MET B 1 174 ? 0.736   -1.538  10.137  1.00 25.59  ? 203 MET B N   1 
ATOM   4794 C CA  . MET B 1 174 ? 0.299   -2.370  11.242  1.00 25.74  ? 203 MET B CA  1 
ATOM   4795 C C   . MET B 1 174 ? 0.798   -3.802  11.104  1.00 23.17  ? 203 MET B C   1 
ATOM   4796 O O   . MET B 1 174 ? 1.127   -4.441  12.109  1.00 26.43  ? 203 MET B O   1 
ATOM   4797 C CB  . MET B 1 174 ? -1.239  -2.386  11.309  1.00 28.22  ? 203 MET B CB  1 
ATOM   4798 C CG  . MET B 1 174 ? -1.832  -1.016  11.612  1.00 27.43  ? 203 MET B CG  1 
ATOM   4799 S SD  . MET B 1 174 ? -1.898  -0.560  13.350  1.00 26.46  ? 203 MET B SD  1 
ATOM   4800 C CE  . MET B 1 174 ? -3.259  -1.617  13.887  1.00 25.74  ? 203 MET B CE  1 
ATOM   4801 N N   . ASP B 1 175 ? 0.748   -4.343  9.878   1.00 23.06  ? 204 ASP B N   1 
ATOM   4802 C CA  . ASP B 1 175 ? 1.258   -5.671  9.595   1.00 22.49  ? 204 ASP B CA  1 
ATOM   4803 C C   . ASP B 1 175 ? 2.753   -5.728  9.916   1.00 22.19  ? 204 ASP B C   1 
ATOM   4804 O O   . ASP B 1 175 ? 3.211   -6.654  10.564  1.00 19.83  ? 204 ASP B O   1 
ATOM   4805 C CB  . ASP B 1 175 ? 1.026   -6.037  8.137   1.00 27.03  ? 204 ASP B CB  1 
ATOM   4806 C CG  . ASP B 1 175 ? -0.383  -6.507  7.770   1.00 30.67  ? 204 ASP B CG  1 
ATOM   4807 O OD1 . ASP B 1 175 ? -1.173  -6.731  8.683   1.00 28.20  ? 204 ASP B OD1 1 
ATOM   4808 O OD2 . ASP B 1 175 ? -0.676  -6.631  6.557   1.00 30.16  ? 204 ASP B OD2 1 
ATOM   4809 N N   . LEU B 1 176 ? 3.504   -4.713  9.464   1.00 22.61  ? 205 LEU B N   1 
ATOM   4810 C CA  . LEU B 1 176 ? 4.937   -4.691  9.667   1.00 21.65  ? 205 LEU B CA  1 
ATOM   4811 C C   . LEU B 1 176 ? 5.253   -4.596  11.160  1.00 20.25  ? 205 LEU B C   1 
ATOM   4812 O O   . LEU B 1 176 ? 6.041   -5.387  11.683  1.00 19.53  ? 205 LEU B O   1 
ATOM   4813 C CB  . LEU B 1 176 ? 5.532   -3.564  8.831   1.00 22.43  ? 205 LEU B CB  1 
ATOM   4814 C CG  . LEU B 1 176 ? 7.035   -3.317  9.045   1.00 25.87  ? 205 LEU B CG  1 
ATOM   4815 C CD1 . LEU B 1 176 ? 7.915   -4.575  9.019   1.00 30.02  ? 205 LEU B CD1 1 
ATOM   4816 C CD2 . LEU B 1 176 ? 7.487   -2.331  7.986   1.00 27.16  ? 205 LEU B CD2 1 
ATOM   4817 N N   . ILE B 1 177 ? 4.696   -3.601  11.851  1.00 21.66  ? 206 ILE B N   1 
ATOM   4818 C CA  . ILE B 1 177 ? 4.897   -3.466  13.278  1.00 22.61  ? 206 ILE B CA  1 
ATOM   4819 C C   . ILE B 1 177 ? 4.592   -4.789  13.986  1.00 23.47  ? 206 ILE B C   1 
ATOM   4820 O O   . ILE B 1 177 ? 5.393   -5.173  14.826  1.00 20.58  ? 206 ILE B O   1 
ATOM   4821 C CB  . ILE B 1 177 ? 4.075   -2.310  13.861  1.00 21.54  ? 206 ILE B CB  1 
ATOM   4822 C CG1 . ILE B 1 177 ? 4.587   -0.994  13.339  1.00 22.77  ? 206 ILE B CG1 1 
ATOM   4823 C CG2 . ILE B 1 177 ? 4.099   -2.351  15.402  1.00 22.52  ? 206 ILE B CG2 1 
ATOM   4824 C CD1 . ILE B 1 177 ? 3.610   0.154   13.547  1.00 23.89  ? 206 ILE B CD1 1 
ATOM   4825 N N   . ALA B 1 178 ? 3.511   -5.498  13.588  1.00 23.45  ? 207 ALA B N   1 
ATOM   4826 C CA  . ALA B 1 178 ? 3.111   -6.769  14.198  1.00 24.23  ? 207 ALA B CA  1 
ATOM   4827 C C   . ALA B 1 178 ? 4.168   -7.864  14.029  1.00 24.69  ? 207 ALA B C   1 
ATOM   4828 O O   . ALA B 1 178 ? 4.336   -8.673  14.937  1.00 25.16  ? 207 ALA B O   1 
ATOM   4829 C CB  . ALA B 1 178 ? 1.791   -7.254  13.659  1.00 24.20  ? 207 ALA B CB  1 
ATOM   4830 N N   . LYS B 1 179 ? 4.884   -7.851  12.898  1.00 21.07  ? 208 LYS B N   1 
ATOM   4831 C CA  . LYS B 1 179 ? 5.795   -8.918  12.521  1.00 24.06  ? 208 LYS B CA  1 
ATOM   4832 C C   . LYS B 1 179 ? 7.208   -8.701  13.059  1.00 21.74  ? 208 LYS B C   1 
ATOM   4833 O O   . LYS B 1 179 ? 7.999   -9.648  13.131  1.00 21.95  ? 208 LYS B O   1 
ATOM   4834 C CB  . LYS B 1 179 ? 5.754   -9.042  10.991  1.00 23.68  ? 208 LYS B CB  1 
ATOM   4835 C CG  . LYS B 1 179 ? 4.401   -9.527  10.529  1.00 26.52  ? 208 LYS B CG  1 
ATOM   4836 C CD  . LYS B 1 179 ? 4.120   -9.517  9.041   1.00 34.85  ? 208 LYS B CD  1 
ATOM   4837 C CE  . LYS B 1 179 ? 2.657   -9.836  8.850   1.00 39.38  ? 208 LYS B CE  1 
ATOM   4838 N NZ  . LYS B 1 179 ? 2.297   -9.526  7.475   1.00 46.76  ? 208 LYS B NZ  1 
ATOM   4839 N N   . LEU B 1 180 ? 7.512   -7.447  13.400  1.00 21.43  ? 209 LEU B N   1 
ATOM   4840 C CA  . LEU B 1 180 ? 8.873   -7.033  13.660  1.00 20.99  ? 209 LEU B CA  1 
ATOM   4841 C C   . LEU B 1 180 ? 9.469   -7.847  14.782  1.00 19.42  ? 209 LEU B C   1 
ATOM   4842 O O   . LEU B 1 180 ? 10.558  -8.430  14.622  1.00 18.06  ? 209 LEU B O   1 
ATOM   4843 C CB  . LEU B 1 180 ? 8.952   -5.525  13.894  1.00 20.14  ? 209 LEU B CB  1 
ATOM   4844 C CG  . LEU B 1 180 ? 9.205   -4.727  12.614  1.00 21.17  ? 209 LEU B CG  1 
ATOM   4845 C CD1 . LEU B 1 180 ? 9.072   -3.239  12.893  1.00 22.52  ? 209 LEU B CD1 1 
ATOM   4846 C CD2 . LEU B 1 180 ? 10.595  -5.055  12.058  1.00 22.46  ? 209 LEU B CD2 1 
ATOM   4847 N N   . PRO B 1 181 ? 8.771   -7.945  15.929  1.00 23.01  ? 210 PRO B N   1 
ATOM   4848 C CA  . PRO B 1 181 ? 9.227   -8.804  17.015  1.00 22.44  ? 210 PRO B CA  1 
ATOM   4849 C C   . PRO B 1 181 ? 9.541   -10.249 16.627  1.00 23.40  ? 210 PRO B C   1 
ATOM   4850 O O   . PRO B 1 181 ? 10.537  -10.786 17.103  1.00 25.81  ? 210 PRO B O   1 
ATOM   4851 C CB  . PRO B 1 181 ? 8.089   -8.743  18.036  1.00 25.14  ? 210 PRO B CB  1 
ATOM   4852 C CG  . PRO B 1 181 ? 7.236   -7.561  17.656  1.00 27.52  ? 210 PRO B CG  1 
ATOM   4853 C CD  . PRO B 1 181 ? 7.540   -7.200  16.237  1.00 24.35  ? 210 PRO B CD  1 
ATOM   4854 N N   . CYS B 1 182 ? 8.725   -10.840 15.728  1.00 26.38  ? 211 CYS B N   1 
ATOM   4855 C CA  . CYS B 1 182 ? 8.926   -12.210 15.292  1.00 27.97  ? 211 CYS B CA  1 
ATOM   4856 C C   . CYS B 1 182 ? 10.232  -12.319 14.504  1.00 27.20  ? 211 CYS B C   1 
ATOM   4857 O O   . CYS B 1 182 ? 11.073  -13.171 14.786  1.00 26.10  ? 211 CYS B O   1 
ATOM   4858 C CB  . CYS B 1 182 ? 7.727   -12.700 14.491  1.00 31.73  ? 211 CYS B CB  1 
ATOM   4859 S SG  . CYS B 1 182 ? 6.178   -12.674 15.433  1.00 35.91  ? 211 CYS B SG  1 
ATOM   4860 N N   . VAL B 1 183 ? 10.412  -11.405 13.547  1.00 27.21  ? 212 VAL B N   1 
ATOM   4861 C CA  . VAL B 1 183 ? 11.646  -11.287 12.782  1.00 24.04  ? 212 VAL B CA  1 
ATOM   4862 C C   . VAL B 1 183 ? 12.844  -11.051 13.709  1.00 21.68  ? 212 VAL B C   1 
ATOM   4863 O O   . VAL B 1 183 ? 13.814  -11.805 13.681  1.00 19.76  ? 212 VAL B O   1 
ATOM   4864 C CB  . VAL B 1 183 ? 11.567  -10.168 11.734  1.00 22.08  ? 212 VAL B CB  1 
ATOM   4865 C CG1 . VAL B 1 183 ? 12.911  -9.977  11.053  1.00 21.33  ? 212 VAL B CG1 1 
ATOM   4866 C CG2 . VAL B 1 183 ? 10.495  -10.457 10.722  1.00 23.10  ? 212 VAL B CG2 1 
ATOM   4867 N N   . ALA B 1 184 ? 12.768  -10.012 14.524  1.00 19.94  ? 213 ALA B N   1 
ATOM   4868 C CA  . ALA B 1 184 ? 13.826  -9.676  15.465  1.00 22.74  ? 213 ALA B CA  1 
ATOM   4869 C C   . ALA B 1 184 ? 14.182  -10.857 16.364  1.00 24.06  ? 213 ALA B C   1 
ATOM   4870 O O   . ALA B 1 184 ? 15.349  -11.054 16.655  1.00 22.19  ? 213 ALA B O   1 
ATOM   4871 C CB  . ALA B 1 184 ? 13.427  -8.491  16.314  1.00 22.12  ? 213 ALA B CB  1 
ATOM   4872 N N   . ALA B 1 185 ? 13.172  -11.606 16.845  1.00 25.14  ? 214 ALA B N   1 
ATOM   4873 C CA  . ALA B 1 185 ? 13.405  -12.726 17.741  1.00 23.15  ? 214 ALA B CA  1 
ATOM   4874 C C   . ALA B 1 185 ? 13.990  -13.925 16.995  1.00 22.99  ? 214 ALA B C   1 
ATOM   4875 O O   . ALA B 1 185 ? 14.830  -14.594 17.559  1.00 25.31  ? 214 ALA B O   1 
ATOM   4876 C CB  . ALA B 1 185 ? 12.149  -13.086 18.496  1.00 26.59  ? 214 ALA B CB  1 
ATOM   4877 N N   . LYS B 1 186 ? 13.592  -14.177 15.744  1.00 23.36  ? 215 LYS B N   1 
ATOM   4878 C CA  . LYS B 1 186 ? 14.202  -15.238 14.961  1.00 27.54  ? 215 LYS B CA  1 
ATOM   4879 C C   . LYS B 1 186 ? 15.696  -14.961 14.771  1.00 25.52  ? 215 LYS B C   1 
ATOM   4880 O O   . LYS B 1 186 ? 16.527  -15.874 14.871  1.00 23.59  ? 215 LYS B O   1 
ATOM   4881 C CB  . LYS B 1 186 ? 13.410  -15.429 13.668  1.00 33.47  ? 215 LYS B CB  1 
ATOM   4882 C CG  . LYS B 1 186 ? 13.458  -16.843 13.066  1.00 44.15  ? 215 LYS B CG  1 
ATOM   4883 C CD  . LYS B 1 186 ? 12.246  -17.764 13.269  1.00 41.87  ? 215 LYS B CD  1 
ATOM   4884 C CE  . LYS B 1 186 ? 12.652  -19.222 13.223  1.00 38.97  ? 215 LYS B CE  1 
ATOM   4885 N N   . ILE B 1 187 ? 16.050  -13.703 14.465  1.00 25.77  ? 216 ILE B N   1 
ATOM   4886 C CA  . ILE B 1 187 ? 17.448  -13.313 14.296  1.00 21.27  ? 216 ILE B CA  1 
ATOM   4887 C C   . ILE B 1 187 ? 18.192  -13.596 15.591  1.00 22.20  ? 216 ILE B C   1 
ATOM   4888 O O   . ILE B 1 187 ? 19.288  -14.162 15.619  1.00 23.04  ? 216 ILE B O   1 
ATOM   4889 C CB  . ILE B 1 187 ? 17.581  -11.833 13.872  1.00 21.17  ? 216 ILE B CB  1 
ATOM   4890 C CG1 . ILE B 1 187 ? 17.098  -11.635 12.444  1.00 21.37  ? 216 ILE B CG1 1 
ATOM   4891 C CG2 . ILE B 1 187 ? 19.010  -11.310 14.070  1.00 20.90  ? 216 ILE B CG2 1 
ATOM   4892 C CD1 . ILE B 1 187 ? 16.759  -10.197 12.092  1.00 21.91  ? 216 ILE B CD1 1 
ATOM   4893 N N   . TYR B 1 188 ? 17.619  -13.164 16.702  1.00 22.03  ? 217 TYR B N   1 
ATOM   4894 C CA  . TYR B 1 188 ? 18.324  -13.322 17.954  1.00 23.59  ? 217 TYR B CA  1 
ATOM   4895 C C   . TYR B 1 188 ? 18.549  -14.811 18.234  1.00 23.55  ? 217 TYR B C   1 
ATOM   4896 O O   . TYR B 1 188 ? 19.643  -15.209 18.560  1.00 26.60  ? 217 TYR B O   1 
ATOM   4897 C CB  . TYR B 1 188 ? 17.497  -12.684 19.074  1.00 24.08  ? 217 TYR B CB  1 
ATOM   4898 C CG  . TYR B 1 188 ? 18.208  -12.605 20.412  1.00 22.74  ? 217 TYR B CG  1 
ATOM   4899 C CD1 . TYR B 1 188 ? 19.206  -11.653 20.649  1.00 22.97  ? 217 TYR B CD1 1 
ATOM   4900 C CD2 . TYR B 1 188 ? 17.877  -13.481 21.451  1.00 27.26  ? 217 TYR B CD2 1 
ATOM   4901 C CE1 . TYR B 1 188 ? 19.855  -11.573 21.873  1.00 22.86  ? 217 TYR B CE1 1 
ATOM   4902 C CE2 . TYR B 1 188 ? 18.523  -13.412 22.676  1.00 26.58  ? 217 TYR B CE2 1 
ATOM   4903 C CZ  . TYR B 1 188 ? 19.505  -12.451 22.889  1.00 25.71  ? 217 TYR B CZ  1 
ATOM   4904 O OH  . TYR B 1 188 ? 20.154  -12.425 24.086  1.00 28.16  ? 217 TYR B OH  1 
ATOM   4905 N N   . ARG B 1 189 ? 17.498  -15.616 18.130  1.00 26.51  ? 218 ARG B N   1 
ATOM   4906 C CA  . ARG B 1 189 ? 17.564  -17.009 18.520  1.00 27.08  ? 218 ARG B CA  1 
ATOM   4907 C C   . ARG B 1 189 ? 18.460  -17.793 17.579  1.00 28.95  ? 218 ARG B C   1 
ATOM   4908 O O   . ARG B 1 189 ? 19.149  -18.720 18.024  1.00 32.06  ? 218 ARG B O   1 
ATOM   4909 C CB  . ARG B 1 189 ? 16.176  -17.638 18.575  1.00 29.24  ? 218 ARG B CB  1 
ATOM   4910 C CG  . ARG B 1 189 ? 15.342  -17.010 19.674  1.00 32.99  ? 218 ARG B CG  1 
ATOM   4911 C CD  . ARG B 1 189 ? 14.114  -17.845 20.018  1.00 36.69  ? 218 ARG B CD  1 
ATOM   4912 N NE  . ARG B 1 189 ? 14.543  -18.852 20.987  1.00 45.52  ? 218 ARG B NE  1 
ATOM   4913 C CZ  . ARG B 1 189 ? 13.968  -19.121 22.146  1.00 43.89  ? 218 ARG B CZ  1 
ATOM   4914 N NH1 . ARG B 1 189 ? 12.762  -18.663 22.428  1.00 41.06  ? 218 ARG B NH1 1 
ATOM   4915 N NH2 . ARG B 1 189 ? 14.597  -19.925 22.968  1.00 43.45  ? 218 ARG B NH2 1 
ATOM   4916 N N   . ASN B 1 190 ? 18.422  -17.454 16.284  1.00 28.36  ? 219 ASN B N   1 
ATOM   4917 C CA  . ASN B 1 190 ? 19.268  -18.113 15.298  1.00 25.51  ? 219 ASN B CA  1 
ATOM   4918 C C   . ASN B 1 190 ? 20.748  -17.806 15.537  1.00 24.92  ? 219 ASN B C   1 
ATOM   4919 O O   . ASN B 1 190 ? 21.591  -18.676 15.389  1.00 23.84  ? 219 ASN B O   1 
ATOM   4920 C CB  . ASN B 1 190 ? 18.856  -17.732 13.886  1.00 29.05  ? 219 ASN B CB  1 
ATOM   4921 C CG  . ASN B 1 190 ? 17.580  -18.425 13.481  1.00 31.72  ? 219 ASN B CG  1 
ATOM   4922 O OD1 . ASN B 1 190 ? 17.100  -19.291 14.210  1.00 31.82  ? 219 ASN B OD1 1 
ATOM   4923 N ND2 . ASN B 1 190 ? 17.051  -18.104 12.308  1.00 32.20  ? 219 ASN B ND2 1 
ATOM   4924 N N   . LEU B 1 191 ? 21.076  -16.570 15.912  1.00 21.55  ? 220 LEU B N   1 
ATOM   4925 C CA  . LEU B 1 191 ? 22.459  -16.200 16.136  1.00 23.29  ? 220 LEU B CA  1 
ATOM   4926 C C   . LEU B 1 191 ? 22.943  -16.637 17.510  1.00 24.66  ? 220 LEU B C   1 
ATOM   4927 O O   . LEU B 1 191 ? 24.096  -17.000 17.650  1.00 26.57  ? 220 LEU B O   1 
ATOM   4928 C CB  . LEU B 1 191 ? 22.610  -14.690 15.974  1.00 22.37  ? 220 LEU B CB  1 
ATOM   4929 C CG  . LEU B 1 191 ? 22.464  -14.174 14.535  1.00 23.62  ? 220 LEU B CG  1 
ATOM   4930 C CD1 . LEU B 1 191 ? 22.255  -12.638 14.532  1.00 25.53  ? 220 LEU B CD1 1 
ATOM   4931 C CD2 . LEU B 1 191 ? 23.668  -14.612 13.712  1.00 22.75  ? 220 LEU B CD2 1 
ATOM   4932 N N   . TYR B 1 192 ? 22.121  -16.454 18.547  1.00 25.40  ? 221 TYR B N   1 
ATOM   4933 C CA  . TYR B 1 192 ? 22.645  -16.484 19.904  1.00 27.89  ? 221 TYR B CA  1 
ATOM   4934 C C   . TYR B 1 192 ? 22.052  -17.632 20.715  1.00 30.77  ? 221 TYR B C   1 
ATOM   4935 O O   . TYR B 1 192 ? 22.401  -17.767 21.862  1.00 29.56  ? 221 TYR B O   1 
ATOM   4936 C CB  . TYR B 1 192 ? 22.374  -15.129 20.540  1.00 28.89  ? 221 TYR B CB  1 
ATOM   4937 C CG  . TYR B 1 192 ? 22.920  -13.971 19.726  1.00 30.35  ? 221 TYR B CG  1 
ATOM   4938 C CD1 . TYR B 1 192 ? 24.242  -13.965 19.287  1.00 33.49  ? 221 TYR B CD1 1 
ATOM   4939 C CD2 . TYR B 1 192 ? 22.096  -12.917 19.337  1.00 31.17  ? 221 TYR B CD2 1 
ATOM   4940 C CE1 . TYR B 1 192 ? 24.745  -12.931 18.508  1.00 31.06  ? 221 TYR B CE1 1 
ATOM   4941 C CE2 . TYR B 1 192 ? 22.577  -11.891 18.538  1.00 30.66  ? 221 TYR B CE2 1 
ATOM   4942 C CZ  . TYR B 1 192 ? 23.906  -11.896 18.132  1.00 31.84  ? 221 TYR B CZ  1 
ATOM   4943 O OH  . TYR B 1 192 ? 24.408  -10.890 17.383  1.00 30.30  ? 221 TYR B OH  1 
ATOM   4944 N N   . ARG B 1 193 ? 21.174  -18.456 20.134  1.00 39.97  ? 222 ARG B N   1 
ATOM   4945 C CA  . ARG B 1 193 ? 20.582  -19.581 20.850  1.00 42.60  ? 222 ARG B CA  1 
ATOM   4946 C C   . ARG B 1 193 ? 20.368  -20.791 19.938  1.00 38.81  ? 222 ARG B C   1 
ATOM   4947 O O   . ARG B 1 193 ? 19.338  -21.465 20.035  1.00 35.52  ? 222 ARG B O   1 
ATOM   4948 C CB  . ARG B 1 193 ? 19.251  -19.152 21.476  1.00 44.25  ? 222 ARG B CB  1 
ATOM   4949 C CG  . ARG B 1 193 ? 19.474  -18.108 22.554  1.00 42.03  ? 222 ARG B CG  1 
ATOM   4950 C CD  . ARG B 1 193 ? 18.273  -17.927 23.440  1.00 53.60  ? 222 ARG B CD  1 
ATOM   4951 N NE  . ARG B 1 193 ? 18.524  -16.803 24.347  1.00 59.63  ? 222 ARG B NE  1 
ATOM   4952 C CZ  . ARG B 1 193 ? 19.514  -16.780 25.213  1.00 52.40  ? 222 ARG B CZ  1 
ATOM   4953 N NH1 . ARG B 1 193 ? 20.097  -17.913 25.549  1.00 63.05  ? 222 ARG B NH1 1 
ATOM   4954 N NH2 . ARG B 1 193 ? 19.903  -15.639 25.747  1.00 45.37  ? 222 ARG B NH2 1 
ATOM   4955 N N   . GLU B 1 194 ? 21.325  -21.023 19.027  1.00 41.08  ? 223 GLU B N   1 
ATOM   4956 C CA  . GLU B 1 194 ? 21.424  -22.273 18.286  1.00 45.01  ? 223 GLU B CA  1 
ATOM   4957 C C   . GLU B 1 194 ? 20.178  -22.589 17.462  1.00 44.26  ? 223 GLU B C   1 
ATOM   4958 O O   . GLU B 1 194 ? 19.877  -23.758 17.235  1.00 43.88  ? 223 GLU B O   1 
ATOM   4959 C CB  . GLU B 1 194 ? 21.644  -23.409 19.287  1.00 49.09  ? 223 GLU B CB  1 
ATOM   4960 C CG  . GLU B 1 194 ? 22.912  -23.228 20.115  1.00 52.62  ? 223 GLU B CG  1 
ATOM   4961 C CD  . GLU B 1 194 ? 22.962  -24.185 21.293  1.00 68.20  ? 223 GLU B CD  1 
ATOM   4962 O OE1 . GLU B 1 194 ? 23.241  -23.718 22.429  1.00 68.58  ? 223 GLU B OE1 1 
ATOM   4963 O OE2 . GLU B 1 194 ? 22.680  -25.393 21.077  1.00 65.52  ? 223 GLU B OE2 1 
ATOM   4964 N N   . GLY B 1 195 ? 19.435  -21.572 17.011  1.00 40.89  ? 224 GLY B N   1 
ATOM   4965 C CA  . GLY B 1 195 ? 18.361  -21.804 16.050  1.00 37.69  ? 224 GLY B CA  1 
ATOM   4966 C C   . GLY B 1 195 ? 17.091  -22.363 16.685  1.00 37.33  ? 224 GLY B C   1 
ATOM   4967 O O   . GLY B 1 195 ? 16.168  -22.769 15.974  1.00 34.97  ? 224 GLY B O   1 
ATOM   4968 N N   . SER B 1 196 ? 17.011  -22.339 18.020  1.00 37.41  ? 225 SER B N   1 
ATOM   4969 C CA  . SER B 1 196 ? 15.783  -22.735 18.697  1.00 42.14  ? 225 SER B CA  1 
ATOM   4970 C C   . SER B 1 196 ? 14.636  -21.824 18.275  1.00 42.42  ? 225 SER B C   1 
ATOM   4971 O O   . SER B 1 196 ? 14.879  -20.687 17.887  1.00 45.34  ? 225 SER B O   1 
ATOM   4972 C CB  . SER B 1 196 ? 15.969  -22.681 20.179  1.00 42.49  ? 225 SER B CB  1 
ATOM   4973 O OG  . SER B 1 196 ? 16.527  -21.426 20.536  1.00 45.13  ? 225 SER B OG  1 
ATOM   4974 N N   . GLY B 1 197 ? 13.399  -22.319 18.403  1.00 39.81  ? 226 GLY B N   1 
ATOM   4975 C CA  . GLY B 1 197 ? 12.199  -21.654 17.902  1.00 36.85  ? 226 GLY B CA  1 
ATOM   4976 C C   . GLY B 1 197 ? 11.709  -20.486 18.769  1.00 36.84  ? 226 GLY B C   1 
ATOM   4977 O O   . GLY B 1 197 ? 11.913  -20.444 19.988  1.00 35.43  ? 226 GLY B O   1 
ATOM   4978 N N   . ILE B 1 198 ? 10.947  -19.570 18.143  1.00 36.46  ? 227 ILE B N   1 
ATOM   4979 C CA  . ILE B 1 198 ? 10.487  -18.370 18.843  1.00 40.71  ? 227 ILE B CA  1 
ATOM   4980 C C   . ILE B 1 198 ? 9.227   -18.647 19.671  1.00 42.53  ? 227 ILE B C   1 
ATOM   4981 O O   . ILE B 1 198 ? 8.860   -17.849 20.546  1.00 39.38  ? 227 ILE B O   1 
ATOM   4982 C CB  . ILE B 1 198 ? 10.316  -17.179 17.884  1.00 37.03  ? 227 ILE B CB  1 
ATOM   4983 C CG1 . ILE B 1 198 ? 9.497   -17.540 16.636  1.00 38.37  ? 227 ILE B CG1 1 
ATOM   4984 C CG2 . ILE B 1 198 ? 11.710  -16.628 17.548  1.00 37.67  ? 227 ILE B CG2 1 
ATOM   4985 C CD1 . ILE B 1 198 ? 9.343   -16.409 15.631  1.00 38.51  ? 227 ILE B CD1 1 
ATOM   4986 N N   . GLY B 1 199 ? 8.592   -19.797 19.439  1.00 45.42  ? 228 GLY B N   1 
ATOM   4987 C CA  . GLY B 1 199 ? 7.374   -20.125 20.164  1.00 41.57  ? 228 GLY B CA  1 
ATOM   4988 C C   . GLY B 1 199 ? 6.202   -19.346 19.579  1.00 42.99  ? 228 GLY B C   1 
ATOM   4989 O O   . GLY B 1 199 ? 6.242   -18.892 18.433  1.00 48.73  ? 228 GLY B O   1 
ATOM   4990 N N   . ALA B 1 200 ? 5.127   -19.218 20.354  1.00 46.28  ? 229 ALA B N   1 
ATOM   4991 C CA  . ALA B 1 200 ? 3.895   -18.705 19.787  1.00 43.01  ? 229 ALA B CA  1 
ATOM   4992 C C   . ALA B 1 200 ? 3.684   -17.272 20.265  1.00 39.96  ? 229 ALA B C   1 
ATOM   4993 O O   . ALA B 1 200 ? 4.319   -16.815 21.215  1.00 38.82  ? 229 ALA B O   1 
ATOM   4994 C CB  . ALA B 1 200 ? 2.739   -19.630 20.126  1.00 44.49  ? 229 ALA B CB  1 
ATOM   4995 N N   . ILE B 1 201 ? 2.856   -16.559 19.512  1.00 38.39  ? 230 ILE B N   1 
ATOM   4996 C CA  . ILE B 1 201 ? 2.272   -15.311 19.958  1.00 43.57  ? 230 ILE B CA  1 
ATOM   4997 C C   . ILE B 1 201 ? 1.151   -15.640 20.937  1.00 46.78  ? 230 ILE B C   1 
ATOM   4998 O O   . ILE B 1 201 ? 0.446   -16.632 20.762  1.00 54.40  ? 230 ILE B O   1 
ATOM   4999 C CB  . ILE B 1 201 ? 1.767   -14.515 18.735  1.00 41.26  ? 230 ILE B CB  1 
ATOM   5000 C CG1 . ILE B 1 201 ? 2.933   -13.933 17.944  1.00 42.24  ? 230 ILE B CG1 1 
ATOM   5001 C CG2 . ILE B 1 201 ? 0.752   -13.441 19.128  1.00 39.42  ? 230 ILE B CG2 1 
ATOM   5002 C CD1 . ILE B 1 201 ? 3.607   -12.731 18.588  1.00 45.69  ? 230 ILE B CD1 1 
ATOM   5003 N N   . ASP B 1 202 ? 0.989   -14.799 21.956  1.00 42.74  ? 231 ASP B N   1 
ATOM   5004 C CA  . ASP B 1 202 ? -0.188  -14.872 22.798  1.00 46.00  ? 231 ASP B CA  1 
ATOM   5005 C C   . ASP B 1 202 ? -1.112  -13.696 22.485  1.00 50.16  ? 231 ASP B C   1 
ATOM   5006 O O   . ASP B 1 202 ? -0.794  -12.531 22.736  1.00 42.67  ? 231 ASP B O   1 
ATOM   5007 C CB  . ASP B 1 202 ? 0.153   -15.019 24.267  1.00 47.63  ? 231 ASP B CB  1 
ATOM   5008 C CG  . ASP B 1 202 ? -1.054  -15.040 25.195  1.00 49.65  ? 231 ASP B CG  1 
ATOM   5009 O OD1 . ASP B 1 202 ? -2.204  -14.921 24.698  1.00 53.85  ? 231 ASP B OD1 1 
ATOM   5010 O OD2 . ASP B 1 202 ? -0.839  -15.166 26.408  1.00 46.79  ? 231 ASP B OD2 1 
ATOM   5011 N N   . SER B 1 203 ? -2.299  -14.070 21.995  1.00 51.61  ? 232 SER B N   1 
ATOM   5012 C CA  . SER B 1 203 ? -3.353  -13.165 21.575  1.00 52.92  ? 232 SER B CA  1 
ATOM   5013 C C   . SER B 1 203 ? -3.668  -12.109 22.639  1.00 49.34  ? 232 SER B C   1 
ATOM   5014 O O   . SER B 1 203 ? -4.215  -11.063 22.303  1.00 46.83  ? 232 SER B O   1 
ATOM   5015 C CB  . SER B 1 203 ? -4.576  -13.987 21.194  1.00 56.36  ? 232 SER B CB  1 
ATOM   5016 O OG  . SER B 1 203 ? -5.634  -13.171 20.715  1.00 60.44  ? 232 SER B OG  1 
ATOM   5017 N N   . ASN B 1 204 ? -3.311  -12.348 23.911  1.00 51.05  ? 233 ASN B N   1 
ATOM   5018 C CA  . ASN B 1 204 ? -3.699  -11.441 24.982  1.00 47.05  ? 233 ASN B CA  1 
ATOM   5019 C C   . ASN B 1 204 ? -2.516  -10.792 25.695  1.00 41.57  ? 233 ASN B C   1 
ATOM   5020 O O   . ASN B 1 204 ? -2.709  -10.192 26.751  1.00 45.39  ? 233 ASN B O   1 
ATOM   5021 C CB  . ASN B 1 204 ? -4.522  -12.148 26.052  1.00 57.00  ? 233 ASN B CB  1 
ATOM   5022 C CG  . ASN B 1 204 ? -5.842  -12.624 25.508  1.00 63.53  ? 233 ASN B CG  1 
ATOM   5023 O OD1 . ASN B 1 204 ? -6.537  -11.876 24.804  1.00 67.44  ? 233 ASN B OD1 1 
ATOM   5024 N ND2 . ASN B 1 204 ? -6.184  -13.869 25.802  1.00 64.75  ? 233 ASN B ND2 1 
ATOM   5025 N N   . LEU B 1 205 ? -1.304  -10.868 25.138  1.00 42.11  ? 234 LEU B N   1 
ATOM   5026 C CA  . LEU B 1 205 ? -0.190  -10.106 25.706  1.00 43.81  ? 234 LEU B CA  1 
ATOM   5027 C C   . LEU B 1 205 ? 0.061   -8.804  24.933  1.00 36.32  ? 234 LEU B C   1 
ATOM   5028 O O   . LEU B 1 205 ? -0.296  -8.667  23.769  1.00 33.65  ? 234 LEU B O   1 
ATOM   5029 C CB  . LEU B 1 205 ? 1.063   -10.978 25.710  1.00 43.21  ? 234 LEU B CB  1 
ATOM   5030 C CG  . LEU B 1 205 ? 0.970   -12.282 26.502  1.00 47.46  ? 234 LEU B CG  1 
ATOM   5031 C CD1 . LEU B 1 205 ? 2.305   -13.036 26.491  1.00 47.32  ? 234 LEU B CD1 1 
ATOM   5032 C CD2 . LEU B 1 205 ? 0.492   -11.992 27.914  1.00 43.72  ? 234 LEU B CD2 1 
ATOM   5033 N N   . ASP B 1 206 ? 0.719   -7.842  25.580  1.00 33.09  ? 235 ASP B N   1 
ATOM   5034 C CA  . ASP B 1 206 ? 1.204   -6.677  24.858  1.00 35.74  ? 235 ASP B CA  1 
ATOM   5035 C C   . ASP B 1 206 ? 2.414   -7.054  23.986  1.00 32.68  ? 235 ASP B C   1 
ATOM   5036 O O   . ASP B 1 206 ? 3.159   -8.005  24.270  1.00 31.05  ? 235 ASP B O   1 
ATOM   5037 C CB  . ASP B 1 206 ? 1.491   -5.516  25.801  1.00 34.70  ? 235 ASP B CB  1 
ATOM   5038 C CG  . ASP B 1 206 ? 2.580   -5.761  26.840  1.00 39.22  ? 235 ASP B CG  1 
ATOM   5039 O OD1 . ASP B 1 206 ? 2.361   -6.610  27.714  1.00 44.52  ? 235 ASP B OD1 1 
ATOM   5040 O OD2 . ASP B 1 206 ? 3.661   -5.140  26.759  1.00 34.72  ? 235 ASP B OD2 1 
ATOM   5041 N N   . TRP B 1 207 ? 2.601   -6.260  22.920  1.00 32.47  ? 236 TRP B N   1 
ATOM   5042 C CA  . TRP B 1 207 ? 3.669   -6.382  21.919  1.00 26.59  ? 236 TRP B CA  1 
ATOM   5043 C C   . TRP B 1 207 ? 5.045   -6.690  22.545  1.00 26.23  ? 236 TRP B C   1 
ATOM   5044 O O   . TRP B 1 207 ? 5.697   -7.675  22.184  1.00 24.87  ? 236 TRP B O   1 
ATOM   5045 C CB  . TRP B 1 207 ? 3.640   -5.049  21.157  1.00 26.38  ? 236 TRP B CB  1 
ATOM   5046 C CG  . TRP B 1 207 ? 4.432   -4.927  19.890  1.00 26.49  ? 236 TRP B CG  1 
ATOM   5047 C CD1 . TRP B 1 207 ? 4.235   -5.606  18.726  1.00 27.65  ? 236 TRP B CD1 1 
ATOM   5048 C CD2 . TRP B 1 207 ? 5.468   -3.950  19.609  1.00 24.60  ? 236 TRP B CD2 1 
ATOM   5049 N NE1 . TRP B 1 207 ? 5.085   -5.147  17.751  1.00 24.83  ? 236 TRP B NE1 1 
ATOM   5050 C CE2 . TRP B 1 207 ? 5.852   -4.130  18.262  1.00 22.86  ? 236 TRP B CE2 1 
ATOM   5051 C CE3 . TRP B 1 207 ? 6.095   -2.951  20.353  1.00 26.17  ? 236 TRP B CE3 1 
ATOM   5052 C CZ2 . TRP B 1 207 ? 6.835   -3.356  17.652  1.00 24.95  ? 236 TRP B CZ2 1 
ATOM   5053 C CZ3 . TRP B 1 207 ? 7.066   -2.173  19.744  1.00 25.68  ? 236 TRP B CZ3 1 
ATOM   5054 C CH2 . TRP B 1 207 ? 7.416   -2.364  18.406  1.00 24.92  ? 236 TRP B CH2 1 
ATOM   5055 N N   . SER B 1 208 ? 5.437   -5.864  23.539  1.00 28.10  ? 237 SER B N   1 
ATOM   5056 C CA  . SER B 1 208 ? 6.703   -5.951  24.259  1.00 29.90  ? 237 SER B CA  1 
ATOM   5057 C C   . SER B 1 208 ? 6.873   -7.301  24.975  1.00 30.14  ? 237 SER B C   1 
ATOM   5058 O O   . SER B 1 208 ? 7.981   -7.836  25.064  1.00 29.04  ? 237 SER B O   1 
ATOM   5059 C CB  . SER B 1 208 ? 6.862   -4.792  25.263  1.00 26.47  ? 237 SER B CB  1 
ATOM   5060 O OG  . SER B 1 208 ? 6.876   -3.522  24.620  1.00 26.21  ? 237 SER B OG  1 
ATOM   5061 N N   . HIS B 1 209 ? 5.777   -7.847  25.515  1.00 31.28  ? 238 HIS B N   1 
ATOM   5062 C CA  . HIS B 1 209 ? 5.841   -9.085  26.275  1.00 32.11  ? 238 HIS B CA  1 
ATOM   5063 C C   . HIS B 1 209 ? 5.879   -10.255 25.307  1.00 27.70  ? 238 HIS B C   1 
ATOM   5064 O O   . HIS B 1 209 ? 6.595   -11.216 25.545  1.00 31.47  ? 238 HIS B O   1 
ATOM   5065 C CB  . HIS B 1 209 ? 4.714   -9.101  27.325  1.00 38.32  ? 238 HIS B CB  1 
ATOM   5066 C CG  . HIS B 1 209 ? 4.728   -10.241 28.280  1.00 42.20  ? 238 HIS B CG  1 
ATOM   5067 N ND1 . HIS B 1 209 ? 3.698   -10.425 29.179  1.00 42.81  ? 238 HIS B ND1 1 
ATOM   5068 C CD2 . HIS B 1 209 ? 5.608   -11.211 28.521  1.00 44.27  ? 238 HIS B CD2 1 
ATOM   5069 C CE1 . HIS B 1 209 ? 3.957   -11.477 29.928  1.00 43.48  ? 238 HIS B CE1 1 
ATOM   5070 N NE2 . HIS B 1 209 ? 5.116   -11.964 29.554  1.00 46.38  ? 238 HIS B NE2 1 
ATOM   5071 N N   . ASN B 1 210 ? 5.133   -10.169 24.199  1.00 26.94  ? 239 ASN B N   1 
ATOM   5072 C CA  . ASN B 1 210 ? 5.273   -11.153 23.138  1.00 28.20  ? 239 ASN B CA  1 
ATOM   5073 C C   . ASN B 1 210 ? 6.715   -11.128 22.647  1.00 30.17  ? 239 ASN B C   1 
ATOM   5074 O O   . ASN B 1 210 ? 7.316   -12.194 22.451  1.00 26.96  ? 239 ASN B O   1 
ATOM   5075 C CB  . ASN B 1 210 ? 4.253   -11.014 22.014  1.00 29.67  ? 239 ASN B CB  1 
ATOM   5076 C CG  . ASN B 1 210 ? 2.936   -11.672 22.362  1.00 35.84  ? 239 ASN B CG  1 
ATOM   5077 O OD1 . ASN B 1 210 ? 2.934   -12.755 22.968  1.00 38.16  ? 239 ASN B OD1 1 
ATOM   5078 N ND2 . ASN B 1 210 ? 1.824   -11.030 22.023  1.00 33.09  ? 239 ASN B ND2 1 
ATOM   5079 N N   . PHE B 1 211 ? 7.281   -9.911  22.540  1.00 26.64  ? 240 PHE B N   1 
ATOM   5080 C CA  . PHE B 1 211 ? 8.658   -9.767  22.080  1.00 29.53  ? 240 PHE B CA  1 
ATOM   5081 C C   . PHE B 1 211 ? 9.628   -10.486 23.023  1.00 25.67  ? 240 PHE B C   1 
ATOM   5082 O O   . PHE B 1 211 ? 10.430  -11.285 22.562  1.00 26.95  ? 240 PHE B O   1 
ATOM   5083 C CB  . PHE B 1 211 ? 9.014   -8.282  21.876  1.00 26.32  ? 240 PHE B CB  1 
ATOM   5084 C CG  . PHE B 1 211 ? 10.322  -8.031  21.130  1.00 25.58  ? 240 PHE B CG  1 
ATOM   5085 C CD1 . PHE B 1 211 ? 10.898  -9.001  20.328  1.00 22.30  ? 240 PHE B CD1 1 
ATOM   5086 C CD2 . PHE B 1 211 ? 10.979  -6.812  21.263  1.00 27.27  ? 240 PHE B CD2 1 
ATOM   5087 C CE1 . PHE B 1 211 ? 12.124  -8.809  19.754  1.00 21.33  ? 240 PHE B CE1 1 
ATOM   5088 C CE2 . PHE B 1 211 ? 12.162  -6.581  20.601  1.00 24.41  ? 240 PHE B CE2 1 
ATOM   5089 C CZ  . PHE B 1 211 ? 12.728  -7.599  19.855  1.00 25.13  ? 240 PHE B CZ  1 
ATOM   5090 N N   . THR B 1 212 ? 9.581   -10.202 24.329  1.00 24.08  ? 241 THR B N   1 
ATOM   5091 C CA  . THR B 1 212 ? 10.542  -10.796 25.236  1.00 26.24  ? 241 THR B CA  1 
ATOM   5092 C C   . THR B 1 212 ? 10.277  -12.303 25.362  1.00 30.42  ? 241 THR B C   1 
ATOM   5093 O O   . THR B 1 212 ? 11.229  -13.040 25.593  1.00 30.66  ? 241 THR B O   1 
ATOM   5094 C CB  . THR B 1 212 ? 10.595  -10.117 26.605  1.00 24.63  ? 241 THR B CB  1 
ATOM   5095 O OG1 . THR B 1 212 ? 9.277   -10.085 27.121  1.00 25.88  ? 241 THR B OG1 1 
ATOM   5096 C CG2 . THR B 1 212 ? 11.102  -8.682  26.559  1.00 27.55  ? 241 THR B CG2 1 
ATOM   5097 N N   . ASN B 1 213 ? 9.019   -12.763 25.206  1.00 30.07  ? 242 ASN B N   1 
ATOM   5098 C CA  . ASN B 1 213 ? 8.746   -14.199 25.191  1.00 32.04  ? 242 ASN B CA  1 
ATOM   5099 C C   . ASN B 1 213 ? 9.510   -14.887 24.069  1.00 32.74  ? 242 ASN B C   1 
ATOM   5100 O O   . ASN B 1 213 ? 10.138  -15.926 24.272  1.00 30.33  ? 242 ASN B O   1 
ATOM   5101 C CB  . ASN B 1 213 ? 7.273   -14.572 25.019  1.00 34.75  ? 242 ASN B CB  1 
ATOM   5102 C CG  . ASN B 1 213 ? 6.483   -14.466 26.311  1.00 38.23  ? 242 ASN B CG  1 
ATOM   5103 O OD1 . ASN B 1 213 ? 7.034   -14.114 27.365  1.00 35.60  ? 242 ASN B OD1 1 
ATOM   5104 N ND2 . ASN B 1 213 ? 5.182   -14.710 26.239  1.00 35.78  ? 242 ASN B ND2 1 
ATOM   5105 N N   . MET B 1 214 ? 9.446   -14.285 22.881  1.00 31.90  ? 243 MET B N   1 
ATOM   5106 C CA  . MET B 1 214 ? 10.008  -14.890 21.691  1.00 27.60  ? 243 MET B CA  1 
ATOM   5107 C C   . MET B 1 214 ? 11.527  -14.811 21.718  1.00 26.80  ? 243 MET B C   1 
ATOM   5108 O O   . MET B 1 214 ? 12.182  -15.637 21.098  1.00 26.78  ? 243 MET B O   1 
ATOM   5109 C CB  . MET B 1 214 ? 9.483   -14.198 20.434  1.00 29.47  ? 243 MET B CB  1 
ATOM   5110 C CG  . MET B 1 214 ? 8.060   -14.551 20.103  1.00 27.37  ? 243 MET B CG  1 
ATOM   5111 S SD  . MET B 1 214 ? 7.493   -13.729 18.605  1.00 31.47  ? 243 MET B SD  1 
ATOM   5112 C CE  . MET B 1 214 ? 7.404   -12.024 19.166  1.00 28.12  ? 243 MET B CE  1 
ATOM   5113 N N   . LEU B 1 215 ? 12.081  -13.801 22.391  1.00 27.02  ? 244 LEU B N   1 
ATOM   5114 C CA  . LEU B 1 215 ? 13.519  -13.715 22.600  1.00 26.84  ? 244 LEU B CA  1 
ATOM   5115 C C   . LEU B 1 215 ? 14.009  -14.796 23.575  1.00 32.62  ? 244 LEU B C   1 
ATOM   5116 O O   . LEU B 1 215 ? 15.214  -15.020 23.667  1.00 32.96  ? 244 LEU B O   1 
ATOM   5117 C CB  . LEU B 1 215 ? 13.914  -12.346 23.140  1.00 26.07  ? 244 LEU B CB  1 
ATOM   5118 C CG  . LEU B 1 215 ? 13.853  -11.146 22.178  1.00 25.30  ? 244 LEU B CG  1 
ATOM   5119 C CD1 . LEU B 1 215 ? 14.022  -9.884  22.968  1.00 26.28  ? 244 LEU B CD1 1 
ATOM   5120 C CD2 . LEU B 1 215 ? 14.908  -11.205 21.142  1.00 25.22  ? 244 LEU B CD2 1 
ATOM   5121 N N   . GLY B 1 216 ? 13.100  -15.376 24.365  1.00 32.41  ? 245 GLY B N   1 
ATOM   5122 C CA  . GLY B 1 216 ? 13.419  -16.436 25.318  1.00 37.17  ? 245 GLY B CA  1 
ATOM   5123 C C   . GLY B 1 216 ? 13.682  -15.923 26.741  1.00 37.93  ? 245 GLY B C   1 
ATOM   5124 O O   . GLY B 1 216 ? 14.250  -16.643 27.552  1.00 37.78  ? 245 GLY B O   1 
ATOM   5125 N N   . TYR B 1 217 ? 13.272  -14.684 27.038  1.00 34.54  ? 246 TYR B N   1 
ATOM   5126 C CA  . TYR B 1 217 ? 13.430  -14.082 28.349  1.00 35.42  ? 246 TYR B CA  1 
ATOM   5127 C C   . TYR B 1 217 ? 12.145  -14.288 29.154  1.00 38.28  ? 246 TYR B C   1 
ATOM   5128 O O   . TYR B 1 217 ? 11.052  -14.346 28.596  1.00 42.38  ? 246 TYR B O   1 
ATOM   5129 C CB  . TYR B 1 217 ? 13.764  -12.589 28.196  1.00 34.80  ? 246 TYR B CB  1 
ATOM   5130 C CG  . TYR B 1 217 ? 15.193  -12.333 27.737  1.00 31.18  ? 246 TYR B CG  1 
ATOM   5131 C CD1 . TYR B 1 217 ? 15.592  -12.635 26.443  1.00 32.37  ? 246 TYR B CD1 1 
ATOM   5132 C CD2 . TYR B 1 217 ? 16.145  -11.821 28.598  1.00 33.67  ? 246 TYR B CD2 1 
ATOM   5133 C CE1 . TYR B 1 217 ? 16.877  -12.392 26.002  1.00 27.72  ? 246 TYR B CE1 1 
ATOM   5134 C CE2 . TYR B 1 217 ? 17.453  -11.616 28.187  1.00 33.41  ? 246 TYR B CE2 1 
ATOM   5135 C CZ  . TYR B 1 217 ? 17.810  -11.911 26.886  1.00 29.71  ? 246 TYR B CZ  1 
ATOM   5136 O OH  . TYR B 1 217 ? 19.045  -11.694 26.440  1.00 26.85  ? 246 TYR B OH  1 
ATOM   5137 N N   . THR B 1 218 ? 12.285  -14.391 30.476  1.00 41.69  ? 247 THR B N   1 
ATOM   5138 C CA  . THR B 1 218 ? 11.149  -14.482 31.381  1.00 42.82  ? 247 THR B CA  1 
ATOM   5139 C C   . THR B 1 218 ? 11.522  -13.739 32.653  1.00 42.95  ? 247 THR B C   1 
ATOM   5140 O O   . THR B 1 218 ? 11.993  -14.327 33.616  1.00 49.96  ? 247 THR B O   1 
ATOM   5141 C CB  . THR B 1 218 ? 10.809  -15.937 31.701  1.00 50.03  ? 247 THR B CB  1 
ATOM   5142 O OG1 . THR B 1 218 ? 12.018  -16.515 32.196  1.00 54.49  ? 247 THR B OG1 1 
ATOM   5143 C CG2 . THR B 1 218 ? 10.237  -16.668 30.501  1.00 50.92  ? 247 THR B CG2 1 
ATOM   5144 N N   . ASP B 1 219 ? 11.284  -12.439 32.636  1.00 40.57  ? 248 ASP B N   1 
ATOM   5145 C CA  . ASP B 1 219 ? 11.783  -11.544 33.654  1.00 34.22  ? 248 ASP B CA  1 
ATOM   5146 C C   . ASP B 1 219 ? 10.941  -10.283 33.511  1.00 35.53  ? 248 ASP B C   1 
ATOM   5147 O O   . ASP B 1 219 ? 11.011  -9.579  32.494  1.00 32.92  ? 248 ASP B O   1 
ATOM   5148 C CB  . ASP B 1 219 ? 13.275  -11.404 33.451  1.00 37.94  ? 248 ASP B CB  1 
ATOM   5149 C CG  . ASP B 1 219 ? 13.992  -10.386 34.313  1.00 40.53  ? 248 ASP B CG  1 
ATOM   5150 O OD1 . ASP B 1 219 ? 13.343  -9.392  34.685  1.00 39.49  ? 248 ASP B OD1 1 
ATOM   5151 O OD2 . ASP B 1 219 ? 15.211  -10.580 34.535  1.00 43.93  ? 248 ASP B OD2 1 
ATOM   5152 N N   . HIS B 1 220 ? 10.068  -10.075 34.493  1.00 34.22  ? 249 HIS B N   1 
ATOM   5153 C CA  . HIS B 1 220 ? 9.119   -8.982  34.471  1.00 35.35  ? 249 HIS B CA  1 
ATOM   5154 C C   . HIS B 1 220 ? 9.876   -7.678  34.261  1.00 33.88  ? 249 HIS B C   1 
ATOM   5155 O O   . HIS B 1 220 ? 9.433   -6.806  33.522  1.00 33.47  ? 249 HIS B O   1 
ATOM   5156 C CB  . HIS B 1 220 ? 8.250   -8.999  35.737  1.00 39.04  ? 249 HIS B CB  1 
ATOM   5157 C CG  . HIS B 1 220 ? 7.396   -7.774  35.893  1.00 39.25  ? 249 HIS B CG  1 
ATOM   5158 N ND1 . HIS B 1 220 ? 6.410   -7.443  34.992  1.00 36.07  ? 249 HIS B ND1 1 
ATOM   5159 C CD2 . HIS B 1 220 ? 7.428   -6.766  36.782  1.00 39.98  ? 249 HIS B CD2 1 
ATOM   5160 C CE1 . HIS B 1 220 ? 5.819   -6.314  35.376  1.00 35.55  ? 249 HIS B CE1 1 
ATOM   5161 N NE2 . HIS B 1 220 ? 6.417   -5.885  36.460  1.00 37.33  ? 249 HIS B NE2 1 
ATOM   5162 N N   . GLN B 1 221 ? 11.021  -7.528  34.915  1.00 34.18  ? 250 GLN B N   1 
ATOM   5163 C CA  . GLN B 1 221 ? 11.670  -6.234  34.905  1.00 37.27  ? 250 GLN B CA  1 
ATOM   5164 C C   . GLN B 1 221 ? 12.286  -5.978  33.535  1.00 36.72  ? 250 GLN B C   1 
ATOM   5165 O O   . GLN B 1 221 ? 12.281  -4.833  33.099  1.00 35.48  ? 250 GLN B O   1 
ATOM   5166 C CB  . GLN B 1 221 ? 12.700  -6.032  36.012  1.00 44.62  ? 250 GLN B CB  1 
ATOM   5167 C CG  . GLN B 1 221 ? 12.096  -5.684  37.374  1.00 59.81  ? 250 GLN B CG  1 
ATOM   5168 C CD  . GLN B 1 221 ? 10.947  -4.688  37.324  1.00 72.86  ? 250 GLN B CD  1 
ATOM   5169 O OE1 . GLN B 1 221 ? 11.055  -3.582  36.775  1.00 72.79  ? 250 GLN B OE1 1 
ATOM   5170 N NE2 . GLN B 1 221 ? 9.813   -5.071  37.899  1.00 76.03  ? 250 GLN B NE2 1 
ATOM   5171 N N   . PHE B 1 222 ? 12.769  -7.042  32.877  1.00 35.25  ? 251 PHE B N   1 
ATOM   5172 C CA  . PHE B 1 222 ? 13.281  -6.968  31.512  1.00 32.67  ? 251 PHE B CA  1 
ATOM   5173 C C   . PHE B 1 222 ? 12.150  -6.582  30.568  1.00 32.47  ? 251 PHE B C   1 
ATOM   5174 O O   . PHE B 1 222 ? 12.346  -5.725  29.719  1.00 31.66  ? 251 PHE B O   1 
ATOM   5175 C CB  . PHE B 1 222 ? 13.955  -8.245  30.995  1.00 31.48  ? 251 PHE B CB  1 
ATOM   5176 C CG  . PHE B 1 222 ? 14.524  -8.135  29.584  1.00 30.89  ? 251 PHE B CG  1 
ATOM   5177 C CD1 . PHE B 1 222 ? 15.391  -7.107  29.234  1.00 29.22  ? 251 PHE B CD1 1 
ATOM   5178 C CD2 . PHE B 1 222 ? 14.102  -8.993  28.586  1.00 30.78  ? 251 PHE B CD2 1 
ATOM   5179 C CE1 . PHE B 1 222 ? 15.841  -6.969  27.937  1.00 29.18  ? 251 PHE B CE1 1 
ATOM   5180 C CE2 . PHE B 1 222 ? 14.600  -8.885  27.297  1.00 30.72  ? 251 PHE B CE2 1 
ATOM   5181 C CZ  . PHE B 1 222 ? 15.468  -7.867  26.974  1.00 28.45  ? 251 PHE B CZ  1 
ATOM   5182 N N   . THR B 1 223 ? 10.963  -7.187  30.718  1.00 32.74  ? 252 THR B N   1 
ATOM   5183 C CA  . THR B 1 223 ? 9.852   -6.820  29.857  1.00 30.40  ? 252 THR B CA  1 
ATOM   5184 C C   . THR B 1 223 ? 9.500   -5.346  30.103  1.00 33.87  ? 252 THR B C   1 
ATOM   5185 O O   . THR B 1 223 ? 9.169   -4.615  29.160  1.00 32.52  ? 252 THR B O   1 
ATOM   5186 C CB  . THR B 1 223 ? 8.689   -7.779  30.068  1.00 29.46  ? 252 THR B CB  1 
ATOM   5187 O OG1 . THR B 1 223 ? 9.077   -9.061  29.583  1.00 27.37  ? 252 THR B OG1 1 
ATOM   5188 C CG2 . THR B 1 223 ? 7.459   -7.377  29.283  1.00 26.20  ? 252 THR B CG2 1 
ATOM   5189 N N   . GLU B 1 224 ? 9.620   -4.887  31.362  1.00 36.02  ? 253 GLU B N   1 
ATOM   5190 C CA  . GLU B 1 224 ? 9.318   -3.503  31.727  1.00 32.10  ? 253 GLU B CA  1 
ATOM   5191 C C   . GLU B 1 224 ? 10.321  -2.552  31.075  1.00 29.62  ? 253 GLU B C   1 
ATOM   5192 O O   . GLU B 1 224 ? 9.928   -1.491  30.604  1.00 26.44  ? 253 GLU B O   1 
ATOM   5193 C CB  . GLU B 1 224 ? 9.265   -3.307  33.241  1.00 32.11  ? 253 GLU B CB  1 
ATOM   5194 C CG  . GLU B 1 224 ? 7.923   -3.723  33.829  1.00 33.52  ? 253 GLU B CG  1 
ATOM   5195 C CD  . GLU B 1 224 ? 6.773   -2.776  33.492  1.00 35.42  ? 253 GLU B CD  1 
ATOM   5196 O OE1 . GLU B 1 224 ? 5.931   -3.079  32.604  1.00 35.38  ? 253 GLU B OE1 1 
ATOM   5197 O OE2 . GLU B 1 224 ? 6.701   -1.728  34.162  1.00 41.08  ? 253 GLU B OE2 1 
ATOM   5198 N N   . LEU B 1 225 ? 11.608  -2.938  31.044  1.00 29.17  ? 254 LEU B N   1 
ATOM   5199 C CA  . LEU B 1 225 ? 12.631  -2.142  30.395  1.00 29.34  ? 254 LEU B CA  1 
ATOM   5200 C C   . LEU B 1 225 ? 12.364  -2.085  28.887  1.00 24.85  ? 254 LEU B C   1 
ATOM   5201 O O   . LEU B 1 225 ? 12.514  -1.031  28.269  1.00 28.33  ? 254 LEU B O   1 
ATOM   5202 C CB  . LEU B 1 225 ? 14.026  -2.701  30.665  1.00 29.27  ? 254 LEU B CB  1 
ATOM   5203 C CG  . LEU B 1 225 ? 15.145  -2.016  29.872  1.00 27.55  ? 254 LEU B CG  1 
ATOM   5204 C CD1 . LEU B 1 225 ? 15.391  -0.579  30.281  1.00 30.62  ? 254 LEU B CD1 1 
ATOM   5205 C CD2 . LEU B 1 225 ? 16.388  -2.870  30.038  1.00 29.16  ? 254 LEU B CD2 1 
ATOM   5206 N N   . THR B 1 226 ? 11.944  -3.207  28.291  1.00 24.85  ? 255 THR B N   1 
ATOM   5207 C CA  . THR B 1 226 ? 11.680  -3.264  26.861  1.00 23.07  ? 255 THR B CA  1 
ATOM   5208 C C   . THR B 1 226 ? 10.557  -2.295  26.511  1.00 27.91  ? 255 THR B C   1 
ATOM   5209 O O   . THR B 1 226 ? 10.700  -1.500  25.571  1.00 28.64  ? 255 THR B O   1 
ATOM   5210 C CB  . THR B 1 226 ? 11.335  -4.681  26.449  1.00 24.96  ? 255 THR B CB  1 
ATOM   5211 O OG1 . THR B 1 226 ? 12.558  -5.377  26.673  1.00 25.28  ? 255 THR B OG1 1 
ATOM   5212 C CG2 . THR B 1 226 ? 10.896  -4.778  24.999  1.00 27.78  ? 255 THR B CG2 1 
ATOM   5213 N N   . ARG B 1 227 ? 9.481   -2.326  27.312  1.00 22.39  ? 256 ARG B N   1 
ATOM   5214 C CA  . ARG B 1 227 ? 8.370   -1.379  27.181  1.00 24.58  ? 256 ARG B CA  1 
ATOM   5215 C C   . ARG B 1 227 ? 8.878   0.059   27.180  1.00 23.03  ? 256 ARG B C   1 
ATOM   5216 O O   . ARG B 1 227 ? 8.592   0.838   26.266  1.00 28.31  ? 256 ARG B O   1 
ATOM   5217 C CB  . ARG B 1 227 ? 7.315   -1.574  28.273  1.00 26.41  ? 256 ARG B CB  1 
ATOM   5218 C CG  . ARG B 1 227 ? 6.538   -2.872  28.152  1.00 28.31  ? 256 ARG B CG  1 
ATOM   5219 C CD  . ARG B 1 227 ? 5.767   -3.220  29.430  1.00 30.09  ? 256 ARG B CD  1 
ATOM   5220 N NE  . ARG B 1 227 ? 4.947   -4.422  29.217  1.00 31.37  ? 256 ARG B NE  1 
ATOM   5221 C CZ  . ARG B 1 227 ? 4.650   -5.345  30.139  1.00 29.26  ? 256 ARG B CZ  1 
ATOM   5222 N NH1 . ARG B 1 227 ? 5.148   -5.267  31.356  1.00 28.65  ? 256 ARG B NH1 1 
ATOM   5223 N NH2 . ARG B 1 227 ? 3.804   -6.310  29.846  1.00 30.45  ? 256 ARG B NH2 1 
ATOM   5224 N N   . LEU B 1 228 ? 9.655   0.429   28.184  1.00 24.81  ? 257 LEU B N   1 
ATOM   5225 C CA  . LEU B 1 228 ? 10.189  1.780   28.216  1.00 24.23  ? 257 LEU B CA  1 
ATOM   5226 C C   . LEU B 1 228 ? 11.103  2.015   27.001  1.00 25.34  ? 257 LEU B C   1 
ATOM   5227 O O   . LEU B 1 228 ? 11.055  3.075   26.378  1.00 23.93  ? 257 LEU B O   1 
ATOM   5228 C CB  . LEU B 1 228 ? 10.932  1.991   29.535  1.00 28.71  ? 257 LEU B CB  1 
ATOM   5229 C CG  . LEU B 1 228 ? 11.705  3.306   29.638  1.00 31.00  ? 257 LEU B CG  1 
ATOM   5230 C CD1 . LEU B 1 228 ? 10.697  4.416   29.920  1.00 28.26  ? 257 LEU B CD1 1 
ATOM   5231 C CD2 . LEU B 1 228 ? 12.823  3.262   30.661  1.00 37.51  ? 257 LEU B CD2 1 
ATOM   5232 N N   . TYR B 1 229 ? 11.966  1.047   26.670  1.00 24.96  ? 258 TYR B N   1 
ATOM   5233 C CA  . TYR B 1 229 ? 13.002  1.264   25.663  1.00 26.32  ? 258 TYR B CA  1 
ATOM   5234 C C   . TYR B 1 229 ? 12.336  1.494   24.304  1.00 26.77  ? 258 TYR B C   1 
ATOM   5235 O O   . TYR B 1 229 ? 12.714  2.397   23.563  1.00 26.40  ? 258 TYR B O   1 
ATOM   5236 C CB  . TYR B 1 229 ? 14.016  0.110   25.653  1.00 26.85  ? 258 TYR B CB  1 
ATOM   5237 C CG  . TYR B 1 229 ? 15.078  0.216   24.571  1.00 24.97  ? 258 TYR B CG  1 
ATOM   5238 C CD1 . TYR B 1 229 ? 14.741  -0.027  23.260  1.00 30.54  ? 258 TYR B CD1 1 
ATOM   5239 C CD2 . TYR B 1 229 ? 16.408  0.497   24.849  1.00 30.44  ? 258 TYR B CD2 1 
ATOM   5240 C CE1 . TYR B 1 229 ? 15.671  0.056   22.246  1.00 31.91  ? 258 TYR B CE1 1 
ATOM   5241 C CE2 . TYR B 1 229 ? 17.363  0.575   23.846  1.00 29.04  ? 258 TYR B CE2 1 
ATOM   5242 C CZ  . TYR B 1 229 ? 16.982  0.390   22.528  1.00 31.99  ? 258 TYR B CZ  1 
ATOM   5243 O OH  . TYR B 1 229 ? 17.819  0.414   21.437  1.00 35.62  ? 258 TYR B OH  1 
ATOM   5244 N N   . LEU B 1 230 ? 11.331  0.666   23.985  1.00 24.86  ? 259 LEU B N   1 
ATOM   5245 C CA  . LEU B 1 230 ? 10.643  0.738   22.711  1.00 24.10  ? 259 LEU B CA  1 
ATOM   5246 C C   . LEU B 1 230 ? 9.847   2.038   22.621  1.00 22.57  ? 259 LEU B C   1 
ATOM   5247 O O   . LEU B 1 230 ? 9.618   2.550   21.542  1.00 19.90  ? 259 LEU B O   1 
ATOM   5248 C CB  . LEU B 1 230 ? 9.757   -0.490  22.532  1.00 23.04  ? 259 LEU B CB  1 
ATOM   5249 C CG  . LEU B 1 230 ? 10.519  -1.821  22.481  1.00 21.95  ? 259 LEU B CG  1 
ATOM   5250 C CD1 . LEU B 1 230 ? 9.665   -3.056  22.259  1.00 21.09  ? 259 LEU B CD1 1 
ATOM   5251 C CD2 . LEU B 1 230 ? 11.534  -1.727  21.388  1.00 23.34  ? 259 LEU B CD2 1 
ATOM   5252 N N   . THR B 1 231 ? 9.404   2.568   23.760  1.00 22.04  ? 260 THR B N   1 
ATOM   5253 C CA  . THR B 1 231 ? 8.672   3.820   23.770  1.00 23.74  ? 260 THR B CA  1 
ATOM   5254 C C   . THR B 1 231 ? 9.632   4.981   23.470  1.00 21.74  ? 260 THR B C   1 
ATOM   5255 O O   . THR B 1 231 ? 9.321   5.805   22.626  1.00 24.19  ? 260 THR B O   1 
ATOM   5256 C CB  . THR B 1 231 ? 7.905   4.018   25.085  1.00 23.14  ? 260 THR B CB  1 
ATOM   5257 O OG1 . THR B 1 231 ? 6.888   3.014   25.085  1.00 22.65  ? 260 THR B OG1 1 
ATOM   5258 C CG2 . THR B 1 231 ? 7.333   5.427   25.143  1.00 22.85  ? 260 THR B CG2 1 
ATOM   5259 N N   . ILE B 1 232 ? 10.785  5.062   24.124  1.00 24.39  ? 261 ILE B N   1 
ATOM   5260 C CA  . ILE B 1 232 ? 11.568  6.292   24.084  1.00 25.20  ? 261 ILE B CA  1 
ATOM   5261 C C   . ILE B 1 232 ? 12.438  6.412   22.826  1.00 22.27  ? 261 ILE B C   1 
ATOM   5262 O O   . ILE B 1 232 ? 12.840  7.519   22.476  1.00 25.00  ? 261 ILE B O   1 
ATOM   5263 C CB  . ILE B 1 232 ? 12.400  6.524   25.366  1.00 30.46  ? 261 ILE B CB  1 
ATOM   5264 C CG1 . ILE B 1 232 ? 13.533  5.525   25.528  1.00 31.26  ? 261 ILE B CG1 1 
ATOM   5265 C CG2 . ILE B 1 232 ? 11.487  6.586   26.591  1.00 28.44  ? 261 ILE B CG2 1 
ATOM   5266 C CD1 . ILE B 1 232 ? 14.398  5.760   26.758  1.00 33.79  ? 261 ILE B CD1 1 
ATOM   5267 N N   . HIS B 1 233 ? 12.774  5.304   22.170  1.00 20.83  ? 262 HIS B N   1 
ATOM   5268 C CA  . HIS B 1 233 ? 13.548  5.372   20.931  1.00 22.79  ? 262 HIS B CA  1 
ATOM   5269 C C   . HIS B 1 233 ? 12.682  5.520   19.674  1.00 18.20  ? 262 HIS B C   1 
ATOM   5270 O O   . HIS B 1 233 ? 13.212  5.442   18.563  1.00 19.99  ? 262 HIS B O   1 
ATOM   5271 C CB  . HIS B 1 233 ? 14.429  4.120   20.783  1.00 26.55  ? 262 HIS B CB  1 
ATOM   5272 C CG  . HIS B 1 233 ? 15.581  4.066   21.741  1.00 35.13  ? 262 HIS B CG  1 
ATOM   5273 N ND1 . HIS B 1 233 ? 15.465  3.642   23.051  1.00 30.84  ? 262 HIS B ND1 1 
ATOM   5274 C CD2 . HIS B 1 233 ? 16.888  4.361   21.559  1.00 37.39  ? 262 HIS B CD2 1 
ATOM   5275 C CE1 . HIS B 1 233 ? 16.657  3.707   23.636  1.00 33.94  ? 262 HIS B CE1 1 
ATOM   5276 N NE2 . HIS B 1 233 ? 17.536  4.133   22.754  1.00 35.06  ? 262 HIS B NE2 1 
ATOM   5277 N N   . SER B 1 234 ? 11.359  5.696   19.846  1.00 20.82  ? 263 SER B N   1 
ATOM   5278 C CA  . SER B 1 234 ? 10.363  5.448   18.821  1.00 19.91  ? 263 SER B CA  1 
ATOM   5279 C C   . SER B 1 234 ? 10.463  6.476   17.693  1.00 20.02  ? 263 SER B C   1 
ATOM   5280 O O   . SER B 1 234 ? 10.241  6.134   16.551  1.00 18.01  ? 263 SER B O   1 
ATOM   5281 C CB  . SER B 1 234 ? 8.990   5.445   19.420  1.00 19.10  ? 263 SER B CB  1 
ATOM   5282 O OG  . SER B 1 234 ? 8.700   6.717   19.970  1.00 22.31  ? 263 SER B OG  1 
ATOM   5283 N N   . ASP B 1 235 ? 10.769  7.734   18.022  1.00 22.28  ? 264 ASP B N   1 
ATOM   5284 C CA  . ASP B 1 235 ? 10.827  8.803   17.032  1.00 26.00  ? 264 ASP B CA  1 
ATOM   5285 C C   . ASP B 1 235 ? 11.731  9.916   17.532  1.00 23.77  ? 264 ASP B C   1 
ATOM   5286 O O   . ASP B 1 235 ? 11.827  10.155  18.736  1.00 21.38  ? 264 ASP B O   1 
ATOM   5287 C CB  . ASP B 1 235 ? 9.432   9.356   16.788  1.00 26.90  ? 264 ASP B CB  1 
ATOM   5288 C CG  . ASP B 1 235 ? 9.152   9.912   15.396  1.00 29.55  ? 264 ASP B CG  1 
ATOM   5289 O OD1 . ASP B 1 235 ? 9.570   9.265   14.383  1.00 26.99  ? 264 ASP B OD1 1 
ATOM   5290 O OD2 . ASP B 1 235 ? 8.462   10.957  15.340  1.00 31.09  ? 264 ASP B OD2 1 
ATOM   5291 N N   . HIS B 1 236 ? 12.422  10.571  16.608  1.00 21.06  ? 265 HIS B N   1 
ATOM   5292 C CA  . HIS B 1 236 ? 13.296  11.664  16.969  1.00 21.38  ? 265 HIS B CA  1 
ATOM   5293 C C   . HIS B 1 236 ? 13.369  12.703  15.850  1.00 21.36  ? 265 HIS B C   1 
ATOM   5294 O O   . HIS B 1 236 ? 14.454  13.003  15.330  1.00 20.97  ? 265 HIS B O   1 
ATOM   5295 C CB  . HIS B 1 236 ? 14.681  11.144  17.374  1.00 24.08  ? 265 HIS B CB  1 
ATOM   5296 C CG  . HIS B 1 236 ? 15.413  12.133  18.236  1.00 31.75  ? 265 HIS B CG  1 
ATOM   5297 N ND1 . HIS B 1 236 ? 16.212  13.145  17.745  1.00 41.57  ? 265 HIS B ND1 1 
ATOM   5298 C CD2 . HIS B 1 236 ? 15.391  12.305  19.560  1.00 33.63  ? 265 HIS B CD2 1 
ATOM   5299 C CE1 . HIS B 1 236 ? 16.684  13.850  18.765  1.00 42.94  ? 265 HIS B CE1 1 
ATOM   5300 N NE2 . HIS B 1 236 ? 16.192  13.343  19.875  1.00 36.02  ? 265 HIS B NE2 1 
ATOM   5301 N N   . GLU B 1 237 ? 12.208  13.226  15.469  1.00 20.64  ? 266 GLU B N   1 
ATOM   5302 C CA  . GLU B 1 237 ? 12.104  14.185  14.375  1.00 26.70  ? 266 GLU B CA  1 
ATOM   5303 C C   . GLU B 1 237 ? 12.370  13.479  13.041  1.00 26.81  ? 266 GLU B C   1 
ATOM   5304 O O   . GLU B 1 237 ? 12.620  12.270  12.990  1.00 21.07  ? 266 GLU B O   1 
ATOM   5305 C CB  . GLU B 1 237 ? 13.064  15.383  14.485  1.00 27.33  ? 266 GLU B CB  1 
ATOM   5306 C CG  . GLU B 1 237 ? 13.001  16.225  15.760  1.00 35.61  ? 266 GLU B CG  1 
ATOM   5307 C CD  . GLU B 1 237 ? 13.346  17.708  15.528  1.00 39.04  ? 266 GLU B CD  1 
ATOM   5308 O OE1 . GLU B 1 237 ? 14.348  17.965  14.816  1.00 40.00  ? 266 GLU B OE1 1 
ATOM   5309 O OE2 . GLU B 1 237 ? 12.626  18.626  16.016  1.00 31.52  ? 266 GLU B OE2 1 
ATOM   5310 N N   . GLY B 1 238 ? 12.423  14.270  11.960  1.00 25.04  ? 267 GLY B N   1 
ATOM   5311 C CA  . GLY B 1 238 ? 12.452  13.739  10.619  1.00 21.49  ? 267 GLY B CA  1 
ATOM   5312 C C   . GLY B 1 238 ? 13.854  13.660  10.053  1.00 22.83  ? 267 GLY B C   1 
ATOM   5313 O O   . GLY B 1 238 ? 14.029  13.009  9.015   1.00 25.38  ? 267 GLY B O   1 
ATOM   5314 N N   . GLY B 1 239 ? 14.814  14.374  10.667  1.00 22.17  ? 268 GLY B N   1 
ATOM   5315 C CA  . GLY B 1 239 ? 16.082  14.670  10.007  1.00 23.37  ? 268 GLY B CA  1 
ATOM   5316 C C   . GLY B 1 239 ? 17.133  13.612  10.296  1.00 23.52  ? 268 GLY B C   1 
ATOM   5317 O O   . GLY B 1 239 ? 18.210  13.634  9.718   1.00 26.46  ? 268 GLY B O   1 
ATOM   5318 N N   . ASN B 1 240 ? 16.850  12.734  11.257  1.00 22.72  ? 269 ASN B N   1 
ATOM   5319 C CA  . ASN B 1 240 ? 17.770  11.653  11.555  1.00 22.34  ? 269 ASN B CA  1 
ATOM   5320 C C   . ASN B 1 240 ? 17.753  10.732  10.333  1.00 20.92  ? 269 ASN B C   1 
ATOM   5321 O O   . ASN B 1 240 ? 16.786  10.711  9.587   1.00 19.37  ? 269 ASN B O   1 
ATOM   5322 C CB  . ASN B 1 240 ? 17.444  11.012  12.905  1.00 24.12  ? 269 ASN B CB  1 
ATOM   5323 C CG  . ASN B 1 240 ? 16.185  10.177  12.869  1.00 23.44  ? 269 ASN B CG  1 
ATOM   5324 O OD1 . ASN B 1 240 ? 16.164  9.086   12.292  1.00 22.98  ? 269 ASN B OD1 1 
ATOM   5325 N ND2 . ASN B 1 240 ? 15.098  10.668  13.440  1.00 25.35  ? 269 ASN B ND2 1 
ATOM   5326 N N   . VAL B 1 241 ? 18.837  9.996   10.136  1.00 20.88  ? 270 VAL B N   1 
ATOM   5327 C CA  . VAL B 1 241 ? 19.061  9.275   8.907   1.00 20.29  ? 270 VAL B CA  1 
ATOM   5328 C C   . VAL B 1 241 ? 17.994  8.208   8.744   1.00 19.29  ? 270 VAL B C   1 
ATOM   5329 O O   . VAL B 1 241 ? 17.521  8.033   7.641   1.00 18.99  ? 270 VAL B O   1 
ATOM   5330 C CB  . VAL B 1 241 ? 20.469  8.677   8.811   1.00 21.58  ? 270 VAL B CB  1 
ATOM   5331 C CG1 . VAL B 1 241 ? 20.639  7.832   7.535   1.00 23.24  ? 270 VAL B CG1 1 
ATOM   5332 C CG2 . VAL B 1 241 ? 21.497  9.802   8.782   1.00 25.89  ? 270 VAL B CG2 1 
ATOM   5333 N N   . SER B 1 242 ? 17.583  7.532   9.805   1.00 18.97  ? 271 SER B N   1 
ATOM   5334 C CA  . SER B 1 242 ? 16.603  6.464   9.615   1.00 19.72  ? 271 SER B CA  1 
ATOM   5335 C C   . SER B 1 242 ? 15.225  7.033   9.266   1.00 18.28  ? 271 SER B C   1 
ATOM   5336 O O   . SER B 1 242 ? 14.551  6.581   8.342   1.00 18.86  ? 271 SER B O   1 
ATOM   5337 C CB  . SER B 1 242 ? 16.597  5.485   10.786  1.00 21.61  ? 271 SER B CB  1 
ATOM   5338 O OG  . SER B 1 242 ? 16.209  6.068   12.008  1.00 19.48  ? 271 SER B OG  1 
ATOM   5339 N N   . ALA B 1 243 ? 14.801  8.085   9.947   1.00 17.84  ? 272 ALA B N   1 
ATOM   5340 C CA  . ALA B 1 243 ? 13.520  8.702   9.646   1.00 18.16  ? 272 ALA B CA  1 
ATOM   5341 C C   . ALA B 1 243 ? 13.556  9.296   8.247   1.00 15.55  ? 272 ALA B C   1 
ATOM   5342 O O   . ALA B 1 243 ? 12.650  9.084   7.470   1.00 17.84  ? 272 ALA B O   1 
ATOM   5343 C CB  . ALA B 1 243 ? 13.105  9.760   10.680  1.00 17.44  ? 272 ALA B CB  1 
ATOM   5344 N N   . HIS B 1 244 ? 14.607  10.042  7.928   1.00 16.57  ? 273 HIS B N   1 
ATOM   5345 C CA  . HIS B 1 244 ? 14.672  10.687  6.633   1.00 16.95  ? 273 HIS B CA  1 
ATOM   5346 C C   . HIS B 1 244 ? 14.722  9.660   5.492   1.00 16.29  ? 273 HIS B C   1 
ATOM   5347 O O   . HIS B 1 244 ? 14.166  9.892   4.436   1.00 13.62  ? 273 HIS B O   1 
ATOM   5348 C CB  . HIS B 1 244 ? 15.825  11.689  6.613   1.00 18.30  ? 273 HIS B CB  1 
ATOM   5349 C CG  . HIS B 1 244 ? 15.963  12.493  5.394   1.00 17.59  ? 273 HIS B CG  1 
ATOM   5350 N ND1 . HIS B 1 244 ? 17.130  13.188  5.139   1.00 19.10  ? 273 HIS B ND1 1 
ATOM   5351 C CD2 . HIS B 1 244 ? 15.141  12.766  4.386   1.00 22.08  ? 273 HIS B CD2 1 
ATOM   5352 C CE1 . HIS B 1 244 ? 17.000  13.826  3.983   1.00 22.07  ? 273 HIS B CE1 1 
ATOM   5353 N NE2 . HIS B 1 244 ? 15.819  13.550  3.484   1.00 20.32  ? 273 HIS B NE2 1 
ATOM   5354 N N   . THR B 1 245 ? 15.527  8.601   5.633   1.00 16.04  ? 274 THR B N   1 
ATOM   5355 C CA  . THR B 1 245 ? 15.522  7.547   4.629   1.00 16.29  ? 274 THR B CA  1 
ATOM   5356 C C   . THR B 1 245 ? 14.086  7.065   4.439   1.00 15.99  ? 274 THR B C   1 
ATOM   5357 O O   . THR B 1 245 ? 13.623  6.912   3.317   1.00 18.06  ? 274 THR B O   1 
ATOM   5358 C CB  . THR B 1 245 ? 16.483  6.420   5.033   1.00 15.48  ? 274 THR B CB  1 
ATOM   5359 O OG1 . THR B 1 245 ? 17.766  7.024   5.157   1.00 18.99  ? 274 THR B OG1 1 
ATOM   5360 C CG2 . THR B 1 245 ? 16.554  5.321   4.001   1.00 15.67  ? 274 THR B CG2 1 
ATOM   5361 N N   . SER B 1 246 ? 13.329  6.834   5.533   1.00 16.43  ? 275 SER B N   1 
ATOM   5362 C CA  . SER B 1 246 ? 12.023  6.223   5.359   1.00 16.63  ? 275 SER B CA  1 
ATOM   5363 C C   . SER B 1 246 ? 11.119  7.214   4.646   1.00 14.65  ? 275 SER B C   1 
ATOM   5364 O O   . SER B 1 246 ? 10.301  6.856   3.827   1.00 16.82  ? 275 SER B O   1 
ATOM   5365 C CB  . SER B 1 246 ? 11.452  5.797   6.663   1.00 18.45  ? 275 SER B CB  1 
ATOM   5366 O OG  . SER B 1 246 ? 11.049  6.944   7.387   1.00 22.72  ? 275 SER B OG  1 
ATOM   5367 N N   . HIS B 1 247 ? 11.382  8.493   4.888   1.00 15.72  ? 276 HIS B N   1 
ATOM   5368 C CA  . HIS B 1 247 ? 10.567  9.551   4.368   1.00 17.00  ? 276 HIS B CA  1 
ATOM   5369 C C   . HIS B 1 247 ? 10.786  9.645   2.857   1.00 17.28  ? 276 HIS B C   1 
ATOM   5370 O O   . HIS B 1 247 ? 9.839   9.759   2.067   1.00 16.87  ? 276 HIS B O   1 
ATOM   5371 C CB  . HIS B 1 247 ? 10.929  10.821  5.155   1.00 18.43  ? 276 HIS B CB  1 
ATOM   5372 C CG  . HIS B 1 247 ? 10.077  11.986  4.817   1.00 21.70  ? 276 HIS B CG  1 
ATOM   5373 N ND1 . HIS B 1 247 ? 8.768   12.168  5.235   1.00 24.42  ? 276 HIS B ND1 1 
ATOM   5374 C CD2 . HIS B 1 247 ? 10.375  13.036  4.016   1.00 25.02  ? 276 HIS B CD2 1 
ATOM   5375 C CE1 . HIS B 1 247 ? 8.302   13.300  4.711   1.00 23.72  ? 276 HIS B CE1 1 
ATOM   5376 N NE2 . HIS B 1 247 ? 9.265   13.844  3.965   1.00 23.21  ? 276 HIS B NE2 1 
ATOM   5377 N N   . LEU B 1 248 ? 12.059  9.547   2.495   1.00 16.67  ? 277 LEU B N   1 
ATOM   5378 C CA  . LEU B 1 248 ? 12.514  9.748   1.144   1.00 15.60  ? 277 LEU B CA  1 
ATOM   5379 C C   . LEU B 1 248 ? 12.082  8.593   0.248   1.00 15.60  ? 277 LEU B C   1 
ATOM   5380 O O   . LEU B 1 248 ? 11.536  8.802   -0.832  1.00 13.46  ? 277 LEU B O   1 
ATOM   5381 C CB  . LEU B 1 248 ? 14.033  9.841   1.261   1.00 18.12  ? 277 LEU B CB  1 
ATOM   5382 C CG  . LEU B 1 248 ? 14.783  9.775   -0.072  1.00 18.27  ? 277 LEU B CG  1 
ATOM   5383 C CD1 . LEU B 1 248 ? 14.302  10.843  -1.000  1.00 21.33  ? 277 LEU B CD1 1 
ATOM   5384 C CD2 . LEU B 1 248 ? 16.238  9.905   0.229   1.00 21.39  ? 277 LEU B CD2 1 
ATOM   5385 N N   . VAL B 1 249 ? 12.342  7.361   0.724   1.00 16.95  ? 278 VAL B N   1 
ATOM   5386 C CA  . VAL B 1 249 ? 11.978  6.178   -0.024  1.00 16.29  ? 278 VAL B CA  1 
ATOM   5387 C C   . VAL B 1 249 ? 10.459  6.086   -0.097  1.00 18.60  ? 278 VAL B C   1 
ATOM   5388 O O   . VAL B 1 249 ? 9.915   5.765   -1.154  1.00 16.87  ? 278 VAL B O   1 
ATOM   5389 C CB  . VAL B 1 249 ? 12.639  4.922   0.582   1.00 15.72  ? 278 VAL B CB  1 
ATOM   5390 C CG1 . VAL B 1 249 ? 12.016  3.593   0.150   1.00 16.06  ? 278 VAL B CG1 1 
ATOM   5391 C CG2 . VAL B 1 249 ? 14.147  4.937   0.335   1.00 14.50  ? 278 VAL B CG2 1 
ATOM   5392 N N   . GLY B 1 250 ? 9.784   6.392   1.012   1.00 18.04  ? 279 GLY B N   1 
ATOM   5393 C CA  . GLY B 1 250 ? 8.329   6.403   1.035   1.00 18.04  ? 279 GLY B CA  1 
ATOM   5394 C C   . GLY B 1 250 ? 7.718   7.403   0.042   1.00 18.25  ? 279 GLY B C   1 
ATOM   5395 O O   . GLY B 1 250 ? 6.651   7.164   -0.450  1.00 16.03  ? 279 GLY B O   1 
ATOM   5396 N N   . SER B 1 251 ? 8.352   8.559   -0.167  1.00 17.37  ? 280 SER B N   1 
ATOM   5397 C CA  . SER B 1 251 ? 7.853   9.591   -1.058  1.00 17.14  ? 280 SER B CA  1 
ATOM   5398 C C   . SER B 1 251 ? 7.842   9.134   -2.521  1.00 16.51  ? 280 SER B C   1 
ATOM   5399 O O   . SER B 1 251 ? 7.133   9.708   -3.344  1.00 17.85  ? 280 SER B O   1 
ATOM   5400 C CB  . SER B 1 251 ? 8.704   10.821  -0.926  1.00 18.62  ? 280 SER B CB  1 
ATOM   5401 O OG  . SER B 1 251 ? 9.917   10.671  -1.676  1.00 17.29  ? 280 SER B OG  1 
ATOM   5402 N N   . ALA B 1 252 ? 8.599   8.106   -2.870  1.00 17.75  ? 281 ALA B N   1 
ATOM   5403 C CA  . ALA B 1 252 ? 8.474   7.501   -4.195  1.00 19.45  ? 281 ALA B CA  1 
ATOM   5404 C C   . ALA B 1 252 ? 7.322   6.487   -4.230  1.00 19.36  ? 281 ALA B C   1 
ATOM   5405 O O   . ALA B 1 252 ? 7.163   5.808   -5.232  1.00 18.61  ? 281 ALA B O   1 
ATOM   5406 C CB  . ALA B 1 252 ? 9.764   6.806   -4.616  1.00 20.84  ? 281 ALA B CB  1 
ATOM   5407 N N   . LEU B 1 253 ? 6.577   6.333   -3.114  1.00 18.53  ? 282 LEU B N   1 
ATOM   5408 C CA  . LEU B 1 253 ? 5.432   5.443   -3.023  1.00 18.50  ? 282 LEU B CA  1 
ATOM   5409 C C   . LEU B 1 253 ? 5.905   3.988   -2.917  1.00 21.90  ? 282 LEU B C   1 
ATOM   5410 O O   . LEU B 1 253 ? 5.143   3.073   -3.230  1.00 20.58  ? 282 LEU B O   1 
ATOM   5411 C CB  . LEU B 1 253 ? 4.413   5.641   -4.151  1.00 21.32  ? 282 LEU B CB  1 
ATOM   5412 C CG  . LEU B 1 253 ? 3.649   6.976   -4.208  1.00 22.88  ? 282 LEU B CG  1 
ATOM   5413 C CD1 . LEU B 1 253 ? 2.454   6.880   -5.178  1.00 25.14  ? 282 LEU B CD1 1 
ATOM   5414 C CD2 . LEU B 1 253 ? 3.234   7.445   -2.841  1.00 21.47  ? 282 LEU B CD2 1 
ATOM   5415 N N   . SER B 1 254 ? 7.168   3.781   -2.529  1.00 18.47  ? 283 SER B N   1 
ATOM   5416 C CA  . SER B 1 254 ? 7.590   2.476   -2.040  1.00 22.88  ? 283 SER B CA  1 
ATOM   5417 C C   . SER B 1 254 ? 6.785   2.163   -0.785  1.00 24.39  ? 283 SER B C   1 
ATOM   5418 O O   . SER B 1 254 ? 6.538   3.061   0.020   1.00 22.64  ? 283 SER B O   1 
ATOM   5419 C CB  . SER B 1 254 ? 9.052   2.455   -1.730  1.00 24.85  ? 283 SER B CB  1 
ATOM   5420 O OG  . SER B 1 254 ? 9.838   2.708   -2.885  1.00 24.97  ? 283 SER B OG  1 
ATOM   5421 N N   . ASP B 1 255 ? 6.398   0.895   -0.630  1.00 21.96  ? 284 ASP B N   1 
ATOM   5422 C CA  . ASP B 1 255 ? 5.524   0.479   0.451   1.00 21.80  ? 284 ASP B CA  1 
ATOM   5423 C C   . ASP B 1 255 ? 6.235   0.484   1.806   1.00 19.14  ? 284 ASP B C   1 
ATOM   5424 O O   . ASP B 1 255 ? 7.449   0.671   1.881   1.00 20.38  ? 284 ASP B O   1 
ATOM   5425 C CB  . ASP B 1 255 ? 4.928   -0.876  0.112   1.00 22.53  ? 284 ASP B CB  1 
ATOM   5426 C CG  . ASP B 1 255 ? 5.960   -1.989  0.014   1.00 27.15  ? 284 ASP B CG  1 
ATOM   5427 O OD1 . ASP B 1 255 ? 6.708   -2.165  0.993   1.00 28.72  ? 284 ASP B OD1 1 
ATOM   5428 O OD2 . ASP B 1 255 ? 6.024   -2.648  -1.050  1.00 27.27  ? 284 ASP B OD2 1 
ATOM   5429 N N   . PRO B 1 256 ? 5.524   0.329   2.946   1.00 17.62  ? 285 PRO B N   1 
ATOM   5430 C CA  . PRO B 1 256 ? 6.163   0.437   4.233   1.00 19.98  ? 285 PRO B CA  1 
ATOM   5431 C C   . PRO B 1 256 ? 7.323   -0.549  4.397   1.00 16.93  ? 285 PRO B C   1 
ATOM   5432 O O   . PRO B 1 256 ? 8.267   -0.254  5.109   1.00 17.32  ? 285 PRO B O   1 
ATOM   5433 C CB  . PRO B 1 256 ? 5.010   0.265   5.242   1.00 19.82  ? 285 PRO B CB  1 
ATOM   5434 C CG  . PRO B 1 256 ? 3.782   0.674   4.443   1.00 20.88  ? 285 PRO B CG  1 
ATOM   5435 C CD  . PRO B 1 256 ? 4.086   0.058   3.070   1.00 21.76  ? 285 PRO B CD  1 
ATOM   5436 N N   . TYR B 1 257 ? 7.237   -1.742  3.824   1.00 17.31  ? 286 TYR B N   1 
ATOM   5437 C CA  . TYR B 1 257 ? 8.312   -2.708  4.024   1.00 18.44  ? 286 TYR B CA  1 
ATOM   5438 C C   . TYR B 1 257 ? 9.614   -2.203  3.384   1.00 17.35  ? 286 TYR B C   1 
ATOM   5439 O O   . TYR B 1 257 ? 10.665  -2.182  4.025   1.00 18.73  ? 286 TYR B O   1 
ATOM   5440 C CB  . TYR B 1 257 ? 7.966   -4.082  3.461   1.00 18.60  ? 286 TYR B CB  1 
ATOM   5441 C CG  . TYR B 1 257 ? 6.760   -4.721  4.115   1.00 21.33  ? 286 TYR B CG  1 
ATOM   5442 C CD1 . TYR B 1 257 ? 6.894   -5.515  5.254   1.00 24.22  ? 286 TYR B CD1 1 
ATOM   5443 C CD2 . TYR B 1 257 ? 5.481   -4.475  3.646   1.00 25.47  ? 286 TYR B CD2 1 
ATOM   5444 C CE1 . TYR B 1 257 ? 5.799   -6.103  5.867   1.00 23.52  ? 286 TYR B CE1 1 
ATOM   5445 C CE2 . TYR B 1 257 ? 4.377   -5.074  4.245   1.00 25.05  ? 286 TYR B CE2 1 
ATOM   5446 C CZ  . TYR B 1 257 ? 4.538   -5.893  5.352   1.00 26.00  ? 286 TYR B CZ  1 
ATOM   5447 O OH  . TYR B 1 257 ? 3.444   -6.490  5.947   1.00 25.59  ? 286 TYR B OH  1 
ATOM   5448 N N   . LEU B 1 258 ? 9.544   -1.786  2.115   1.00 16.73  ? 287 LEU B N   1 
ATOM   5449 C CA  . LEU B 1 258 ? 10.737  -1.262  1.484   1.00 20.43  ? 287 LEU B CA  1 
ATOM   5450 C C   . LEU B 1 258 ? 11.269  -0.005  2.201   1.00 19.23  ? 287 LEU B C   1 
ATOM   5451 O O   . LEU B 1 258 ? 12.474  0.147   2.324   1.00 20.09  ? 287 LEU B O   1 
ATOM   5452 C CB  . LEU B 1 258 ? 10.377  -0.960  0.031   1.00 21.00  ? 287 LEU B CB  1 
ATOM   5453 C CG  . LEU B 1 258 ? 9.961   -2.171  -0.819  1.00 19.59  ? 287 LEU B CG  1 
ATOM   5454 C CD1 . LEU B 1 258 ? 9.691   -1.829  -2.272  1.00 21.78  ? 287 LEU B CD1 1 
ATOM   5455 C CD2 . LEU B 1 258 ? 11.002  -3.248  -0.708  1.00 19.02  ? 287 LEU B CD2 1 
ATOM   5456 N N   . SER B 1 259 ? 10.390  0.940   2.565   1.00 19.30  ? 288 SER B N   1 
ATOM   5457 C CA  . SER B 1 259 ? 10.782  2.187   3.236   1.00 19.98  ? 288 SER B CA  1 
ATOM   5458 C C   . SER B 1 259 ? 11.457  1.907   4.572   1.00 22.19  ? 288 SER B C   1 
ATOM   5459 O O   . SER B 1 259 ? 12.416  2.572   4.936   1.00 22.46  ? 288 SER B O   1 
ATOM   5460 C CB  . SER B 1 259 ? 9.580   3.077   3.477   1.00 21.80  ? 288 SER B CB  1 
ATOM   5461 O OG  . SER B 1 259 ? 8.932   3.263   2.243   1.00 24.22  ? 288 SER B OG  1 
ATOM   5462 N N   . PHE B 1 260 ? 10.934  0.925   5.301   1.00 18.32  ? 289 PHE B N   1 
ATOM   5463 C CA  . PHE B 1 260 ? 11.467  0.627   6.613   1.00 19.44  ? 289 PHE B CA  1 
ATOM   5464 C C   . PHE B 1 260 ? 12.799  -0.101  6.440   1.00 18.23  ? 289 PHE B C   1 
ATOM   5465 O O   . PHE B 1 260 ? 13.777  0.212   7.119   1.00 14.91  ? 289 PHE B O   1 
ATOM   5466 C CB  . PHE B 1 260 ? 10.435  -0.119  7.469   1.00 20.27  ? 289 PHE B CB  1 
ATOM   5467 C CG  . PHE B 1 260 ? 10.969  -0.394  8.862   1.00 21.48  ? 289 PHE B CG  1 
ATOM   5468 C CD1 . PHE B 1 260 ? 11.068  0.631   9.786   1.00 18.94  ? 289 PHE B CD1 1 
ATOM   5469 C CD2 . PHE B 1 260 ? 11.440  -1.646  9.218   1.00 20.51  ? 289 PHE B CD2 1 
ATOM   5470 C CE1 . PHE B 1 260 ? 11.640  0.392   11.009  1.00 22.72  ? 289 PHE B CE1 1 
ATOM   5471 C CE2 . PHE B 1 260 ? 12.020  -1.852  10.454  1.00 21.20  ? 289 PHE B CE2 1 
ATOM   5472 C CZ  . PHE B 1 260 ? 12.118  -0.851  11.336  1.00 19.90  ? 289 PHE B CZ  1 
ATOM   5473 N N   . ALA B 1 261 ? 12.884  -1.023  5.476   1.00 16.56  ? 290 ALA B N   1 
ATOM   5474 C CA  . ALA B 1 261 ? 14.139  -1.747  5.339   1.00 17.92  ? 290 ALA B CA  1 
ATOM   5475 C C   . ALA B 1 261 ? 15.246  -0.774  4.935   1.00 17.07  ? 290 ALA B C   1 
ATOM   5476 O O   . ALA B 1 261 ? 16.364  -0.927  5.370   1.00 17.99  ? 290 ALA B O   1 
ATOM   5477 C CB  . ALA B 1 261 ? 14.010  -2.876  4.360   1.00 21.02  ? 290 ALA B CB  1 
ATOM   5478 N N   . ALA B 1 262 ? 14.952  0.193   4.057   1.00 20.03  ? 291 ALA B N   1 
ATOM   5479 C CA  . ALA B 1 262 ? 15.949  1.187   3.678   1.00 20.50  ? 291 ALA B CA  1 
ATOM   5480 C C   . ALA B 1 262 ? 16.370  1.929   4.921   1.00 20.44  ? 291 ALA B C   1 
ATOM   5481 O O   . ALA B 1 262 ? 17.550  2.179   5.079   1.00 18.58  ? 291 ALA B O   1 
ATOM   5482 C CB  . ALA B 1 262 ? 15.429  2.164   2.651   1.00 19.57  ? 291 ALA B CB  1 
ATOM   5483 N N   . ALA B 1 263 ? 15.391  2.323   5.754   1.00 19.20  ? 292 ALA B N   1 
ATOM   5484 C CA  . ALA B 1 263 ? 15.703  3.001   7.010   1.00 18.17  ? 292 ALA B CA  1 
ATOM   5485 C C   . ALA B 1 263 ? 16.663  2.204   7.892   1.00 17.89  ? 292 ALA B C   1 
ATOM   5486 O O   . ALA B 1 263 ? 17.472  2.775   8.590   1.00 17.42  ? 292 ALA B O   1 
ATOM   5487 C CB  . ALA B 1 263 ? 14.456  3.296   7.822   1.00 18.84  ? 292 ALA B CB  1 
ATOM   5488 N N   . MET B 1 264 ? 16.506  0.885   7.927   1.00 18.12  ? 293 MET B N   1 
ATOM   5489 C CA  . MET B 1 264 ? 17.344  0.058   8.771   1.00 19.06  ? 293 MET B CA  1 
ATOM   5490 C C   . MET B 1 264 ? 18.766  0.004   8.238   1.00 18.47  ? 293 MET B C   1 
ATOM   5491 O O   . MET B 1 264 ? 19.708  -0.009  9.004   1.00 21.78  ? 293 MET B O   1 
ATOM   5492 C CB  . MET B 1 264 ? 16.742  -1.343  8.881   1.00 19.26  ? 293 MET B CB  1 
ATOM   5493 C CG  . MET B 1 264 ? 15.433  -1.313  9.632   1.00 19.26  ? 293 MET B CG  1 
ATOM   5494 S SD  . MET B 1 264 ? 15.554  -0.738  11.331  1.00 22.28  ? 293 MET B SD  1 
ATOM   5495 C CE  . MET B 1 264 ? 14.999  0.958   11.183  1.00 23.74  ? 293 MET B CE  1 
ATOM   5496 N N   . ASN B 1 265 ? 18.921  0.029   6.927   1.00 17.10  ? 294 ASN B N   1 
ATOM   5497 C CA  . ASN B 1 265 ? 20.242  0.207   6.336   1.00 20.83  ? 294 ASN B CA  1 
ATOM   5498 C C   . ASN B 1 265 ? 20.869  1.541   6.747   1.00 20.00  ? 294 ASN B C   1 
ATOM   5499 O O   . ASN B 1 265 ? 22.067  1.629   6.952   1.00 20.60  ? 294 ASN B O   1 
ATOM   5500 C CB  . ASN B 1 265 ? 20.174  0.084   4.822   1.00 22.42  ? 294 ASN B CB  1 
ATOM   5501 C CG  . ASN B 1 265 ? 20.046  -1.350  4.343   1.00 23.99  ? 294 ASN B CG  1 
ATOM   5502 O OD1 . ASN B 1 265 ? 19.847  -2.290  5.111   1.00 20.51  ? 294 ASN B OD1 1 
ATOM   5503 N ND2 . ASN B 1 265 ? 20.104  -1.526  3.045   1.00 25.75  ? 294 ASN B ND2 1 
ATOM   5504 N N   . GLY B 1 266 ? 20.070  2.587   6.899   1.00 19.73  ? 295 GLY B N   1 
ATOM   5505 C CA  . GLY B 1 266 ? 20.572  3.853   7.385   1.00 20.55  ? 295 GLY B CA  1 
ATOM   5506 C C   . GLY B 1 266 ? 20.917  3.789   8.869   1.00 22.40  ? 295 GLY B C   1 
ATOM   5507 O O   . GLY B 1 266 ? 22.010  4.202   9.285   1.00 22.62  ? 295 GLY B O   1 
ATOM   5508 N N   . LEU B 1 267 ? 20.034  3.180   9.656   1.00 19.02  ? 296 LEU B N   1 
ATOM   5509 C CA  . LEU B 1 267 ? 20.292  2.969   11.077  1.00 21.97  ? 296 LEU B CA  1 
ATOM   5510 C C   . LEU B 1 267 ? 21.539  2.123   11.338  1.00 20.14  ? 296 LEU B C   1 
ATOM   5511 O O   . LEU B 1 267 ? 22.120  2.224   12.406  1.00 22.66  ? 296 LEU B O   1 
ATOM   5512 C CB  . LEU B 1 267 ? 19.096  2.305   11.741  1.00 22.99  ? 296 LEU B CB  1 
ATOM   5513 C CG  . LEU B 1 267 ? 19.126  2.283   13.270  1.00 23.56  ? 296 LEU B CG  1 
ATOM   5514 C CD1 . LEU B 1 267 ? 19.262  3.720   13.793  1.00 25.12  ? 296 LEU B CD1 1 
ATOM   5515 C CD2 . LEU B 1 267 ? 17.861  1.615   13.730  1.00 22.38  ? 296 LEU B CD2 1 
ATOM   5516 N N   . ALA B 1 268 ? 21.923  1.291   10.371  1.00 21.28  ? 297 ALA B N   1 
ATOM   5517 C CA  . ALA B 1 268 ? 23.003  0.329   10.543  1.00 22.41  ? 297 ALA B CA  1 
ATOM   5518 C C   . ALA B 1 268 ? 24.328  1.064   10.451  1.00 20.59  ? 297 ALA B C   1 
ATOM   5519 O O   . ALA B 1 268 ? 25.350  0.485   10.818  1.00 24.67  ? 297 ALA B O   1 
ATOM   5520 C CB  . ALA B 1 268 ? 22.952  -0.816  9.534   1.00 20.53  ? 297 ALA B CB  1 
ATOM   5521 N N   . GLY B 1 269 ? 24.287  2.311   9.991   1.00 20.22  ? 298 GLY B N   1 
ATOM   5522 C CA  . GLY B 1 269 ? 25.493  3.088   9.787   1.00 23.61  ? 298 GLY B CA  1 
ATOM   5523 C C   . GLY B 1 269 ? 26.155  3.424   11.124  1.00 24.76  ? 298 GLY B C   1 
ATOM   5524 O O   . GLY B 1 269 ? 25.475  3.831   12.069  1.00 25.36  ? 298 GLY B O   1 
ATOM   5525 N N   . PRO B 1 270 ? 27.491  3.320   11.252  1.00 24.25  ? 299 PRO B N   1 
ATOM   5526 C CA  . PRO B 1 270 ? 28.147  3.689   12.509  1.00 31.93  ? 299 PRO B CA  1 
ATOM   5527 C C   . PRO B 1 270 ? 27.859  5.088   13.066  1.00 32.77  ? 299 PRO B C   1 
ATOM   5528 O O   . PRO B 1 270 ? 27.816  5.256   14.283  1.00 37.69  ? 299 PRO B O   1 
ATOM   5529 C CB  . PRO B 1 270 ? 29.662  3.441   12.279  1.00 33.82  ? 299 PRO B CB  1 
ATOM   5530 C CG  . PRO B 1 270 ? 29.790  2.840   10.878  1.00 28.77  ? 299 PRO B CG  1 
ATOM   5531 C CD  . PRO B 1 270 ? 28.406  2.757   10.265  1.00 28.20  ? 299 PRO B CD  1 
ATOM   5532 N N   . LEU B 1 271 ? 27.610  6.093   12.229  1.00 31.99  ? 300 LEU B N   1 
ATOM   5533 C CA  . LEU B 1 271 ? 27.304  7.413   12.774  1.00 33.52  ? 300 LEU B CA  1 
ATOM   5534 C C   . LEU B 1 271 ? 25.823  7.608   13.114  1.00 37.01  ? 300 LEU B C   1 
ATOM   5535 O O   . LEU B 1 271 ? 25.420  8.742   13.384  1.00 36.05  ? 300 LEU B O   1 
ATOM   5536 C CB  . LEU B 1 271 ? 27.746  8.464   11.763  1.00 29.32  ? 300 LEU B CB  1 
ATOM   5537 C CG  . LEU B 1 271 ? 29.251  8.567   11.550  1.00 30.34  ? 300 LEU B CG  1 
ATOM   5538 C CD1 . LEU B 1 271 ? 29.543  9.805   10.703  1.00 33.23  ? 300 LEU B CD1 1 
ATOM   5539 C CD2 . LEU B 1 271 ? 30.020  8.620   12.861  1.00 33.91  ? 300 LEU B CD2 1 
ATOM   5540 N N   . HIS B 1 272 ? 25.022  6.533   13.038  1.00 43.19  ? 301 HIS B N   1 
ATOM   5541 C CA  . HIS B 1 272 ? 23.626  6.547   13.474  1.00 51.12  ? 301 HIS B CA  1 
ATOM   5542 C C   . HIS B 1 272 ? 23.371  5.530   14.605  1.00 50.89  ? 301 HIS B C   1 
ATOM   5543 O O   . HIS B 1 272 ? 23.011  5.895   15.724  1.00 56.40  ? 301 HIS B O   1 
ATOM   5544 C CB  . HIS B 1 272 ? 22.696  6.354   12.265  1.00 52.49  ? 301 HIS B CB  1 
ATOM   5545 C CG  . HIS B 1 272 ? 21.285  6.789   12.514  1.00 47.37  ? 301 HIS B CG  1 
ATOM   5546 N ND1 . HIS B 1 272 ? 20.968  7.738   13.451  1.00 47.32  ? 301 HIS B ND1 1 
ATOM   5547 C CD2 . HIS B 1 272 ? 20.110  6.425   11.966  1.00 52.52  ? 301 HIS B CD2 1 
ATOM   5548 C CE1 . HIS B 1 272 ? 19.653  7.925   13.479  1.00 52.11  ? 301 HIS B CE1 1 
ATOM   5549 N NE2 . HIS B 1 272 ? 19.102  7.133   12.586  1.00 47.53  ? 301 HIS B NE2 1 
ATOM   5550 N N   . GLY B 1 273 ? 23.554  4.235   14.338  1.00 47.37  ? 302 GLY B N   1 
ATOM   5551 C CA  . GLY B 1 273 ? 22.946  3.230   15.190  1.00 50.90  ? 302 GLY B CA  1 
ATOM   5552 C C   . GLY B 1 273 ? 23.906  2.512   16.141  1.00 52.77  ? 302 GLY B C   1 
ATOM   5553 O O   . GLY B 1 273 ? 23.432  1.631   16.860  1.00 54.26  ? 302 GLY B O   1 
ATOM   5554 N N   . LEU B 1 274 ? 25.207  2.874   16.180  1.00 51.56  ? 303 LEU B N   1 
ATOM   5555 C CA  . LEU B 1 274 ? 26.203  2.088   16.912  1.00 53.17  ? 303 LEU B CA  1 
ATOM   5556 C C   . LEU B 1 274 ? 26.668  2.759   18.211  1.00 51.79  ? 303 LEU B C   1 
ATOM   5557 O O   . LEU B 1 274 ? 27.604  2.284   18.853  1.00 55.76  ? 303 LEU B O   1 
ATOM   5558 C CB  . LEU B 1 274 ? 27.406  1.750   16.031  1.00 52.83  ? 303 LEU B CB  1 
ATOM   5559 C CG  . LEU B 1 274 ? 27.325  0.392   15.321  1.00 62.35  ? 303 LEU B CG  1 
ATOM   5560 C CD1 . LEU B 1 274 ? 26.632  0.518   13.958  1.00 56.08  ? 303 LEU B CD1 1 
ATOM   5561 C CD2 . LEU B 1 274 ? 28.696  -0.281  15.202  1.00 60.13  ? 303 LEU B CD2 1 
ATOM   5562 N N   . ALA B 1 275 ? 26.015  3.841   18.624  1.00 50.87  ? 304 ALA B N   1 
ATOM   5563 C CA  . ALA B 1 275 ? 26.475  4.605   19.774  1.00 50.14  ? 304 ALA B CA  1 
ATOM   5564 C C   . ALA B 1 275 ? 26.326  3.787   21.053  1.00 49.00  ? 304 ALA B C   1 
ATOM   5565 O O   . ALA B 1 275 ? 27.123  3.940   21.971  1.00 52.96  ? 304 ALA B O   1 
ATOM   5566 C CB  . ALA B 1 275 ? 25.691  5.897   19.873  1.00 49.80  ? 304 ALA B CB  1 
ATOM   5567 N N   . ASN B 1 276 ? 25.282  2.951   21.103  1.00 41.19  ? 305 ASN B N   1 
ATOM   5568 C CA  . ASN B 1 276 ? 24.969  2.120   22.251  1.00 45.31  ? 305 ASN B CA  1 
ATOM   5569 C C   . ASN B 1 276 ? 26.160  1.223   22.591  1.00 44.57  ? 305 ASN B C   1 
ATOM   5570 O O   . ASN B 1 276 ? 26.601  1.161   23.745  1.00 38.50  ? 305 ASN B O   1 
ATOM   5571 C CB  . ASN B 1 276 ? 23.690  1.317   22.007  1.00 44.77  ? 305 ASN B CB  1 
ATOM   5572 C CG  . ASN B 1 276 ? 23.273  0.523   23.226  1.00 47.03  ? 305 ASN B CG  1 
ATOM   5573 O OD1 . ASN B 1 276 ? 24.103  0.213   24.090  1.00 46.87  ? 305 ASN B OD1 1 
ATOM   5574 N ND2 . ASN B 1 276 ? 22.003  0.161   23.315  1.00 40.54  ? 305 ASN B ND2 1 
ATOM   5575 N N   . GLN B 1 277 ? 26.672  0.539   21.565  1.00 43.83  ? 306 GLN B N   1 
ATOM   5576 C CA  . GLN B 1 277 ? 27.722  -0.458  21.723  1.00 47.36  ? 306 GLN B CA  1 
ATOM   5577 C C   . GLN B 1 277 ? 29.065  0.181   22.085  1.00 45.16  ? 306 GLN B C   1 
ATOM   5578 O O   . GLN B 1 277 ? 29.765  -0.307  22.976  1.00 35.20  ? 306 GLN B O   1 
ATOM   5579 C CB  . GLN B 1 277 ? 27.753  -1.277  20.432  1.00 51.56  ? 306 GLN B CB  1 
ATOM   5580 C CG  . GLN B 1 277 ? 26.398  -1.901  20.102  1.00 55.20  ? 306 GLN B CG  1 
ATOM   5581 C CD  . GLN B 1 277 ? 25.532  -1.133  19.114  1.00 57.74  ? 306 GLN B CD  1 
ATOM   5582 O OE1 . GLN B 1 277 ? 25.135  0.023   19.342  1.00 44.93  ? 306 GLN B OE1 1 
ATOM   5583 N NE2 . GLN B 1 277 ? 25.167  -1.818  18.030  1.00 56.75  ? 306 GLN B NE2 1 
ATOM   5584 N N   . GLU B 1 278 ? 29.433  1.261   21.389  1.00 49.12  ? 307 GLU B N   1 
ATOM   5585 C CA  . GLU B 1 278 ? 30.615  2.048   21.733  1.00 51.77  ? 307 GLU B CA  1 
ATOM   5586 C C   . GLU B 1 278 ? 30.712  2.290   23.243  1.00 49.88  ? 307 GLU B C   1 
ATOM   5587 O O   . GLU B 1 278 ? 31.730  1.997   23.873  1.00 46.38  ? 307 GLU B O   1 
ATOM   5588 C CB  . GLU B 1 278 ? 30.539  3.437   21.107  1.00 50.89  ? 307 GLU B CB  1 
ATOM   5589 C CG  . GLU B 1 278 ? 30.918  3.490   19.630  1.00 61.62  ? 307 GLU B CG  1 
ATOM   5590 C CD  . GLU B 1 278 ? 30.903  4.928   19.116  1.00 72.53  ? 307 GLU B CD  1 
ATOM   5591 O OE1 . GLU B 1 278 ? 31.265  5.874   19.878  1.00 67.12  ? 307 GLU B OE1 1 
ATOM   5592 O OE2 . GLU B 1 278 ? 30.530  5.102   17.932  1.00 71.17  ? 307 GLU B OE2 1 
ATOM   5593 N N   . VAL B 1 279 ? 29.638  2.855   23.809  1.00 49.01  ? 308 VAL B N   1 
ATOM   5594 C CA  . VAL B 1 279 ? 29.588  3.181   25.224  1.00 45.34  ? 308 VAL B CA  1 
ATOM   5595 C C   . VAL B 1 279 ? 29.873  1.928   26.055  1.00 42.77  ? 308 VAL B C   1 
ATOM   5596 O O   . VAL B 1 279 ? 30.705  1.965   26.955  1.00 40.17  ? 308 VAL B O   1 
ATOM   5597 C CB  . VAL B 1 279 ? 28.247  3.848   25.605  1.00 41.51  ? 308 VAL B CB  1 
ATOM   5598 C CG1 . VAL B 1 279 ? 28.083  4.074   27.103  1.00 40.04  ? 308 VAL B CG1 1 
ATOM   5599 C CG2 . VAL B 1 279 ? 28.030  5.175   24.887  1.00 42.02  ? 308 VAL B CG2 1 
ATOM   5600 N N   . LEU B 1 280 ? 29.196  0.811   25.776  1.00 42.91  ? 309 LEU B N   1 
ATOM   5601 C CA  . LEU B 1 280 ? 29.286  -0.345  26.659  1.00 40.97  ? 309 LEU B CA  1 
ATOM   5602 C C   . LEU B 1 280 ? 30.675  -0.986  26.577  1.00 45.04  ? 309 LEU B C   1 
ATOM   5603 O O   . LEU B 1 280 ? 31.145  -1.580  27.548  1.00 44.02  ? 309 LEU B O   1 
ATOM   5604 C CB  . LEU B 1 280 ? 28.157  -1.329  26.355  1.00 37.43  ? 309 LEU B CB  1 
ATOM   5605 C CG  . LEU B 1 280 ? 28.172  -2.637  27.144  1.00 36.81  ? 309 LEU B CG  1 
ATOM   5606 C CD1 . LEU B 1 280 ? 27.959  -2.427  28.644  1.00 36.19  ? 309 LEU B CD1 1 
ATOM   5607 C CD2 . LEU B 1 280 ? 27.119  -3.546  26.572  1.00 34.83  ? 309 LEU B CD2 1 
ATOM   5608 N N   . VAL B 1 281 ? 31.331  -0.885  25.417  1.00 49.04  ? 310 VAL B N   1 
ATOM   5609 C CA  . VAL B 1 281 ? 32.681  -1.404  25.260  1.00 53.47  ? 310 VAL B CA  1 
ATOM   5610 C C   . VAL B 1 281 ? 33.624  -0.620  26.171  1.00 54.81  ? 310 VAL B C   1 
ATOM   5611 O O   . VAL B 1 281 ? 34.490  -1.195  26.847  1.00 46.46  ? 310 VAL B O   1 
ATOM   5612 C CB  . VAL B 1 281 ? 33.101  -1.299  23.784  1.00 54.57  ? 310 VAL B CB  1 
ATOM   5613 C CG1 . VAL B 1 281 ? 34.586  -1.583  23.594  1.00 61.51  ? 310 VAL B CG1 1 
ATOM   5614 C CG2 . VAL B 1 281 ? 32.263  -2.216  22.899  1.00 54.71  ? 310 VAL B CG2 1 
ATOM   5615 N N   . TRP B 1 282 ? 33.416  0.702   26.153  1.00 59.45  ? 311 TRP B N   1 
ATOM   5616 C CA  . TRP B 1 282 ? 34.178  1.670   26.923  1.00 63.13  ? 311 TRP B CA  1 
ATOM   5617 C C   . TRP B 1 282 ? 34.001  1.415   28.420  1.00 59.63  ? 311 TRP B C   1 
ATOM   5618 O O   . TRP B 1 282 ? 35.001  1.277   29.123  1.00 56.16  ? 311 TRP B O   1 
ATOM   5619 C CB  . TRP B 1 282 ? 33.744  3.084   26.509  1.00 70.68  ? 311 TRP B CB  1 
ATOM   5620 C CG  . TRP B 1 282 ? 34.591  4.208   27.040  1.00 79.98  ? 311 TRP B CG  1 
ATOM   5621 C CD1 . TRP B 1 282 ? 35.805  4.629   26.579  1.00 82.45  ? 311 TRP B CD1 1 
ATOM   5622 C CD2 . TRP B 1 282 ? 34.232  5.107   28.111  1.00 93.72  ? 311 TRP B CD2 1 
ATOM   5623 N NE1 . TRP B 1 282 ? 36.245  5.698   27.314  1.00 84.77  ? 311 TRP B NE1 1 
ATOM   5624 C CE2 . TRP B 1 282 ? 35.300  6.019   28.254  1.00 93.43  ? 311 TRP B CE2 1 
ATOM   5625 C CE3 . TRP B 1 282 ? 33.125  5.219   28.963  1.00 97.19  ? 311 TRP B CE3 1 
ATOM   5626 C CZ2 . TRP B 1 282 ? 35.283  7.028   29.214  1.00 98.96  ? 311 TRP B CZ2 1 
ATOM   5627 C CZ3 . TRP B 1 282 ? 33.106  6.225   29.903  1.00 96.35  ? 311 TRP B CZ3 1 
ATOM   5628 C CH2 . TRP B 1 282 ? 34.173  7.114   30.025  1.00 100.80 ? 311 TRP B CH2 1 
ATOM   5629 N N   . LEU B 1 283 ? 32.744  1.313   28.891  1.00 48.85  ? 312 LEU B N   1 
ATOM   5630 C CA  . LEU B 1 283 ? 32.459  1.058   30.303  1.00 50.10  ? 312 LEU B CA  1 
ATOM   5631 C C   . LEU B 1 283 ? 33.089  -0.253  30.780  1.00 45.76  ? 312 LEU B C   1 
ATOM   5632 O O   . LEU B 1 283 ? 33.642  -0.312  31.873  1.00 44.54  ? 312 LEU B O   1 
ATOM   5633 C CB  . LEU B 1 283 ? 30.959  1.020   30.562  1.00 48.87  ? 312 LEU B CB  1 
ATOM   5634 C CG  . LEU B 1 283 ? 30.197  2.315   30.288  1.00 50.75  ? 312 LEU B CG  1 
ATOM   5635 C CD1 . LEU B 1 283 ? 28.705  2.039   30.216  1.00 49.50  ? 312 LEU B CD1 1 
ATOM   5636 C CD2 . LEU B 1 283 ? 30.521  3.316   31.370  1.00 50.29  ? 312 LEU B CD2 1 
ATOM   5637 N N   . THR B 1 284 ? 32.938  -1.326  29.992  1.00 49.27  ? 313 THR B N   1 
ATOM   5638 C CA  . THR B 1 284 ? 33.573  -2.606  30.291  1.00 56.82  ? 313 THR B CA  1 
ATOM   5639 C C   . THR B 1 284 ? 35.087  -2.401  30.401  1.00 64.08  ? 313 THR B C   1 
ATOM   5640 O O   . THR B 1 284 ? 35.709  -2.852  31.366  1.00 61.22  ? 313 THR B O   1 
ATOM   5641 C CB  . THR B 1 284 ? 33.206  -3.640  29.218  1.00 54.19  ? 313 THR B CB  1 
ATOM   5642 O OG1 . THR B 1 284 ? 31.793  -3.827  29.299  1.00 53.23  ? 313 THR B OG1 1 
ATOM   5643 C CG2 . THR B 1 284 ? 33.889  -4.983  29.421  1.00 50.38  ? 313 THR B CG2 1 
ATOM   5644 N N   . GLN B 1 285 ? 35.648  -1.685  29.411  1.00 74.60  ? 314 GLN B N   1 
ATOM   5645 C CA  . GLN B 1 285 ? 37.070  -1.388  29.329  1.00 75.78  ? 314 GLN B CA  1 
ATOM   5646 C C   . GLN B 1 285 ? 37.523  -0.538  30.515  1.00 81.28  ? 314 GLN B C   1 
ATOM   5647 O O   . GLN B 1 285 ? 38.656  -0.689  30.957  1.00 88.08  ? 314 GLN B O   1 
ATOM   5648 C CB  . GLN B 1 285 ? 37.399  -0.670  28.020  1.00 72.91  ? 314 GLN B CB  1 
ATOM   5649 C CG  . GLN B 1 285 ? 38.889  -0.436  27.818  1.00 82.57  ? 314 GLN B CG  1 
ATOM   5650 C CD  . GLN B 1 285 ? 39.263  -0.353  26.355  1.00 93.72  ? 314 GLN B CD  1 
ATOM   5651 O OE1 . GLN B 1 285 ? 38.749  0.491   25.614  1.00 102.20 ? 314 GLN B OE1 1 
ATOM   5652 N NE2 . GLN B 1 285 ? 40.146  -1.239  25.914  1.00 94.69  ? 314 GLN B NE2 1 
ATOM   5653 N N   . LEU B 1 286 ? 36.637  0.349   31.003  1.00 82.83  ? 315 LEU B N   1 
ATOM   5654 C CA  . LEU B 1 286 ? 36.916  1.243   32.122  1.00 82.24  ? 315 LEU B CA  1 
ATOM   5655 C C   . LEU B 1 286 ? 37.089  0.435   33.412  1.00 81.12  ? 315 LEU B C   1 
ATOM   5656 O O   . LEU B 1 286 ? 37.918  0.787   34.245  1.00 76.25  ? 315 LEU B O   1 
ATOM   5657 C CB  . LEU B 1 286 ? 35.816  2.297   32.269  1.00 79.68  ? 315 LEU B CB  1 
ATOM   5658 C CG  . LEU B 1 286 ? 36.238  3.656   32.837  1.00 78.78  ? 315 LEU B CG  1 
ATOM   5659 C CD1 . LEU B 1 286 ? 37.025  4.481   31.816  1.00 79.78  ? 315 LEU B CD1 1 
ATOM   5660 C CD2 . LEU B 1 286 ? 34.996  4.401   33.302  1.00 74.91  ? 315 LEU B CD2 1 
ATOM   5661 N N   . GLN B 1 287 ? 36.328  -0.656  33.576  1.00 80.35  ? 316 GLN B N   1 
ATOM   5662 C CA  . GLN B 1 287 ? 36.608  -1.610  34.642  1.00 86.65  ? 316 GLN B CA  1 
ATOM   5663 C C   . GLN B 1 287 ? 37.693  -2.591  34.178  1.00 83.66  ? 316 GLN B C   1 
ATOM   5664 O O   . GLN B 1 287 ? 37.565  -3.800  34.337  1.00 72.77  ? 316 GLN B O   1 
ATOM   5665 C CB  . GLN B 1 287 ? 35.289  -2.221  35.116  1.00 85.97  ? 316 GLN B CB  1 
ATOM   5666 C CG  . GLN B 1 287 ? 34.361  -1.221  35.802  1.00 85.18  ? 316 GLN B CG  1 
ATOM   5667 C CD  . GLN B 1 287 ? 32.977  -1.749  36.139  1.00 92.42  ? 316 GLN B CD  1 
ATOM   5668 O OE1 . GLN B 1 287 ? 32.178  -1.077  36.803  1.00 100.08 ? 316 GLN B OE1 1 
ATOM   5669 N NE2 . GLN B 1 287 ? 32.655  -2.957  35.699  1.00 92.78  ? 316 GLN B NE2 1 
ATOM   5670 N N   . LYS B 1 288 ? 38.751  -2.049  33.559  1.00 90.57  ? 317 LYS B N   1 
ATOM   5671 C CA  . LYS B 1 288 ? 40.045  -2.704  33.454  1.00 100.45 ? 317 LYS B CA  1 
ATOM   5672 C C   . LYS B 1 288 ? 40.903  -2.224  34.616  1.00 101.05 ? 317 LYS B C   1 
ATOM   5673 O O   . LYS B 1 288 ? 41.290  -3.012  35.477  1.00 107.01 ? 317 LYS B O   1 
ATOM   5674 C CB  . LYS B 1 288 ? 40.788  -2.357  32.153  1.00 104.68 ? 317 LYS B CB  1 
ATOM   5675 C CG  . LYS B 1 288 ? 40.538  -3.254  30.946  1.00 107.74 ? 317 LYS B CG  1 
ATOM   5676 C CD  . LYS B 1 288 ? 39.160  -3.906  30.877  1.00 111.72 ? 317 LYS B CD  1 
ATOM   5677 C CE  . LYS B 1 288 ? 39.010  -4.849  29.722  1.00 110.94 ? 317 LYS B CE  1 
ATOM   5678 N NZ  . LYS B 1 288 ? 39.490  -4.294  28.454  1.00 107.81 ? 317 LYS B NZ  1 
ATOM   5679 N N   . GLU B 1 289 ? 41.156  -0.909  34.618  1.00 102.24 ? 318 GLU B N   1 
ATOM   5680 C CA  . GLU B 1 289 ? 42.063  -0.270  35.552  1.00 106.01 ? 318 GLU B CA  1 
ATOM   5681 C C   . GLU B 1 289 ? 41.293  0.100   36.818  1.00 109.87 ? 318 GLU B C   1 
ATOM   5682 O O   . GLU B 1 289 ? 41.620  -0.367  37.905  1.00 136.04 ? 318 GLU B O   1 
ATOM   5683 C CB  . GLU B 1 289 ? 42.700  0.925   34.839  1.00 101.00 ? 318 GLU B CB  1 
ATOM   5684 N N   . VAL B 1 290 ? 40.233  0.891   36.643  1.00 101.79 ? 319 VAL B N   1 
ATOM   5685 C CA  . VAL B 1 290 ? 39.376  1.351   37.774  1.00 95.42  ? 319 VAL B CA  1 
ATOM   5686 C C   . VAL B 1 290 ? 39.071  0.246   38.789  1.00 83.67  ? 319 VAL B C   1 
ATOM   5687 O O   . VAL B 1 290 ? 39.131  0.536   40.004  1.00 73.03  ? 319 VAL B O   1 
ATOM   5688 C CB  . VAL B 1 290 ? 38.094  1.752   37.025  1.00 102.33 ? 319 VAL B CB  1 
ATOM   5689 C CG1 . VAL B 1 290 ? 36.827  1.627   37.857  1.00 106.30 ? 319 VAL B CG1 1 
ATOM   5690 C CG2 . VAL B 1 290 ? 38.205  3.086   36.294  1.00 102.50 ? 319 VAL B CG2 1 
ATOM   5691 N N   . GLY B 1 291 ? 38.653  -0.944  38.384  1.00 83.25  ? 320 GLY B N   1 
ATOM   5692 C CA  . GLY B 1 291 ? 38.144  -1.882  39.405  1.00 91.34  ? 320 GLY B CA  1 
ATOM   5693 C C   . GLY B 1 291 ? 36.705  -1.472  39.733  1.00 104.03 ? 320 GLY B C   1 
ATOM   5694 O O   . GLY B 1 291 ? 36.019  -1.012  38.813  1.00 116.59 ? 320 GLY B O   1 
ATOM   5695 N N   . LYS B 1 292 ? 36.227  -1.628  40.976  1.00 111.32 ? 321 LYS B N   1 
ATOM   5696 C CA  . LYS B 1 292 ? 34.861  -1.129  41.321  1.00 116.83 ? 321 LYS B CA  1 
ATOM   5697 C C   . LYS B 1 292 ? 35.022  0.020   42.342  1.00 129.61 ? 321 LYS B C   1 
ATOM   5698 O O   . LYS B 1 292 ? 34.909  -0.281  43.539  1.00 141.15 ? 321 LYS B O   1 
ATOM   5699 C CB  . LYS B 1 292 ? 33.887  -2.255  41.693  1.00 101.70 ? 321 LYS B CB  1 
ATOM   5700 C CG  . LYS B 1 292 ? 34.189  -3.141  42.894  1.00 102.19 ? 321 LYS B CG  1 
ATOM   5701 C CD  . LYS B 1 292 ? 33.087  -3.027  43.942  1.00 103.35 ? 321 LYS B CD  1 
ATOM   5702 C CE  . LYS B 1 292 ? 31.722  -3.100  43.320  1.00 95.56  ? 321 LYS B CE  1 
ATOM   5703 N NZ  . LYS B 1 292 ? 30.837  -1.993  43.699  1.00 92.07  ? 321 LYS B NZ  1 
ATOM   5704 N N   . ASP B 1 293 ? 35.300  1.259   41.877  1.00 121.48 ? 322 ASP B N   1 
ATOM   5705 C CA  . ASP B 1 293 ? 35.456  2.498   42.714  1.00 111.93 ? 322 ASP B CA  1 
ATOM   5706 C C   . ASP B 1 293 ? 36.608  3.346   42.156  1.00 102.01 ? 322 ASP B C   1 
ATOM   5707 O O   . ASP B 1 293 ? 37.712  2.778   42.002  1.00 91.26  ? 322 ASP B O   1 
ATOM   5708 C CB  . ASP B 1 293 ? 35.759  2.287   44.189  1.00 113.56 ? 322 ASP B CB  1 
ATOM   5709 C CG  . ASP B 1 293 ? 36.167  3.538   44.954  1.00 110.70 ? 322 ASP B CG  1 
ATOM   5710 O OD1 . ASP B 1 293 ? 35.373  4.502   44.967  1.00 93.29  ? 322 ASP B OD1 1 
ATOM   5711 O OD2 . ASP B 1 293 ? 37.279  3.540   45.523  1.00 113.21 ? 322 ASP B OD2 1 
ATOM   5712 N N   . VAL B 1 294 ? 36.268  4.661   41.879  1.00 114.51 ? 323 VAL B N   1 
ATOM   5713 C CA  . VAL B 1 294 ? 37.421  5.508   41.425  1.00 121.98 ? 323 VAL B CA  1 
ATOM   5714 C C   . VAL B 1 294 ? 37.164  7.012   41.613  1.00 108.53 ? 323 VAL B C   1 
ATOM   5715 O O   . VAL B 1 294 ? 36.331  7.369   42.474  1.00 80.08  ? 323 VAL B O   1 
ATOM   5716 C CB  . VAL B 1 294 ? 37.819  5.254   39.960  1.00 124.13 ? 323 VAL B CB  1 
ATOM   5717 C CG1 . VAL B 1 294 ? 39.071  4.395   39.871  1.00 127.74 ? 323 VAL B CG1 1 
ATOM   5718 C CG2 . VAL B 1 294 ? 36.666  4.704   39.131  1.00 120.04 ? 323 VAL B CG2 1 
ATOM   5719 N N   . SER B 1 295 ? 37.837  7.834   40.663  1.00 101.45 ? 324 SER B N   1 
ATOM   5720 C CA  . SER B 1 295 ? 37.806  9.275   40.848  1.00 99.26  ? 324 SER B CA  1 
ATOM   5721 C C   . SER B 1 295 ? 37.670  9.954   39.488  1.00 99.00  ? 324 SER B C   1 
ATOM   5722 O O   . SER B 1 295 ? 37.527  9.287   38.461  1.00 90.92  ? 324 SER B O   1 
ATOM   5723 C CB  . SER B 1 295 ? 39.050  9.760   41.552  1.00 87.75  ? 324 SER B CB  1 
ATOM   5724 O OG  . SER B 1 295 ? 39.610  8.728   42.346  1.00 80.18  ? 324 SER B OG  1 
ATOM   5725 N N   . ASP B 1 296 ? 37.743  11.291  39.511  1.00 100.19 ? 325 ASP B N   1 
ATOM   5726 C CA  . ASP B 1 296 ? 37.672  12.090  38.303  1.00 101.47 ? 325 ASP B CA  1 
ATOM   5727 C C   . ASP B 1 296 ? 39.037  12.171  37.626  1.00 101.01 ? 325 ASP B C   1 
ATOM   5728 O O   . ASP B 1 296 ? 39.072  12.346  36.416  1.00 91.33  ? 325 ASP B O   1 
ATOM   5729 C CB  . ASP B 1 296 ? 37.005  13.442  38.519  1.00 110.91 ? 325 ASP B CB  1 
ATOM   5730 C CG  . ASP B 1 296 ? 37.537  14.329  39.634  1.00 125.06 ? 325 ASP B CG  1 
ATOM   5731 O OD1 . ASP B 1 296 ? 38.759  14.593  39.653  1.00 132.79 ? 325 ASP B OD1 1 
ATOM   5732 O OD2 . ASP B 1 296 ? 36.706  14.789  40.448  1.00 135.89 ? 325 ASP B OD2 1 
ATOM   5733 N N   . GLU B 1 297 ? 40.149  12.035  38.368  1.00 112.07 ? 326 GLU B N   1 
ATOM   5734 C CA  . GLU B 1 297 ? 41.457  11.940  37.726  1.00 116.93 ? 326 GLU B CA  1 
ATOM   5735 C C   . GLU B 1 297 ? 41.407  10.777  36.750  1.00 113.10 ? 326 GLU B C   1 
ATOM   5736 O O   . GLU B 1 297 ? 41.648  10.932  35.556  1.00 106.20 ? 326 GLU B O   1 
ATOM   5737 C CB  . GLU B 1 297 ? 42.653  11.706  38.656  1.00 114.92 ? 326 GLU B CB  1 
ATOM   5738 C CG  . GLU B 1 297 ? 43.381  12.995  39.018  1.00 117.76 ? 326 GLU B CG  1 
ATOM   5739 C CD  . GLU B 1 297 ? 42.388  14.098  39.342  1.00 130.20 ? 326 GLU B CD  1 
ATOM   5740 O OE1 . GLU B 1 297 ? 41.528  13.865  40.220  1.00 146.51 ? 326 GLU B OE1 1 
ATOM   5741 O OE2 . GLU B 1 297 ? 42.452  15.177  38.715  1.00 125.18 ? 326 GLU B OE2 1 
ATOM   5742 N N   . LYS B 1 298 ? 41.052  9.622   37.305  1.00 113.51 ? 327 LYS B N   1 
ATOM   5743 C CA  . LYS B 1 298 ? 40.743  8.438   36.528  1.00 110.33 ? 327 LYS B CA  1 
ATOM   5744 C C   . LYS B 1 298 ? 39.955  8.863   35.284  1.00 105.41 ? 327 LYS B C   1 
ATOM   5745 O O   . LYS B 1 298 ? 40.319  8.521   34.161  1.00 101.55 ? 327 LYS B O   1 
ATOM   5746 C CB  . LYS B 1 298 ? 40.033  7.469   37.485  1.00 109.17 ? 327 LYS B CB  1 
ATOM   5747 C CG  . LYS B 1 298 ? 40.598  7.388   38.920  1.00 104.62 ? 327 LYS B CG  1 
ATOM   5748 C CD  . LYS B 1 298 ? 42.107  7.186   39.055  1.00 100.79 ? 327 LYS B CD  1 
ATOM   5749 C CE  . LYS B 1 298 ? 42.584  5.788   38.765  1.00 92.76  ? 327 LYS B CE  1 
ATOM   5750 N NZ  . LYS B 1 298 ? 42.413  4.870   39.893  1.00 86.27  ? 327 LYS B NZ  1 
ATOM   5751 N N   . LEU B 1 299 ? 38.913  9.675   35.502  1.00 110.48 ? 328 LEU B N   1 
ATOM   5752 C CA  . LEU B 1 299 ? 37.999  10.106  34.454  1.00 111.62 ? 328 LEU B CA  1 
ATOM   5753 C C   . LEU B 1 299 ? 38.606  11.250  33.638  1.00 103.47 ? 328 LEU B C   1 
ATOM   5754 O O   . LEU B 1 299 ? 38.889  11.075  32.458  1.00 94.82  ? 328 LEU B O   1 
ATOM   5755 C CB  . LEU B 1 299 ? 36.702  10.498  35.163  1.00 122.85 ? 328 LEU B CB  1 
ATOM   5756 C CG  . LEU B 1 299 ? 35.372  10.110  34.506  1.00 130.08 ? 328 LEU B CG  1 
ATOM   5757 C CD1 . LEU B 1 299 ? 35.453  9.065   33.404  1.00 127.46 ? 328 LEU B CD1 1 
ATOM   5758 C CD2 . LEU B 1 299 ? 34.488  9.591   35.640  1.00 131.68 ? 328 LEU B CD2 1 
ATOM   5759 N N   . ARG B 1 300 ? 38.773  12.461  34.238  1.00 105.55 ? 329 ARG B N   1 
ATOM   5760 C CA  . ARG B 1 300 ? 39.288  13.601  33.431  1.00 100.56 ? 329 ARG B CA  1 
ATOM   5761 C C   . ARG B 1 300 ? 40.544  13.188  32.653  1.00 95.80  ? 329 ARG B C   1 
ATOM   5762 O O   . ARG B 1 300 ? 40.897  13.949  31.732  1.00 90.93  ? 329 ARG B O   1 
ATOM   5763 C CB  . ARG B 1 300 ? 39.577  14.831  34.300  1.00 105.66 ? 329 ARG B CB  1 
ATOM   5764 N N   . ASP B 1 301 ? 41.362  12.091  33.128  1.00 103.70 ? 330 ASP B N   1 
ATOM   5765 C CA  . ASP B 1 301 ? 42.590  11.908  32.318  1.00 106.02 ? 330 ASP B CA  1 
ATOM   5766 C C   . ASP B 1 301 ? 42.121  11.631  30.899  1.00 104.68 ? 330 ASP B C   1 
ATOM   5767 O O   . ASP B 1 301 ? 42.002  12.563  30.118  1.00 111.31 ? 330 ASP B O   1 
ATOM   5768 C CB  . ASP B 1 301 ? 43.462  10.769  32.817  1.00 106.88 ? 330 ASP B CB  1 
ATOM   5769 C CG  . ASP B 1 301 ? 44.688  11.190  33.611  1.00 113.21 ? 330 ASP B CG  1 
ATOM   5770 O OD1 . ASP B 1 301 ? 45.264  12.247  33.281  1.00 103.25 ? 330 ASP B OD1 1 
ATOM   5771 O OD2 . ASP B 1 301 ? 45.056  10.457  34.553  1.00 126.92 ? 330 ASP B OD2 1 
ATOM   5772 N N   . TYR B 1 302 ? 41.436  10.323  30.699  1.00 99.54  ? 331 TYR B N   1 
ATOM   5773 C CA  . TYR B 1 302 ? 40.933  10.026  29.362  1.00 89.79  ? 331 TYR B CA  1 
ATOM   5774 C C   . TYR B 1 302 ? 40.150  11.229  28.843  1.00 98.55  ? 331 TYR B C   1 
ATOM   5775 O O   . TYR B 1 302 ? 40.442  11.746  27.770  1.00 92.67  ? 331 TYR B O   1 
ATOM   5776 C CB  . TYR B 1 302 ? 40.054  8.770   29.319  1.00 82.82  ? 331 TYR B CB  1 
ATOM   5777 N N   . ILE B 1 303 ? 39.189  11.705  29.641  1.00 108.06 ? 332 ILE B N   1 
ATOM   5778 C CA  . ILE B 1 303 ? 38.362  12.847  29.277  1.00 116.22 ? 332 ILE B CA  1 
ATOM   5779 C C   . ILE B 1 303 ? 39.217  13.897  28.554  1.00 116.71 ? 332 ILE B C   1 
ATOM   5780 O O   . ILE B 1 303 ? 38.799  14.377  27.505  1.00 95.79  ? 332 ILE B O   1 
ATOM   5781 C CB  . ILE B 1 303 ? 37.633  13.392  30.527  1.00 125.76 ? 332 ILE B CB  1 
ATOM   5782 C CG1 . ILE B 1 303 ? 36.395  12.554  30.929  1.00 126.78 ? 332 ILE B CG1 1 
ATOM   5783 C CG2 . ILE B 1 303 ? 37.242  14.864  30.365  1.00 127.46 ? 332 ILE B CG2 1 
ATOM   5784 C CD1 . ILE B 1 303 ? 36.446  11.071  30.594  1.00 128.27 ? 332 ILE B CD1 1 
ATOM   5785 N N   . TRP B 1 304 ? 40.403  14.235  29.103  1.00 132.65 ? 333 TRP B N   1 
ATOM   5786 C CA  . TRP B 1 304 ? 41.375  15.128  28.466  1.00 134.97 ? 333 TRP B CA  1 
ATOM   5787 C C   . TRP B 1 304 ? 42.383  14.334  27.628  1.00 116.33 ? 333 TRP B C   1 
ATOM   5788 O O   . TRP B 1 304 ? 42.808  14.778  26.567  1.00 99.02  ? 333 TRP B O   1 
ATOM   5789 C CB  . TRP B 1 304 ? 42.127  15.985  29.502  1.00 147.77 ? 333 TRP B CB  1 
ATOM   5790 C CG  . TRP B 1 304 ? 41.441  17.261  29.929  1.00 162.87 ? 333 TRP B CG  1 
ATOM   5791 C CD1 . TRP B 1 304 ? 40.503  17.385  30.912  1.00 165.64 ? 333 TRP B CD1 1 
ATOM   5792 C CD2 . TRP B 1 304 ? 41.670  18.600  29.425  1.00 174.52 ? 333 TRP B CD2 1 
ATOM   5793 N NE1 . TRP B 1 304 ? 40.112  18.691  31.040  1.00 173.81 ? 333 TRP B NE1 1 
ATOM   5794 C CE2 . TRP B 1 304 ? 40.810  19.462  30.146  1.00 177.98 ? 333 TRP B CE2 1 
ATOM   5795 C CE3 . TRP B 1 304 ? 42.500  19.156  28.441  1.00 166.49 ? 333 TRP B CE3 1 
ATOM   5796 C CZ2 . TRP B 1 304 ? 40.764  20.836  29.912  1.00 170.21 ? 333 TRP B CZ2 1 
ATOM   5797 C CZ3 . TRP B 1 304 ? 42.454  20.516  28.214  1.00 161.86 ? 333 TRP B CZ3 1 
ATOM   5798 C CH2 . TRP B 1 304 ? 41.598  21.344  28.941  1.00 162.37 ? 333 TRP B CH2 1 
ATOM   5799 N N   . ASN B 1 305 ? 42.780  13.157  28.120  1.00 118.62 ? 334 ASN B N   1 
ATOM   5800 C CA  . ASN B 1 305 ? 43.709  12.286  27.415  1.00 122.01 ? 334 ASN B CA  1 
ATOM   5801 C C   . ASN B 1 305 ? 43.019  11.564  26.257  1.00 122.29 ? 334 ASN B C   1 
ATOM   5802 O O   . ASN B 1 305 ? 43.642  10.715  25.626  1.00 114.37 ? 334 ASN B O   1 
ATOM   5803 C CB  . ASN B 1 305 ? 44.324  11.246  28.346  1.00 126.10 ? 334 ASN B CB  1 
ATOM   5804 C CG  . ASN B 1 305 ? 44.872  11.855  29.614  1.00 138.85 ? 334 ASN B CG  1 
ATOM   5805 O OD1 . ASN B 1 305 ? 44.962  13.083  29.726  1.00 153.13 ? 334 ASN B OD1 1 
ATOM   5806 N ND2 . ASN B 1 305 ? 45.242  11.020  30.575  1.00 142.42 ? 334 ASN B ND2 1 
ATOM   5807 N N   . THR B 1 306 ? 41.738  11.885  25.999  1.00 129.10 ? 335 THR B N   1 
ATOM   5808 C CA  . THR B 1 306 ? 40.969  11.306  24.904  1.00 134.30 ? 335 THR B CA  1 
ATOM   5809 C C   . THR B 1 306 ? 40.365  12.423  24.052  1.00 142.32 ? 335 THR B C   1 
ATOM   5810 O O   . THR B 1 306 ? 40.577  12.443  22.841  1.00 132.14 ? 335 THR B O   1 
ATOM   5811 C CB  . THR B 1 306 ? 39.880  10.369  25.432  1.00 130.22 ? 335 THR B CB  1 
ATOM   5812 O OG1 . THR B 1 306 ? 40.519  9.351   26.196  1.00 144.50 ? 335 THR B OG1 1 
ATOM   5813 C CG2 . THR B 1 306 ? 39.080  9.726   24.314  1.00 117.01 ? 335 THR B CG2 1 
ATOM   5814 N N   . LEU B 1 307 ? 39.607  13.338  24.682  1.00 153.40 ? 336 LEU B N   1 
ATOM   5815 C CA  . LEU B 1 307 ? 39.001  14.469  23.984  1.00 155.78 ? 336 LEU B CA  1 
ATOM   5816 C C   . LEU B 1 307 ? 40.092  15.388  23.431  1.00 154.19 ? 336 LEU B C   1 
ATOM   5817 O O   . LEU B 1 307 ? 39.947  15.908  22.325  1.00 154.14 ? 336 LEU B O   1 
ATOM   5818 C CB  . LEU B 1 307 ? 38.003  15.246  24.851  1.00 157.45 ? 336 LEU B CB  1 
ATOM   5819 C CG  . LEU B 1 307 ? 36.518  14.904  24.664  1.00 156.92 ? 336 LEU B CG  1 
ATOM   5820 C CD1 . LEU B 1 307 ? 35.713  15.145  25.929  1.00 158.39 ? 336 LEU B CD1 1 
ATOM   5821 C CD2 . LEU B 1 307 ? 35.915  15.702  23.517  1.00 151.11 ? 336 LEU B CD2 1 
ATOM   5822 N N   . ASN B 1 308 ? 41.172  15.587  24.200  1.00 152.59 ? 337 ASN B N   1 
ATOM   5823 C CA  . ASN B 1 308 ? 42.322  16.351  23.735  1.00 143.59 ? 337 ASN B CA  1 
ATOM   5824 C C   . ASN B 1 308 ? 43.309  15.428  23.009  1.00 128.59 ? 337 ASN B C   1 
ATOM   5825 O O   . ASN B 1 308 ? 44.221  15.919  22.343  1.00 114.88 ? 337 ASN B O   1 
ATOM   5826 C CB  . ASN B 1 308 ? 42.964  17.160  24.864  1.00 150.49 ? 337 ASN B CB  1 
ATOM   5827 C CG  . ASN B 1 308 ? 42.238  18.455  25.166  1.00 153.11 ? 337 ASN B CG  1 
ATOM   5828 O OD1 . ASN B 1 308 ? 41.011  18.467  25.321  1.00 159.34 ? 337 ASN B OD1 1 
ATOM   5829 N ND2 . ASN B 1 308 ? 42.974  19.554  25.265  1.00 144.81 ? 337 ASN B ND2 1 
ATOM   5830 N N   . SER B 1 309 ? 43.132  14.100  23.125  1.00 118.86 ? 338 SER B N   1 
ATOM   5831 C CA  . SER B 1 309 ? 43.920  13.137  22.360  1.00 116.45 ? 338 SER B CA  1 
ATOM   5832 C C   . SER B 1 309 ? 43.396  13.016  20.931  1.00 124.03 ? 338 SER B C   1 
ATOM   5833 O O   . SER B 1 309 ? 44.182  12.929  19.986  1.00 116.50 ? 338 SER B O   1 
ATOM   5834 C CB  . SER B 1 309 ? 43.949  11.772  23.003  1.00 106.00 ? 338 SER B CB  1 
ATOM   5835 O OG  . SER B 1 309 ? 44.772  11.751  24.159  1.00 99.65  ? 338 SER B OG  1 
ATOM   5836 N N   . GLY B 1 310 ? 42.064  12.936  20.796  1.00 136.15 ? 339 GLY B N   1 
ATOM   5837 C CA  . GLY B 1 310 ? 41.438  12.775  19.466  1.00 137.91 ? 339 GLY B CA  1 
ATOM   5838 C C   . GLY B 1 310 ? 39.994  12.301  19.557  1.00 141.60 ? 339 GLY B C   1 
ATOM   5839 O O   . GLY B 1 310 ? 39.144  12.900  18.866  1.00 140.45 ? 339 GLY B O   1 
ATOM   5840 N N   . ARG B 1 311 ? 39.710  11.271  20.366  1.00 147.84 ? 340 ARG B N   1 
ATOM   5841 C CA  . ARG B 1 311 ? 38.340  10.692  20.462  1.00 144.34 ? 340 ARG B CA  1 
ATOM   5842 C C   . ARG B 1 311 ? 37.437  11.413  21.471  1.00 140.97 ? 340 ARG B C   1 
ATOM   5843 O O   . ARG B 1 311 ? 37.422  12.664  21.474  1.00 154.60 ? 340 ARG B O   1 
ATOM   5844 C CB  . ARG B 1 311 ? 38.439  9.201   20.806  1.00 135.56 ? 340 ARG B CB  1 
ATOM   5845 C CG  . ARG B 1 311 ? 39.107  8.373   19.718  1.00 128.53 ? 340 ARG B CG  1 
ATOM   5846 C CD  . ARG B 1 311 ? 40.579  8.125   20.008  1.00 125.06 ? 340 ARG B CD  1 
ATOM   5847 N NE  . ARG B 1 311 ? 40.811  7.874   21.434  1.00 121.89 ? 340 ARG B NE  1 
ATOM   5848 C CZ  . ARG B 1 311 ? 40.629  6.696   22.014  1.00 114.11 ? 340 ARG B CZ  1 
ATOM   5849 N NH1 . ARG B 1 311 ? 39.879  6.599   23.096  1.00 103.54 ? 340 ARG B NH1 1 
ATOM   5850 N NH2 . ARG B 1 311 ? 41.197  5.617   21.507  1.00 115.49 ? 340 ARG B NH2 1 
ATOM   5851 N N   . VAL B 1 312 ? 36.695  10.720  22.366  1.00 117.32 ? 341 VAL B N   1 
ATOM   5852 C CA  . VAL B 1 312 ? 35.583  11.316  23.089  1.00 101.22 ? 341 VAL B CA  1 
ATOM   5853 C C   . VAL B 1 312 ? 35.227  10.490  24.322  1.00 87.51  ? 341 VAL B C   1 
ATOM   5854 O O   . VAL B 1 312 ? 35.819  9.443   24.563  1.00 72.88  ? 341 VAL B O   1 
ATOM   5855 C CB  . VAL B 1 312 ? 34.389  11.427  22.120  1.00 101.52 ? 341 VAL B CB  1 
ATOM   5856 C CG1 . VAL B 1 312 ? 33.768  10.062  21.840  1.00 98.37  ? 341 VAL B CG1 1 
ATOM   5857 C CG2 . VAL B 1 312 ? 33.341  12.426  22.605  1.00 107.80 ? 341 VAL B CG2 1 
ATOM   5858 N N   . VAL B 1 313 ? 34.561  11.030  25.255  1.00 83.97  ? 342 VAL B N   1 
ATOM   5859 C CA  . VAL B 1 313 ? 33.870  10.273  26.291  1.00 79.20  ? 342 VAL B CA  1 
ATOM   5860 C C   . VAL B 1 313 ? 32.543  9.785   25.716  1.00 69.97  ? 342 VAL B C   1 
ATOM   5861 O O   . VAL B 1 313 ? 31.574  10.542  25.705  1.00 74.83  ? 342 VAL B O   1 
ATOM   5862 C CB  . VAL B 1 313 ? 33.592  11.084  27.570  1.00 81.77  ? 342 VAL B CB  1 
ATOM   5863 C CG1 . VAL B 1 313 ? 33.256  10.167  28.743  1.00 82.03  ? 342 VAL B CG1 1 
ATOM   5864 C CG2 . VAL B 1 313 ? 34.743  12.021  27.910  1.00 84.53  ? 342 VAL B CG2 1 
ATOM   5865 N N   . PRO B 1 314 ? 32.431  8.512   25.267  1.00 63.50  ? 343 PRO B N   1 
ATOM   5866 C CA  . PRO B 1 314 ? 31.257  8.090   24.498  1.00 66.64  ? 343 PRO B CA  1 
ATOM   5867 C C   . PRO B 1 314 ? 29.933  8.341   25.229  1.00 56.15  ? 343 PRO B C   1 
ATOM   5868 O O   . PRO B 1 314 ? 29.775  8.009   26.406  1.00 50.80  ? 343 PRO B O   1 
ATOM   5869 C CB  . PRO B 1 314 ? 31.538  6.595   24.203  1.00 67.17  ? 343 PRO B CB  1 
ATOM   5870 C CG  . PRO B 1 314 ? 32.575  6.182   25.237  1.00 67.27  ? 343 PRO B CG  1 
ATOM   5871 C CD  . PRO B 1 314 ? 33.400  7.422   25.486  1.00 61.21  ? 343 PRO B CD  1 
ATOM   5872 N N   . GLY B 1 315 ? 29.010  8.995   24.518  1.00 60.57  ? 344 GLY B N   1 
ATOM   5873 C CA  . GLY B 1 315 ? 27.659  9.242   24.993  1.00 64.66  ? 344 GLY B CA  1 
ATOM   5874 C C   . GLY B 1 315 ? 27.513  10.600  25.679  1.00 70.27  ? 344 GLY B C   1 
ATOM   5875 O O   . GLY B 1 315 ? 26.754  10.695  26.643  1.00 67.44  ? 344 GLY B O   1 
ATOM   5876 N N   . TYR B 1 316 ? 28.207  11.633  25.158  1.00 79.11  ? 345 TYR B N   1 
ATOM   5877 C CA  . TYR B 1 316 ? 28.139  12.993  25.682  1.00 77.52  ? 345 TYR B CA  1 
ATOM   5878 C C   . TYR B 1 316 ? 28.232  14.040  24.556  1.00 91.79  ? 345 TYR B C   1 
ATOM   5879 O O   . TYR B 1 316 ? 29.007  14.986  24.663  1.00 95.07  ? 345 TYR B O   1 
ATOM   5880 C CB  . TYR B 1 316 ? 29.235  13.078  26.753  1.00 71.07  ? 345 TYR B CB  1 
ATOM   5881 C CG  . TYR B 1 316 ? 28.859  12.454  28.091  1.00 67.93  ? 345 TYR B CG  1 
ATOM   5882 C CD1 . TYR B 1 316 ? 28.143  13.169  29.042  1.00 63.43  ? 345 TYR B CD1 1 
ATOM   5883 C CD2 . TYR B 1 316 ? 29.199  11.141  28.405  1.00 67.44  ? 345 TYR B CD2 1 
ATOM   5884 C CE1 . TYR B 1 316 ? 27.779  12.605  30.261  1.00 63.04  ? 345 TYR B CE1 1 
ATOM   5885 C CE2 . TYR B 1 316 ? 28.831  10.561  29.615  1.00 58.56  ? 345 TYR B CE2 1 
ATOM   5886 C CZ  . TYR B 1 316 ? 28.119  11.291  30.557  1.00 63.31  ? 345 TYR B CZ  1 
ATOM   5887 O OH  . TYR B 1 316 ? 27.749  10.718  31.766  1.00 48.44  ? 345 TYR B OH  1 
ATOM   5888 N N   . GLY B 1 317 ? 27.410  13.898  23.494  1.00 103.17 ? 346 GLY B N   1 
ATOM   5889 C CA  . GLY B 1 317 ? 27.295  14.859  22.394  1.00 100.88 ? 346 GLY B CA  1 
ATOM   5890 C C   . GLY B 1 317 ? 25.959  14.694  21.656  1.00 116.34 ? 346 GLY B C   1 
ATOM   5891 O O   . GLY B 1 317 ? 25.081  13.999  22.160  1.00 141.93 ? 346 GLY B O   1 
ATOM   5892 N N   . HIS B 1 318 ? 25.551  15.825  20.863  1.00 119.07 ? 347 HIS B N   1 
ATOM   5893 C CA  . HIS B 1 318 ? 24.616  15.374  19.825  1.00 126.92 ? 347 HIS B CA  1 
ATOM   5894 C C   . HIS B 1 318 ? 24.789  16.209  18.548  1.00 131.02 ? 347 HIS B C   1 
ATOM   5895 O O   . HIS B 1 318 ? 25.768  16.942  18.413  1.00 129.87 ? 347 HIS B O   1 
ATOM   5896 C CB  . HIS B 1 318 ? 23.144  15.375  20.287  1.00 127.39 ? 347 HIS B CB  1 
ATOM   5897 C CG  . HIS B 1 318 ? 22.222  14.464  19.503  1.00 120.91 ? 347 HIS B CG  1 
ATOM   5898 N ND1 . HIS B 1 318 ? 22.550  13.172  19.141  1.00 114.90 ? 347 HIS B ND1 1 
ATOM   5899 C CD2 . HIS B 1 318 ? 20.982  14.661  19.015  1.00 110.58 ? 347 HIS B CD2 1 
ATOM   5900 C CE1 . HIS B 1 318 ? 21.546  12.624  18.464  1.00 108.28 ? 347 HIS B CE1 1 
ATOM   5901 N NE2 . HIS B 1 318 ? 20.583  13.510  18.375  1.00 100.85 ? 347 HIS B NE2 1 
ATOM   5902 N N   . ALA B 1 319 ? 23.799  15.826  17.423  1.00 129.47 ? 348 ALA B N   1 
ATOM   5903 C CA  . ALA B 1 319 ? 23.713  16.603  16.193  1.00 119.57 ? 348 ALA B CA  1 
ATOM   5904 C C   . ALA B 1 319 ? 22.860  17.866  16.371  1.00 118.75 ? 348 ALA B C   1 
ATOM   5905 O O   . ALA B 1 319 ? 22.973  18.783  15.559  1.00 99.14  ? 348 ALA B O   1 
ATOM   5906 C CB  . ALA B 1 319 ? 23.158  15.724  15.081  1.00 111.01 ? 348 ALA B CB  1 
ATOM   5907 N N   . VAL B 1 320 ? 21.612  17.672  17.342  1.00 120.71 ? 349 VAL B N   1 
ATOM   5908 C CA  . VAL B 1 320 ? 21.055  19.045  17.568  1.00 111.34 ? 349 VAL B CA  1 
ATOM   5909 C C   . VAL B 1 320 ? 20.616  19.290  19.026  1.00 113.91 ? 349 VAL B C   1 
ATOM   5910 O O   . VAL B 1 320 ? 20.467  20.478  19.390  1.00 122.55 ? 349 VAL B O   1 
ATOM   5911 C CB  . VAL B 1 320 ? 19.868  19.134  16.589  1.00 102.36 ? 349 VAL B CB  1 
ATOM   5912 C CG1 . VAL B 1 320 ? 18.800  18.084  16.873  1.00 98.06  ? 349 VAL B CG1 1 
ATOM   5913 C CG2 . VAL B 1 320 ? 19.261  20.528  16.503  1.00 95.36  ? 349 VAL B CG2 1 
ATOM   5914 N N   . LEU B 1 321 ? 20.777  18.289  19.930  1.00 103.76 ? 350 LEU B N   1 
ATOM   5915 C CA  . LEU B 1 321 ? 20.291  18.391  21.307  1.00 99.50  ? 350 LEU B CA  1 
ATOM   5916 C C   . LEU B 1 321 ? 21.111  19.413  22.109  1.00 93.02  ? 350 LEU B C   1 
ATOM   5917 O O   . LEU B 1 321 ? 21.989  20.066  21.544  1.00 78.60  ? 350 LEU B O   1 
ATOM   5918 C CB  . LEU B 1 321 ? 20.290  16.989  21.937  1.00 107.20 ? 350 LEU B CB  1 
ATOM   5919 C CG  . LEU B 1 321 ? 18.960  16.215  21.917  1.00 104.33 ? 350 LEU B CG  1 
ATOM   5920 C CD1 . LEU B 1 321 ? 19.135  14.703  21.877  1.00 96.66  ? 350 LEU B CD1 1 
ATOM   5921 C CD2 . LEU B 1 321 ? 18.099  16.574  23.126  1.00 107.32 ? 350 LEU B CD2 1 
ATOM   5922 N N   . ARG B 1 322 ? 20.778  19.522  23.404  1.00 87.57  ? 351 ARG B N   1 
ATOM   5923 C CA  . ARG B 1 322 ? 21.434  20.527  24.270  1.00 87.62  ? 351 ARG B CA  1 
ATOM   5924 C C   . ARG B 1 322 ? 20.908  20.426  25.720  1.00 84.80  ? 351 ARG B C   1 
ATOM   5925 O O   . ARG B 1 322 ? 20.335  21.423  26.188  1.00 71.35  ? 351 ARG B O   1 
ATOM   5926 C CB  . ARG B 1 322 ? 21.117  21.879  23.628  1.00 90.61  ? 351 ARG B CB  1 
ATOM   5927 N N   . LYS B 1 323 ? 21.113  19.289  26.392  1.00 95.04  ? 352 LYS B N   1 
ATOM   5928 C CA  . LYS B 1 323 ? 20.734  19.103  27.829  1.00 101.73 ? 352 LYS B CA  1 
ATOM   5929 C C   . LYS B 1 323 ? 20.624  17.605  28.108  1.00 89.24  ? 352 LYS B C   1 
ATOM   5930 O O   . LYS B 1 323 ? 20.437  16.843  27.149  1.00 91.92  ? 352 LYS B O   1 
ATOM   5931 C CB  . LYS B 1 323 ? 19.383  19.581  28.369  1.00 109.19 ? 352 LYS B CB  1 
ATOM   5932 N N   . THR B 1 324 ? 20.720  17.225  29.377  1.00 71.12  ? 353 THR B N   1 
ATOM   5933 C CA  . THR B 1 324 ? 20.589  15.800  29.751  1.00 73.51  ? 353 THR B CA  1 
ATOM   5934 C C   . THR B 1 324 ? 19.352  15.246  29.092  1.00 65.94  ? 353 THR B C   1 
ATOM   5935 O O   . THR B 1 324 ? 18.235  15.614  29.517  1.00 62.71  ? 353 THR B O   1 
ATOM   5936 C CB  . THR B 1 324 ? 20.542  15.623  31.267  1.00 80.08  ? 353 THR B CB  1 
ATOM   5937 O OG1 . THR B 1 324 ? 21.784  16.125  31.749  1.00 85.94  ? 353 THR B OG1 1 
ATOM   5938 C CG2 . THR B 1 324 ? 20.388  14.165  31.662  1.00 80.40  ? 353 THR B CG2 1 
ATOM   5939 N N   . ASP B 1 325 ? 19.539  14.409  28.077  1.00 58.51  ? 354 ASP B N   1 
ATOM   5940 C CA  . ASP B 1 325 ? 18.442  13.778  27.365  1.00 50.15  ? 354 ASP B CA  1 
ATOM   5941 C C   . ASP B 1 325 ? 17.459  13.181  28.375  1.00 50.67  ? 354 ASP B C   1 
ATOM   5942 O O   . ASP B 1 325 ? 17.837  12.430  29.274  1.00 50.05  ? 354 ASP B O   1 
ATOM   5943 C CB  . ASP B 1 325 ? 19.032  12.785  26.384  1.00 51.82  ? 354 ASP B CB  1 
ATOM   5944 C CG  . ASP B 1 325 ? 18.088  12.212  25.342  1.00 55.59  ? 354 ASP B CG  1 
ATOM   5945 O OD1 . ASP B 1 325 ? 16.856  12.283  25.554  1.00 51.38  ? 354 ASP B OD1 1 
ATOM   5946 O OD2 . ASP B 1 325 ? 18.610  11.707  24.324  1.00 58.36  ? 354 ASP B OD2 1 
ATOM   5947 N N   . PRO B 1 326 ? 16.158  13.539  28.307  1.00 52.87  ? 355 PRO B N   1 
ATOM   5948 C CA  . PRO B 1 326 ? 15.134  12.839  29.089  1.00 51.88  ? 355 PRO B CA  1 
ATOM   5949 C C   . PRO B 1 326 ? 15.179  11.330  28.868  1.00 41.35  ? 355 PRO B C   1 
ATOM   5950 O O   . PRO B 1 326 ? 14.771  10.570  29.744  1.00 40.26  ? 355 PRO B O   1 
ATOM   5951 C CB  . PRO B 1 326 ? 13.797  13.453  28.611  1.00 50.83  ? 355 PRO B CB  1 
ATOM   5952 C CG  . PRO B 1 326 ? 14.199  14.790  28.053  1.00 52.31  ? 355 PRO B CG  1 
ATOM   5953 C CD  . PRO B 1 326 ? 15.610  14.628  27.486  1.00 51.54  ? 355 PRO B CD  1 
ATOM   5954 N N   . ARG B 1 327 ? 15.662  10.915  27.689  1.00 43.56  ? 356 ARG B N   1 
ATOM   5955 C CA  . ARG B 1 327 ? 15.761  9.502   27.348  1.00 45.76  ? 356 ARG B CA  1 
ATOM   5956 C C   . ARG B 1 327 ? 16.771  8.800   28.275  1.00 44.80  ? 356 ARG B C   1 
ATOM   5957 O O   . ARG B 1 327 ? 16.584  7.629   28.606  1.00 42.90  ? 356 ARG B O   1 
ATOM   5958 C CB  . ARG B 1 327 ? 15.996  9.341   25.837  1.00 45.54  ? 356 ARG B CB  1 
ATOM   5959 C CG  . ARG B 1 327 ? 14.833  9.705   24.916  1.00 47.89  ? 356 ARG B CG  1 
ATOM   5960 C CD  . ARG B 1 327 ? 15.059  9.395   23.402  1.00 44.40  ? 356 ARG B CD  1 
ATOM   5961 N NE  . ARG B 1 327 ? 16.194  10.181  22.913  1.00 40.69  ? 356 ARG B NE  1 
ATOM   5962 C CZ  . ARG B 1 327 ? 16.837  10.140  21.753  1.00 42.76  ? 356 ARG B CZ  1 
ATOM   5963 N NH1 . ARG B 1 327 ? 16.379  9.474   20.700  1.00 43.38  ? 356 ARG B NH1 1 
ATOM   5964 N NH2 . ARG B 1 327 ? 17.967  10.810  21.656  1.00 44.80  ? 356 ARG B NH2 1 
ATOM   5965 N N   . TYR B 1 328 ? 17.804  9.519   28.753  1.00 51.55  ? 357 TYR B N   1 
ATOM   5966 C CA  . TYR B 1 328 ? 18.737  9.005   29.762  1.00 46.08  ? 357 TYR B CA  1 
ATOM   5967 C C   . TYR B 1 328 ? 18.110  8.938   31.157  1.00 45.92  ? 357 TYR B C   1 
ATOM   5968 O O   . TYR B 1 328 ? 18.219  7.898   31.838  1.00 39.90  ? 357 TYR B O   1 
ATOM   5969 C CB  . TYR B 1 328 ? 19.978  9.894   29.847  1.00 49.39  ? 357 TYR B CB  1 
ATOM   5970 C CG  . TYR B 1 328 ? 21.061  9.472   30.830  1.00 48.83  ? 357 TYR B CG  1 
ATOM   5971 C CD1 . TYR B 1 328 ? 21.019  9.880   32.162  1.00 58.89  ? 357 TYR B CD1 1 
ATOM   5972 C CD2 . TYR B 1 328 ? 22.170  8.740   30.420  1.00 49.72  ? 357 TYR B CD2 1 
ATOM   5973 C CE1 . TYR B 1 328 ? 22.016  9.540   33.067  1.00 57.11  ? 357 TYR B CE1 1 
ATOM   5974 C CE2 . TYR B 1 328 ? 23.180  8.401   31.311  1.00 53.15  ? 357 TYR B CE2 1 
ATOM   5975 C CZ  . TYR B 1 328 ? 23.108  8.807   32.637  1.00 56.35  ? 357 TYR B CZ  1 
ATOM   5976 O OH  . TYR B 1 328 ? 24.081  8.485   33.541  1.00 46.46  ? 357 TYR B OH  1 
ATOM   5977 N N   . THR B 1 329 ? 17.506  10.065  31.588  1.00 41.91  ? 358 THR B N   1 
ATOM   5978 C CA  . THR B 1 329 ? 16.875  10.169  32.895  1.00 44.29  ? 358 THR B CA  1 
ATOM   5979 C C   . THR B 1 329 ? 15.900  9.005   33.094  1.00 47.01  ? 358 THR B C   1 
ATOM   5980 O O   . THR B 1 329 ? 15.878  8.394   34.166  1.00 48.83  ? 358 THR B O   1 
ATOM   5981 C CB  . THR B 1 329 ? 16.172  11.522  33.029  1.00 43.92  ? 358 THR B CB  1 
ATOM   5982 O OG1 . THR B 1 329 ? 17.195  12.482  32.810  1.00 47.25  ? 358 THR B OG1 1 
ATOM   5983 C CG2 . THR B 1 329 ? 15.559  11.745  34.400  1.00 45.13  ? 358 THR B CG2 1 
ATOM   5984 N N   . CYS B 1 330 ? 15.084  8.743   32.056  1.00 44.25  ? 359 CYS B N   1 
ATOM   5985 C CA  . CYS B 1 330 ? 14.231  7.568   31.954  1.00 46.13  ? 359 CYS B CA  1 
ATOM   5986 C C   . CYS B 1 330 ? 14.875  6.291   32.497  1.00 36.25  ? 359 CYS B C   1 
ATOM   5987 O O   . CYS B 1 330 ? 14.302  5.595   33.332  1.00 38.45  ? 359 CYS B O   1 
ATOM   5988 C CB  . CYS B 1 330 ? 13.907  7.271   30.489  1.00 48.49  ? 359 CYS B CB  1 
ATOM   5989 S SG  . CYS B 1 330 ? 12.294  7.896   29.999  1.00 67.65  ? 359 CYS B SG  1 
ATOM   5990 N N   . GLN B 1 331 ? 16.031  5.944   31.944  1.00 34.56  ? 360 GLN B N   1 
ATOM   5991 C CA  . GLN B 1 331 ? 16.671  4.672   32.254  1.00 38.94  ? 360 GLN B CA  1 
ATOM   5992 C C   . GLN B 1 331 ? 17.287  4.756   33.660  1.00 39.31  ? 360 GLN B C   1 
ATOM   5993 O O   . GLN B 1 331 ? 17.237  3.802   34.434  1.00 43.50  ? 360 GLN B O   1 
ATOM   5994 C CB  . GLN B 1 331 ? 17.646  4.372   31.108  1.00 43.57  ? 360 GLN B CB  1 
ATOM   5995 C CG  . GLN B 1 331 ? 16.979  4.311   29.732  1.00 45.44  ? 360 GLN B CG  1 
ATOM   5996 C CD  . GLN B 1 331 ? 17.900  3.965   28.578  1.00 48.01  ? 360 GLN B CD  1 
ATOM   5997 O OE1 . GLN B 1 331 ? 18.221  2.798   28.347  1.00 48.08  ? 360 GLN B OE1 1 
ATOM   5998 N NE2 . GLN B 1 331 ? 18.268  4.967   27.786  1.00 46.81  ? 360 GLN B NE2 1 
ATOM   5999 N N   . ARG B 1 332 ? 17.815  5.930   34.017  1.00 40.39  ? 361 ARG B N   1 
ATOM   6000 C CA  . ARG B 1 332 ? 18.445  6.140   35.322  1.00 39.95  ? 361 ARG B CA  1 
ATOM   6001 C C   . ARG B 1 332 ? 17.464  5.885   36.466  1.00 40.33  ? 361 ARG B C   1 
ATOM   6002 O O   . ARG B 1 332 ? 17.762  5.123   37.391  1.00 42.14  ? 361 ARG B O   1 
ATOM   6003 C CB  . ARG B 1 332 ? 19.064  7.536   35.417  1.00 42.02  ? 361 ARG B CB  1 
ATOM   6004 C CG  . ARG B 1 332 ? 19.601  7.844   36.809  1.00 45.93  ? 361 ARG B CG  1 
ATOM   6005 C CD  . ARG B 1 332 ? 20.311  9.205   36.887  1.00 49.20  ? 361 ARG B CD  1 
ATOM   6006 N NE  . ARG B 1 332 ? 20.646  9.547   38.275  1.00 49.89  ? 361 ARG B NE  1 
ATOM   6007 C CZ  . ARG B 1 332 ? 21.464  8.862   39.078  1.00 54.41  ? 361 ARG B CZ  1 
ATOM   6008 N NH1 . ARG B 1 332 ? 21.947  7.691   38.724  1.00 60.41  ? 361 ARG B NH1 1 
ATOM   6009 N NH2 . ARG B 1 332 ? 21.777  9.329   40.271  1.00 58.07  ? 361 ARG B NH2 1 
ATOM   6010 N N   . GLU B 1 333 ? 16.303  6.536   36.412  1.00 37.02  ? 362 GLU B N   1 
ATOM   6011 C CA  . GLU B 1 333 ? 15.222  6.269   37.352  1.00 37.29  ? 362 GLU B CA  1 
ATOM   6012 C C   . GLU B 1 333 ? 14.878  4.778   37.363  1.00 42.57  ? 362 GLU B C   1 
ATOM   6013 O O   . GLU B 1 333 ? 14.567  4.178   38.415  1.00 38.39  ? 362 GLU B O   1 
ATOM   6014 C CB  . GLU B 1 333 ? 13.993  7.106   36.982  1.00 40.85  ? 362 GLU B CB  1 
ATOM   6015 C CG  . GLU B 1 333 ? 14.244  8.619   37.057  1.00 46.57  ? 362 GLU B CG  1 
ATOM   6016 C CD  . GLU B 1 333 ? 13.284  9.521   36.294  1.00 49.44  ? 362 GLU B CD  1 
ATOM   6017 O OE1 . GLU B 1 333 ? 12.497  8.956   35.503  1.00 49.39  ? 362 GLU B OE1 1 
ATOM   6018 O OE2 . GLU B 1 333 ? 13.317  10.773  36.464  1.00 57.16  ? 362 GLU B OE2 1 
ATOM   6019 N N   . PHE B 1 334 ? 14.929  4.174   36.169  1.00 40.16  ? 363 PHE B N   1 
ATOM   6020 C CA  . PHE B 1 334 ? 14.598  2.766   36.040  1.00 38.51  ? 363 PHE B CA  1 
ATOM   6021 C C   . PHE B 1 334 ? 15.599  1.947   36.859  1.00 42.75  ? 363 PHE B C   1 
ATOM   6022 O O   . PHE B 1 334 ? 15.215  1.028   37.613  1.00 37.33  ? 363 PHE B O   1 
ATOM   6023 C CB  . PHE B 1 334 ? 14.578  2.325   34.574  1.00 33.64  ? 363 PHE B CB  1 
ATOM   6024 C CG  . PHE B 1 334 ? 14.179  0.866   34.463  1.00 35.69  ? 363 PHE B CG  1 
ATOM   6025 C CD1 . PHE B 1 334 ? 15.142  -0.132  34.563  1.00 34.85  ? 363 PHE B CD1 1 
ATOM   6026 C CD2 . PHE B 1 334 ? 12.838  0.501   34.335  1.00 31.30  ? 363 PHE B CD2 1 
ATOM   6027 C CE1 . PHE B 1 334 ? 14.775  -1.466  34.503  1.00 35.79  ? 363 PHE B CE1 1 
ATOM   6028 C CE2 . PHE B 1 334 ? 12.486  -0.834  34.242  1.00 31.60  ? 363 PHE B CE2 1 
ATOM   6029 C CZ  . PHE B 1 334 ? 13.450  -1.812  34.335  1.00 36.62  ? 363 PHE B CZ  1 
ATOM   6030 N N   . ALA B 1 335 ? 16.882  2.292   36.678  1.00 40.74  ? 364 ALA B N   1 
ATOM   6031 C CA  . ALA B 1 335 ? 17.974  1.510   37.251  1.00 50.17  ? 364 ALA B CA  1 
ATOM   6032 C C   . ALA B 1 335 ? 18.045  1.717   38.769  1.00 47.46  ? 364 ALA B C   1 
ATOM   6033 O O   . ALA B 1 335 ? 18.312  0.774   39.513  1.00 42.79  ? 364 ALA B O   1 
ATOM   6034 C CB  . ALA B 1 335 ? 19.273  1.864   36.556  1.00 49.66  ? 364 ALA B CB  1 
ATOM   6035 N N   . LEU B 1 336 ? 17.783  2.954   39.213  1.00 51.48  ? 365 LEU B N   1 
ATOM   6036 C CA  . LEU B 1 336 ? 17.815  3.306   40.623  1.00 51.14  ? 365 LEU B CA  1 
ATOM   6037 C C   . LEU B 1 336 ? 16.731  2.523   41.358  1.00 49.92  ? 365 LEU B C   1 
ATOM   6038 O O   . LEU B 1 336 ? 16.956  2.063   42.467  1.00 54.28  ? 365 LEU B O   1 
ATOM   6039 C CB  . LEU B 1 336 ? 17.661  4.815   40.810  1.00 55.11  ? 365 LEU B CB  1 
ATOM   6040 C CG  . LEU B 1 336 ? 18.852  5.688   40.383  1.00 54.71  ? 365 LEU B CG  1 
ATOM   6041 C CD1 . LEU B 1 336 ? 18.444  7.150   40.270  1.00 51.75  ? 365 LEU B CD1 1 
ATOM   6042 C CD2 . LEU B 1 336 ? 20.023  5.568   41.356  1.00 56.63  ? 365 LEU B CD2 1 
ATOM   6043 N N   . LYS B 1 337 ? 15.571  2.329   40.729  1.00 48.43  ? 366 LYS B N   1 
ATOM   6044 C CA  . LYS B 1 337 ? 14.526  1.521   41.327  1.00 47.98  ? 366 LYS B CA  1 
ATOM   6045 C C   . LYS B 1 337 ? 14.910  0.040   41.371  1.00 46.59  ? 366 LYS B C   1 
ATOM   6046 O O   . LYS B 1 337 ? 14.640  -0.624  42.371  1.00 42.59  ? 366 LYS B O   1 
ATOM   6047 C CB  . LYS B 1 337 ? 13.179  1.605   40.597  1.00 48.94  ? 366 LYS B CB  1 
ATOM   6048 C CG  . LYS B 1 337 ? 12.403  2.874   40.782  1.00 54.04  ? 366 LYS B CG  1 
ATOM   6049 C CD  . LYS B 1 337 ? 11.276  3.030   39.773  1.00 56.77  ? 366 LYS B CD  1 
ATOM   6050 C CE  . LYS B 1 337 ? 10.762  4.436   39.748  1.00 59.63  ? 366 LYS B CE  1 
ATOM   6051 N NZ  . LYS B 1 337 ? 9.868   4.654   38.613  1.00 60.75  ? 366 LYS B NZ  1 
ATOM   6052 N N   . HIS B 1 338 ? 15.476  -0.496  40.282  1.00 44.78  ? 367 HIS B N   1 
ATOM   6053 C CA  . HIS B 1 338 ? 15.363  -1.926  40.027  1.00 43.96  ? 367 HIS B CA  1 
ATOM   6054 C C   . HIS B 1 338 ? 16.699  -2.660  40.119  1.00 41.33  ? 367 HIS B C   1 
ATOM   6055 O O   . HIS B 1 338 ? 16.707  -3.879  40.271  1.00 43.98  ? 367 HIS B O   1 
ATOM   6056 C CB  . HIS B 1 338 ? 14.693  -2.196  38.667  1.00 45.01  ? 367 HIS B CB  1 
ATOM   6057 C CG  . HIS B 1 338 ? 13.283  -1.687  38.545  1.00 52.25  ? 367 HIS B CG  1 
ATOM   6058 N ND1 . HIS B 1 338 ? 12.276  -2.025  39.429  1.00 52.43  ? 367 HIS B ND1 1 
ATOM   6059 C CD2 . HIS B 1 338 ? 12.705  -0.885  37.621  1.00 48.90  ? 367 HIS B CD2 1 
ATOM   6060 C CE1 . HIS B 1 338 ? 11.142  -1.441  39.056  1.00 51.98  ? 367 HIS B CE1 1 
ATOM   6061 N NE2 . HIS B 1 338 ? 11.382  -0.734  37.970  1.00 51.75  ? 367 HIS B NE2 1 
ATOM   6062 N N   . LEU B 1 339 ? 17.814  -1.947  39.965  1.00 37.87  ? 368 LEU B N   1 
ATOM   6063 C CA  . LEU B 1 339 ? 19.126  -2.568  40.028  1.00 42.75  ? 368 LEU B CA  1 
ATOM   6064 C C   . LEU B 1 339 ? 20.110  -1.588  40.644  1.00 42.55  ? 368 LEU B C   1 
ATOM   6065 O O   . LEU B 1 339 ? 21.126  -1.280  40.028  1.00 42.01  ? 368 LEU B O   1 
ATOM   6066 C CB  . LEU B 1 339 ? 19.631  -2.977  38.644  1.00 42.46  ? 368 LEU B CB  1 
ATOM   6067 C CG  . LEU B 1 339 ? 19.571  -1.911  37.546  1.00 41.53  ? 368 LEU B CG  1 
ATOM   6068 C CD1 . LEU B 1 339 ? 20.838  -1.896  36.722  1.00 41.32  ? 368 LEU B CD1 1 
ATOM   6069 C CD2 . LEU B 1 339 ? 18.367  -2.157  36.635  1.00 42.17  ? 368 LEU B CD2 1 
ATOM   6070 N N   . PRO B 1 340 ? 19.859  -1.066  41.865  1.00 41.21  ? 369 PRO B N   1 
ATOM   6071 C CA  . PRO B 1 340 ? 20.808  -0.130  42.463  1.00 43.46  ? 369 PRO B CA  1 
ATOM   6072 C C   . PRO B 1 340 ? 22.189  -0.744  42.767  1.00 42.86  ? 369 PRO B C   1 
ATOM   6073 O O   . PRO B 1 340 ? 23.194  -0.032  42.765  1.00 42.69  ? 369 PRO B O   1 
ATOM   6074 C CB  . PRO B 1 340 ? 20.066  0.383   43.724  1.00 43.20  ? 369 PRO B CB  1 
ATOM   6075 C CG  . PRO B 1 340 ? 18.951  -0.628  44.014  1.00 41.06  ? 369 PRO B CG  1 
ATOM   6076 C CD  . PRO B 1 340 ? 18.723  -1.409  42.740  1.00 41.02  ? 369 PRO B CD  1 
ATOM   6077 N N   . ASN B 1 341 ? 22.258  -2.073  42.968  1.00 45.25  ? 370 ASN B N   1 
ATOM   6078 C CA  . ASN B 1 341 ? 23.473  -2.717  43.455  1.00 46.92  ? 370 ASN B CA  1 
ATOM   6079 C C   . ASN B 1 341 ? 24.380  -3.217  42.331  1.00 53.35  ? 370 ASN B C   1 
ATOM   6080 O O   . ASN B 1 341 ? 25.442  -3.763  42.624  1.00 55.62  ? 370 ASN B O   1 
ATOM   6081 C CB  . ASN B 1 341 ? 23.156  -3.866  44.404  1.00 46.51  ? 370 ASN B CB  1 
ATOM   6082 C CG  . ASN B 1 341 ? 22.592  -3.349  45.711  1.00 51.14  ? 370 ASN B CG  1 
ATOM   6083 O OD1 . ASN B 1 341 ? 23.183  -2.456  46.333  1.00 62.03  ? 370 ASN B OD1 1 
ATOM   6084 N ND2 . ASN B 1 341 ? 21.429  -3.838  46.115  1.00 46.40  ? 370 ASN B ND2 1 
ATOM   6085 N N   . ASP B 1 342 ? 23.972  -3.019  41.064  1.00 56.77  ? 371 ASP B N   1 
ATOM   6086 C CA  . ASP B 1 342 ? 24.735  -3.476  39.911  1.00 50.76  ? 371 ASP B CA  1 
ATOM   6087 C C   . ASP B 1 342 ? 26.007  -2.641  39.746  1.00 46.04  ? 371 ASP B C   1 
ATOM   6088 O O   . ASP B 1 342 ? 25.929  -1.420  39.630  1.00 43.65  ? 371 ASP B O   1 
ATOM   6089 C CB  . ASP B 1 342 ? 23.941  -3.382  38.615  1.00 48.40  ? 371 ASP B CB  1 
ATOM   6090 C CG  . ASP B 1 342 ? 24.749  -3.739  37.373  1.00 43.58  ? 371 ASP B CG  1 
ATOM   6091 O OD1 . ASP B 1 342 ? 25.008  -4.939  37.185  1.00 42.62  ? 371 ASP B OD1 1 
ATOM   6092 O OD2 . ASP B 1 342 ? 25.185  -2.808  36.673  1.00 45.95  ? 371 ASP B OD2 1 
ATOM   6093 N N   . PRO B 1 343 ? 27.214  -3.270  39.712  1.00 50.19  ? 372 PRO B N   1 
ATOM   6094 C CA  . PRO B 1 343 ? 28.468  -2.541  39.456  1.00 44.04  ? 372 PRO B CA  1 
ATOM   6095 C C   . PRO B 1 343 ? 28.476  -1.550  38.287  1.00 44.24  ? 372 PRO B C   1 
ATOM   6096 O O   . PRO B 1 343 ? 28.879  -0.400  38.464  1.00 43.84  ? 372 PRO B O   1 
ATOM   6097 C CB  . PRO B 1 343 ? 29.494  -3.687  39.235  1.00 46.29  ? 372 PRO B CB  1 
ATOM   6098 C CG  . PRO B 1 343 ? 28.948  -4.853  40.041  1.00 47.45  ? 372 PRO B CG  1 
ATOM   6099 C CD  . PRO B 1 343 ? 27.430  -4.704  39.976  1.00 48.08  ? 372 PRO B CD  1 
ATOM   6100 N N   . MET B 1 344 ? 28.068  -1.998  37.087  1.00 41.94  ? 373 MET B N   1 
ATOM   6101 C CA  . MET B 1 344 ? 28.158  -1.173  35.887  1.00 47.05  ? 373 MET B CA  1 
ATOM   6102 C C   . MET B 1 344 ? 27.194  0.014   35.966  1.00 42.74  ? 373 MET B C   1 
ATOM   6103 O O   . MET B 1 344 ? 27.529  1.140   35.609  1.00 38.90  ? 373 MET B O   1 
ATOM   6104 C CB  . MET B 1 344 ? 27.821  -1.975  34.619  1.00 51.64  ? 373 MET B CB  1 
ATOM   6105 C CG  . MET B 1 344 ? 28.880  -2.992  34.232  1.00 62.48  ? 373 MET B CG  1 
ATOM   6106 S SD  . MET B 1 344 ? 30.432  -2.262  33.662  1.00 66.45  ? 373 MET B SD  1 
ATOM   6107 C CE  . MET B 1 344 ? 29.940  -1.720  32.019  1.00 61.51  ? 373 MET B CE  1 
ATOM   6108 N N   . PHE B 1 345 ? 25.953  -0.252  36.368  1.00 43.52  ? 374 PHE B N   1 
ATOM   6109 C CA  . PHE B 1 345 ? 25.034  0.844   36.592  1.00 44.45  ? 374 PHE B CA  1 
ATOM   6110 C C   . PHE B 1 345 ? 25.711  1.824   37.548  1.00 44.57  ? 374 PHE B C   1 
ATOM   6111 O O   . PHE B 1 345 ? 25.787  3.016   37.256  1.00 45.68  ? 374 PHE B O   1 
ATOM   6112 C CB  . PHE B 1 345 ? 23.678  0.404   37.159  1.00 51.13  ? 374 PHE B CB  1 
ATOM   6113 C CG  . PHE B 1 345 ? 22.897  1.592   37.704  1.00 52.50  ? 374 PHE B CG  1 
ATOM   6114 C CD1 . PHE B 1 345 ? 22.880  2.803   37.009  1.00 51.11  ? 374 PHE B CD1 1 
ATOM   6115 C CD2 . PHE B 1 345 ? 22.259  1.521   38.943  1.00 53.54  ? 374 PHE B CD2 1 
ATOM   6116 C CE1 . PHE B 1 345 ? 22.210  3.902   37.526  1.00 59.84  ? 374 PHE B CE1 1 
ATOM   6117 C CE2 . PHE B 1 345 ? 21.587  2.623   39.454  1.00 58.37  ? 374 PHE B CE2 1 
ATOM   6118 C CZ  . PHE B 1 345 ? 21.560  3.810   38.740  1.00 58.08  ? 374 PHE B CZ  1 
ATOM   6119 N N   . LYS B 1 346 ? 26.237  1.300   38.669  1.00 41.16  ? 375 LYS B N   1 
ATOM   6120 C CA  . LYS B 1 346 ? 26.888  2.148   39.666  1.00 47.22  ? 375 LYS B CA  1 
ATOM   6121 C C   . LYS B 1 346 ? 27.977  3.020   39.020  1.00 43.48  ? 375 LYS B C   1 
ATOM   6122 O O   . LYS B 1 346 ? 28.065  4.212   39.313  1.00 44.36  ? 375 LYS B O   1 
ATOM   6123 C CB  . LYS B 1 346 ? 27.409  1.302   40.829  1.00 47.49  ? 375 LYS B CB  1 
ATOM   6124 C CG  . LYS B 1 346 ? 26.390  0.859   41.881  1.00 48.48  ? 375 LYS B CG  1 
ATOM   6125 C CD  . LYS B 1 346 ? 27.124  0.150   43.020  1.00 58.43  ? 375 LYS B CD  1 
ATOM   6126 C CE  . LYS B 1 346 ? 26.524  0.312   44.385  1.00 62.38  ? 375 LYS B CE  1 
ATOM   6127 N NZ  . LYS B 1 346 ? 27.519  0.036   45.427  1.00 60.42  ? 375 LYS B NZ  1 
ATOM   6128 N N   . LEU B 1 347 ? 28.763  2.431   38.103  1.00 48.35  ? 376 LEU B N   1 
ATOM   6129 C CA  . LEU B 1 347 ? 29.784  3.157   37.366  1.00 41.72  ? 376 LEU B CA  1 
ATOM   6130 C C   . LEU B 1 347 ? 29.109  4.226   36.523  1.00 43.15  ? 376 LEU B C   1 
ATOM   6131 O O   . LEU B 1 347 ? 29.603  5.347   36.421  1.00 46.41  ? 376 LEU B O   1 
ATOM   6132 C CB  . LEU B 1 347 ? 30.617  2.230   36.485  1.00 43.51  ? 376 LEU B CB  1 
ATOM   6133 C CG  . LEU B 1 347 ? 31.536  2.916   35.464  1.00 49.25  ? 376 LEU B CG  1 
ATOM   6134 C CD1 . LEU B 1 347 ? 32.556  3.825   36.127  1.00 50.35  ? 376 LEU B CD1 1 
ATOM   6135 C CD2 . LEU B 1 347 ? 32.267  1.877   34.604  1.00 51.81  ? 376 LEU B CD2 1 
ATOM   6136 N N   . VAL B 1 348 ? 27.986  3.860   35.899  1.00 44.41  ? 377 VAL B N   1 
ATOM   6137 C CA  . VAL B 1 348 ? 27.316  4.798   35.018  1.00 49.74  ? 377 VAL B CA  1 
ATOM   6138 C C   . VAL B 1 348 ? 26.770  5.952   35.866  1.00 48.05  ? 377 VAL B C   1 
ATOM   6139 O O   . VAL B 1 348 ? 26.957  7.113   35.511  1.00 39.79  ? 377 VAL B O   1 
ATOM   6140 C CB  . VAL B 1 348 ? 26.268  4.088   34.135  1.00 53.47  ? 377 VAL B CB  1 
ATOM   6141 C CG1 . VAL B 1 348 ? 25.227  5.034   33.548  1.00 53.36  ? 377 VAL B CG1 1 
ATOM   6142 C CG2 . VAL B 1 348 ? 26.942  3.296   33.019  1.00 52.02  ? 377 VAL B CG2 1 
ATOM   6143 N N   . ALA B 1 349 ? 26.230  5.635   37.052  1.00 48.84  ? 378 ALA B N   1 
ATOM   6144 C CA  . ALA B 1 349 ? 25.789  6.654   38.002  1.00 56.07  ? 378 ALA B CA  1 
ATOM   6145 C C   . ALA B 1 349 ? 26.937  7.565   38.453  1.00 60.22  ? 378 ALA B C   1 
ATOM   6146 O O   . ALA B 1 349 ? 26.701  8.747   38.710  1.00 57.62  ? 378 ALA B O   1 
ATOM   6147 C CB  . ALA B 1 349 ? 25.114  6.008   39.193  1.00 53.92  ? 378 ALA B CB  1 
ATOM   6148 N N   . GLN B 1 350 ? 28.155  7.011   38.589  1.00 63.34  ? 379 GLN B N   1 
ATOM   6149 C CA  . GLN B 1 350 ? 29.335  7.788   38.963  1.00 65.98  ? 379 GLN B CA  1 
ATOM   6150 C C   . GLN B 1 350 ? 29.771  8.723   37.834  1.00 57.55  ? 379 GLN B C   1 
ATOM   6151 O O   . GLN B 1 350 ? 30.261  9.818   38.083  1.00 48.71  ? 379 GLN B O   1 
ATOM   6152 C CB  . GLN B 1 350 ? 30.572  6.931   39.232  1.00 71.17  ? 379 GLN B CB  1 
ATOM   6153 C CG  . GLN B 1 350 ? 30.841  6.600   40.698  1.00 73.07  ? 379 GLN B CG  1 
ATOM   6154 C CD  . GLN B 1 350 ? 32.042  5.689   40.870  1.00 72.64  ? 379 GLN B CD  1 
ATOM   6155 O OE1 . GLN B 1 350 ? 32.093  4.578   40.325  1.00 67.53  ? 379 GLN B OE1 1 
ATOM   6156 N NE2 . GLN B 1 350 ? 33.042  6.160   41.605  1.00 75.10  ? 379 GLN B NE2 1 
ATOM   6157 N N   . LEU B 1 351 ? 29.631  8.265   36.590  1.00 57.12  ? 380 LEU B N   1 
ATOM   6158 C CA  . LEU B 1 351 ? 30.063  9.037   35.442  1.00 53.23  ? 380 LEU B CA  1 
ATOM   6159 C C   . LEU B 1 351 ? 29.147  10.232  35.206  1.00 56.22  ? 380 LEU B C   1 
ATOM   6160 O O   . LEU B 1 351 ? 29.499  11.148  34.467  1.00 62.63  ? 380 LEU B O   1 
ATOM   6161 C CB  . LEU B 1 351 ? 30.050  8.055   34.283  1.00 57.47  ? 380 LEU B CB  1 
ATOM   6162 C CG  . LEU B 1 351 ? 31.191  7.037   34.292  1.00 58.19  ? 380 LEU B CG  1 
ATOM   6163 C CD1 . LEU B 1 351 ? 30.861  5.837   33.433  1.00 60.54  ? 380 LEU B CD1 1 
ATOM   6164 C CD2 . LEU B 1 351 ? 32.462  7.685   33.786  1.00 58.55  ? 380 LEU B CD2 1 
ATOM   6165 N N   . TYR B 1 352 ? 27.971  10.225  35.843  1.00 62.49  ? 381 TYR B N   1 
ATOM   6166 C CA  . TYR B 1 352 ? 26.997  11.290  35.641  1.00 70.55  ? 381 TYR B CA  1 
ATOM   6167 C C   . TYR B 1 352 ? 27.300  12.496  36.538  1.00 65.47  ? 381 TYR B C   1 
ATOM   6168 O O   . TYR B 1 352 ? 26.627  13.514  36.444  1.00 68.71  ? 381 TYR B O   1 
ATOM   6169 C CB  . TYR B 1 352 ? 25.594  10.707  35.863  1.00 70.79  ? 381 TYR B CB  1 
ATOM   6170 C CG  . TYR B 1 352 ? 24.423  11.645  35.576  1.00 71.64  ? 381 TYR B CG  1 
ATOM   6171 C CD1 . TYR B 1 352 ? 24.422  12.482  34.461  1.00 59.72  ? 381 TYR B CD1 1 
ATOM   6172 C CD2 . TYR B 1 352 ? 23.319  11.702  36.431  1.00 72.42  ? 381 TYR B CD2 1 
ATOM   6173 C CE1 . TYR B 1 352 ? 23.370  13.344  34.210  1.00 62.18  ? 381 TYR B CE1 1 
ATOM   6174 C CE2 . TYR B 1 352 ? 22.254  12.557  36.180  1.00 72.12  ? 381 TYR B CE2 1 
ATOM   6175 C CZ  . TYR B 1 352 ? 22.283  13.378  35.065  1.00 63.64  ? 381 TYR B CZ  1 
ATOM   6176 O OH  . TYR B 1 352 ? 21.256  14.230  34.792  1.00 71.63  ? 381 TYR B OH  1 
ATOM   6177 N N   . LYS B 1 353 ? 28.301  12.403  37.417  1.00 72.58  ? 382 LYS B N   1 
ATOM   6178 C CA  . LYS B 1 353 ? 28.731  13.567  38.177  1.00 73.89  ? 382 LYS B CA  1 
ATOM   6179 C C   . LYS B 1 353 ? 29.935  14.203  37.490  1.00 84.87  ? 382 LYS B C   1 
ATOM   6180 O O   . LYS B 1 353 ? 29.987  15.423  37.319  1.00 87.08  ? 382 LYS B O   1 
ATOM   6181 C CB  . LYS B 1 353 ? 29.086  13.187  39.613  1.00 75.66  ? 382 LYS B CB  1 
ATOM   6182 C CG  . LYS B 1 353 ? 28.109  12.218  40.282  1.00 84.16  ? 382 LYS B CG  1 
ATOM   6183 C CD  . LYS B 1 353 ? 28.610  11.662  41.614  1.00 85.45  ? 382 LYS B CD  1 
ATOM   6184 C CE  . LYS B 1 353 ? 28.525  12.649  42.739  1.00 82.67  ? 382 LYS B CE  1 
ATOM   6185 N NZ  . LYS B 1 353 ? 29.316  12.217  43.895  1.00 78.79  ? 382 LYS B NZ  1 
ATOM   6186 N N   . ILE B 1 354 ? 30.862  13.349  37.042  1.00 88.24  ? 383 ILE B N   1 
ATOM   6187 C CA  . ILE B 1 354 ? 32.217  13.763  36.724  1.00 96.82  ? 383 ILE B CA  1 
ATOM   6188 C C   . ILE B 1 354 ? 32.316  14.334  35.312  1.00 97.80  ? 383 ILE B C   1 
ATOM   6189 O O   . ILE B 1 354 ? 32.716  15.482  35.162  1.00 108.38 ? 383 ILE B O   1 
ATOM   6190 C CB  . ILE B 1 354 ? 33.186  12.584  36.924  1.00 108.29 ? 383 ILE B CB  1 
ATOM   6191 C CG1 . ILE B 1 354 ? 33.173  12.084  38.380  1.00 104.10 ? 383 ILE B CG1 1 
ATOM   6192 C CG2 . ILE B 1 354 ? 34.593  12.949  36.441  1.00 115.86 ? 383 ILE B CG2 1 
ATOM   6193 C CD1 . ILE B 1 354 ? 33.329  13.175  39.427  1.00 105.17 ? 383 ILE B CD1 1 
ATOM   6194 N N   . VAL B 1 355 ? 32.012  13.528  34.284  1.00 97.23  ? 384 VAL B N   1 
ATOM   6195 C CA  . VAL B 1 355 ? 32.233  13.940  32.903  1.00 99.23  ? 384 VAL B CA  1 
ATOM   6196 C C   . VAL B 1 355 ? 31.547  15.285  32.652  1.00 97.64  ? 384 VAL B C   1 
ATOM   6197 O O   . VAL B 1 355 ? 32.046  16.092  31.862  1.00 98.52  ? 384 VAL B O   1 
ATOM   6198 C CB  . VAL B 1 355 ? 31.790  12.867  31.886  1.00 94.88  ? 384 VAL B CB  1 
ATOM   6199 C CG1 . VAL B 1 355 ? 31.674  13.416  30.464  1.00 91.83  ? 384 VAL B CG1 1 
ATOM   6200 C CG2 . VAL B 1 355 ? 32.728  11.668  31.917  1.00 95.01  ? 384 VAL B CG2 1 
ATOM   6201 N N   . PRO B 1 356 ? 30.385  15.568  33.295  1.00 92.93  ? 385 PRO B N   1 
ATOM   6202 C CA  . PRO B 1 356 ? 29.879  16.940  33.404  1.00 91.46  ? 385 PRO B CA  1 
ATOM   6203 C C   . PRO B 1 356 ? 30.710  17.806  34.354  1.00 86.32  ? 385 PRO B C   1 
ATOM   6204 O O   . PRO B 1 356 ? 30.156  18.537  35.169  1.00 82.88  ? 385 PRO B O   1 
ATOM   6205 C CB  . PRO B 1 356 ? 28.421  16.750  33.906  1.00 91.03  ? 385 PRO B CB  1 
ATOM   6206 C CG  . PRO B 1 356 ? 28.121  15.275  33.716  1.00 84.21  ? 385 PRO B CG  1 
ATOM   6207 C CD  . PRO B 1 356 ? 29.457  14.586  33.886  1.00 87.48  ? 385 PRO B CD  1 
ATOM   6208 N N   . ASN B 1 357 ? 32.033  17.777  34.128  1.00 96.87  ? 386 ASN B N   1 
ATOM   6209 C CA  . ASN B 1 357 ? 32.945  18.699  34.852  1.00 89.70  ? 386 ASN B CA  1 
ATOM   6210 C C   . ASN B 1 357 ? 33.008  19.953  33.985  1.00 101.08 ? 386 ASN B C   1 
ATOM   6211 O O   . ASN B 1 357 ? 34.050  20.645  34.024  1.00 101.68 ? 386 ASN B O   1 
ATOM   6212 C CB  . ASN B 1 357 ? 34.333  18.104  35.060  1.00 81.63  ? 386 ASN B CB  1 
ATOM   6213 C CG  . ASN B 1 357 ? 34.972  17.660  33.765  1.00 72.41  ? 386 ASN B CG  1 
ATOM   6214 O OD1 . ASN B 1 357 ? 34.722  16.545  33.295  1.00 69.91  ? 386 ASN B OD1 1 
ATOM   6215 N ND2 . ASN B 1 357 ? 35.802  18.509  33.176  1.00 66.27  ? 386 ASN B ND2 1 
ATOM   6216 N N   . VAL B 1 358 ? 32.054  20.376  33.352  1.00 110.76 ? 387 VAL B N   1 
ATOM   6217 C CA  . VAL B 1 358 ? 31.929  21.391  32.260  1.00 106.61 ? 387 VAL B CA  1 
ATOM   6218 C C   . VAL B 1 358 ? 33.042  21.090  31.241  1.00 107.98 ? 387 VAL B C   1 
ATOM   6219 O O   . VAL B 1 358 ? 34.023  21.862  31.186  1.00 114.44 ? 387 VAL B O   1 
ATOM   6220 C CB  . VAL B 1 358 ? 31.954  22.865  32.717  1.00 103.08 ? 387 VAL B CB  1 
ATOM   6221 C CG1 . VAL B 1 358 ? 31.471  23.803  31.617  1.00 103.89 ? 387 VAL B CG1 1 
ATOM   6222 C CG2 . VAL B 1 358 ? 31.138  23.077  33.988  1.00 101.71 ? 387 VAL B CG2 1 
ATOM   6223 N N   . LEU B 1 359 ? 32.824  20.128  30.337  1.00 118.71 ? 388 LEU B N   1 
ATOM   6224 C CA  . LEU B 1 359 ? 33.844  19.784  29.309  1.00 130.43 ? 388 LEU B CA  1 
ATOM   6225 C C   . LEU B 1 359 ? 33.906  20.902  28.254  1.00 134.12 ? 388 LEU B C   1 
ATOM   6226 O O   . LEU B 1 359 ? 34.620  20.721  27.244  1.00 118.97 ? 388 LEU B O   1 
ATOM   6227 C CB  . LEU B 1 359 ? 33.539  18.426  28.677  1.00 131.32 ? 388 LEU B CB  1 
ATOM   6228 C CG  . LEU B 1 359 ? 32.091  18.198  28.230  1.00 129.08 ? 388 LEU B CG  1 
ATOM   6229 C CD1 . LEU B 1 359 ? 31.968  18.285  26.719  1.00 123.23 ? 388 LEU B CD1 1 
ATOM   6230 C CD2 . LEU B 1 359 ? 31.592  16.850  28.718  1.00 127.04 ? 388 LEU B CD2 1 
ATOM   6231 N N   . LEU B 1 360 ? 33.207  22.017  28.490  1.00 147.21 ? 389 LEU B N   1 
ATOM   6232 C CA  . LEU B 1 360 ? 33.244  23.175  27.560  1.00 152.35 ? 389 LEU B CA  1 
ATOM   6233 C C   . LEU B 1 360 ? 34.646  23.802  27.578  1.00 151.25 ? 389 LEU B C   1 
ATOM   6234 O O   . LEU B 1 360 ? 34.895  24.701  26.750  1.00 165.27 ? 389 LEU B O   1 
ATOM   6235 C CB  . LEU B 1 360 ? 32.176  24.184  27.975  1.00 157.93 ? 389 LEU B CB  1 
ATOM   6236 C CG  . LEU B 1 360 ? 30.920  24.224  27.100  1.00 162.33 ? 389 LEU B CG  1 
ATOM   6237 C CD1 . LEU B 1 360 ? 31.291  24.283  25.628  1.00 162.42 ? 389 LEU B CD1 1 
ATOM   6238 C CD2 . LEU B 1 360 ? 30.023  23.032  27.384  1.00 152.64 ? 389 LEU B CD2 1 
ATOM   6239 N N   . GLU B 1 361 ? 35.518  23.365  28.493  1.00 136.33 ? 390 GLU B N   1 
ATOM   6240 C CA  . GLU B 1 361 ? 36.918  23.861  28.504  1.00 127.52 ? 390 GLU B CA  1 
ATOM   6241 C C   . GLU B 1 361 ? 37.483  23.736  27.082  1.00 138.06 ? 390 GLU B C   1 
ATOM   6242 O O   . GLU B 1 361 ? 38.057  24.727  26.581  1.00 153.96 ? 390 GLU B O   1 
ATOM   6243 C CB  . GLU B 1 361 ? 37.782  23.067  29.482  1.00 112.21 ? 390 GLU B CB  1 
ATOM   6244 C CG  . GLU B 1 361 ? 37.052  21.890  30.123  1.00 95.45  ? 390 GLU B CG  1 
ATOM   6245 C CD  . GLU B 1 361 ? 37.352  20.534  29.513  1.00 82.46  ? 390 GLU B CD  1 
ATOM   6246 O OE1 . GLU B 1 361 ? 37.663  20.477  28.305  1.00 72.55  ? 390 GLU B OE1 1 
ATOM   6247 O OE2 . GLU B 1 361 ? 37.274  19.530  30.252  1.00 77.28  ? 390 GLU B OE2 1 
ATOM   6248 N N   . GLN B 1 362 ? 37.320  22.564  26.461  1.00 135.86 ? 391 GLN B N   1 
ATOM   6249 C CA  . GLN B 1 362 ? 37.791  22.371  25.066  1.00 127.83 ? 391 GLN B CA  1 
ATOM   6250 C C   . GLN B 1 362 ? 36.891  23.171  24.112  1.00 121.97 ? 391 GLN B C   1 
ATOM   6251 O O   . GLN B 1 362 ? 37.408  23.660  23.085  1.00 110.12 ? 391 GLN B O   1 
ATOM   6252 C CB  . GLN B 1 362 ? 37.787  20.898  24.665  1.00 121.21 ? 391 GLN B CB  1 
ATOM   6253 C CG  . GLN B 1 362 ? 38.908  20.526  23.701  1.00 113.51 ? 391 GLN B CG  1 
ATOM   6254 C CD  . GLN B 1 362 ? 38.621  19.272  22.906  1.00 109.06 ? 391 GLN B CD  1 
ATOM   6255 O OE1 . GLN B 1 362 ? 39.429  18.833  22.081  1.00 92.44  ? 391 GLN B OE1 1 
ATOM   6256 N NE2 . GLN B 1 362 ? 37.459  18.684  23.148  1.00 116.25 ? 391 GLN B NE2 1 
ATOM   6257 N N   . GLY B 1 363 ? 35.601  23.298  24.437  1.00 124.90 ? 392 GLY B N   1 
ATOM   6258 C CA  . GLY B 1 363 ? 34.720  24.083  23.586  1.00 124.90 ? 392 GLY B CA  1 
ATOM   6259 C C   . GLY B 1 363 ? 34.271  23.318  22.341  1.00 126.99 ? 392 GLY B C   1 
ATOM   6260 O O   . GLY B 1 363 ? 33.721  23.927  21.427  1.00 123.51 ? 392 GLY B O   1 
ATOM   6261 N N   . LYS B 1 364 ? 34.484  21.991  22.326  1.00 133.05 ? 393 LYS B N   1 
ATOM   6262 C CA  . LYS B 1 364 ? 34.305  21.167  21.134  1.00 136.97 ? 393 LYS B CA  1 
ATOM   6263 C C   . LYS B 1 364 ? 33.253  20.092  21.398  1.00 129.70 ? 393 LYS B C   1 
ATOM   6264 O O   . LYS B 1 364 ? 33.585  18.999  21.856  1.00 125.65 ? 393 LYS B O   1 
ATOM   6265 C CB  . LYS B 1 364 ? 35.619  20.505  20.690  1.00 140.61 ? 393 LYS B CB  1 
ATOM   6266 C CG  . LYS B 1 364 ? 36.351  21.114  19.490  1.00 134.70 ? 393 LYS B CG  1 
ATOM   6267 C CD  . LYS B 1 364 ? 37.820  20.703  19.402  1.00 132.94 ? 393 LYS B CD  1 
ATOM   6268 C CE  . LYS B 1 364 ? 38.837  21.737  19.813  1.00 137.63 ? 393 LYS B CE  1 
ATOM   6269 N NZ  . LYS B 1 364 ? 38.368  22.800  20.710  1.00 142.69 ? 393 LYS B NZ  1 
ATOM   6270 N N   . ALA B 1 365 ? 31.964  20.446  21.249  1.00 129.33 ? 394 ALA B N   1 
ATOM   6271 C CA  . ALA B 1 365 ? 30.825  19.505  21.461  1.00 130.26 ? 394 ALA B CA  1 
ATOM   6272 C C   . ALA B 1 365 ? 29.521  20.297  21.544  1.00 127.22 ? 394 ALA B C   1 
ATOM   6273 O O   . ALA B 1 365 ? 28.523  19.849  20.935  1.00 103.63 ? 394 ALA B O   1 
ATOM   6274 C CB  . ALA B 1 365 ? 30.951  18.675  22.726  1.00 133.53 ? 394 ALA B CB  1 
ATOM   6275 N N   . LYS B 1 366 ? 29.518  21.394  22.311  1.00 139.52 ? 395 LYS B N   1 
ATOM   6276 C CA  . LYS B 1 366 ? 28.274  22.182  22.535  1.00 135.77 ? 395 LYS B CA  1 
ATOM   6277 C C   . LYS B 1 366 ? 27.240  21.274  23.226  1.00 137.82 ? 395 LYS B C   1 
ATOM   6278 O O   . LYS B 1 366 ? 26.027  21.490  23.005  1.00 141.06 ? 395 LYS B O   1 
ATOM   6279 C CB  . LYS B 1 366 ? 27.736  22.798  21.237  1.00 126.38 ? 395 LYS B CB  1 
ATOM   6280 N N   . ASN B 1 367 ? 27.707  20.313  24.032  1.00 139.32 ? 396 ASN B N   1 
ATOM   6281 C CA  . ASN B 1 367 ? 26.794  19.376  24.747  1.00 139.74 ? 396 ASN B CA  1 
ATOM   6282 C C   . ASN B 1 367 ? 27.570  18.639  25.842  1.00 115.09 ? 396 ASN B C   1 
ATOM   6283 O O   . ASN B 1 367 ? 28.170  17.589  25.535  1.00 111.07 ? 396 ASN B O   1 
ATOM   6284 C CB  . ASN B 1 367 ? 26.134  18.383  23.796  1.00 153.48 ? 396 ASN B CB  1 
ATOM   6285 C CG  . ASN B 1 367 ? 24.710  18.075  24.194  1.00 164.64 ? 396 ASN B CG  1 
ATOM   6286 O OD1 . ASN B 1 367 ? 24.329  18.274  25.353  1.00 184.99 ? 396 ASN B OD1 1 
ATOM   6287 N ND2 . ASN B 1 367 ? 23.911  17.592  23.254  1.00 157.53 ? 396 ASN B ND2 1 
ATOM   6288 N N   . PRO B 1 368 ? 27.590  19.129  27.101  1.00 95.42  ? 397 PRO B N   1 
ATOM   6289 C CA  . PRO B 1 368 ? 28.239  18.408  28.207  1.00 87.95  ? 397 PRO B CA  1 
ATOM   6290 C C   . PRO B 1 368 ? 27.414  17.405  29.018  1.00 81.21  ? 397 PRO B C   1 
ATOM   6291 O O   . PRO B 1 368 ? 27.770  17.097  30.156  1.00 77.57  ? 397 PRO B O   1 
ATOM   6292 C CB  . PRO B 1 368 ? 28.643  19.613  29.078  1.00 87.45  ? 397 PRO B CB  1 
ATOM   6293 C CG  . PRO B 1 368 ? 27.450  20.531  28.986  1.00 88.06  ? 397 PRO B CG  1 
ATOM   6294 C CD  . PRO B 1 368 ? 26.958  20.383  27.547  1.00 90.76  ? 397 PRO B CD  1 
ATOM   6295 N N   . TRP B 1 369 ? 26.329  16.885  28.423  1.00 81.96  ? 398 TRP B N   1 
ATOM   6296 C CA  . TRP B 1 369 ? 25.343  16.074  29.128  1.00 73.17  ? 398 TRP B CA  1 
ATOM   6297 C C   . TRP B 1 369 ? 25.142  14.738  28.413  1.00 59.56  ? 398 TRP B C   1 
ATOM   6298 O O   . TRP B 1 369 ? 25.341  14.645  27.202  1.00 57.83  ? 398 TRP B O   1 
ATOM   6299 C CB  . TRP B 1 369 ? 24.023  16.850  29.241  1.00 79.17  ? 398 TRP B CB  1 
ATOM   6300 C CG  . TRP B 1 369 ? 24.183  18.203  29.885  1.00 82.97  ? 398 TRP B CG  1 
ATOM   6301 C CD1 . TRP B 1 369 ? 24.138  19.425  29.278  1.00 83.02  ? 398 TRP B CD1 1 
ATOM   6302 C CD2 . TRP B 1 369 ? 24.439  18.457  31.283  1.00 83.49  ? 398 TRP B CD2 1 
ATOM   6303 N NE1 . TRP B 1 369 ? 24.335  20.421  30.198  1.00 84.37  ? 398 TRP B NE1 1 
ATOM   6304 C CE2 . TRP B 1 369 ? 24.525  19.860  31.436  1.00 84.91  ? 398 TRP B CE2 1 
ATOM   6305 C CE3 . TRP B 1 369 ? 24.597  17.641  32.412  1.00 85.06  ? 398 TRP B CE3 1 
ATOM   6306 C CZ2 . TRP B 1 369 ? 24.761  20.455  32.674  1.00 81.51  ? 398 TRP B CZ2 1 
ATOM   6307 C CZ3 . TRP B 1 369 ? 24.829  18.233  33.635  1.00 86.38  ? 398 TRP B CZ3 1 
ATOM   6308 C CH2 . TRP B 1 369 ? 24.910  19.622  33.762  1.00 82.52  ? 398 TRP B CH2 1 
ATOM   6309 N N   . PRO B 1 370 ? 24.770  13.654  29.132  1.00 53.16  ? 399 PRO B N   1 
ATOM   6310 C CA  . PRO B 1 370 ? 24.724  12.320  28.522  1.00 56.38  ? 399 PRO B CA  1 
ATOM   6311 C C   . PRO B 1 370 ? 23.493  12.178  27.633  1.00 52.55  ? 399 PRO B C   1 
ATOM   6312 O O   . PRO B 1 370 ? 22.433  12.685  27.982  1.00 53.52  ? 399 PRO B O   1 
ATOM   6313 C CB  . PRO B 1 370 ? 24.698  11.361  29.733  1.00 59.68  ? 399 PRO B CB  1 
ATOM   6314 C CG  . PRO B 1 370 ? 24.063  12.182  30.856  1.00 59.47  ? 399 PRO B CG  1 
ATOM   6315 C CD  . PRO B 1 370 ? 24.373  13.645  30.552  1.00 55.18  ? 399 PRO B CD  1 
ATOM   6316 N N   . ASN B 1 371 ? 23.649  11.520  26.475  1.00 61.97  ? 400 ASN B N   1 
ATOM   6317 C CA  . ASN B 1 371 ? 22.529  11.245  25.581  1.00 62.01  ? 400 ASN B CA  1 
ATOM   6318 C C   . ASN B 1 371 ? 21.894  9.896   25.945  1.00 68.36  ? 400 ASN B C   1 
ATOM   6319 O O   . ASN B 1 371 ? 22.298  9.243   26.918  1.00 62.57  ? 400 ASN B O   1 
ATOM   6320 C CB  . ASN B 1 371 ? 22.955  11.313  24.117  1.00 59.48  ? 400 ASN B CB  1 
ATOM   6321 C CG  . ASN B 1 371 ? 23.603  10.032  23.649  1.00 58.96  ? 400 ASN B CG  1 
ATOM   6322 O OD1 . ASN B 1 371 ? 23.722  9.081   24.425  1.00 60.50  ? 400 ASN B OD1 1 
ATOM   6323 N ND2 . ASN B 1 371 ? 24.021  9.973   22.394  1.00 60.39  ? 400 ASN B ND2 1 
ATOM   6324 N N   . VAL B 1 372 ? 20.897  9.484   25.139  1.00 63.44  ? 401 VAL B N   1 
ATOM   6325 C CA  . VAL B 1 372 ? 20.184  8.230   25.339  1.00 54.78  ? 401 VAL B CA  1 
ATOM   6326 C C   . VAL B 1 372 ? 21.183  7.073   25.477  1.00 49.55  ? 401 VAL B C   1 
ATOM   6327 O O   . VAL B 1 372 ? 21.128  6.336   26.457  1.00 45.67  ? 401 VAL B O   1 
ATOM   6328 C CB  . VAL B 1 372 ? 19.130  7.975   24.230  1.00 54.81  ? 401 VAL B CB  1 
ATOM   6329 C CG1 . VAL B 1 372 ? 19.665  8.066   22.803  1.00 49.06  ? 401 VAL B CG1 1 
ATOM   6330 C CG2 . VAL B 1 372 ? 18.415  6.641   24.413  1.00 58.49  ? 401 VAL B CG2 1 
ATOM   6331 N N   . ASP B 1 373 ? 22.118  6.976   24.524  1.00 50.65  ? 402 ASP B N   1 
ATOM   6332 C CA  . ASP B 1 373 ? 22.995  5.826   24.304  1.00 54.05  ? 402 ASP B CA  1 
ATOM   6333 C C   . ASP B 1 373 ? 23.953  5.549   25.471  1.00 50.02  ? 402 ASP B C   1 
ATOM   6334 O O   . ASP B 1 373 ? 24.522  4.464   25.564  1.00 46.03  ? 402 ASP B O   1 
ATOM   6335 C CB  . ASP B 1 373 ? 23.772  6.023   23.011  1.00 59.14  ? 402 ASP B CB  1 
ATOM   6336 C CG  . ASP B 1 373 ? 22.938  6.057   21.732  1.00 64.04  ? 402 ASP B CG  1 
ATOM   6337 O OD1 . ASP B 1 373 ? 22.202  5.075   21.482  1.00 72.06  ? 402 ASP B OD1 1 
ATOM   6338 O OD2 . ASP B 1 373 ? 23.039  7.053   20.977  1.00 62.52  ? 402 ASP B OD2 1 
ATOM   6339 N N   . ALA B 1 374 ? 24.128  6.528   26.363  1.00 45.88  ? 403 ALA B N   1 
ATOM   6340 C CA  . ALA B 1 374 ? 25.000  6.401   27.519  1.00 48.35  ? 403 ALA B CA  1 
ATOM   6341 C C   . ALA B 1 374 ? 24.477  5.363   28.511  1.00 44.55  ? 403 ALA B C   1 
ATOM   6342 O O   . ALA B 1 374 ? 25.265  4.799   29.274  1.00 41.73  ? 403 ALA B O   1 
ATOM   6343 C CB  . ALA B 1 374 ? 25.160  7.762   28.197  1.00 46.92  ? 403 ALA B CB  1 
ATOM   6344 N N   . HIS B 1 375 ? 23.156  5.151   28.538  1.00 40.33  ? 404 HIS B N   1 
ATOM   6345 C CA  . HIS B 1 375 ? 22.555  4.369   29.607  1.00 39.55  ? 404 HIS B CA  1 
ATOM   6346 C C   . HIS B 1 375 ? 22.060  3.017   29.100  1.00 34.10  ? 404 HIS B C   1 
ATOM   6347 O O   . HIS B 1 375 ? 21.852  2.109   29.890  1.00 37.00  ? 404 HIS B O   1 
ATOM   6348 C CB  . HIS B 1 375 ? 21.442  5.162   30.312  1.00 39.44  ? 404 HIS B CB  1 
ATOM   6349 C CG  . HIS B 1 375 ? 21.419  4.944   31.789  1.00 43.29  ? 404 HIS B CG  1 
ATOM   6350 N ND1 . HIS B 1 375 ? 21.372  3.691   32.362  1.00 46.17  ? 404 HIS B ND1 1 
ATOM   6351 C CD2 . HIS B 1 375 ? 21.463  5.825   32.822  1.00 47.50  ? 404 HIS B CD2 1 
ATOM   6352 C CE1 . HIS B 1 375 ? 21.386  3.821   33.691  1.00 48.99  ? 404 HIS B CE1 1 
ATOM   6353 N NE2 . HIS B 1 375 ? 21.440  5.109   33.996  1.00 41.77  ? 404 HIS B NE2 1 
ATOM   6354 N N   . SER B 1 376 ? 21.931  2.844   27.783  1.00 32.57  ? 405 SER B N   1 
ATOM   6355 C CA  . SER B 1 376 ? 21.089  1.766   27.294  1.00 31.85  ? 405 SER B CA  1 
ATOM   6356 C C   . SER B 1 376 ? 21.758  0.410   27.519  1.00 26.38  ? 405 SER B C   1 
ATOM   6357 O O   . SER B 1 376 ? 21.138  -0.462  28.118  1.00 32.05  ? 405 SER B O   1 
ATOM   6358 C CB  . SER B 1 376 ? 20.610  2.029   25.850  1.00 33.31  ? 405 SER B CB  1 
ATOM   6359 O OG  . SER B 1 376 ? 21.659  2.450   24.988  1.00 39.09  ? 405 SER B OG  1 
ATOM   6360 N N   . GLY B 1 377 ? 23.036  0.276   27.142  1.00 27.28  ? 406 GLY B N   1 
ATOM   6361 C CA  . GLY B 1 377 ? 23.794  -0.966  27.156  1.00 28.80  ? 406 GLY B CA  1 
ATOM   6362 C C   . GLY B 1 377 ? 23.942  -1.628  28.523  1.00 31.89  ? 406 GLY B C   1 
ATOM   6363 O O   . GLY B 1 377 ? 23.732  -2.828  28.649  1.00 32.35  ? 406 GLY B O   1 
ATOM   6364 N N   . VAL B 1 378 ? 24.288  -0.858  29.560  1.00 36.35  ? 407 VAL B N   1 
ATOM   6365 C CA  . VAL B 1 378 ? 24.364  -1.423  30.903  1.00 34.14  ? 407 VAL B CA  1 
ATOM   6366 C C   . VAL B 1 378 ? 23.063  -2.121  31.289  1.00 32.26  ? 407 VAL B C   1 
ATOM   6367 O O   . VAL B 1 378 ? 23.088  -3.202  31.890  1.00 32.22  ? 407 VAL B O   1 
ATOM   6368 C CB  . VAL B 1 378 ? 24.756  -0.359  31.942  1.00 40.01  ? 407 VAL B CB  1 
ATOM   6369 C CG1 . VAL B 1 378 ? 26.228  0.015   31.788  1.00 41.29  ? 407 VAL B CG1 1 
ATOM   6370 C CG2 . VAL B 1 378 ? 23.861  0.887   31.881  1.00 38.64  ? 407 VAL B CG2 1 
ATOM   6371 N N   . LEU B 1 379 ? 21.914  -1.518  30.966  1.00 30.92  ? 408 LEU B N   1 
ATOM   6372 C CA  . LEU B 1 379 ? 20.646  -2.098  31.378  1.00 29.51  ? 408 LEU B CA  1 
ATOM   6373 C C   . LEU B 1 379 ? 20.375  -3.388  30.631  1.00 31.09  ? 408 LEU B C   1 
ATOM   6374 O O   . LEU B 1 379 ? 19.922  -4.392  31.206  1.00 27.52  ? 408 LEU B O   1 
ATOM   6375 C CB  . LEU B 1 379 ? 19.595  -1.039  31.079  1.00 32.24  ? 408 LEU B CB  1 
ATOM   6376 C CG  . LEU B 1 379 ? 19.726  0.223   31.923  1.00 32.28  ? 408 LEU B CG  1 
ATOM   6377 C CD1 . LEU B 1 379 ? 18.586  1.191   31.673  1.00 32.20  ? 408 LEU B CD1 1 
ATOM   6378 C CD2 . LEU B 1 379 ? 19.777  -0.209  33.393  1.00 35.55  ? 408 LEU B CD2 1 
ATOM   6379 N N   . LEU B 1 380 ? 20.636  -3.333  29.319  1.00 28.57  ? 409 LEU B N   1 
ATOM   6380 C CA  . LEU B 1 380 ? 20.514  -4.535  28.497  1.00 27.90  ? 409 LEU B CA  1 
ATOM   6381 C C   . LEU B 1 380 ? 21.403  -5.651  29.054  1.00 26.72  ? 409 LEU B C   1 
ATOM   6382 O O   . LEU B 1 380 ? 20.970  -6.797  29.226  1.00 26.13  ? 409 LEU B O   1 
ATOM   6383 C CB  . LEU B 1 380 ? 20.804  -4.236  27.018  1.00 26.70  ? 409 LEU B CB  1 
ATOM   6384 C CG  . LEU B 1 380 ? 19.819  -3.280  26.329  1.00 27.56  ? 409 LEU B CG  1 
ATOM   6385 C CD1 . LEU B 1 380 ? 20.279  -2.969  24.911  1.00 30.49  ? 409 LEU B CD1 1 
ATOM   6386 C CD2 . LEU B 1 380 ? 18.388  -3.837  26.342  1.00 27.73  ? 409 LEU B CD2 1 
ATOM   6387 N N   . GLN B 1 381 ? 22.677  -5.340  29.270  1.00 30.92  ? 410 GLN B N   1 
ATOM   6388 C CA  . GLN B 1 381 ? 23.609  -6.351  29.758  1.00 35.74  ? 410 GLN B CA  1 
ATOM   6389 C C   . GLN B 1 381 ? 23.145  -6.925  31.106  1.00 33.84  ? 410 GLN B C   1 
ATOM   6390 O O   . GLN B 1 381 ? 23.219  -8.133  31.312  1.00 31.53  ? 410 GLN B O   1 
ATOM   6391 C CB  . GLN B 1 381 ? 25.013  -5.764  29.895  1.00 38.22  ? 410 GLN B CB  1 
ATOM   6392 C CG  . GLN B 1 381 ? 25.993  -6.684  30.610  1.00 43.61  ? 410 GLN B CG  1 
ATOM   6393 C CD  . GLN B 1 381 ? 27.354  -6.048  30.785  1.00 47.34  ? 410 GLN B CD  1 
ATOM   6394 O OE1 . GLN B 1 381 ? 27.689  -5.504  31.847  1.00 57.26  ? 410 GLN B OE1 1 
ATOM   6395 N NE2 . GLN B 1 381 ? 28.134  -6.069  29.716  1.00 46.88  ? 410 GLN B NE2 1 
ATOM   6396 N N   . TYR B 1 382 ? 22.636  -6.067  32.002  1.00 32.82  ? 411 TYR B N   1 
ATOM   6397 C CA  . TYR B 1 382 ? 22.214  -6.485  33.343  1.00 31.73  ? 411 TYR B CA  1 
ATOM   6398 C C   . TYR B 1 382 ? 21.171  -7.584  33.243  1.00 33.43  ? 411 TYR B C   1 
ATOM   6399 O O   . TYR B 1 382 ? 21.196  -8.553  34.006  1.00 31.74  ? 411 TYR B O   1 
ATOM   6400 C CB  . TYR B 1 382 ? 21.682  -5.310  34.182  1.00 35.85  ? 411 TYR B CB  1 
ATOM   6401 C CG  . TYR B 1 382 ? 21.132  -5.723  35.544  1.00 35.02  ? 411 TYR B CG  1 
ATOM   6402 C CD1 . TYR B 1 382 ? 21.981  -6.004  36.615  1.00 34.84  ? 411 TYR B CD1 1 
ATOM   6403 C CD2 . TYR B 1 382 ? 19.760  -5.856  35.758  1.00 36.78  ? 411 TYR B CD2 1 
ATOM   6404 C CE1 . TYR B 1 382 ? 21.486  -6.374  37.857  1.00 32.56  ? 411 TYR B CE1 1 
ATOM   6405 C CE2 . TYR B 1 382 ? 19.255  -6.266  36.983  1.00 34.72  ? 411 TYR B CE2 1 
ATOM   6406 C CZ  . TYR B 1 382 ? 20.120  -6.511  38.046  1.00 35.68  ? 411 TYR B CZ  1 
ATOM   6407 O OH  . TYR B 1 382 ? 19.625  -6.912  39.262  1.00 32.86  ? 411 TYR B OH  1 
ATOM   6408 N N   . TYR B 1 383 ? 20.258  -7.430  32.279  1.00 30.69  ? 412 TYR B N   1 
ATOM   6409 C CA  . TYR B 1 383 ? 19.171  -8.375  32.101  1.00 27.60  ? 412 TYR B CA  1 
ATOM   6410 C C   . TYR B 1 383 ? 19.599  -9.576  31.277  1.00 26.25  ? 412 TYR B C   1 
ATOM   6411 O O   . TYR B 1 383 ? 18.765  -10.459 31.058  1.00 29.73  ? 412 TYR B O   1 
ATOM   6412 C CB  . TYR B 1 383 ? 17.948  -7.658  31.517  1.00 26.48  ? 412 TYR B CB  1 
ATOM   6413 C CG  . TYR B 1 383 ? 17.293  -6.845  32.615  1.00 27.61  ? 412 TYR B CG  1 
ATOM   6414 C CD1 . TYR B 1 383 ? 16.608  -7.480  33.647  1.00 34.60  ? 412 TYR B CD1 1 
ATOM   6415 C CD2 . TYR B 1 383 ? 17.455  -5.478  32.696  1.00 28.25  ? 412 TYR B CD2 1 
ATOM   6416 C CE1 . TYR B 1 383 ? 16.063  -6.768  34.691  1.00 30.98  ? 412 TYR B CE1 1 
ATOM   6417 C CE2 . TYR B 1 383 ? 16.891  -4.751  33.727  1.00 32.94  ? 412 TYR B CE2 1 
ATOM   6418 C CZ  . TYR B 1 383 ? 16.196  -5.399  34.721  1.00 29.53  ? 412 TYR B CZ  1 
ATOM   6419 O OH  . TYR B 1 383 ? 15.657  -4.663  35.721  1.00 33.30  ? 412 TYR B OH  1 
ATOM   6420 N N   . GLY B 1 384 ? 20.874  -9.646  30.868  1.00 27.08  ? 413 GLY B N   1 
ATOM   6421 C CA  . GLY B 1 384 ? 21.398  -10.864 30.243  1.00 29.35  ? 413 GLY B CA  1 
ATOM   6422 C C   . GLY B 1 384 ? 21.447  -10.800 28.702  1.00 34.37  ? 413 GLY B C   1 
ATOM   6423 O O   . GLY B 1 384 ? 21.820  -11.765 28.048  1.00 34.41  ? 413 GLY B O   1 
ATOM   6424 N N   . MET B 1 385 ? 21.042  -9.656  28.145  1.00 33.36  ? 414 MET B N   1 
ATOM   6425 C CA  . MET B 1 385 ? 21.127  -9.299  26.736  1.00 31.36  ? 414 MET B CA  1 
ATOM   6426 C C   . MET B 1 385 ? 22.521  -8.722  26.456  1.00 27.59  ? 414 MET B C   1 
ATOM   6427 O O   . MET B 1 385 ? 22.727  -7.508  26.448  1.00 26.08  ? 414 MET B O   1 
ATOM   6428 C CB  . MET B 1 385 ? 19.948  -8.346  26.495  1.00 32.64  ? 414 MET B CB  1 
ATOM   6429 C CG  . MET B 1 385 ? 19.991  -7.417  25.314  1.00 41.45  ? 414 MET B CG  1 
ATOM   6430 S SD  . MET B 1 385 ? 19.243  -8.010  23.792  1.00 37.63  ? 414 MET B SD  1 
ATOM   6431 C CE  . MET B 1 385 ? 17.720  -8.959  23.927  1.00 33.68  ? 414 MET B CE  1 
ATOM   6432 N N   . THR B 1 386 ? 23.494  -9.620  26.245  1.00 28.48  ? 415 THR B N   1 
ATOM   6433 C CA  . THR B 1 386 ? 24.908  -9.246  26.170  1.00 29.17  ? 415 THR B CA  1 
ATOM   6434 C C   . THR B 1 386 ? 25.418  -9.142  24.724  1.00 28.23  ? 415 THR B C   1 
ATOM   6435 O O   . THR B 1 386 ? 26.528  -8.661  24.485  1.00 30.78  ? 415 THR B O   1 
ATOM   6436 C CB  . THR B 1 386 ? 25.761  -10.218 26.992  1.00 32.10  ? 415 THR B CB  1 
ATOM   6437 O OG1 . THR B 1 386 ? 25.614  -11.514 26.442  1.00 31.22  ? 415 THR B OG1 1 
ATOM   6438 C CG2 . THR B 1 386 ? 25.352  -10.327 28.449  1.00 32.95  ? 415 THR B CG2 1 
ATOM   6439 N N   . GLU B 1 387 ? 24.619  -9.521  23.720  1.00 30.85  ? 416 GLU B N   1 
ATOM   6440 C CA  . GLU B 1 387 ? 25.134  -9.612  22.347  1.00 28.57  ? 416 GLU B CA  1 
ATOM   6441 C C   . GLU B 1 387 ? 25.025  -8.244  21.674  1.00 27.54  ? 416 GLU B C   1 
ATOM   6442 O O   . GLU B 1 387 ? 23.997  -7.867  21.091  1.00 29.10  ? 416 GLU B O   1 
ATOM   6443 C CB  . GLU B 1 387 ? 24.410  -10.740 21.624  1.00 30.46  ? 416 GLU B CB  1 
ATOM   6444 C CG  . GLU B 1 387 ? 24.435  -12.045 22.409  1.00 32.36  ? 416 GLU B CG  1 
ATOM   6445 C CD  . GLU B 1 387 ? 23.297  -12.223 23.392  1.00 31.24  ? 416 GLU B CD  1 
ATOM   6446 O OE1 . GLU B 1 387 ? 23.210  -13.401 23.748  1.00 32.21  ? 416 GLU B OE1 1 
ATOM   6447 O OE2 . GLU B 1 387 ? 22.492  -11.316 23.760  1.00 26.64  ? 416 GLU B OE2 1 
ATOM   6448 N N   . MET B 1 388 ? 26.077  -7.450  21.836  1.00 28.54  ? 417 MET B N   1 
ATOM   6449 C CA  . MET B 1 388 ? 26.005  -6.031  21.511  1.00 28.90  ? 417 MET B CA  1 
ATOM   6450 C C   . MET B 1 388 ? 25.700  -5.801  20.024  1.00 27.40  ? 417 MET B C   1 
ATOM   6451 O O   . MET B 1 388 ? 25.121  -4.790  19.646  1.00 23.68  ? 417 MET B O   1 
ATOM   6452 C CB  . MET B 1 388 ? 27.333  -5.334  21.816  1.00 32.36  ? 417 MET B CB  1 
ATOM   6453 C CG  . MET B 1 388 ? 27.691  -5.320  23.266  1.00 36.25  ? 417 MET B CG  1 
ATOM   6454 S SD  . MET B 1 388 ? 29.235  -4.407  23.473  1.00 47.44  ? 417 MET B SD  1 
ATOM   6455 C CE  . MET B 1 388 ? 30.105  -5.624  24.476  1.00 49.76  ? 417 MET B CE  1 
ATOM   6456 N N   . ASN B 1 389 ? 26.109  -6.738  19.182  1.00 29.03  ? 418 ASN B N   1 
ATOM   6457 C CA  . ASN B 1 389 ? 25.854  -6.633  17.765  1.00 32.82  ? 418 ASN B CA  1 
ATOM   6458 C C   . ASN B 1 389 ? 24.362  -6.514  17.526  1.00 31.66  ? 418 ASN B C   1 
ATOM   6459 O O   . ASN B 1 389 ? 23.978  -6.035  16.483  1.00 34.30  ? 418 ASN B O   1 
ATOM   6460 C CB  . ASN B 1 389 ? 26.420  -7.810  16.979  1.00 37.00  ? 418 ASN B CB  1 
ATOM   6461 C CG  . ASN B 1 389 ? 27.887  -7.627  16.682  1.00 39.77  ? 418 ASN B CG  1 
ATOM   6462 O OD1 . ASN B 1 389 ? 28.447  -6.550  16.936  1.00 39.80  ? 418 ASN B OD1 1 
ATOM   6463 N ND2 . ASN B 1 389 ? 28.507  -8.650  16.117  1.00 40.81  ? 418 ASN B ND2 1 
ATOM   6464 N N   . TYR B 1 390 ? 23.550  -6.941  18.497  1.00 28.57  ? 419 TYR B N   1 
ATOM   6465 C CA  . TYR B 1 390 ? 22.109  -7.032  18.335  1.00 25.25  ? 419 TYR B CA  1 
ATOM   6466 C C   . TYR B 1 390 ? 21.380  -5.761  18.781  1.00 23.59  ? 419 TYR B C   1 
ATOM   6467 O O   . TYR B 1 390 ? 20.206  -5.608  18.485  1.00 24.52  ? 419 TYR B O   1 
ATOM   6468 C CB  . TYR B 1 390 ? 21.587  -8.209  19.154  1.00 23.60  ? 419 TYR B CB  1 
ATOM   6469 C CG  . TYR B 1 390 ? 20.105  -8.464  18.935  1.00 21.10  ? 419 TYR B CG  1 
ATOM   6470 C CD1 . TYR B 1 390 ? 19.670  -9.165  17.842  1.00 18.82  ? 419 TYR B CD1 1 
ATOM   6471 C CD2 . TYR B 1 390 ? 19.153  -8.068  19.857  1.00 20.00  ? 419 TYR B CD2 1 
ATOM   6472 C CE1 . TYR B 1 390 ? 18.328  -9.381  17.613  1.00 20.85  ? 419 TYR B CE1 1 
ATOM   6473 C CE2 . TYR B 1 390 ? 17.809  -8.339  19.673  1.00 19.73  ? 419 TYR B CE2 1 
ATOM   6474 C CZ  . TYR B 1 390 ? 17.384  -8.983  18.534  1.00 19.41  ? 419 TYR B CZ  1 
ATOM   6475 O OH  . TYR B 1 390 ? 16.062  -9.304  18.293  1.00 18.54  ? 419 TYR B OH  1 
ATOM   6476 N N   . TYR B 1 391 ? 22.058  -4.855  19.500  1.00 20.88  ? 420 TYR B N   1 
ATOM   6477 C CA  . TYR B 1 391 ? 21.407  -3.736  20.164  1.00 20.96  ? 420 TYR B CA  1 
ATOM   6478 C C   . TYR B 1 391 ? 20.724  -2.819  19.162  1.00 22.45  ? 420 TYR B C   1 
ATOM   6479 O O   . TYR B 1 391 ? 19.624  -2.334  19.398  1.00 20.36  ? 420 TYR B O   1 
ATOM   6480 C CB  . TYR B 1 391 ? 22.410  -2.939  21.021  1.00 22.40  ? 420 TYR B CB  1 
ATOM   6481 C CG  . TYR B 1 391 ? 22.890  -3.606  22.313  1.00 24.15  ? 420 TYR B CG  1 
ATOM   6482 C CD1 . TYR B 1 391 ? 22.415  -4.847  22.724  1.00 22.53  ? 420 TYR B CD1 1 
ATOM   6483 C CD2 . TYR B 1 391 ? 23.859  -2.994  23.113  1.00 23.16  ? 420 TYR B CD2 1 
ATOM   6484 C CE1 . TYR B 1 391 ? 22.895  -5.462  23.867  1.00 25.39  ? 420 TYR B CE1 1 
ATOM   6485 C CE2 . TYR B 1 391 ? 24.353  -3.603  24.253  1.00 25.34  ? 420 TYR B CE2 1 
ATOM   6486 C CZ  . TYR B 1 391 ? 23.882  -4.852  24.614  1.00 27.28  ? 420 TYR B CZ  1 
ATOM   6487 O OH  . TYR B 1 391 ? 24.270  -5.449  25.769  1.00 23.75  ? 420 TYR B OH  1 
ATOM   6488 N N   . THR B 1 392 ? 21.331  -2.613  17.991  1.00 20.75  ? 421 THR B N   1 
ATOM   6489 C CA  . THR B 1 392 ? 20.700  -1.720  17.037  1.00 22.83  ? 421 THR B CA  1 
ATOM   6490 C C   . THR B 1 392 ? 19.400  -2.293  16.448  1.00 19.87  ? 421 THR B C   1 
ATOM   6491 O O   . THR B 1 392 ? 18.505  -1.519  16.115  1.00 19.88  ? 421 THR B O   1 
ATOM   6492 C CB  . THR B 1 392 ? 21.703  -1.337  15.958  1.00 25.55  ? 421 THR B CB  1 
ATOM   6493 O OG1 . THR B 1 392 ? 22.871  -0.857  16.624  1.00 29.46  ? 421 THR B OG1 1 
ATOM   6494 C CG2 . THR B 1 392 ? 21.124  -0.197  15.140  1.00 31.10  ? 421 THR B CG2 1 
ATOM   6495 N N   . VAL B 1 393 ? 19.202  -3.622  16.491  1.00 21.27  ? 422 VAL B N   1 
ATOM   6496 C CA  . VAL B 1 393 ? 17.929  -4.236  16.118  1.00 21.36  ? 422 VAL B CA  1 
ATOM   6497 C C   . VAL B 1 393 ? 16.799  -3.745  17.033  1.00 20.16  ? 422 VAL B C   1 
ATOM   6498 O O   . VAL B 1 393 ? 15.691  -3.427  16.581  1.00 19.78  ? 422 VAL B O   1 
ATOM   6499 C CB  . VAL B 1 393 ? 18.042  -5.775  16.158  1.00 23.73  ? 422 VAL B CB  1 
ATOM   6500 C CG1 . VAL B 1 393 ? 16.697  -6.493  16.062  1.00 23.37  ? 422 VAL B CG1 1 
ATOM   6501 C CG2 . VAL B 1 393 ? 18.960  -6.258  15.056  1.00 24.37  ? 422 VAL B CG2 1 
ATOM   6502 N N   . LEU B 1 394 ? 17.101  -3.673  18.324  1.00 20.69  ? 423 LEU B N   1 
ATOM   6503 C CA  . LEU B 1 394 ? 16.134  -3.181  19.283  1.00 24.60  ? 423 LEU B CA  1 
ATOM   6504 C C   . LEU B 1 394 ? 15.768  -1.730  18.937  1.00 23.41  ? 423 LEU B C   1 
ATOM   6505 O O   . LEU B 1 394 ? 14.617  -1.336  18.999  1.00 26.43  ? 423 LEU B O   1 
ATOM   6506 C CB  . LEU B 1 394 ? 16.696  -3.290  20.702  1.00 26.93  ? 423 LEU B CB  1 
ATOM   6507 C CG  . LEU B 1 394 ? 16.856  -4.704  21.279  1.00 28.59  ? 423 LEU B CG  1 
ATOM   6508 C CD1 . LEU B 1 394 ? 17.467  -4.666  22.659  1.00 27.54  ? 423 LEU B CD1 1 
ATOM   6509 C CD2 . LEU B 1 394 ? 15.553  -5.442  21.345  1.00 25.58  ? 423 LEU B CD2 1 
ATOM   6510 N N   . PHE B 1 395 ? 16.765  -0.922  18.634  1.00 22.03  ? 424 PHE B N   1 
ATOM   6511 C CA  . PHE B 1 395 ? 16.544  0.460   18.227  1.00 22.30  ? 424 PHE B CA  1 
ATOM   6512 C C   . PHE B 1 395 ? 15.645  0.485   17.002  1.00 22.35  ? 424 PHE B C   1 
ATOM   6513 O O   . PHE B 1 395 ? 14.750  1.313   16.936  1.00 25.23  ? 424 PHE B O   1 
ATOM   6514 C CB  . PHE B 1 395 ? 17.891  1.137   17.966  1.00 25.27  ? 424 PHE B CB  1 
ATOM   6515 C CG  . PHE B 1 395 ? 17.988  2.650   17.786  1.00 24.24  ? 424 PHE B CG  1 
ATOM   6516 C CD1 . PHE B 1 395 ? 16.879  3.446   17.525  1.00 27.64  ? 424 PHE B CD1 1 
ATOM   6517 C CD2 . PHE B 1 395 ? 19.226  3.278   17.891  1.00 31.88  ? 424 PHE B CD2 1 
ATOM   6518 C CE1 . PHE B 1 395 ? 17.006  4.831   17.376  1.00 29.04  ? 424 PHE B CE1 1 
ATOM   6519 C CE2 . PHE B 1 395 ? 19.360  4.668   17.731  1.00 31.76  ? 424 PHE B CE2 1 
ATOM   6520 C CZ  . PHE B 1 395 ? 18.238  5.437   17.482  1.00 30.87  ? 424 PHE B CZ  1 
ATOM   6521 N N   . GLY B 1 396 ? 15.888  -0.405  16.027  1.00 20.50  ? 425 GLY B N   1 
ATOM   6522 C CA  . GLY B 1 396 ? 15.104  -0.466  14.801  1.00 21.23  ? 425 GLY B CA  1 
ATOM   6523 C C   . GLY B 1 396 ? 13.619  -0.769  15.057  1.00 21.88  ? 425 GLY B C   1 
ATOM   6524 O O   . GLY B 1 396 ? 12.730  -0.095  14.528  1.00 20.29  ? 425 GLY B O   1 
ATOM   6525 N N   . VAL B 1 397 ? 13.367  -1.810  15.853  1.00 20.52  ? 426 VAL B N   1 
ATOM   6526 C CA  . VAL B 1 397 ? 12.032  -2.232  16.202  1.00 19.88  ? 426 VAL B CA  1 
ATOM   6527 C C   . VAL B 1 397 ? 11.280  -1.038  16.809  1.00 19.70  ? 426 VAL B C   1 
ATOM   6528 O O   . VAL B 1 397 ? 10.131  -0.777  16.496  1.00 22.01  ? 426 VAL B O   1 
ATOM   6529 C CB  . VAL B 1 397 ? 12.068  -3.440  17.144  1.00 20.38  ? 426 VAL B CB  1 
ATOM   6530 C CG1 . VAL B 1 397 ? 10.678  -3.710  17.714  1.00 21.55  ? 426 VAL B CG1 1 
ATOM   6531 C CG2 . VAL B 1 397 ? 12.589  -4.705  16.479  1.00 21.22  ? 426 VAL B CG2 1 
ATOM   6532 N N   . SER B 1 398 ? 11.953  -0.261  17.644  1.00 18.38  ? 427 SER B N   1 
ATOM   6533 C CA  . SER B 1 398 ? 11.362  0.905   18.259  1.00 20.34  ? 427 SER B CA  1 
ATOM   6534 C C   . SER B 1 398 ? 11.047  1.975   17.223  1.00 20.28  ? 427 SER B C   1 
ATOM   6535 O O   . SER B 1 398 ? 9.966   2.581   17.228  1.00 17.83  ? 427 SER B O   1 
ATOM   6536 C CB  . SER B 1 398 ? 12.283  1.485   19.268  1.00 21.64  ? 427 SER B CB  1 
ATOM   6537 O OG  . SER B 1 398 ? 11.650  2.641   19.781  1.00 23.06  ? 427 SER B OG  1 
ATOM   6538 N N   . ARG B 1 399 ? 12.046  2.243   16.368  1.00 20.44  ? 428 ARG B N   1 
ATOM   6539 C CA  . ARG B 1 399 ? 11.951  3.352   15.438  1.00 20.40  ? 428 ARG B CA  1 
ATOM   6540 C C   . ARG B 1 399 ? 10.838  3.118   14.422  1.00 19.71  ? 428 ARG B C   1 
ATOM   6541 O O   . ARG B 1 399 ? 10.265  4.057   13.843  1.00 19.44  ? 428 ARG B O   1 
ATOM   6542 C CB  . ARG B 1 399 ? 13.344  3.595   14.853  1.00 19.75  ? 428 ARG B CB  1 
ATOM   6543 C CG  . ARG B 1 399 ? 13.433  4.823   13.962  1.00 20.85  ? 428 ARG B CG  1 
ATOM   6544 C CD  . ARG B 1 399 ? 12.904  6.076   14.572  1.00 18.63  ? 428 ARG B CD  1 
ATOM   6545 N NE  . ARG B 1 399 ? 13.495  6.447   15.858  1.00 20.81  ? 428 ARG B NE  1 
ATOM   6546 C CZ  . ARG B 1 399 ? 14.560  7.256   16.027  1.00 21.98  ? 428 ARG B CZ  1 
ATOM   6547 N NH1 . ARG B 1 399 ? 15.282  7.712   15.012  1.00 20.97  ? 428 ARG B NH1 1 
ATOM   6548 N NH2 . ARG B 1 399 ? 14.926  7.578   17.231  1.00 24.00  ? 428 ARG B NH2 1 
ATOM   6549 N N   . ALA B 1 400 ? 10.515  1.856   14.206  1.00 20.34  ? 429 ALA B N   1 
ATOM   6550 C CA  . ALA B 1 400 ? 9.370   1.522   13.380  1.00 20.18  ? 429 ALA B CA  1 
ATOM   6551 C C   . ALA B 1 400 ? 8.133   2.333   13.775  1.00 17.95  ? 429 ALA B C   1 
ATOM   6552 O O   . ALA B 1 400 ? 7.366   2.740   12.897  1.00 17.84  ? 429 ALA B O   1 
ATOM   6553 C CB  . ALA B 1 400 ? 9.085   0.054   13.463  1.00 18.18  ? 429 ALA B CB  1 
ATOM   6554 N N   . LEU B 1 401 ? 7.927   2.539   15.077  1.00 18.83  ? 430 LEU B N   1 
ATOM   6555 C CA  . LEU B 1 401 ? 6.702   3.160   15.535  1.00 21.72  ? 430 LEU B CA  1 
ATOM   6556 C C   . LEU B 1 401 ? 6.622   4.581   15.007  1.00 20.89  ? 430 LEU B C   1 
ATOM   6557 O O   . LEU B 1 401 ? 5.567   4.998   14.502  1.00 23.91  ? 430 LEU B O   1 
ATOM   6558 C CB  . LEU B 1 401 ? 6.593   3.113   17.064  1.00 23.29  ? 430 LEU B CB  1 
ATOM   6559 C CG  . LEU B 1 401 ? 6.657   1.697   17.641  1.00 24.93  ? 430 LEU B CG  1 
ATOM   6560 C CD1 . LEU B 1 401 ? 6.469   1.720   19.144  1.00 29.02  ? 430 LEU B CD1 1 
ATOM   6561 C CD2 . LEU B 1 401 ? 5.665   0.735   17.020  1.00 26.28  ? 430 LEU B CD2 1 
ATOM   6562 N N   . GLY B 1 402 ? 7.761   5.284   15.100  1.00 19.70  ? 431 GLY B N   1 
ATOM   6563 C CA  . GLY B 1 402 ? 7.834   6.672   14.692  1.00 17.47  ? 431 GLY B CA  1 
ATOM   6564 C C   . GLY B 1 402 ? 7.700   6.836   13.187  1.00 18.11  ? 431 GLY B C   1 
ATOM   6565 O O   . GLY B 1 402 ? 6.895   7.630   12.729  1.00 20.41  ? 431 GLY B O   1 
ATOM   6566 N N   . VAL B 1 403 ? 8.532   6.124   12.418  1.00 15.81  ? 432 VAL B N   1 
ATOM   6567 C CA  . VAL B 1 403 ? 8.628   6.397   11.007  1.00 18.08  ? 432 VAL B CA  1 
ATOM   6568 C C   . VAL B 1 403 ? 7.371   5.913   10.280  1.00 19.45  ? 432 VAL B C   1 
ATOM   6569 O O   . VAL B 1 403 ? 7.019   6.520   9.277   1.00 18.88  ? 432 VAL B O   1 
ATOM   6570 C CB  . VAL B 1 403 ? 9.917   5.862   10.358  1.00 18.51  ? 432 VAL B CB  1 
ATOM   6571 C CG1 . VAL B 1 403 ? 11.138  6.440   11.043  1.00 21.12  ? 432 VAL B CG1 1 
ATOM   6572 C CG2 . VAL B 1 403 ? 9.949   4.339   10.296  1.00 16.76  ? 432 VAL B CG2 1 
ATOM   6573 N N   . LEU B 1 404 ? 6.720   4.847   10.777  1.00 19.60  ? 433 LEU B N   1 
ATOM   6574 C CA  . LEU B 1 404 ? 5.481   4.353   10.187  1.00 18.88  ? 433 LEU B CA  1 
ATOM   6575 C C   . LEU B 1 404 ? 4.296   5.257   10.541  1.00 20.94  ? 433 LEU B C   1 
ATOM   6576 O O   . LEU B 1 404 ? 3.431   5.481   9.710   1.00 20.88  ? 433 LEU B O   1 
ATOM   6577 C CB  . LEU B 1 404 ? 5.237   2.884   10.522  1.00 18.52  ? 433 LEU B CB  1 
ATOM   6578 C CG  . LEU B 1 404 ? 6.348   1.952   10.016  1.00 18.51  ? 433 LEU B CG  1 
ATOM   6579 C CD1 . LEU B 1 404 ? 6.112   0.522   10.400  1.00 18.45  ? 433 LEU B CD1 1 
ATOM   6580 C CD2 . LEU B 1 404 ? 6.569   2.111   8.508   1.00 19.72  ? 433 LEU B CD2 1 
ATOM   6581 N N   . ALA B 1 405 ? 4.240   5.771   11.769  1.00 20.83  ? 434 ALA B N   1 
ATOM   6582 C CA  . ALA B 1 405 ? 3.205   6.720   12.095  1.00 19.49  ? 434 ALA B CA  1 
ATOM   6583 C C   . ALA B 1 405 ? 3.327   7.903   11.142  1.00 22.35  ? 434 ALA B C   1 
ATOM   6584 O O   . ALA B 1 405 ? 2.310   8.290   10.564  1.00 21.03  ? 434 ALA B O   1 
ATOM   6585 C CB  . ALA B 1 405 ? 3.281   7.112   13.549  1.00 19.73  ? 434 ALA B CB  1 
ATOM   6586 N N   . GLN B 1 406 ? 4.564   8.384   10.876  1.00 19.08  ? 435 GLN B N   1 
ATOM   6587 C CA  . GLN B 1 406 ? 4.697   9.506   9.963   1.00 22.21  ? 435 GLN B CA  1 
ATOM   6588 C C   . GLN B 1 406 ? 4.380   9.073   8.523   1.00 20.29  ? 435 GLN B C   1 
ATOM   6589 O O   . GLN B 1 406 ? 3.771   9.831   7.775   1.00 18.79  ? 435 GLN B O   1 
ATOM   6590 C CB  . GLN B 1 406 ? 6.066   10.186  10.016  1.00 25.37  ? 435 GLN B CB  1 
ATOM   6591 C CG  . GLN B 1 406 ? 6.255   11.265  8.954   1.00 27.20  ? 435 GLN B CG  1 
ATOM   6592 C CD  . GLN B 1 406 ? 5.286   12.433  9.056   1.00 27.59  ? 435 GLN B CD  1 
ATOM   6593 O OE1 . GLN B 1 406 ? 4.912   12.875  10.141  1.00 25.92  ? 435 GLN B OE1 1 
ATOM   6594 N NE2 . GLN B 1 406 ? 4.899   12.972  7.916   1.00 23.05  ? 435 GLN B NE2 1 
ATOM   6595 N N   . LEU B 1 407 ? 4.759   7.856   8.116   1.00 18.17  ? 436 LEU B N   1 
ATOM   6596 C CA  . LEU B 1 407 ? 4.518   7.438   6.740   1.00 19.83  ? 436 LEU B CA  1 
ATOM   6597 C C   . LEU B 1 407 ? 3.027   7.481   6.365   1.00 20.96  ? 436 LEU B C   1 
ATOM   6598 O O   . LEU B 1 407 ? 2.654   7.876   5.249   1.00 19.33  ? 436 LEU B O   1 
ATOM   6599 C CB  . LEU B 1 407 ? 5.093   6.036   6.576   1.00 21.65  ? 436 LEU B CB  1 
ATOM   6600 C CG  . LEU B 1 407 ? 5.125   5.485   5.157   1.00 21.65  ? 436 LEU B CG  1 
ATOM   6601 C CD1 . LEU B 1 407 ? 6.040   6.368   4.328   1.00 23.78  ? 436 LEU B CD1 1 
ATOM   6602 C CD2 . LEU B 1 407 ? 5.614   4.058   5.115   1.00 23.54  ? 436 LEU B CD2 1 
ATOM   6603 N N   . ILE B 1 408 ? 2.179   7.051   7.300   1.00 20.73  ? 437 ILE B N   1 
ATOM   6604 C CA  . ILE B 1 408 ? 0.736   7.084   7.143   1.00 22.39  ? 437 ILE B CA  1 
ATOM   6605 C C   . ILE B 1 408 ? 0.311   8.520   6.866   1.00 21.73  ? 437 ILE B C   1 
ATOM   6606 O O   . ILE B 1 408 ? -0.412  8.796   5.907   1.00 21.24  ? 437 ILE B O   1 
ATOM   6607 C CB  . ILE B 1 408 ? 0.014   6.469   8.358   1.00 24.37  ? 437 ILE B CB  1 
ATOM   6608 C CG1 . ILE B 1 408 ? 0.356   5.015   8.587   1.00 23.10  ? 437 ILE B CG1 1 
ATOM   6609 C CG2 . ILE B 1 408 ? -1.505  6.646   8.224   1.00 26.18  ? 437 ILE B CG2 1 
ATOM   6610 C CD1 . ILE B 1 408 ? 0.099   4.523   10.013  1.00 20.24  ? 437 ILE B CD1 1 
ATOM   6611 N N   . TRP B 1 409 ? 0.821   9.442   7.676   1.00 23.70  ? 438 TRP B N   1 
ATOM   6612 C CA  . TRP B 1 409 ? 0.450   10.835  7.546   1.00 25.11  ? 438 TRP B CA  1 
ATOM   6613 C C   . TRP B 1 409 ? 1.011   11.444  6.263   1.00 21.98  ? 438 TRP B C   1 
ATOM   6614 O O   . TRP B 1 409 ? 0.366   12.274  5.667   1.00 24.42  ? 438 TRP B O   1 
ATOM   6615 C CB  . TRP B 1 409 ? 0.861   11.621  8.804   1.00 25.89  ? 438 TRP B CB  1 
ATOM   6616 C CG  . TRP B 1 409 ? -0.196  11.485  9.869   1.00 26.36  ? 438 TRP B CG  1 
ATOM   6617 C CD1 . TRP B 1 409 ? -0.238  10.636  10.950  1.00 24.31  ? 438 TRP B CD1 1 
ATOM   6618 C CD2 . TRP B 1 409 ? -1.452  12.190  9.860   1.00 27.11  ? 438 TRP B CD2 1 
ATOM   6619 N NE1 . TRP B 1 409 ? -1.423  10.794  11.632  1.00 24.13  ? 438 TRP B NE1 1 
ATOM   6620 C CE2 . TRP B 1 409 ? -2.190  11.733  10.979  1.00 26.00  ? 438 TRP B CE2 1 
ATOM   6621 C CE3 . TRP B 1 409 ? -2.027  13.136  9.008   1.00 30.49  ? 438 TRP B CE3 1 
ATOM   6622 C CZ2 . TRP B 1 409 ? -3.456  12.237  11.277  1.00 25.29  ? 438 TRP B CZ2 1 
ATOM   6623 C CZ3 . TRP B 1 409 ? -3.281  13.632  9.311   1.00 27.39  ? 438 TRP B CZ3 1 
ATOM   6624 C CH2 . TRP B 1 409 ? -3.974  13.189  10.435  1.00 26.03  ? 438 TRP B CH2 1 
ATOM   6625 N N   . SER B 1 410 ? 2.226   11.080  5.841   1.00 20.18  ? 439 SER B N   1 
ATOM   6626 C CA  . SER B 1 410 ? 2.798   11.642  4.618   1.00 21.04  ? 439 SER B CA  1 
ATOM   6627 C C   . SER B 1 410 ? 1.883   11.328  3.433   1.00 20.05  ? 439 SER B C   1 
ATOM   6628 O O   . SER B 1 410 ? 1.538   12.205  2.636   1.00 25.11  ? 439 SER B O   1 
ATOM   6629 C CB  . SER B 1 410 ? 4.258   11.165  4.381   1.00 19.70  ? 439 SER B CB  1 
ATOM   6630 O OG  . SER B 1 410 ? 5.106   11.612  5.423   1.00 18.68  ? 439 SER B OG  1 
ATOM   6631 N N   . ARG B 1 411 ? 1.351   10.111  3.392   1.00 21.35  ? 440 ARG B N   1 
ATOM   6632 C CA  . ARG B 1 411 ? 0.487   9.705   2.291   1.00 20.21  ? 440 ARG B CA  1 
ATOM   6633 C C   . ARG B 1 411 ? -0.904  10.306  2.461   1.00 21.44  ? 440 ARG B C   1 
ATOM   6634 O O   . ARG B 1 411 ? -1.471  10.811  1.514   1.00 21.00  ? 440 ARG B O   1 
ATOM   6635 C CB  . ARG B 1 411 ? 0.470   8.189   2.215   1.00 20.62  ? 440 ARG B CB  1 
ATOM   6636 C CG  . ARG B 1 411 ? 1.855   7.590   2.027   1.00 22.85  ? 440 ARG B CG  1 
ATOM   6637 C CD  . ARG B 1 411 ? 2.438   7.697   0.587   1.00 24.05  ? 440 ARG B CD  1 
ATOM   6638 N NE  . ARG B 1 411 ? 3.042   8.997   0.277   1.00 22.36  ? 440 ARG B NE  1 
ATOM   6639 C CZ  . ARG B 1 411 ? 4.120   9.463   0.853   1.00 22.09  ? 440 ARG B CZ  1 
ATOM   6640 N NH1 . ARG B 1 411 ? 4.805   8.686   1.640   1.00 22.36  ? 440 ARG B NH1 1 
ATOM   6641 N NH2 . ARG B 1 411 ? 4.548   10.682  0.608   1.00 19.73  ? 440 ARG B NH2 1 
ATOM   6642 N N   . ALA B 1 412 ? -1.418  10.334  3.691   1.00 22.30  ? 441 ALA B N   1 
ATOM   6643 C CA  . ALA B 1 412 ? -2.698  10.957  3.959   1.00 22.52  ? 441 ALA B CA  1 
ATOM   6644 C C   . ALA B 1 412 ? -2.693  12.400  3.464   1.00 23.62  ? 441 ALA B C   1 
ATOM   6645 O O   . ALA B 1 412 ? -3.712  12.862  2.972   1.00 24.47  ? 441 ALA B O   1 
ATOM   6646 C CB  . ALA B 1 412 ? -3.019  10.926  5.445   1.00 24.25  ? 441 ALA B CB  1 
ATOM   6647 N N   . LEU B 1 413 ? -1.573  13.101  3.687   1.00 23.00  ? 442 LEU B N   1 
ATOM   6648 C CA  . LEU B 1 413 ? -1.422  14.505  3.388   1.00 22.86  ? 442 LEU B CA  1 
ATOM   6649 C C   . LEU B 1 413 ? -0.891  14.747  1.994   1.00 24.38  ? 442 LEU B C   1 
ATOM   6650 O O   . LEU B 1 413 ? -0.791  15.907  1.608   1.00 26.41  ? 442 LEU B O   1 
ATOM   6651 C CB  . LEU B 1 413 ? -0.506  15.181  4.392   1.00 23.57  ? 442 LEU B CB  1 
ATOM   6652 C CG  . LEU B 1 413 ? -1.014  15.206  5.837   1.00 24.21  ? 442 LEU B CG  1 
ATOM   6653 C CD1 . LEU B 1 413 ? -0.005  15.811  6.774   1.00 23.01  ? 442 LEU B CD1 1 
ATOM   6654 C CD2 . LEU B 1 413 ? -2.340  15.968  5.905   1.00 22.59  ? 442 LEU B CD2 1 
ATOM   6655 N N   . GLY B 1 414 ? -0.636  13.688  1.224   1.00 24.76  ? 443 GLY B N   1 
ATOM   6656 C CA  . GLY B 1 414 ? -0.305  13.832  -0.192  1.00 21.71  ? 443 GLY B CA  1 
ATOM   6657 C C   . GLY B 1 414 ? 1.092   14.429  -0.401  1.00 23.01  ? 443 GLY B C   1 
ATOM   6658 O O   . GLY B 1 414 ? 1.349   14.959  -1.473  1.00 22.97  ? 443 GLY B O   1 
ATOM   6659 N N   . PHE B 1 415 ? 2.012   14.278  0.575   1.00 21.22  ? 444 PHE B N   1 
ATOM   6660 C CA  . PHE B 1 415 ? 3.406   14.684  0.397   1.00 21.89  ? 444 PHE B CA  1 
ATOM   6661 C C   . PHE B 1 415 ? 3.971   14.121  -0.903  1.00 21.38  ? 444 PHE B C   1 
ATOM   6662 O O   . PHE B 1 415 ? 3.839   12.922  -1.143  1.00 22.83  ? 444 PHE B O   1 
ATOM   6663 C CB  . PHE B 1 415 ? 4.332   14.297  1.559   1.00 20.25  ? 444 PHE B CB  1 
ATOM   6664 C CG  . PHE B 1 415 ? 4.049   15.042  2.862   1.00 23.36  ? 444 PHE B CG  1 
ATOM   6665 C CD1 . PHE B 1 415 ? 3.037   15.998  2.934   1.00 20.87  ? 444 PHE B CD1 1 
ATOM   6666 C CD2 . PHE B 1 415 ? 4.841   14.845  3.992   1.00 19.97  ? 444 PHE B CD2 1 
ATOM   6667 C CE1 . PHE B 1 415 ? 2.844   16.729  4.082   1.00 20.32  ? 444 PHE B CE1 1 
ATOM   6668 C CE2 . PHE B 1 415 ? 4.613   15.554  5.144   1.00 19.86  ? 444 PHE B CE2 1 
ATOM   6669 C CZ  . PHE B 1 415 ? 3.585   16.464  5.197   1.00 20.80  ? 444 PHE B CZ  1 
ATOM   6670 N N   . PRO B 1 416 ? 4.635   14.949  -1.750  1.00 19.55  ? 445 PRO B N   1 
ATOM   6671 C CA  . PRO B 1 416 ? 5.171   14.500  -3.033  1.00 19.09  ? 445 PRO B CA  1 
ATOM   6672 C C   . PRO B 1 416 ? 6.542   13.840  -2.878  1.00 17.13  ? 445 PRO B C   1 
ATOM   6673 O O   . PRO B 1 416 ? 7.086   13.747  -1.786  1.00 16.20  ? 445 PRO B O   1 
ATOM   6674 C CB  . PRO B 1 416 ? 5.269   15.836  -3.828  1.00 20.75  ? 445 PRO B CB  1 
ATOM   6675 C CG  . PRO B 1 416 ? 5.753   16.781  -2.744  1.00 21.38  ? 445 PRO B CG  1 
ATOM   6676 C CD  . PRO B 1 416 ? 4.918   16.385  -1.518  1.00 20.46  ? 445 PRO B CD  1 
ATOM   6677 N N   . LEU B 1 417 ? 7.068   13.409  -4.016  1.00 19.34  ? 446 LEU B N   1 
ATOM   6678 C CA  . LEU B 1 417 ? 8.411   12.856  -4.142  1.00 19.79  ? 446 LEU B CA  1 
ATOM   6679 C C   . LEU B 1 417 ? 9.428   13.863  -3.606  1.00 22.07  ? 446 LEU B C   1 
ATOM   6680 O O   . LEU B 1 417 ? 9.409   15.046  -3.958  1.00 21.62  ? 446 LEU B O   1 
ATOM   6681 C CB  . LEU B 1 417 ? 8.642   12.555  -5.627  1.00 23.52  ? 446 LEU B CB  1 
ATOM   6682 C CG  . LEU B 1 417 ? 9.966   11.913  -6.063  1.00 27.95  ? 446 LEU B CG  1 
ATOM   6683 C CD1 . LEU B 1 417 ? 9.970   10.405  -5.839  1.00 28.54  ? 446 LEU B CD1 1 
ATOM   6684 C CD2 . LEU B 1 417 ? 10.266  12.231  -7.551  1.00 28.17  ? 446 LEU B CD2 1 
ATOM   6685 N N   . GLU B 1 418 ? 10.331  13.390  -2.755  1.00 19.46  ? 447 GLU B N   1 
ATOM   6686 C CA  . GLU B 1 418 ? 11.449  14.221  -2.336  1.00 22.47  ? 447 GLU B CA  1 
ATOM   6687 C C   . GLU B 1 418 ? 12.502  14.171  -3.441  1.00 21.52  ? 447 GLU B C   1 
ATOM   6688 O O   . GLU B 1 418 ? 13.031  13.112  -3.750  1.00 21.18  ? 447 GLU B O   1 
ATOM   6689 C CB  . GLU B 1 418 ? 12.002  13.750  -0.994  1.00 21.68  ? 447 GLU B CB  1 
ATOM   6690 C CG  . GLU B 1 418 ? 13.220  14.538  -0.523  1.00 23.69  ? 447 GLU B CG  1 
ATOM   6691 C CD  . GLU B 1 418 ? 13.631  14.228  0.918   1.00 27.18  ? 447 GLU B CD  1 
ATOM   6692 O OE1 . GLU B 1 418 ? 14.846  14.059  1.206   1.00 25.81  ? 447 GLU B OE1 1 
ATOM   6693 O OE2 . GLU B 1 418 ? 12.721  14.100  1.768   1.00 25.63  ? 447 GLU B OE2 1 
ATOM   6694 N N   . ARG B 1 419 ? 12.848  15.341  -3.963  1.00 22.57  ? 448 ARG B N   1 
ATOM   6695 C CA  . ARG B 1 419 ? 13.716  15.471  -5.116  1.00 26.25  ? 448 ARG B CA  1 
ATOM   6696 C C   . ARG B 1 419 ? 14.339  16.859  -5.038  1.00 27.32  ? 448 ARG B C   1 
ATOM   6697 O O   . ARG B 1 419 ? 13.874  17.763  -5.717  1.00 27.55  ? 448 ARG B O   1 
ATOM   6698 C CB  . ARG B 1 419 ? 12.923  15.349  -6.420  1.00 29.49  ? 448 ARG B CB  1 
ATOM   6699 C CG  . ARG B 1 419 ? 13.622  14.835  -7.673  1.00 38.72  ? 448 ARG B CG  1 
ATOM   6700 C CD  . ARG B 1 419 ? 14.871  15.569  -8.127  1.00 40.82  ? 448 ARG B CD  1 
ATOM   6701 N NE  . ARG B 1 419 ? 15.639  14.838  -9.154  1.00 42.48  ? 448 ARG B NE  1 
ATOM   6702 C CZ  . ARG B 1 419 ? 16.883  15.141  -9.560  1.00 45.13  ? 448 ARG B CZ  1 
ATOM   6703 N NH1 . ARG B 1 419 ? 17.465  14.444  -10.534 1.00 41.00  ? 448 ARG B NH1 1 
ATOM   6704 N NH2 . ARG B 1 419 ? 17.533  16.154  -8.982  1.00 50.94  ? 448 ARG B NH2 1 
ATOM   6705 N N   . PRO B 1 420 ? 15.380  17.078  -4.216  1.00 25.82  ? 449 PRO B N   1 
ATOM   6706 C CA  . PRO B 1 420 ? 16.098  18.357  -4.214  1.00 24.43  ? 449 PRO B CA  1 
ATOM   6707 C C   . PRO B 1 420 ? 16.978  18.445  -5.449  1.00 26.15  ? 449 PRO B C   1 
ATOM   6708 O O   . PRO B 1 420 ? 17.139  17.466  -6.156  1.00 23.36  ? 449 PRO B O   1 
ATOM   6709 C CB  . PRO B 1 420 ? 16.929  18.306  -2.970  1.00 22.44  ? 449 PRO B CB  1 
ATOM   6710 C CG  . PRO B 1 420 ? 17.252  16.818  -2.832  1.00 24.93  ? 449 PRO B CG  1 
ATOM   6711 C CD  . PRO B 1 420 ? 16.007  16.092  -3.322  1.00 23.31  ? 449 PRO B CD  1 
ATOM   6712 N N   . LYS B 1 421 ? 17.592  19.620  -5.635  1.00 24.15  ? 450 LYS B N   1 
ATOM   6713 C CA  . LYS B 1 421 ? 18.531  19.849  -6.724  1.00 27.46  ? 450 LYS B CA  1 
ATOM   6714 C C   . LYS B 1 421 ? 19.941  19.633  -6.182  1.00 22.48  ? 450 LYS B C   1 
ATOM   6715 O O   . LYS B 1 421 ? 20.268  20.117  -5.118  1.00 25.51  ? 450 LYS B O   1 
ATOM   6716 C CB  . LYS B 1 421 ? 18.315  21.282  -7.260  1.00 32.52  ? 450 LYS B CB  1 
ATOM   6717 C CG  . LYS B 1 421 ? 19.311  21.799  -8.282  1.00 34.98  ? 450 LYS B CG  1 
ATOM   6718 C CD  . LYS B 1 421 ? 19.041  21.232  -9.664  1.00 40.64  ? 450 LYS B CD  1 
ATOM   6719 C CE  . LYS B 1 421 ? 20.208  21.267  -10.583 1.00 42.50  ? 450 LYS B CE  1 
ATOM   6720 N NZ  . LYS B 1 421 ? 19.807  20.475  -11.737 1.00 43.62  ? 450 LYS B NZ  1 
ATOM   6721 N N   . SER B 1 422 ? 20.781  18.894  -6.901  1.00 21.96  ? 451 SER B N   1 
ATOM   6722 C CA  . SER B 1 422 ? 22.180  18.793  -6.562  1.00 21.91  ? 451 SER B CA  1 
ATOM   6723 C C   . SER B 1 422 ? 22.978  19.705  -7.474  1.00 23.47  ? 451 SER B C   1 
ATOM   6724 O O   . SER B 1 422 ? 22.482  20.088  -8.532  1.00 22.36  ? 451 SER B O   1 
ATOM   6725 C CB  . SER B 1 422 ? 22.672  17.403  -6.639  1.00 20.80  ? 451 SER B CB  1 
ATOM   6726 O OG  . SER B 1 422 ? 22.726  16.960  -7.969  1.00 18.32  ? 451 SER B OG  1 
ATOM   6727 N N   . MET B 1 423 ? 24.223  19.981  -7.065  1.00 23.79  ? 452 MET B N   1 
ATOM   6728 C CA  . MET B 1 423 ? 25.193  20.711  -7.867  1.00 24.31  ? 452 MET B CA  1 
ATOM   6729 C C   . MET B 1 423 ? 26.548  20.082  -7.644  1.00 20.59  ? 452 MET B C   1 
ATOM   6730 O O   . MET B 1 423 ? 26.782  19.519  -6.576  1.00 24.59  ? 452 MET B O   1 
ATOM   6731 C CB  . MET B 1 423 ? 25.330  22.154  -7.382  1.00 26.71  ? 452 MET B CB  1 
ATOM   6732 C CG  . MET B 1 423 ? 23.986  22.818  -7.253  1.00 36.19  ? 452 MET B CG  1 
ATOM   6733 S SD  . MET B 1 423 ? 23.672  23.525  -8.872  1.00 47.31  ? 452 MET B SD  1 
ATOM   6734 C CE  . MET B 1 423 ? 24.301  25.060  -8.159  1.00 37.00  ? 452 MET B CE  1 
ATOM   6735 N N   . SER B 1 424 ? 27.405  20.150  -8.649  1.00 21.24  ? 453 SER B N   1 
ATOM   6736 C CA  . SER B 1 424 ? 28.809  19.834  -8.488  1.00 24.21  ? 453 SER B CA  1 
ATOM   6737 C C   . SER B 1 424 ? 29.597  21.014  -7.903  1.00 22.93  ? 453 SER B C   1 
ATOM   6738 O O   . SER B 1 424 ? 29.178  22.174  -7.929  1.00 22.25  ? 453 SER B O   1 
ATOM   6739 C CB  . SER B 1 424 ? 29.407  19.423  -9.805  1.00 27.54  ? 453 SER B CB  1 
ATOM   6740 O OG  . SER B 1 424 ? 29.594  20.527  -10.687 1.00 24.71  ? 453 SER B OG  1 
ATOM   6741 N N   . THR B 1 425 ? 30.810  20.721  -7.456  1.00 25.44  ? 454 THR B N   1 
ATOM   6742 C CA  . THR B 1 425 ? 31.720  21.774  -7.029  1.00 28.44  ? 454 THR B CA  1 
ATOM   6743 C C   . THR B 1 425 ? 31.948  22.733  -8.202  1.00 30.54  ? 454 THR B C   1 
ATOM   6744 O O   . THR B 1 425 ? 31.798  23.958  -8.068  1.00 28.39  ? 454 THR B O   1 
ATOM   6745 C CB  . THR B 1 425 ? 33.009  21.151  -6.512  1.00 28.52  ? 454 THR B CB  1 
ATOM   6746 O OG1 . THR B 1 425 ? 32.722  20.510  -5.268  1.00 27.09  ? 454 THR B OG1 1 
ATOM   6747 C CG2 . THR B 1 425 ? 34.067  22.201  -6.239  1.00 27.58  ? 454 THR B CG2 1 
ATOM   6748 N N   . GLU B 1 426 ? 32.279  22.162  -9.366  1.00 31.07  ? 455 GLU B N   1 
ATOM   6749 C CA  . GLU B 1 426 ? 32.472  22.952  -10.571 1.00 34.01  ? 455 GLU B CA  1 
ATOM   6750 C C   . GLU B 1 426 ? 31.239  23.825  -10.784 1.00 36.90  ? 455 GLU B C   1 
ATOM   6751 O O   . GLU B 1 426 ? 31.346  25.050  -10.941 1.00 37.84  ? 455 GLU B O   1 
ATOM   6752 C CB  . GLU B 1 426 ? 32.769  22.039  -11.764 1.00 41.53  ? 455 GLU B CB  1 
ATOM   6753 C CG  . GLU B 1 426 ? 33.326  22.783  -12.978 1.00 53.59  ? 455 GLU B CG  1 
ATOM   6754 C CD  . GLU B 1 426 ? 33.531  22.013  -14.283 1.00 64.21  ? 455 GLU B CD  1 
ATOM   6755 O OE1 . GLU B 1 426 ? 34.175  22.616  -15.182 1.00 63.13  ? 455 GLU B OE1 1 
ATOM   6756 O OE2 . GLU B 1 426 ? 33.046  20.860  -14.440 1.00 65.38  ? 455 GLU B OE2 1 
ATOM   6757 N N   . GLY B 1 427 ? 30.057  23.186  -10.814 1.00 34.27  ? 456 GLY B N   1 
ATOM   6758 C CA  . GLY B 1 427 ? 28.806  23.912  -10.984 1.00 29.99  ? 456 GLY B CA  1 
ATOM   6759 C C   . GLY B 1 427 ? 28.606  25.025  -9.961  1.00 32.25  ? 456 GLY B C   1 
ATOM   6760 O O   . GLY B 1 427 ? 28.140  26.111  -10.288 1.00 33.74  ? 456 GLY B O   1 
ATOM   6761 N N   . LEU B 1 428 ? 28.897  24.746  -8.693  1.00 34.56  ? 457 LEU B N   1 
ATOM   6762 C CA  . LEU B 1 428 ? 28.679  25.714  -7.635  1.00 32.63  ? 457 LEU B CA  1 
ATOM   6763 C C   . LEU B 1 428 ? 29.611  26.901  -7.789  1.00 38.32  ? 457 LEU B C   1 
ATOM   6764 O O   . LEU B 1 428 ? 29.206  28.011  -7.461  1.00 39.73  ? 457 LEU B O   1 
ATOM   6765 C CB  . LEU B 1 428 ? 28.892  25.117  -6.243  1.00 32.20  ? 457 LEU B CB  1 
ATOM   6766 C CG  . LEU B 1 428 ? 27.641  24.833  -5.428  1.00 32.75  ? 457 LEU B CG  1 
ATOM   6767 C CD1 . LEU B 1 428 ? 28.134  24.282  -4.105  1.00 35.66  ? 457 LEU B CD1 1 
ATOM   6768 C CD2 . LEU B 1 428 ? 26.719  26.015  -5.209  1.00 31.36  ? 457 LEU B CD2 1 
ATOM   6769 N N   . MET B 1 429 ? 30.874  26.624  -8.153  1.00 39.79  ? 458 MET B N   1 
ATOM   6770 C CA  . MET B 1 429 ? 31.869  27.667  -8.366  1.00 40.48  ? 458 MET B CA  1 
ATOM   6771 C C   . MET B 1 429 ? 31.390  28.654  -9.428  1.00 43.28  ? 458 MET B C   1 
ATOM   6772 O O   . MET B 1 429 ? 31.567  29.860  -9.264  1.00 48.55  ? 458 MET B O   1 
ATOM   6773 C CB  . MET B 1 429 ? 33.221  27.075  -8.770  1.00 38.80  ? 458 MET B CB  1 
ATOM   6774 C CG  . MET B 1 429 ? 33.951  26.475  -7.610  1.00 39.59  ? 458 MET B CG  1 
ATOM   6775 S SD  . MET B 1 429 ? 35.436  25.570  -8.071  1.00 46.00  ? 458 MET B SD  1 
ATOM   6776 C CE  . MET B 1 429 ? 36.016  25.492  -6.373  1.00 47.72  ? 458 MET B CE  1 
ATOM   6777 N N   . LYS B 1 430 ? 30.768  28.142  -10.492 1.00 46.79  ? 459 LYS B N   1 
ATOM   6778 C CA  . LYS B 1 430 ? 30.293  28.998  -11.570 1.00 49.33  ? 459 LYS B CA  1 
ATOM   6779 C C   . LYS B 1 430 ? 29.016  29.725  -11.151 1.00 47.52  ? 459 LYS B C   1 
ATOM   6780 O O   . LYS B 1 430 ? 28.791  30.859  -11.555 1.00 47.50  ? 459 LYS B O   1 
ATOM   6781 C CB  . LYS B 1 430 ? 30.066  28.280  -12.908 1.00 51.00  ? 459 LYS B CB  1 
ATOM   6782 C CG  . LYS B 1 430 ? 31.327  27.785  -13.621 1.00 58.74  ? 459 LYS B CG  1 
ATOM   6783 C CD  . LYS B 1 430 ? 31.294  27.886  -15.148 1.00 73.37  ? 459 LYS B CD  1 
ATOM   6784 C CE  . LYS B 1 430 ? 30.130  27.207  -15.824 1.00 78.45  ? 459 LYS B CE  1 
ATOM   6785 N NZ  . LYS B 1 430 ? 30.175  25.750  -15.672 1.00 83.68  ? 459 LYS B NZ  1 
ATOM   6786 N N   . PHE B 1 431 ? 28.174  29.063  -10.363 1.00 50.46  ? 460 PHE B N   1 
ATOM   6787 C CA  . PHE B 1 431 ? 26.918  29.643  -9.927  1.00 51.64  ? 460 PHE B CA  1 
ATOM   6788 C C   . PHE B 1 431 ? 27.163  30.866  -9.057  1.00 53.57  ? 460 PHE B C   1 
ATOM   6789 O O   . PHE B 1 431 ? 26.368  31.794  -9.123  1.00 54.61  ? 460 PHE B O   1 
ATOM   6790 C CB  . PHE B 1 431 ? 26.077  28.630  -9.149  1.00 52.30  ? 460 PHE B CB  1 
ATOM   6791 C CG  . PHE B 1 431 ? 24.701  29.144  -8.753  1.00 49.99  ? 460 PHE B CG  1 
ATOM   6792 C CD1 . PHE B 1 431 ? 23.672  29.218  -9.689  1.00 50.23  ? 460 PHE B CD1 1 
ATOM   6793 C CD2 . PHE B 1 431 ? 24.434  29.545  -7.450  1.00 50.15  ? 460 PHE B CD2 1 
ATOM   6794 C CE1 . PHE B 1 431 ? 22.411  29.685  -9.332  1.00 45.16  ? 460 PHE B CE1 1 
ATOM   6795 C CE2 . PHE B 1 431 ? 23.161  29.998  -7.096  1.00 52.80  ? 460 PHE B CE2 1 
ATOM   6796 C CZ  . PHE B 1 431 ? 22.157  30.074  -8.040  1.00 43.61  ? 460 PHE B CZ  1 
ATOM   6797 N N   . VAL B 1 432 ? 28.240  30.853  -8.248  1.00 57.61  ? 461 VAL B N   1 
ATOM   6798 C CA  . VAL B 1 432 ? 28.474  31.890  -7.248  1.00 57.91  ? 461 VAL B CA  1 
ATOM   6799 C C   . VAL B 1 432 ? 29.138  33.118  -7.870  1.00 58.09  ? 461 VAL B C   1 
ATOM   6800 O O   . VAL B 1 432 ? 28.975  34.217  -7.344  1.00 63.46  ? 461 VAL B O   1 
ATOM   6801 C CB  . VAL B 1 432 ? 29.278  31.477  -6.000  1.00 53.84  ? 461 VAL B CB  1 
ATOM   6802 C CG1 . VAL B 1 432 ? 28.655  30.274  -5.307  1.00 53.30  ? 461 VAL B CG1 1 
ATOM   6803 C CG2 . VAL B 1 432 ? 30.752  31.262  -6.296  1.00 57.07  ? 461 VAL B CG2 1 
ATOM   6804 N N   . ASP B 1 433 ? 29.919  32.933  -8.936  1.00 63.75  ? 462 ASP B N   1 
ATOM   6805 C CA  . ASP B 1 433 ? 30.548  34.060  -9.613  1.00 73.71  ? 462 ASP B CA  1 
ATOM   6806 C C   . ASP B 1 433 ? 29.470  35.028  -10.101 1.00 79.20  ? 462 ASP B C   1 
ATOM   6807 O O   . ASP B 1 433 ? 29.543  36.226  -9.822  1.00 84.64  ? 462 ASP B O   1 
ATOM   6808 C CB  . ASP B 1 433 ? 31.524  33.582  -10.676 1.00 69.97  ? 462 ASP B CB  1 
ATOM   6809 C CG  . ASP B 1 433 ? 32.780  32.947  -10.100 1.00 69.93  ? 462 ASP B CG  1 
ATOM   6810 O OD1 . ASP B 1 433 ? 32.854  32.834  -8.854  1.00 85.03  ? 462 ASP B OD1 1 
ATOM   6811 O OD2 . ASP B 1 433 ? 33.680  32.591  -10.885 1.00 60.57  ? 462 ASP B OD2 1 
ATOM   6812 N N   . SER B 1 434 ? 28.461  34.481  -10.792 1.00 76.36  ? 463 SER B N   1 
ATOM   6813 C CA  . SER B 1 434 ? 27.236  35.201  -11.117 1.00 77.82  ? 463 SER B CA  1 
ATOM   6814 C C   . SER B 1 434 ? 26.414  35.478  -9.842  1.00 70.37  ? 463 SER B C   1 
ATOM   6815 O O   . SER B 1 434 ? 25.274  35.996  -9.965  1.00 61.25  ? 463 SER B O   1 
ATOM   6816 C CB  . SER B 1 434 ? 26.439  34.428  -12.148 1.00 77.12  ? 463 SER B CB  1 
ATOM   6817 O OG  . SER B 1 434 ? 26.464  33.031  -11.876 1.00 79.09  ? 463 SER B OG  1 
HETATM 6818 N N1A . COA C 2 .   ? 0.724   14.129  -19.449 1.00 78.70  ? 501 COA A N1A 1 
HETATM 6819 C C2A . COA C 2 .   ? -0.224  14.933  -18.944 1.00 77.96  ? 501 COA A C2A 1 
HETATM 6820 N N3A . COA C 2 .   ? -0.118  15.871  -18.006 1.00 75.23  ? 501 COA A N3A 1 
HETATM 6821 C C4A . COA C 2 .   ? 1.146   15.959  -17.562 1.00 73.89  ? 501 COA A C4A 1 
HETATM 6822 C C5A . COA C 2 .   ? 2.227   15.213  -17.986 1.00 74.30  ? 501 COA A C5A 1 
HETATM 6823 C C6A . COA C 2 .   ? 1.994   14.247  -18.986 1.00 69.41  ? 501 COA A C6A 1 
HETATM 6824 N N6A . COA C 2 .   ? 2.938   13.453  -19.488 1.00 62.72  ? 501 COA A N6A 1 
HETATM 6825 N N7A . COA C 2 .   ? 3.372   15.588  -17.291 1.00 74.17  ? 501 COA A N7A 1 
HETATM 6826 C C8A . COA C 2 .   ? 2.968   16.535  -16.476 1.00 79.74  ? 501 COA A C8A 1 
HETATM 6827 N N9A . COA C 2 .   ? 1.626   16.816  -16.611 1.00 81.20  ? 501 COA A N9A 1 
HETATM 6828 C C1B . COA C 2 .   ? 0.829   17.766  -15.825 1.00 90.90  ? 501 COA A C1B 1 
HETATM 6829 C C2B . COA C 2 .   ? 1.072   17.631  -14.323 1.00 89.99  ? 501 COA A C2B 1 
HETATM 6830 O O2B . COA C 2 .   ? 0.363   16.553  -13.754 1.00 89.84  ? 501 COA A O2B 1 
HETATM 6831 C C3B . COA C 2 .   ? 0.563   18.990  -13.855 1.00 91.20  ? 501 COA A C3B 1 
HETATM 6832 O O3B . COA C 2 .   ? -0.863  18.957  -13.881 1.00 86.53  ? 501 COA A O3B 1 
HETATM 6833 P P3B . COA C 2 .   ? -1.670  19.620  -12.644 1.00 93.62  ? 501 COA A P3B 1 
HETATM 6834 O O7A . COA C 2 .   ? -1.665  18.683  -11.432 1.00 61.82  ? 501 COA A O7A 1 
HETATM 6835 O O8A . COA C 2 .   ? -3.057  19.774  -13.257 1.00 77.66  ? 501 COA A O8A 1 
HETATM 6836 O O9A . COA C 2 .   ? -1.023  20.958  -12.333 1.00 85.05  ? 501 COA A O9A 1 
HETATM 6837 C C4B . COA C 2 .   ? 1.144   19.905  -14.935 1.00 94.39  ? 501 COA A C4B 1 
HETATM 6838 O O4B . COA C 2 .   ? 1.179   19.096  -16.143 1.00 94.98  ? 501 COA A O4B 1 
HETATM 6839 C C5B . COA C 2 .   ? 2.530   20.433  -14.648 1.00 92.39  ? 501 COA A C5B 1 
HETATM 6840 O O5B . COA C 2 .   ? 3.224   19.502  -13.774 1.00 92.81  ? 501 COA A O5B 1 
HETATM 6841 P P1A . COA C 2 .   ? 4.828   19.450  -13.715 1.00 82.17  ? 501 COA A P1A 1 
HETATM 6842 O O1A . COA C 2 .   ? 5.361   20.840  -13.587 1.00 82.05  ? 501 COA A O1A 1 
HETATM 6843 O O2A . COA C 2 .   ? 5.329   18.573  -14.815 1.00 89.50  ? 501 COA A O2A 1 
HETATM 6844 O O3A . COA C 2 .   ? 5.018   18.679  -12.318 1.00 93.92  ? 501 COA A O3A 1 
HETATM 6845 P P2A . COA C 2 .   ? 5.721   17.367  -11.707 1.00 93.29  ? 501 COA A P2A 1 
HETATM 6846 O O4A . COA C 2 .   ? 7.151   17.691  -11.422 1.00 87.26  ? 501 COA A O4A 1 
HETATM 6847 O O5A . COA C 2 .   ? 4.842   16.892  -10.590 1.00 80.64  ? 501 COA A O5A 1 
HETATM 6848 O O6A . COA C 2 .   ? 5.695   16.293  -12.917 1.00 85.93  ? 501 COA A O6A 1 
HETATM 6849 C CBP . COA C 2 .   ? 6.403   14.025  -13.625 1.00 73.14  ? 501 COA A CBP 1 
HETATM 6850 C CCP . COA C 2 .   ? 6.853   15.415  -13.156 1.00 76.32  ? 501 COA A CCP 1 
HETATM 6851 C CDP . COA C 2 .   ? 7.615   13.309  -14.239 1.00 73.10  ? 501 COA A CDP 1 
HETATM 6852 C CEP . COA C 2 .   ? 5.923   13.204  -12.420 1.00 73.44  ? 501 COA A CEP 1 
HETATM 6853 C CAP . COA C 2 .   ? 5.266   14.145  -14.656 1.00 63.89  ? 501 COA A CAP 1 
HETATM 6854 O OAP . COA C 2 .   ? 5.782   14.815  -15.789 1.00 56.53  ? 501 COA A OAP 1 
HETATM 6855 C C9P . COA C 2 .   ? 4.571   12.856  -15.089 1.00 61.49  ? 501 COA A C9P 1 
HETATM 6856 O O9P . COA C 2 .   ? 3.426   12.627  -14.688 1.00 49.50  ? 501 COA A O9P 1 
HETATM 6857 N N8P . COA C 2 .   ? 5.220   12.042  -15.919 1.00 57.26  ? 501 COA A N8P 1 
HETATM 6858 C C7P . COA C 2 .   ? 4.695   10.747  -16.359 1.00 51.71  ? 501 COA A C7P 1 
HETATM 6859 C C6P . COA C 2 .   ? 5.411   9.567   -15.710 1.00 47.58  ? 501 COA A C6P 1 
HETATM 6860 C C5P . COA C 2 .   ? 6.841   9.444   -16.199 1.00 50.51  ? 501 COA A C5P 1 
HETATM 6861 O O5P . COA C 2 .   ? 7.093   9.494   -17.400 1.00 45.44  ? 501 COA A O5P 1 
HETATM 6862 N N4P . COA C 2 .   ? 7.818   9.310   -15.289 1.00 50.62  ? 501 COA A N4P 1 
HETATM 6863 C C3P . COA C 2 .   ? 9.225   9.118   -15.630 1.00 54.88  ? 501 COA A C3P 1 
HETATM 6864 C C2P . COA C 2 .   ? 10.103  10.261  -15.155 1.00 56.96  ? 501 COA A C2P 1 
HETATM 6865 S S1P . COA C 2 .   ? 10.418  10.199  -13.366 1.00 64.87  ? 501 COA A S1P 1 
HETATM 6866 C C   . ACE D 3 .   ? 13.302  9.089   -14.909 1.00 54.32  ? 502 ACE A C   1 
HETATM 6867 O O   . ACE D 3 .   ? 13.954  10.069  -15.137 1.00 59.95  ? 502 ACE A O   1 
HETATM 6868 C CH3 . ACE D 3 .   ? 13.624  8.093   -13.785 1.00 49.13  ? 502 ACE A CH3 1 
HETATM 6869 O O1  . OAA E 4 .   ? 14.428  12.244  -10.634 1.00 40.88  ? 503 OAA A O1  1 
HETATM 6870 O O2  . OAA E 4 .   ? 15.930  12.150  -12.292 1.00 41.28  ? 503 OAA A O2  1 
HETATM 6871 O O4  . OAA E 4 .   ? 17.240  8.887   -13.714 1.00 30.59  ? 503 OAA A O4  1 
HETATM 6872 O O5  . OAA E 4 .   ? 16.805  9.055   -11.666 1.00 33.50  ? 503 OAA A O5  1 
HETATM 6873 O O3  . OAA E 4 .   ? 15.026  10.139  -14.273 1.00 38.26  ? 503 OAA A O3  1 
HETATM 6874 C C1  . OAA E 4 .   ? 14.950  11.667  -11.615 1.00 41.52  ? 503 OAA A C1  1 
HETATM 6875 C C2  . OAA E 4 .   ? 14.408  10.294  -12.011 1.00 35.83  ? 503 OAA A C2  1 
HETATM 6876 C C3  . OAA E 4 .   ? 15.320  9.813   -13.116 1.00 42.52  ? 503 OAA A C3  1 
HETATM 6877 C C4  . OAA E 4 .   ? 16.484  9.196   -12.830 1.00 31.69  ? 503 OAA A C4  1 
HETATM 6878 O O   . HOH F 5 .   ? -5.548  0.596   -39.459 1.00 59.23  ? 601 HOH A O   1 
HETATM 6879 O O   . HOH F 5 .   ? 12.390  7.069   -14.872 1.00 60.22  ? 602 HOH A O   1 
HETATM 6880 O O   . HOH F 5 .   ? 36.067  3.261   13.138  1.00 49.91  ? 603 HOH A O   1 
HETATM 6881 O O   . HOH F 5 .   ? 16.759  -5.815  -35.490 1.00 56.23  ? 604 HOH A O   1 
HETATM 6882 O O   . HOH F 5 .   ? 8.346   15.816  -30.981 1.00 59.55  ? 605 HOH A O   1 
HETATM 6883 O O   . HOH F 5 .   ? 31.801  35.104  -3.607  1.00 55.15  ? 606 HOH A O   1 
HETATM 6884 O O   . HOH F 5 .   ? 7.885   -12.174 -8.418  1.00 34.68  ? 607 HOH A O   1 
HETATM 6885 O O   . HOH F 5 .   ? 17.793  14.734  -27.133 1.00 52.87  ? 608 HOH A O   1 
HETATM 6886 O O   . HOH F 5 .   ? 46.302  2.858   1.878   1.00 34.35  ? 609 HOH A O   1 
HETATM 6887 O O   . HOH F 5 .   ? 38.664  -13.374 -13.877 1.00 39.29  ? 610 HOH A O   1 
HETATM 6888 O O   . HOH F 5 .   ? 39.658  14.756  -13.244 1.00 49.40  ? 611 HOH A O   1 
HETATM 6889 O O   . HOH F 5 .   ? 31.475  0.475   -34.418 1.00 55.19  ? 612 HOH A O   1 
HETATM 6890 O O   . HOH F 5 .   ? 39.838  -11.299 -14.781 1.00 39.01  ? 613 HOH A O   1 
HETATM 6891 O O   . HOH F 5 .   ? 10.618  -19.883 -14.763 1.00 42.81  ? 614 HOH A O   1 
HETATM 6892 O O   . HOH F 5 .   ? 30.142  -3.881  -20.770 1.00 23.77  ? 615 HOH A O   1 
HETATM 6893 O O   . HOH F 5 .   ? 23.247  3.742   -31.443 1.00 46.92  ? 616 HOH A O   1 
HETATM 6894 O O   . HOH F 5 .   ? 5.223   -17.921 -5.901  1.00 48.43  ? 617 HOH A O   1 
HETATM 6895 O O   . HOH F 5 .   ? 38.234  20.013  1.255   1.00 42.99  ? 618 HOH A O   1 
HETATM 6896 O O   . HOH F 5 .   ? 34.112  8.495   11.559  1.00 37.62  ? 619 HOH A O   1 
HETATM 6897 O O   . HOH F 5 .   ? 26.081  17.272  8.782   1.00 43.05  ? 620 HOH A O   1 
HETATM 6898 O O   . HOH F 5 .   ? -1.458  2.315   -40.220 1.00 63.29  ? 621 HOH A O   1 
HETATM 6899 O O   . HOH F 5 .   ? 37.284  5.337   11.551  1.00 36.19  ? 622 HOH A O   1 
HETATM 6900 O O   . HOH F 5 .   ? -4.338  19.982  -23.033 1.00 57.96  ? 623 HOH A O   1 
HETATM 6901 O O   . HOH F 5 .   ? 46.012  7.796   5.153   1.00 43.50  ? 624 HOH A O   1 
HETATM 6902 O O   . HOH F 5 .   ? 18.710  -6.091  -33.768 1.00 33.74  ? 625 HOH A O   1 
HETATM 6903 O O   . HOH F 5 .   ? 20.867  8.290   -16.253 1.00 29.29  ? 626 HOH A O   1 
HETATM 6904 O O   . HOH F 5 .   ? 22.226  9.608   -9.899  1.00 19.91  ? 627 HOH A O   1 
HETATM 6905 O O   . HOH F 5 .   ? 4.035   19.905  16.699  1.00 32.99  ? 628 HOH A O   1 
HETATM 6906 O O   . HOH F 5 .   ? 42.061  -1.423  -8.235  1.00 27.22  ? 629 HOH A O   1 
HETATM 6907 O O   . HOH F 5 .   ? 29.633  5.496   3.216   1.00 22.29  ? 630 HOH A O   1 
HETATM 6908 O O   . HOH F 5 .   ? 15.640  12.615  -3.662  1.00 18.64  ? 631 HOH A O   1 
HETATM 6909 O O   . HOH F 5 .   ? 44.409  14.603  -14.125 1.00 45.34  ? 632 HOH A O   1 
HETATM 6910 O O   . HOH F 5 .   ? 20.305  20.219  10.762  1.00 30.09  ? 633 HOH A O   1 
HETATM 6911 O O   . HOH F 5 .   ? 25.138  17.314  -9.073  1.00 25.63  ? 634 HOH A O   1 
HETATM 6912 O O   . HOH F 5 .   ? 36.643  1.937   -28.842 1.00 33.67  ? 635 HOH A O   1 
HETATM 6913 O O   . HOH F 5 .   ? 35.837  16.126  -16.575 1.00 38.20  ? 636 HOH A O   1 
HETATM 6914 O O   . HOH F 5 .   ? 29.908  10.817  6.864   1.00 16.96  ? 637 HOH A O   1 
HETATM 6915 O O   . HOH F 5 .   ? 27.446  10.325  9.784   1.00 38.31  ? 638 HOH A O   1 
HETATM 6916 O O   . HOH F 5 .   ? 34.008  -7.923  -17.339 1.00 30.39  ? 639 HOH A O   1 
HETATM 6917 O O   . HOH F 5 .   ? 35.421  -13.182 -7.563  1.00 34.00  ? 640 HOH A O   1 
HETATM 6918 O O   . HOH F 5 .   ? 25.732  -2.198  -32.397 1.00 47.56  ? 641 HOH A O   1 
HETATM 6919 O O   . HOH F 5 .   ? 24.155  15.502  1.903   1.00 22.22  ? 642 HOH A O   1 
HETATM 6920 O O   . HOH F 5 .   ? 37.455  15.669  13.966  1.00 54.63  ? 643 HOH A O   1 
HETATM 6921 O O   . HOH F 5 .   ? 35.011  17.151  -6.610  1.00 46.27  ? 644 HOH A O   1 
HETATM 6922 O O   . HOH F 5 .   ? 5.927   17.527  -17.520 1.00 49.31  ? 645 HOH A O   1 
HETATM 6923 O O   . HOH F 5 .   ? 49.483  -0.463  -8.270  1.00 38.34  ? 646 HOH A O   1 
HETATM 6924 O O   . HOH F 5 .   ? 48.784  1.157   -13.244 1.00 42.34  ? 647 HOH A O   1 
HETATM 6925 O O   . HOH F 5 .   ? 43.978  22.188  -5.164  1.00 51.65  ? 648 HOH A O   1 
HETATM 6926 O O   . HOH F 5 .   ? 39.164  13.179  -20.585 1.00 32.11  ? 649 HOH A O   1 
HETATM 6927 O O   . HOH F 5 .   ? 8.958   2.006   -21.851 1.00 26.00  ? 650 HOH A O   1 
HETATM 6928 O O   . HOH F 5 .   ? 7.609   -3.844  -11.330 1.00 36.91  ? 651 HOH A O   1 
HETATM 6929 O O   . HOH F 5 .   ? 30.410  -1.704  -28.096 1.00 31.40  ? 652 HOH A O   1 
HETATM 6930 O O   . HOH F 5 .   ? 42.507  -2.778  -5.855  1.00 29.30  ? 653 HOH A O   1 
HETATM 6931 O O   . HOH F 5 .   ? 27.296  -8.447  7.749   1.00 26.00  ? 654 HOH A O   1 
HETATM 6932 O O   . HOH F 5 .   ? 7.487   -1.127  -5.417  1.00 32.01  ? 655 HOH A O   1 
HETATM 6933 O O   . HOH F 5 .   ? 13.603  -2.989  -3.709  1.00 24.61  ? 656 HOH A O   1 
HETATM 6934 O O   . HOH F 5 .   ? 21.437  11.691  -26.968 1.00 35.99  ? 657 HOH A O   1 
HETATM 6935 O O   . HOH F 5 .   ? 26.748  14.464  3.092   1.00 23.89  ? 658 HOH A O   1 
HETATM 6936 O O   . HOH F 5 .   ? 27.192  9.729   -1.792  1.00 17.98  ? 659 HOH A O   1 
HETATM 6937 O O   . HOH F 5 .   ? 8.941   2.195   -24.617 1.00 33.71  ? 660 HOH A O   1 
HETATM 6938 O O   . HOH F 5 .   ? 28.166  -0.831  7.082   1.00 25.31  ? 661 HOH A O   1 
HETATM 6939 O O   . HOH F 5 .   ? 29.487  -16.922 -7.795  1.00 36.64  ? 662 HOH A O   1 
HETATM 6940 O O   . HOH F 5 .   ? 37.739  13.432  15.654  1.00 47.12  ? 663 HOH A O   1 
HETATM 6941 O O   . HOH F 5 .   ? 10.426  18.411  1.932   1.00 22.40  ? 664 HOH A O   1 
HETATM 6942 O O   . HOH F 5 .   ? 32.481  -16.588 -23.454 1.00 45.96  ? 665 HOH A O   1 
HETATM 6943 O O   . HOH F 5 .   ? 10.842  -4.010  -4.370  1.00 30.52  ? 666 HOH A O   1 
HETATM 6944 O O   . HOH F 5 .   ? 48.393  14.494  -5.941  1.00 39.50  ? 667 HOH A O   1 
HETATM 6945 O O   . HOH F 5 .   ? 42.302  8.366   -19.258 1.00 37.18  ? 668 HOH A O   1 
HETATM 6946 O O   . HOH F 5 .   ? 27.282  9.435   1.110   1.00 14.30  ? 669 HOH A O   1 
HETATM 6947 O O   . HOH F 5 .   ? 35.203  -11.230 -5.486  1.00 55.04  ? 670 HOH A O   1 
HETATM 6948 O O   . HOH F 5 .   ? 36.671  10.421  4.973   1.00 30.58  ? 671 HOH A O   1 
HETATM 6949 O O   . HOH F 5 .   ? 5.809   -8.035  -22.362 1.00 51.36  ? 672 HOH A O   1 
HETATM 6950 O O   . HOH F 5 .   ? 28.521  17.131  -15.373 1.00 21.83  ? 673 HOH A O   1 
HETATM 6951 O O   . HOH F 5 .   ? 26.553  16.379  -0.426  1.00 22.30  ? 674 HOH A O   1 
HETATM 6952 O O   . HOH F 5 .   ? 35.401  14.936  -7.811  1.00 27.63  ? 675 HOH A O   1 
HETATM 6953 O O   . HOH F 5 .   ? 37.948  -7.078  6.528   1.00 51.87  ? 676 HOH A O   1 
HETATM 6954 O O   . HOH F 5 .   ? 42.795  -2.751  -25.104 1.00 48.60  ? 677 HOH A O   1 
HETATM 6955 O O   . HOH F 5 .   ? 17.244  -4.905  1.906   1.00 30.16  ? 678 HOH A O   1 
HETATM 6956 O O   . HOH F 5 .   ? 26.046  8.103   -3.648  1.00 22.02  ? 679 HOH A O   1 
HETATM 6957 O O   . HOH F 5 .   ? 15.652  -17.204 0.512   1.00 30.85  ? 680 HOH A O   1 
HETATM 6958 O O   . HOH F 5 .   ? 23.307  14.271  -22.592 1.00 30.92  ? 681 HOH A O   1 
HETATM 6959 O O   . HOH F 5 .   ? 12.988  -3.286  -38.476 1.00 41.60  ? 682 HOH A O   1 
HETATM 6960 O O   . HOH F 5 .   ? 33.048  11.011  4.897   1.00 24.75  ? 683 HOH A O   1 
HETATM 6961 O O   . HOH F 5 .   ? 40.457  9.082   11.685  1.00 29.48  ? 684 HOH A O   1 
HETATM 6962 O O   . HOH F 5 .   ? 30.268  0.518   8.057   1.00 25.65  ? 685 HOH A O   1 
HETATM 6963 O O   . HOH F 5 .   ? 35.072  -18.732 -18.439 1.00 50.13  ? 686 HOH A O   1 
HETATM 6964 O O   . HOH F 5 .   ? 30.581  20.960  6.785   1.00 42.98  ? 687 HOH A O   1 
HETATM 6965 O O   . HOH F 5 .   ? 45.091  10.219  -1.689  1.00 35.54  ? 688 HOH A O   1 
HETATM 6966 O O   . HOH F 5 .   ? 0.441   5.172   -12.568 1.00 48.72  ? 689 HOH A O   1 
HETATM 6967 O O   . HOH F 5 .   ? 39.781  11.064  2.661   1.00 42.29  ? 690 HOH A O   1 
HETATM 6968 O O   . HOH F 5 .   ? 35.427  23.156  4.487   1.00 52.97  ? 691 HOH A O   1 
HETATM 6969 O O   . HOH F 5 .   ? 29.877  16.766  -13.035 1.00 32.59  ? 692 HOH A O   1 
HETATM 6970 O O   . HOH F 5 .   ? 32.801  14.120  7.791   1.00 43.40  ? 693 HOH A O   1 
HETATM 6971 O O   . HOH F 5 .   ? 38.756  -4.774  5.908   1.00 51.32  ? 694 HOH A O   1 
HETATM 6972 O O   . HOH F 5 .   ? 5.824   -4.056  -14.283 1.00 57.47  ? 695 HOH A O   1 
HETATM 6973 O O   . HOH F 5 .   ? 33.037  19.355  -9.640  1.00 31.79  ? 696 HOH A O   1 
HETATM 6974 O O   . HOH F 5 .   ? 38.670  33.527  -5.544  1.00 42.11  ? 697 HOH A O   1 
HETATM 6975 O O   . HOH F 5 .   ? -0.585  4.621   -41.394 1.00 57.39  ? 698 HOH A O   1 
HETATM 6976 O O   . HOH F 5 .   ? 19.072  13.764  -19.233 1.00 33.13  ? 699 HOH A O   1 
HETATM 6977 O O   . HOH F 5 .   ? 5.455   -8.551  -17.929 1.00 40.48  ? 700 HOH A O   1 
HETATM 6978 O O   . HOH F 5 .   ? 27.854  12.170  1.868   1.00 27.56  ? 701 HOH A O   1 
HETATM 6979 O O   . HOH F 5 .   ? 46.508  13.861  -10.791 1.00 49.34  ? 702 HOH A O   1 
HETATM 6980 O O   . HOH F 5 .   ? 33.691  3.004   -22.442 1.00 26.50  ? 703 HOH A O   1 
HETATM 6981 O O   . HOH F 5 .   ? 35.443  20.417  2.711   1.00 39.74  ? 704 HOH A O   1 
HETATM 6982 O O   . HOH F 5 .   ? -3.563  2.194   -20.872 1.00 49.89  ? 705 HOH A O   1 
HETATM 6983 O O   . HOH F 5 .   ? 3.556   -7.587  -14.450 1.00 50.35  ? 706 HOH A O   1 
HETATM 6984 O O   . HOH F 5 .   ? 29.176  13.608  10.277  1.00 27.42  ? 707 HOH A O   1 
HETATM 6985 O O   . HOH F 5 .   ? 7.479   -9.733  -15.284 1.00 41.51  ? 708 HOH A O   1 
HETATM 6986 O O   . HOH F 5 .   ? 31.627  -8.936  -13.505 1.00 32.16  ? 709 HOH A O   1 
HETATM 6987 O O   . HOH F 5 .   ? 6.450   6.271   -25.914 1.00 38.01  ? 710 HOH A O   1 
HETATM 6988 O O   . HOH F 5 .   ? 13.593  10.675  -8.252  1.00 24.50  ? 711 HOH A O   1 
HETATM 6989 O O   . HOH F 5 .   ? 45.665  11.100  -11.346 1.00 48.53  ? 712 HOH A O   1 
HETATM 6990 O O   . HOH F 5 .   ? 17.384  26.494  -3.477  1.00 33.57  ? 713 HOH A O   1 
HETATM 6991 O O   . HOH F 5 .   ? 8.726   -15.572 -18.811 1.00 41.60  ? 714 HOH A O   1 
HETATM 6992 O O   . HOH F 5 .   ? 29.650  -17.656 -12.594 1.00 53.75  ? 715 HOH A O   1 
HETATM 6993 O O   . HOH F 5 .   ? 2.442   18.273  0.226   1.00 28.87  ? 716 HOH A O   1 
HETATM 6994 O O   . HOH F 5 .   ? 19.961  -19.223 -11.494 1.00 50.47  ? 717 HOH A O   1 
HETATM 6995 O O   . HOH F 5 .   ? 11.266  7.669   -31.155 1.00 42.72  ? 718 HOH A O   1 
HETATM 6996 O O   . HOH F 5 .   ? 38.568  8.933   2.783   1.00 24.76  ? 719 HOH A O   1 
HETATM 6997 O O   . HOH F 5 .   ? 45.617  -0.884  -2.412  1.00 38.36  ? 720 HOH A O   1 
HETATM 6998 O O   . HOH F 5 .   ? 25.411  35.756  -0.131  1.00 35.82  ? 721 HOH A O   1 
HETATM 6999 O O   . HOH F 5 .   ? -4.001  6.490   -19.942 1.00 51.82  ? 722 HOH A O   1 
HETATM 7000 O O   . HOH F 5 .   ? 40.926  13.293  11.980  1.00 48.47  ? 723 HOH A O   1 
HETATM 7001 O O   . HOH F 5 .   ? 35.969  27.285  5.231   1.00 48.26  ? 724 HOH A O   1 
HETATM 7002 O O   . HOH F 5 .   ? 11.319  -18.993 -7.736  1.00 46.99  ? 725 HOH A O   1 
HETATM 7003 O O   . HOH F 5 .   ? 17.332  24.999  -7.590  1.00 43.83  ? 726 HOH A O   1 
HETATM 7004 O O   . HOH F 5 .   ? 33.171  16.572  -27.890 1.00 51.52  ? 727 HOH A O   1 
HETATM 7005 O O   . HOH F 5 .   ? 8.817   21.910  14.502  1.00 26.40  ? 728 HOH A O   1 
HETATM 7006 O O   . HOH F 5 .   ? 43.799  -14.170 -21.968 1.00 48.33  ? 729 HOH A O   1 
HETATM 7007 O O   . HOH F 5 .   ? 9.117   -7.068  -34.631 1.00 45.74  ? 730 HOH A O   1 
HETATM 7008 O O   . HOH F 5 .   ? -2.450  6.894   -17.589 1.00 52.20  ? 731 HOH A O   1 
HETATM 7009 O O   . HOH F 5 .   ? 37.842  -15.001 -10.127 1.00 53.36  ? 732 HOH A O   1 
HETATM 7010 O O   . HOH F 5 .   ? 11.693  -11.573 -29.025 1.00 58.45  ? 733 HOH A O   1 
HETATM 7011 O O   . HOH F 5 .   ? 34.907  -19.786 -16.289 1.00 51.66  ? 734 HOH A O   1 
HETATM 7012 O O   . HOH F 5 .   ? -7.616  15.915  -32.473 1.00 48.45  ? 735 HOH A O   1 
HETATM 7013 O O   . HOH F 5 .   ? 10.077  -24.067 -12.750 1.00 49.43  ? 736 HOH A O   1 
HETATM 7014 O O   . HOH F 5 .   ? 30.529  -18.657 1.322   1.00 28.21  ? 737 HOH A O   1 
HETATM 7015 O O   . HOH F 5 .   ? 41.963  16.254  -13.437 1.00 50.58  ? 738 HOH A O   1 
HETATM 7016 O O   . HOH F 5 .   ? 34.955  35.970  2.407   1.00 48.74  ? 739 HOH A O   1 
HETATM 7017 O O   . HOH F 5 .   ? 26.714  -17.612 -23.423 1.00 54.02  ? 740 HOH A O   1 
HETATM 7018 O O   . HOH F 5 .   ? 9.485   -13.469 -25.272 1.00 58.62  ? 741 HOH A O   1 
HETATM 7019 O O   . HOH F 5 .   ? 42.018  -15.623 -19.278 1.00 61.31  ? 742 HOH A O   1 
HETATM 7020 O O   . HOH F 5 .   ? 16.043  29.378  -4.567  1.00 42.10  ? 743 HOH A O   1 
HETATM 7021 O O   . HOH F 5 .   ? 38.017  8.132   12.602  1.00 55.37  ? 744 HOH A O   1 
HETATM 7022 O O   . HOH F 5 .   ? 4.652   21.224  -31.850 1.00 46.83  ? 745 HOH A O   1 
HETATM 7023 O O   . HOH F 5 .   ? 30.881  -0.566  10.447  1.00 34.18  ? 746 HOH A O   1 
HETATM 7024 O O   . HOH F 5 .   ? 44.246  -4.221  -23.803 1.00 45.43  ? 747 HOH A O   1 
HETATM 7025 O O   . HOH F 5 .   ? 4.357   21.757  -29.572 1.00 55.85  ? 748 HOH A O   1 
HETATM 7026 O O   . HOH F 5 .   ? 17.046  10.842  -31.870 1.00 52.34  ? 749 HOH A O   1 
HETATM 7027 O O   . HOH F 5 .   ? 30.472  21.234  -19.350 1.00 49.89  ? 750 HOH A O   1 
HETATM 7028 O O   . HOH F 5 .   ? 10.794  12.573  -12.576 1.00 49.85  ? 751 HOH A O   1 
HETATM 7029 O O   . HOH F 5 .   ? 20.293  33.115  -4.101  1.00 48.09  ? 752 HOH A O   1 
HETATM 7030 O O   . HOH F 5 .   ? 19.086  26.904  -21.623 1.00 49.65  ? 753 HOH A O   1 
HETATM 7031 O O   . HOH F 5 .   ? 4.310   -6.173  -29.811 1.00 55.82  ? 754 HOH A O   1 
HETATM 7032 O O   . HOH F 5 .   ? 38.605  15.030  -19.721 1.00 53.18  ? 755 HOH A O   1 
HETATM 7033 O O   . HOH F 5 .   ? 1.384   17.641  17.512  1.00 48.11  ? 756 HOH A O   1 
HETATM 7034 O O   . HOH F 5 .   ? 19.418  6.571   -36.828 1.00 47.99  ? 757 HOH A O   1 
HETATM 7035 O O   . HOH F 5 .   ? 19.704  25.031  -24.150 1.00 52.33  ? 758 HOH A O   1 
HETATM 7036 O O   . HOH F 5 .   ? 48.312  0.005   -19.730 1.00 44.33  ? 759 HOH A O   1 
HETATM 7037 O O   . HOH F 5 .   ? 28.757  -11.266 -32.944 1.00 51.47  ? 760 HOH A O   1 
HETATM 7038 O O   . HOH F 5 .   ? 35.836  13.783  7.653   1.00 43.71  ? 761 HOH A O   1 
HETATM 7039 O O   . HOH F 5 .   ? 18.148  22.774  15.828  1.00 50.13  ? 762 HOH A O   1 
HETATM 7040 O O   . HOH F 5 .   ? 7.105   38.687  14.597  1.00 52.78  ? 763 HOH A O   1 
HETATM 7041 O O   . HOH F 5 .   ? 7.258   22.806  17.508  1.00 39.89  ? 764 HOH A O   1 
HETATM 7042 O O   . HOH F 5 .   ? 23.946  22.769  -15.338 1.00 49.73  ? 765 HOH A O   1 
HETATM 7043 O O   . HOH F 5 .   ? 16.179  25.354  -21.030 1.00 41.43  ? 766 HOH A O   1 
HETATM 7044 O O   . HOH F 5 .   ? 12.582  35.860  -1.456  1.00 38.46  ? 767 HOH A O   1 
HETATM 7045 O O   . HOH F 5 .   ? 2.053   -5.428  -29.048 1.00 46.38  ? 768 HOH A O   1 
HETATM 7046 O O   . HOH F 5 .   ? 2.298   -0.905  -14.840 1.00 41.18  ? 769 HOH A O   1 
HETATM 7047 O O   . HOH F 5 .   ? 31.669  -9.819  -31.824 1.00 48.20  ? 770 HOH A O   1 
HETATM 7048 O O   . HOH F 5 .   ? 28.135  19.655  -15.999 1.00 43.33  ? 771 HOH A O   1 
HETATM 7049 O O   . HOH F 5 .   ? 35.781  17.050  -14.024 1.00 41.40  ? 772 HOH A O   1 
HETATM 7050 O O   . HOH F 5 .   ? 9.653   36.374  17.663  1.00 56.28  ? 773 HOH A O   1 
HETATM 7051 O O   . HOH F 5 .   ? 48.507  17.429  -5.323  1.00 48.67  ? 774 HOH A O   1 
HETATM 7052 O O   . HOH F 5 .   ? 5.469   -2.293  -7.021  1.00 36.25  ? 775 HOH A O   1 
HETATM 7053 O O   . HOH F 5 .   ? 38.993  18.377  -16.431 1.00 54.17  ? 776 HOH A O   1 
HETATM 7054 O O   . HOH F 5 .   ? 44.862  -16.148 -22.962 1.00 47.38  ? 777 HOH A O   1 
HETATM 7055 O O   . HOH F 5 .   ? 6.082   12.519  -8.911  1.00 33.81  ? 778 HOH A O   1 
HETATM 7056 O O   . HOH F 5 .   ? 5.744   38.705  16.974  1.00 54.70  ? 779 HOH A O   1 
HETATM 7057 O O   . HOH F 5 .   ? 25.971  -19.023 -9.371  1.00 44.24  ? 780 HOH A O   1 
HETATM 7058 O O   . HOH F 5 .   ? 22.660  29.249  -24.516 1.00 38.48  ? 781 HOH A O   1 
HETATM 7059 O O   . HOH F 5 .   ? 41.788  19.465  -15.332 1.00 47.66  ? 782 HOH A O   1 
HETATM 7060 O O   . HOH F 5 .   ? 11.972  35.956  -4.183  1.00 49.43  ? 783 HOH A O   1 
HETATM 7061 O O   . HOH G 5 .   ? 21.290  -15.669 24.116  1.00 34.85  ? 501 HOH B O   1 
HETATM 7062 O O   . HOH G 5 .   ? 27.946  4.935   16.513  1.00 45.75  ? 502 HOH B O   1 
HETATM 7063 O O   . HOH G 5 .   ? 27.154  4.678   41.443  1.00 40.06  ? 503 HOH B O   1 
HETATM 7064 O O   . HOH G 5 .   ? 20.285  4.003   23.747  1.00 51.48  ? 504 HOH B O   1 
HETATM 7065 O O   . HOH G 5 .   ? 20.236  0.605   21.258  1.00 34.44  ? 505 HOH B O   1 
HETATM 7066 O O   . HOH G 5 .   ? 31.135  -0.595  39.369  1.00 52.71  ? 506 HOH B O   1 
HETATM 7067 O O   . HOH G 5 .   ? 1.100   -6.319  4.906   1.00 26.74  ? 507 HOH B O   1 
HETATM 7068 O O   . HOH G 5 .   ? 1.867   34.596  -5.097  1.00 47.41  ? 508 HOH B O   1 
HETATM 7069 O O   . HOH G 5 .   ? 28.619  37.440  -7.896  1.00 60.43  ? 509 HOH B O   1 
HETATM 7070 O O   . HOH G 5 .   ? 24.786  9.786   39.849  1.00 50.84  ? 510 HOH B O   1 
HETATM 7071 O O   . HOH G 5 .   ? 7.645   17.575  30.715  1.00 41.64  ? 511 HOH B O   1 
HETATM 7072 O O   . HOH G 5 .   ? -2.397  2.421   32.605  1.00 38.69  ? 512 HOH B O   1 
HETATM 7073 O O   . HOH G 5 .   ? 3.912   -1.237  31.814  1.00 31.36  ? 513 HOH B O   1 
HETATM 7074 O O   . HOH G 5 .   ? 30.326  19.474  -12.872 1.00 34.95  ? 514 HOH B O   1 
HETATM 7075 O O   . HOH G 5 .   ? 9.125   -12.363 28.284  1.00 30.33  ? 515 HOH B O   1 
HETATM 7076 O O   . HOH G 5 .   ? 13.628  8.612   20.281  1.00 37.11  ? 516 HOH B O   1 
HETATM 7077 O O   . HOH G 5 .   ? 31.478  19.232  37.269  1.00 50.03  ? 517 HOH B O   1 
HETATM 7078 O O   . HOH G 5 .   ? -2.728  -14.583 28.070  1.00 50.20  ? 518 HOH B O   1 
HETATM 7079 O O   . HOH G 5 .   ? 12.064  6.552   34.218  1.00 47.31  ? 519 HOH B O   1 
HETATM 7080 O O   . HOH G 5 .   ? 26.941  -1.044  9.415   1.00 35.15  ? 520 HOH B O   1 
HETATM 7081 O O   . HOH G 5 .   ? 7.316   9.648   2.745   1.00 18.70  ? 521 HOH B O   1 
HETATM 7082 O O   . HOH G 5 .   ? -5.100  30.566  4.244   1.00 41.11  ? 522 HOH B O   1 
HETATM 7083 O O   . HOH G 5 .   ? -2.785  4.847   -7.977  1.00 37.71  ? 523 HOH B O   1 
HETATM 7084 O O   . HOH G 5 .   ? -6.315  -0.862  32.465  1.00 54.63  ? 524 HOH B O   1 
HETATM 7085 O O   . HOH G 5 .   ? 18.839  -15.807 11.374  1.00 30.73  ? 525 HOH B O   1 
HETATM 7086 O O   . HOH G 5 .   ? 0.215   33.773  9.866   1.00 27.75  ? 526 HOH B O   1 
HETATM 7087 O O   . HOH G 5 .   ? 18.977  12.860  7.318   1.00 22.08  ? 527 HOH B O   1 
HETATM 7088 O O   . HOH G 5 .   ? 23.292  -4.048  8.484   1.00 23.44  ? 528 HOH B O   1 
HETATM 7089 O O   . HOH G 5 .   ? 4.322   -14.864 23.734  1.00 29.57  ? 529 HOH B O   1 
HETATM 7090 O O   . HOH G 5 .   ? 12.230  9.801   13.839  1.00 23.86  ? 530 HOH B O   1 
HETATM 7091 O O   . HOH G 5 .   ? 10.496  15.512  1.610   1.00 24.51  ? 531 HOH B O   1 
HETATM 7092 O O   . HOH G 5 .   ? 7.775   14.445  0.669   1.00 24.43  ? 532 HOH B O   1 
HETATM 7093 O O   . HOH G 5 .   ? 26.384  28.620  6.298   1.00 39.33  ? 533 HOH B O   1 
HETATM 7094 O O   . HOH G 5 .   ? 0.673   3.182   26.448  1.00 27.33  ? 534 HOH B O   1 
HETATM 7095 O O   . HOH G 5 .   ? 15.565  28.608  9.270   1.00 39.97  ? 535 HOH B O   1 
HETATM 7096 O O   . HOH G 5 .   ? 27.076  -3.795  15.464  1.00 37.58  ? 536 HOH B O   1 
HETATM 7097 O O   . HOH G 5 .   ? 21.857  -16.533 11.312  1.00 28.94  ? 537 HOH B O   1 
HETATM 7098 O O   . HOH G 5 .   ? 22.925  -9.189  35.926  1.00 29.74  ? 538 HOH B O   1 
HETATM 7099 O O   . HOH G 5 .   ? 25.908  -11.766 12.760  1.00 33.39  ? 539 HOH B O   1 
HETATM 7100 O O   . HOH G 5 .   ? 20.255  27.336  9.662   1.00 48.36  ? 540 HOH B O   1 
HETATM 7101 O O   . HOH G 5 .   ? 15.395  28.588  13.586  1.00 48.33  ? 541 HOH B O   1 
HETATM 7102 O O   . HOH G 5 .   ? 5.013   5.345   0.661   1.00 20.62  ? 542 HOH B O   1 
HETATM 7103 O O   . HOH G 5 .   ? 14.947  -6.168  37.834  1.00 42.69  ? 543 HOH B O   1 
HETATM 7104 O O   . HOH G 5 .   ? 15.174  12.019  37.960  1.00 52.48  ? 544 HOH B O   1 
HETATM 7105 O O   . HOH G 5 .   ? 26.450  -15.999 16.807  1.00 37.08  ? 545 HOH B O   1 
HETATM 7106 O O   . HOH G 5 .   ? 14.091  19.964  -7.263  1.00 33.17  ? 546 HOH B O   1 
HETATM 7107 O O   . HOH G 5 .   ? 4.175   -3.472  24.597  1.00 29.50  ? 547 HOH B O   1 
HETATM 7108 O O   . HOH G 5 .   ? -5.476  11.303  1.641   1.00 38.94  ? 548 HOH B O   1 
HETATM 7109 O O   . HOH G 5 .   ? -8.084  -2.755  9.808   1.00 29.44  ? 549 HOH B O   1 
HETATM 7110 O O   . HOH G 5 .   ? -0.892  -13.360 11.704  1.00 39.14  ? 550 HOH B O   1 
HETATM 7111 O O   . HOH G 5 .   ? 22.378  -20.028 3.447   1.00 36.09  ? 551 HOH B O   1 
HETATM 7112 O O   . HOH G 5 .   ? -11.045 10.858  15.063  1.00 34.86  ? 552 HOH B O   1 
HETATM 7113 O O   . HOH G 5 .   ? 6.836   -17.031 22.197  1.00 36.64  ? 553 HOH B O   1 
HETATM 7114 O O   . HOH G 5 .   ? -2.215  -4.290  26.245  1.00 38.00  ? 554 HOH B O   1 
HETATM 7115 O O   . HOH G 5 .   ? 1.914   35.693  2.625   1.00 24.62  ? 555 HOH B O   1 
HETATM 7116 O O   . HOH G 5 .   ? 33.608  1.009   37.798  1.00 54.47  ? 556 HOH B O   1 
HETATM 7117 O O   . HOH G 5 .   ? 1.511   13.862  -3.955  1.00 36.38  ? 557 HOH B O   1 
HETATM 7118 O O   . HOH G 5 .   ? 4.665   10.740  -2.844  1.00 21.44  ? 558 HOH B O   1 
HETATM 7119 O O   . HOH G 5 .   ? 22.095  16.560  35.941  1.00 54.99  ? 559 HOH B O   1 
HETATM 7120 O O   . HOH G 5 .   ? 9.476   17.586  13.232  1.00 26.78  ? 560 HOH B O   1 
HETATM 7121 O O   . HOH G 5 .   ? 0.518   -7.641  21.368  1.00 29.34  ? 561 HOH B O   1 
HETATM 7122 O O   . HOH G 5 .   ? 37.566  18.357  26.578  1.00 48.30  ? 562 HOH B O   1 
HETATM 7123 O O   . HOH G 5 .   ? 1.535   10.721  -1.227  1.00 22.27  ? 563 HOH B O   1 
HETATM 7124 O O   . HOH G 5 .   ? -10.803 -1.934  10.196  1.00 43.92  ? 564 HOH B O   1 
HETATM 7125 O O   . HOH G 5 .   ? 26.390  26.480  -12.373 1.00 41.25  ? 565 HOH B O   1 
HETATM 7126 O O   . HOH G 5 .   ? -8.003  -6.055  18.176  1.00 45.31  ? 566 HOH B O   1 
HETATM 7127 O O   . HOH G 5 .   ? -7.697  -1.343  11.901  1.00 28.41  ? 567 HOH B O   1 
HETATM 7128 O O   . HOH G 5 .   ? 47.290  11.885  28.859  1.00 55.31  ? 568 HOH B O   1 
HETATM 7129 O O   . HOH G 5 .   ? 25.088  -1.868  12.240  1.00 47.03  ? 569 HOH B O   1 
HETATM 7130 O O   . HOH G 5 .   ? 25.023  -3.951  33.714  1.00 28.89  ? 570 HOH B O   1 
HETATM 7131 O O   . HOH G 5 .   ? 7.189   9.812   5.673   1.00 19.95  ? 571 HOH B O   1 
HETATM 7132 O O   . HOH G 5 .   ? 11.177  14.584  26.532  1.00 28.62  ? 572 HOH B O   1 
HETATM 7133 O O   . HOH G 5 .   ? 31.959  18.395  3.391   1.00 33.04  ? 573 HOH B O   1 
HETATM 7134 O O   . HOH G 5 .   ? 2.846   -8.585  17.276  1.00 35.07  ? 574 HOH B O   1 
HETATM 7135 O O   . HOH G 5 .   ? 7.303   -8.653  -3.694  1.00 25.49  ? 575 HOH B O   1 
HETATM 7136 O O   . HOH G 5 .   ? 0.200   -1.525  -12.927 1.00 47.53  ? 576 HOH B O   1 
HETATM 7137 O O   . HOH G 5 .   ? 24.059  18.181  1.556   1.00 22.27  ? 577 HOH B O   1 
HETATM 7138 O O   . HOH G 5 .   ? 8.421   8.034   7.394   1.00 19.40  ? 578 HOH B O   1 
HETATM 7139 O O   . HOH G 5 .   ? 2.246   -9.246  19.911  1.00 27.26  ? 579 HOH B O   1 
HETATM 7140 O O   . HOH G 5 .   ? 7.978   16.461  4.248   1.00 19.16  ? 580 HOH B O   1 
HETATM 7141 O O   . HOH G 5 .   ? 31.816  3.194   16.328  1.00 51.61  ? 581 HOH B O   1 
HETATM 7142 O O   . HOH G 5 .   ? -3.278  17.155  1.980   1.00 32.74  ? 582 HOH B O   1 
HETATM 7143 O O   . HOH G 5 .   ? 13.511  -20.514 25.490  1.00 39.04  ? 583 HOH B O   1 
HETATM 7144 O O   . HOH G 5 .   ? -3.144  -16.748 21.767  1.00 38.07  ? 584 HOH B O   1 
HETATM 7145 O O   . HOH G 5 .   ? 18.639  30.855  7.198   1.00 39.34  ? 585 HOH B O   1 
HETATM 7146 O O   . HOH G 5 .   ? 14.497  -19.023 15.274  1.00 29.87  ? 586 HOH B O   1 
HETATM 7147 O O   . HOH G 5 .   ? 24.016  -19.495 18.984  1.00 42.37  ? 587 HOH B O   1 
HETATM 7148 O O   . HOH G 5 .   ? -11.752 7.792   -1.382  1.00 38.90  ? 588 HOH B O   1 
HETATM 7149 O O   . HOH G 5 .   ? 16.474  -11.834 32.319  1.00 38.72  ? 589 HOH B O   1 
HETATM 7150 O O   . HOH G 5 .   ? 20.878  10.609  12.024  1.00 26.86  ? 590 HOH B O   1 
HETATM 7151 O O   . HOH G 5 .   ? 6.440   -0.747  -3.130  1.00 28.98  ? 591 HOH B O   1 
HETATM 7152 O O   . HOH G 5 .   ? 3.983   -14.948 28.816  1.00 43.63  ? 592 HOH B O   1 
HETATM 7153 O O   . HOH G 5 .   ? -3.954  9.077   0.914   1.00 25.26  ? 593 HOH B O   1 
HETATM 7154 O O   . HOH G 5 .   ? 9.947   -17.409 26.716  1.00 48.68  ? 594 HOH B O   1 
HETATM 7155 O O   . HOH G 5 .   ? -4.820  13.406  24.641  1.00 31.30  ? 595 HOH B O   1 
HETATM 7156 O O   . HOH G 5 .   ? 9.015   -22.245 17.975  1.00 52.18  ? 596 HOH B O   1 
HETATM 7157 O O   . HOH G 5 .   ? 29.621  -16.209 4.729   1.00 38.81  ? 597 HOH B O   1 
HETATM 7158 O O   . HOH G 5 .   ? 13.163  11.902  31.754  1.00 47.62  ? 598 HOH B O   1 
HETATM 7159 O O   . HOH G 5 .   ? 6.040   17.265  19.185  1.00 25.65  ? 599 HOH B O   1 
HETATM 7160 O O   . HOH G 5 .   ? 12.935  -17.616 0.865   1.00 36.67  ? 600 HOH B O   1 
HETATM 7161 O O   . HOH G 5 .   ? 9.333   35.827  2.678   1.00 33.28  ? 601 HOH B O   1 
HETATM 7162 O O   . HOH G 5 .   ? 26.705  11.240  14.186  1.00 40.40  ? 602 HOH B O   1 
HETATM 7163 O O   . HOH G 5 .   ? 15.213  13.944  23.563  1.00 41.79  ? 603 HOH B O   1 
HETATM 7164 O O   . HOH G 5 .   ? 42.069  5.029   24.236  1.00 48.22  ? 604 HOH B O   1 
HETATM 7165 O O   . HOH G 5 .   ? -0.578  -14.166 14.382  1.00 49.25  ? 605 HOH B O   1 
HETATM 7166 O O   . HOH G 5 .   ? 4.081   0.503   -4.186  1.00 28.08  ? 606 HOH B O   1 
HETATM 7167 O O   . HOH G 5 .   ? -7.963  8.825   20.243  1.00 32.13  ? 607 HOH B O   1 
HETATM 7168 O O   . HOH G 5 .   ? 17.123  25.062  11.657  1.00 45.75  ? 608 HOH B O   1 
HETATM 7169 O O   . HOH G 5 .   ? 16.603  26.761  7.159   1.00 44.75  ? 609 HOH B O   1 
HETATM 7170 O O   . HOH G 5 .   ? 33.937  25.673  -12.239 1.00 38.64  ? 610 HOH B O   1 
HETATM 7171 O O   . HOH G 5 .   ? 27.964  -2.800  18.022  1.00 47.74  ? 611 HOH B O   1 
HETATM 7172 O O   . HOH G 5 .   ? -0.898  20.739  1.221   1.00 41.68  ? 612 HOH B O   1 
HETATM 7173 O O   . HOH G 5 .   ? 25.813  -3.845  46.270  1.00 47.07  ? 613 HOH B O   1 
HETATM 7174 O O   . HOH G 5 .   ? 9.665   -21.409 2.669   1.00 31.92  ? 614 HOH B O   1 
HETATM 7175 O O   . HOH G 5 .   ? 10.263  -21.648 22.155  1.00 43.96  ? 615 HOH B O   1 
HETATM 7176 O O   . HOH G 5 .   ? -17.223 5.337   16.718  1.00 48.31  ? 616 HOH B O   1 
HETATM 7177 O O   . HOH G 5 .   ? 38.007  24.066  18.009  1.00 48.88  ? 617 HOH B O   1 
HETATM 7178 O O   . HOH G 5 .   ? -0.324  -9.612  5.992   1.00 44.69  ? 618 HOH B O   1 
HETATM 7179 O O   . HOH G 5 .   ? 27.208  16.983  2.235   1.00 26.26  ? 619 HOH B O   1 
HETATM 7180 O O   . HOH G 5 .   ? -4.990  -13.960 13.063  1.00 43.12  ? 620 HOH B O   1 
HETATM 7181 O O   . HOH G 5 .   ? 19.135  -13.423 31.578  1.00 71.13  ? 621 HOH B O   1 
HETATM 7182 O O   . HOH G 5 .   ? 36.311  1.782   24.328  1.00 40.54  ? 622 HOH B O   1 
HETATM 7183 O O   . HOH G 5 .   ? 3.747   -7.900  32.441  1.00 46.03  ? 623 HOH B O   1 
HETATM 7184 O O   . HOH G 5 .   ? 5.212   13.509  -6.480  1.00 26.24  ? 624 HOH B O   1 
HETATM 7185 O O   . HOH G 5 .   ? 6.861   -5.056  -4.961  1.00 35.97  ? 625 HOH B O   1 
HETATM 7186 O O   . HOH G 5 .   ? 3.509   -0.795  -6.277  1.00 33.24  ? 626 HOH B O   1 
HETATM 7187 O O   . HOH G 5 .   ? -10.545 13.964  18.050  1.00 42.25  ? 627 HOH B O   1 
HETATM 7188 O O   . HOH G 5 .   ? 5.217   -16.736 12.517  1.00 44.85  ? 628 HOH B O   1 
HETATM 7189 O O   . HOH G 5 .   ? 3.795   -15.702 1.112   1.00 44.01  ? 629 HOH B O   1 
HETATM 7190 O O   . HOH G 5 .   ? 17.079  -18.907 1.978   1.00 29.41  ? 630 HOH B O   1 
HETATM 7191 O O   . HOH G 5 .   ? 31.225  21.022  24.965  1.00 53.40  ? 631 HOH B O   1 
HETATM 7192 O O   . HOH G 5 .   ? -11.875 13.365  14.235  1.00 53.04  ? 632 HOH B O   1 
HETATM 7193 O O   . HOH G 5 .   ? 15.289  -23.745 2.722   1.00 45.75  ? 633 HOH B O   1 
HETATM 7194 O O   . HOH G 5 .   ? 7.195   -2.881  37.741  1.00 45.38  ? 634 HOH B O   1 
HETATM 7195 O O   . HOH G 5 .   ? -0.539  -0.554  37.068  1.00 56.28  ? 635 HOH B O   1 
HETATM 7196 O O   . HOH G 5 .   ? 6.631   36.029  0.366   1.00 43.12  ? 636 HOH B O   1 
HETATM 7197 O O   . HOH G 5 .   ? -0.050  16.572  -8.366  1.00 49.43  ? 637 HOH B O   1 
HETATM 7198 O O   . HOH G 5 .   ? -2.556  -14.306 18.038  1.00 50.90  ? 638 HOH B O   1 
HETATM 7199 O O   . HOH G 5 .   ? -10.839 15.289  15.804  1.00 59.87  ? 639 HOH B O   1 
HETATM 7200 O O   . HOH G 5 .   ? -1.137  16.571  -3.094  1.00 47.28  ? 640 HOH B O   1 
HETATM 7201 O O   . HOH G 5 .   ? -17.834 3.060   16.970  1.00 52.91  ? 641 HOH B O   1 
HETATM 7202 O O   . HOH G 5 .   ? -7.561  25.381  8.842   1.00 55.75  ? 642 HOH B O   1 
HETATM 7203 O O   . HOH G 5 .   ? -2.152  17.441  -1.144  1.00 54.65  ? 643 HOH B O   1 
HETATM 7204 O O   . HOH G 5 .   ? 7.522   -17.506 26.876  1.00 47.20  ? 644 HOH B O   1 
HETATM 7205 O O   . HOH G 5 .   ? 20.272  -14.190 30.006  1.00 64.82  ? 645 HOH B O   1 
HETATM 7206 O O   . HOH G 5 .   ? 10.456  23.130  18.691  1.00 56.23  ? 646 HOH B O   1 
HETATM 7207 O O   . HOH G 5 .   ? 4.267   22.280  27.243  1.00 55.73  ? 647 HOH B O   1 
HETATM 7208 O O   . HOH G 5 .   ? 2.918   11.663  -4.750  1.00 33.24  ? 648 HOH B O   1 
HETATM 7209 O O   . HOH G 5 .   ? 22.487  22.477  -12.875 1.00 36.31  ? 649 HOH B O   1 
HETATM 7210 O O   . HOH G 5 .   ? -8.071  11.763  1.495   1.00 46.81  ? 650 HOH B O   1 
HETATM 7211 O O   . HOH G 5 .   ? 32.628  25.335  -18.277 1.00 54.06  ? 651 HOH B O   1 
HETATM 7212 O O   . HOH G 5 .   ? -9.842  12.019  22.106  1.00 48.59  ? 652 HOH B O   1 
HETATM 7213 O O   . HOH G 5 .   ? 34.595  7.218   37.728  1.00 53.72  ? 653 HOH B O   1 
HETATM 7214 O O   . HOH G 5 .   ? 21.612  30.875  6.284   1.00 46.66  ? 654 HOH B O   1 
HETATM 7215 O O   . HOH G 5 .   ? 12.068  22.652  16.578  1.00 39.41  ? 655 HOH B O   1 
HETATM 7216 O O   . HOH G 5 .   ? 2.638   18.926  -2.955  1.00 42.64  ? 656 HOH B O   1 
HETATM 7217 O O   . HOH G 5 .   ? 6.024   19.858  19.679  1.00 37.15  ? 657 HOH B O   1 
HETATM 7218 O O   . HOH G 5 .   ? 34.394  3.243   20.292  1.00 51.05  ? 658 HOH B O   1 
HETATM 7219 O O   . HOH G 5 .   ? 6.385   -11.771 33.802  1.00 46.60  ? 659 HOH B O   1 
HETATM 7220 O O   . HOH G 5 .   ? -4.798  25.740  13.114  1.00 51.43  ? 660 HOH B O   1 
HETATM 7221 O O   . HOH G 5 .   ? 25.863  -3.955  49.171  1.00 44.20  ? 661 HOH B O   1 
HETATM 7222 O O   . HOH G 5 .   ? 27.937  -9.762  31.730  1.00 54.86  ? 662 HOH B O   1 
HETATM 7223 O O   . HOH G 5 .   ? 5.515   -15.548 15.083  1.00 60.01  ? 663 HOH B O   1 
HETATM 7224 O O   . HOH G 5 .   ? 22.960  -9.482  38.341  1.00 39.39  ? 664 HOH B O   1 
HETATM 7225 O O   . HOH G 5 .   ? -4.822  -15.036 15.206  1.00 55.33  ? 665 HOH B O   1 
HETATM 7226 O O   . HOH G 5 .   ? 33.639  0.852   19.891  1.00 55.83  ? 666 HOH B O   1 
HETATM 7227 O O   . HOH G 5 .   ? -9.756  10.102  20.309  1.00 50.18  ? 667 HOH B O   1 
HETATM 7228 O O   . HOH G 5 .   ? -2.989  4.957   -11.523 1.00 57.36  ? 668 HOH B O   1 
HETATM 7229 O O   . HOH G 5 .   ? 17.762  29.942  9.978   1.00 49.90  ? 669 HOH B O   1 
HETATM 7230 O O   . HOH G 5 .   ? 11.307  7.772   41.808  1.00 52.55  ? 670 HOH B O   1 
HETATM 7231 O O   . HOH G 5 .   ? -6.392  25.716  11.116  1.00 52.57  ? 671 HOH B O   1 
HETATM 7232 O O   . HOH G 5 .   ? 26.394  15.959  13.237  1.00 39.17  ? 672 HOH B O   1 
HETATM 7233 O O   . HOH G 5 .   ? -5.245  12.170  28.843  1.00 55.56  ? 673 HOH B O   1 
HETATM 7234 O O   . HOH G 5 .   ? -6.071  -16.792 13.230  1.00 48.35  ? 674 HOH B O   1 
# 
