data_8RZF
# 
_entry.id   8RZF 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   8RZF         pdb_00008rzf 10.2210/pdb8rzf/pdb 
WWPDB D_1292136549 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2024-11-06 
2 'Structure model' 1 1 2024-12-04 
# 
_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_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            citation 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume' 
2 2 'Structure model' '_citation.page_first'     
3 2 'Structure model' '_citation.page_last'      
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8RZF 
_pdbx_database_status.recvd_initial_deposition_date   2024-02-12 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_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                 3 
_pdbx_contact_author.email              nicolas.leulliot@u-paris.fr 
_pdbx_contact_author.name_first         NICOLAS 
_pdbx_contact_author.name_last          LEULLIOT 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0283-4298 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Vayssieres, M.' 1 0000-0001-6721-2575 
'Blaud, M.'      2 0000-0001-8425-9754 
'Leulliot, N.'   3 0000-0003-0283-4298 
# 
_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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Nucleic Acids Res.' 
_citation.journal_id_ASTM           NARHAD 
_citation.journal_id_CSD            0389 
_citation.journal_id_ISSN           1362-4962 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            52 
_citation.language                  ? 
_citation.page_first                13386 
_citation.page_last                 13401 
_citation.title                     'RNase W, a conserved ribonuclease family with a novel active site.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1093/nar/gkae907 
_citation.pdbx_database_id_PubMed   39445822 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Vayssieres, M.'     1 0000-0002-1382-1794 
primary 'Juttner, M.'        2 ?                   
primary 'Haas, K.'           3 ?                   
primary 'Ancelin, A.'        4 ?                   
primary 'Marchfelder, A.'    5 ?                   
primary 'Leulliot, N.'       6 ?                   
primary 'Ferreira-Cerca, S.' 7 0000-0002-0522-843X 
primary 'Blaud, M.'          8 0000-0001-8425-9754 
# 
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 'Probable ribonuclease FAU-1' 48512.684 1   3.1.26.- ? ? ? 
2 non-polymer syn 'MAGNESIUM ION'               24.305    2   ?        ? ? ? 
3 water       nat water                         18.015    247 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'RNA-binding protein FAU-1' 
# 
_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       
;MRVRIRGIYATALTYLFLKNGFEIVQQTPQIAERFFMDIIRSPADVTVKDGIDKGEIVSVGEDIYNFMRSIFKYSPIWRS
PIKLYSVVSTEDCKFMNFIVEPCLSEGLVIKPPVEGKIILSSPRAVGKFAMVWKGDGRTFFSEHIDERDSQRLLSVSIPF
NKKGYNVKWRSNAAMATTAELKEELENLTMRYSYNDFREQGEDFLKVTLSLEDKLFLDDIRSLVINTMKFHHMLKMTYSN
EVDIEEGKVNPSPEKLLTSLIGDNMIEAIEHVKPNGKRVLLKGGTIVQKEIGRDYYWLKIRREFKSGGIYDGLNLKIEDG
DYDLVELDSRNWYQIHRYHDRNNNLKGLYVNISTPPELLKNRIRYLDLEVDVVKVNNTVNIIDLEELEANKPILGEFLYK
KALEIAQNIKDKLNEDKI
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MRVRIRGIYATALTYLFLKNGFEIVQQTPQIAERFFMDIIRSPADVTVKDGIDKGEIVSVGEDIYNFMRSIFKYSPIWRS
PIKLYSVVSTEDCKFMNFIVEPCLSEGLVIKPPVEGKIILSSPRAVGKFAMVWKGDGRTFFSEHIDERDSQRLLSVSIPF
NKKGYNVKWRSNAAMATTAELKEELENLTMRYSYNDFREQGEDFLKVTLSLEDKLFLDDIRSLVINTMKFHHMLKMTYSN
EVDIEEGKVNPSPEKLLTSLIGDNMIEAIEHVKPNGKRVLLKGGTIVQKEIGRDYYWLKIRREFKSGGIYDGLNLKIEDG
DYDLVELDSRNWYQIHRYHDRNNNLKGLYVNISTPPELLKNRIRYLDLEVDVVKVNNTVNIIDLEELEANKPILGEFLYK
KALEIAQNIKDKLNEDKI
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'MAGNESIUM ION' MG  
3 water           HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ARG n 
1 3   VAL n 
1 4   ARG n 
1 5   ILE n 
1 6   ARG n 
1 7   GLY n 
1 8   ILE n 
1 9   TYR n 
1 10  ALA n 
1 11  THR n 
1 12  ALA n 
1 13  LEU n 
1 14  THR n 
1 15  TYR n 
1 16  LEU n 
1 17  PHE n 
1 18  LEU n 
1 19  LYS n 
1 20  ASN n 
1 21  GLY n 
1 22  PHE n 
1 23  GLU n 
1 24  ILE n 
1 25  VAL n 
1 26  GLN n 
1 27  GLN n 
1 28  THR n 
1 29  PRO n 
1 30  GLN n 
1 31  ILE n 
1 32  ALA n 
1 33  GLU n 
1 34  ARG n 
1 35  PHE n 
1 36  PHE n 
1 37  MET n 
1 38  ASP n 
1 39  ILE n 
1 40  ILE n 
1 41  ARG n 
1 42  SER n 
1 43  PRO n 
1 44  ALA n 
1 45  ASP n 
1 46  VAL n 
1 47  THR n 
1 48  VAL n 
1 49  LYS n 
1 50  ASP n 
1 51  GLY n 
1 52  ILE n 
1 53  ASP n 
1 54  LYS n 
1 55  GLY n 
1 56  GLU n 
1 57  ILE n 
1 58  VAL n 
1 59  SER n 
1 60  VAL n 
1 61  GLY n 
1 62  GLU n 
1 63  ASP n 
1 64  ILE n 
1 65  TYR n 
1 66  ASN n 
1 67  PHE n 
1 68  MET n 
1 69  ARG n 
1 70  SER n 
1 71  ILE n 
1 72  PHE n 
1 73  LYS n 
1 74  TYR n 
1 75  SER n 
1 76  PRO n 
1 77  ILE n 
1 78  TRP n 
1 79  ARG n 
1 80  SER n 
1 81  PRO n 
1 82  ILE n 
1 83  LYS n 
1 84  LEU n 
1 85  TYR n 
1 86  SER n 
1 87  VAL n 
1 88  VAL n 
1 89  SER n 
1 90  THR n 
1 91  GLU n 
1 92  ASP n 
1 93  CYS n 
1 94  LYS n 
1 95  PHE n 
1 96  MET n 
1 97  ASN n 
1 98  PHE n 
1 99  ILE n 
1 100 VAL n 
1 101 GLU n 
1 102 PRO n 
1 103 CYS n 
1 104 LEU n 
1 105 SER n 
1 106 GLU n 
1 107 GLY n 
1 108 LEU n 
1 109 VAL n 
1 110 ILE n 
1 111 LYS n 
1 112 PRO n 
1 113 PRO n 
1 114 VAL n 
1 115 GLU n 
1 116 GLY n 
1 117 LYS n 
1 118 ILE n 
1 119 ILE n 
1 120 LEU n 
1 121 SER n 
1 122 SER n 
1 123 PRO n 
1 124 ARG n 
1 125 ALA n 
1 126 VAL n 
1 127 GLY n 
1 128 LYS n 
1 129 PHE n 
1 130 ALA n 
1 131 MET n 
1 132 VAL n 
1 133 TRP n 
1 134 LYS n 
1 135 GLY n 
1 136 ASP n 
1 137 GLY n 
1 138 ARG n 
1 139 THR n 
1 140 PHE n 
1 141 PHE n 
1 142 SER n 
1 143 GLU n 
1 144 HIS n 
1 145 ILE n 
1 146 ASP n 
1 147 GLU n 
1 148 ARG n 
1 149 ASP n 
1 150 SER n 
1 151 GLN n 
1 152 ARG n 
1 153 LEU n 
1 154 LEU n 
1 155 SER n 
1 156 VAL n 
1 157 SER n 
1 158 ILE n 
1 159 PRO n 
1 160 PHE n 
1 161 ASN n 
1 162 LYS n 
1 163 LYS n 
1 164 GLY n 
1 165 TYR n 
1 166 ASN n 
1 167 VAL n 
1 168 LYS n 
1 169 TRP n 
1 170 ARG n 
1 171 SER n 
1 172 ASN n 
1 173 ALA n 
1 174 ALA n 
1 175 MET n 
1 176 ALA n 
1 177 THR n 
1 178 THR n 
1 179 ALA n 
1 180 GLU n 
1 181 LEU n 
1 182 LYS n 
1 183 GLU n 
1 184 GLU n 
1 185 LEU n 
1 186 GLU n 
1 187 ASN n 
1 188 LEU n 
1 189 THR n 
1 190 MET n 
1 191 ARG n 
1 192 TYR n 
1 193 SER n 
1 194 TYR n 
1 195 ASN n 
1 196 ASP n 
1 197 PHE n 
1 198 ARG n 
1 199 GLU n 
1 200 GLN n 
1 201 GLY n 
1 202 GLU n 
1 203 ASP n 
1 204 PHE n 
1 205 LEU n 
1 206 LYS n 
1 207 VAL n 
1 208 THR n 
1 209 LEU n 
1 210 SER n 
1 211 LEU n 
1 212 GLU n 
1 213 ASP n 
1 214 LYS n 
1 215 LEU n 
1 216 PHE n 
1 217 LEU n 
1 218 ASP n 
1 219 ASP n 
1 220 ILE n 
1 221 ARG n 
1 222 SER n 
1 223 LEU n 
1 224 VAL n 
1 225 ILE n 
1 226 ASN n 
1 227 THR n 
1 228 MET n 
1 229 LYS n 
1 230 PHE n 
1 231 HIS n 
1 232 HIS n 
1 233 MET n 
1 234 LEU n 
1 235 LYS n 
1 236 MET n 
1 237 THR n 
1 238 TYR n 
1 239 SER n 
1 240 ASN n 
1 241 GLU n 
1 242 VAL n 
1 243 ASP n 
1 244 ILE n 
1 245 GLU n 
1 246 GLU n 
1 247 GLY n 
1 248 LYS n 
1 249 VAL n 
1 250 ASN n 
1 251 PRO n 
1 252 SER n 
1 253 PRO n 
1 254 GLU n 
1 255 LYS n 
1 256 LEU n 
1 257 LEU n 
1 258 THR n 
1 259 SER n 
1 260 LEU n 
1 261 ILE n 
1 262 GLY n 
1 263 ASP n 
1 264 ASN n 
1 265 MET n 
1 266 ILE n 
1 267 GLU n 
1 268 ALA n 
1 269 ILE n 
1 270 GLU n 
1 271 HIS n 
1 272 VAL n 
1 273 LYS n 
1 274 PRO n 
1 275 ASN n 
1 276 GLY n 
1 277 LYS n 
1 278 ARG n 
1 279 VAL n 
1 280 LEU n 
1 281 LEU n 
1 282 LYS n 
1 283 GLY n 
1 284 GLY n 
1 285 THR n 
1 286 ILE n 
1 287 VAL n 
1 288 GLN n 
1 289 LYS n 
1 290 GLU n 
1 291 ILE n 
1 292 GLY n 
1 293 ARG n 
1 294 ASP n 
1 295 TYR n 
1 296 TYR n 
1 297 TRP n 
1 298 LEU n 
1 299 LYS n 
1 300 ILE n 
1 301 ARG n 
1 302 ARG n 
1 303 GLU n 
1 304 PHE n 
1 305 LYS n 
1 306 SER n 
1 307 GLY n 
1 308 GLY n 
1 309 ILE n 
1 310 TYR n 
1 311 ASP n 
1 312 GLY n 
1 313 LEU n 
1 314 ASN n 
1 315 LEU n 
1 316 LYS n 
1 317 ILE n 
1 318 GLU n 
1 319 ASP n 
1 320 GLY n 
1 321 ASP n 
1 322 TYR n 
1 323 ASP n 
1 324 LEU n 
1 325 VAL n 
1 326 GLU n 
1 327 LEU n 
1 328 ASP n 
1 329 SER n 
1 330 ARG n 
1 331 ASN n 
1 332 TRP n 
1 333 TYR n 
1 334 GLN n 
1 335 ILE n 
1 336 HIS n 
1 337 ARG n 
1 338 TYR n 
1 339 HIS n 
1 340 ASP n 
1 341 ARG n 
1 342 ASN n 
1 343 ASN n 
1 344 ASN n 
1 345 LEU n 
1 346 LYS n 
1 347 GLY n 
1 348 LEU n 
1 349 TYR n 
1 350 VAL n 
1 351 ASN n 
1 352 ILE n 
1 353 SER n 
1 354 THR n 
1 355 PRO n 
1 356 PRO n 
1 357 GLU n 
1 358 LEU n 
1 359 LEU n 
1 360 LYS n 
1 361 ASN n 
1 362 ARG n 
1 363 ILE n 
1 364 ARG n 
1 365 TYR n 
1 366 LEU n 
1 367 ASP n 
1 368 LEU n 
1 369 GLU n 
1 370 VAL n 
1 371 ASP n 
1 372 VAL n 
1 373 VAL n 
1 374 LYS n 
1 375 VAL n 
1 376 ASN n 
1 377 ASN n 
1 378 THR n 
1 379 VAL n 
1 380 ASN n 
1 381 ILE n 
1 382 ILE n 
1 383 ASP n 
1 384 LEU n 
1 385 GLU n 
1 386 GLU n 
1 387 LEU n 
1 388 GLU n 
1 389 ALA n 
1 390 ASN n 
1 391 LYS n 
1 392 PRO n 
1 393 ILE n 
1 394 LEU n 
1 395 GLY n 
1 396 GLU n 
1 397 PHE n 
1 398 LEU n 
1 399 TYR n 
1 400 LYS n 
1 401 LYS n 
1 402 ALA n 
1 403 LEU n 
1 404 GLU n 
1 405 ILE n 
1 406 ALA n 
1 407 GLN n 
1 408 ASN n 
1 409 ILE n 
1 410 LYS n 
1 411 ASP n 
1 412 LYS n 
1 413 LEU n 
1 414 ASN n 
1 415 GLU n 
1 416 ASP n 
1 417 LYS n 
1 418 ILE 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                   418 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'fau-1, Saci_1213' 
_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      'Sulfolobus acidocaldarius' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2285 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
MG  non-polymer         . 'MAGNESIUM ION' ? 'Mg 2'           24.305  
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   MET 1   1   1   MET MET A . n 
A 1 2   ARG 2   2   2   ARG ARG A . n 
A 1 3   VAL 3   3   3   VAL VAL A . n 
A 1 4   ARG 4   4   4   ARG ARG A . n 
A 1 5   ILE 5   5   5   ILE ILE A . n 
A 1 6   ARG 6   6   6   ARG ARG A . n 
A 1 7   GLY 7   7   7   GLY GLY A . n 
A 1 8   ILE 8   8   8   ILE ILE A . n 
A 1 9   TYR 9   9   9   TYR TYR A . n 
A 1 10  ALA 10  10  10  ALA ALA A . n 
A 1 11  THR 11  11  11  THR THR A . n 
A 1 12  ALA 12  12  12  ALA ALA A . n 
A 1 13  LEU 13  13  13  LEU LEU A . n 
A 1 14  THR 14  14  14  THR THR A . n 
A 1 15  TYR 15  15  15  TYR TYR A . n 
A 1 16  LEU 16  16  16  LEU LEU A . n 
A 1 17  PHE 17  17  17  PHE PHE A . n 
A 1 18  LEU 18  18  18  LEU LEU A . n 
A 1 19  LYS 19  19  19  LYS LYS A . n 
A 1 20  ASN 20  20  20  ASN ASN A . n 
A 1 21  GLY 21  21  21  GLY GLY A . n 
A 1 22  PHE 22  22  22  PHE PHE A . n 
A 1 23  GLU 23  23  23  GLU GLU A . n 
A 1 24  ILE 24  24  24  ILE ILE A . n 
A 1 25  VAL 25  25  25  VAL VAL A . n 
A 1 26  GLN 26  26  26  GLN GLN A . n 
A 1 27  GLN 27  27  27  GLN GLN A . n 
A 1 28  THR 28  28  28  THR THR A . n 
A 1 29  PRO 29  29  29  PRO PRO A . n 
A 1 30  GLN 30  30  30  GLN GLN A . n 
A 1 31  ILE 31  31  31  ILE ILE A . n 
A 1 32  ALA 32  32  32  ALA ALA A . n 
A 1 33  GLU 33  33  33  GLU GLU A . n 
A 1 34  ARG 34  34  34  ARG ARG A . n 
A 1 35  PHE 35  35  35  PHE PHE A . n 
A 1 36  PHE 36  36  36  PHE PHE A . n 
A 1 37  MET 37  37  37  MET MET A . n 
A 1 38  ASP 38  38  38  ASP ASP A . n 
A 1 39  ILE 39  39  39  ILE ILE A . n 
A 1 40  ILE 40  40  40  ILE ILE A . n 
A 1 41  ARG 41  41  41  ARG ARG A . n 
A 1 42  SER 42  42  42  SER SER A . n 
A 1 43  PRO 43  43  43  PRO PRO A . n 
A 1 44  ALA 44  44  44  ALA ALA A . n 
A 1 45  ASP 45  45  45  ASP ASP A . n 
A 1 46  VAL 46  46  46  VAL VAL A . n 
A 1 47  THR 47  47  47  THR THR A . n 
A 1 48  VAL 48  48  48  VAL VAL A . n 
A 1 49  LYS 49  49  49  LYS LYS A . n 
A 1 50  ASP 50  50  50  ASP ASP A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  ILE 52  52  52  ILE ILE A . n 
A 1 53  ASP 53  53  53  ASP ASP A . n 
A 1 54  LYS 54  54  54  LYS LYS A . n 
A 1 55  GLY 55  55  55  GLY GLY A . n 
A 1 56  GLU 56  56  56  GLU GLU A . n 
A 1 57  ILE 57  57  57  ILE ILE A . n 
A 1 58  VAL 58  58  58  VAL VAL A . n 
A 1 59  SER 59  59  59  SER SER A . n 
A 1 60  VAL 60  60  60  VAL VAL A . n 
A 1 61  GLY 61  61  61  GLY GLY A . n 
A 1 62  GLU 62  62  62  GLU GLU A . n 
A 1 63  ASP 63  63  63  ASP ASP A . n 
A 1 64  ILE 64  64  64  ILE ILE A . n 
A 1 65  TYR 65  65  65  TYR TYR A . n 
A 1 66  ASN 66  66  66  ASN ASN A . n 
A 1 67  PHE 67  67  67  PHE PHE A . n 
A 1 68  MET 68  68  68  MET MET A . n 
A 1 69  ARG 69  69  69  ARG ARG A . n 
A 1 70  SER 70  70  70  SER SER A . n 
A 1 71  ILE 71  71  71  ILE ILE A . n 
A 1 72  PHE 72  72  72  PHE PHE A . n 
A 1 73  LYS 73  73  73  LYS LYS A . n 
A 1 74  TYR 74  74  74  TYR TYR A . n 
A 1 75  SER 75  75  75  SER SER A . n 
A 1 76  PRO 76  76  76  PRO PRO A . n 
A 1 77  ILE 77  77  77  ILE ILE A . n 
A 1 78  TRP 78  78  78  TRP TRP A . n 
A 1 79  ARG 79  79  79  ARG ARG A . n 
A 1 80  SER 80  80  80  SER SER A . n 
A 1 81  PRO 81  81  81  PRO PRO A . n 
A 1 82  ILE 82  82  82  ILE ILE A . n 
A 1 83  LYS 83  83  83  LYS LYS A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  TYR 85  85  85  TYR TYR A . n 
A 1 86  SER 86  86  86  SER SER A . n 
A 1 87  VAL 87  87  87  VAL VAL A . n 
A 1 88  VAL 88  88  88  VAL VAL A . n 
A 1 89  SER 89  89  89  SER SER A . n 
A 1 90  THR 90  90  90  THR THR A . n 
A 1 91  GLU 91  91  91  GLU GLU A . n 
A 1 92  ASP 92  92  92  ASP ASP A . n 
A 1 93  CYS 93  93  93  CYS CYS A . n 
A 1 94  LYS 94  94  94  LYS LYS A . n 
A 1 95  PHE 95  95  95  PHE PHE A . n 
A 1 96  MET 96  96  96  MET MET A . n 
A 1 97  ASN 97  97  97  ASN ASN A . n 
A 1 98  PHE 98  98  98  PHE PHE A . n 
A 1 99  ILE 99  99  99  ILE ILE A . n 
A 1 100 VAL 100 100 100 VAL VAL A . n 
A 1 101 GLU 101 101 101 GLU GLU A . n 
A 1 102 PRO 102 102 102 PRO PRO A . n 
A 1 103 CYS 103 103 103 CYS CYS A . n 
A 1 104 LEU 104 104 104 LEU LEU A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 GLU 106 106 106 GLU GLU A . n 
A 1 107 GLY 107 107 107 GLY GLY A . n 
A 1 108 LEU 108 108 108 LEU LEU A . n 
A 1 109 VAL 109 109 109 VAL VAL A . n 
A 1 110 ILE 110 110 110 ILE ILE A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 PRO 112 112 112 PRO PRO A . n 
A 1 113 PRO 113 113 113 PRO PRO A . n 
A 1 114 VAL 114 114 114 VAL VAL A . n 
A 1 115 GLU 115 115 115 GLU GLU A . n 
A 1 116 GLY 116 116 116 GLY GLY A . n 
A 1 117 LYS 117 117 117 LYS LYS A . n 
A 1 118 ILE 118 118 118 ILE ILE A . n 
A 1 119 ILE 119 119 119 ILE ILE A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 SER 121 121 121 SER SER A . n 
A 1 122 SER 122 122 122 SER SER A . n 
A 1 123 PRO 123 123 123 PRO PRO A . n 
A 1 124 ARG 124 124 124 ARG ARG A . n 
A 1 125 ALA 125 125 125 ALA ALA A . n 
A 1 126 VAL 126 126 126 VAL VAL A . n 
A 1 127 GLY 127 127 127 GLY GLY A . n 
A 1 128 LYS 128 128 128 LYS LYS A . n 
A 1 129 PHE 129 129 129 PHE PHE A . n 
A 1 130 ALA 130 130 130 ALA ALA A . n 
A 1 131 MET 131 131 131 MET MET A . n 
A 1 132 VAL 132 132 132 VAL VAL A . n 
A 1 133 TRP 133 133 133 TRP TRP A . n 
A 1 134 LYS 134 134 134 LYS LYS A . n 
A 1 135 GLY 135 135 135 GLY GLY A . n 
A 1 136 ASP 136 136 136 ASP ASP A . n 
A 1 137 GLY 137 137 137 GLY GLY A . n 
A 1 138 ARG 138 138 138 ARG ARG A . n 
A 1 139 THR 139 139 139 THR THR A . n 
A 1 140 PHE 140 140 140 PHE PHE A . n 
A 1 141 PHE 141 141 141 PHE PHE A . n 
A 1 142 SER 142 142 142 SER SER A . n 
A 1 143 GLU 143 143 143 GLU GLU A . n 
A 1 144 HIS 144 144 144 HIS HIS A . n 
A 1 145 ILE 145 145 145 ILE ILE A . n 
A 1 146 ASP 146 146 146 ASP ASP A . n 
A 1 147 GLU 147 147 147 GLU GLU A . n 
A 1 148 ARG 148 148 148 ARG ARG A . n 
A 1 149 ASP 149 149 149 ASP ASP A . n 
A 1 150 SER 150 150 150 SER SER A . n 
A 1 151 GLN 151 151 151 GLN GLN A . n 
A 1 152 ARG 152 152 152 ARG ARG A . n 
A 1 153 LEU 153 153 153 LEU LEU A . n 
A 1 154 LEU 154 154 154 LEU LEU A . n 
A 1 155 SER 155 155 155 SER SER A . n 
A 1 156 VAL 156 156 156 VAL VAL A . n 
A 1 157 SER 157 157 157 SER SER A . n 
A 1 158 ILE 158 158 158 ILE ILE A . n 
A 1 159 PRO 159 159 159 PRO PRO A . n 
A 1 160 PHE 160 160 160 PHE PHE A . n 
A 1 161 ASN 161 161 161 ASN ASN A . n 
A 1 162 LYS 162 162 162 LYS LYS A . n 
A 1 163 LYS 163 163 163 LYS LYS A . n 
A 1 164 GLY 164 164 164 GLY GLY A . n 
A 1 165 TYR 165 165 165 TYR TYR A . n 
A 1 166 ASN 166 166 166 ASN ASN A . n 
A 1 167 VAL 167 167 167 VAL VAL A . n 
A 1 168 LYS 168 168 168 LYS LYS A . n 
A 1 169 TRP 169 169 169 TRP TRP A . n 
A 1 170 ARG 170 170 170 ARG ARG A . n 
A 1 171 SER 171 171 171 SER SER A . n 
A 1 172 ASN 172 172 172 ASN ASN A . n 
A 1 173 ALA 173 173 173 ALA ALA A . n 
A 1 174 ALA 174 174 174 ALA ALA A . n 
A 1 175 MET 175 175 175 MET MET A . n 
A 1 176 ALA 176 176 176 ALA ALA A . n 
A 1 177 THR 177 177 177 THR THR A . n 
A 1 178 THR 178 178 178 THR THR A . n 
A 1 179 ALA 179 179 179 ALA ALA A . n 
A 1 180 GLU 180 180 180 GLU GLU A . n 
A 1 181 LEU 181 181 181 LEU LEU A . n 
A 1 182 LYS 182 182 182 LYS LYS A . n 
A 1 183 GLU 183 183 183 GLU GLU A . n 
A 1 184 GLU 184 184 184 GLU GLU A . n 
A 1 185 LEU 185 185 185 LEU LEU A . n 
A 1 186 GLU 186 186 186 GLU GLU A . n 
A 1 187 ASN 187 187 187 ASN ASN A . n 
A 1 188 LEU 188 188 188 LEU LEU A . n 
A 1 189 THR 189 189 189 THR THR A . n 
A 1 190 MET 190 190 190 MET MET A . n 
A 1 191 ARG 191 191 191 ARG ARG A . n 
A 1 192 TYR 192 192 192 TYR TYR A . n 
A 1 193 SER 193 193 193 SER SER A . n 
A 1 194 TYR 194 194 194 TYR TYR A . n 
A 1 195 ASN 195 195 195 ASN ASN A . n 
A 1 196 ASP 196 196 196 ASP ASP A . n 
A 1 197 PHE 197 197 197 PHE PHE A . n 
A 1 198 ARG 198 198 198 ARG ARG A . n 
A 1 199 GLU 199 199 199 GLU GLU A . n 
A 1 200 GLN 200 200 200 GLN GLN A . n 
A 1 201 GLY 201 201 201 GLY GLY A . n 
A 1 202 GLU 202 202 202 GLU GLU A . n 
A 1 203 ASP 203 203 203 ASP ASP A . n 
A 1 204 PHE 204 204 204 PHE PHE A . n 
A 1 205 LEU 205 205 205 LEU LEU A . n 
A 1 206 LYS 206 206 206 LYS LYS A . n 
A 1 207 VAL 207 207 207 VAL VAL A . n 
A 1 208 THR 208 208 208 THR THR A . n 
A 1 209 LEU 209 209 209 LEU LEU A . n 
A 1 210 SER 210 210 210 SER SER A . n 
A 1 211 LEU 211 211 211 LEU LEU A . n 
A 1 212 GLU 212 212 212 GLU GLU A . n 
A 1 213 ASP 213 213 213 ASP ASP A . n 
A 1 214 LYS 214 214 214 LYS LYS A . n 
A 1 215 LEU 215 215 215 LEU LEU A . n 
A 1 216 PHE 216 216 216 PHE PHE A . n 
A 1 217 LEU 217 217 217 LEU LEU A . n 
A 1 218 ASP 218 218 218 ASP ASP A . n 
A 1 219 ASP 219 219 219 ASP ASP A . n 
A 1 220 ILE 220 220 220 ILE ILE A . n 
A 1 221 ARG 221 221 221 ARG ARG A . n 
A 1 222 SER 222 222 222 SER SER A . n 
A 1 223 LEU 223 223 223 LEU LEU A . n 
A 1 224 VAL 224 224 224 VAL VAL A . n 
A 1 225 ILE 225 225 225 ILE ILE A . n 
A 1 226 ASN 226 226 226 ASN ASN A . n 
A 1 227 THR 227 227 227 THR THR A . n 
A 1 228 MET 228 228 228 MET MET A . n 
A 1 229 LYS 229 229 229 LYS LYS A . n 
A 1 230 PHE 230 230 230 PHE PHE A . n 
A 1 231 HIS 231 231 231 HIS HIS A . n 
A 1 232 HIS 232 232 232 HIS HIS A . n 
A 1 233 MET 233 233 233 MET MET A . n 
A 1 234 LEU 234 234 234 LEU LEU A . n 
A 1 235 LYS 235 235 235 LYS LYS A . n 
A 1 236 MET 236 236 236 MET MET A . n 
A 1 237 THR 237 237 237 THR THR A . n 
A 1 238 TYR 238 238 238 TYR TYR A . n 
A 1 239 SER 239 239 239 SER SER A . n 
A 1 240 ASN 240 240 240 ASN ASN A . n 
A 1 241 GLU 241 241 241 GLU GLU A . n 
A 1 242 VAL 242 242 242 VAL VAL A . n 
A 1 243 ASP 243 243 243 ASP ASP A . n 
A 1 244 ILE 244 244 244 ILE ILE A . n 
A 1 245 GLU 245 245 245 GLU GLU A . n 
A 1 246 GLU 246 246 246 GLU GLU A . n 
A 1 247 GLY 247 247 247 GLY GLY A . n 
A 1 248 LYS 248 248 248 LYS LYS A . n 
A 1 249 VAL 249 249 249 VAL VAL A . n 
A 1 250 ASN 250 250 250 ASN ASN A . n 
A 1 251 PRO 251 251 251 PRO PRO A . n 
A 1 252 SER 252 252 252 SER SER A . n 
A 1 253 PRO 253 253 253 PRO PRO A . n 
A 1 254 GLU 254 254 254 GLU GLU A . n 
A 1 255 LYS 255 255 255 LYS LYS A . n 
A 1 256 LEU 256 256 256 LEU LEU A . n 
A 1 257 LEU 257 257 257 LEU LEU A . n 
A 1 258 THR 258 258 258 THR THR A . n 
A 1 259 SER 259 259 259 SER SER A . n 
A 1 260 LEU 260 260 260 LEU LEU A . n 
A 1 261 ILE 261 261 261 ILE ILE A . n 
A 1 262 GLY 262 262 262 GLY GLY A . n 
A 1 263 ASP 263 263 263 ASP ASP A . n 
A 1 264 ASN 264 264 264 ASN ASN A . n 
A 1 265 MET 265 265 265 MET MET A . n 
A 1 266 ILE 266 266 266 ILE ILE A . n 
A 1 267 GLU 267 267 267 GLU GLU A . n 
A 1 268 ALA 268 268 268 ALA ALA A . n 
A 1 269 ILE 269 269 269 ILE ILE A . n 
A 1 270 GLU 270 270 270 GLU GLU A . n 
A 1 271 HIS 271 271 271 HIS HIS A . n 
A 1 272 VAL 272 272 272 VAL VAL A . n 
A 1 273 LYS 273 273 273 LYS LYS A . n 
A 1 274 PRO 274 274 274 PRO PRO A . n 
A 1 275 ASN 275 275 275 ASN ASN A . n 
A 1 276 GLY 276 276 276 GLY GLY A . n 
A 1 277 LYS 277 277 277 LYS LYS A . n 
A 1 278 ARG 278 278 278 ARG ARG A . n 
A 1 279 VAL 279 279 279 VAL VAL A . n 
A 1 280 LEU 280 280 280 LEU LEU A . n 
A 1 281 LEU 281 281 281 LEU LEU A . n 
A 1 282 LYS 282 282 282 LYS LYS A . n 
A 1 283 GLY 283 283 283 GLY GLY A . n 
A 1 284 GLY 284 284 284 GLY GLY A . n 
A 1 285 THR 285 285 285 THR THR A . n 
A 1 286 ILE 286 286 286 ILE ILE A . n 
A 1 287 VAL 287 287 287 VAL VAL A . n 
A 1 288 GLN 288 288 288 GLN GLN A . n 
A 1 289 LYS 289 289 289 LYS LYS A . n 
A 1 290 GLU 290 290 290 GLU GLU A . n 
A 1 291 ILE 291 291 291 ILE ILE A . n 
A 1 292 GLY 292 292 292 GLY GLY A . n 
A 1 293 ARG 293 293 293 ARG ARG A . n 
A 1 294 ASP 294 294 294 ASP ASP A . n 
A 1 295 TYR 295 295 295 TYR TYR A . n 
A 1 296 TYR 296 296 296 TYR TYR A . n 
A 1 297 TRP 297 297 297 TRP TRP A . n 
A 1 298 LEU 298 298 298 LEU LEU A . n 
A 1 299 LYS 299 299 299 LYS LYS A . n 
A 1 300 ILE 300 300 300 ILE ILE A . n 
A 1 301 ARG 301 301 301 ARG ARG A . n 
A 1 302 ARG 302 302 302 ARG ARG A . n 
A 1 303 GLU 303 303 303 GLU GLU A . n 
A 1 304 PHE 304 304 304 PHE PHE A . n 
A 1 305 LYS 305 305 305 LYS LYS A . n 
A 1 306 SER 306 306 306 SER SER A . n 
A 1 307 GLY 307 307 307 GLY GLY A . n 
A 1 308 GLY 308 308 308 GLY GLY A . n 
A 1 309 ILE 309 309 309 ILE ILE A . n 
A 1 310 TYR 310 310 310 TYR TYR A . n 
A 1 311 ASP 311 311 311 ASP ASP A . n 
A 1 312 GLY 312 312 312 GLY GLY A . n 
A 1 313 LEU 313 313 313 LEU LEU A . n 
A 1 314 ASN 314 314 314 ASN ASN A . n 
A 1 315 LEU 315 315 315 LEU LEU A . n 
A 1 316 LYS 316 316 316 LYS LYS A . n 
A 1 317 ILE 317 317 317 ILE ILE A . n 
A 1 318 GLU 318 318 318 GLU GLU A . n 
A 1 319 ASP 319 319 319 ASP ASP A . n 
A 1 320 GLY 320 320 320 GLY GLY A . n 
A 1 321 ASP 321 321 321 ASP ASP A . n 
A 1 322 TYR 322 322 322 TYR TYR A . n 
A 1 323 ASP 323 323 323 ASP ASP A . n 
A 1 324 LEU 324 324 324 LEU LEU A . n 
A 1 325 VAL 325 325 325 VAL VAL A . n 
A 1 326 GLU 326 326 326 GLU GLU A . n 
A 1 327 LEU 327 327 327 LEU LEU A . n 
A 1 328 ASP 328 328 328 ASP ASP A . n 
A 1 329 SER 329 329 329 SER SER A . n 
A 1 330 ARG 330 330 330 ARG ARG A . n 
A 1 331 ASN 331 331 331 ASN ASN A . n 
A 1 332 TRP 332 332 332 TRP TRP A . n 
A 1 333 TYR 333 333 333 TYR TYR A . n 
A 1 334 GLN 334 334 334 GLN GLN A . n 
A 1 335 ILE 335 335 335 ILE ILE A . n 
A 1 336 HIS 336 336 336 HIS HIS A . n 
A 1 337 ARG 337 337 337 ARG ARG A . n 
A 1 338 TYR 338 338 338 TYR TYR A . n 
A 1 339 HIS 339 339 339 HIS HIS A . n 
A 1 340 ASP 340 340 340 ASP ASP A . n 
A 1 341 ARG 341 341 341 ARG ARG A . n 
A 1 342 ASN 342 342 342 ASN ASN A . n 
A 1 343 ASN 343 343 343 ASN ASN A . n 
A 1 344 ASN 344 344 344 ASN ASN A . n 
A 1 345 LEU 345 345 345 LEU LEU A . n 
A 1 346 LYS 346 346 346 LYS LYS A . n 
A 1 347 GLY 347 347 347 GLY GLY A . n 
A 1 348 LEU 348 348 348 LEU LEU A . n 
A 1 349 TYR 349 349 349 TYR TYR A . n 
A 1 350 VAL 350 350 350 VAL VAL A . n 
A 1 351 ASN 351 351 351 ASN ASN A . n 
A 1 352 ILE 352 352 352 ILE ILE A . n 
A 1 353 SER 353 353 353 SER SER A . n 
A 1 354 THR 354 354 354 THR THR A . n 
A 1 355 PRO 355 355 355 PRO PRO A . n 
A 1 356 PRO 356 356 356 PRO PRO A . n 
A 1 357 GLU 357 357 357 GLU GLU A . n 
A 1 358 LEU 358 358 358 LEU LEU A . n 
A 1 359 LEU 359 359 359 LEU LEU A . n 
A 1 360 LYS 360 360 360 LYS LYS A . n 
A 1 361 ASN 361 361 361 ASN ASN A . n 
A 1 362 ARG 362 362 362 ARG ARG A . n 
A 1 363 ILE 363 363 363 ILE ILE A . n 
A 1 364 ARG 364 364 364 ARG ARG A . n 
A 1 365 TYR 365 365 365 TYR TYR A . n 
A 1 366 LEU 366 366 366 LEU LEU A . n 
A 1 367 ASP 367 367 367 ASP ASP A . n 
A 1 368 LEU 368 368 368 LEU LEU A . n 
A 1 369 GLU 369 369 369 GLU GLU A . n 
A 1 370 VAL 370 370 370 VAL VAL A . n 
A 1 371 ASP 371 371 371 ASP ASP A . n 
A 1 372 VAL 372 372 372 VAL VAL A . n 
A 1 373 VAL 373 373 373 VAL VAL A . n 
A 1 374 LYS 374 374 374 LYS LYS A . n 
A 1 375 VAL 375 375 375 VAL VAL A . n 
A 1 376 ASN 376 376 376 ASN ASN A . n 
A 1 377 ASN 377 377 377 ASN ASN A . n 
A 1 378 THR 378 378 378 THR THR A . n 
A 1 379 VAL 379 379 379 VAL VAL A . n 
A 1 380 ASN 380 380 380 ASN ASN A . n 
A 1 381 ILE 381 381 381 ILE ILE A . n 
A 1 382 ILE 382 382 382 ILE ILE A . n 
A 1 383 ASP 383 383 383 ASP ASP A . n 
A 1 384 LEU 384 384 384 LEU LEU A . n 
A 1 385 GLU 385 385 385 GLU GLU A . n 
A 1 386 GLU 386 386 386 GLU GLU A . n 
A 1 387 LEU 387 387 387 LEU LEU A . n 
A 1 388 GLU 388 388 388 GLU GLU A . n 
A 1 389 ALA 389 389 389 ALA ALA A . n 
A 1 390 ASN 390 390 390 ASN ASN A . n 
A 1 391 LYS 391 391 391 LYS LYS A . n 
A 1 392 PRO 392 392 392 PRO PRO A . n 
A 1 393 ILE 393 393 393 ILE ILE A . n 
A 1 394 LEU 394 394 394 LEU LEU A . n 
A 1 395 GLY 395 395 395 GLY GLY A . n 
A 1 396 GLU 396 396 396 GLU GLU A . n 
A 1 397 PHE 397 397 397 PHE PHE A . n 
A 1 398 LEU 398 398 398 LEU LEU A . n 
A 1 399 TYR 399 399 399 TYR TYR A . n 
A 1 400 LYS 400 400 400 LYS LYS A . n 
A 1 401 LYS 401 401 401 LYS LYS A . n 
A 1 402 ALA 402 402 402 ALA ALA A . n 
A 1 403 LEU 403 403 403 LEU LEU A . n 
A 1 404 GLU 404 404 404 GLU GLU A . n 
A 1 405 ILE 405 405 405 ILE ILE A . n 
A 1 406 ALA 406 406 406 ALA ALA A . n 
A 1 407 GLN 407 407 407 GLN GLN A . n 
A 1 408 ASN 408 408 408 ASN ASN A . n 
A 1 409 ILE 409 409 409 ILE ILE A . n 
A 1 410 LYS 410 410 410 LYS LYS A . n 
A 1 411 ASP 411 411 411 ASP ASP A . n 
A 1 412 LYS 412 412 412 LYS LYS A . n 
A 1 413 LEU 413 413 413 LEU LEU A . n 
A 1 414 ASN 414 414 414 ASN ASN A . n 
A 1 415 GLU 415 415 415 GLU GLU A . n 
A 1 416 ASP 416 416 ?   ?   ?   A . n 
A 1 417 LYS 417 417 ?   ?   ?   A . n 
A 1 418 ILE 418 418 ?   ?   ?   A . 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 
B 2 MG  1   501 1   MG  MG  A . 
C 2 MG  1   502 2   MG  MG  A . 
D 3 HOH 1   601 41  HOH HOH A . 
D 3 HOH 2   602 90  HOH HOH A . 
D 3 HOH 3   603 192 HOH HOH A . 
D 3 HOH 4   604 227 HOH HOH A . 
D 3 HOH 5   605 169 HOH HOH A . 
D 3 HOH 6   606 89  HOH HOH A . 
D 3 HOH 7   607 4   HOH HOH A . 
D 3 HOH 8   608 75  HOH HOH A . 
D 3 HOH 9   609 69  HOH HOH A . 
D 3 HOH 10  610 2   HOH HOH A . 
D 3 HOH 11  611 203 HOH HOH A . 
D 3 HOH 12  612 195 HOH HOH A . 
D 3 HOH 13  613 128 HOH HOH A . 
D 3 HOH 14  614 85  HOH HOH A . 
D 3 HOH 15  615 55  HOH HOH A . 
D 3 HOH 16  616 74  HOH HOH A . 
D 3 HOH 17  617 147 HOH HOH A . 
D 3 HOH 18  618 7   HOH HOH A . 
D 3 HOH 19  619 139 HOH HOH A . 
D 3 HOH 20  620 248 HOH HOH A . 
D 3 HOH 21  621 8   HOH HOH A . 
D 3 HOH 22  622 197 HOH HOH A . 
D 3 HOH 23  623 6   HOH HOH A . 
D 3 HOH 24  624 62  HOH HOH A . 
D 3 HOH 25  625 218 HOH HOH A . 
D 3 HOH 26  626 223 HOH HOH A . 
D 3 HOH 27  627 57  HOH HOH A . 
D 3 HOH 28  628 37  HOH HOH A . 
D 3 HOH 29  629 142 HOH HOH A . 
D 3 HOH 30  630 144 HOH HOH A . 
D 3 HOH 31  631 25  HOH HOH A . 
D 3 HOH 32  632 165 HOH HOH A . 
D 3 HOH 33  633 200 HOH HOH A . 
D 3 HOH 34  634 141 HOH HOH A . 
D 3 HOH 35  635 96  HOH HOH A . 
D 3 HOH 36  636 186 HOH HOH A . 
D 3 HOH 37  637 99  HOH HOH A . 
D 3 HOH 38  638 243 HOH HOH A . 
D 3 HOH 39  639 163 HOH HOH A . 
D 3 HOH 40  640 103 HOH HOH A . 
D 3 HOH 41  641 49  HOH HOH A . 
D 3 HOH 42  642 17  HOH HOH A . 
D 3 HOH 43  643 32  HOH HOH A . 
D 3 HOH 44  644 11  HOH HOH A . 
D 3 HOH 45  645 220 HOH HOH A . 
D 3 HOH 46  646 64  HOH HOH A . 
D 3 HOH 47  647 127 HOH HOH A . 
D 3 HOH 48  648 133 HOH HOH A . 
D 3 HOH 49  649 202 HOH HOH A . 
D 3 HOH 50  650 168 HOH HOH A . 
D 3 HOH 51  651 151 HOH HOH A . 
D 3 HOH 52  652 52  HOH HOH A . 
D 3 HOH 53  653 140 HOH HOH A . 
D 3 HOH 54  654 65  HOH HOH A . 
D 3 HOH 55  655 43  HOH HOH A . 
D 3 HOH 56  656 79  HOH HOH A . 
D 3 HOH 57  657 63  HOH HOH A . 
D 3 HOH 58  658 135 HOH HOH A . 
D 3 HOH 59  659 214 HOH HOH A . 
D 3 HOH 60  660 83  HOH HOH A . 
D 3 HOH 61  661 33  HOH HOH A . 
D 3 HOH 62  662 56  HOH HOH A . 
D 3 HOH 63  663 28  HOH HOH A . 
D 3 HOH 64  664 211 HOH HOH A . 
D 3 HOH 65  665 18  HOH HOH A . 
D 3 HOH 66  666 129 HOH HOH A . 
D 3 HOH 67  667 84  HOH HOH A . 
D 3 HOH 68  668 112 HOH HOH A . 
D 3 HOH 69  669 58  HOH HOH A . 
D 3 HOH 70  670 226 HOH HOH A . 
D 3 HOH 71  671 157 HOH HOH A . 
D 3 HOH 72  672 231 HOH HOH A . 
D 3 HOH 73  673 126 HOH HOH A . 
D 3 HOH 74  674 234 HOH HOH A . 
D 3 HOH 75  675 183 HOH HOH A . 
D 3 HOH 76  676 176 HOH HOH A . 
D 3 HOH 77  677 184 HOH HOH A . 
D 3 HOH 78  678 178 HOH HOH A . 
D 3 HOH 79  679 26  HOH HOH A . 
D 3 HOH 80  680 86  HOH HOH A . 
D 3 HOH 81  681 44  HOH HOH A . 
D 3 HOH 82  682 53  HOH HOH A . 
D 3 HOH 83  683 94  HOH HOH A . 
D 3 HOH 84  684 185 HOH HOH A . 
D 3 HOH 85  685 111 HOH HOH A . 
D 3 HOH 86  686 12  HOH HOH A . 
D 3 HOH 87  687 47  HOH HOH A . 
D 3 HOH 88  688 131 HOH HOH A . 
D 3 HOH 89  689 191 HOH HOH A . 
D 3 HOH 90  690 22  HOH HOH A . 
D 3 HOH 91  691 10  HOH HOH A . 
D 3 HOH 92  692 72  HOH HOH A . 
D 3 HOH 93  693 121 HOH HOH A . 
D 3 HOH 94  694 15  HOH HOH A . 
D 3 HOH 95  695 189 HOH HOH A . 
D 3 HOH 96  696 78  HOH HOH A . 
D 3 HOH 97  697 166 HOH HOH A . 
D 3 HOH 98  698 14  HOH HOH A . 
D 3 HOH 99  699 113 HOH HOH A . 
D 3 HOH 100 700 50  HOH HOH A . 
D 3 HOH 101 701 125 HOH HOH A . 
D 3 HOH 102 702 67  HOH HOH A . 
D 3 HOH 103 703 146 HOH HOH A . 
D 3 HOH 104 704 250 HOH HOH A . 
D 3 HOH 105 705 82  HOH HOH A . 
D 3 HOH 106 706 98  HOH HOH A . 
D 3 HOH 107 707 73  HOH HOH A . 
D 3 HOH 108 708 71  HOH HOH A . 
D 3 HOH 109 709 35  HOH HOH A . 
D 3 HOH 110 710 101 HOH HOH A . 
D 3 HOH 111 711 120 HOH HOH A . 
D 3 HOH 112 712 153 HOH HOH A . 
D 3 HOH 113 713 242 HOH HOH A . 
D 3 HOH 114 714 13  HOH HOH A . 
D 3 HOH 115 715 181 HOH HOH A . 
D 3 HOH 116 716 161 HOH HOH A . 
D 3 HOH 117 717 80  HOH HOH A . 
D 3 HOH 118 718 60  HOH HOH A . 
D 3 HOH 119 719 3   HOH HOH A . 
D 3 HOH 120 720 109 HOH HOH A . 
D 3 HOH 121 721 138 HOH HOH A . 
D 3 HOH 122 722 221 HOH HOH A . 
D 3 HOH 123 723 24  HOH HOH A . 
D 3 HOH 124 724 5   HOH HOH A . 
D 3 HOH 125 725 225 HOH HOH A . 
D 3 HOH 126 726 95  HOH HOH A . 
D 3 HOH 127 727 110 HOH HOH A . 
D 3 HOH 128 728 16  HOH HOH A . 
D 3 HOH 129 729 236 HOH HOH A . 
D 3 HOH 130 730 30  HOH HOH A . 
D 3 HOH 131 731 116 HOH HOH A . 
D 3 HOH 132 732 229 HOH HOH A . 
D 3 HOH 133 733 21  HOH HOH A . 
D 3 HOH 134 734 233 HOH HOH A . 
D 3 HOH 135 735 68  HOH HOH A . 
D 3 HOH 136 736 224 HOH HOH A . 
D 3 HOH 137 737 137 HOH HOH A . 
D 3 HOH 138 738 59  HOH HOH A . 
D 3 HOH 139 739 167 HOH HOH A . 
D 3 HOH 140 740 230 HOH HOH A . 
D 3 HOH 141 741 100 HOH HOH A . 
D 3 HOH 142 742 152 HOH HOH A . 
D 3 HOH 143 743 27  HOH HOH A . 
D 3 HOH 144 744 107 HOH HOH A . 
D 3 HOH 145 745 108 HOH HOH A . 
D 3 HOH 146 746 132 HOH HOH A . 
D 3 HOH 147 747 81  HOH HOH A . 
D 3 HOH 148 748 190 HOH HOH A . 
D 3 HOH 149 749 70  HOH HOH A . 
D 3 HOH 150 750 23  HOH HOH A . 
D 3 HOH 151 751 34  HOH HOH A . 
D 3 HOH 152 752 206 HOH HOH A . 
D 3 HOH 153 753 217 HOH HOH A . 
D 3 HOH 154 754 171 HOH HOH A . 
D 3 HOH 155 755 122 HOH HOH A . 
D 3 HOH 156 756 9   HOH HOH A . 
D 3 HOH 157 757 20  HOH HOH A . 
D 3 HOH 158 758 61  HOH HOH A . 
D 3 HOH 159 759 117 HOH HOH A . 
D 3 HOH 160 760 179 HOH HOH A . 
D 3 HOH 161 761 235 HOH HOH A . 
D 3 HOH 162 762 210 HOH HOH A . 
D 3 HOH 163 763 76  HOH HOH A . 
D 3 HOH 164 764 180 HOH HOH A . 
D 3 HOH 165 765 88  HOH HOH A . 
D 3 HOH 166 766 232 HOH HOH A . 
D 3 HOH 167 767 255 HOH HOH A . 
D 3 HOH 168 768 87  HOH HOH A . 
D 3 HOH 169 769 46  HOH HOH A . 
D 3 HOH 170 770 174 HOH HOH A . 
D 3 HOH 171 771 19  HOH HOH A . 
D 3 HOH 172 772 160 HOH HOH A . 
D 3 HOH 173 773 175 HOH HOH A . 
D 3 HOH 174 774 91  HOH HOH A . 
D 3 HOH 175 775 156 HOH HOH A . 
D 3 HOH 176 776 148 HOH HOH A . 
D 3 HOH 177 777 105 HOH HOH A . 
D 3 HOH 178 778 251 HOH HOH A . 
D 3 HOH 179 779 31  HOH HOH A . 
D 3 HOH 180 780 48  HOH HOH A . 
D 3 HOH 181 781 245 HOH HOH A . 
D 3 HOH 182 782 29  HOH HOH A . 
D 3 HOH 183 783 196 HOH HOH A . 
D 3 HOH 184 784 150 HOH HOH A . 
D 3 HOH 185 785 92  HOH HOH A . 
D 3 HOH 186 786 173 HOH HOH A . 
D 3 HOH 187 787 118 HOH HOH A . 
D 3 HOH 188 788 102 HOH HOH A . 
D 3 HOH 189 789 247 HOH HOH A . 
D 3 HOH 190 790 1   HOH HOH A . 
D 3 HOH 191 791 155 HOH HOH A . 
D 3 HOH 192 792 215 HOH HOH A . 
D 3 HOH 193 793 145 HOH HOH A . 
D 3 HOH 194 794 209 HOH HOH A . 
D 3 HOH 195 795 66  HOH HOH A . 
D 3 HOH 196 796 194 HOH HOH A . 
D 3 HOH 197 797 104 HOH HOH A . 
D 3 HOH 198 798 177 HOH HOH A . 
D 3 HOH 199 799 130 HOH HOH A . 
D 3 HOH 200 800 246 HOH HOH A . 
D 3 HOH 201 801 249 HOH HOH A . 
D 3 HOH 202 802 204 HOH HOH A . 
D 3 HOH 203 803 77  HOH HOH A . 
D 3 HOH 204 804 51  HOH HOH A . 
D 3 HOH 205 805 193 HOH HOH A . 
D 3 HOH 206 806 237 HOH HOH A . 
D 3 HOH 207 807 158 HOH HOH A . 
D 3 HOH 208 808 42  HOH HOH A . 
D 3 HOH 209 809 198 HOH HOH A . 
D 3 HOH 210 810 199 HOH HOH A . 
D 3 HOH 211 811 134 HOH HOH A . 
D 3 HOH 212 812 240 HOH HOH A . 
D 3 HOH 213 813 244 HOH HOH A . 
D 3 HOH 214 814 188 HOH HOH A . 
D 3 HOH 215 815 40  HOH HOH A . 
D 3 HOH 216 816 216 HOH HOH A . 
D 3 HOH 217 817 45  HOH HOH A . 
D 3 HOH 218 818 159 HOH HOH A . 
D 3 HOH 219 819 106 HOH HOH A . 
D 3 HOH 220 820 239 HOH HOH A . 
D 3 HOH 221 821 154 HOH HOH A . 
D 3 HOH 222 822 119 HOH HOH A . 
D 3 HOH 223 823 114 HOH HOH A . 
D 3 HOH 224 824 36  HOH HOH A . 
D 3 HOH 225 825 208 HOH HOH A . 
D 3 HOH 226 826 170 HOH HOH A . 
D 3 HOH 227 827 254 HOH HOH A . 
D 3 HOH 228 828 149 HOH HOH A . 
D 3 HOH 229 829 162 HOH HOH A . 
D 3 HOH 230 830 172 HOH HOH A . 
D 3 HOH 231 831 213 HOH HOH A . 
D 3 HOH 232 832 187 HOH HOH A . 
D 3 HOH 233 833 207 HOH HOH A . 
D 3 HOH 234 834 253 HOH HOH A . 
D 3 HOH 235 835 123 HOH HOH A . 
D 3 HOH 236 836 252 HOH HOH A . 
D 3 HOH 237 837 219 HOH HOH A . 
D 3 HOH 238 838 241 HOH HOH A . 
D 3 HOH 239 839 182 HOH HOH A . 
D 3 HOH 240 840 201 HOH HOH A . 
D 3 HOH 241 841 143 HOH HOH A . 
D 3 HOH 242 842 238 HOH HOH A . 
D 3 HOH 243 843 164 HOH HOH A . 
D 3 HOH 244 844 93  HOH HOH A . 
D 3 HOH 245 845 228 HOH HOH A . 
D 3 HOH 246 846 124 HOH HOH A . 
D 3 HOH 247 847 212 HOH HOH A . 
# 
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       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.20.1_4487 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS      ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS      ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP   ? ? ? .           4 
? refinement       ? ? ? ? ? ? ? ? ? ? ? BUSTER   ? ? ? .           5 
? 'model building' ? ? ? ? ? ? ? ? ? ? ? ARP/wARP ? ? ? .           6 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8RZF 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     76.230 
_cell.length_a_esd                 ? 
_cell.length_b                     76.230 
_cell.length_b_esd                 ? 
_cell.length_c                     84.640 
_cell.length_c_esd                 ? 
_cell.volume                       491844.132 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8RZF 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                76 
_symmetry.space_group_name_Hall            'P 4w' 
_symmetry.space_group_name_H-M             'P 41' 
_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                   8RZF 
_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             2.55 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          51.83 
_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    'HEPES pH 7.5, MgCl2, polyacrylic acid (5,100) sodium salt' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_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 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2017-05-18 
_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   0.9786 
_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                        'SOLEIL BEAMLINE PROXIMA 2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9786 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'PROXIMA 2' 
_diffrn_source.pdbx_synchrotron_site       SOLEIL 
# 
_reflns.B_iso_Wilson_estimate                          31.54 
_reflns.entry_id                                       8RZF 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.0 
_reflns.d_resolution_low                               28.3 
_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                                     30609 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.0 
_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                                ? 
_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                                   0.9 
_reflns.pdbx_CC_star                                   0.99 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.04 
_reflns_shell.d_res_low                                     2.11 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.1 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3052 
_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                               4.3 
_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                               ? 
_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                                  0.4 
_reflns_shell.pdbx_CC_star                                  0.8 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.4 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_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]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               35.28 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_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                                 8RZF 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.04 
_refine.ls_d_res_low                             28.3 
_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                     30609 
_refine.ls_number_reflns_R_free                  1531 
_refine.ls_number_reflns_R_work                  29078 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.65 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1927 
_refine.ls_R_factor_R_free                       0.2138 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1915 
_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                    'FLAT BULK SOLVENT MODEL' 
_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                          1.34 
_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               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_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                 22.7735 
_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                             ? 
_refine.overall_SU_ML                            0.2622 
_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                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.04 
_refine_hist.d_res_low                        28.3 
_refine_hist.number_atoms_solvent             247 
_refine_hist.number_atoms_total               3637 
_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        3388 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         2 
_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' ? 0.0135  ? 3454 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.2454  ? 4658 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0865  ? 514  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0068  ? 596  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 15.0195 ? 1326 ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_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 
_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 
'X-RAY DIFFRACTION' 2.04 2.11 . . 140 2650 98.94  . . . . 0.2661 . . . . . . . . . . . 0.3105 
'X-RAY DIFFRACTION' 2.11 2.18 . . 138 2617 100.00 . . . . 0.2489 . . . . . . . . . . . 0.2917 
'X-RAY DIFFRACTION' 2.19 2.27 . . 137 2607 99.71  . . . . 0.2882 . . . . . . . . . . . 0.3240 
'X-RAY DIFFRACTION' 2.27 2.38 . . 140 2645 99.86  . . . . 0.2370 . . . . . . . . . . . 0.2898 
'X-RAY DIFFRACTION' 2.38 2.50 . . 139 2641 99.78  . . . . 0.2247 . . . . . . . . . . . 0.2802 
'X-RAY DIFFRACTION' 2.50 2.66 . . 138 2635 100.00 . . . . 0.2293 . . . . . . . . . . . 0.2417 
'X-RAY DIFFRACTION' 2.66 2.86 . . 140 2646 99.93  . . . . 0.2111 . . . . . . . . . . . 0.2480 
'X-RAY DIFFRACTION' 2.86 3.15 . . 139 2647 99.93  . . . . 0.1963 . . . . . . . . . . . 0.2327 
'X-RAY DIFFRACTION' 3.15 3.61 . . 139 2652 99.64  . . . . 0.1768 . . . . . . . . . . . 0.1702 
'X-RAY DIFFRACTION' 3.61 4.54 . . 140 2649 99.22  . . . . 0.1529 . . . . . . . . . . . 0.1656 
'X-RAY DIFFRACTION' 4.54 28.3 . . 141 2689 99.26  . . . . 0.1555 . . . . . . . . . . . 0.1739 
# 
_struct.entry_id                     8RZF 
_struct.title                        'RNase W from Sulfolobus acidocaldarius' 
_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        8RZF 
_struct_keywords.text            'Ribonuclease, FAU-1, Archaea, Ribosome biogenesis, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
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 2 ? 
C N N 2 ? 
D N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    FAU1_SULAC 
_struct_ref.pdbx_db_accession          Q4J9H1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MRVRIRGIYATALTYLFLKNGFEIVQQTPQIAERFFMDIIRSPADVTVKDGIDKGEIVSVGEDIYNFMRSIFKYSPIWRS
PIKLYSVVSTEDCKFMNFIVEPCLSEGLVIKPPVEGKIILSSPRAVGKFAMVWKGDGRTFFSEHIDERDSQRLLSVSIPF
NKKGYNVKWRSNAAMATTAELKEELENLTMRYSYNDFREQGEDFLKVTLSLEDKLFLDDIRSLVINTMKFHHMLKMTYSN
EVDIEEGKVNPSPEKLLTSLIGDNMIEAIEHVKPNGKRVLLKGGTIVQKEIGRDYYWLKIRREFKSGGIYDGLNLKIEDG
DYDLVELDSRNWYQIHRYHDRNNNLKGLYVNISTPPELLKNRIRYLDLEVDVVKVNNTVNIIDLEELEANKPILGEFLYK
KALEIAQNIKDKLNEDKI
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8RZF 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 418 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q4J9H1 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  418 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       418 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
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)' 190   ? 
1 MORE         -14   ? 
1 'SSA (A^2)'  19410 ? 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 TYR A 9   ? ASN A 20  ? TYR A 9   ASN A 20  1 ? 12 
HELX_P HELX_P2  AA2 THR A 28  ? PHE A 35  ? THR A 28  PHE A 35  1 ? 8  
HELX_P HELX_P3  AA3 ILE A 64  ? PHE A 72  ? ILE A 64  PHE A 72  1 ? 9  
HELX_P HELX_P4  AA4 ASP A 146 ? LYS A 163 ? ASP A 146 LYS A 163 1 ? 18 
HELX_P HELX_P5  AA5 SER A 171 ? ALA A 176 ? SER A 171 ALA A 176 5 ? 6  
HELX_P HELX_P6  AA6 THR A 177 ? TYR A 194 ? THR A 177 TYR A 194 1 ? 18 
HELX_P HELX_P7  AA7 SER A 210 ? LEU A 223 ? SER A 210 LEU A 223 1 ? 14 
HELX_P HELX_P8  AA8 PHE A 230 ? LYS A 235 ? PHE A 230 LYS A 235 1 ? 6  
HELX_P HELX_P9  AA9 SER A 239 ? LYS A 248 ? SER A 239 LYS A 248 1 ? 10 
HELX_P HELX_P10 AB1 PRO A 253 ? ILE A 261 ? PRO A 253 ILE A 261 1 ? 9  
HELX_P HELX_P11 AB2 ASP A 383 ? ASN A 390 ? ASP A 383 ASN A 390 1 ? 8  
HELX_P HELX_P12 AB3 ASN A 390 ? GLY A 395 ? ASN A 390 GLY A 395 1 ? 6  
HELX_P HELX_P13 AB4 GLY A 395 ? ASN A 414 ? GLY A 395 ASN A 414 1 ? 20 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ? ? A CYS 93  SG  ? ? ? 1_555 A CYS 103 SG ? ? A CYS 93  A CYS 103 1_555 ? ? ? ? ? ? ? 2.028 ? ? 
metalc1 metalc ? ? A ASN 351 OD1 ? ? ? 1_555 B MG  .   MG ? ? A ASN 351 A MG  501 1_555 ? ? ? ? ? ? ? 2.443 ? ? 
metalc2 metalc ? ? A ASP 367 OD1 ? ? ? 1_555 B MG  .   MG ? ? A ASP 367 A MG  501 1_555 ? ? ? ? ? ? ? 2.221 ? ? 
metalc3 metalc ? ? A ASP 371 OD1 ? ? ? 1_555 B MG  .   MG ? ? A ASP 371 A MG  501 1_555 ? ? ? ? ? ? ? 2.101 ? ? 
metalc4 metalc ? ? B MG  .   MG  ? ? ? 1_555 D HOH .   O  ? ? A MG  501 A HOH 641 1_555 ? ? ? ? ? ? ? 2.220 ? ? 
metalc5 metalc ? ? C MG  .   MG  ? ? ? 1_555 D HOH .   O  ? ? A MG  502 A HOH 601 1_555 ? ? ? ? ? ? ? 2.643 ? ? 
metalc6 metalc ? ? C MG  .   MG  ? ? ? 1_555 D HOH .   O  ? ? A MG  502 A HOH 817 1_555 ? ? ? ? ? ? ? 2.752 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 OD1 ? A ASN 351 ? A ASN 351 ? 1_555 MG ? B MG . ? A MG 501 ? 1_555 OD1 ? A ASP 367 ? A ASP 367 ? 1_555 82.6  ? 
2 OD1 ? A ASN 351 ? A ASN 351 ? 1_555 MG ? B MG . ? A MG 501 ? 1_555 OD1 ? A ASP 371 ? A ASP 371 ? 1_555 90.4  ? 
3 OD1 ? A ASP 367 ? A ASP 367 ? 1_555 MG ? B MG . ? A MG 501 ? 1_555 OD1 ? A ASP 371 ? A ASP 371 ? 1_555 155.5 ? 
4 OD1 ? A ASN 351 ? A ASN 351 ? 1_555 MG ? B MG . ? A MG 501 ? 1_555 O   ? D HOH .   ? A HOH 641 ? 1_555 137.9 ? 
5 OD1 ? A ASP 367 ? A ASP 367 ? 1_555 MG ? B MG . ? A MG 501 ? 1_555 O   ? D HOH .   ? A HOH 641 ? 1_555 85.1  ? 
6 OD1 ? A ASP 371 ? A ASP 371 ? 1_555 MG ? B MG . ? A MG 501 ? 1_555 O   ? D HOH .   ? A HOH 641 ? 1_555 114.9 ? 
7 O   ? D HOH .   ? A HOH 601 ? 1_555 MG ? C MG . ? A MG 502 ? 1_555 O   ? D HOH .   ? A HOH 817 ? 1_555 81.6  ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      CYS 
_pdbx_modification_feature.label_asym_id                      A 
_pdbx_modification_feature.label_seq_id                       93 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     CYS 
_pdbx_modification_feature.modified_residue_label_asym_id     A 
_pdbx_modification_feature.modified_residue_label_seq_id      103 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       CYS 
_pdbx_modification_feature.auth_asym_id                       A 
_pdbx_modification_feature.auth_seq_id                        93 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      CYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      A 
_pdbx_modification_feature.modified_residue_auth_seq_id       103 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_555 
_pdbx_modification_feature.comp_id_linking_atom               SG 
_pdbx_modification_feature.modified_residue_id_linking_atom   SG 
_pdbx_modification_feature.modified_residue_id                . 
_pdbx_modification_feature.ref_pcm_id                         . 
_pdbx_modification_feature.ref_comp_id                        . 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Disulfide bridge' 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          GLU 
_struct_mon_prot_cis.label_seq_id           101 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           GLU 
_struct_mon_prot_cis.auth_seq_id            101 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    102 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     102 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       -10.12 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6  ? 
AA2 ? 5  ? 
AA3 ? 4  ? 
AA4 ? 10 ? 
AA5 ? 2  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2  ? parallel      
AA1 2 3  ? parallel      
AA1 3 4  ? anti-parallel 
AA1 4 5  ? anti-parallel 
AA1 5 6  ? anti-parallel 
AA2 1 2  ? anti-parallel 
AA2 2 3  ? anti-parallel 
AA2 3 4  ? parallel      
AA2 4 5  ? anti-parallel 
AA3 1 2  ? anti-parallel 
AA3 2 3  ? anti-parallel 
AA3 3 4  ? parallel      
AA4 3 4  ? anti-parallel 
AA4 4 5  ? anti-parallel 
AA4 5 6  ? anti-parallel 
AA4 6 7  ? anti-parallel 
AA4 7 8  ? anti-parallel 
AA4 8 9  ? anti-parallel 
AA4 9 10 ? anti-parallel 
AA5 1 2  ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  GLU A 23  ? ILE A 24  ? GLU A 23  ILE A 24  
AA1 2  ARG A 2   ? ILE A 5   ? ARG A 2   ILE A 5   
AA1 3  VAL A 46  ? ASP A 50  ? VAL A 46  ASP A 50  
AA1 4  GLU A 56  ? GLY A 61  ? GLU A 56  GLY A 61  
AA1 5  ASP A 203 ? THR A 208 ? ASP A 203 THR A 208 
AA1 6  ILE A 77  ? ARG A 79  ? ILE A 77  ARG A 79  
AA2 1  VAL A 87  ? SER A 89  ? VAL A 87  SER A 89  
AA2 2  GLU A 106 ? LYS A 111 ? GLU A 106 LYS A 111 
AA2 3  LYS A 117 ? SER A 121 ? LYS A 117 SER A 121 
AA2 4  PHE A 98  ? GLU A 101 ? PHE A 98  GLU A 101 
AA2 5  LYS A 94  ? PHE A 95  ? LYS A 94  PHE A 95  
AA3 1  ALA A 125 ? VAL A 126 ? ALA A 125 VAL A 126 
AA3 2  ALA A 130 ? LYS A 134 ? ALA A 130 LYS A 134 
AA3 3  TYR A 165 ? TRP A 169 ? TYR A 165 TRP A 169 
AA3 4  THR A 139 ? PHE A 141 ? THR A 139 PHE A 141 
AA4 1  GLU A 357 ? LEU A 359 ? GLU A 357 LEU A 359 
AA4 2  THR A 378 ? ILE A 382 ? THR A 378 ILE A 382 
AA4 3  MET A 265 ? VAL A 272 ? MET A 265 VAL A 272 
AA4 4  ARG A 278 ? ILE A 291 ? ARG A 278 ILE A 291 
AA4 5  TYR A 296 ? GLU A 303 ? TYR A 296 GLU A 303 
AA4 6  TYR A 322 ? ASP A 328 ? TYR A 322 ASP A 328 
AA4 7  TYR A 333 ? HIS A 339 ? TYR A 333 HIS A 339 
AA4 8  LEU A 345 ? SER A 353 ? LEU A 345 SER A 353 
AA4 9  ARG A 362 ? VAL A 375 ? ARG A 362 VAL A 375 
AA4 10 THR A 378 ? ILE A 382 ? THR A 378 ILE A 382 
AA5 1  ILE A 309 ? TYR A 310 ? ILE A 309 TYR A 310 
AA5 2  LEU A 315 ? LYS A 316 ? LEU A 315 LYS A 316 
# 
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  O GLU A 23  ? O GLU A 23  N VAL A 3   ? N VAL A 3   
AA1 2 3  N ARG A 4   ? N ARG A 4   O VAL A 48  ? O VAL A 48  
AA1 3 4  N LYS A 49  ? N LYS A 49  O VAL A 58  ? O VAL A 58  
AA1 4 5  N ILE A 57  ? N ILE A 57  O VAL A 207 ? O VAL A 207 
AA1 5 6  O LYS A 206 ? O LYS A 206 N TRP A 78  ? N TRP A 78  
AA2 1 2  N VAL A 88  ? N VAL A 88  O GLY A 107 ? O GLY A 107 
AA2 2 3  N LEU A 108 ? N LEU A 108 O SER A 121 ? O SER A 121 
AA2 3 4  O ILE A 118 ? O ILE A 118 N ILE A 99  ? N ILE A 99  
AA2 4 5  O PHE A 98  ? O PHE A 98  N PHE A 95  ? N PHE A 95  
AA3 1 2  N ALA A 125 ? N ALA A 125 O VAL A 132 ? O VAL A 132 
AA3 2 3  N TRP A 133 ? N TRP A 133 O ASN A 166 ? O ASN A 166 
AA3 3 4  O VAL A 167 ? O VAL A 167 N PHE A 140 ? N PHE A 140 
AA4 3 4  N HIS A 271 ? N HIS A 271 O VAL A 279 ? O VAL A 279 
AA4 4 5  N THR A 285 ? N THR A 285 O ARG A 301 ? O ARG A 301 
AA4 5 6  N ILE A 300 ? N ILE A 300 O VAL A 325 ? O VAL A 325 
AA4 6 7  N TYR A 322 ? N TYR A 322 O HIS A 339 ? O HIS A 339 
AA4 7 8  N TYR A 338 ? N TYR A 338 O LYS A 346 ? O LYS A 346 
AA4 8 9  N VAL A 350 ? N VAL A 350 O VAL A 372 ? O VAL A 372 
AA4 9 10 N VAL A 373 ? N VAL A 373 O ASN A 380 ? O ASN A 380 
AA5 1 2  N TYR A 310 ? N TYR A 310 O LEU A 315 ? O LEU A 315 
# 
_pdbx_entry_details.entry_id                   8RZF 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   OD2 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   ASP 
_pdbx_validate_close_contact.auth_seq_id_1    371 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    601 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.11 
# 
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 MET A 96  ? ? 54.34   -119.75 
2 1 SER A 239 ? ? -123.11 -96.07  
3 1 ILE A 261 ? ? -112.63 55.35   
4 1 TRP A 332 ? ? -93.05  32.94   
5 1 GLU A 369 ? ? 73.91   -59.31  
6 1 ASN A 376 ? ? 59.05   -115.97 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z       
2 -y,x,z+1/4  
3 y,-x,z+3/4  
4 -x,-y,z+1/2 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A ASP 416 ? A ASP 416 
2 1 Y 1 A LYS 417 ? A LYS 417 
3 1 Y 1 A ILE 418 ? A ILE 418 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
GLN N    N  N N 88  
GLN CA   C  N S 89  
GLN C    C  N N 90  
GLN O    O  N N 91  
GLN CB   C  N N 92  
GLN CG   C  N N 93  
GLN CD   C  N N 94  
GLN OE1  O  N N 95  
GLN NE2  N  N N 96  
GLN OXT  O  N N 97  
GLN H    H  N N 98  
GLN H2   H  N N 99  
GLN HA   H  N N 100 
GLN HB2  H  N N 101 
GLN HB3  H  N N 102 
GLN HG2  H  N N 103 
GLN HG3  H  N N 104 
GLN HE21 H  N N 105 
GLN HE22 H  N N 106 
GLN HXT  H  N N 107 
GLU N    N  N N 108 
GLU CA   C  N S 109 
GLU C    C  N N 110 
GLU O    O  N N 111 
GLU CB   C  N N 112 
GLU CG   C  N N 113 
GLU CD   C  N N 114 
GLU OE1  O  N N 115 
GLU OE2  O  N N 116 
GLU OXT  O  N N 117 
GLU H    H  N N 118 
GLU H2   H  N N 119 
GLU HA   H  N N 120 
GLU HB2  H  N N 121 
GLU HB3  H  N N 122 
GLU HG2  H  N N 123 
GLU HG3  H  N N 124 
GLU HE2  H  N N 125 
GLU HXT  H  N N 126 
GLY N    N  N N 127 
GLY CA   C  N N 128 
GLY C    C  N N 129 
GLY O    O  N N 130 
GLY OXT  O  N N 131 
GLY H    H  N N 132 
GLY H2   H  N N 133 
GLY HA2  H  N N 134 
GLY HA3  H  N N 135 
GLY HXT  H  N N 136 
HIS N    N  N N 137 
HIS CA   C  N S 138 
HIS C    C  N N 139 
HIS O    O  N N 140 
HIS CB   C  N N 141 
HIS CG   C  Y N 142 
HIS ND1  N  Y N 143 
HIS CD2  C  Y N 144 
HIS CE1  C  Y N 145 
HIS NE2  N  Y N 146 
HIS OXT  O  N N 147 
HIS H    H  N N 148 
HIS H2   H  N N 149 
HIS HA   H  N N 150 
HIS HB2  H  N N 151 
HIS HB3  H  N N 152 
HIS HD1  H  N N 153 
HIS HD2  H  N N 154 
HIS HE1  H  N N 155 
HIS HE2  H  N N 156 
HIS HXT  H  N N 157 
HOH O    O  N N 158 
HOH H1   H  N N 159 
HOH H2   H  N N 160 
ILE N    N  N N 161 
ILE CA   C  N S 162 
ILE C    C  N N 163 
ILE O    O  N N 164 
ILE CB   C  N S 165 
ILE CG1  C  N N 166 
ILE CG2  C  N N 167 
ILE CD1  C  N N 168 
ILE OXT  O  N N 169 
ILE H    H  N N 170 
ILE H2   H  N N 171 
ILE HA   H  N N 172 
ILE HB   H  N N 173 
ILE HG12 H  N N 174 
ILE HG13 H  N N 175 
ILE HG21 H  N N 176 
ILE HG22 H  N N 177 
ILE HG23 H  N N 178 
ILE HD11 H  N N 179 
ILE HD12 H  N N 180 
ILE HD13 H  N N 181 
ILE HXT  H  N N 182 
LEU N    N  N N 183 
LEU CA   C  N S 184 
LEU C    C  N N 185 
LEU O    O  N N 186 
LEU CB   C  N N 187 
LEU CG   C  N N 188 
LEU CD1  C  N N 189 
LEU CD2  C  N N 190 
LEU OXT  O  N N 191 
LEU H    H  N N 192 
LEU H2   H  N N 193 
LEU HA   H  N N 194 
LEU HB2  H  N N 195 
LEU HB3  H  N N 196 
LEU HG   H  N N 197 
LEU HD11 H  N N 198 
LEU HD12 H  N N 199 
LEU HD13 H  N N 200 
LEU HD21 H  N N 201 
LEU HD22 H  N N 202 
LEU HD23 H  N N 203 
LEU HXT  H  N N 204 
LYS N    N  N N 205 
LYS CA   C  N S 206 
LYS C    C  N N 207 
LYS O    O  N N 208 
LYS CB   C  N N 209 
LYS CG   C  N N 210 
LYS CD   C  N N 211 
LYS CE   C  N N 212 
LYS NZ   N  N N 213 
LYS OXT  O  N N 214 
LYS H    H  N N 215 
LYS H2   H  N N 216 
LYS HA   H  N N 217 
LYS HB2  H  N N 218 
LYS HB3  H  N N 219 
LYS HG2  H  N N 220 
LYS HG3  H  N N 221 
LYS HD2  H  N N 222 
LYS HD3  H  N N 223 
LYS HE2  H  N N 224 
LYS HE3  H  N N 225 
LYS HZ1  H  N N 226 
LYS HZ2  H  N N 227 
LYS HZ3  H  N N 228 
LYS HXT  H  N N 229 
MET N    N  N N 230 
MET CA   C  N S 231 
MET C    C  N N 232 
MET O    O  N N 233 
MET CB   C  N N 234 
MET CG   C  N N 235 
MET SD   S  N N 236 
MET CE   C  N N 237 
MET OXT  O  N N 238 
MET H    H  N N 239 
MET H2   H  N N 240 
MET HA   H  N N 241 
MET HB2  H  N N 242 
MET HB3  H  N N 243 
MET HG2  H  N N 244 
MET HG3  H  N N 245 
MET HE1  H  N N 246 
MET HE2  H  N N 247 
MET HE3  H  N N 248 
MET HXT  H  N N 249 
MG  MG   MG N N 250 
PHE N    N  N N 251 
PHE CA   C  N S 252 
PHE C    C  N N 253 
PHE O    O  N N 254 
PHE CB   C  N N 255 
PHE CG   C  Y N 256 
PHE CD1  C  Y N 257 
PHE CD2  C  Y N 258 
PHE CE1  C  Y N 259 
PHE CE2  C  Y N 260 
PHE CZ   C  Y N 261 
PHE OXT  O  N N 262 
PHE H    H  N N 263 
PHE H2   H  N N 264 
PHE HA   H  N N 265 
PHE HB2  H  N N 266 
PHE HB3  H  N N 267 
PHE HD1  H  N N 268 
PHE HD2  H  N N 269 
PHE HE1  H  N N 270 
PHE HE2  H  N N 271 
PHE HZ   H  N N 272 
PHE HXT  H  N N 273 
PRO N    N  N N 274 
PRO CA   C  N S 275 
PRO C    C  N N 276 
PRO O    O  N N 277 
PRO CB   C  N N 278 
PRO CG   C  N N 279 
PRO CD   C  N N 280 
PRO OXT  O  N N 281 
PRO H    H  N N 282 
PRO HA   H  N N 283 
PRO HB2  H  N N 284 
PRO HB3  H  N N 285 
PRO HG2  H  N N 286 
PRO HG3  H  N N 287 
PRO HD2  H  N N 288 
PRO HD3  H  N N 289 
PRO HXT  H  N N 290 
SER N    N  N N 291 
SER CA   C  N S 292 
SER C    C  N N 293 
SER O    O  N N 294 
SER CB   C  N N 295 
SER OG   O  N N 296 
SER OXT  O  N N 297 
SER H    H  N N 298 
SER H2   H  N N 299 
SER HA   H  N N 300 
SER HB2  H  N N 301 
SER HB3  H  N N 302 
SER HG   H  N N 303 
SER HXT  H  N N 304 
THR N    N  N N 305 
THR CA   C  N S 306 
THR C    C  N N 307 
THR O    O  N N 308 
THR CB   C  N R 309 
THR OG1  O  N N 310 
THR CG2  C  N N 311 
THR OXT  O  N N 312 
THR H    H  N N 313 
THR H2   H  N N 314 
THR HA   H  N N 315 
THR HB   H  N N 316 
THR HG1  H  N N 317 
THR HG21 H  N N 318 
THR HG22 H  N N 319 
THR HG23 H  N N 320 
THR HXT  H  N N 321 
TRP N    N  N N 322 
TRP CA   C  N S 323 
TRP C    C  N N 324 
TRP O    O  N N 325 
TRP CB   C  N N 326 
TRP CG   C  Y N 327 
TRP CD1  C  Y N 328 
TRP CD2  C  Y N 329 
TRP NE1  N  Y N 330 
TRP CE2  C  Y N 331 
TRP CE3  C  Y N 332 
TRP CZ2  C  Y N 333 
TRP CZ3  C  Y N 334 
TRP CH2  C  Y N 335 
TRP OXT  O  N N 336 
TRP H    H  N N 337 
TRP H2   H  N N 338 
TRP HA   H  N N 339 
TRP HB2  H  N N 340 
TRP HB3  H  N N 341 
TRP HD1  H  N N 342 
TRP HE1  H  N N 343 
TRP HE3  H  N N 344 
TRP HZ2  H  N N 345 
TRP HZ3  H  N N 346 
TRP HH2  H  N N 347 
TRP HXT  H  N N 348 
TYR N    N  N N 349 
TYR CA   C  N S 350 
TYR C    C  N N 351 
TYR O    O  N N 352 
TYR CB   C  N N 353 
TYR CG   C  Y N 354 
TYR CD1  C  Y N 355 
TYR CD2  C  Y N 356 
TYR CE1  C  Y N 357 
TYR CE2  C  Y N 358 
TYR CZ   C  Y N 359 
TYR OH   O  N N 360 
TYR OXT  O  N N 361 
TYR H    H  N N 362 
TYR H2   H  N N 363 
TYR HA   H  N N 364 
TYR HB2  H  N N 365 
TYR HB3  H  N N 366 
TYR HD1  H  N N 367 
TYR HD2  H  N N 368 
TYR HE1  H  N N 369 
TYR HE2  H  N N 370 
TYR HH   H  N N 371 
TYR HXT  H  N N 372 
VAL N    N  N N 373 
VAL CA   C  N S 374 
VAL C    C  N N 375 
VAL O    O  N N 376 
VAL CB   C  N N 377 
VAL CG1  C  N N 378 
VAL CG2  C  N N 379 
VAL OXT  O  N N 380 
VAL H    H  N N 381 
VAL H2   H  N N 382 
VAL HA   H  N N 383 
VAL HB   H  N N 384 
VAL HG11 H  N N 385 
VAL HG12 H  N N 386 
VAL HG13 H  N N 387 
VAL HG21 H  N N 388 
VAL HG22 H  N N 389 
VAL HG23 H  N N 390 
VAL HXT  H  N N 391 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TRP N   CA   sing N N 306 
TRP N   H    sing N N 307 
TRP N   H2   sing N N 308 
TRP CA  C    sing N N 309 
TRP CA  CB   sing N N 310 
TRP CA  HA   sing N N 311 
TRP C   O    doub N N 312 
TRP C   OXT  sing N N 313 
TRP CB  CG   sing N N 314 
TRP CB  HB2  sing N N 315 
TRP CB  HB3  sing N N 316 
TRP CG  CD1  doub Y N 317 
TRP CG  CD2  sing Y N 318 
TRP CD1 NE1  sing Y N 319 
TRP CD1 HD1  sing N N 320 
TRP CD2 CE2  doub Y N 321 
TRP CD2 CE3  sing Y N 322 
TRP NE1 CE2  sing Y N 323 
TRP NE1 HE1  sing N N 324 
TRP CE2 CZ2  sing Y N 325 
TRP CE3 CZ3  doub Y N 326 
TRP CE3 HE3  sing N N 327 
TRP CZ2 CH2  doub Y N 328 
TRP CZ2 HZ2  sing N N 329 
TRP CZ3 CH2  sing Y N 330 
TRP CZ3 HZ3  sing N N 331 
TRP CH2 HH2  sing N N 332 
TRP OXT HXT  sing N N 333 
TYR N   CA   sing N N 334 
TYR N   H    sing N N 335 
TYR N   H2   sing N N 336 
TYR CA  C    sing N N 337 
TYR CA  CB   sing N N 338 
TYR CA  HA   sing N N 339 
TYR C   O    doub N N 340 
TYR C   OXT  sing N N 341 
TYR CB  CG   sing N N 342 
TYR CB  HB2  sing N N 343 
TYR CB  HB3  sing N N 344 
TYR CG  CD1  doub Y N 345 
TYR CG  CD2  sing Y N 346 
TYR CD1 CE1  sing Y N 347 
TYR CD1 HD1  sing N N 348 
TYR CD2 CE2  doub Y N 349 
TYR CD2 HD2  sing N N 350 
TYR CE1 CZ   doub Y N 351 
TYR CE1 HE1  sing N N 352 
TYR CE2 CZ   sing Y N 353 
TYR CE2 HE2  sing N N 354 
TYR CZ  OH   sing N N 355 
TYR OH  HH   sing N N 356 
TYR OXT HXT  sing N N 357 
VAL N   CA   sing N N 358 
VAL N   H    sing N N 359 
VAL N   H2   sing N N 360 
VAL CA  C    sing N N 361 
VAL CA  CB   sing N N 362 
VAL CA  HA   sing N N 363 
VAL C   O    doub N N 364 
VAL C   OXT  sing N N 365 
VAL CB  CG1  sing N N 366 
VAL CB  CG2  sing N N 367 
VAL CB  HB   sing N N 368 
VAL CG1 HG11 sing N N 369 
VAL CG1 HG12 sing N N 370 
VAL CG1 HG13 sing N N 371 
VAL CG2 HG21 sing N N 372 
VAL CG2 HG22 sing N N 373 
VAL CG2 HG23 sing N N 374 
VAL OXT HXT  sing N N 375 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Other government'                                    ?      ? 1 
'Centre National de la Recherche Scientifique (CNRS)' France ? 2 
# 
_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   8RZA 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 41' 
_space_group.name_Hall        'P 4w' 
_space_group.IT_number        76 
_space_group.crystal_system   tetragonal 
_space_group.id               1 
# 
_atom_sites.entry_id                    8RZF 
_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]   0.013118 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.013118 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.011815 
_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 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C  ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
MG ? ? 9.41153 2.53737 ? ? 2.59044  63.03566 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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   . MET A 1 1   ? 28.97500 -9.31900  42.05400 1.000 34.09000 ? 1   MET A N   1 
ATOM   2    C  CA  . MET A 1 1   ? 27.93600 -9.72600  42.98800 1.000 35.52000 ? 1   MET A CA  1 
ATOM   3    C  C   . MET A 1 1   ? 27.67200 -8.61300  43.96000 1.000 30.00000 ? 1   MET A C   1 
ATOM   4    O  O   . MET A 1 1   ? 28.59400 -7.89300  44.34400 1.000 29.67000 ? 1   MET A O   1 
ATOM   5    C  CB  . MET A 1 1   ? 28.31700 -10.97000 43.79300 1.000 33.16000 ? 1   MET A CB  1 
ATOM   6    C  CG  . MET A 1 1   ? 28.09900 -12.29300 43.11500 1.000 44.86000 ? 1   MET A CG  1 
ATOM   7    S  SD  . MET A 1 1   ? 28.52700 -13.60800 44.28300 1.000 53.21000 ? 1   MET A SD  1 
ATOM   8    C  CE  . MET A 1 1   ? 28.60300 -12.64600 45.75500 1.000 26.02000 ? 1   MET A CE  1 
ATOM   9    N  N   . ARG A 1 2   ? 26.41900 -8.50500  44.38600 1.000 23.80000 ? 2   ARG A N   1 
ATOM   10   C  CA  . ARG A 1 2   ? 26.02700 -7.51400  45.37300 1.000 27.78000 ? 2   ARG A CA  1 
ATOM   11   C  C   . ARG A 1 2   ? 26.14200 -8.12100  46.76700 1.000 26.16000 ? 2   ARG A C   1 
ATOM   12   O  O   . ARG A 1 2   ? 25.63100 -9.22200  47.01500 1.000 27.31000 ? 2   ARG A O   1 
ATOM   13   C  CB  . ARG A 1 2   ? 24.60600 -7.04000  45.08500 1.000 27.03000 ? 2   ARG A CB  1 
ATOM   14   C  CG  . ARG A 1 2   ? 24.51100 -6.30800  43.75700 1.000 29.40000 ? 2   ARG A CG  1 
ATOM   15   C  CD  . ARG A 1 2   ? 23.08000 -6.15400  43.28500 1.000 37.36000 ? 2   ARG A CD  1 
ATOM   16   N  NE  . ARG A 1 2   ? 22.40700 -7.45000  43.27800 1.000 44.33000 ? 2   ARG A NE  1 
ATOM   17   C  CZ  . ARG A 1 2   ? 21.12000 -7.63100  42.99100 1.000 42.66000 ? 2   ARG A CZ  1 
ATOM   18   N  NH1 . ARG A 1 2   ? 20.36000 -6.59600  42.66600 1.000 36.40000 ? 2   ARG A NH1 1 
ATOM   19   N  NH2 . ARG A 1 2   ? 20.59700 -8.85500  43.03200 1.000 39.72000 ? 2   ARG A NH2 1 
ATOM   20   N  N   . VAL A 1 3   ? 26.82800 -7.41600  47.67200 1.000 22.62000 ? 3   VAL A N   1 
ATOM   21   C  CA  . VAL A 1 3   ? 27.08400 -7.94300  49.00500 1.000 27.65000 ? 3   VAL A CA  1 
ATOM   22   C  C   . VAL A 1 3   ? 26.59200 -6.95000  50.05100 1.000 24.54000 ? 3   VAL A C   1 
ATOM   23   O  O   . VAL A 1 3   ? 26.72600 -5.73100  49.90500 1.000 23.45000 ? 3   VAL A O   1 
ATOM   24   C  CB  . VAL A 1 3   ? 28.57100 -8.30300  49.24100 1.000 27.63000 ? 3   VAL A CB  1 
ATOM   25   C  CG1 . VAL A 1 3   ? 29.43500 -7.09300  49.16500 1.000 31.06000 ? 3   VAL A CG1 1 
ATOM   26   C  CG2 . VAL A 1 3   ? 28.74700 -8.98600  50.60500 1.000 24.58000 ? 3   VAL A CG2 1 
ATOM   27   N  N   . ARG A 1 4   ? 26.01400 -7.50400  51.09900 1.000 25.11000 ? 4   ARG A N   1 
ATOM   28   C  CA  . ARG A 1 4   ? 25.49100 -6.82900  52.27700 1.000 25.37000 ? 4   ARG A CA  1 
ATOM   29   C  C   . ARG A 1 4   ? 26.34300 -7.27100  53.46200 1.000 26.43000 ? 4   ARG A C   1 
ATOM   30   O  O   . ARG A 1 4   ? 26.53600 -8.47700  53.64700 1.000 23.10000 ? 4   ARG A O   1 
ATOM   31   C  CB  . ARG A 1 4   ? 24.04800 -7.29000  52.42500 1.000 28.69000 ? 4   ARG A CB  1 
ATOM   32   C  CG  . ARG A 1 4   ? 23.20100 -6.70000  53.44300 1.000 36.19000 ? 4   ARG A CG  1 
ATOM   33   C  CD  . ARG A 1 4   ? 21.79900 -7.10400  53.07300 1.000 34.89000 ? 4   ARG A CD  1 
ATOM   34   N  NE  . ARG A 1 4   ? 21.47600 -8.49600  53.34500 1.000 30.68000 ? 4   ARG A NE  1 
ATOM   35   C  CZ  . ARG A 1 4   ? 20.22900 -8.91200  53.53100 1.000 31.38000 ? 4   ARG A CZ  1 
ATOM   36   N  NH1 . ARG A 1 4   ? 19.22300 -8.03000  53.46200 1.000 29.99000 ? 4   ARG A NH1 1 
ATOM   37   N  NH2 . ARG A 1 4   ? 19.98400 -10.18700 53.77900 1.000 24.84000 ? 4   ARG A NH2 1 
ATOM   38   N  N   . ILE A 1 5   ? 26.87200 -6.31600  54.24800 1.000 26.13000 ? 5   ILE A N   1 
ATOM   39   C  CA  . ILE A 1 5   ? 27.78800 -6.62100  55.34800 1.000 27.43000 ? 5   ILE A CA  1 
ATOM   40   C  C   . ILE A 1 5   ? 27.29700 -5.96100  56.64000 1.000 28.53000 ? 5   ILE A C   1 
ATOM   41   O  O   . ILE A 1 5   ? 26.96800 -4.76900  56.64900 1.000 22.87000 ? 5   ILE A O   1 
ATOM   42   C  CB  . ILE A 1 5   ? 29.23100 -6.17000  55.03800 1.000 28.13000 ? 5   ILE A CB  1 
ATOM   43   C  CG1 . ILE A 1 5   ? 29.68400 -6.71500  53.68400 1.000 24.60000 ? 5   ILE A CG1 1 
ATOM   44   C  CG2 . ILE A 1 5   ? 30.16600 -6.65500  56.13600 1.000 25.28000 ? 5   ILE A CG2 1 
ATOM   45   C  CD1 . ILE A 1 5   ? 30.76700 -5.93500  53.02900 1.000 25.29000 ? 5   ILE A CD1 1 
ATOM   46   N  N   . ARG A 1 6   ? 27.28100 -6.74100  57.73700 1.000 27.55000 ? 6   ARG A N   1 
ATOM   47   C  CA  . ARG A 1 6   ? 26.91300 -6.28300  59.07700 1.000 28.37000 ? 6   ARG A CA  1 
ATOM   48   C  C   . ARG A 1 6   ? 27.89500 -6.83500  60.11300 1.000 27.78000 ? 6   ARG A C   1 
ATOM   49   O  O   . ARG A 1 6   ? 28.47800 -7.90400  59.93100 1.000 20.63000 ? 6   ARG A O   1 
ATOM   50   C  CB  . ARG A 1 6   ? 25.49100 -6.73100  59.45800 1.000 23.08000 ? 6   ARG A CB  1 
ATOM   51   C  CG  . ARG A 1 6   ? 24.37900 -5.93400  58.78200 1.000 44.62000 ? 6   ARG A CG  1 
ATOM   52   C  CD  . ARG A 1 6   ? 24.58800 -4.41300  58.92800 1.000 45.16000 ? 6   ARG A CD  1 
ATOM   53   N  NE  . ARG A 1 6   ? 23.48300 -3.61300  58.38400 1.000 45.45000 ? 6   ARG A NE  1 
ATOM   54   C  CZ  . ARG A 1 6   ? 23.42600 -3.13100  57.13900 1.000 49.53000 ? 6   ARG A CZ  1 
ATOM   55   N  NH1 . ARG A 1 6   ? 24.41600 -3.36000  56.28100 1.000 43.21000 ? 6   ARG A NH1 1 
ATOM   56   N  NH2 . ARG A 1 6   ? 22.36800 -2.42200  56.74500 1.000 47.80000 ? 6   ARG A NH2 1 
ATOM   57   N  N   . GLY A 1 7   ? 28.04100 -6.12900  61.22000 1.000 25.90000 ? 7   GLY A N   1 
ATOM   58   C  CA  . GLY A 1 7   ? 28.76100 -6.67000  62.36200 1.000 27.43000 ? 7   GLY A CA  1 
ATOM   59   C  C   . GLY A 1 7   ? 30.05500 -5.92000  62.61600 1.000 27.11000 ? 7   GLY A C   1 
ATOM   60   O  O   . GLY A 1 7   ? 30.36900 -4.92200  61.95800 1.000 23.11000 ? 7   GLY A O   1 
ATOM   61   N  N   . ILE A 1 8   ? 30.82800 -6.43200  63.58400 1.000 23.56000 ? 8   ILE A N   1 
ATOM   62   C  CA  . ILE A 1 8   ? 31.99100 -5.67500  64.05300 1.000 27.56000 ? 8   ILE A CA  1 
ATOM   63   C  C   . ILE A 1 8   ? 33.09600 -5.62800  63.01100 1.000 24.87000 ? 8   ILE A C   1 
ATOM   64   O  O   . ILE A 1 8   ? 33.99300 -4.79000  63.11600 1.000 25.26000 ? 8   ILE A O   1 
ATOM   65   C  CB  . ILE A 1 8   ? 32.57900 -6.20800  65.38200 1.000 26.25000 ? 8   ILE A CB  1 
ATOM   66   C  CG1 . ILE A 1 8   ? 32.96000 -7.68100  65.25500 1.000 32.46000 ? 8   ILE A CG1 1 
ATOM   67   C  CG2 . ILE A 1 8   ? 31.61900 -5.94800  66.53800 1.000 22.23000 ? 8   ILE A CG2 1 
ATOM   68   C  CD1 . ILE A 1 8   ? 33.72600 -8.20400  66.44600 1.000 31.02000 ? 8   ILE A CD1 1 
ATOM   69   N  N   . TYR A 1 9   ? 33.06000 -6.49400  62.00000 1.000 24.81000 ? 9   TYR A N   1 
ATOM   70   C  CA  . TYR A 1 9   ? 34.07800 -6.48500  60.95900 1.000 25.26000 ? 9   TYR A CA  1 
ATOM   71   C  C   . TYR A 1 9   ? 33.66000 -5.68100  59.72500 1.000 25.18000 ? 9   TYR A C   1 
ATOM   72   O  O   . TYR A 1 9   ? 34.37000 -5.71200  58.71000 1.000 23.29000 ? 9   TYR A O   1 
ATOM   73   C  CB  . TYR A 1 9   ? 34.42300 -7.92700  60.57100 1.000 26.02000 ? 9   TYR A CB  1 
ATOM   74   C  CG  . TYR A 1 9   ? 34.76800 -8.79200  61.76100 1.000 27.34000 ? 9   TYR A CG  1 
ATOM   75   C  CD1 . TYR A 1 9   ? 36.03200 -8.72500  62.35800 1.000 28.93000 ? 9   TYR A CD1 1 
ATOM   76   C  CD2 . TYR A 1 9   ? 33.83200 -9.67700  62.30000 1.000 30.59000 ? 9   TYR A CD2 1 
ATOM   77   C  CE1 . TYR A 1 9   ? 36.34600 -9.52600  63.46100 1.000 26.43000 ? 9   TYR A CE1 1 
ATOM   78   C  CE2 . TYR A 1 9   ? 34.14400 -10.48000 63.39800 1.000 27.31000 ? 9   TYR A CE2 1 
ATOM   79   C  CZ  . TYR A 1 9   ? 35.39400 -10.39100 63.97000 1.000 27.62000 ? 9   TYR A CZ  1 
ATOM   80   O  OH  . TYR A 1 9   ? 35.69500 -11.17900 65.05300 1.000 28.12000 ? 9   TYR A OH  1 
ATOM   81   N  N   . ALA A 1 10  ? 32.54600 -4.93900  59.80100 1.000 21.60000 ? 10  ALA A N   1 
ATOM   82   C  CA  . ALA A 1 10  ? 31.87300 -4.47600  58.58000 1.000 25.80000 ? 10  ALA A CA  1 
ATOM   83   C  C   . ALA A 1 10  ? 32.71300 -3.46200  57.80200 1.000 22.30000 ? 10  ALA A C   1 
ATOM   84   O  O   . ALA A 1 10  ? 32.73900 -3.50000  56.57500 1.000 25.12000 ? 10  ALA A O   1 
ATOM   85   C  CB  . ALA A 1 10  ? 30.49700 -3.88700  58.91400 1.000 23.16000 ? 10  ALA A CB  1 
ATOM   86   N  N   . THR A 1 11  ? 33.41300 -2.55400  58.48400 1.000 24.84000 ? 11  THR A N   1 
ATOM   87   C  CA  . THR A 1 11  ? 34.21900 -1.58000  57.75200 1.000 27.98000 ? 11  THR A CA  1 
ATOM   88   C  C   . THR A 1 11  ? 35.37100 -2.26900  57.03600 1.000 26.08000 ? 11  THR A C   1 
ATOM   89   O  O   . THR A 1 11  ? 35.55100 -2.10000  55.82400 1.000 24.61000 ? 11  THR A O   1 
ATOM   90   C  CB  . THR A 1 11  ? 34.73300 -0.48000  58.68800 1.000 26.55000 ? 11  THR A CB  1 
ATOM   91   O  OG1 . THR A 1 11  ? 33.61700 0.30200   59.13400 1.000 29.07000 ? 11  THR A OG1 1 
ATOM   92   C  CG2 . THR A 1 11  ? 35.68100 0.45000   57.95900 1.000 23.45000 ? 11  THR A CG2 1 
ATOM   93   N  N   . ALA A 1 12  ? 36.14000 -3.08400  57.76100 1.000 26.83000 ? 12  ALA A N   1 
ATOM   94   C  CA  . ALA A 1 12  ? 37.25300 -3.78100  57.12400 1.000 25.78000 ? 12  ALA A CA  1 
ATOM   95   C  C   . ALA A 1 12  ? 36.76300 -4.68800  56.00400 1.000 26.70000 ? 12  ALA A C   1 
ATOM   96   O  O   . ALA A 1 12  ? 37.38900 -4.76700  54.93800 1.000 26.17000 ? 12  ALA A O   1 
ATOM   97   C  CB  . ALA A 1 12  ? 38.04800 -4.58200  58.16200 1.000 30.97000 ? 12  ALA A CB  1 
ATOM   98   N  N   . LEU A 1 13  ? 35.63400 -5.36700  56.21400 1.000 25.85000 ? 13  LEU A N   1 
ATOM   99   C  CA  . LEU A 1 13  ? 35.12300 -6.26200  55.18300 1.000 24.89000 ? 13  LEU A CA  1 
ATOM   100  C  C   . LEU A 1 13  ? 34.62100 -5.48200  53.97900 1.000 25.27000 ? 13  LEU A C   1 
ATOM   101  O  O   . LEU A 1 13  ? 34.72800 -5.95800  52.84500 1.000 23.72000 ? 13  LEU A O   1 
ATOM   102  C  CB  . LEU A 1 13  ? 34.01200 -7.15500  55.73300 1.000 29.24000 ? 13  LEU A CB  1 
ATOM   103  C  CG  . LEU A 1 13  ? 34.42900 -8.32500  56.65000 1.000 34.70000 ? 13  LEU A CG  1 
ATOM   104  C  CD1 . LEU A 1 13  ? 33.20700 -8.95500  57.26500 1.000 25.19000 ? 13  LEU A CD1 1 
ATOM   105  C  CD2 . LEU A 1 13  ? 35.25100 -9.38600  55.90000 1.000 30.47000 ? 13  LEU A CD2 1 
ATOM   106  N  N   . THR A 1 14  ? 34.05300 -4.29200  54.20200 1.000 23.36000 ? 14  THR A N   1 
ATOM   107  C  CA  . THR A 1 14  ? 33.56900 -3.49000  53.08200 1.000 24.19000 ? 14  THR A CA  1 
ATOM   108  C  C   . THR A 1 14  ? 34.72400 -3.06400  52.18300 1.000 29.60000 ? 14  THR A C   1 
ATOM   109  O  O   . THR A 1 14  ? 34.62900 -3.14400  50.95000 1.000 29.02000 ? 14  THR A O   1 
ATOM   110  C  CB  . THR A 1 14  ? 32.79900 -2.28300  53.60900 1.000 27.32000 ? 14  THR A CB  1 
ATOM   111  O  OG1 . THR A 1 14  ? 31.60400 -2.75100  54.24300 1.000 27.73000 ? 14  THR A OG1 1 
ATOM   112  C  CG2 . THR A 1 14  ? 32.41000 -1.32300  52.48000 1.000 24.95000 ? 14  THR A CG2 1 
ATOM   113  N  N   . TYR A 1 15  ? 35.83500 -2.65200  52.78900 1.000 25.89000 ? 15  TYR A N   1 
ATOM   114  C  CA  . TYR A 1 15  ? 37.03600 -2.31200  52.04100 1.000 28.15000 ? 15  TYR A CA  1 
ATOM   115  C  C   . TYR A 1 15  ? 37.50400 -3.48900  51.19300 1.000 29.87000 ? 15  TYR A C   1 
ATOM   116  O  O   . TYR A 1 15  ? 37.75400 -3.34300  49.99100 1.000 32.24000 ? 15  TYR A O   1 
ATOM   117  C  CB  . TYR A 1 15  ? 38.12800 -1.88100  53.02500 1.000 28.74000 ? 15  TYR A CB  1 
ATOM   118  C  CG  . TYR A 1 15  ? 39.41500 -1.41600  52.38800 1.000 34.87000 ? 15  TYR A CG  1 
ATOM   119  C  CD1 . TYR A 1 15  ? 40.38700 -2.33400  51.96700 1.000 35.38000 ? 15  TYR A CD1 1 
ATOM   120  C  CD2 . TYR A 1 15  ? 39.67900 -0.06200  52.22500 1.000 35.20000 ? 15  TYR A CD2 1 
ATOM   121  C  CE1 . TYR A 1 15  ? 41.57600 -1.90900  51.39100 1.000 30.40000 ? 15  TYR A CE1 1 
ATOM   122  C  CE2 . TYR A 1 15  ? 40.88100 0.36500   51.65300 1.000 38.55000 ? 15  TYR A CE2 1 
ATOM   123  C  CZ  . TYR A 1 15  ? 41.81100 -0.56400  51.24100 1.000 34.35000 ? 15  TYR A CZ  1 
ATOM   124  O  OH  . TYR A 1 15  ? 42.98500 -0.12900  50.68100 1.000 46.51000 ? 15  TYR A OH  1 
ATOM   125  N  N   . LEU A 1 16  ? 37.61400 -4.67200  51.80500 1.000 28.58000 ? 16  LEU A N   1 
ATOM   126  C  CA  . LEU A 1 16  ? 38.16900 -5.83100  51.10300 1.000 31.89000 ? 16  LEU A CA  1 
ATOM   127  C  C   . LEU A 1 16  ? 37.23500 -6.32400  50.00100 1.000 33.41000 ? 16  LEU A C   1 
ATOM   128  O  O   . LEU A 1 16  ? 37.69900 -6.74800  48.93900 1.000 33.74000 ? 16  LEU A O   1 
ATOM   129  C  CB  . LEU A 1 16  ? 38.47300 -6.96100  52.09000 1.000 23.36000 ? 16  LEU A CB  1 
ATOM   130  C  CG  . LEU A 1 16  ? 39.60400 -6.69200  53.08400 1.000 30.63000 ? 16  LEU A CG  1 
ATOM   131  C  CD1 . LEU A 1 16  ? 39.59500 -7.73600  54.19400 1.000 27.51000 ? 16  LEU A CD1 1 
ATOM   132  C  CD2 . LEU A 1 16  ? 40.94000 -6.69400  52.34600 1.000 27.06000 ? 16  LEU A CD2 1 
ATOM   133  N  N   . PHE A 1 17  ? 35.92100 -6.29900  50.22800 1.000 29.56000 ? 17  PHE A N   1 
ATOM   134  C  CA  . PHE A 1 17  ? 35.01800 -6.72700  49.15700 1.000 31.52000 ? 17  PHE A CA  1 
ATOM   135  C  C   . PHE A 1 17  ? 35.05100 -5.74800  47.98800 1.000 34.36000 ? 17  PHE A C   1 
ATOM   136  O  O   . PHE A 1 17  ? 35.07700 -6.16200  46.82600 1.000 34.72000 ? 17  PHE A O   1 
ATOM   137  C  CB  . PHE A 1 17  ? 33.59000 -6.87800  49.67600 1.000 25.80000 ? 17  PHE A CB  1 
ATOM   138  C  CG  . PHE A 1 17  ? 33.30300 -8.21200  50.28100 1.000 33.02000 ? 17  PHE A CG  1 
ATOM   139  C  CD1 . PHE A 1 17  ? 32.89700 -9.27200  49.49000 1.000 28.60000 ? 17  PHE A CD1 1 
ATOM   140  C  CD2 . PHE A 1 17  ? 33.42300 -8.40200  51.64500 1.000 27.83000 ? 17  PHE A CD2 1 
ATOM   141  C  CE1 . PHE A 1 17  ? 32.63500 -10.49900 50.04100 1.000 34.02000 ? 17  PHE A CE1 1 
ATOM   142  C  CE2 . PHE A 1 17  ? 33.15600 -9.62600  52.20200 1.000 30.15000 ? 17  PHE A CE2 1 
ATOM   143  C  CZ  . PHE A 1 17  ? 32.76300 -10.68000 51.39700 1.000 32.42000 ? 17  PHE A CZ  1 
ATOM   144  N  N   . LEU A 1 18  ? 35.02200 -4.44800  48.27800 1.000 31.07000 ? 18  LEU A N   1 
ATOM   145  C  CA  . LEU A 1 18  ? 35.16700 -3.44000  47.23300 1.000 32.80000 ? 18  LEU A CA  1 
ATOM   146  C  C   . LEU A 1 18  ? 36.44400 -3.67400  46.44300 1.000 39.20000 ? 18  LEU A C   1 
ATOM   147  O  O   . LEU A 1 18  ? 36.41700 -3.85200  45.22100 1.000 38.46000 ? 18  LEU A O   1 
ATOM   148  C  CB  . LEU A 1 18  ? 35.20000 -2.05500  47.86100 1.000 32.47000 ? 18  LEU A CB  1 
ATOM   149  C  CG  . LEU A 1 18  ? 33.91400 -1.29600  48.12000 1.000 32.81000 ? 18  LEU A CG  1 
ATOM   150  C  CD1 . LEU A 1 18  ? 34.30400 -0.02100  48.83900 1.000 36.44000 ? 18  LEU A CD1 1 
ATOM   151  C  CD2 . LEU A 1 18  ? 33.16300 -0.99100  46.80700 1.000 38.29000 ? 18  LEU A CD2 1 
ATOM   152  N  N   . LYS A 1 19  ? 37.57700 -3.71100  47.15100 1.000 40.79000 ? 19  LYS A N   1 
ATOM   153  C  CA  . LYS A 1 19  ? 38.87500 -3.94100  46.52900 1.000 44.79000 ? 19  LYS A CA  1 
ATOM   154  C  C   . LYS A 1 19  ? 38.86500 -5.14500  45.59400 1.000 44.83000 ? 19  LYS A C   1 
ATOM   155  O  O   . LYS A 1 19  ? 39.67100 -5.20200  44.66000 1.000 48.77000 ? 19  LYS A O   1 
ATOM   156  C  CB  . LYS A 1 19  ? 39.94200 -4.09400  47.63100 1.000 42.10000 ? 19  LYS A CB  1 
ATOM   157  C  CG  . LYS A 1 19  ? 41.06500 -5.08400  47.30900 1.000 49.97000 ? 19  LYS A CG  1 
ATOM   158  C  CD  . LYS A 1 19  ? 42.26600 -4.93000  48.23400 1.000 50.99000 ? 19  LYS A CD  1 
ATOM   159  C  CE  . LYS A 1 19  ? 43.10300 -6.21300  48.27000 1.000 52.84000 ? 19  LYS A CE  1 
ATOM   160  N  NZ  . LYS A 1 19  ? 44.55000 -5.91500  48.40000 1.000 47.96000 ? 19  LYS A NZ  1 
ATOM   161  N  N   . ASN A 1 20  ? 37.94900 -6.08700  45.79100 1.000 44.88000 ? 20  ASN A N   1 
ATOM   162  C  CA  . ASN A 1 20  ? 37.87800 -7.28500  44.96900 1.000 41.59000 ? 20  ASN A CA  1 
ATOM   163  C  C   . ASN A 1 20  ? 36.70300 -7.29300  44.00100 1.000 33.97000 ? 20  ASN A C   1 
ATOM   164  O  O   . ASN A 1 20  ? 36.32600 -8.36100  43.50700 1.000 42.67000 ? 20  ASN A O   1 
ATOM   165  C  CB  . ASN A 1 20  ? 37.82000 -8.50900  45.86700 1.000 38.03000 ? 20  ASN A CB  1 
ATOM   166  C  CG  . ASN A 1 20  ? 39.16800 -8.83700  46.47000 1.000 54.55000 ? 20  ASN A CG  1 
ATOM   167  O  OD1 . ASN A 1 20  ? 39.98800 -9.52300  45.84800 1.000 57.91000 ? 20  ASN A OD1 1 
ATOM   168  N  ND2 . ASN A 1 20  ? 39.39800 -8.37800  47.70100 1.000 47.91000 ? 20  ASN A ND2 1 
ATOM   169  N  N   . GLY A 1 21  ? 36.10200 -6.14000  43.73100 1.000 34.76000 ? 21  GLY A N   1 
ATOM   170  C  CA  . GLY A 1 21  ? 35.16400 -6.02100  42.63600 1.000 38.02000 ? 21  GLY A CA  1 
ATOM   171  C  C   . GLY A 1 21  ? 33.70100 -6.23700  42.95600 1.000 34.05000 ? 21  GLY A C   1 
ATOM   172  O  O   . GLY A 1 21  ? 32.88300 -6.16200  42.03600 1.000 34.45000 ? 21  GLY A O   1 
ATOM   173  N  N   . PHE A 1 22  ? 33.34500 -6.50200  44.21200 1.000 30.04000 ? 22  PHE A N   1 
ATOM   174  C  CA  . PHE A 1 22  ? 31.94500 -6.64900  44.59500 1.000 34.94000 ? 22  PHE A CA  1 
ATOM   175  C  C   . PHE A 1 22  ? 31.24300 -5.29600  44.65500 1.000 33.51000 ? 22  PHE A C   1 
ATOM   176  O  O   . PHE A 1 22  ? 31.84600 -4.26700  44.97300 1.000 31.51000 ? 22  PHE A O   1 
ATOM   177  C  CB  . PHE A 1 22  ? 31.81400 -7.31400  45.97600 1.000 32.05000 ? 22  PHE A CB  1 
ATOM   178  C  CG  . PHE A 1 22  ? 32.21100 -8.76100  46.01400 1.000 29.35000 ? 22  PHE A CG  1 
ATOM   179  C  CD1 . PHE A 1 22  ? 33.53700 -9.13500  45.92400 1.000 36.48000 ? 22  PHE A CD1 1 
ATOM   180  C  CD2 . PHE A 1 22  ? 31.25900 -9.74600  46.17500 1.000 41.69000 ? 22  PHE A CD2 1 
ATOM   181  C  CE1 . PHE A 1 22  ? 33.91100 -10.46500 45.96200 1.000 37.72000 ? 22  PHE A CE1 1 
ATOM   182  C  CE2 . PHE A 1 22  ? 31.63400 -11.09800 46.22300 1.000 45.60000 ? 22  PHE A CE2 1 
ATOM   183  C  CZ  . PHE A 1 22  ? 32.95700 -11.44800 46.11800 1.000 35.82000 ? 22  PHE A CZ  1 
ATOM   184  N  N   . GLU A 1 23  ? 29.93600 -5.31900  44.39900 1.000 29.17000 ? 23  GLU A N   1 
ATOM   185  C  CA  . GLU A 1 23  ? 29.07200 -4.17400  44.62700 1.000 31.75000 ? 23  GLU A CA  1 
ATOM   186  C  C   . GLU A 1 23  ? 28.55700 -4.20800  46.06800 1.000 31.40000 ? 23  GLU A C   1 
ATOM   187  O  O   . GLU A 1 23  ? 27.96200 -5.20500  46.49900 1.000 33.24000 ? 23  GLU A O   1 
ATOM   188  C  CB  . GLU A 1 23  ? 27.90900 -4.19500  43.63000 1.000 31.22000 ? 23  GLU A CB  1 
ATOM   189  C  CG  . GLU A 1 23  ? 27.12500 -2.89300  43.53900 1.000 45.10000 ? 23  GLU A CG  1 
ATOM   190  C  CD  . GLU A 1 23  ? 26.01300 -2.93900  42.48000 1.000 58.36000 ? 23  GLU A CD  1 
ATOM   191  O  OE1 . GLU A 1 23  ? 26.03900 -3.83100  41.59200 1.000 57.17000 ? 23  GLU A OE1 1 
ATOM   192  O  OE2 . GLU A 1 23  ? 25.11600 -2.06900  42.53000 1.000 65.11000 ? 23  GLU A OE2 1 
ATOM   193  N  N   . ILE A 1 24  ? 28.79400 -3.13700  46.81400 1.000 31.88000 ? 24  ILE A N   1 
ATOM   194  C  CA  . ILE A 1 24  ? 28.28000 -3.01900  48.17900 1.000 28.91000 ? 24  ILE A CA  1 
ATOM   195  C  C   . ILE A 1 24  ? 26.88000 -2.43200  48.12800 1.000 27.50000 ? 24  ILE A C   1 
ATOM   196  O  O   . ILE A 1 24  ? 26.66400 -1.38300  47.51500 1.000 29.92000 ? 24  ILE A O   1 
ATOM   197  C  CB  . ILE A 1 24  ? 29.19600 -2.13800  49.04700 1.000 26.59000 ? 24  ILE A CB  1 
ATOM   198  C  CG1 . ILE A 1 24  ? 30.64800 -2.56400  48.91100 1.000 27.80000 ? 24  ILE A CG1 1 
ATOM   199  C  CG2 . ILE A 1 24  ? 28.75400 -2.20000  50.49800 1.000 31.71000 ? 24  ILE A CG2 1 
ATOM   200  C  CD1 . ILE A 1 24  ? 30.88000 -4.01200  49.24200 1.000 28.11000 ? 24  ILE A CD1 1 
ATOM   201  N  N   . VAL A 1 25  ? 25.93300 -3.06700  48.81200 1.000 23.49000 ? 25  VAL A N   1 
ATOM   202  C  CA  . VAL A 1 25  ? 24.57400 -2.55600  48.86900 1.000 27.02000 ? 25  VAL A CA  1 
ATOM   203  C  C   . VAL A 1 25  ? 24.09300 -2.53900  50.31600 1.000 32.40000 ? 25  VAL A C   1 
ATOM   204  O  O   . VAL A 1 25  ? 24.71200 -3.11500  51.22000 1.000 25.02000 ? 25  VAL A O   1 
ATOM   205  C  CB  . VAL A 1 25  ? 23.58900 -3.37300  48.00200 1.000 26.11000 ? 25  VAL A CB  1 
ATOM   206  C  CG1 . VAL A 1 25  ? 24.11300 -3.51300  46.55200 1.000 25.23000 ? 25  VAL A CG1 1 
ATOM   207  C  CG2 . VAL A 1 25  ? 23.33800 -4.72900  48.63500 1.000 24.52000 ? 25  VAL A CG2 1 
ATOM   208  N  N   . GLN A 1 26  ? 22.96500 -1.84900  50.51200 1.000 25.26000 ? 26  GLN A N   1 
ATOM   209  C  CA  . GLN A 1 26  ? 22.29900 -1.73700  51.80600 1.000 26.66000 ? 26  GLN A CA  1 
ATOM   210  C  C   . GLN A 1 26  ? 23.26600 -1.27200  52.88800 1.000 27.80000 ? 26  GLN A C   1 
ATOM   211  O  O   . GLN A 1 26  ? 23.26100 -1.77200  54.01000 1.000 27.25000 ? 26  GLN A O   1 
ATOM   212  C  CB  . GLN A 1 26  ? 21.63000 -3.05700  52.17900 1.000 24.46000 ? 26  GLN A CB  1 
ATOM   213  C  CG  . GLN A 1 26  ? 20.69800 -3.53100  51.07600 1.000 26.66000 ? 26  GLN A CG  1 
ATOM   214  C  CD  . GLN A 1 26  ? 19.99700 -4.82900  51.40800 1.000 30.49000 ? 26  GLN A CD  1 
ATOM   215  O  OE1 . GLN A 1 26  ? 19.63200 -5.06700  52.55700 1.000 27.99000 ? 26  GLN A OE1 1 
ATOM   216  N  NE2 . GLN A 1 26  ? 19.81700 -5.68800  50.39900 1.000 30.27000 ? 26  GLN A NE2 1 
ATOM   217  N  N   . GLN A 1 27  ? 24.12300 -0.31900  52.53200 1.000 27.67000 ? 27  GLN A N   1 
ATOM   218  C  CA  . GLN A 1 27  ? 25.01200 0.28100   53.51200 1.000 27.04000 ? 27  GLN A CA  1 
ATOM   219  C  C   . GLN A 1 27  ? 24.19700 1.03100   54.55900 1.000 34.16000 ? 27  GLN A C   1 
ATOM   220  O  O   . GLN A 1 27  ? 23.16600 1.63600   54.25100 1.000 30.04000 ? 27  GLN A O   1 
ATOM   221  C  CB  . GLN A 1 27  ? 25.97400 1.26300   52.84200 1.000 29.20000 ? 27  GLN A CB  1 
ATOM   222  C  CG  . GLN A 1 27  ? 26.84200 0.70200   51.73700 1.000 29.65000 ? 27  GLN A CG  1 
ATOM   223  C  CD  . GLN A 1 27  ? 26.24600 0.91600   50.35300 1.000 32.37000 ? 27  GLN A CD  1 
ATOM   224  O  OE1 . GLN A 1 27  ? 25.03000 0.81200   50.15200 1.000 31.08000 ? 27  GLN A OE1 1 
ATOM   225  N  NE2 . GLN A 1 27  ? 27.10600 1.20500   49.38300 1.000 35.26000 ? 27  GLN A NE2 1 
ATOM   226  N  N   . THR A 1 28  ? 24.67900 1.01500   55.79500 1.000 33.78000 ? 28  THR A N   1 
ATOM   227  C  CA  . THR A 1 28  ? 24.23200 1.98100   56.77800 1.000 35.60000 ? 28  THR A CA  1 
ATOM   228  C  C   . THR A 1 28  ? 24.76500 3.36600   56.40900 1.000 36.97000 ? 28  THR A C   1 
ATOM   229  O  O   . THR A 1 28  ? 25.75200 3.48300   55.67800 1.000 31.41000 ? 28  THR A O   1 
ATOM   230  C  CB  . THR A 1 28  ? 24.73800 1.59000   58.15700 1.000 40.36000 ? 28  THR A CB  1 
ATOM   231  O  OG1 . THR A 1 28  ? 26.16900 1.70000   58.16200 1.000 36.65000 ? 28  THR A OG1 1 
ATOM   232  C  CG2 . THR A 1 28  ? 24.32300 0.15100   58.49300 1.000 35.09000 ? 28  THR A CG2 1 
ATOM   233  N  N   . PRO A 1 29  ? 24.13200 4.43800   56.90400 1.000 37.56000 ? 29  PRO A N   1 
ATOM   234  C  CA  . PRO A 1 29  ? 24.64500 5.78100   56.58100 1.000 33.64000 ? 29  PRO A CA  1 
ATOM   235  C  C   . PRO A 1 29  ? 26.06200 5.99800   57.06100 1.000 30.73000 ? 29  PRO A C   1 
ATOM   236  O  O   . PRO A 1 29  ? 26.80200 6.79600   56.47900 1.000 37.45000 ? 29  PRO A O   1 
ATOM   237  C  CB  . PRO A 1 29  ? 23.65900 6.72100   57.29500 1.000 30.08000 ? 29  PRO A CB  1 
ATOM   238  C  CG  . PRO A 1 29  ? 22.44700 5.87700   57.55300 1.000 33.74000 ? 29  PRO A CG  1 
ATOM   239  C  CD  . PRO A 1 29  ? 22.94800 4.50000   57.78100 1.000 32.31000 ? 29  PRO A CD  1 
ATOM   240  N  N   . GLN A 1 30  ? 26.46600 5.30800   58.11800 1.000 36.51000 ? 30  GLN A N   1 
ATOM   241  C  CA  . GLN A 1 30  ? 27.81700 5.48400   58.62700 1.000 35.17000 ? 30  GLN A CA  1 
ATOM   242  C  C   . GLN A 1 30  ? 28.83800 4.77300   57.75200 1.000 33.98000 ? 30  GLN A C   1 
ATOM   243  O  O   . GLN A 1 30  ? 29.95800 5.26300   57.58600 1.000 36.20000 ? 30  GLN A O   1 
ATOM   244  C  CB  . GLN A 1 30  ? 27.89700 4.99400   60.07400 1.000 34.63000 ? 30  GLN A CB  1 
ATOM   245  C  CG  . GLN A 1 30  ? 27.15000 5.89600   61.05400 1.000 30.35000 ? 30  GLN A CG  1 
ATOM   246  C  CD  . GLN A 1 30  ? 25.63500 5.72300   61.01000 1.000 37.46000 ? 30  GLN A CD  1 
ATOM   247  O  OE1 . GLN A 1 30  ? 25.10600 4.79400   60.38500 1.000 37.49000 ? 30  GLN A OE1 1 
ATOM   248  N  NE2 . GLN A 1 30  ? 24.92800 6.61500   61.69500 1.000 43.71000 ? 30  GLN A NE2 1 
ATOM   249  N  N   . ILE A 1 31  ? 28.47900 3.63200   57.17600 1.000 35.91000 ? 31  ILE A N   1 
ATOM   250  C  CA  . ILE A 1 31  ? 29.37300 2.98500   56.22300 1.000 35.80000 ? 31  ILE A CA  1 
ATOM   251  C  C   . ILE A 1 31  ? 29.47400 3.81300   54.95300 1.000 38.99000 ? 31  ILE A C   1 
ATOM   252  O  O   . ILE A 1 31  ? 30.57400 4.05200   54.43700 1.000 38.75000 ? 31  ILE A O   1 
ATOM   253  C  CB  . ILE A 1 31  ? 28.89500 1.55400   55.92600 1.000 36.49000 ? 31  ILE A CB  1 
ATOM   254  C  CG1 . ILE A 1 31  ? 29.15700 0.67300   57.14300 1.000 34.44000 ? 31  ILE A CG1 1 
ATOM   255  C  CG2 . ILE A 1 31  ? 29.57100 1.00500   54.67800 1.000 34.33000 ? 31  ILE A CG2 1 
ATOM   256  C  CD1 . ILE A 1 31  ? 30.61300 0.62100   57.53700 1.000 36.00000 ? 31  ILE A CD1 1 
ATOM   257  N  N   . ALA A 1 32  ? 28.32500 4.24800   54.42500 1.000 32.69000 ? 32  ALA A N   1 
ATOM   258  C  CA  . ALA A 1 32  ? 28.31600 5.11500   53.25000 1.000 42.17000 ? 32  ALA A CA  1 
ATOM   259  C  C   . ALA A 1 32  ? 29.27000 6.28600   53.42800 1.000 42.43000 ? 32  ALA A C   1 
ATOM   260  O  O   . ALA A 1 32  ? 30.08800 6.58200   52.54900 1.000 41.16000 ? 32  ALA A O   1 
ATOM   261  C  CB  . ALA A 1 32  ? 26.89900 5.62100   52.98200 1.000 35.90000 ? 32  ALA A CB  1 
ATOM   262  N  N   . GLU A 1 33  ? 29.19900 6.94800   54.58300 1.000 39.90000 ? 33  GLU A N   1 
ATOM   263  C  CA  . GLU A 1 33  ? 30.01000 8.13800   54.78900 1.000 35.72000 ? 33  GLU A CA  1 
ATOM   264  C  C   . GLU A 1 33  ? 31.49400 7.79500   54.83000 1.000 37.28000 ? 33  GLU A C   1 
ATOM   265  O  O   . GLU A 1 33  ? 32.32100 8.55200   54.30900 1.000 42.47000 ? 33  GLU A O   1 
ATOM   266  C  CB  . GLU A 1 33  ? 29.57700 8.83900   56.06800 1.000 36.17000 ? 33  GLU A CB  1 
ATOM   267  C  CG  . GLU A 1 33  ? 30.25500 10.17600  56.29400 1.000 46.16000 ? 33  GLU A CG  1 
ATOM   268  C  CD  . GLU A 1 33  ? 29.77400 10.86000  57.55400 1.000 51.63000 ? 33  GLU A CD  1 
ATOM   269  O  OE1 . GLU A 1 33  ? 28.96700 10.25000  58.28900 1.000 58.97000 ? 33  GLU A OE1 1 
ATOM   270  O  OE2 . GLU A 1 33  ? 30.19200 12.01100  57.80200 1.000 60.06000 ? 33  GLU A OE2 1 
ATOM   271  N  N   . ARG A 1 34  ? 31.85100 6.65600   55.43800 1.000 35.74000 ? 34  ARG A N   1 
ATOM   272  C  CA  . ARG A 1 34  ? 33.26200 6.28700   55.57600 1.000 33.88000 ? 34  ARG A CA  1 
ATOM   273  C  C   . ARG A 1 34  ? 33.90200 5.95100   54.24200 1.000 32.98000 ? 34  ARG A C   1 
ATOM   274  O  O   . ARG A 1 34  ? 35.11800 6.11700   54.08500 1.000 32.04000 ? 34  ARG A O   1 
ATOM   275  C  CB  . ARG A 1 34  ? 33.42100 5.09000   56.51400 1.000 29.92000 ? 34  ARG A CB  1 
ATOM   276  C  CG  . ARG A 1 34  ? 33.10800 5.41400   57.93700 1.000 35.02000 ? 34  ARG A CG  1 
ATOM   277  C  CD  . ARG A 1 34  ? 33.20500 4.20000   58.80200 1.000 31.81000 ? 34  ARG A CD  1 
ATOM   278  N  NE  . ARG A 1 34  ? 32.87300 4.52600   60.18100 1.000 36.49000 ? 34  ARG A NE  1 
ATOM   279  C  CZ  . ARG A 1 34  ? 32.79500 3.63200   61.16100 1.000 41.74000 ? 34  ARG A CZ  1 
ATOM   280  N  NH1 . ARG A 1 34  ? 33.02900 2.34000   60.90300 1.000 32.34000 ? 34  ARG A NH1 1 
ATOM   281  N  NH2 . ARG A 1 34  ? 32.48600 4.03000   62.39500 1.000 39.14000 ? 34  ARG A NH2 1 
ATOM   282  N  N   . PHE A 1 35  ? 33.11900 5.46100   53.28300 1.000 33.18000 ? 35  PHE A N   1 
ATOM   283  C  CA  . PHE A 1 35  ? 33.64300 5.08000   51.98000 1.000 35.43000 ? 35  PHE A CA  1 
ATOM   284  C  C   . PHE A 1 35  ? 33.22600 6.04300   50.87900 1.000 35.76000 ? 35  PHE A C   1 
ATOM   285  O  O   . PHE A 1 35  ? 33.40600 5.72700   49.69900 1.000 38.82000 ? 35  PHE A O   1 
ATOM   286  C  CB  . PHE A 1 35  ? 33.21500 3.64800   51.63300 1.000 41.37000 ? 35  PHE A CB  1 
ATOM   287  C  CG  . PHE A 1 35  ? 33.85200 2.60100   52.51300 1.000 35.37000 ? 35  PHE A CG  1 
ATOM   288  C  CD1 . PHE A 1 35  ? 35.09500 2.06500   52.19900 1.000 29.13000 ? 35  PHE A CD1 1 
ATOM   289  C  CD2 . PHE A 1 35  ? 33.21200 2.16900   53.66400 1.000 32.89000 ? 35  PHE A CD2 1 
ATOM   290  C  CE1 . PHE A 1 35  ? 35.69100 1.10900   53.03000 1.000 31.84000 ? 35  PHE A CE1 1 
ATOM   291  C  CE2 . PHE A 1 35  ? 33.80400 1.20400   54.50100 1.000 34.38000 ? 35  PHE A CE2 1 
ATOM   292  C  CZ  . PHE A 1 35  ? 35.03300 0.67900   54.18300 1.000 26.26000 ? 35  PHE A CZ  1 
ATOM   293  N  N   . PHE A 1 36  ? 32.68100 7.20600   51.24100 1.000 38.71000 ? 36  PHE A N   1 
ATOM   294  C  CA  . PHE A 1 36  ? 32.25700 8.23600   50.28700 1.000 42.58000 ? 36  PHE A CA  1 
ATOM   295  C  C   . PHE A 1 36  ? 31.42300 7.63800   49.15600 1.000 39.78000 ? 36  PHE A C   1 
ATOM   296  O  O   . PHE A 1 36  ? 31.66900 7.88100   47.97300 1.000 48.16000 ? 36  PHE A O   1 
ATOM   297  C  CB  . PHE A 1 36  ? 33.46400 8.99100   49.72700 1.000 40.84000 ? 36  PHE A CB  1 
ATOM   298  C  CG  . PHE A 1 36  ? 34.45400 9.41600   50.77500 1.000 46.87000 ? 36  PHE A CG  1 
ATOM   299  C  CD1 . PHE A 1 36  ? 34.16200 10.46500  51.63500 1.000 49.49000 ? 36  PHE A CD1 1 
ATOM   300  C  CD2 . PHE A 1 36  ? 35.66700 8.76000   50.91000 1.000 42.35000 ? 36  PHE A CD2 1 
ATOM   301  C  CE1 . PHE A 1 36  ? 35.06300 10.85700  52.61200 1.000 44.13000 ? 36  PHE A CE1 1 
ATOM   302  C  CE2 . PHE A 1 36  ? 36.57600 9.15100   51.88100 1.000 49.06000 ? 36  PHE A CE2 1 
ATOM   303  C  CZ  . PHE A 1 36  ? 36.27400 10.20200  52.73200 1.000 45.90000 ? 36  PHE A CZ  1 
ATOM   304  N  N   . MET A 1 37  ? 30.44700 6.81800   49.52100 1.000 36.05000 ? 37  MET A N   1 
ATOM   305  C  CA  . MET A 1 37  ? 29.65200 6.13400   48.51600 1.000 42.17000 ? 37  MET A CA  1 
ATOM   306  C  C   . MET A 1 37  ? 28.17200 6.31000   48.81000 1.000 36.72000 ? 37  MET A C   1 
ATOM   307  O  O   . MET A 1 37  ? 27.76000 6.57100   49.94500 1.000 34.97000 ? 37  MET A O   1 
ATOM   308  C  CB  . MET A 1 37  ? 29.99800 4.63000   48.41300 1.000 44.93000 ? 37  MET A CB  1 
ATOM   309  C  CG  . MET A 1 37  ? 29.79000 3.79700   49.66400 1.000 43.09000 ? 37  MET A CG  1 
ATOM   310  S  SD  . MET A 1 37  ? 30.28100 2.06200   49.39200 1.000 48.40000 ? 37  MET A SD  1 
ATOM   311  C  CE  . MET A 1 37  ? 30.47500 1.50300   51.07800 1.000 43.57000 ? 37  MET A CE  1 
ATOM   312  N  N   . ASP A 1 38  ? 27.38400 6.18300   47.74800 1.000 37.71000 ? 38  ASP A N   1 
ATOM   313  C  CA  . ASP A 1 38  ? 25.93600 6.21800   47.87000 1.000 35.38000 ? 38  ASP A CA  1 
ATOM   314  C  C   . ASP A 1 38  ? 25.43100 4.93700   48.52600 1.000 36.31000 ? 38  ASP A C   1 
ATOM   315  O  O   . ASP A 1 38  ? 25.98400 3.85300   48.32600 1.000 34.71000 ? 38  ASP A O   1 
ATOM   316  C  CB  . ASP A 1 38  ? 25.28400 6.37300   46.49400 1.000 38.13000 ? 38  ASP A CB  1 
ATOM   317  C  CG  . ASP A 1 38  ? 25.58000 7.72400   45.83100 1.000 46.99000 ? 38  ASP A CG  1 
ATOM   318  O  OD1 . ASP A 1 38  ? 26.13600 8.63400   46.49200 1.000 39.81000 ? 38  ASP A OD1 1 
ATOM   319  O  OD2 . ASP A 1 38  ? 25.23400 7.87800   44.63500 1.000 47.07000 ? 38  ASP A OD2 1 
ATOM   320  N  N   . ILE A 1 39  ? 24.36100 5.07600   49.30900 1.000 33.62000 ? 39  ILE A N   1 
ATOM   321  C  CA  . ILE A 1 39  ? 23.60000 3.93100   49.79700 1.000 35.66000 ? 39  ILE A CA  1 
ATOM   322  C  C   . ILE A 1 39  ? 22.83000 3.32400   48.63200 1.000 37.24000 ? 39  ILE A C   1 
ATOM   323  O  O   . ILE A 1 39  ? 21.95800 3.97800   48.04800 1.000 32.37000 ? 39  ILE A O   1 
ATOM   324  C  CB  . ILE A 1 39  ? 22.63300 4.35600   50.91100 1.000 31.77000 ? 39  ILE A CB  1 
ATOM   325  C  CG1 . ILE A 1 39  ? 23.39000 4.87100   52.13600 1.000 35.45000 ? 39  ILE A CG1 1 
ATOM   326  C  CG2 . ILE A 1 39  ? 21.70700 3.20600   51.28400 1.000 38.03000 ? 39  ILE A CG2 1 
ATOM   327  C  CD1 . ILE A 1 39  ? 22.48100 5.59800   53.13600 1.000 35.85000 ? 39  ILE A CD1 1 
ATOM   328  N  N   . ILE A 1 40  ? 23.13800 2.07500   48.29000 1.000 31.06000 ? 40  ILE A N   1 
ATOM   329  C  CA  . ILE A 1 40  ? 22.43900 1.36100   47.22500 1.000 33.71000 ? 40  ILE A CA  1 
ATOM   330  C  C   . ILE A 1 40  ? 21.32300 0.54300   47.86500 1.000 30.21000 ? 40  ILE A C   1 
ATOM   331  O  O   . ILE A 1 40  ? 21.59400 -0.39100  48.62500 1.000 30.82000 ? 40  ILE A O   1 
ATOM   332  C  CB  . ILE A 1 40  ? 23.39300 0.46300   46.43300 1.000 30.43000 ? 40  ILE A CB  1 
ATOM   333  C  CG1 . ILE A 1 40  ? 24.60100 1.26600   45.92400 1.000 33.48000 ? 40  ILE A CG1 1 
ATOM   334  C  CG2 . ILE A 1 40  ? 22.64200 -0.26200  45.32300 1.000 30.65000 ? 40  ILE A CG2 1 
ATOM   335  C  CD1 . ILE A 1 40  ? 24.25100 2.46200   45.03700 1.000 37.62000 ? 40  ILE A CD1 1 
ATOM   336  N  N   . ARG A 1 41  ? 20.06500 0.88400   47.57100 1.000 32.84000 ? 41  ARG A N   1 
ATOM   337  C  CA  . ARG A 1 41  ? 18.91600 0.12500   48.08100 1.000 31.22000 ? 41  ARG A CA  1 
ATOM   338  C  C   . ARG A 1 41  ? 18.51800 -0.98200  47.10500 1.000 32.48000 ? 41  ARG A C   1 
ATOM   339  O  O   . ARG A 1 41  ? 17.41300 -1.00200  46.55500 1.000 37.40000 ? 41  ARG A O   1 
ATOM   340  C  CB  . ARG A 1 41  ? 17.73200 1.05000   48.36300 1.000 32.02000 ? 41  ARG A CB  1 
ATOM   341  C  CG  . ARG A 1 41  ? 17.96100 2.01200   49.51100 1.000 36.71000 ? 41  ARG A CG  1 
ATOM   342  C  CD  . ARG A 1 41  ? 16.74700 2.88900   49.79700 1.000 38.59000 ? 41  ARG A CD  1 
ATOM   343  N  NE  . ARG A 1 41  ? 15.59400 2.10600   50.24400 1.000 41.02000 ? 41  ARG A NE  1 
ATOM   344  C  CZ  . ARG A 1 41  ? 15.42900 1.63900   51.48200 1.000 43.22000 ? 41  ARG A CZ  1 
ATOM   345  N  NH1 . ARG A 1 41  ? 16.34800 1.86800   52.41600 1.000 42.36000 ? 41  ARG A NH1 1 
ATOM   346  N  NH2 . ARG A 1 41  ? 14.34800 0.92800   51.78600 1.000 41.22000 ? 41  ARG A NH2 1 
ATOM   347  N  N   . SER A 1 42  ? 19.44400 -1.92500  46.90700 1.000 29.49000 ? 42  SER A N   1 
ATOM   348  C  CA  . SER A 1 42  ? 19.20700 -3.08600  46.06100 1.000 27.78000 ? 42  SER A CA  1 
ATOM   349  C  C   . SER A 1 42  ? 19.39500 -4.38700  46.83300 1.000 28.46000 ? 42  SER A C   1 
ATOM   350  O  O   . SER A 1 42  ? 20.22300 -4.45700  47.75300 1.000 25.77000 ? 42  SER A O   1 
ATOM   351  C  CB  . SER A 1 42  ? 20.15400 -3.08700  44.86300 1.000 30.63000 ? 42  SER A CB  1 
ATOM   352  O  OG  . SER A 1 42  ? 19.82300 -2.00200  44.02500 1.000 43.73000 ? 42  SER A OG  1 
ATOM   353  N  N   . PRO A 1 43  ? 18.65200 -5.43900  46.46200 1.000 28.48000 ? 43  PRO A N   1 
ATOM   354  C  CA  . PRO A 1 43  ? 18.84100 -6.75000  47.09900 1.000 26.84000 ? 43  PRO A CA  1 
ATOM   355  C  C   . PRO A 1 43  ? 20.28700 -7.21200  46.99000 1.000 28.27000 ? 43  PRO A C   1 
ATOM   356  O  O   . PRO A 1 43  ? 20.99600 -6.90300  46.03000 1.000 27.62000 ? 43  PRO A O   1 
ATOM   357  C  CB  . PRO A 1 43  ? 17.90400 -7.67400  46.30500 1.000 27.37000 ? 43  PRO A CB  1 
ATOM   358  C  CG  . PRO A 1 43  ? 16.92000 -6.76800  45.68100 1.000 30.20000 ? 43  PRO A CG  1 
ATOM   359  C  CD  . PRO A 1 43  ? 17.62200 -5.47800  45.41200 1.000 27.47000 ? 43  PRO A CD  1 
ATOM   360  N  N   . ALA A 1 44  ? 20.72400 -7.95300  48.00100 1.000 29.32000 ? 44  ALA A N   1 
ATOM   361  C  CA  . ALA A 1 44  ? 22.07600 -8.46800  48.07900 1.000 23.26000 ? 44  ALA A CA  1 
ATOM   362  C  C   . ALA A 1 44  ? 22.07900 -9.90700  47.60800 1.000 25.00000 ? 44  ALA A C   1 
ATOM   363  O  O   . ALA A 1 44  ? 21.14100 -10.65900 47.87800 1.000 27.13000 ? 44  ALA A O   1 
ATOM   364  C  CB  . ALA A 1 44  ? 22.60000 -8.37900  49.50600 1.000 25.15000 ? 44  ALA A CB  1 
ATOM   365  N  N   . ASP A 1 45  ? 23.11500 -10.27400 46.87400 1.000 24.16000 ? 45  ASP A N   1 
ATOM   366  C  CA  . ASP A 1 45  ? 23.27800 -11.65800 46.46400 1.000 29.76000 ? 45  ASP A CA  1 
ATOM   367  C  C   . ASP A 1 45  ? 23.89900 -12.49600 47.56400 1.000 27.79000 ? 45  ASP A C   1 
ATOM   368  O  O   . ASP A 1 45  ? 23.77400 -13.72200 47.55400 1.000 27.26000 ? 45  ASP A O   1 
ATOM   369  C  CB  . ASP A 1 45  ? 24.14300 -11.74000 45.20000 1.000 24.24000 ? 45  ASP A CB  1 
ATOM   370  C  CG  . ASP A 1 45  ? 23.54100 -10.96700 44.03100 1.000 34.26000 ? 45  ASP A CG  1 
ATOM   371  O  OD1 . ASP A 1 45  ? 22.44600 -11.35200 43.56900 1.000 36.77000 ? 45  ASP A OD1 1 
ATOM   372  O  OD2 . ASP A 1 45  ? 24.15100 -9.96600  43.58100 1.000 35.61000 ? 45  ASP A OD2 1 
ATOM   373  N  N   . VAL A 1 46  ? 24.55100 -11.85700 48.51700 1.000 27.16000 ? 46  VAL A N   1 
ATOM   374  C  CA  . VAL A 1 46  ? 25.23200 -12.57000 49.58000 1.000 28.69000 ? 46  VAL A CA  1 
ATOM   375  C  C   . VAL A 1 46  ? 25.33000 -11.61600 50.75900 1.000 25.47000 ? 46  VAL A C   1 
ATOM   376  O  O   . VAL A 1 46  ? 25.52400 -10.40500 50.58800 1.000 25.08000 ? 46  VAL A O   1 
ATOM   377  C  CB  . VAL A 1 46  ? 26.61600 -13.08000 49.11800 1.000 26.25000 ? 46  VAL A CB  1 
ATOM   378  C  CG1 . VAL A 1 46  ? 27.51200 -11.90200 48.81900 1.000 24.78000 ? 46  VAL A CG1 1 
ATOM   379  C  CG2 . VAL A 1 46  ? 27.25300 -13.99700 50.19000 1.000 26.52000 ? 46  VAL A CG2 1 
ATOM   380  N  N   . THR A 1 47  ? 25.14200 -12.16700 51.94700 1.000 22.45000 ? 47  THR A N   1 
ATOM   381  C  CA  . THR A 1 47  ? 25.07700 -11.41300 53.18600 1.000 21.35000 ? 47  THR A CA  1 
ATOM   382  C  C   . THR A 1 47  ? 26.18000 -11.91700 54.09500 1.000 26.88000 ? 47  THR A C   1 
ATOM   383  O  O   . THR A 1 47  ? 26.26900 -13.12500 54.34200 1.000 23.52000 ? 47  THR A O   1 
ATOM   384  C  CB  . THR A 1 47  ? 23.72600 -11.61600 53.86800 1.000 29.92000 ? 47  THR A CB  1 
ATOM   385  O  OG1 . THR A 1 47  ? 22.68900 -11.03200 53.06000 1.000 25.52000 ? 47  THR A OG1 1 
ATOM   386  C  CG2 . THR A 1 47  ? 23.73900 -11.00700 55.28300 1.000 27.75000 ? 47  THR A CG2 1 
ATOM   387  N  N   . VAL A 1 48  ? 27.00800 -10.99900 54.59300 1.000 23.79000 ? 48  VAL A N   1 
ATOM   388  C  CA  . VAL A 1 48  ? 28.13400 -11.32500 55.46000 1.000 21.87000 ? 48  VAL A CA  1 
ATOM   389  C  C   . VAL A 1 48  ? 27.91700 -10.63000 56.79900 1.000 27.84000 ? 48  VAL A C   1 
ATOM   390  O  O   . VAL A 1 48  ? 27.64900 -9.42000  56.84000 1.000 24.73000 ? 48  VAL A O   1 
ATOM   391  C  CB  . VAL A 1 48  ? 29.47000 -10.89500 54.82500 1.000 24.41000 ? 48  VAL A CB  1 
ATOM   392  C  CG1 . VAL A 1 48  ? 30.63100 -11.34500 55.70300 1.000 23.41000 ? 48  VAL A CG1 1 
ATOM   393  C  CG2 . VAL A 1 48  ? 29.60900 -11.47000 53.42000 1.000 24.31000 ? 48  VAL A CG2 1 
ATOM   394  N  N   . LYS A 1 49  ? 28.03700 -11.38500 57.89100 1.000 23.86000 ? 49  LYS A N   1 
ATOM   395  C  CA  . LYS A 1 49  ? 27.74100 -10.84400 59.21500 1.000 23.17000 ? 49  LYS A CA  1 
ATOM   396  C  C   . LYS A 1 49  ? 28.48400 -11.64600 60.28200 1.000 22.86000 ? 49  LYS A C   1 
ATOM   397  O  O   . LYS A 1 49  ? 29.10400 -12.66900 59.99500 1.000 19.42000 ? 49  LYS A O   1 
ATOM   398  C  CB  . LYS A 1 49  ? 26.24100 -10.88400 59.47300 1.000 28.25000 ? 49  LYS A CB  1 
ATOM   399  C  CG  . LYS A 1 49  ? 25.76300 -12.31500 59.65800 1.000 26.28000 ? 49  LYS A CG  1 
ATOM   400  C  CD  . LYS A 1 49  ? 24.25900 -12.40400 59.55600 1.000 36.98000 ? 49  LYS A CD  1 
ATOM   401  C  CE  . LYS A 1 49  ? 23.78300 -13.85600 59.65400 1.000 42.47000 ? 49  LYS A CE  1 
ATOM   402  N  NZ  . LYS A 1 49  ? 22.30500 -13.94100 59.47700 1.000 47.54000 ? 49  LYS A NZ  1 
ATOM   403  N  N   . ASP A 1 50  ? 28.43400 -11.15200 61.52000 1.000 26.02000 ? 50  ASP A N   1 
ATOM   404  C  CA  . ASP A 1 50  ? 29.02100 -11.88800 62.64100 1.000 24.59000 ? 50  ASP A CA  1 
ATOM   405  C  C   . ASP A 1 50  ? 28.27500 -13.18700 62.85800 1.000 27.08000 ? 50  ASP A C   1 
ATOM   406  O  O   . ASP A 1 50  ? 27.05800 -13.26700 62.65600 1.000 31.17000 ? 50  ASP A O   1 
ATOM   407  C  CB  . ASP A 1 50  ? 28.95700 -11.08600 63.94000 1.000 27.97000 ? 50  ASP A CB  1 
ATOM   408  C  CG  . ASP A 1 50  ? 29.73700 -9.78200  63.87800 1.000 37.68000 ? 50  ASP A CG  1 
ATOM   409  O  OD1 . ASP A 1 50  ? 30.56900 -9.61800  62.94600 1.000 36.89000 ? 50  ASP A OD1 1 
ATOM   410  O  OD2 . ASP A 1 50  ? 29.51400 -8.92800  64.77600 1.000 42.02000 ? 50  ASP A OD2 1 
ATOM   411  N  N   . GLY A 1 51  ? 29.00100 -14.20500 63.29600 1.000 27.77000 ? 51  GLY A N   1 
ATOM   412  C  CA  . GLY A 1 51  ? 28.35600 -15.42200 63.74100 1.000 31.34000 ? 51  GLY A CA  1 
ATOM   413  C  C   . GLY A 1 51  ? 27.77800 -15.25500 65.13900 1.000 31.27000 ? 51  GLY A C   1 
ATOM   414  O  O   . GLY A 1 51  ? 27.81600 -14.18400 65.75000 1.000 31.62000 ? 51  GLY A O   1 
ATOM   415  N  N   . ILE A 1 52  ? 27.24700 -16.36600 65.65900 1.000 34.58000 ? 52  ILE A N   1 
ATOM   416  C  CA  . ILE A 1 52  ? 26.73100 -16.39600 67.03000 1.000 37.69000 ? 52  ILE A CA  1 
ATOM   417  C  C   . ILE A 1 52  ? 27.81200 -15.98600 68.01700 1.000 35.72000 ? 52  ILE A C   1 
ATOM   418  O  O   . ILE A 1 52  ? 27.53500 -15.34600 69.03400 1.000 34.10000 ? 52  ILE A O   1 
ATOM   419  C  CB  . ILE A 1 52  ? 26.18800 -17.80000 67.37100 1.000 38.69000 ? 52  ILE A CB  1 
ATOM   420  C  CG1 . ILE A 1 52  ? 25.07900 -18.20500 66.40700 1.000 41.61000 ? 52  ILE A CG1 1 
ATOM   421  C  CG2 . ILE A 1 52  ? 25.71000 -17.84800 68.81200 1.000 43.27000 ? 52  ILE A CG2 1 
ATOM   422  C  CD1 . ILE A 1 52  ? 24.00800 -17.15200 66.24300 1.000 49.03000 ? 52  ILE A CD1 1 
ATOM   423  N  N   . ASP A 1 53  ? 29.04500 -16.38500 67.76000 1.000 34.89000 ? 53  ASP A N   1 
ATOM   424  C  CA  . ASP A 1 53  ? 30.19400 -15.85900 68.47700 1.000 31.14000 ? 53  ASP A CA  1 
ATOM   425  C  C   . ASP A 1 53  ? 30.85200 -14.78400 67.62800 1.000 31.87000 ? 53  ASP A C   1 
ATOM   426  O  O   . ASP A 1 53  ? 31.08000 -14.98200 66.42600 1.000 28.19000 ? 53  ASP A O   1 
ATOM   427  C  CB  . ASP A 1 53  ? 31.19900 -16.95500 68.79600 1.000 33.15000 ? 53  ASP A CB  1 
ATOM   428  C  CG  . ASP A 1 53  ? 32.40600 -16.42400 69.54900 1.000 34.01000 ? 53  ASP A CG  1 
ATOM   429  O  OD1 . ASP A 1 53  ? 32.37800 -16.37900 70.80500 1.000 31.64000 ? 53  ASP A OD1 1 
ATOM   430  O  OD2 . ASP A 1 53  ? 33.39000 -16.06000 68.87000 1.000 29.63000 ? 53  ASP A OD2 1 
ATOM   431  N  N   . LYS A 1 54  ? 31.15200 -13.64900 68.25100 1.000 27.89000 ? 54  LYS A N   1 
ATOM   432  C  CA  . LYS A 1 54  ? 31.68600 -12.53600 67.48300 1.000 33.41000 ? 54  LYS A CA  1 
ATOM   433  C  C   . LYS A 1 54  ? 33.05700 -12.83800 66.89600 1.000 31.37000 ? 54  LYS A C   1 
ATOM   434  O  O   . LYS A 1 54  ? 33.52800 -12.07900 66.04900 1.000 27.52000 ? 54  LYS A O   1 
ATOM   435  C  CB  . LYS A 1 54  ? 31.74900 -11.28400 68.34400 1.000 32.75000 ? 54  LYS A CB  1 
ATOM   436  C  CG  . LYS A 1 54  ? 30.51600 -10.41100 68.24200 1.000 36.57000 ? 54  LYS A CG  1 
ATOM   437  C  CD  . LYS A 1 54  ? 30.67300 -9.18400  69.13000 1.000 32.85000 ? 54  LYS A CD  1 
ATOM   438  C  CE  . LYS A 1 54  ? 29.33000 -8.73100  69.66000 1.000 52.29000 ? 54  LYS A CE  1 
ATOM   439  N  NZ  . LYS A 1 54  ? 28.41200 -8.38100  68.54500 1.000 56.63000 ? 54  LYS A NZ  1 
ATOM   440  N  N   . GLY A 1 55  ? 33.69900 -13.92700 67.31100 1.000 28.47000 ? 55  GLY A N   1 
ATOM   441  C  CA  . GLY A 1 55  ? 34.93300 -14.28000 66.65900 1.000 25.65000 ? 55  GLY A CA  1 
ATOM   442  C  C   . GLY A 1 55  ? 34.74900 -14.99500 65.34700 1.000 26.76000 ? 55  GLY A C   1 
ATOM   443  O  O   . GLY A 1 55  ? 35.73600 -15.42900 64.75100 1.000 28.54000 ? 55  GLY A O   1 
ATOM   444  N  N   . GLU A 1 56  ? 33.51200 -15.12500 64.86600 1.000 25.50000 ? 56  GLU A N   1 
ATOM   445  C  CA  . GLU A 1 56  ? 33.22800 -15.76800 63.58900 1.000 26.34000 ? 56  GLU A CA  1 
ATOM   446  C  C   . GLU A 1 56  ? 32.53800 -14.81000 62.62600 1.000 27.31000 ? 56  GLU A C   1 
ATOM   447  O  O   . GLU A 1 56  ? 31.74700 -13.94500 63.02600 1.000 24.78000 ? 56  GLU A O   1 
ATOM   448  C  CB  . GLU A 1 56  ? 32.34400 -17.01100 63.78200 1.000 27.90000 ? 56  GLU A CB  1 
ATOM   449  C  CG  . GLU A 1 56  ? 33.07600 -18.14500 64.49500 1.000 30.44000 ? 56  GLU A CG  1 
ATOM   450  C  CD  . GLU A 1 56  ? 32.15600 -19.07500 65.29100 1.000 54.39000 ? 56  GLU A CD  1 
ATOM   451  O  OE1 . GLU A 1 56  ? 30.95300 -18.75900 65.48600 1.000 47.87000 ? 56  GLU A OE1 1 
ATOM   452  O  OE2 . GLU A 1 56  ? 32.65300 -20.13700 65.72200 1.000 48.47000 ? 56  GLU A OE2 1 
ATOM   453  N  N   . ILE A 1 57  ? 32.82000 -15.00200 61.33900 1.000 23.27000 ? 57  ILE A N   1 
ATOM   454  C  CA  . ILE A 1 57  ? 32.11900 -14.32600 60.25100 1.000 24.24000 ? 57  ILE A CA  1 
ATOM   455  C  C   . ILE A 1 57  ? 31.33000 -15.38600 59.49800 1.000 24.55000 ? 57  ILE A C   1 
ATOM   456  O  O   . ILE A 1 57  ? 31.85400 -16.46400 59.20700 1.000 24.65000 ? 57  ILE A O   1 
ATOM   457  C  CB  . ILE A 1 57  ? 33.10500 -13.60200 59.31900 1.000 26.01000 ? 57  ILE A CB  1 
ATOM   458  C  CG1 . ILE A 1 57  ? 33.78800 -12.43800 60.02800 1.000 28.36000 ? 57  ILE A CG1 1 
ATOM   459  C  CG2 . ILE A 1 57  ? 32.39700 -13.11800 58.06100 1.000 30.80000 ? 57  ILE A CG2 1 
ATOM   460  C  CD1 . ILE A 1 57  ? 34.90800 -11.80600 59.17300 1.000 28.45000 ? 57  ILE A CD1 1 
ATOM   461  N  N   . VAL A 1 58  ? 30.07700 -15.10800 59.19700 1.000 24.38000 ? 58  VAL A N   1 
ATOM   462  C  CA  . VAL A 1 58  ? 29.30900 -16.07400 58.41800 1.000 23.28000 ? 58  VAL A CA  1 
ATOM   463  C  C   . VAL A 1 58  ? 28.84100 -15.39800 57.14500 1.000 23.12000 ? 58  VAL A C   1 
ATOM   464  O  O   . VAL A 1 58  ? 28.64700 -14.17600 57.09800 1.000 24.97000 ? 58  VAL A O   1 
ATOM   465  C  CB  . VAL A 1 58  ? 28.10600 -16.67400 59.18300 1.000 30.23000 ? 58  VAL A CB  1 
ATOM   466  C  CG1 . VAL A 1 58  ? 28.58700 -17.54300 60.37100 1.000 28.87000 ? 58  VAL A CG1 1 
ATOM   467  C  CG2 . VAL A 1 58  ? 27.16000 -15.59200 59.65400 1.000 29.29000 ? 58  VAL A CG2 1 
ATOM   468  N  N   . SER A 1 59  ? 28.66400 -16.20800 56.10600 1.000 21.20000 ? 59  SER A N   1 
ATOM   469  C  CA  . SER A 1 59  ? 28.19700 -15.73200 54.81800 1.000 26.72000 ? 59  SER A CA  1 
ATOM   470  C  C   . SER A 1 59  ? 27.04900 -16.60700 54.32500 1.000 27.00000 ? 59  SER A C   1 
ATOM   471  O  O   . SER A 1 59  ? 27.15100 -17.84100 54.33300 1.000 26.20000 ? 59  SER A O   1 
ATOM   472  C  CB  . SER A 1 59  ? 29.33700 -15.73000 53.80900 1.000 23.87000 ? 59  SER A CB  1 
ATOM   473  O  OG  . SER A 1 59  ? 28.81400 -15.52700 52.53100 1.000 30.68000 ? 59  SER A OG  1 
ATOM   474  N  N   . VAL A 1 60  ? 25.96900 -15.97000 53.88500 1.000 24.97000 ? 60  VAL A N   1 
ATOM   475  C  CA  . VAL A 1 60  ? 24.76700 -16.66700 53.43000 1.000 26.30000 ? 60  VAL A CA  1 
ATOM   476  C  C   . VAL A 1 60  ? 24.35900 -16.10200 52.07800 1.000 26.77000 ? 60  VAL A C   1 
ATOM   477  O  O   . VAL A 1 60  ? 24.36700 -14.87900 51.88800 1.000 27.66000 ? 60  VAL A O   1 
ATOM   478  C  CB  . VAL A 1 60  ? 23.60700 -16.52400 54.43600 1.000 26.50000 ? 60  VAL A CB  1 
ATOM   479  C  CG1 . VAL A 1 60  ? 22.28800 -17.02800 53.81400 1.000 29.52000 ? 60  VAL A CG1 1 
ATOM   480  C  CG2 . VAL A 1 60  ? 23.93900 -17.25900 55.71500 1.000 29.81000 ? 60  VAL A CG2 1 
ATOM   481  N  N   . GLY A 1 61  ? 24.00300 -16.98700 51.14200 1.000 27.62000 ? 61  GLY A N   1 
ATOM   482  C  CA  . GLY A 1 61  ? 23.61900 -16.56300 49.80600 1.000 28.01000 ? 61  GLY A CA  1 
ATOM   483  C  C   . GLY A 1 61  ? 24.41600 -17.27600 48.72200 1.000 32.51000 ? 61  GLY A C   1 
ATOM   484  O  O   . GLY A 1 61  ? 24.59000 -18.49700 48.75900 1.000 29.78000 ? 61  GLY A O   1 
ATOM   485  N  N   . GLU A 1 62  ? 24.88500 -16.50800 47.73900 1.000 30.50000 ? 62  GLU A N   1 
ATOM   486  C  CA  . GLU A 1 62  ? 25.74100 -17.09400 46.71700 1.000 34.62000 ? 62  GLU A CA  1 
ATOM   487  C  C   . GLU A 1 62  ? 27.05700 -17.54000 47.34500 1.000 34.44000 ? 62  GLU A C   1 
ATOM   488  O  O   . GLU A 1 62  ? 27.48300 -17.02500 48.38500 1.000 32.53000 ? 62  GLU A O   1 
ATOM   489  C  CB  . GLU A 1 62  ? 25.98800 -16.10900 45.57200 1.000 28.45000 ? 62  GLU A CB  1 
ATOM   490  C  CG  . GLU A 1 62  ? 24.71200 -15.67200 44.81500 1.000 43.64000 ? 62  GLU A CG  1 
ATOM   491  C  CD  . GLU A 1 62  ? 24.04700 -16.81100 44.02100 1.000 54.20000 ? 62  GLU A CD  1 
ATOM   492  O  OE1 . GLU A 1 62  ? 24.73600 -17.50100 43.23000 1.000 60.84000 ? 62  GLU A OE1 1 
ATOM   493  O  OE2 . GLU A 1 62  ? 22.82200 -17.02900 44.21100 1.000 55.09000 ? 62  GLU A OE2 1 
ATOM   494  N  N   . ASP A 1 63  ? 27.67600 -18.53700 46.73100 1.000 32.47000 ? 63  ASP A N   1 
ATOM   495  C  CA  . ASP A 1 63  ? 28.92000 -19.07900 47.25500 1.000 32.99000 ? 63  ASP A CA  1 
ATOM   496  C  C   . ASP A 1 63  ? 30.04100 -18.06600 47.05100 1.000 30.11000 ? 63  ASP A C   1 
ATOM   497  O  O   . ASP A 1 63  ? 30.29300 -17.63500 45.92300 1.000 28.59000 ? 63  ASP A O   1 
ATOM   498  C  CB  . ASP A 1 63  ? 29.24000 -20.39400 46.56200 1.000 34.90000 ? 63  ASP A CB  1 
ATOM   499  C  CG  . ASP A 1 63  ? 30.48600 -21.06000 47.12300 1.000 42.15000 ? 63  ASP A CG  1 
ATOM   500  O  OD1 . ASP A 1 63  ? 30.70800 -20.98500 48.35100 1.000 42.44000 ? 63  ASP A OD1 1 
ATOM   501  O  OD2 . ASP A 1 63  ? 31.25600 -21.63000 46.31900 1.000 50.49000 ? 63  ASP A OD2 1 
ATOM   502  N  N   . ILE A 1 64  ? 30.69300 -17.65500 48.13700 1.000 29.64000 ? 64  ILE A N   1 
ATOM   503  C  CA  . ILE A 1 64  ? 31.86100 -16.79200 48.00000 1.000 30.69000 ? 64  ILE A CA  1 
ATOM   504  C  C   . ILE A 1 64  ? 33.07300 -17.44500 48.64900 1.000 28.03000 ? 64  ILE A C   1 
ATOM   505  O  O   . ILE A 1 64  ? 34.02700 -16.75500 49.02800 1.000 26.40000 ? 64  ILE A O   1 
ATOM   506  C  CB  . ILE A 1 64  ? 31.61200 -15.38100 48.58300 1.000 34.65000 ? 64  ILE A CB  1 
ATOM   507  C  CG1 . ILE A 1 64  ? 31.12800 -15.43900 50.03700 1.000 25.58000 ? 64  ILE A CG1 1 
ATOM   508  C  CG2 . ILE A 1 64  ? 30.61900 -14.64200 47.72900 1.000 29.38000 ? 64  ILE A CG2 1 
ATOM   509  C  CD1 . ILE A 1 64  ? 31.29300 -14.11500 50.80900 1.000 25.15000 ? 64  ILE A CD1 1 
ATOM   510  N  N   . TYR A 1 65  ? 33.05900 -18.78100 48.73600 1.000 25.22000 ? 65  TYR A N   1 
ATOM   511  C  CA  . TYR A 1 65  ? 34.09800 -19.50400 49.46700 1.000 24.30000 ? 65  TYR A CA  1 
ATOM   512  C  C   . TYR A 1 65  ? 35.48600 -19.20100 48.92100 1.000 26.93000 ? 65  TYR A C   1 
ATOM   513  O  O   . TYR A 1 65  ? 36.41900 -18.90500 49.68200 1.000 26.16000 ? 65  TYR A O   1 
ATOM   514  C  CB  . TYR A 1 65  ? 33.82800 -21.01100 49.42100 1.000 30.11000 ? 65  TYR A CB  1 
ATOM   515  C  CG  . TYR A 1 65  ? 34.99000 -21.82100 49.95800 1.000 32.62000 ? 65  TYR A CG  1 
ATOM   516  C  CD1 . TYR A 1 65  ? 35.14500 -22.01600 51.32400 1.000 28.33000 ? 65  TYR A CD1 1 
ATOM   517  C  CD2 . TYR A 1 65  ? 35.93800 -22.36300 49.10600 1.000 31.39000 ? 65  TYR A CD2 1 
ATOM   518  C  CE1 . TYR A 1 65  ? 36.20200 -22.72600 51.82800 1.000 26.67000 ? 65  TYR A CE1 1 
ATOM   519  C  CE2 . TYR A 1 65  ? 37.00400 -23.07600 49.59500 1.000 38.48000 ? 65  TYR A CE2 1 
ATOM   520  C  CZ  . TYR A 1 65  ? 37.13100 -23.25300 50.96300 1.000 40.35000 ? 65  TYR A CZ  1 
ATOM   521  O  OH  . TYR A 1 65  ? 38.18300 -23.97500 51.45000 1.000 36.45000 ? 65  TYR A OH  1 
ATOM   522  N  N   . ASN A 1 66  ? 35.65300 -19.30000 47.59800 1.000 26.43000 ? 66  ASN A N   1 
ATOM   523  C  CA  . ASN A 1 66  ? 36.98100 -19.09500 47.03000 1.000 29.23000 ? 66  ASN A CA  1 
ATOM   524  C  C   . ASN A 1 66  ? 37.46400 -17.69000 47.30500 1.000 28.84000 ? 66  ASN A C   1 
ATOM   525  O  O   . ASN A 1 66  ? 38.65600 -17.47400 47.55500 1.000 31.34000 ? 66  ASN A O   1 
ATOM   526  C  CB  . ASN A 1 66  ? 36.97400 -19.39100 45.53300 1.000 32.40000 ? 66  ASN A CB  1 
ATOM   527  C  CG  . ASN A 1 66  ? 36.68800 -20.86000 45.23700 1.000 36.65000 ? 66  ASN A CG  1 
ATOM   528  O  OD1 . ASN A 1 66  ? 37.21300 -21.74900 45.90100 1.000 35.56000 ? 66  ASN A OD1 1 
ATOM   529  N  ND2 . ASN A 1 66  ? 35.84700 -21.11200 44.24300 1.000 39.01000 ? 66  ASN A ND2 1 
ATOM   530  N  N   . PHE A 1 67  ? 36.54700 -16.72600 47.32500 1.000 30.21000 ? 67  PHE A N   1 
ATOM   531  C  CA  . PHE A 1 67  ? 36.97300 -15.38100 47.65200 1.000 30.08000 ? 67  PHE A CA  1 
ATOM   532  C  C   . PHE A 1 67  ? 37.36300 -15.25800 49.12900 1.000 33.92000 ? 67  PHE A C   1 
ATOM   533  O  O   . PHE A 1 67  ? 38.36400 -14.61100 49.46700 1.000 29.67000 ? 67  PHE A O   1 
ATOM   534  C  CB  . PHE A 1 67  ? 35.88500 -14.37800 47.29800 1.000 34.59000 ? 67  PHE A CB  1 
ATOM   535  C  CG  . PHE A 1 67  ? 36.23100 -13.03000 47.73700 1.000 40.58000 ? 67  PHE A CG  1 
ATOM   536  C  CD1 . PHE A 1 67  ? 37.35100 -12.41800 47.21600 1.000 46.53000 ? 67  PHE A CD1 1 
ATOM   537  C  CD2 . PHE A 1 67  ? 35.52900 -12.40300 48.73800 1.000 40.33000 ? 67  PHE A CD2 1 
ATOM   538  C  CE1 . PHE A 1 67  ? 37.73300 -11.19200 47.65400 1.000 57.56000 ? 67  PHE A CE1 1 
ATOM   539  C  CE2 . PHE A 1 67  ? 35.90500 -11.14700 49.17400 1.000 46.61000 ? 67  PHE A CE2 1 
ATOM   540  C  CZ  . PHE A 1 67  ? 37.01400 -10.53600 48.62500 1.000 47.73000 ? 67  PHE A CZ  1 
ATOM   541  N  N   . MET A 1 68  ? 36.59500 -15.87000 50.02400 1.000 25.60000 ? 68  MET A N   1 
ATOM   542  C  CA  . MET A 1 68  ? 36.92400 -15.75800 51.44200 1.000 29.79000 ? 68  MET A CA  1 
ATOM   543  C  C   . MET A 1 68  ? 38.22500 -16.47900 51.76800 1.000 27.84000 ? 68  MET A C   1 
ATOM   544  O  O   . MET A 1 68  ? 39.04300 -15.97700 52.55100 1.000 23.29000 ? 68  MET A O   1 
ATOM   545  C  CB  . MET A 1 68  ? 35.76700 -16.29400 52.27600 1.000 23.24000 ? 68  MET A CB  1 
ATOM   546  C  CG  . MET A 1 68  ? 34.53600 -15.41700 52.16800 1.000 26.67000 ? 68  MET A CG  1 
ATOM   547  S  SD  . MET A 1 68  ? 34.74400 -13.95400 53.21100 1.000 36.43000 ? 68  MET A SD  1 
ATOM   548  C  CE  . MET A 1 68  ? 35.25000 -12.76200 52.03400 1.000 41.80000 ? 68  MET A CE  1 
ATOM   549  N  N   . ARG A 1 69  ? 38.46200 -17.62200 51.12800 1.000 25.57000 ? 69  ARG A N   1 
ATOM   550  C  CA  . ARG A 1 69  ? 39.69800 -18.34800 51.37600 1.000 28.71000 ? 69  ARG A CA  1 
ATOM   551  C  C   . ARG A 1 69  ? 40.93800 -17.57900 50.90700 1.000 30.74000 ? 69  ARG A C   1 
ATOM   552  O  O   . ARG A 1 69  ? 42.03700 -17.84600 51.40200 1.000 36.71000 ? 69  ARG A O   1 
ATOM   553  C  CB  . ARG A 1 69  ? 39.62400 -19.75000 50.75000 1.000 24.18000 ? 69  ARG A CB  1 
ATOM   554  C  CG  . ARG A 1 69  ? 40.89600 -20.58500 50.96800 1.000 30.91000 ? 69  ARG A CG  1 
ATOM   555  C  CD  . ARG A 1 69  ? 41.29400 -20.58300 52.45600 1.000 27.75000 ? 69  ARG A CD  1 
ATOM   556  N  NE  . ARG A 1 69  ? 40.58000 -21.60200 53.20100 1.000 39.98000 ? 69  ARG A NE  1 
ATOM   557  C  CZ  . ARG A 1 69  ? 40.76300 -21.81800 54.49400 1.000 40.06000 ? 69  ARG A CZ  1 
ATOM   558  N  NH1 . ARG A 1 69  ? 41.61300 -21.03800 55.14500 1.000 34.38000 ? 69  ARG A NH1 1 
ATOM   559  N  NH2 . ARG A 1 69  ? 40.09200 -22.77600 55.12500 1.000 40.73000 ? 69  ARG A NH2 1 
ATOM   560  N  N   . SER A 1 70  ? 40.80300 -16.59200 50.01800 1.000 31.56000 ? 70  SER A N   1 
ATOM   561  C  CA  . SER A 1 70  ? 41.98100 -15.81900 49.63200 1.000 35.75000 ? 70  SER A CA  1 
ATOM   562  C  C   . SER A 1 70  ? 42.15400 -14.54700 50.44800 1.000 33.27000 ? 70  SER A C   1 
ATOM   563  O  O   . SER A 1 70  ? 43.26300 -14.01100 50.51300 1.000 37.47000 ? 70  SER A O   1 
ATOM   564  C  CB  . SER A 1 70  ? 41.94400 -15.47300 48.13700 1.000 33.63000 ? 70  SER A CB  1 
ATOM   565  O  OG  . SER A 1 70  ? 41.09000 -14.39000 47.85300 1.000 34.85000 ? 70  SER A OG  1 
ATOM   566  N  N   . ILE A 1 71  ? 41.09100 -14.04500 51.06500 1.000 30.33000 ? 71  ILE A N   1 
ATOM   567  C  CA  . ILE A 1 71  ? 41.24200 -12.95400 52.02100 1.000 32.61000 ? 71  ILE A CA  1 
ATOM   568  C  C   . ILE A 1 71  ? 41.81000 -13.47200 53.34100 1.000 33.97000 ? 71  ILE A C   1 
ATOM   569  O  O   . ILE A 1 71  ? 42.73100 -12.88100 53.91600 1.000 31.57000 ? 71  ILE A O   1 
ATOM   570  C  CB  . ILE A 1 71  ? 39.89500 -12.23900 52.24100 1.000 33.76000 ? 71  ILE A CB  1 
ATOM   571  C  CG1 . ILE A 1 71  ? 39.30500 -11.76500 50.91400 1.000 40.20000 ? 71  ILE A CG1 1 
ATOM   572  C  CG2 . ILE A 1 71  ? 40.07600 -11.05600 53.15800 1.000 34.86000 ? 71  ILE A CG2 1 
ATOM   573  C  CD1 . ILE A 1 71  ? 40.23000 -10.83000 50.16200 1.000 45.11000 ? 71  ILE A CD1 1 
ATOM   574  N  N   . PHE A 1 72  ? 41.26100 -14.57000 53.84900 1.000 29.20000 ? 72  PHE A N   1 
ATOM   575  C  CA  . PHE A 1 72  ? 41.56300 -15.04700 55.19700 1.000 33.84000 ? 72  PHE A CA  1 
ATOM   576  C  C   . PHE A 1 72  ? 42.44700 -16.28400 55.07700 1.000 31.32000 ? 72  PHE A C   1 
ATOM   577  O  O   . PHE A 1 72  ? 41.97000 -17.41700 55.09600 1.000 30.69000 ? 72  PHE A O   1 
ATOM   578  C  CB  . PHE A 1 72  ? 40.27700 -15.32500 55.96700 1.000 26.34000 ? 72  PHE A CB  1 
ATOM   579  C  CG  . PHE A 1 72  ? 39.43600 -14.10200 56.15400 1.000 31.22000 ? 72  PHE A CG  1 
ATOM   580  C  CD1 . PHE A 1 72  ? 39.81400 -13.12400 57.07000 1.000 30.97000 ? 72  PHE A CD1 1 
ATOM   581  C  CD2 . PHE A 1 72  ? 38.30600 -13.89300 55.38500 1.000 27.04000 ? 72  PHE A CD2 1 
ATOM   582  C  CE1 . PHE A 1 72  ? 39.05700 -11.97700 57.23900 1.000 34.87000 ? 72  PHE A CE1 1 
ATOM   583  C  CE2 . PHE A 1 72  ? 37.54100 -12.73900 55.54200 1.000 31.44000 ? 72  PHE A CE2 1 
ATOM   584  C  CZ  . PHE A 1 72  ? 37.92000 -11.78100 56.47400 1.000 34.35000 ? 72  PHE A CZ  1 
ATOM   585  N  N   . LYS A 1 73  ? 43.75000 -16.04800 54.96900 1.000 30.68000 ? 73  LYS A N   1 
ATOM   586  C  CA  . LYS A 1 73  ? 44.70500 -17.13200 54.80500 1.000 31.44000 ? 73  LYS A CA  1 
ATOM   587  C  C   . LYS A 1 73  ? 44.97200 -17.87700 56.10400 1.000 31.73000 ? 73  LYS A C   1 
ATOM   588  O  O   . LYS A 1 73  ? 45.34600 -19.05600 56.06100 1.000 29.07000 ? 73  LYS A O   1 
ATOM   589  C  CB  . LYS A 1 73  ? 46.01200 -16.57300 54.22900 1.000 36.48000 ? 73  LYS A CB  1 
ATOM   590  C  CG  . LYS A 1 73  ? 45.77500 -15.78700 52.93200 1.000 43.59000 ? 73  LYS A CG  1 
ATOM   591  C  CD  . LYS A 1 73  ? 46.91700 -15.93100 51.94900 1.000 44.72000 ? 73  LYS A CD  1 
ATOM   592  C  CE  . LYS A 1 73  ? 46.57700 -15.29700 50.60200 1.000 45.08000 ? 73  LYS A CE  1 
ATOM   593  N  NZ  . LYS A 1 73  ? 47.82500 -14.86200 49.90200 1.000 57.95000 ? 73  LYS A NZ  1 
ATOM   594  N  N   . TYR A 1 74  ? 44.76100 -17.23600 57.25100 1.000 27.76000 ? 74  TYR A N   1 
ATOM   595  C  CA  . TYR A 1 74  ? 45.15500 -17.80800 58.53200 1.000 27.09000 ? 74  TYR A CA  1 
ATOM   596  C  C   . TYR A 1 74  ? 43.95300 -18.09500 59.41700 1.000 31.48000 ? 74  TYR A C   1 
ATOM   597  O  O   . TYR A 1 74  ? 44.03000 -18.01500 60.64700 1.000 27.88000 ? 74  TYR A O   1 
ATOM   598  C  CB  . TYR A 1 74  ? 46.16100 -16.90200 59.23500 1.000 26.94000 ? 74  TYR A CB  1 
ATOM   599  C  CG  . TYR A 1 74  ? 47.39200 -16.77600 58.39900 1.000 28.90000 ? 74  TYR A CG  1 
ATOM   600  C  CD1 . TYR A 1 74  ? 48.32900 -17.81100 58.35900 1.000 32.37000 ? 74  TYR A CD1 1 
ATOM   601  C  CD2 . TYR A 1 74  ? 47.59300 -15.66000 57.58500 1.000 33.29000 ? 74  TYR A CD2 1 
ATOM   602  C  CE1 . TYR A 1 74  ? 49.46100 -17.72400 57.55300 1.000 40.99000 ? 74  TYR A CE1 1 
ATOM   603  C  CE2 . TYR A 1 74  ? 48.70700 -15.56100 56.77900 1.000 41.07000 ? 74  TYR A CE2 1 
ATOM   604  C  CZ  . TYR A 1 74  ? 49.64100 -16.59500 56.76400 1.000 44.52000 ? 74  TYR A CZ  1 
ATOM   605  O  OH  . TYR A 1 74  ? 50.75100 -16.49700 55.96300 1.000 52.84000 ? 74  TYR A OH  1 
ATOM   606  N  N   . SER A 1 75  ? 42.83000 -18.48200 58.80400 1.000 24.20000 ? 75  SER A N   1 
ATOM   607  C  CA  . SER A 1 75  ? 41.64900 -18.79900 59.55700 1.000 22.05000 ? 75  SER A CA  1 
ATOM   608  C  C   . SER A 1 75  ? 40.99700 -20.03500 58.97000 1.000 24.98000 ? 75  SER A C   1 
ATOM   609  O  O   . SER A 1 75  ? 40.94300 -20.17700 57.73800 1.000 20.26000 ? 75  SER A O   1 
ATOM   610  C  CB  . SER A 1 75  ? 40.64900 -17.63600 59.53000 1.000 27.63000 ? 75  SER A CB  1 
ATOM   611  O  OG  . SER A 1 75  ? 41.23500 -16.49100 60.08800 1.000 24.56000 ? 75  SER A OG  1 
ATOM   612  N  N   . PRO A 1 76  ? 40.51800 -20.94500 59.81600 1.000 26.92000 ? 76  PRO A N   1 
ATOM   613  C  CA  . PRO A 1 76  ? 39.68300 -22.03500 59.31900 1.000 26.59000 ? 76  PRO A CA  1 
ATOM   614  C  C   . PRO A 1 76  ? 38.45200 -21.46900 58.64900 1.000 26.30000 ? 76  PRO A C   1 
ATOM   615  O  O   . PRO A 1 76  ? 37.91000 -20.44200 59.07000 1.000 24.35000 ? 76  PRO A O   1 
ATOM   616  C  CB  . PRO A 1 76  ? 39.30400 -22.82200 60.58900 1.000 23.62000 ? 76  PRO A CB  1 
ATOM   617  C  CG  . PRO A 1 76  ? 40.33700 -22.42100 61.62400 1.000 28.18000 ? 76  PRO A CG  1 
ATOM   618  C  CD  . PRO A 1 76  ? 40.80600 -21.04700 61.25600 1.000 25.30000 ? 76  PRO A CD  1 
ATOM   619  N  N   . ILE A 1 77  ? 38.03000 -22.13800 57.58000 1.000 24.23000 ? 77  ILE A N   1 
ATOM   620  C  CA  . ILE A 1 77  ? 36.81800 -21.76000 56.85700 1.000 27.93000 ? 77  ILE A CA  1 
ATOM   621  C  C   . ILE A 1 77  ? 36.04300 -23.03700 56.57100 1.000 24.99000 ? 77  ILE A C   1 
ATOM   622  O  O   . ILE A 1 77  ? 36.58800 -23.99400 56.01500 1.000 27.23000 ? 77  ILE A O   1 
ATOM   623  C  CB  . ILE A 1 77  ? 37.11500 -21.00200 55.55800 1.000 23.02000 ? 77  ILE A CB  1 
ATOM   624  C  CG1 . ILE A 1 77  ? 37.96000 -19.77500 55.85600 1.000 22.41000 ? 77  ILE A CG1 1 
ATOM   625  C  CG2 . ILE A 1 77  ? 35.82300 -20.57100 54.88000 1.000 26.39000 ? 77  ILE A CG2 1 
ATOM   626  C  CD1 . ILE A 1 77  ? 38.22500 -18.94000 54.62700 1.000 25.31000 ? 77  ILE A CD1 1 
ATOM   627  N  N   . TRP A 1 78  ? 34.80400 -23.08300 57.00100 1.000 24.89000 ? 78  TRP A N   1 
ATOM   628  C  CA  . TRP A 1 78  ? 33.97700 -24.25000 56.76500 1.000 27.47000 ? 78  TRP A CA  1 
ATOM   629  C  C   . TRP A 1 78  ? 32.88500 -23.87100 55.78000 1.000 25.99000 ? 78  TRP A C   1 
ATOM   630  O  O   . TRP A 1 78  ? 32.13100 -22.92800 56.02200 1.000 22.90000 ? 78  TRP A O   1 
ATOM   631  C  CB  . TRP A 1 78  ? 33.38900 -24.76300 58.07100 1.000 26.07000 ? 78  TRP A CB  1 
ATOM   632  C  CG  . TRP A 1 78  ? 32.49400 -25.92600 57.89900 1.000 29.82000 ? 78  TRP A CG  1 
ATOM   633  C  CD1 . TRP A 1 78  ? 32.86000 -27.22400 57.65800 1.000 28.73000 ? 78  TRP A CD1 1 
ATOM   634  C  CD2 . TRP A 1 78  ? 31.06900 -25.91800 57.99200 1.000 31.74000 ? 78  TRP A CD2 1 
ATOM   635  N  NE1 . TRP A 1 78  ? 31.74000 -28.02100 57.58200 1.000 28.71000 ? 78  TRP A NE1 1 
ATOM   636  C  CE2 . TRP A 1 78  ? 30.62900 -27.24300 57.78600 1.000 34.65000 ? 78  TRP A CE2 1 
ATOM   637  C  CE3 . TRP A 1 78  ? 30.11800 -24.91400 58.22700 1.000 32.03000 ? 78  TRP A CE3 1 
ATOM   638  C  CZ2 . TRP A 1 78  ? 29.28100 -27.59000 57.79800 1.000 34.26000 ? 78  TRP A CZ2 1 
ATOM   639  C  CZ3 . TRP A 1 78  ? 28.78900 -25.26100 58.25800 1.000 29.98000 ? 78  TRP A CZ3 1 
ATOM   640  C  CH2 . TRP A 1 78  ? 28.37600 -26.58400 58.04300 1.000 30.74000 ? 78  TRP A CH2 1 
ATOM   641  N  N   . ARG A 1 79  ? 32.82400 -24.59900 54.67300 1.000 29.06000 ? 79  ARG A N   1 
ATOM   642  C  CA  . ARG A 1 79  ? 31.76300 -24.49000 53.67500 1.000 31.88000 ? 79  ARG A CA  1 
ATOM   643  C  C   . ARG A 1 79  ? 30.72300 -25.57000 53.95700 1.000 30.48000 ? 79  ARG A C   1 
ATOM   644  O  O   . ARG A 1 79  ? 31.07100 -26.75100 54.06300 1.000 27.26000 ? 79  ARG A O   1 
ATOM   645  C  CB  . ARG A 1 79  ? 32.38000 -24.64900 52.27600 1.000 35.53000 ? 79  ARG A CB  1 
ATOM   646  C  CG  . ARG A 1 79  ? 31.49700 -24.42600 51.04500 1.000 38.23000 ? 79  ARG A CG  1 
ATOM   647  C  CD  . ARG A 1 79  ? 32.22000 -25.04100 49.81700 1.000 41.12000 ? 79  ARG A CD  1 
ATOM   648  N  NE  . ARG A 1 79  ? 32.04600 -24.27100 48.58900 1.000 48.45000 ? 79  ARG A NE  1 
ATOM   649  C  CZ  . ARG A 1 79  ? 32.93300 -24.22000 47.59000 1.000 53.21000 ? 79  ARG A CZ  1 
ATOM   650  N  NH1 . ARG A 1 79  ? 34.08100 -24.89800 47.65500 1.000 44.97000 ? 79  ARG A NH1 1 
ATOM   651  N  NH2 . ARG A 1 79  ? 32.67300 -23.47800 46.51300 1.000 50.74000 ? 79  ARG A NH2 1 
ATOM   652  N  N   . SER A 1 80  ? 29.45600 -25.18000 54.09500 1.000 27.37000 ? 80  SER A N   1 
ATOM   653  C  CA  . SER A 1 80  ? 28.43400 -26.18800 54.39900 1.000 32.31000 ? 80  SER A CA  1 
ATOM   654  C  C   . SER A 1 80  ? 28.17400 -27.07000 53.17700 1.000 30.22000 ? 80  SER A C   1 
ATOM   655  O  O   . SER A 1 80  ? 27.91500 -26.54500 52.08700 1.000 29.83000 ? 80  SER A O   1 
ATOM   656  C  CB  . SER A 1 80  ? 27.13400 -25.54000 54.86300 1.000 29.62000 ? 80  SER A CB  1 
ATOM   657  O  OG  . SER A 1 80  ? 26.14300 -26.52000 55.11000 1.000 28.39000 ? 80  SER A OG  1 
ATOM   658  N  N   . PRO A 1 81  ? 28.23800 -28.40600 53.31600 1.000 30.27000 ? 81  PRO A N   1 
ATOM   659  C  CA  . PRO A 1 81  ? 27.75800 -29.29200 52.23300 1.000 33.98000 ? 81  PRO A CA  1 
ATOM   660  C  C   . PRO A 1 81  ? 26.24900 -29.24100 52.04000 1.000 32.41000 ? 81  PRO A C   1 
ATOM   661  O  O   . PRO A 1 81  ? 25.75400 -29.70400 51.00600 1.000 35.70000 ? 81  PRO A O   1 
ATOM   662  C  CB  . PRO A 1 81  ? 28.17500 -30.69800 52.69800 1.000 28.77000 ? 81  PRO A CB  1 
ATOM   663  C  CG  . PRO A 1 81  ? 28.47300 -30.58100 54.13900 1.000 29.46000 ? 81  PRO A CG  1 
ATOM   664  C  CD  . PRO A 1 81  ? 28.50200 -29.13900 54.56100 1.000 30.87000 ? 81  PRO A CD  1 
ATOM   665  N  N   . ILE A 1 82  ? 25.50600 -28.77800 53.03900 1.000 34.04000 ? 82  ILE A N   1 
ATOM   666  C  CA  . ILE A 1 82  ? 24.05300 -28.68300 53.00200 1.000 36.61000 ? 82  ILE A CA  1 
ATOM   667  C  C   . ILE A 1 82  ? 23.70700 -27.21900 52.82800 1.000 28.01000 ? 82  ILE A C   1 
ATOM   668  O  O   . ILE A 1 82  ? 24.15700 -26.38900 53.61900 1.000 35.11000 ? 82  ILE A O   1 
ATOM   669  C  CB  . ILE A 1 82  ? 23.42200 -29.21300 54.30500 1.000 31.87000 ? 82  ILE A CB  1 
ATOM   670  C  CG1 . ILE A 1 82  ? 23.97800 -30.58100 54.69600 1.000 36.19000 ? 82  ILE A CG1 1 
ATOM   671  C  CG2 . ILE A 1 82  ? 21.90500 -29.21200 54.19900 1.000 36.38000 ? 82  ILE A CG2 1 
ATOM   672  C  CD1 . ILE A 1 82  ? 23.68900 -31.69400 53.68900 1.000 42.86000 ? 82  ILE A CD1 1 
ATOM   673  N  N   . LYS A 1 83  ? 22.89000 -26.89900 51.83300 1.000 34.06000 ? 83  LYS A N   1 
ATOM   674  C  CA  . LYS A 1 83  ? 22.49000 -25.51000 51.66300 1.000 28.50000 ? 83  LYS A CA  1 
ATOM   675  C  C   . LYS A 1 83  ? 21.51100 -25.12100 52.75700 1.000 28.12000 ? 83  LYS A C   1 
ATOM   676  O  O   . LYS A 1 83  ? 20.63500 -25.90400 53.13800 1.000 30.77000 ? 83  LYS A O   1 
ATOM   677  C  CB  . LYS A 1 83  ? 21.86300 -25.27500 50.29200 1.000 31.55000 ? 83  LYS A CB  1 
ATOM   678  C  CG  . LYS A 1 83  ? 22.79700 -25.55900 49.12000 1.000 34.18000 ? 83  LYS A CG  1 
ATOM   679  C  CD  . LYS A 1 83  ? 22.51900 -24.60700 47.97200 1.000 40.94000 ? 83  LYS A CD  1 
ATOM   680  C  CE  . LYS A 1 83  ? 23.44700 -24.86000 46.77900 1.000 51.92000 ? 83  LYS A CE  1 
ATOM   681  N  NZ  . LYS A 1 83  ? 22.78600 -24.52300 45.48300 1.000 54.84000 ? 83  LYS A NZ  1 
ATOM   682  N  N   . LEU A 1 84  ? 21.68400 -23.91700 53.27800 1.000 26.32000 ? 84  LEU A N   1 
ATOM   683  C  CA  . LEU A 1 84  ? 20.71000 -23.35200 54.19700 1.000 29.48000 ? 84  LEU A CA  1 
ATOM   684  C  C   . LEU A 1 84  ? 19.38200 -23.16200 53.47200 1.000 32.10000 ? 84  LEU A C   1 
ATOM   685  O  O   . LEU A 1 84  ? 19.35400 -22.78400 52.29800 1.000 30.44000 ? 84  LEU A O   1 
ATOM   686  C  CB  . LEU A 1 84  ? 21.22400 -22.02400 54.73500 1.000 30.37000 ? 84  LEU A CB  1 
ATOM   687  C  CG  . LEU A 1 84  ? 20.49200 -21.28200 55.85000 1.000 32.88000 ? 84  LEU A CG  1 
ATOM   688  C  CD1 . LEU A 1 84  ? 20.18300 -22.19400 57.03300 1.000 32.57000 ? 84  LEU A CD1 1 
ATOM   689  C  CD2 . LEU A 1 84  ? 21.34900 -20.10300 56.27100 1.000 35.57000 ? 84  LEU A CD2 1 
ATOM   690  N  N   . TYR A 1 85  ? 18.28400 -23.47100 54.16000 1.000 27.55000 ? 85  TYR A N   1 
ATOM   691  C  CA  . TYR A 1 85  ? 16.92500 -23.37000 53.63600 1.000 28.32000 ? 85  TYR A CA  1 
ATOM   692  C  C   . TYR A 1 85  ? 16.62700 -24.35600 52.51500 1.000 31.97000 ? 85  TYR A C   1 
ATOM   693  O  O   . TYR A 1 85  ? 15.60200 -24.20900 51.82500 1.000 32.27000 ? 85  TYR A O   1 
ATOM   694  C  CB  . TYR A 1 85  ? 16.60100 -21.95000 53.15800 1.000 25.96000 ? 85  TYR A CB  1 
ATOM   695  C  CG  . TYR A 1 85  ? 16.86400 -20.96300 54.24600 1.000 31.27000 ? 85  TYR A CG  1 
ATOM   696  C  CD1 . TYR A 1 85  ? 16.34500 -21.17400 55.51300 1.000 31.39000 ? 85  TYR A CD1 1 
ATOM   697  C  CD2 . TYR A 1 85  ? 17.64700 -19.84900 54.03100 1.000 31.63000 ? 85  TYR A CD2 1 
ATOM   698  C  CE1 . TYR A 1 85  ? 16.59200 -20.30400 56.52200 1.000 36.71000 ? 85  TYR A CE1 1 
ATOM   699  C  CE2 . TYR A 1 85  ? 17.90100 -18.96900 55.04200 1.000 34.54000 ? 85  TYR A CE2 1 
ATOM   700  C  CZ  . TYR A 1 85  ? 17.37500 -19.20600 56.29200 1.000 33.79000 ? 85  TYR A CZ  1 
ATOM   701  O  OH  . TYR A 1 85  ? 17.62000 -18.34000 57.32900 1.000 40.04000 ? 85  TYR A OH  1 
ATOM   702  N  N   . SER A 1 86  ? 17.47400 -25.36100 52.31100 1.000 26.22000 ? 86  SER A N   1 
ATOM   703  C  CA  . SER A 1 86  ? 17.03200 -26.49800 51.53200 1.000 29.74000 ? 86  SER A CA  1 
ATOM   704  C  C   . SER A 1 86  ? 16.00800 -27.28800 52.34400 1.000 24.93000 ? 86  SER A C   1 
ATOM   705  O  O   . SER A 1 86  ? 15.82500 -27.06700 53.53800 1.000 28.48000 ? 86  SER A O   1 
ATOM   706  C  CB  . SER A 1 86  ? 18.21500 -27.39100 51.15600 1.000 29.30000 ? 86  SER A CB  1 
ATOM   707  O  OG  . SER A 1 86  ? 18.88300 -27.82800 52.33200 1.000 32.29000 ? 86  SER A OG  1 
ATOM   708  N  N   . VAL A 1 87  ? 15.32700 -28.21700 51.69400 1.000 28.18000 ? 87  VAL A N   1 
ATOM   709  C  CA  . VAL A 1 87  ? 14.35600 -29.06600 52.36900 1.000 28.40000 ? 87  VAL A CA  1 
ATOM   710  C  C   . VAL A 1 87  ? 14.81100 -30.49900 52.18800 1.000 30.28000 ? 87  VAL A C   1 
ATOM   711  O  O   . VAL A 1 87  ? 15.05600 -30.93300 51.05900 1.000 35.10000 ? 87  VAL A O   1 
ATOM   712  C  CB  . VAL A 1 87  ? 12.92200 -28.87200 51.84500 1.000 30.11000 ? 87  VAL A CB  1 
ATOM   713  C  CG1 . VAL A 1 87  ? 11.97800 -29.90800 52.50400 1.000 29.51000 ? 87  VAL A CG1 1 
ATOM   714  C  CG2 . VAL A 1 87  ? 12.44000 -27.43200 52.12700 1.000 25.86000 ? 87  VAL A CG2 1 
ATOM   715  N  N   . VAL A 1 88  ? 14.95000 -31.22300 53.29700 1.000 31.12000 ? 88  VAL A N   1 
ATOM   716  C  CA  . VAL A 1 88  ? 15.58000 -32.53400 53.27900 1.000 34.53000 ? 88  VAL A CA  1 
ATOM   717  C  C   . VAL A 1 88  ? 14.65100 -33.57500 53.88700 1.000 32.68000 ? 88  VAL A C   1 
ATOM   718  O  O   . VAL A 1 88  ? 13.76900 -33.27100 54.69600 1.000 30.53000 ? 88  VAL A O   1 
ATOM   719  C  CB  . VAL A 1 88  ? 16.94400 -32.52300 54.00700 1.000 34.31000 ? 88  VAL A CB  1 
ATOM   720  C  CG1 . VAL A 1 88  ? 17.89100 -31.57900 53.29000 1.000 33.83000 ? 88  VAL A CG1 1 
ATOM   721  C  CG2 . VAL A 1 88  ? 16.75400 -32.11600 55.46500 1.000 26.35000 ? 88  VAL A CG2 1 
ATOM   722  N  N   . SER A 1 89  ? 14.85300 -34.81500 53.45400 1.000 35.74000 ? 89  SER A N   1 
ATOM   723  C  CA  . SER A 1 89  ? 14.12100 -35.98100 53.92500 1.000 37.50000 ? 89  SER A CA  1 
ATOM   724  C  C   . SER A 1 89  ? 15.00400 -36.76400 54.87700 1.000 31.85000 ? 89  SER A C   1 
ATOM   725  O  O   . SER A 1 89  ? 16.17500 -37.02200 54.58700 1.000 38.10000 ? 89  SER A O   1 
ATOM   726  C  CB  . SER A 1 89  ? 13.69900 -36.86900 52.75700 1.000 36.16000 ? 89  SER A CB  1 
ATOM   727  O  OG  . SER A 1 89  ? 12.81600 -36.20100 51.87300 1.000 39.38000 ? 89  SER A OG  1 
ATOM   728  N  N   . THR A 1 90  ? 14.42300 -37.17400 55.99000 1.000 31.84000 ? 90  THR A N   1 
ATOM   729  C  CA  . THR A 1 90  ? 15.15100 -37.72500 57.12200 1.000 39.94000 ? 90  THR A CA  1 
ATOM   730  C  C   . THR A 1 90  ? 14.74800 -39.17500 57.34900 1.000 38.50000 ? 90  THR A C   1 
ATOM   731  O  O   . THR A 1 90  ? 13.60900 -39.56800 57.08700 1.000 38.38000 ? 90  THR A O   1 
ATOM   732  C  CB  . THR A 1 90  ? 14.86200 -36.87100 58.37600 1.000 30.77000 ? 90  THR A CB  1 
ATOM   733  O  OG1 . THR A 1 90  ? 15.70600 -35.70800 58.35500 1.000 40.91000 ? 90  THR A OG1 1 
ATOM   734  C  CG2 . THR A 1 90  ? 15.07900 -37.64500 59.65400 1.000 38.79000 ? 90  THR A CG2 1 
ATOM   735  N  N   . GLU A 1 91  ? 15.69400 -39.97400 57.83000 1.000 43.53000 ? 91  GLU A N   1 
ATOM   736  C  CA  . GLU A 1 91  ? 15.39100 -41.31100 58.31300 1.000 48.46000 ? 91  GLU A CA  1 
ATOM   737  C  C   . GLU A 1 91  ? 16.15900 -41.55400 59.60000 1.000 43.52000 ? 91  GLU A C   1 
ATOM   738  O  O   . GLU A 1 91  ? 17.34300 -41.21900 59.69800 1.000 42.17000 ? 91  GLU A O   1 
ATOM   739  C  CB  . GLU A 1 91  ? 15.75700 -42.38500 57.28600 1.000 47.53000 ? 91  GLU A CB  1 
ATOM   740  C  CG  . GLU A 1 91  ? 14.58300 -43.01700 56.59300 1.000 54.59000 ? 91  GLU A CG  1 
ATOM   741  C  CD  . GLU A 1 91  ? 14.99400 -44.27600 55.85700 1.000 61.58000 ? 91  GLU A CD  1 
ATOM   742  O  OE1 . GLU A 1 91  ? 15.51400 -45.20300 56.51600 1.000 71.06000 ? 91  GLU A OE1 1 
ATOM   743  O  OE2 . GLU A 1 91  ? 14.81300 -44.33400 54.62000 1.000 60.31000 ? 91  GLU A OE2 1 
ATOM   744  N  N   . ASP A 1 92  ? 15.48200 -42.14500 60.58100 1.000 45.19000 ? 92  ASP A N   1 
ATOM   745  C  CA  . ASP A 1 92  ? 16.08600 -42.42300 61.88200 1.000 45.08000 ? 92  ASP A CA  1 
ATOM   746  C  C   . ASP A 1 92  ? 16.72500 -41.17100 62.45700 1.000 42.90000 ? 92  ASP A C   1 
ATOM   747  O  O   . ASP A 1 92  ? 17.77100 -41.24200 63.10900 1.000 39.59000 ? 92  ASP A O   1 
ATOM   748  C  CB  . ASP A 1 92  ? 17.11000 -43.55500 61.78700 1.000 46.38000 ? 92  ASP A CB  1 
ATOM   749  C  CG  . ASP A 1 92  ? 16.47000 -44.88000 61.38100 1.000 60.39000 ? 92  ASP A CG  1 
ATOM   750  O  OD1 . ASP A 1 92  ? 15.57400 -45.35300 62.11600 1.000 61.04000 ? 92  ASP A OD1 1 
ATOM   751  O  OD2 . ASP A 1 92  ? 16.83400 -45.43600 60.31900 1.000 57.04000 ? 92  ASP A OD2 1 
ATOM   752  N  N   . CYS A 1 93  ? 16.12300 -40.01100 62.19400 1.000 33.55000 ? 93  CYS A N   1 
ATOM   753  C  CA  . CYS A 1 93  ? 16.60300 -38.75400 62.74800 1.000 37.73000 ? 93  CYS A CA  1 
ATOM   754  C  C   . CYS A 1 93  ? 18.01300 -38.41700 62.22800 1.000 41.24000 ? 93  CYS A C   1 
ATOM   755  O  O   . CYS A 1 93  ? 18.82700 -37.80900 62.92400 1.000 37.60000 ? 93  CYS A O   1 
ATOM   756  C  CB  . CYS A 1 93  ? 16.55700 -38.77300 64.28700 1.000 39.49000 ? 93  CYS A CB  1 
ATOM   757  S  SG  . CYS A 1 93  ? 16.40300 -37.11500 65.03000 1.000 45.35000 ? 93  CYS A SG  1 
ATOM   758  N  N   . LYS A 1 94  ? 18.29700 -38.82300 60.98600 1.000 35.01000 ? 94  LYS A N   1 
ATOM   759  C  CA  . LYS A 1 94  ? 19.57000 -38.54000 60.33400 1.000 38.39000 ? 94  LYS A CA  1 
ATOM   760  C  C   . LYS A 1 94  ? 19.31200 -38.03500 58.92800 1.000 34.68000 ? 94  LYS A C   1 
ATOM   761  O  O   . LYS A 1 94  ? 18.33200 -38.41900 58.28200 1.000 36.94000 ? 94  LYS A O   1 
ATOM   762  C  CB  . LYS A 1 94  ? 20.47900 -39.77400 60.22500 1.000 43.92000 ? 94  LYS A CB  1 
ATOM   763  C  CG  . LYS A 1 94  ? 21.06700 -40.31600 61.49600 1.000 44.15000 ? 94  LYS A CG  1 
ATOM   764  C  CD  . LYS A 1 94  ? 22.00500 -41.48200 61.15800 1.000 43.18000 ? 94  LYS A CD  1 
ATOM   765  C  CE  . LYS A 1 94  ? 21.45900 -42.33300 60.02200 1.000 50.84000 ? 94  LYS A CE  1 
ATOM   766  N  NZ  . LYS A 1 94  ? 22.55000 -43.02800 59.28300 1.000 67.05000 ? 94  LYS A NZ  1 
ATOM   767  N  N   . PHE A 1 95  ? 20.19000 -37.16700 58.45400 1.000 36.66000 ? 95  PHE A N   1 
ATOM   768  C  CA  . PHE A 1 95  ? 20.23100 -36.81500 57.04200 1.000 37.24000 ? 95  PHE A CA  1 
ATOM   769  C  C   . PHE A 1 95  ? 21.66100 -36.98500 56.58200 1.000 39.29000 ? 95  PHE A C   1 
ATOM   770  O  O   . PHE A 1 95  ? 22.56800 -36.33200 57.11400 1.000 37.74000 ? 95  PHE A O   1 
ATOM   771  C  CB  . PHE A 1 95  ? 19.75100 -35.39100 56.76400 1.000 30.36000 ? 95  PHE A CB  1 
ATOM   772  C  CG  . PHE A 1 95  ? 19.83900 -35.03200 55.31200 1.000 38.26000 ? 95  PHE A CG  1 
ATOM   773  C  CD1 . PHE A 1 95  ? 19.02800 -35.66500 54.38300 1.000 40.57000 ? 95  PHE A CD1 1 
ATOM   774  C  CD2 . PHE A 1 95  ? 20.76800 -34.10300 54.86200 1.000 36.88000 ? 95  PHE A CD2 1 
ATOM   775  C  CE1 . PHE A 1 95  ? 19.11000 -35.35500 53.03600 1.000 37.52000 ? 95  PHE A CE1 1 
ATOM   776  C  CE2 . PHE A 1 95  ? 20.86200 -33.79700 53.52100 1.000 37.07000 ? 95  PHE A CE2 1 
ATOM   777  C  CZ  . PHE A 1 95  ? 20.03000 -34.42800 52.60300 1.000 41.83000 ? 95  PHE A CZ  1 
ATOM   778  N  N   . MET A 1 96  ? 21.85400 -37.87100 55.61600 1.000 37.95000 ? 96  MET A N   1 
ATOM   779  C  CA  . MET A 1 96  ? 23.20100 -38.18800 55.18900 1.000 42.17000 ? 96  MET A CA  1 
ATOM   780  C  C   . MET A 1 96  ? 24.01800 -38.60900 56.39000 1.000 47.30000 ? 96  MET A C   1 
ATOM   781  O  O   . MET A 1 96  ? 23.66600 -39.56900 57.06600 1.000 51.01000 ? 96  MET A O   1 
ATOM   782  C  CB  . MET A 1 96  ? 23.80700 -36.98800 54.49000 1.000 43.53000 ? 96  MET A CB  1 
ATOM   783  C  CG  . MET A 1 96  ? 23.14700 -36.86400 53.16200 1.000 50.97000 ? 96  MET A CG  1 
ATOM   784  S  SD  . MET A 1 96  ? 23.90300 -35.56900 52.22500 1.000 67.85000 ? 96  MET A SD  1 
ATOM   785  C  CE  . MET A 1 96  ? 25.34300 -36.48500 51.76300 1.000 61.90000 ? 96  MET A CE  1 
ATOM   786  N  N   . ASN A 1 97  ? 25.08900 -37.87700 56.67300 1.000 47.63000 ? 97  ASN A N   1 
ATOM   787  C  CA  . ASN A 1 97  ? 25.96400 -38.22300 57.78100 1.000 48.71000 ? 97  ASN A CA  1 
ATOM   788  C  C   . ASN A 1 97  ? 25.70300 -37.38500 59.01700 1.000 51.79000 ? 97  ASN A C   1 
ATOM   789  O  O   . ASN A 1 97  ? 26.51700 -37.39900 59.94300 1.000 54.40000 ? 97  ASN A O   1 
ATOM   790  C  CB  . ASN A 1 97  ? 27.43300 -38.10800 57.38400 1.000 58.89000 ? 97  ASN A CB  1 
ATOM   791  C  CG  . ASN A 1 97  ? 27.92900 -39.31300 56.58100 1.000 73.96000 ? 97  ASN A CG  1 
ATOM   792  O  OD1 . ASN A 1 97  ? 27.35300 -40.40500 56.67500 1.000 69.20000 ? 97  ASN A OD1 1 
ATOM   793  N  ND2 . ASN A 1 97  ? 28.91900 -39.10200 55.72400 1.000 72.06000 ? 97  ASN A ND2 1 
ATOM   794  N  N   . PHE A 1 98  ? 24.55900 -36.70200 59.08500 1.000 40.90000 ? 98  PHE A N   1 
ATOM   795  C  CA  . PHE A 1 98  ? 24.31600 -35.70900 60.12200 1.000 46.12000 ? 98  PHE A CA  1 
ATOM   796  C  C   . PHE A 1 98  ? 23.10200 -36.07100 60.96100 1.000 40.62000 ? 98  PHE A C   1 
ATOM   797  O  O   . PHE A 1 98  ? 22.14000 -36.67200 60.47600 1.000 39.84000 ? 98  PHE A O   1 
ATOM   798  C  CB  . PHE A 1 98  ? 24.08100 -34.31300 59.52700 1.000 39.98000 ? 98  PHE A CB  1 
ATOM   799  C  CG  . PHE A 1 98  ? 25.17900 -33.84200 58.63500 1.000 43.70000 ? 98  PHE A CG  1 
ATOM   800  C  CD1 . PHE A 1 98  ? 26.43400 -33.57000 59.14800 1.000 45.96000 ? 98  PHE A CD1 1 
ATOM   801  C  CD2 . PHE A 1 98  ? 24.96900 -33.68100 57.27400 1.000 39.74000 ? 98  PHE A CD2 1 
ATOM   802  C  CE1 . PHE A 1 98  ? 27.47200 -33.13600 58.31700 1.000 37.31000 ? 98  PHE A CE1 1 
ATOM   803  C  CE2 . PHE A 1 98  ? 26.00400 -33.25300 56.44000 1.000 39.87000 ? 98  PHE A CE2 1 
ATOM   804  C  CZ  . PHE A 1 98  ? 27.25600 -32.98900 56.96700 1.000 36.66000 ? 98  PHE A CZ  1 
ATOM   805  N  N   . ILE A 1 99  ? 23.15900 -35.67700 62.22400 1.000 37.26000 ? 99  ILE A N   1 
ATOM   806  C  CA  . ILE A 1 99  ? 22.00000 -35.68100 63.10400 1.000 39.35000 ? 99  ILE A CA  1 
ATOM   807  C  C   . ILE A 1 99  ? 21.11000 -34.49400 62.75200 1.000 39.84000 ? 99  ILE A C   1 
ATOM   808  O  O   . ILE A 1 99  ? 21.59400 -33.41900 62.36500 1.000 35.65000 ? 99  ILE A O   1 
ATOM   809  C  CB  . ILE A 1 99  ? 22.46000 -35.60600 64.57300 1.000 40.27000 ? 99  ILE A CB  1 
ATOM   810  C  CG1 . ILE A 1 99  ? 23.62100 -36.55700 64.82200 1.000 48.22000 ? 99  ILE A CG1 1 
ATOM   811  C  CG2 . ILE A 1 99  ? 21.31100 -35.86400 65.52400 1.000 41.38000 ? 99  ILE A CG2 1 
ATOM   812  C  CD1 . ILE A 1 99  ? 24.31800 -36.28500 66.13600 1.000 54.88000 ? 99  ILE A CD1 1 
ATOM   813  N  N   . VAL A 1 100 ? 19.79700 -34.66900 62.89600 1.000 37.75000 ? 100 VAL A N   1 
ATOM   814  C  CA  . VAL A 1 100 ? 18.86700 -33.55900 62.72300 1.000 36.34000 ? 100 VAL A CA  1 
ATOM   815  C  C   . VAL A 1 100 ? 18.08900 -33.37900 64.01800 1.000 34.01000 ? 100 VAL A C   1 
ATOM   816  O  O   . VAL A 1 100 ? 17.91700 -34.32600 64.79300 1.000 33.60000 ? 100 VAL A O   1 
ATOM   817  C  CB  . VAL A 1 100 ? 17.91300 -33.75700 61.51800 1.000 36.04000 ? 100 VAL A CB  1 
ATOM   818  C  CG1 . VAL A 1 100 ? 18.70800 -34.05600 60.23900 1.000 30.02000 ? 100 VAL A CG1 1 
ATOM   819  C  CG2 . VAL A 1 100 ? 16.86800 -34.84500 61.79600 1.000 32.51000 ? 100 VAL A CG2 1 
ATOM   820  N  N   . GLU A 1 101 ? 17.61000 -32.17800 64.22100 1.000 32.08000 ? 101 GLU A N   1 
ATOM   821  C  CA  . GLU A 1 101 ? 16.79200 -31.82300 65.39100 1.000 38.36000 ? 101 GLU A CA  1 
ATOM   822  C  C   . GLU A 1 101 ? 15.91900 -30.63200 64.99600 1.000 36.33000 ? 101 GLU A C   1 
ATOM   823  O  O   . GLU A 1 101 ? 16.45700 -29.68400 64.46600 1.000 37.78000 ? 101 GLU A O   1 
ATOM   824  C  CB  . GLU A 1 101 ? 17.68200 -31.42300 66.56300 1.000 48.45000 ? 101 GLU A CB  1 
ATOM   825  C  CG  . GLU A 1 101 ? 16.90900 -30.91000 67.75900 1.000 60.01000 ? 101 GLU A CG  1 
ATOM   826  C  CD  . GLU A 1 101 ? 17.75900 -30.70800 68.99700 1.000 73.38000 ? 101 GLU A CD  1 
ATOM   827  O  OE1 . GLU A 1 101 ? 18.67900 -29.86700 68.95500 1.000 76.96000 ? 101 GLU A OE1 1 
ATOM   828  O  OE2 . GLU A 1 101 ? 17.50500 -31.39700 69.99700 1.000 79.76000 ? 101 GLU A OE2 1 
ATOM   829  N  N   . PRO A 1 102 ? 14.59800 -30.64600 65.21900 1.000 36.70000 ? 102 PRO A N   1 
ATOM   830  C  CA  . PRO A 1 102 ? 13.91000 -31.85900 65.63800 1.000 38.45000 ? 102 PRO A CA  1 
ATOM   831  C  C   . PRO A 1 102 ? 13.88200 -32.98300 64.59100 1.000 38.32000 ? 102 PRO A C   1 
ATOM   832  O  O   . PRO A 1 102 ? 14.31300 -32.75500 63.49800 1.000 34.31000 ? 102 PRO A O   1 
ATOM   833  C  CB  . PRO A 1 102 ? 12.50700 -31.34400 65.94000 1.000 36.45000 ? 102 PRO A CB  1 
ATOM   834  C  CG  . PRO A 1 102 ? 12.33000 -30.18500 65.01100 1.000 34.89000 ? 102 PRO A CG  1 
ATOM   835  C  CD  . PRO A 1 102 ? 13.69200 -29.53500 64.98600 1.000 32.26000 ? 102 PRO A CD  1 
ATOM   836  N  N   . CYS A 1 103 ? 13.34900 -34.14700 64.95900 1.000 37.42000 ? 103 CYS A N   1 
ATOM   837  C  CA  . CYS A 1 103 ? 13.38700 -35.33600 64.06100 1.000 41.32000 ? 103 CYS A CA  1 
ATOM   838  C  C   . CYS A 1 103 ? 12.24800 -35.31000 63.04200 1.000 40.61000 ? 103 CYS A C   1 
ATOM   839  O  O   . CYS A 1 103 ? 11.54200 -36.29600 62.94600 1.000 45.62000 ? 103 CYS A O   1 
ATOM   840  C  CB  . CYS A 1 103 ? 13.31300 -36.65000 64.83700 1.000 44.35000 ? 103 CYS A CB  1 
ATOM   841  S  SG  . CYS A 1 103 ? 14.64000 -36.98900 66.02500 1.000 56.16000 ? 103 CYS A SG  1 
ATOM   842  N  N   . LEU A 1 104 ? 12.10300 -34.22200 62.30900 1.000 40.13000 ? 104 LEU A N   1 
ATOM   843  C  CA  . LEU A 1 104 ? 11.11300 -34.14000 61.24500 1.000 42.19000 ? 104 LEU A CA  1 
ATOM   844  C  C   . LEU A 1 104 ? 11.52300 -35.06700 60.11000 1.000 37.93000 ? 104 LEU A C   1 
ATOM   845  O  O   . LEU A 1 104 ? 12.69800 -35.13600 59.75000 1.000 41.85000 ? 104 LEU A O   1 
ATOM   846  C  CB  . LEU A 1 104 ? 10.98600 -32.70300 60.73400 1.000 31.09000 ? 104 LEU A CB  1 
ATOM   847  C  CG  . LEU A 1 104 ? 10.72000 -31.69200 61.84500 1.000 31.68000 ? 104 LEU A CG  1 
ATOM   848  C  CD1 . LEU A 1 104 ? 10.67000 -30.29700 61.30100 1.000 25.50000 ? 104 LEU A CD1 1 
ATOM   849  C  CD2 . LEU A 1 104 ? 9.43900  -32.03600 62.56200 1.000 33.24000 ? 104 LEU A CD2 1 
ATOM   850  N  N   . SER A 1 105 ? 10.55200 -35.80300 59.56500 1.000 38.32000 ? 105 SER A N   1 
ATOM   851  C  CA  . SER A 1 105 ? 10.82500 -36.64700 58.40200 1.000 37.82000 ? 105 SER A CA  1 
ATOM   852  C  C   . SER A 1 105 ? 11.07500 -35.81000 57.16100 1.000 37.55000 ? 105 SER A C   1 
ATOM   853  O  O   . SER A 1 105 ? 11.77200 -36.25100 56.23800 1.000 39.48000 ? 105 SER A O   1 
ATOM   854  C  CB  . SER A 1 105 ? 9.66000  -37.59600 58.15400 1.000 41.26000 ? 105 SER A CB  1 
ATOM   855  O  OG  . SER A 1 105 ? 9.68300  -38.65500 59.10200 1.000 51.53000 ? 105 SER A OG  1 
ATOM   856  N  N   . GLU A 1 106 ? 10.49400 -34.61600 57.11500 1.000 33.46000 ? 106 GLU A N   1 
ATOM   857  C  CA  . GLU A 1 106 ? 10.76500 -33.62500 56.09000 1.000 37.27000 ? 106 GLU A CA  1 
ATOM   858  C  C   . GLU A 1 106 ? 10.93200 -32.29700 56.79500 1.000 28.40000 ? 106 GLU A C   1 
ATOM   859  O  O   . GLU A 1 106 ? 10.10600 -31.93500 57.63800 1.000 25.88000 ? 106 GLU A O   1 
ATOM   860  C  CB  . GLU A 1 106 ? 9.62900  -33.55000 55.06700 1.000 36.32000 ? 106 GLU A CB  1 
ATOM   861  C  CG  . GLU A 1 106 ? 10.01100 -32.84800 53.80100 1.000 38.51000 ? 106 GLU A CG  1 
ATOM   862  C  CD  . GLU A 1 106 ? 10.49800 -33.81600 52.73400 1.000 48.70000 ? 106 GLU A CD  1 
ATOM   863  O  OE1 . GLU A 1 106 ? 10.92700 -34.93700 53.10000 1.000 52.38000 ? 106 GLU A OE1 1 
ATOM   864  O  OE2 . GLU A 1 106 ? 10.43900 -33.45900 51.53300 1.000 54.53000 ? 106 GLU A OE2 1 
ATOM   865  N  N   . GLY A 1 107 ? 11.98500 -31.57400 56.46300 1.000 30.08000 ? 107 GLY A N   1 
ATOM   866  C  CA  . GLY A 1 107 ? 12.26900 -30.35700 57.19200 1.000 28.85000 ? 107 GLY A CA  1 
ATOM   867  C  C   . GLY A 1 107 ? 13.08400 -29.36700 56.39900 1.000 32.08000 ? 107 GLY A C   1 
ATOM   868  O  O   . GLY A 1 107 ? 13.87600 -29.73300 55.51700 1.000 25.40000 ? 107 GLY A O   1 
ATOM   869  N  N   . LEU A 1 108 ? 12.89300 -28.09600 56.74900 1.000 24.78000 ? 108 LEU A N   1 
ATOM   870  C  CA  . LEU A 1 108 ? 13.68900 -26.98900 56.24500 1.000 29.86000 ? 108 LEU A CA  1 
ATOM   871  C  C   . LEU A 1 108 ? 14.94200 -26.84100 57.09800 1.000 28.51000 ? 108 LEU A C   1 
ATOM   872  O  O   . LEU A 1 108 ? 14.84900 -26.68000 58.32200 1.000 26.67000 ? 108 LEU A O   1 
ATOM   873  C  CB  . LEU A 1 108 ? 12.85800 -25.71100 56.28300 1.000 24.32000 ? 108 LEU A CB  1 
ATOM   874  C  CG  . LEU A 1 108 ? 13.55300 -24.46300 55.76700 1.000 29.42000 ? 108 LEU A CG  1 
ATOM   875  C  CD1 . LEU A 1 108 ? 13.57000 -24.44500 54.23000 1.000 26.59000 ? 108 LEU A CD1 1 
ATOM   876  C  CD2 . LEU A 1 108 ? 12.80800 -23.28800 56.33500 1.000 28.65000 ? 108 LEU A CD2 1 
ATOM   877  N  N   . VAL A 1 109 ? 16.10800 -26.90800 56.45800 1.000 26.06000 ? 109 VAL A N   1 
ATOM   878  C  CA  . VAL A 1 109 ? 17.38600 -26.68800 57.12900 1.000 26.47000 ? 109 VAL A CA  1 
ATOM   879  C  C   . VAL A 1 109 ? 17.45600 -25.22800 57.54800 1.000 29.34000 ? 109 VAL A C   1 
ATOM   880  O  O   . VAL A 1 109 ? 17.55700 -24.34000 56.69800 1.000 29.27000 ? 109 VAL A O   1 
ATOM   881  C  CB  . VAL A 1 109 ? 18.56900 -27.04900 56.22200 1.000 25.36000 ? 109 VAL A CB  1 
ATOM   882  C  CG1 . VAL A 1 109 ? 19.91300 -26.75600 56.94400 1.000 27.35000 ? 109 VAL A CG1 1 
ATOM   883  C  CG2 . VAL A 1 109 ? 18.47400 -28.49300 55.74400 1.000 26.99000 ? 109 VAL A CG2 1 
ATOM   884  N  N   . ILE A 1 110 ? 17.41800 -24.95700 58.84800 1.000 26.02000 ? 110 ILE A N   1 
ATOM   885  C  CA  . ILE A 1 110 ? 17.54300 -23.57600 59.29600 1.000 29.05000 ? 110 ILE A CA  1 
ATOM   886  C  C   . ILE A 1 110 ? 18.85100 -23.30400 60.02100 1.000 28.46000 ? 110 ILE A C   1 
ATOM   887  O  O   . ILE A 1 110 ? 19.17500 -22.12800 60.25100 1.000 28.68000 ? 110 ILE A O   1 
ATOM   888  C  CB  . ILE A 1 110 ? 16.33300 -23.13800 60.14700 1.000 24.98000 ? 110 ILE A CB  1 
ATOM   889  C  CG1 . ILE A 1 110 ? 16.27600 -23.88600 61.47400 1.000 32.29000 ? 110 ILE A CG1 1 
ATOM   890  C  CG2 . ILE A 1 110 ? 15.05700 -23.39000 59.37700 1.000 24.67000 ? 110 ILE A CG2 1 
ATOM   891  C  CD1 . ILE A 1 110 ? 15.26500 -23.28500 62.46800 1.000 24.43000 ? 110 ILE A CD1 1 
ATOM   892  N  N   . LYS A 1 111 ? 19.63100 -24.33400 60.35300 1.000 25.15000 ? 111 LYS A N   1 
ATOM   893  C  CA  . LYS A 1 111 ? 21.00700 -24.13700 60.79700 1.000 31.70000 ? 111 LYS A CA  1 
ATOM   894  C  C   . LYS A 1 111 ? 21.86100 -25.22900 60.16000 1.000 30.86000 ? 111 LYS A C   1 
ATOM   895  O  O   . LYS A 1 111 ? 21.51800 -26.42300 60.26800 1.000 33.17000 ? 111 LYS A O   1 
ATOM   896  C  CB  . LYS A 1 111 ? 21.15400 -24.17200 62.31800 1.000 28.12000 ? 111 LYS A CB  1 
ATOM   897  C  CG  . LYS A 1 111 ? 22.59600 -24.00000 62.80600 1.000 33.72000 ? 111 LYS A CG  1 
ATOM   898  C  CD  . LYS A 1 111 ? 22.75900 -24.43400 64.26600 1.000 48.78000 ? 111 LYS A CD  1 
ATOM   899  C  CE  . LYS A 1 111 ? 24.00100 -23.81300 64.90900 1.000 53.36000 ? 111 LYS A CE  1 
ATOM   900  N  NZ  . LYS A 1 111 ? 23.94700 -23.92900 66.39600 1.000 60.02000 ? 111 LYS A NZ  1 
ATOM   901  N  N   . PRO A 1 112 ? 22.97600 -24.86600 59.53300 1.000 34.22000 ? 112 PRO A N   1 
ATOM   902  C  CA  . PRO A 1 112 ? 23.80400 -25.84800 58.84600 1.000 30.46000 ? 112 PRO A CA  1 
ATOM   903  C  C   . PRO A 1 112 ? 24.52700 -26.72600 59.85400 1.000 33.30000 ? 112 PRO A C   1 
ATOM   904  O  O   . PRO A 1 112 ? 24.53500 -26.42100 61.05500 1.000 32.69000 ? 112 PRO A O   1 
ATOM   905  C  CB  . PRO A 1 112 ? 24.79400 -24.97900 58.04600 1.000 35.75000 ? 112 PRO A CB  1 
ATOM   906  C  CG  . PRO A 1 112 ? 24.38500 -23.52900 58.31500 1.000 35.51000 ? 112 PRO A CG  1 
ATOM   907  C  CD  . PRO A 1 112 ? 23.61200 -23.53600 59.56200 1.000 33.56000 ? 112 PRO A CD  1 
ATOM   908  N  N   . PRO A 1 113 ? 25.13600 -27.82900 59.41000 1.000 31.69000 ? 113 PRO A N   1 
ATOM   909  C  CA  . PRO A 1 113 ? 25.77000 -28.79400 60.34300 1.000 33.09000 ? 113 PRO A CA  1 
ATOM   910  C  C   . PRO A 1 113 ? 27.20600 -28.43600 60.71800 1.000 41.37000 ? 113 PRO A C   1 
ATOM   911  O  O   . PRO A 1 113 ? 28.16800 -29.16500 60.40700 1.000 36.59000 ? 113 PRO A O   1 
ATOM   912  C  CB  . PRO A 1 113 ? 25.69700 -30.10100 59.54900 1.000 36.90000 ? 113 PRO A CB  1 
ATOM   913  C  CG  . PRO A 1 113 ? 25.81400 -29.66000 58.12300 1.000 33.63000 ? 113 PRO A CG  1 
ATOM   914  C  CD  . PRO A 1 113 ? 25.06300 -28.35900 58.03600 1.000 30.35000 ? 113 PRO A CD  1 
ATOM   915  N  N   . VAL A 1 114 ? 27.37000 -27.30600 61.41500 1.000 36.85000 ? 114 VAL A N   1 
ATOM   916  C  CA  . VAL A 1 114 ? 28.71600 -26.85200 61.75600 1.000 37.74000 ? 114 VAL A CA  1 
ATOM   917  C  C   . VAL A 1 114 ? 29.45200 -27.91600 62.55700 1.000 50.03000 ? 114 VAL A C   1 
ATOM   918  O  O   . VAL A 1 114 ? 30.66400 -28.11400 62.37500 1.000 43.35000 ? 114 VAL A O   1 
ATOM   919  C  CB  . VAL A 1 114 ? 28.66600 -25.50300 62.50400 1.000 37.01000 ? 114 VAL A CB  1 
ATOM   920  C  CG1 . VAL A 1 114 ? 28.33700 -24.39700 61.53000 1.000 37.37000 ? 114 VAL A CG1 1 
ATOM   921  C  CG2 . VAL A 1 114 ? 27.63700 -25.53200 63.65900 1.000 41.46000 ? 114 VAL A CG2 1 
ATOM   922  N  N   . GLU A 1 115 ? 28.73400 -28.64700 63.41500 1.000 47.86000 ? 115 GLU A N   1 
ATOM   923  C  CA  . GLU A 1 115 ? 29.30000 -29.73300 64.20900 1.000 40.10000 ? 115 GLU A CA  1 
ATOM   924  C  C   . GLU A 1 115 ? 28.44700 -30.98700 64.08300 1.000 44.68000 ? 115 GLU A C   1 
ATOM   925  O  O   . GLU A 1 115 ? 28.08300 -31.63200 65.07100 1.000 47.49000 ? 115 GLU A O   1 
ATOM   926  C  CB  . GLU A 1 115 ? 29.45300 -29.30500 65.66400 1.000 45.70000 ? 115 GLU A CB  1 
ATOM   927  C  CG  . GLU A 1 115 ? 30.38700 -28.10700 65.82700 1.000 49.95000 ? 115 GLU A CG  1 
ATOM   928  C  CD  . GLU A 1 115 ? 30.56200 -27.67800 67.27600 1.000 60.82000 ? 115 GLU A CD  1 
ATOM   929  O  OE1 . GLU A 1 115 ? 30.41100 -28.53100 68.18600 1.000 61.54000 ? 115 GLU A OE1 1 
ATOM   930  O  OE2 . GLU A 1 115 ? 30.85500 -26.48000 67.50300 1.000 58.03000 ? 115 GLU A OE2 1 
ATOM   931  N  N   . GLY A 1 116 ? 28.12900 -31.35900 62.84300 1.000 39.96000 ? 116 GLY A N   1 
ATOM   932  C  CA  . GLY A 1 116 ? 27.41200 -32.58800 62.57500 1.000 42.45000 ? 116 GLY A CA  1 
ATOM   933  C  C   . GLY A 1 116 ? 25.94800 -32.59700 62.95300 1.000 41.19000 ? 116 GLY A C   1 
ATOM   934  O  O   . GLY A 1 116 ? 25.31300 -33.65700 62.85900 1.000 45.25000 ? 116 GLY A O   1 
ATOM   935  N  N   . LYS A 1 117 ? 25.38500 -31.46600 63.37200 1.000 31.91000 ? 117 LYS A N   1 
ATOM   936  C  CA  . LYS A 1 117 ? 23.98200 -31.37700 63.74600 1.000 32.05000 ? 117 LYS A CA  1 
ATOM   937  C  C   . LYS A 1 117 ? 23.26400 -30.33800 62.89400 1.000 34.68000 ? 117 LYS A C   1 
ATOM   938  O  O   . LYS A 1 117 ? 23.69700 -29.18400 62.81400 1.000 36.38000 ? 117 LYS A O   1 
ATOM   939  C  CB  . LYS A 1 117 ? 23.83400 -31.01800 65.21700 1.000 36.12000 ? 117 LYS A CB  1 
ATOM   940  C  CG  . LYS A 1 117 ? 22.49800 -31.42600 65.77600 1.000 38.96000 ? 117 LYS A CG  1 
ATOM   941  C  CD  . LYS A 1 117 ? 22.08000 -30.46500 66.85700 1.000 53.34000 ? 117 LYS A CD  1 
ATOM   942  C  CE  . LYS A 1 117 ? 21.12300 -31.14000 67.83200 1.000 59.78000 ? 117 LYS A CE  1 
ATOM   943  N  NZ  . LYS A 1 117 ? 21.79800 -32.05700 68.81700 1.000 59.13000 ? 117 LYS A NZ  1 
ATOM   944  N  N   . ILE A 1 118 ? 22.16100 -30.74200 62.27500 1.000 28.55000 ? 118 ILE A N   1 
ATOM   945  C  CA  . ILE A 1 118 ? 21.34200 -29.85800 61.45400 1.000 29.47000 ? 118 ILE A CA  1 
ATOM   946  C  C   . ILE A 1 118 ? 20.09600 -29.49600 62.24400 1.000 30.25000 ? 118 ILE A C   1 
ATOM   947  O  O   . ILE A 1 118 ? 19.43800 -30.37800 62.80400 1.000 37.10000 ? 118 ILE A O   1 
ATOM   948  C  CB  . ILE A 1 118 ? 20.96400 -30.53500 60.13100 1.000 32.89000 ? 118 ILE A CB  1 
ATOM   949  C  CG1 . ILE A 1 118 ? 22.19200 -30.64700 59.22600 1.000 32.83000 ? 118 ILE A CG1 1 
ATOM   950  C  CG2 . ILE A 1 118 ? 19.79500 -29.80200 59.43100 1.000 25.42000 ? 118 ILE A CG2 1 
ATOM   951  C  CD1 . ILE A 1 118 ? 21.95900 -31.54300 58.04300 1.000 27.59000 ? 118 ILE A CD1 1 
ATOM   952  N  N   . ILE A 1 119 ? 19.76700 -28.21100 62.30700 1.000 27.96000 ? 119 ILE A N   1 
ATOM   953  C  CA  . ILE A 1 119 ? 18.48800 -27.79200 62.87500 1.000 27.20000 ? 119 ILE A CA  1 
ATOM   954  C  C   . ILE A 1 119 ? 17.46400 -27.66500 61.75500 1.000 28.37000 ? 119 ILE A C   1 
ATOM   955  O  O   . ILE A 1 119 ? 17.73200 -27.05800 60.71100 1.000 29.79000 ? 119 ILE A O   1 
ATOM   956  C  CB  . ILE A 1 119 ? 18.60600 -26.47400 63.65900 1.000 28.11000 ? 119 ILE A CB  1 
ATOM   957  C  CG1 . ILE A 1 119 ? 19.82700 -26.49400 64.56700 1.000 29.04000 ? 119 ILE A CG1 1 
ATOM   958  C  CG2 . ILE A 1 119 ? 17.34800 -26.25500 64.48400 1.000 23.95000 ? 119 ILE A CG2 1 
ATOM   959  C  CD1 . ILE A 1 119 ? 19.64700 -27.32900 65.79600 1.000 39.53000 ? 119 ILE A CD1 1 
ATOM   960  N  N   . LEU A 1 120 ? 16.29800 -28.25900 61.96800 1.000 26.38000 ? 120 LEU A N   1 
ATOM   961  C  CA  . LEU A 1 120 ? 15.19600 -28.27600 61.02600 1.000 25.53000 ? 120 LEU A CA  1 
ATOM   962  C  C   . LEU A 1 120 ? 14.02200 -27.48400 61.58800 1.000 27.69000 ? 120 LEU A C   1 
ATOM   963  O  O   . LEU A 1 120 ? 13.89500 -27.30100 62.79800 1.000 28.81000 ? 120 LEU A O   1 
ATOM   964  C  CB  . LEU A 1 120 ? 14.75600 -29.71400 60.74900 1.000 21.87000 ? 120 LEU A CB  1 
ATOM   965  C  CG  . LEU A 1 120 ? 15.75300 -30.62600 60.04300 1.000 29.03000 ? 120 LEU A CG  1 
ATOM   966  C  CD1 . LEU A 1 120 ? 15.11000 -31.99600 59.87400 1.000 25.36000 ? 120 LEU A CD1 1 
ATOM   967  C  CD2 . LEU A 1 120 ? 16.20000 -30.05300 58.67500 1.000 25.53000 ? 120 LEU A CD2 1 
ATOM   968  N  N   . SER A 1 121 ? 13.16900 -27.00000 60.69100 1.000 29.64000 ? 121 SER A N   1 
ATOM   969  C  CA  . SER A 1 121 ? 11.80700 -26.59400 61.01600 1.000 29.82000 ? 121 SER A CA  1 
ATOM   970  C  C   . SER A 1 121 ? 10.91000 -27.14500 59.91700 1.000 30.87000 ? 121 SER A C   1 
ATOM   971  O  O   . SER A 1 121 ? 11.38800 -27.75600 58.95300 1.000 26.47000 ? 121 SER A O   1 
ATOM   972  C  CB  . SER A 1 121 ? 11.66700 -25.07300 61.13000 1.000 32.11000 ? 121 SER A CB  1 
ATOM   973  O  OG  . SER A 1 121 ? 11.69000 -24.50800 59.83300 1.000 41.17000 ? 121 SER A OG  1 
ATOM   974  N  N   . SER A 1 122 ? 9.60200  -26.93700 60.04100 1.000 27.79000 ? 122 SER A N   1 
ATOM   975  C  CA  . SER A 1 122 ? 8.72600  -27.54200 59.05000 1.000 31.03000 ? 122 SER A CA  1 
ATOM   976  C  C   . SER A 1 122 ? 9.00200  -26.90800 57.68100 1.000 26.80000 ? 122 SER A C   1 
ATOM   977  O  O   . SER A 1 122 ? 9.46100  -25.76500 57.59900 1.000 25.13000 ? 122 SER A O   1 
ATOM   978  C  CB  . SER A 1 122 ? 7.25700  -27.39800 59.45200 1.000 28.95000 ? 122 SER A CB  1 
ATOM   979  O  OG  . SER A 1 122 ? 6.92000  -26.04300 59.58100 1.000 42.57000 ? 122 SER A OG  1 
ATOM   980  N  N   . PRO A 1 123 ? 8.81000  -27.66300 56.60200 1.000 26.63000 ? 123 PRO A N   1 
ATOM   981  C  CA  . PRO A 1 123 ? 9.15800  -27.16200 55.26500 1.000 24.31000 ? 123 PRO A CA  1 
ATOM   982  C  C   . PRO A 1 123 ? 8.51300  -25.81600 54.94500 1.000 27.88000 ? 123 PRO A C   1 
ATOM   983  O  O   . PRO A 1 123 ? 7.39200  -25.51100 55.36300 1.000 26.96000 ? 123 PRO A O   1 
ATOM   984  C  CB  . PRO A 1 123 ? 8.63400  -28.25900 54.34000 1.000 27.08000 ? 123 PRO A CB  1 
ATOM   985  C  CG  . PRO A 1 123 ? 8.66900  -29.52000 55.19100 1.000 29.27000 ? 123 PRO A CG  1 
ATOM   986  C  CD  . PRO A 1 123 ? 8.38900  -29.07700 56.59200 1.000 25.47000 ? 123 PRO A CD  1 
ATOM   987  N  N   . ARG A 1 124 ? 9.25500  -24.99400 54.21700 1.000 27.75000 ? 124 ARG A N   1 
ATOM   988  C  CA  . ARG A 1 124 ? 8.74900  -23.74700 53.67100 1.000 29.72000 ? 124 ARG A CA  1 
ATOM   989  C  C   . ARG A 1 124 ? 9.33800  -23.57000 52.28200 1.000 30.37000 ? 124 ARG A C   1 
ATOM   990  O  O   . ARG A 1 124 ? 10.45900 -24.01500 52.01800 1.000 24.58000 ? 124 ARG A O   1 
ATOM   991  C  CB  . ARG A 1 124 ? 9.13200  -22.53800 54.52400 1.000 27.54000 ? 124 ARG A CB  1 
ATOM   992  C  CG  . ARG A 1 124 ? 8.89500  -22.68900 56.02400 1.000 34.06000 ? 124 ARG A CG  1 
ATOM   993  C  CD  . ARG A 1 124 ? 9.23000  -21.36200 56.68600 1.000 31.12000 ? 124 ARG A CD  1 
ATOM   994  N  NE  . ARG A 1 124 ? 8.90200  -21.30500 58.10100 1.000 37.10000 ? 124 ARG A NE  1 
ATOM   995  C  CZ  . ARG A 1 124 ? 9.26600  -20.30900 58.90100 1.000 39.04000 ? 124 ARG A CZ  1 
ATOM   996  N  NH1 . ARG A 1 124 ? 9.97000  -19.28600 58.41800 1.000 35.23000 ? 124 ARG A NH1 1 
ATOM   997  N  NH2 . ARG A 1 124 ? 8.92000  -20.33000 60.18100 1.000 45.64000 ? 124 ARG A NH2 1 
ATOM   998  N  N   . ALA A 1 125 ? 8.57100  -22.92800 51.39800 1.000 28.20000 ? 125 ALA A N   1 
ATOM   999  C  CA  . ALA A 1 125 ? 9.07800  -22.51400 50.09400 1.000 28.27000 ? 125 ALA A CA  1 
ATOM   1000 C  C   . ALA A 1 125 ? 9.85100  -21.21400 50.28200 1.000 24.63000 ? 125 ALA A C   1 
ATOM   1001 O  O   . ALA A 1 125 ? 9.30100  -20.23700 50.79300 1.000 27.01000 ? 125 ALA A O   1 
ATOM   1002 C  CB  . ALA A 1 125 ? 7.93000  -22.33800 49.09600 1.000 28.41000 ? 125 ALA A CB  1 
ATOM   1003 N  N   . VAL A 1 126 ? 11.13200 -21.19900 49.93000 1.000 21.38000 ? 126 VAL A N   1 
ATOM   1004 C  CA  . VAL A 1 126 ? 11.98500 -20.06100 50.25000 1.000 24.68000 ? 126 VAL A CA  1 
ATOM   1005 C  C   . VAL A 1 126 ? 12.50000 -19.43800 48.96700 1.000 24.67000 ? 126 VAL A C   1 
ATOM   1006 O  O   . VAL A 1 126 ? 13.04900 -20.13900 48.10800 1.000 23.35000 ? 126 VAL A O   1 
ATOM   1007 C  CB  . VAL A 1 126 ? 13.16600 -20.46000 51.16100 1.000 28.98000 ? 126 VAL A CB  1 
ATOM   1008 C  CG1 . VAL A 1 126 ? 14.01600 -19.21800 51.45600 1.000 27.04000 ? 126 VAL A CG1 1 
ATOM   1009 C  CG2 . VAL A 1 126 ? 12.65000 -21.10700 52.46400 1.000 25.91000 ? 126 VAL A CG2 1 
ATOM   1010 N  N   . GLY A 1 127 ? 12.34900 -18.11600 48.85700 1.000 26.23000 ? 127 GLY A N   1 
ATOM   1011 C  CA  . GLY A 1 127 ? 13.01600 -17.32500 47.84400 1.000 25.03000 ? 127 GLY A CA  1 
ATOM   1012 C  C   . GLY A 1 127 ? 13.90400 -16.28100 48.49800 1.000 23.20000 ? 127 GLY A C   1 
ATOM   1013 O  O   . GLY A 1 127 ? 14.05900 -16.24500 49.72100 1.000 22.31000 ? 127 GLY A O   1 
ATOM   1014 N  N   . LYS A 1 128 ? 14.47200 -15.41600 47.66300 1.000 23.22000 ? 128 LYS A N   1 
ATOM   1015 C  CA  . LYS A 1 128 ? 15.35600 -14.37000 48.17700 1.000 24.94000 ? 128 LYS A CA  1 
ATOM   1016 C  C   . LYS A 1 128 ? 14.61500 -13.38500 49.08200 1.000 22.29000 ? 128 LYS A C   1 
ATOM   1017 O  O   . LYS A 1 128 ? 15.21900 -12.76500 49.96800 1.000 23.27000 ? 128 LYS A O   1 
ATOM   1018 C  CB  . LYS A 1 128 ? 16.02300 -13.61900 47.02000 1.000 31.30000 ? 128 LYS A CB  1 
ATOM   1019 C  CG  . LYS A 1 128 ? 17.22000 -12.80600 47.46900 1.000 36.04000 ? 128 LYS A CG  1 
ATOM   1020 C  CD  . LYS A 1 128 ? 17.53900 -11.65100 46.51400 1.000 41.48000 ? 128 LYS A CD  1 
ATOM   1021 C  CE  . LYS A 1 128 ? 18.47900 -12.06800 45.39100 1.000 42.07000 ? 128 LYS A CE  1 
ATOM   1022 N  NZ  . LYS A 1 128 ? 19.69700 -12.70700 45.93200 1.000 53.78000 ? 128 LYS A NZ  1 
ATOM   1023 N  N   . PHE A 1 129 ? 13.30900 -13.22600 48.88000 1.000 25.90000 ? 129 PHE A N   1 
ATOM   1024 C  CA  . PHE A 1 129 ? 12.55300 -12.18200 49.55100 1.000 24.75000 ? 129 PHE A CA  1 
ATOM   1025 C  C   . PHE A 1 129 ? 11.59500 -12.69000 50.62400 1.000 25.44000 ? 129 PHE A C   1 
ATOM   1026 O  O   . PHE A 1 129 ? 11.18300 -11.90100 51.48100 1.000 24.76000 ? 129 PHE A O   1 
ATOM   1027 C  CB  . PHE A 1 129 ? 11.77000 -11.36800 48.51000 1.000 24.73000 ? 129 PHE A CB  1 
ATOM   1028 C  CG  . PHE A 1 129 ? 12.63300 -10.82300 47.39900 1.000 27.76000 ? 129 PHE A CG  1 
ATOM   1029 C  CD1 . PHE A 1 129 ? 13.80200 -10.12000 47.68800 1.000 23.86000 ? 129 PHE A CD1 1 
ATOM   1030 C  CD2 . PHE A 1 129 ? 12.28100 -11.01400 46.05800 1.000 27.20000 ? 129 PHE A CD2 1 
ATOM   1031 C  CE1 . PHE A 1 129 ? 14.61500 -9.61500  46.65600 1.000 29.81000 ? 129 PHE A CE1 1 
ATOM   1032 C  CE2 . PHE A 1 129 ? 13.08500 -10.49900 45.03600 1.000 30.39000 ? 129 PHE A CE2 1 
ATOM   1033 C  CZ  . PHE A 1 129 ? 14.25800 -9.80300  45.34500 1.000 28.65000 ? 129 PHE A CZ  1 
ATOM   1034 N  N   . ALA A 1 130 ? 11.24400 -13.97700 50.61500 1.000 25.27000 ? 130 ALA A N   1 
ATOM   1035 C  CA  . ALA A 1 130 ? 10.15800 -14.44000 51.46700 1.000 25.06000 ? 130 ALA A CA  1 
ATOM   1036 C  C   . ALA A 1 130 ? 10.24200 -15.94600 51.63900 1.000 28.90000 ? 130 ALA A C   1 
ATOM   1037 O  O   . ALA A 1 130 ? 10.92100 -16.65300 50.88000 1.000 25.17000 ? 130 ALA A O   1 
ATOM   1038 C  CB  . ALA A 1 130 ? 8.78700  -14.04500 50.89000 1.000 26.35000 ? 130 ALA A CB  1 
ATOM   1039 N  N   . MET A 1 131 ? 9.54600  -16.41900 52.66700 1.000 26.46000 ? 131 MET A N   1 
ATOM   1040 C  CA  . MET A 1 131 ? 9.29200  -17.83100 52.90800 1.000 28.18000 ? 131 MET A CA  1 
ATOM   1041 C  C   . MET A 1 131 ? 7.79300  -17.97900 53.10400 1.000 29.61000 ? 131 MET A C   1 
ATOM   1042 O  O   . MET A 1 131 ? 7.16000  -17.13600 53.74400 1.000 28.50000 ? 131 MET A O   1 
ATOM   1043 C  CB  . MET A 1 131 ? 10.06500 -18.35000 54.15500 1.000 26.57000 ? 131 MET A CB  1 
ATOM   1044 C  CG  . MET A 1 131 ? 11.49100 -17.85700 54.20400 1.000 32.59000 ? 131 MET A CG  1 
ATOM   1045 S  SD  . MET A 1 131 ? 12.53100 -18.27200 55.64300 1.000 40.21000 ? 131 MET A SD  1 
ATOM   1046 C  CE  . MET A 1 131 ? 12.14200 -19.97000 55.86500 1.000 40.56000 ? 131 MET A CE  1 
ATOM   1047 N  N   . VAL A 1 132 ? 7.21300  -19.02200 52.53100 1.000 28.14000 ? 132 VAL A N   1 
ATOM   1048 C  CA  . VAL A 1 132 ? 5.77800  -19.21400 52.66100 1.000 31.77000 ? 132 VAL A CA  1 
ATOM   1049 C  C   . VAL A 1 132 ? 5.51100  -20.65200 53.07200 1.000 32.50000 ? 132 VAL A C   1 
ATOM   1050 O  O   . VAL A 1 132 ? 6.26000  -21.57500 52.72500 1.000 26.92000 ? 132 VAL A O   1 
ATOM   1051 C  CB  . VAL A 1 132 ? 5.00000  -18.86600 51.36900 1.000 27.31000 ? 132 VAL A CB  1 
ATOM   1052 C  CG1 . VAL A 1 132 ? 5.38600  -17.47000 50.84400 1.000 23.80000 ? 132 VAL A CG1 1 
ATOM   1053 C  CG2 . VAL A 1 132 ? 5.20200  -19.94200 50.32200 1.000 25.98000 ? 132 VAL A CG2 1 
ATOM   1054 N  N   . TRP A 1 133 ? 4.43300  -20.83600 53.82300 1.000 30.28000 ? 133 TRP A N   1 
ATOM   1055 C  CA  . TRP A 1 133 ? 3.98800  -22.17500 54.17300 1.000 34.13000 ? 133 TRP A CA  1 
ATOM   1056 C  C   . TRP A 1 133 ? 2.53100  -22.08800 54.62500 1.000 36.12000 ? 133 TRP A C   1 
ATOM   1057 O  O   . TRP A 1 133 ? 1.96400  -21.00300 54.74500 1.000 38.83000 ? 133 TRP A O   1 
ATOM   1058 C  CB  . TRP A 1 133 ? 4.91400  -22.79700 55.22500 1.000 32.60000 ? 133 TRP A CB  1 
ATOM   1059 C  CG  . TRP A 1 133 ? 4.89400  -22.15900 56.58900 1.000 35.27000 ? 133 TRP A CG  1 
ATOM   1060 C  CD1 . TRP A 1 133 ? 4.36600  -22.69300 57.73100 1.000 36.33000 ? 133 TRP A CD1 1 
ATOM   1061 C  CD2 . TRP A 1 133 ? 5.45600  -20.88700 56.96400 1.000 33.36000 ? 133 TRP A CD2 1 
ATOM   1062 N  NE1 . TRP A 1 133 ? 4.55300  -21.83400 58.78500 1.000 38.50000 ? 133 TRP A NE1 1 
ATOM   1063 C  CE2 . TRP A 1 133 ? 5.21000  -20.71400 58.34100 1.000 34.91000 ? 133 TRP A CE2 1 
ATOM   1064 C  CE3 . TRP A 1 133 ? 6.13000  -19.87900 56.26800 1.000 32.00000 ? 133 TRP A CE3 1 
ATOM   1065 C  CZ2 . TRP A 1 133 ? 5.62000  -19.57900 59.03700 1.000 34.53000 ? 133 TRP A CZ2 1 
ATOM   1066 C  CZ3 . TRP A 1 133 ? 6.52900  -18.74500 56.95600 1.000 31.14000 ? 133 TRP A CZ3 1 
ATOM   1067 C  CH2 . TRP A 1 133 ? 6.26900  -18.60400 58.32600 1.000 34.15000 ? 133 TRP A CH2 1 
ATOM   1068 N  N   . LYS A 1 134 ? 1.92200  -23.24600 54.85700 1.000 38.41000 ? 134 LYS A N   1 
ATOM   1069 C  CA  . LYS A 1 134 ? 0.53200  -23.31000 55.29400 1.000 38.81000 ? 134 LYS A CA  1 
ATOM   1070 C  C   . LYS A 1 134 ? 0.39800  -23.00000 56.77600 1.000 38.86000 ? 134 LYS A C   1 
ATOM   1071 O  O   . LYS A 1 134 ? 1.14400  -23.53500 57.60100 1.000 44.72000 ? 134 LYS A O   1 
ATOM   1072 C  CB  . LYS A 1 134 ? -0.03700 -24.70800 55.04100 1.000 47.12000 ? 134 LYS A CB  1 
ATOM   1073 C  CG  . LYS A 1 134 ? -0.58900 -24.90900 53.65600 1.000 47.11000 ? 134 LYS A CG  1 
ATOM   1074 C  CD  . LYS A 1 134 ? -1.05000 -23.60300 53.02200 1.000 46.06000 ? 134 LYS A CD  1 
ATOM   1075 C  CE  . LYS A 1 134 ? -2.19600 -23.86900 52.03500 1.000 60.42000 ? 134 LYS A CE  1 
ATOM   1076 N  NZ  . LYS A 1 134 ? -1.90800 -25.00100 51.08500 1.000 59.75000 ? 134 LYS A NZ  1 
ATOM   1077 N  N   . GLY A 1 135 ? -0.58200 -22.16600 57.11900 1.000 48.98000 ? 135 GLY A N   1 
ATOM   1078 C  CA  . GLY A 1 135 ? -0.89700 -21.87100 58.50700 1.000 44.42000 ? 135 GLY A CA  1 
ATOM   1079 C  C   . GLY A 1 135 ? -2.16100 -21.05200 58.66700 1.000 46.63000 ? 135 GLY A C   1 
ATOM   1080 O  O   . GLY A 1 135 ? -3.02800 -21.08000 57.79400 1.000 48.59000 ? 135 GLY A O   1 
ATOM   1081 N  N   . ASP A 1 136 ? -2.19800 -20.29800 59.75600 1.000 43.92000 ? 136 ASP A N   1 
ATOM   1082 C  CA  . ASP A 1 136 ? -3.33600 -19.42800 60.10700 1.000 48.45000 ? 136 ASP A CA  1 
ATOM   1083 C  C   . ASP A 1 136 ? -3.46600 -18.35100 59.03500 1.000 44.91000 ? 136 ASP A C   1 
ATOM   1084 O  O   . ASP A 1 136 ? -4.54300 -18.00600 58.67600 1.000 52.48000 ? 136 ASP A O   1 
ATOM   1085 C  CB  . ASP A 1 136 ? -3.06500 -18.77700 61.45200 1.000 51.85000 ? 136 ASP A CB  1 
ATOM   1086 C  CG  . ASP A 1 136 ? -2.79300 -19.75000 62.58100 1.000 58.80000 ? 136 ASP A CG  1 
ATOM   1087 O  OD1 . ASP A 1 136 ? -3.25400 -20.87700 62.49800 1.000 59.39000 ? 136 ASP A OD1 1 
ATOM   1088 O  OD2 . ASP A 1 136 ? -2.15700 -19.34100 63.54800 1.000 60.54000 ? 136 ASP A OD2 1 
ATOM   1089 N  N   . GLY A 1 137 ? -2.35300 -17.86700 58.54500 1.000 43.61000 ? 137 GLY A N   1 
ATOM   1090 C  CA  . GLY A 1 137 ? -2.37900 -16.81800 57.52800 1.000 40.59000 ? 137 GLY A CA  1 
ATOM   1091 C  C   . GLY A 1 137 ? -1.86100 -15.54700 58.13200 1.000 48.03000 ? 137 GLY A C   1 
ATOM   1092 O  O   . GLY A 1 137 ? -2.57300 -14.58400 58.11100 1.000 51.12000 ? 137 GLY A O   1 
ATOM   1093 N  N   . ARG A 1 138 ? -0.65100 -15.60000 58.66500 1.000 43.46000 ? 138 ARG A N   1 
ATOM   1094 C  CA  . ARG A 1 138 ? -0.00300 -14.44500 59.30700 1.000 44.14000 ? 138 ARG A CA  1 
ATOM   1095 C  C   . ARG A 1 138 ? 1.23000  -14.01500 58.51900 1.000 45.48000 ? 138 ARG A C   1 
ATOM   1096 O  O   . ARG A 1 138 ? 1.82600  -14.82500 57.83100 1.000 38.23000 ? 138 ARG A O   1 
ATOM   1097 C  CB  . ARG A 1 138 ? 0.48200  -14.87300 60.68700 1.000 48.56000 ? 138 ARG A CB  1 
ATOM   1098 C  CG  . ARG A 1 138 ? -0.58000 -14.79700 61.77100 1.000 52.67000 ? 138 ARG A CG  1 
ATOM   1099 C  CD  . ARG A 1 138 ? 0.04200  -15.05100 63.11800 1.000 53.66000 ? 138 ARG A CD  1 
ATOM   1100 N  NE  . ARG A 1 138 ? 0.10900  -16.48100 63.28500 1.000 71.08000 ? 138 ARG A NE  1 
ATOM   1101 C  CZ  . ARG A 1 138 ? 0.70300  -17.10900 64.29000 1.000 68.83000 ? 138 ARG A CZ  1 
ATOM   1102 N  NH1 . ARG A 1 138 ? 1.32700  -16.42200 65.23500 1.000 58.12000 ? 138 ARG A NH1 1 
ATOM   1103 N  NH2 . ARG A 1 138 ? 0.68200  -18.42600 64.31900 1.000 59.53000 ? 138 ARG A NH2 1 
ATOM   1104 N  N   . THR A 1 139 ? 1.58400  -12.75600 58.67700 1.000 41.36000 ? 139 THR A N   1 
ATOM   1105 C  CA  . THR A 1 139 ? 2.77700  -12.18100 58.03200 1.000 42.56000 ? 139 THR A CA  1 
ATOM   1106 C  C   . THR A 1 139 ? 3.82300  -11.89100 59.11000 1.000 43.03000 ? 139 THR A C   1 
ATOM   1107 O  O   . THR A 1 139 ? 3.50500  -11.21700 60.05300 1.000 42.50000 ? 139 THR A O   1 
ATOM   1108 C  CB  . THR A 1 139 ? 2.43000  -10.89500 57.29900 1.000 36.86000 ? 139 THR A CB  1 
ATOM   1109 O  OG1 . THR A 1 139 ? 1.59400  -11.20800 56.19800 1.000 43.55000 ? 139 THR A OG1 1 
ATOM   1110 C  CG2 . THR A 1 139 ? 3.66500  -10.16300 56.83900 1.000 43.11000 ? 139 THR A CG2 1 
ATOM   1111 N  N   . PHE A 1 140 ? 5.01000  -12.45200 58.96200 1.000 40.66000 ? 140 PHE A N   1 
ATOM   1112 C  CA  . PHE A 1 140 ? 6.13100  -12.22400 59.86300 1.000 34.68000 ? 140 PHE A CA  1 
ATOM   1113 C  C   . PHE A 1 140 ? 7.21300  -11.41200 59.16700 1.000 39.63000 ? 140 PHE A C   1 
ATOM   1114 O  O   . PHE A 1 140 ? 7.34200  -11.44600 57.94200 1.000 36.41000 ? 140 PHE A O   1 
ATOM   1115 C  CB  . PHE A 1 140 ? 6.70200  -13.54800 60.35200 1.000 35.03000 ? 140 PHE A CB  1 
ATOM   1116 C  CG  . PHE A 1 140 ? 5.67900  -14.41800 61.00700 1.000 45.69000 ? 140 PHE A CG  1 
ATOM   1117 C  CD1 . PHE A 1 140 ? 5.37700  -14.26000 62.35400 1.000 42.65000 ? 140 PHE A CD1 1 
ATOM   1118 C  CD2 . PHE A 1 140 ? 4.98200  -15.36500 60.27100 1.000 41.09000 ? 140 PHE A CD2 1 
ATOM   1119 C  CE1 . PHE A 1 140 ? 4.42000  -15.04700 62.96000 1.000 44.64000 ? 140 PHE A CE1 1 
ATOM   1120 C  CE2 . PHE A 1 140 ? 4.02400  -16.15800 60.87100 1.000 47.51000 ? 140 PHE A CE2 1 
ATOM   1121 C  CZ  . PHE A 1 140 ? 3.74300  -15.99600 62.22000 1.000 50.73000 ? 140 PHE A CZ  1 
ATOM   1122 N  N   . PHE A 1 141 ? 7.99000  -10.67000 59.96100 1.000 38.44000 ? 141 PHE A N   1 
ATOM   1123 C  CA  . PHE A 1 141 ? 9.03700  -9.79800  59.44400 1.000 36.20000 ? 141 PHE A CA  1 
ATOM   1124 C  C   . PHE A 1 141 ? 10.38400 -10.16200 60.05300 1.000 41.07000 ? 141 PHE A C   1 
ATOM   1125 O  O   . PHE A 1 141 ? 10.47100 -10.48900 61.24000 1.000 39.03000 ? 141 PHE A O   1 
ATOM   1126 C  CB  . PHE A 1 141 ? 8.72900  -8.32300  59.73400 1.000 38.85000 ? 141 PHE A CB  1 
ATOM   1127 C  CG  . PHE A 1 141 ? 7.45900  -7.83100  59.09900 1.000 46.04000 ? 141 PHE A CG  1 
ATOM   1128 C  CD1 . PHE A 1 141 ? 6.24200  -7.96500  59.75700 1.000 39.55000 ? 141 PHE A CD1 1 
ATOM   1129 C  CD2 . PHE A 1 141 ? 7.47900  -7.24100  57.83500 1.000 42.97000 ? 141 PHE A CD2 1 
ATOM   1130 C  CE1 . PHE A 1 141 ? 5.07500  -7.51000  59.17900 1.000 43.78000 ? 141 PHE A CE1 1 
ATOM   1131 C  CE2 . PHE A 1 141 ? 6.30800  -6.79000  57.24200 1.000 41.98000 ? 141 PHE A CE2 1 
ATOM   1132 C  CZ  . PHE A 1 141 ? 5.10500  -6.92200  57.92000 1.000 43.67000 ? 141 PHE A CZ  1 
ATOM   1133 N  N   . SER A 1 142 ? 11.42600 -10.12800 59.22100 1.000 41.06000 ? 142 SER A N   1 
ATOM   1134 C  CA  . SER A 1 142 ? 12.79900 -10.12300 59.71500 1.000 35.14000 ? 142 SER A CA  1 
ATOM   1135 C  C   . SER A 1 142 ? 12.99800 -8.93100  60.63900 1.000 36.75000 ? 142 SER A C   1 
ATOM   1136 O  O   . SER A 1 142 ? 12.37000 -7.88000  60.45800 1.000 33.00000 ? 142 SER A O   1 
ATOM   1137 C  CB  . SER A 1 142 ? 13.77300 -10.05500 58.53100 1.000 40.63000 ? 142 SER A CB  1 
ATOM   1138 O  OG  . SER A 1 142 ? 15.09100 -9.65000  58.90000 1.000 43.60000 ? 142 SER A OG  1 
ATOM   1139 N  N   . GLU A 1 143 ? 13.86700 -9.10000  61.64600 1.000 48.24000 ? 143 GLU A N   1 
ATOM   1140 C  CA  . GLU A 1 143 ? 14.19500 -7.97600  62.53100 1.000 42.30000 ? 143 GLU A CA  1 
ATOM   1141 C  C   . GLU A 1 143 ? 14.78100 -6.78700  61.78800 1.000 43.12000 ? 143 GLU A C   1 
ATOM   1142 O  O   . GLU A 1 143 ? 14.61700 -5.65200  62.23700 1.000 42.39000 ? 143 GLU A O   1 
ATOM   1143 C  CB  . GLU A 1 143 ? 15.21300 -8.41700  63.60500 1.000 49.15000 ? 143 GLU A CB  1 
ATOM   1144 C  CG  . GLU A 1 143 ? 14.64500 -9.45700  64.58100 1.000 62.91000 ? 143 GLU A CG  1 
ATOM   1145 C  CD  . GLU A 1 143 ? 15.13300 -10.86000 64.27100 1.000 87.21000 ? 143 GLU A CD  1 
ATOM   1146 O  OE1 . GLU A 1 143 ? 15.39000 -11.13100 63.07700 1.000 78.09000 ? 143 GLU A OE1 1 
ATOM   1147 O  OE2 . GLU A 1 143 ? 15.32300 -11.65700 65.22000 1.000 95.67000 ? 143 GLU A OE2 1 
ATOM   1148 N  N   . HIS A 1 144 ? 15.43300 -7.04100  60.65700 1.000 38.81000 ? 144 HIS A N   1 
ATOM   1149 C  CA  . HIS A 1 144 ? 16.20100 -6.02200  59.96700 1.000 38.59000 ? 144 HIS A CA  1 
ATOM   1150 C  C   . HIS A 1 144 ? 15.40200 -5.27600  58.92000 1.000 35.17000 ? 144 HIS A C   1 
ATOM   1151 O  O   . HIS A 1 144 ? 15.99300 -4.64000  58.04200 1.000 46.35000 ? 144 HIS A O   1 
ATOM   1152 C  CB  . HIS A 1 144 ? 17.44700 -6.64300  59.34300 1.000 34.99000 ? 144 HIS A CB  1 
ATOM   1153 C  CG  . HIS A 1 144 ? 18.36400 -7.24000  60.35700 1.000 44.19000 ? 144 HIS A CG  1 
ATOM   1154 N  ND1 . HIS A 1 144 ? 18.40700 -8.59400  60.60600 1.000 52.52000 ? 144 HIS A ND1 1 
ATOM   1155 C  CD2 . HIS A 1 144 ? 19.21100 -6.66600  61.24500 1.000 44.46000 ? 144 HIS A CD2 1 
ATOM   1156 C  CE1 . HIS A 1 144 ? 19.26700 -8.83400  61.57900 1.000 51.16000 ? 144 HIS A CE1 1 
ATOM   1157 N  NE2 . HIS A 1 144 ? 19.76700 -7.68000  61.98600 1.000 48.97000 ? 144 HIS A NE2 1 
ATOM   1158 N  N   . ILE A 1 145 ? 14.08200 -5.28700  59.02100 1.000 32.86000 ? 145 ILE A N   1 
ATOM   1159 C  CA  . ILE A 1 145 ? 13.22500 -4.49300  58.14900 1.000 37.30000 ? 145 ILE A CA  1 
ATOM   1160 C  C   . ILE A 1 145 ? 12.80700 -3.25000  58.92000 1.000 33.74000 ? 145 ILE A C   1 
ATOM   1161 O  O   . ILE A 1 145 ? 12.21700 -3.35700  59.99800 1.000 37.46000 ? 145 ILE A O   1 
ATOM   1162 C  CB  . ILE A 1 145 ? 12.01500 -5.31200  57.68400 1.000 35.06000 ? 145 ILE A CB  1 
ATOM   1163 C  CG1 . ILE A 1 145 ? 12.51100 -6.53400  56.89800 1.000 39.37000 ? 145 ILE A CG1 1 
ATOM   1164 C  CG2 . ILE A 1 145 ? 11.06500 -4.46400  56.85600 1.000 33.28000 ? 145 ILE A CG2 1 
ATOM   1165 C  CD1 . ILE A 1 145 ? 11.42500 -7.46500  56.39500 1.000 34.66000 ? 145 ILE A CD1 1 
ATOM   1166 N  N   . ASP A 1 146 ? 13.15100 -2.06900  58.40700 1.000 36.58000 ? 146 ASP A N   1 
ATOM   1167 C  CA  . ASP A 1 146 ? 12.67600 -0.83600  59.03000 1.000 40.69000 ? 146 ASP A CA  1 
ATOM   1168 C  C   . ASP A 1 146 ? 11.15800 -0.75600  58.95200 1.000 41.88000 ? 146 ASP A C   1 
ATOM   1169 O  O   . ASP A 1 146 ? 10.53300 -1.33300  58.05500 1.000 38.03000 ? 146 ASP A O   1 
ATOM   1170 C  CB  . ASP A 1 146 ? 13.28200 0.38700   58.34400 1.000 43.69000 ? 146 ASP A CB  1 
ATOM   1171 C  CG  . ASP A 1 146 ? 14.77500 0.50600   58.56200 1.000 55.48000 ? 146 ASP A CG  1 
ATOM   1172 O  OD1 . ASP A 1 146 ? 15.31500 -0.18300  59.46200 1.000 55.20000 ? 146 ASP A OD1 1 
ATOM   1173 O  OD2 . ASP A 1 146 ? 15.41100 1.29000   57.82000 1.000 59.14000 ? 146 ASP A OD2 1 
ATOM   1174 N  N   . GLU A 1 147 ? 10.55800 -0.02600  59.90300 1.000 46.41000 ? 147 GLU A N   1 
ATOM   1175 C  CA  . GLU A 1 147 ? 9.10100  0.13200   59.89900 1.000 45.00000 ? 147 GLU A CA  1 
ATOM   1176 C  C   . GLU A 1 147 ? 8.62500  0.78900   58.61900 1.000 42.41000 ? 147 GLU A C   1 
ATOM   1177 O  O   . GLU A 1 147 ? 7.55400  0.44800   58.11100 1.000 44.72000 ? 147 GLU A O   1 
ATOM   1178 C  CB  . GLU A 1 147 ? 8.62600  0.95300   61.10300 1.000 45.92000 ? 147 GLU A CB  1 
ATOM   1179 C  CG  . GLU A 1 147 ? 7.08200  1.00300   61.24300 1.000 46.42000 ? 147 GLU A CG  1 
ATOM   1180 C  CD  . GLU A 1 147 ? 6.38800  2.14400   60.45500 1.000 54.49000 ? 147 GLU A CD  1 
ATOM   1181 O  OE1 . GLU A 1 147 ? 7.04500  3.13400   60.05400 1.000 46.07000 ? 147 GLU A OE1 1 
ATOM   1182 O  OE2 . GLU A 1 147 ? 5.16100  2.04600   60.23600 1.000 74.31000 ? 147 GLU A OE2 1 
ATOM   1183 N  N   . ARG A 1 148 ? 9.40800  1.74300   58.08900 1.000 39.54000 ? 148 ARG A N   1 
ATOM   1184 C  CA  . ARG A 1 148 ? 9.00400  2.47300   56.89300 1.000 43.33000 ? 148 ARG A CA  1 
ATOM   1185 C  C   . ARG A 1 148 ? 8.77200  1.52500   55.72400 1.000 46.18000 ? 148 ARG A C   1 
ATOM   1186 O  O   . ARG A 1 148 ? 8.03900  1.85800   54.78800 1.000 51.45000 ? 148 ARG A O   1 
ATOM   1187 C  CB  . ARG A 1 148 ? 10.04000 3.52800   56.49800 1.000 41.12000 ? 148 ARG A CB  1 
ATOM   1188 C  CG  . ARG A 1 148 ? 11.37200 2.97900   56.00000 1.000 54.24000 ? 148 ARG A CG  1 
ATOM   1189 C  CD  . ARG A 1 148 ? 12.43400 4.10300   55.91500 1.000 55.43000 ? 148 ARG A CD  1 
ATOM   1190 N  NE  . ARG A 1 148 ? 12.78500 4.52700   57.26800 1.000 57.62000 ? 148 ARG A NE  1 
ATOM   1191 C  CZ  . ARG A 1 148 ? 14.02700 4.72900   57.69100 1.000 48.91000 ? 148 ARG A CZ  1 
ATOM   1192 N  NH1 . ARG A 1 148 ? 15.03900 4.54700   56.87300 1.000 58.14000 ? 148 ARG A NH1 1 
ATOM   1193 N  NH2 . ARG A 1 148 ? 14.26600 5.09000   58.94200 1.000 63.41000 ? 148 ARG A NH2 1 
ATOM   1194 N  N   . ASP A 1 149 ? 9.38000  0.33600   55.75400 1.000 48.81000 ? 149 ASP A N   1 
ATOM   1195 C  CA  . ASP A 1 149 ? 9.27800  -0.63500  54.67000 1.000 48.50000 ? 149 ASP A CA  1 
ATOM   1196 C  C   . ASP A 1 149 ? 8.28300  -1.75100  54.95400 1.000 44.96000 ? 149 ASP A C   1 
ATOM   1197 O  O   . ASP A 1 149 ? 7.95800  -2.50600  54.03900 1.000 41.65000 ? 149 ASP A O   1 
ATOM   1198 C  CB  . ASP A 1 149 ? 10.66000 -1.24300  54.39100 1.000 41.37000 ? 149 ASP A CB  1 
ATOM   1199 C  CG  . ASP A 1 149 ? 11.65300 -0.21700  53.85100 1.000 48.24000 ? 149 ASP A CG  1 
ATOM   1200 O  OD1 . ASP A 1 149 ? 11.27100 0.59300   52.97300 1.000 49.88000 ? 149 ASP A OD1 1 
ATOM   1201 O  OD2 . ASP A 1 149 ? 12.83700 -0.26200  54.26100 1.000 43.43000 ? 149 ASP A OD2 1 
ATOM   1202 N  N   . SER A 1 150 ? 7.79700  -1.87900  56.19200 1.000 46.23000 ? 150 SER A N   1 
ATOM   1203 C  CA  . SER A 1 150 ? 6.94000  -3.01000  56.54200 1.000 43.54000 ? 150 SER A CA  1 
ATOM   1204 C  C   . SER A 1 150 ? 5.57800  -2.93500  55.85000 1.000 47.46000 ? 150 SER A C   1 
ATOM   1205 O  O   . SER A 1 150 ? 5.06000  -3.96000  55.39000 1.000 45.75000 ? 150 SER A O   1 
ATOM   1206 C  CB  . SER A 1 150 ? 6.75000  -3.06900  58.04800 1.000 38.84000 ? 150 SER A CB  1 
ATOM   1207 O  OG  . SER A 1 150 ? 6.14800  -1.86600  58.49100 1.000 51.92000 ? 150 SER A OG  1 
ATOM   1208 N  N   . GLN A 1 151 ? 4.96200  -1.74600  55.79900 1.000 45.58000 ? 151 GLN A N   1 
ATOM   1209 C  CA  . GLN A 1 151 ? 3.58800  -1.64300  55.30300 1.000 47.73000 ? 151 GLN A CA  1 
ATOM   1210 C  C   . GLN A 1 151 ? 3.48100  -2.05500  53.83500 1.000 42.85000 ? 151 GLN A C   1 
ATOM   1211 O  O   . GLN A 1 151 ? 2.49000  -2.67500  53.42200 1.000 46.06000 ? 151 GLN A O   1 
ATOM   1212 C  CB  . GLN A 1 151 ? 3.05600  -0.22000  55.48300 1.000 49.31000 ? 151 GLN A CB  1 
ATOM   1213 C  CG  . GLN A 1 151 ? 1.67500  -0.01100  54.85700 1.000 58.11000 ? 151 GLN A CG  1 
ATOM   1214 C  CD  . GLN A 1 151 ? 0.67100  -1.04100  55.35700 1.000 62.67000 ? 151 GLN A CD  1 
ATOM   1215 O  OE1 . GLN A 1 151 ? 0.42800  -1.14300  56.56500 1.000 62.68000 ? 151 GLN A OE1 1 
ATOM   1216 N  NE2 . GLN A 1 151 ? 0.10400  -1.82700  54.43800 1.000 51.59000 ? 151 GLN A NE2 1 
ATOM   1217 N  N   . ARG A 1 152 ? 4.46400  -1.67900  53.02000 1.000 39.70000 ? 152 ARG A N   1 
ATOM   1218 C  CA  . ARG A 1 152 ? 4.45500  -2.13300  51.63700 1.000 39.53000 ? 152 ARG A CA  1 
ATOM   1219 C  C   . ARG A 1 152 ? 4.43500  -3.65300  51.57900 1.000 37.79000 ? 152 ARG A C   1 
ATOM   1220 O  O   . ARG A 1 152 ? 3.64000  -4.25100  50.84500 1.000 36.43000 ? 152 ARG A O   1 
ATOM   1221 C  CB  . ARG A 1 152 ? 5.66500  -1.57900  50.89200 1.000 41.72000 ? 152 ARG A CB  1 
ATOM   1222 C  CG  . ARG A 1 152 ? 5.53100  -1.71600  49.41000 1.000 35.29000 ? 152 ARG A CG  1 
ATOM   1223 C  CD  . ARG A 1 152 ? 6.68800  -1.08100  48.70600 1.000 36.39000 ? 152 ARG A CD  1 
ATOM   1224 N  NE  . ARG A 1 152 ? 7.98300  -1.65400  49.07000 1.000 44.42000 ? 152 ARG A NE  1 
ATOM   1225 C  CZ  . ARG A 1 152 ? 8.68900  -2.45000  48.27700 1.000 36.77000 ? 152 ARG A CZ  1 
ATOM   1226 N  NH1 . ARG A 1 152 ? 8.20700  -2.77700  47.08900 1.000 38.40000 ? 152 ARG A NH1 1 
ATOM   1227 N  NH2 . ARG A 1 152 ? 9.88000  -2.90300  48.66100 1.000 36.24000 ? 152 ARG A NH2 1 
ATOM   1228 N  N   . LEU A 1 153 ? 5.28400  -4.29200  52.38500 1.000 34.05000 ? 153 LEU A N   1 
ATOM   1229 C  CA  . LEU A 1 153 ? 5.34900  -5.74600  52.39200 1.000 42.08000 ? 153 LEU A CA  1 
ATOM   1230 C  C   . LEU A 1 153 ? 4.02700  -6.34700  52.83200 1.000 35.12000 ? 153 LEU A C   1 
ATOM   1231 O  O   . LEU A 1 153 ? 3.55300  -7.32200  52.24100 1.000 35.94000 ? 153 LEU A O   1 
ATOM   1232 C  CB  . LEU A 1 153 ? 6.48200  -6.22600  53.30800 1.000 32.03000 ? 153 LEU A CB  1 
ATOM   1233 C  CG  . LEU A 1 153 ? 7.87700  -5.68800  52.98500 1.000 39.16000 ? 153 LEU A CG  1 
ATOM   1234 C  CD1 . LEU A 1 153 ? 8.94400  -6.51200  53.70200 1.000 33.61000 ? 153 LEU A CD1 1 
ATOM   1235 C  CD2 . LEU A 1 153 ? 8.10800  -5.68900  51.48800 1.000 30.59000 ? 153 LEU A CD2 1 
ATOM   1236 N  N   . LEU A 1 154 ? 3.41400  -5.77100  53.86200 1.000 32.48000 ? 154 LEU A N   1 
ATOM   1237 C  CA  . LEU A 1 154 ? 2.15500  -6.30800  54.36500 1.000 37.45000 ? 154 LEU A CA  1 
ATOM   1238 C  C   . LEU A 1 154 ? 1.07700  -6.25600  53.29600 1.000 37.89000 ? 154 LEU A C   1 
ATOM   1239 O  O   . LEU A 1 154 ? 0.34000  -7.23100  53.09500 1.000 39.68000 ? 154 LEU A O   1 
ATOM   1240 C  CB  . LEU A 1 154 ? 1.72500  -5.54200  55.61000 1.000 44.06000 ? 154 LEU A CB  1 
ATOM   1241 C  CG  . LEU A 1 154 ? 0.55300  -6.18000  56.35100 1.000 43.05000 ? 154 LEU A CG  1 
ATOM   1242 C  CD1 . LEU A 1 154 ? 0.92300  -7.57900  56.82700 1.000 42.07000 ? 154 LEU A CD1 1 
ATOM   1243 C  CD2 . LEU A 1 154 ? 0.11900  -5.28000  57.50900 1.000 43.56000 ? 154 LEU A CD2 1 
ATOM   1244 N  N   . SER A 1 155 ? 0.99500  -5.13700  52.57900 1.000 41.05000 ? 155 SER A N   1 
ATOM   1245 C  CA  . SER A 1 155 ? 0.04500  -5.01300  51.48200 1.000 40.75000 ? 155 SER A CA  1 
ATOM   1246 C  C   . SER A 1 155 ? 0.21700  -6.12000  50.45000 1.000 36.97000 ? 155 SER A C   1 
ATOM   1247 O  O   . SER A 1 155 ? -0.75500 -6.52700  49.80800 1.000 38.04000 ? 155 SER A O   1 
ATOM   1248 C  CB  . SER A 1 155 ? 0.19800  -3.63400  50.82500 1.000 40.06000 ? 155 SER A CB  1 
ATOM   1249 O  OG  . SER A 1 155 ? 1.03300  -3.68300  49.66700 1.000 46.45000 ? 155 SER A OG  1 
ATOM   1250 N  N   . VAL A 1 156 ? 1.43600  -6.62700  50.27900 1.000 38.36000 ? 156 VAL A N   1 
ATOM   1251 C  CA  . VAL A 1 156 ? 1.63100  -7.69100  49.30300 1.000 36.96000 ? 156 VAL A CA  1 
ATOM   1252 C  C   . VAL A 1 156 ? 1.24300  -9.04200  49.88800 1.000 29.76000 ? 156 VAL A C   1 
ATOM   1253 O  O   . VAL A 1 156 ? 0.61500  -9.86100  49.20900 1.000 33.44000 ? 156 VAL A O   1 
ATOM   1254 C  CB  . VAL A 1 156 ? 3.08000  -7.68300  48.77800 1.000 37.42000 ? 156 VAL A CB  1 
ATOM   1255 C  CG1 . VAL A 1 156 ? 3.34600  -8.91600  47.90900 1.000 32.88000 ? 156 VAL A CG1 1 
ATOM   1256 C  CG2 . VAL A 1 156 ? 3.33700  -6.40300  47.98700 1.000 37.05000 ? 156 VAL A CG2 1 
ATOM   1257 N  N   . SER A 1 157 ? 1.58000  -9.29700  51.14800 1.000 30.90000 ? 157 SER A N   1 
ATOM   1258 C  CA  . SER A 1 157 ? 1.33500  -10.62400 51.70300 1.000 34.83000 ? 157 SER A CA  1 
ATOM   1259 C  C   . SER A 1 157 ? -0.07200 -10.81300 52.26600 1.000 36.34000 ? 157 SER A C   1 
ATOM   1260 O  O   . SER A 1 157 ? -0.48900 -11.96500 52.44700 1.000 39.78000 ? 157 SER A O   1 
ATOM   1261 C  CB  . SER A 1 157 ? 2.36800  -10.95900 52.79300 1.000 30.47000 ? 157 SER A CB  1 
ATOM   1262 O  OG  . SER A 1 157 ? 2.45400  -9.93100  53.76200 1.000 36.61000 ? 157 SER A OG  1 
ATOM   1263 N  N   . ILE A 1 158 ? -0.80300 -9.72500  52.56100 1.000 38.15000 ? 158 ILE A N   1 
ATOM   1264 C  CA  . ILE A 1 158 ? -2.18000 -9.86100  53.05700 1.000 41.40000 ? 158 ILE A CA  1 
ATOM   1265 C  C   . ILE A 1 158 ? -3.03000 -10.77200 52.17500 1.000 38.64000 ? 158 ILE A C   1 
ATOM   1266 O  O   . ILE A 1 158 ? -3.60300 -11.73800 52.70100 1.000 45.20000 ? 158 ILE A O   1 
ATOM   1267 C  CB  . ILE A 1 158 ? -2.81900 -8.47300  53.25000 1.000 42.89000 ? 158 ILE A CB  1 
ATOM   1268 C  CG1 . ILE A 1 158 ? -2.52300 -7.92400  54.64600 1.000 43.53000 ? 158 ILE A CG1 1 
ATOM   1269 C  CG2 . ILE A 1 158 ? -4.33100 -8.57100  53.04100 1.000 43.75000 ? 158 ILE A CG2 1 
ATOM   1270 C  CD1 . ILE A 1 158 ? -2.63000 -6.40900  54.74600 1.000 42.90000 ? 158 ILE A CD1 1 
ATOM   1271 N  N   . PRO A 1 159 ? -3.14400 -10.54800 50.85300 1.000 36.12000 ? 159 PRO A N   1 
ATOM   1272 C  CA  . PRO A 1 159 ? -3.94100 -11.47000 50.01700 1.000 39.46000 ? 159 PRO A CA  1 
ATOM   1273 C  C   . PRO A 1 159 ? -3.63000 -12.93700 50.26100 1.000 42.90000 ? 159 PRO A C   1 
ATOM   1274 O  O   . PRO A 1 159 ? -4.54900 -13.76400 50.36500 1.000 44.28000 ? 159 PRO A O   1 
ATOM   1275 C  CB  . PRO A 1 159 ? -3.56400 -11.07100 48.58500 1.000 35.43000 ? 159 PRO A CB  1 
ATOM   1276 C  CG  . PRO A 1 159 ? -3.06500 -9.69300  48.67700 1.000 45.96000 ? 159 PRO A CG  1 
ATOM   1277 C  CD  . PRO A 1 159 ? -2.44300 -9.54000  50.03400 1.000 37.95000 ? 159 PRO A CD  1 
ATOM   1278 N  N   . PHE A 1 160 ? -2.34600 -13.27600 50.38200 1.000 35.13000 ? 160 PHE A N   1 
ATOM   1279 C  CA  . PHE A 1 160 ? -1.94500 -14.66700 50.54700 1.000 39.61000 ? 160 PHE A CA  1 
ATOM   1280 C  C   . PHE A 1 160 ? -2.22800 -15.19100 51.95200 1.000 38.06000 ? 160 PHE A C   1 
ATOM   1281 O  O   . PHE A 1 160 ? -2.50500 -16.38700 52.12500 1.000 38.40000 ? 160 PHE A O   1 
ATOM   1282 C  CB  . PHE A 1 160 ? -0.46800 -14.80600 50.18500 1.000 36.18000 ? 160 PHE A CB  1 
ATOM   1283 C  CG  . PHE A 1 160 ? -0.17900 -14.50100 48.74600 1.000 33.96000 ? 160 PHE A CG  1 
ATOM   1284 C  CD1 . PHE A 1 160 ? 0.10200  -13.20200 48.33700 1.000 31.11000 ? 160 PHE A CD1 1 
ATOM   1285 C  CD2 . PHE A 1 160 ? -0.20000 -15.51500 47.79400 1.000 32.98000 ? 160 PHE A CD2 1 
ATOM   1286 C  CE1 . PHE A 1 160 ? 0.37000  -12.92200 47.00400 1.000 37.83000 ? 160 PHE A CE1 1 
ATOM   1287 C  CE2 . PHE A 1 160 ? 0.06200  -15.24200 46.45900 1.000 31.55000 ? 160 PHE A CE2 1 
ATOM   1288 C  CZ  . PHE A 1 160 ? 0.34900  -13.93900 46.06000 1.000 32.21000 ? 160 PHE A CZ  1 
ATOM   1289 N  N   . ASN A 1 161 ? -2.16300 -14.32100 52.96100 1.000 40.07000 ? 161 ASN A N   1 
ATOM   1290 C  CA  . ASN A 1 161 ? -2.65800 -14.69600 54.28000 1.000 43.14000 ? 161 ASN A CA  1 
ATOM   1291 C  C   . ASN A 1 161 ? -4.12500 -15.10800 54.21600 1.000 43.48000 ? 161 ASN A C   1 
ATOM   1292 O  O   . ASN A 1 161 ? -4.52600 -16.09000 54.85000 1.000 43.29000 ? 161 ASN A O   1 
ATOM   1293 C  CB  . ASN A 1 161 ? -2.46800 -13.53900 55.26700 1.000 47.68000 ? 161 ASN A CB  1 
ATOM   1294 C  CG  . ASN A 1 161 ? -1.00400 -13.17400 55.48000 1.000 48.86000 ? 161 ASN A CG  1 
ATOM   1295 O  OD1 . ASN A 1 161 ? -0.10000 -14.01800 55.34800 1.000 44.52000 ? 161 ASN A OD1 1 
ATOM   1296 N  ND2 . ASN A 1 161 ? -0.76100 -11.91300 55.81600 1.000 38.53000 ? 161 ASN A ND2 1 
ATOM   1297 N  N   . LYS A 1 162 ? -4.94000 -14.36600 53.45700 1.000 44.50000 ? 162 LYS A N   1 
ATOM   1298 C  CA  . LYS A 1 162 ? -6.35300 -14.71700 53.32500 1.000 47.65000 ? 162 LYS A CA  1 
ATOM   1299 C  C   . LYS A 1 162 ? -6.52800 -16.13300 52.80400 1.000 47.12000 ? 162 LYS A C   1 
ATOM   1300 O  O   . LYS A 1 162 ? -7.48600 -16.81500 53.18000 1.000 46.63000 ? 162 LYS A O   1 
ATOM   1301 C  CB  . LYS A 1 162 ? -7.06300 -13.74800 52.38400 1.000 49.43000 ? 162 LYS A CB  1 
ATOM   1302 C  CG  . LYS A 1 162 ? -6.88500 -12.29000 52.71400 1.000 47.84000 ? 162 LYS A CG  1 
ATOM   1303 C  CD  . LYS A 1 162 ? -7.75500 -11.87600 53.87600 1.000 57.36000 ? 162 LYS A CD  1 
ATOM   1304 C  CE  . LYS A 1 162 ? -7.56100 -10.39100 54.19100 1.000 58.35000 ? 162 LYS A CE  1 
ATOM   1305 N  NZ  . LYS A 1 162 ? -8.09600 -9.49600  53.10500 1.000 55.17000 ? 162 LYS A NZ  1 
ATOM   1306 N  N   . LYS A 1 163 ? -5.61200 -16.58400 51.94100 1.000 43.21000 ? 163 LYS A N   1 
ATOM   1307 C  CA  . LYS A 1 163 ? -5.63300 -17.91700 51.35600 1.000 38.96000 ? 163 LYS A CA  1 
ATOM   1308 C  C   . LYS A 1 163 ? -5.04900 -18.97900 52.27700 1.000 43.12000 ? 163 LYS A C   1 
ATOM   1309 O  O   . LYS A 1 163 ? -4.99100 -20.15000 51.88400 1.000 43.40000 ? 163 LYS A O   1 
ATOM   1310 C  CB  . LYS A 1 163 ? -4.87400 -17.91300 50.02700 1.000 42.39000 ? 163 LYS A CB  1 
ATOM   1311 C  CG  . LYS A 1 163 ? -5.52000 -17.07900 48.91100 1.000 46.59000 ? 163 LYS A CG  1 
ATOM   1312 C  CD  . LYS A 1 163 ? -4.86200 -17.36700 47.56300 1.000 48.06000 ? 163 LYS A CD  1 
ATOM   1313 C  CE  . LYS A 1 163 ? -4.29500 -16.10600 46.91100 1.000 53.49000 ? 163 LYS A CE  1 
ATOM   1314 N  NZ  . LYS A 1 163 ? -3.27100 -16.43300 45.86700 1.000 46.70000 ? 163 LYS A NZ  1 
ATOM   1315 N  N   . GLY A 1 164 ? -4.62800 -18.61300 53.48500 1.000 38.25000 ? 164 GLY A N   1 
ATOM   1316 C  CA  . GLY A 1 164 ? -4.07600 -19.57700 54.41200 1.000 44.73000 ? 164 GLY A CA  1 
ATOM   1317 C  C   . GLY A 1 164 ? -2.57900 -19.77200 54.32900 1.000 48.00000 ? 164 GLY A C   1 
ATOM   1318 O  O   . GLY A 1 164 ? -2.06500 -20.75500 54.88400 1.000 44.33000 ? 164 GLY A O   1 
ATOM   1319 N  N   . TYR A 1 165 ? -1.86000 -18.86800 53.66400 1.000 39.83000 ? 165 TYR A N   1 
ATOM   1320 C  CA  . TYR A 1 165 ? -0.40600 -18.91800 53.59700 1.000 36.77000 ? 165 TYR A CA  1 
ATOM   1321 C  C   . TYR A 1 165 ? 0.20700  -17.99400 54.64400 1.000 34.76000 ? 165 TYR A C   1 
ATOM   1322 O  O   . TYR A 1 165 ? -0.11300 -16.80000 54.70000 1.000 36.61000 ? 165 TYR A O   1 
ATOM   1323 C  CB  . TYR A 1 165 ? 0.08800  -18.53100 52.20800 1.000 35.23000 ? 165 TYR A CB  1 
ATOM   1324 C  CG  . TYR A 1 165 ? -0.14500 -19.59200 51.16300 1.000 40.06000 ? 165 TYR A CG  1 
ATOM   1325 C  CD1 . TYR A 1 165 ? 0.71300  -20.68400 51.05500 1.000 37.43000 ? 165 TYR A CD1 1 
ATOM   1326 C  CD2 . TYR A 1 165 ? -1.21500 -19.49800 50.26600 1.000 43.81000 ? 165 TYR A CD2 1 
ATOM   1327 C  CE1 . TYR A 1 165 ? 0.51000  -21.66700 50.08400 1.000 40.77000 ? 165 TYR A CE1 1 
ATOM   1328 C  CE2 . TYR A 1 165 ? -1.42700 -20.48000 49.29400 1.000 36.36000 ? 165 TYR A CE2 1 
ATOM   1329 C  CZ  . TYR A 1 165 ? -0.56000 -21.55800 49.21600 1.000 39.07000 ? 165 TYR A CZ  1 
ATOM   1330 O  OH  . TYR A 1 165 ? -0.74700 -22.52500 48.25600 1.000 49.68000 ? 165 TYR A OH  1 
ATOM   1331 N  N   . ASN A 1 166 ? 1.08200  -18.54500 55.46700 1.000 32.79000 ? 166 ASN A N   1 
ATOM   1332 C  CA  . ASN A 1 166 ? 1.97600  -17.71200 56.25100 1.000 34.33000 ? 166 ASN A CA  1 
ATOM   1333 C  C   . ASN A 1 166 ? 3.07200  -17.16700 55.35000 1.000 33.15000 ? 166 ASN A C   1 
ATOM   1334 O  O   . ASN A 1 166 ? 3.59300  -17.87600 54.48100 1.000 33.64000 ? 166 ASN A O   1 
ATOM   1335 C  CB  . ASN A 1 166 ? 2.58900  -18.51500 57.39300 1.000 39.16000 ? 166 ASN A CB  1 
ATOM   1336 C  CG  . ASN A 1 166 ? 1.58600  -18.84600 58.48100 1.000 39.52000 ? 166 ASN A CG  1 
ATOM   1337 O  OD1 . ASN A 1 166 ? 0.59900  -18.13500 58.68000 1.000 38.17000 ? 166 ASN A OD1 1 
ATOM   1338 N  ND2 . ASN A 1 166 ? 1.84500  -19.92800 59.19600 1.000 45.08000 ? 166 ASN A ND2 1 
ATOM   1339 N  N   . VAL A 1 167 ? 3.42700  -15.90500 55.55800 1.000 37.03000 ? 167 VAL A N   1 
ATOM   1340 C  CA  . VAL A 1 167 ? 4.49200  -15.26600 54.79100 1.000 31.90000 ? 167 VAL A CA  1 
ATOM   1341 C  C   . VAL A 1 167 ? 5.51500  -14.69500 55.76600 1.000 34.84000 ? 167 VAL A C   1 
ATOM   1342 O  O   . VAL A 1 167 ? 5.17700  -13.86100 56.61600 1.000 36.10000 ? 167 VAL A O   1 
ATOM   1343 C  CB  . VAL A 1 167 ? 3.94300  -14.16900 53.86800 1.000 34.46000 ? 167 VAL A CB  1 
ATOM   1344 C  CG1 . VAL A 1 167 ? 5.08200  -13.42400 53.20400 1.000 33.67000 ? 167 VAL A CG1 1 
ATOM   1345 C  CG2 . VAL A 1 167 ? 2.99700  -14.77100 52.81800 1.000 29.87000 ? 167 VAL A CG2 1 
ATOM   1346 N  N   . LYS A 1 168 ? 6.75300  -15.15900 55.66600 1.000 28.44000 ? 168 LYS A N   1 
ATOM   1347 C  CA  . LYS A 1 168 ? 7.86900  -14.52900 56.36100 1.000 29.85000 ? 168 LYS A CA  1 
ATOM   1348 C  C   . LYS A 1 168 ? 8.62000  -13.63600 55.36700 1.000 31.42000 ? 168 LYS A C   1 
ATOM   1349 O  O   . LYS A 1 168 ? 9.21900  -14.13300 54.41000 1.000 30.64000 ? 168 LYS A O   1 
ATOM   1350 C  CB  . LYS A 1 168 ? 8.77500  -15.59800 56.96300 1.000 28.05000 ? 168 LYS A CB  1 
ATOM   1351 C  CG  . LYS A 1 168 ? 10.09800 -15.07000 57.47600 1.000 40.26000 ? 168 LYS A CG  1 
ATOM   1352 C  CD  . LYS A 1 168 ? 9.89400  -14.18700 58.70200 1.000 46.19000 ? 168 LYS A CD  1 
ATOM   1353 C  CE  . LYS A 1 168 ? 11.22000 -13.68500 59.25900 1.000 42.51000 ? 168 LYS A CE  1 
ATOM   1354 N  NZ  . LYS A 1 168 ? 11.84800 -14.68500 60.15400 1.000 47.78000 ? 168 LYS A NZ  1 
ATOM   1355 N  N   . TRP A 1 169 ? 8.60200  -12.32700 55.58500 1.000 27.96000 ? 169 TRP A N   1 
ATOM   1356 C  CA  . TRP A 1 169 ? 9.39200  -11.44000 54.73900 1.000 26.92000 ? 169 TRP A CA  1 
ATOM   1357 C  C   . TRP A 1 169 ? 10.84200 -11.42500 55.19800 1.000 29.73000 ? 169 TRP A C   1 
ATOM   1358 O  O   . TRP A 1 169 ? 11.12100 -11.25800 56.38600 1.000 31.45000 ? 169 TRP A O   1 
ATOM   1359 C  CB  . TRP A 1 169 ? 8.83100  -10.02500 54.75200 1.000 33.81000 ? 169 TRP A CB  1 
ATOM   1360 C  CG  . TRP A 1 169 ? 7.51000  -9.89300  54.06900 1.000 39.82000 ? 169 TRP A CG  1 
ATOM   1361 C  CD1 . TRP A 1 169 ? 6.30400  -9.63500  54.66000 1.000 37.21000 ? 169 TRP A CD1 1 
ATOM   1362 C  CD2 . TRP A 1 169 ? 7.25300  -10.00700 52.66100 1.000 35.02000 ? 169 TRP A CD2 1 
ATOM   1363 N  NE1 . TRP A 1 169 ? 5.31400  -9.58800  53.70700 1.000 34.76000 ? 169 TRP A NE1 1 
ATOM   1364 C  CE2 . TRP A 1 169 ? 5.87100  -9.80200  52.47200 1.000 34.67000 ? 169 TRP A CE2 1 
ATOM   1365 C  CE3 . TRP A 1 169 ? 8.05800  -10.26100 51.54400 1.000 29.31000 ? 169 TRP A CE3 1 
ATOM   1366 C  CZ2 . TRP A 1 169 ? 5.27400  -9.84500  51.20800 1.000 34.07000 ? 169 TRP A CZ2 1 
ATOM   1367 C  CZ3 . TRP A 1 169 ? 7.46700  -10.29800 50.29500 1.000 31.22000 ? 169 TRP A CZ3 1 
ATOM   1368 C  CH2 . TRP A 1 169 ? 6.08800  -10.09200 50.13500 1.000 32.44000 ? 169 TRP A CH2 1 
ATOM   1369 N  N   . ARG A 1 170 ? 11.75800 -11.61000 54.25500 1.000 27.88000 ? 170 ARG A N   1 
ATOM   1370 C  CA  . ARG A 1 170 ? 13.19100 -11.52500 54.50000 1.000 26.51000 ? 170 ARG A CA  1 
ATOM   1371 C  C   . ARG A 1 170 ? 13.66200 -10.09200 54.27600 1.000 24.68000 ? 170 ARG A C   1 
ATOM   1372 O  O   . ARG A 1 170 ? 13.00000 -9.30000  53.61000 1.000 25.48000 ? 170 ARG A O   1 
ATOM   1373 C  CB  . ARG A 1 170 ? 13.94000 -12.51700 53.60200 1.000 27.95000 ? 170 ARG A CB  1 
ATOM   1374 C  CG  . ARG A 1 170 ? 13.50700 -13.97100 53.83800 1.000 26.39000 ? 170 ARG A CG  1 
ATOM   1375 C  CD  . ARG A 1 170 ? 14.27600 -14.98600 52.97400 1.000 26.15000 ? 170 ARG A CD  1 
ATOM   1376 N  NE  . ARG A 1 170 ? 15.64400 -15.20200 53.43600 1.000 31.21000 ? 170 ARG A NE  1 
ATOM   1377 C  CZ  . ARG A 1 170 ? 16.60100 -15.77700 52.71400 1.000 28.37000 ? 170 ARG A CZ  1 
ATOM   1378 N  NH1 . ARG A 1 170 ? 16.35000 -16.20700 51.48800 1.000 26.28000 ? 170 ARG A NH1 1 
ATOM   1379 N  NH2 . ARG A 1 170 ? 17.80800 -15.92500 53.21800 1.000 31.22000 ? 170 ARG A NH2 1 
ATOM   1380 N  N   . SER A 1 171 ? 14.79600 -9.73300  54.88900 1.000 29.97000 ? 171 SER A N   1 
ATOM   1381 C  CA  . SER A 1 171 ? 15.16800 -8.31700  54.87800 1.000 28.36000 ? 171 SER A CA  1 
ATOM   1382 C  C   . SER A 1 171 ? 15.45500 -7.81900  53.46200 1.000 30.94000 ? 171 SER A C   1 
ATOM   1383 O  O   . SER A 1 171 ? 15.21300 -6.64200  53.15800 1.000 26.77000 ? 171 SER A O   1 
ATOM   1384 C  CB  . SER A 1 171 ? 16.36600 -8.05400  55.80300 1.000 26.37000 ? 171 SER A CB  1 
ATOM   1385 O  OG  . SER A 1 171 ? 17.54300 -8.66800  55.32400 1.000 33.00000 ? 171 SER A OG  1 
ATOM   1386 N  N   . ASN A 1 172 ? 15.93700 -8.69300  52.56700 1.000 27.47000 ? 172 ASN A N   1 
ATOM   1387 C  CA  . ASN A 1 172 ? 16.11500 -8.26000  51.18400 1.000 30.48000 ? 172 ASN A CA  1 
ATOM   1388 C  C   . ASN A 1 172 ? 14.81500 -7.77800  50.55600 1.000 25.25000 ? 172 ASN A C   1 
ATOM   1389 O  O   . ASN A 1 172 ? 14.86200 -6.96200  49.63900 1.000 27.91000 ? 172 ASN A O   1 
ATOM   1390 C  CB  . ASN A 1 172 ? 16.69500 -9.37900  50.32200 1.000 25.19000 ? 172 ASN A CB  1 
ATOM   1391 C  CG  . ASN A 1 172 ? 18.19800 -9.31400  50.21400 1.000 26.53000 ? 172 ASN A CG  1 
ATOM   1392 O  OD1 . ASN A 1 172 ? 18.79600 -8.23400  50.13300 1.000 27.07000 ? 172 ASN A OD1 1 
ATOM   1393 N  ND2 . ASN A 1 172 ? 18.82600 -10.47900 50.20500 1.000 27.99000 ? 172 ASN A ND2 1 
ATOM   1394 N  N   . ALA A 1 173 ? 13.65500 -8.25400  51.02800 1.000 29.83000 ? 173 ALA A N   1 
ATOM   1395 C  CA  . ALA A 1 173 ? 12.38300 -7.85200  50.41900 1.000 25.44000 ? 173 ALA A CA  1 
ATOM   1396 C  C   . ALA A 1 173 ? 12.18000 -6.34000  50.44700 1.000 29.19000 ? 173 ALA A C   1 
ATOM   1397 O  O   . ALA A 1 173 ? 11.46100 -5.79200  49.60200 1.000 32.04000 ? 173 ALA A O   1 
ATOM   1398 C  CB  . ALA A 1 173 ? 11.21500 -8.54600  51.12400 1.000 24.78000 ? 173 ALA A CB  1 
ATOM   1399 N  N   . ALA A 1 174 ? 12.78800 -5.64800  51.41100 1.000 30.42000 ? 174 ALA A N   1 
ATOM   1400 C  CA  . ALA A 1 174 ? 12.57300 -4.21800  51.54100 1.000 32.55000 ? 174 ALA A CA  1 
ATOM   1401 C  C   . ALA A 1 174 ? 13.15800 -3.45800  50.37000 1.000 29.26000 ? 174 ALA A C   1 
ATOM   1402 O  O   . ALA A 1 174 ? 12.69000 -2.35900  50.07900 1.000 33.63000 ? 174 ALA A O   1 
ATOM   1403 C  CB  . ALA A 1 174 ? 13.15900 -3.70900  52.87000 1.000 32.39000 ? 174 ALA A CB  1 
ATOM   1404 N  N   . MET A 1 175 ? 14.14300 -4.03100  49.67400 1.000 30.54000 ? 175 MET A N   1 
ATOM   1405 C  CA  . MET A 1 175 ? 14.80800 -3.39300  48.54000 1.000 32.35000 ? 175 MET A CA  1 
ATOM   1406 C  C   . MET A 1 175 ? 14.25400 -3.82900  47.18800 1.000 35.13000 ? 175 MET A C   1 
ATOM   1407 O  O   . MET A 1 175 ? 14.74400 -3.35900  46.15800 1.000 27.03000 ? 175 MET A O   1 
ATOM   1408 C  CB  . MET A 1 175 ? 16.31100 -3.69700  48.57200 1.000 30.70000 ? 175 MET A CB  1 
ATOM   1409 C  CG  . MET A 1 175 ? 16.88700 -3.55400  49.95300 1.000 35.30000 ? 175 MET A CG  1 
ATOM   1410 S  SD  . MET A 1 175 ? 16.90400 -1.82200  50.40300 1.000 39.63000 ? 175 MET A SD  1 
ATOM   1411 C  CE  . MET A 1 175 ? 17.27500 -1.94500  52.16100 1.000 41.88000 ? 175 MET A CE  1 
ATOM   1412 N  N   . ALA A 1 176 ? 13.26000 -4.71400  47.16200 1.000 32.90000 ? 176 ALA A N   1 
ATOM   1413 C  CA  . ALA A 1 176 ? 12.74000 -5.25000  45.91200 1.000 32.96000 ? 176 ALA A CA  1 
ATOM   1414 C  C   . ALA A 1 176 ? 11.57200 -4.40800  45.41400 1.000 33.63000 ? 176 ALA A C   1 
ATOM   1415 O  O   . ALA A 1 176 ? 10.78800 -3.87700  46.20600 1.000 32.97000 ? 176 ALA A O   1 
ATOM   1416 C  CB  . ALA A 1 176 ? 12.28200 -6.69700  46.10200 1.000 30.19000 ? 176 ALA A CB  1 
ATOM   1417 N  N   . THR A 1 177 ? 11.44500 -4.30900  44.09200 1.000 33.33000 ? 177 THR A N   1 
ATOM   1418 C  CA  . THR A 1 177 ? 10.26900 -3.65700  43.52700 1.000 35.38000 ? 177 THR A CA  1 
ATOM   1419 C  C   . THR A 1 177 ? 8.99800  -4.38000  43.97600 1.000 36.43000 ? 177 THR A C   1 
ATOM   1420 O  O   . THR A 1 177 ? 9.01000  -5.56500  44.32700 1.000 31.57000 ? 177 THR A O   1 
ATOM   1421 C  CB  . THR A 1 177 ? 10.34400 -3.61400  41.99300 1.000 41.64000 ? 177 THR A CB  1 
ATOM   1422 O  OG1 . THR A 1 177 ? 10.12800 -4.92600  41.45100 1.000 35.45000 ? 177 THR A OG1 1 
ATOM   1423 C  CG2 . THR A 1 177 ? 11.71100 -3.07300  41.51700 1.000 38.40000 ? 177 THR A CG2 1 
ATOM   1424 N  N   . THR A 1 178 ? 7.88500  -3.63900  43.97700 1.000 37.62000 ? 178 THR A N   1 
ATOM   1425 C  CA  . THR A 1 178 ? 6.61200  -4.22600  44.38600 1.000 33.16000 ? 178 THR A CA  1 
ATOM   1426 C  C   . THR A 1 178 ? 6.17000  -5.32500  43.43000 1.000 37.25000 ? 178 THR A C   1 
ATOM   1427 O  O   . THR A 1 178 ? 5.50700  -6.28300  43.84600 1.000 35.52000 ? 178 THR A O   1 
ATOM   1428 C  CB  . THR A 1 178 ? 5.54300  -3.14100  44.47600 1.000 40.80000 ? 178 THR A CB  1 
ATOM   1429 O  OG1 . THR A 1 178 ? 5.89800  -2.22100  45.51300 1.000 42.32000 ? 178 THR A OG1 1 
ATOM   1430 C  CG2 . THR A 1 178 ? 4.16900  -3.74900  44.79100 1.000 37.76000 ? 178 THR A CG2 1 
ATOM   1431 N  N   . ALA A 1 179 ? 6.52100  -5.20900  42.15000 1.000 36.16000 ? 179 ALA A N   1 
ATOM   1432 C  CA  . ALA A 1 179 ? 6.15400  -6.25600  41.20800 1.000 34.23000 ? 179 ALA A CA  1 
ATOM   1433 C  C   . ALA A 1 179 ? 6.97400  -7.51800  41.45100 1.000 35.51000 ? 179 ALA A C   1 
ATOM   1434 O  O   . ALA A 1 179 ? 6.44500  -8.63000  41.36100 1.000 36.09000 ? 179 ALA A O   1 
ATOM   1435 C  CB  . ALA A 1 179 ? 6.32400  -5.76000  39.77400 1.000 34.88000 ? 179 ALA A CB  1 
ATOM   1436 N  N   . GLU A 1 180 ? 8.27400  -7.35900  41.74100 1.000 33.89000 ? 180 GLU A N   1 
ATOM   1437 C  CA  . GLU A 1 180 ? 9.12400  -8.47800  42.14500 1.000 36.21000 ? 180 GLU A CA  1 
ATOM   1438 C  C   . GLU A 1 180 ? 8.52600  -9.22500  43.33700 1.000 35.64000 ? 180 GLU A C   1 
ATOM   1439 O  O   . GLU A 1 180 ? 8.45000  -10.45700 43.34400 1.000 35.38000 ? 180 GLU A O   1 
ATOM   1440 C  CB  . GLU A 1 180 ? 10.52100 -7.96900  42.50900 1.000 33.23000 ? 180 GLU A CB  1 
ATOM   1441 C  CG  . GLU A 1 180 ? 11.53900 -7.95600  41.39700 1.000 40.88000 ? 180 GLU A CG  1 
ATOM   1442 C  CD  . GLU A 1 180 ? 12.92000 -7.50300  41.88600 1.000 45.40000 ? 180 GLU A CD  1 
ATOM   1443 O  OE1 . GLU A 1 180 ? 13.02800 -6.37800  42.43500 1.000 36.54000 ? 180 GLU A OE1 1 
ATOM   1444 O  OE2 . GLU A 1 180 ? 13.89600 -8.28200  41.73300 1.000 55.28000 ? 180 GLU A OE2 1 
ATOM   1445 N  N   . LEU A 1 181 ? 8.10300  -8.48600  44.36200 1.000 30.67000 ? 181 LEU A N   1 
ATOM   1446 C  CA  . LEU A 1 181 ? 7.52500  -9.11600  45.54200 1.000 33.05000 ? 181 LEU A CA  1 
ATOM   1447 C  C   . LEU A 1 181 ? 6.27900  -9.91900  45.19000 1.000 35.97000 ? 181 LEU A C   1 
ATOM   1448 O  O   . LEU A 1 181 ? 6.09700  -11.04100 45.68500 1.000 31.70000 ? 181 LEU A O   1 
ATOM   1449 C  CB  . LEU A 1 181 ? 7.21100  -8.05300  46.59300 1.000 33.30000 ? 181 LEU A CB  1 
ATOM   1450 C  CG  . LEU A 1 181 ? 8.45300  -7.30600  47.08600 1.000 33.31000 ? 181 LEU A CG  1 
ATOM   1451 C  CD1 . LEU A 1 181 ? 8.03800  -6.17600  47.99900 1.000 37.42000 ? 181 LEU A CD1 1 
ATOM   1452 C  CD2 . LEU A 1 181 ? 9.41900  -8.26100  47.81500 1.000 34.31000 ? 181 LEU A CD2 1 
ATOM   1453 N  N   . LYS A 1 182 ? 5.40800  -9.36700  44.33500 1.000 36.48000 ? 182 LYS A N   1 
ATOM   1454 C  CA  . LYS A 1 182 ? 4.17100  -10.07400 44.00200 1.000 35.09000 ? 182 LYS A CA  1 
ATOM   1455 C  C   . LYS A 1 182 ? 4.48000  -11.34400 43.23200 1.000 29.12000 ? 182 LYS A C   1 
ATOM   1456 O  O   . LYS A 1 182 ? 3.97000  -12.42200 43.55200 1.000 34.51000 ? 182 LYS A O   1 
ATOM   1457 C  CB  . LYS A 1 182 ? 3.22400  -9.16400  43.22000 1.000 33.14000 ? 182 LYS A CB  1 
ATOM   1458 C  CG  . LYS A 1 182 ? 2.59000  -8.11200  44.12400 1.000 41.92000 ? 182 LYS A CG  1 
ATOM   1459 C  CD  . LYS A 1 182 ? 1.76500  -7.14100  43.33700 1.000 42.20000 ? 182 LYS A CD  1 
ATOM   1460 C  CE  . LYS A 1 182 ? 0.99300  -6.19300  44.21800 1.000 46.81000 ? 182 LYS A CE  1 
ATOM   1461 N  NZ  . LYS A 1 182 ? 0.93300  -4.85300  43.55700 1.000 56.00000 ? 182 LYS A NZ  1 
ATOM   1462 N  N   . GLU A 1 183 ? 5.35200  -11.23200 42.23900 1.000 31.61000 ? 183 GLU A N   1 
ATOM   1463 C  CA  . GLU A 1 183 ? 5.83600  -12.39800 41.51600 1.000 36.10000 ? 183 GLU A CA  1 
ATOM   1464 C  C   . GLU A 1 183 ? 6.45100  -13.42400 42.46500 1.000 36.17000 ? 183 GLU A C   1 
ATOM   1465 O  O   . GLU A 1 183 ? 6.24600  -14.63000 42.30100 1.000 33.15000 ? 183 GLU A O   1 
ATOM   1466 C  CB  . GLU A 1 183 ? 6.85200  -11.93300 40.48400 1.000 36.22000 ? 183 GLU A CB  1 
ATOM   1467 C  CG  . GLU A 1 183 ? 7.30300  -12.95100 39.49900 1.000 42.48000 ? 183 GLU A CG  1 
ATOM   1468 C  CD  . GLU A 1 183 ? 8.31700  -12.35500 38.55200 1.000 60.43000 ? 183 GLU A CD  1 
ATOM   1469 O  OE1 . GLU A 1 183 ? 9.30300  -11.76200 39.05100 1.000 61.89000 ? 183 GLU A OE1 1 
ATOM   1470 O  OE2 . GLU A 1 183 ? 8.10700  -12.44400 37.32000 1.000 59.97000 ? 183 GLU A OE2 1 
ATOM   1471 N  N   . GLU A 1 184 ? 7.20400  -12.95800 43.47000 1.000 36.60000 ? 184 GLU A N   1 
ATOM   1472 C  CA  . GLU A 1 184 ? 7.83300  -13.86600 44.42700 1.000 37.31000 ? 184 GLU A CA  1 
ATOM   1473 C  C   . GLU A 1 184 ? 6.79400  -14.69900 45.17200 1.000 32.89000 ? 184 GLU A C   1 
ATOM   1474 O  O   . GLU A 1 184 ? 6.91000  -15.92900 45.25600 1.000 29.74000 ? 184 GLU A O   1 
ATOM   1475 C  CB  . GLU A 1 184 ? 8.68900  -13.06900 45.41400 1.000 36.80000 ? 184 GLU A CB  1 
ATOM   1476 C  CG  . GLU A 1 184 ? 9.22100  -13.87500 46.61400 1.000 33.62000 ? 184 GLU A CG  1 
ATOM   1477 C  CD  . GLU A 1 184 ? 10.61600 -14.42700 46.35300 1.000 34.19000 ? 184 GLU A CD  1 
ATOM   1478 O  OE1 . GLU A 1 184 ? 10.90400 -14.77400 45.18900 1.000 40.72000 ? 184 GLU A OE1 1 
ATOM   1479 O  OE2 . GLU A 1 184 ? 11.43500 -14.49100 47.29800 1.000 34.98000 ? 184 GLU A OE2 1 
ATOM   1480 N  N   . LEU A 1 185 ? 5.77800  -14.04800 45.73500 1.000 27.40000 ? 185 LEU A N   1 
ATOM   1481 C  CA  . LEU A 1 185 ? 4.78200  -14.79200 46.49600 1.000 30.29000 ? 185 LEU A CA  1 
ATOM   1482 C  C   . LEU A 1 185 ? 3.94500  -15.69200 45.59000 1.000 33.68000 ? 185 LEU A C   1 
ATOM   1483 O  O   . LEU A 1 185 ? 3.53600  -16.78100 46.01400 1.000 31.36000 ? 185 LEU A O   1 
ATOM   1484 C  CB  . LEU A 1 185 ? 3.89000  -13.83600 47.28800 1.000 25.62000 ? 185 LEU A CB  1 
ATOM   1485 C  CG  . LEU A 1 185 ? 4.54600  -13.12200 48.47200 1.000 29.78000 ? 185 LEU A CG  1 
ATOM   1486 C  CD1 . LEU A 1 185 ? 3.50200  -12.52200 49.40100 1.000 29.39000 ? 185 LEU A CD1 1 
ATOM   1487 C  CD2 . LEU A 1 185 ? 5.48300  -14.07100 49.25200 1.000 25.53000 ? 185 LEU A CD2 1 
ATOM   1488 N  N   . GLU A 1 186 ? 3.69000  -15.27000 44.34600 1.000 29.84000 ? 186 GLU A N   1 
ATOM   1489 C  CA  . GLU A 1 186 ? 3.00800  -16.15600 43.41000 1.000 34.49000 ? 186 GLU A CA  1 
ATOM   1490 C  C   . GLU A 1 186 ? 3.82100  -17.42500 43.17600 1.000 29.46000 ? 186 GLU A C   1 
ATOM   1491 O  O   . GLU A 1 186 ? 3.29100  -18.54100 43.25200 1.000 31.43000 ? 186 GLU A O   1 
ATOM   1492 C  CB  . GLU A 1 186 ? 2.73200  -15.42500 42.08900 1.000 29.54000 ? 186 GLU A CB  1 
ATOM   1493 C  CG  . GLU A 1 186 ? 1.65900  -14.34900 42.21900 1.000 34.93000 ? 186 GLU A CG  1 
ATOM   1494 C  CD  . GLU A 1 186 ? 1.57900  -13.41800 41.00900 1.000 42.40000 ? 186 GLU A CD  1 
ATOM   1495 O  OE1 . GLU A 1 186 ? 2.44400  -13.50200 40.10700 1.000 41.04000 ? 186 GLU A OE1 1 
ATOM   1496 O  OE2 . GLU A 1 186 ? 0.64800  -12.58600 40.97100 1.000 40.10000 ? 186 GLU A OE2 1 
ATOM   1497 N  N   . ASN A 1 187 ? 5.11700  -17.26900 42.89700 1.000 32.17000 ? 187 ASN A N   1 
ATOM   1498 C  CA  . ASN A 1 187 ? 5.97300  -18.41900 42.62000 1.000 30.05000 ? 187 ASN A CA  1 
ATOM   1499 C  C   . ASN A 1 187 ? 6.13900  -19.29200 43.85600 1.000 29.73000 ? 187 ASN A C   1 
ATOM   1500 O  O   . ASN A 1 187 ? 6.11000  -20.52200 43.76200 1.000 31.20000 ? 187 ASN A O   1 
ATOM   1501 C  CB  . ASN A 1 187 ? 7.34700  -17.95000 42.11900 1.000 29.07000 ? 187 ASN A CB  1 
ATOM   1502 C  CG  . ASN A 1 187 ? 7.26100  -17.10500 40.85200 1.000 43.32000 ? 187 ASN A CG  1 
ATOM   1503 O  OD1 . ASN A 1 187 ? 6.23700  -17.09200 40.17100 1.000 45.01000 ? 187 ASN A OD1 1 
ATOM   1504 N  ND2 . ASN A 1 187 ? 8.34700  -16.40300 40.52500 1.000 46.99000 ? 187 ASN A ND2 1 
ATOM   1505 N  N   . LEU A 1 188 ? 6.34100  -18.67200 45.01700 1.000 26.74000 ? 188 LEU A N   1 
ATOM   1506 C  CA  . LEU A 1 188 ? 6.57700  -19.43700 46.23400 1.000 28.11000 ? 188 LEU A CA  1 
ATOM   1507 C  C   . LEU A 1 188 ? 5.33800  -20.22700 46.63600 1.000 25.60000 ? 188 LEU A C   1 
ATOM   1508 O  O   . LEU A 1 188 ? 5.42900  -21.41300 46.96000 1.000 23.96000 ? 188 LEU A O   1 
ATOM   1509 C  CB  . LEU A 1 188 ? 7.02700  -18.50000 47.36500 1.000 27.25000 ? 188 LEU A CB  1 
ATOM   1510 C  CG  . LEU A 1 188 ? 8.45600  -17.94000 47.23100 1.000 26.44000 ? 188 LEU A CG  1 
ATOM   1511 C  CD1 . LEU A 1 188 ? 8.90100  -17.27200 48.53400 1.000 24.95000 ? 188 LEU A CD1 1 
ATOM   1512 C  CD2 . LEU A 1 188 ? 9.44500  -19.02200 46.83100 1.000 25.68000 ? 188 LEU A CD2 1 
ATOM   1513 N  N   . THR A 1 189 ? 4.16500  -19.59400 46.62800 1.000 28.30000 ? 189 THR A N   1 
ATOM   1514 C  CA  . THR A 1 189 ? 2.97500  -20.33000 47.03100 1.000 27.77000 ? 189 THR A CA  1 
ATOM   1515 C  C   . THR A 1 189 ? 2.72600  -21.48700 46.07200 1.000 29.28000 ? 189 THR A C   1 
ATOM   1516 O  O   . THR A 1 189 ? 2.39500  -22.60100 46.49900 1.000 29.30000 ? 189 THR A O   1 
ATOM   1517 C  CB  . THR A 1 189 ? 1.76500  -19.39900 47.11500 1.000 31.05000 ? 189 THR A CB  1 
ATOM   1518 O  OG1 . THR A 1 189 ? 1.62400  -18.66700 45.89300 1.000 31.93000 ? 189 THR A OG1 1 
ATOM   1519 C  CG2 . THR A 1 189 ? 1.93200  -18.41500 48.27200 1.000 32.38000 ? 189 THR A CG2 1 
ATOM   1520 N  N   . MET A 1 190 ? 3.00800  -21.29400 44.79600 1.000 30.21000 ? 190 MET A N   1 
ATOM   1521 C  CA  . MET A 1 190 ? 2.79300  -22.36700 43.79800 1.000 32.36000 ? 190 MET A CA  1 
ATOM   1522 C  C   . MET A 1 190 ? 3.76400  -23.53200 44.04300 1.000 29.72000 ? 190 MET A C   1 
ATOM   1523 O  O   . MET A 1 190 ? 3.33100  -24.66800 43.98500 1.000 32.52000 ? 190 MET A O   1 
ATOM   1524 C  CB  . MET A 1 190 ? 2.94100  -21.83800 42.37300 1.000 35.38000 ? 190 MET A CB  1 
ATOM   1525 C  CG  . MET A 1 190 ? 3.00700  -22.92400 41.32600 1.000 40.98000 ? 190 MET A CG  1 
ATOM   1526 S  SD  . MET A 1 190 ? 2.81200  -22.26200 39.66200 1.000 63.90000 ? 190 MET A SD  1 
ATOM   1527 C  CE  . MET A 1 190 ? 1.11500  -21.69300 39.73100 1.000 51.12000 ? 190 MET A CE  1 
ATOM   1528 N  N   . ARG A 1 191 ? 5.02200  -23.23000 44.32200 1.000 30.00000 ? 191 ARG A N   1 
ATOM   1529 C  CA  . ARG A 1 191 ? 6.04200  -24.28100 44.55200 1.000 30.31000 ? 191 ARG A CA  1 
ATOM   1530 C  C   . ARG A 1 191 ? 5.68700  -25.03300 45.84000 1.000 29.09000 ? 191 ARG A C   1 
ATOM   1531 O  O   . ARG A 1 191 ? 5.79400  -26.24700 45.85500 1.000 27.56000 ? 191 ARG A O   1 
ATOM   1532 C  CB  . ARG A 1 191 ? 7.43900  -23.66100 44.61300 1.000 29.23000 ? 191 ARG A CB  1 
ATOM   1533 C  CG  . ARG A 1 191 ? 8.01600  -23.19300 43.28600 1.000 31.93000 ? 191 ARG A CG  1 
ATOM   1534 C  CD  . ARG A 1 191 ? 9.39500  -22.60800 43.52000 1.000 33.81000 ? 191 ARG A CD  1 
ATOM   1535 N  NE  . ARG A 1 191 ? 10.03500 -23.40700 44.54500 1.000 42.02000 ? 191 ARG A NE  1 
ATOM   1536 C  CZ  . ARG A 1 191 ? 10.83800 -22.95300 45.49200 1.000 32.67000 ? 191 ARG A CZ  1 
ATOM   1537 N  NH1 . ARG A 1 191 ? 11.15600 -21.67400 45.55500 1.000 34.48000 ? 191 ARG A NH1 1 
ATOM   1538 N  NH2 . ARG A 1 191 ? 11.32600 -23.79600 46.37600 1.000 32.43000 ? 191 ARG A NH2 1 
ATOM   1539 N  N   . TYR A 1 192 ? 5.25000  -24.30100 46.85400 1.000 23.24000 ? 192 TYR A N   1 
ATOM   1540 C  CA  . TYR A 1 192 ? 4.84500  -24.93700 48.12400 1.000 26.66000 ? 192 TYR A CA  1 
ATOM   1541 C  C   . TYR A 1 192 ? 3.69500  -25.90100 47.85300 1.000 28.90000 ? 192 TYR A C   1 
ATOM   1542 O  O   . TYR A 1 192 ? 3.74100  -27.02200 48.32700 1.000 33.70000 ? 192 TYR A O   1 
ATOM   1543 C  CB  . TYR A 1 192 ? 4.46700  -23.90800 49.18500 1.000 25.11000 ? 192 TYR A CB  1 
ATOM   1544 C  CG  . TYR A 1 192 ? 4.12000  -24.52900 50.51200 1.000 30.51000 ? 192 TYR A CG  1 
ATOM   1545 C  CD1 . TYR A 1 192 ? 5.10300  -24.84200 51.43300 1.000 27.20000 ? 192 TYR A CD1 1 
ATOM   1546 C  CD2 . TYR A 1 192 ? 2.81000  -24.82500 50.83900 1.000 35.25000 ? 192 TYR A CD2 1 
ATOM   1547 C  CE1 . TYR A 1 192 ? 4.79100  -25.41700 52.65100 1.000 32.87000 ? 192 TYR A CE1 1 
ATOM   1548 C  CE2 . TYR A 1 192 ? 2.48000  -25.39900 52.05200 1.000 34.12000 ? 192 TYR A CE2 1 
ATOM   1549 C  CZ  . TYR A 1 192 ? 3.47400  -25.69700 52.96100 1.000 31.78000 ? 192 TYR A CZ  1 
ATOM   1550 O  OH  . TYR A 1 192 ? 3.15400  -26.25700 54.15800 1.000 33.19000 ? 192 TYR A OH  1 
ATOM   1551 N  N   . SER A 1 193 ? 2.71300  -25.44700 47.08900 1.000 28.75000 ? 193 SER A N   1 
ATOM   1552 C  CA  . SER A 1 193 ? 1.56000  -26.30700 46.85300 1.000 28.82000 ? 193 SER A CA  1 
ATOM   1553 C  C   . SER A 1 193 ? 1.92300  -27.54700 46.04500 1.000 26.30000 ? 193 SER A C   1 
ATOM   1554 O  O   . SER A 1 193 ? 1.20100  -28.54300 46.12200 1.000 35.27000 ? 193 SER A O   1 
ATOM   1555 C  CB  . SER A 1 193 ? 0.44900  -25.52600 46.14900 1.000 24.58000 ? 193 SER A CB  1 
ATOM   1556 O  OG  . SER A 1 193 ? 0.68400  -25.46800 44.75100 1.000 36.32000 ? 193 SER A OG  1 
ATOM   1557 N  N   . TYR A 1 194 ? 3.01400  -27.52200 45.27000 1.000 29.79000 ? 194 TYR A N   1 
ATOM   1558 C  CA  . TYR A 1 194 ? 3.49800  -28.73400 44.61000 1.000 27.86000 ? 194 TYR A CA  1 
ATOM   1559 C  C   . TYR A 1 194 ? 4.56300  -29.46200 45.42000 1.000 31.49000 ? 194 TYR A C   1 
ATOM   1560 O  O   . TYR A 1 194 ? 5.13300  -30.44500 44.92800 1.000 30.12000 ? 194 TYR A O   1 
ATOM   1561 C  CB  . TYR A 1 194 ? 4.07400  -28.43000 43.23400 1.000 25.93000 ? 194 TYR A CB  1 
ATOM   1562 C  CG  . TYR A 1 194 ? 3.06800  -28.14900 42.13500 1.000 34.99000 ? 194 TYR A CG  1 
ATOM   1563 C  CD1 . TYR A 1 194 ? 2.38300  -29.18400 41.48500 1.000 31.12000 ? 194 TYR A CD1 1 
ATOM   1564 C  CD2 . TYR A 1 194 ? 2.84100  -26.84500 41.71500 1.000 34.05000 ? 194 TYR A CD2 1 
ATOM   1565 C  CE1 . TYR A 1 194 ? 1.48200  -28.91000 40.45400 1.000 31.08000 ? 194 TYR A CE1 1 
ATOM   1566 C  CE2 . TYR A 1 194 ? 1.95200  -26.56200 40.69800 1.000 37.47000 ? 194 TYR A CE2 1 
ATOM   1567 C  CZ  . TYR A 1 194 ? 1.27400  -27.58500 40.07300 1.000 35.84000 ? 194 TYR A CZ  1 
ATOM   1568 O  OH  . TYR A 1 194 ? 0.40200  -27.23900 39.06400 1.000 41.60000 ? 194 TYR A OH  1 
ATOM   1569 N  N   . ASN A 1 195 ? 4.86900  -28.98600 46.62700 1.000 27.18000 ? 195 ASN A N   1 
ATOM   1570 C  CA  . ASN A 1 195 ? 5.90600  -29.59700 47.45100 1.000 31.41000 ? 195 ASN A CA  1 
ATOM   1571 C  C   . ASN A 1 195 ? 7.25200  -29.57900 46.72600 1.000 32.80000 ? 195 ASN A C   1 
ATOM   1572 O  O   . ASN A 1 195 ? 8.01900  -30.54500 46.77000 1.000 30.61000 ? 195 ASN A O   1 
ATOM   1573 C  CB  . ASN A 1 195 ? 5.51800  -31.01600 47.84600 1.000 32.29000 ? 195 ASN A CB  1 
ATOM   1574 C  CG  . ASN A 1 195 ? 6.15900  -31.44100 49.12200 1.000 34.14000 ? 195 ASN A CG  1 
ATOM   1575 O  OD1 . ASN A 1 195 ? 5.92000  -30.84700 50.17800 1.000 37.95000 ? 195 ASN A OD1 1 
ATOM   1576 N  ND2 . ASN A 1 195 ? 6.99800  -32.46100 49.04400 1.000 29.34000 ? 195 ASN A ND2 1 
ATOM   1577 N  N   . ASP A 1 196 ? 7.53300  -28.46700 46.04700 1.000 30.10000 ? 196 ASP A N   1 
ATOM   1578 C  CA  . ASP A 1 196 ? 8.68800  -28.32700 45.15600 1.000 35.15000 ? 196 ASP A CA  1 
ATOM   1579 C  C   . ASP A 1 196 ? 9.67500  -27.37000 45.81300 1.000 28.65000 ? 196 ASP A C   1 
ATOM   1580 O  O   . ASP A 1 196 ? 9.47000  -26.15700 45.81600 1.000 29.71000 ? 196 ASP A O   1 
ATOM   1581 C  CB  . ASP A 1 196 ? 8.25400  -27.82100 43.78000 1.000 33.00000 ? 196 ASP A CB  1 
ATOM   1582 C  CG  . ASP A 1 196 ? 9.42400  -27.61100 42.82300 1.000 36.12000 ? 196 ASP A CG  1 
ATOM   1583 O  OD1 . ASP A 1 196 ? 10.55900 -28.06700 43.09800 1.000 40.39000 ? 196 ASP A OD1 1 
ATOM   1584 O  OD2 . ASP A 1 196 ? 9.19900  -26.98200 41.77000 1.000 40.38000 ? 196 ASP A OD2 1 
ATOM   1585 N  N   . PHE A 1 197 ? 10.75200 -27.91800 46.35600 1.000 29.84000 ? 197 PHE A N   1 
ATOM   1586 C  CA  . PHE A 1 197 ? 11.76000 -27.11700 47.02700 1.000 24.75000 ? 197 PHE A CA  1 
ATOM   1587 C  C   . PHE A 1 197 ? 13.12500 -27.23500 46.37500 1.000 35.07000 ? 197 PHE A C   1 
ATOM   1588 O  O   . PHE A 1 197 ? 14.12500 -26.81200 46.97400 1.000 32.29000 ? 197 PHE A O   1 
ATOM   1589 C  CB  . PHE A 1 197 ? 11.83200 -27.52400 48.49200 1.000 28.95000 ? 197 PHE A CB  1 
ATOM   1590 C  CG  . PHE A 1 197 ? 10.50700 -27.47500 49.19000 1.000 32.37000 ? 197 PHE A CG  1 
ATOM   1591 C  CD1 . PHE A 1 197 ? 9.91400  -26.25100 49.49300 1.000 28.50000 ? 197 PHE A CD1 1 
ATOM   1592 C  CD2 . PHE A 1 197 ? 9.84300  -28.64400 49.52100 1.000 27.54000 ? 197 PHE A CD2 1 
ATOM   1593 C  CE1 . PHE A 1 197 ? 8.69500  -26.19600 50.14300 1.000 26.49000 ? 197 PHE A CE1 1 
ATOM   1594 C  CE2 . PHE A 1 197 ? 8.62000  -28.60600 50.16900 1.000 31.15000 ? 197 PHE A CE2 1 
ATOM   1595 C  CZ  . PHE A 1 197 ? 8.04200  -27.37900 50.48400 1.000 33.03000 ? 197 PHE A CZ  1 
ATOM   1596 N  N   . ARG A 1 198 ? 13.18700 -27.79000 45.16300 1.000 32.75000 ? 198 ARG A N   1 
ATOM   1597 C  CA  . ARG A 1 198 ? 14.45800 -28.00500 44.49400 1.000 33.95000 ? 198 ARG A CA  1 
ATOM   1598 C  C   . ARG A 1 198 ? 15.19800 -26.68800 44.32200 1.000 36.78000 ? 198 ARG A C   1 
ATOM   1599 O  O   . ARG A 1 198 ? 14.59400 -25.65300 44.02900 1.000 36.37000 ? 198 ARG A O   1 
ATOM   1600 C  CB  . ARG A 1 198 ? 14.21800 -28.65200 43.13400 1.000 34.11000 ? 198 ARG A CB  1 
ATOM   1601 C  CG  . ARG A 1 198 ? 13.73900 -30.08200 43.21600 1.000 39.37000 ? 198 ARG A CG  1 
ATOM   1602 C  CD  . ARG A 1 198 ? 13.37300 -30.59400 41.83000 1.000 45.35000 ? 198 ARG A CD  1 
ATOM   1603 N  NE  . ARG A 1 198 ? 12.27900 -29.81600 41.26900 1.000 41.70000 ? 198 ARG A NE  1 
ATOM   1604 C  CZ  . ARG A 1 198 ? 11.87900 -29.87000 40.00600 1.000 50.21000 ? 198 ARG A CZ  1 
ATOM   1605 N  NH1 . ARG A 1 198 ? 12.48900 -30.68000 39.14400 1.000 52.18000 ? 198 ARG A NH1 1 
ATOM   1606 N  NH2 . ARG A 1 198 ? 10.86300 -29.11200 39.61300 1.000 40.47000 ? 198 ARG A NH2 1 
ATOM   1607 N  N   . GLU A 1 199 ? 16.51000 -26.72800 44.54300 1.000 40.85000 ? 199 GLU A N   1 
ATOM   1608 C  CA  . GLU A 1 199 ? 17.42300 -25.62700 44.25200 1.000 38.45000 ? 199 GLU A CA  1 
ATOM   1609 C  C   . GLU A 1 199 ? 17.13400 -24.38600 45.08300 1.000 36.43000 ? 199 GLU A C   1 
ATOM   1610 O  O   . GLU A 1 199 ? 17.69400 -23.31800 44.82000 1.000 40.42000 ? 199 GLU A O   1 
ATOM   1611 C  CB  . GLU A 1 199 ? 17.39800 -25.27600 42.75200 1.000 45.16000 ? 199 GLU A CB  1 
ATOM   1612 C  CG  . GLU A 1 199 ? 18.53700 -25.90200 41.96700 1.000 58.62000 ? 199 GLU A CG  1 
ATOM   1613 C  CD  . GLU A 1 199 ? 18.22600 -26.10900 40.48900 1.000 71.11000 ? 199 GLU A CD  1 
ATOM   1614 O  OE1 . GLU A 1 199 ? 17.29000 -26.88000 40.17800 1.000 70.69000 ? 199 GLU A OE1 1 
ATOM   1615 O  OE2 . GLU A 1 199 ? 18.93400 -25.51800 39.63900 1.000 73.19000 ? 199 GLU A OE2 1 
ATOM   1616 N  N   . GLN A 1 200 ? 16.27600 -24.49400 46.09200 1.000 33.91000 ? 200 GLN A N   1 
ATOM   1617 C  CA  . GLN A 1 200 ? 15.91000 -23.33400 46.89200 1.000 34.55000 ? 200 GLN A CA  1 
ATOM   1618 C  C   . GLN A 1 200 ? 16.96000 -22.97300 47.94500 1.000 30.95000 ? 200 GLN A C   1 
ATOM   1619 O  O   . GLN A 1 200 ? 16.96600 -21.83400 48.42800 1.000 34.28000 ? 200 GLN A O   1 
ATOM   1620 C  CB  . GLN A 1 200 ? 14.53000 -23.60500 47.50600 1.000 33.12000 ? 200 GLN A CB  1 
ATOM   1621 C  CG  . GLN A 1 200 ? 14.30700 -23.12600 48.90600 1.000 38.73000 ? 200 GLN A CG  1 
ATOM   1622 C  CD  . GLN A 1 200 ? 12.91100 -23.47000 49.42300 1.000 33.03000 ? 200 GLN A CD  1 
ATOM   1623 O  OE1 . GLN A 1 200 ? 11.91700 -23.31800 48.71400 1.000 27.47000 ? 200 GLN A OE1 1 
ATOM   1624 N  NE2 . GLN A 1 200 ? 12.83400 -23.87400 50.68200 1.000 28.09000 ? 200 GLN A NE2 1 
ATOM   1625 N  N   . GLY A 1 201 ? 17.87900 -23.88100 48.27000 1.000 29.09000 ? 201 GLY A N   1 
ATOM   1626 C  CA  . GLY A 1 201 ? 18.83500 -23.60700 49.32700 1.000 32.00000 ? 201 GLY A CA  1 
ATOM   1627 C  C   . GLY A 1 201 ? 19.84800 -22.52100 48.98000 1.000 36.06000 ? 201 GLY A C   1 
ATOM   1628 O  O   . GLY A 1 201 ? 20.10100 -22.17900 47.81900 1.000 31.29000 ? 201 GLY A O   1 
ATOM   1629 N  N   . GLU A 1 202 ? 20.46200 -21.98500 50.03700 1.000 33.64000 ? 202 GLU A N   1 
ATOM   1630 C  CA  . GLU A 1 202 ? 21.46800 -20.93600 49.94100 1.000 36.54000 ? 202 GLU A CA  1 
ATOM   1631 C  C   . GLU A 1 202 ? 22.79100 -21.44200 50.50500 1.000 29.49000 ? 202 GLU A C   1 
ATOM   1632 O  O   . GLU A 1 202 ? 22.81600 -22.26800 51.42500 1.000 31.07000 ? 202 GLU A O   1 
ATOM   1633 C  CB  . GLU A 1 202 ? 21.00500 -19.65800 50.68400 1.000 33.50000 ? 202 GLU A CB  1 
ATOM   1634 C  CG  . GLU A 1 202 ? 19.93600 -18.91900 49.90100 1.000 40.40000 ? 202 GLU A CG  1 
ATOM   1635 C  CD  . GLU A 1 202 ? 19.34700 -17.72300 50.61900 1.000 44.12000 ? 202 GLU A CD  1 
ATOM   1636 O  OE1 . GLU A 1 202 ? 19.63800 -17.54300 51.81500 1.000 46.87000 ? 202 GLU A OE1 1 
ATOM   1637 O  OE2 . GLU A 1 202 ? 18.58100 -16.96300 49.97600 1.000 51.87000 ? 202 GLU A OE2 1 
ATOM   1638 N  N   . ASP A 1 203 ? 23.89000 -20.96700 49.92900 1.000 30.49000 ? 203 ASP A N   1 
ATOM   1639 C  CA  . ASP A 1 203 ? 25.21400 -21.40300 50.35700 1.000 28.39000 ? 203 ASP A CA  1 
ATOM   1640 C  C   . ASP A 1 203 ? 25.62100 -20.72800 51.66000 1.000 28.26000 ? 203 ASP A C   1 
ATOM   1641 O  O   . ASP A 1 203 ? 25.30400 -19.56300 51.91300 1.000 27.31000 ? 203 ASP A O   1 
ATOM   1642 C  CB  . ASP A 1 203 ? 26.25000 -21.11800 49.28100 1.000 31.37000 ? 203 ASP A CB  1 
ATOM   1643 C  CG  . ASP A 1 203 ? 26.13000 -22.06700 48.10600 1.000 40.47000 ? 203 ASP A CG  1 
ATOM   1644 O  OD1 . ASP A 1 203 ? 26.33100 -23.28400 48.32400 1.000 42.71000 ? 203 ASP A OD1 1 
ATOM   1645 O  OD2 . ASP A 1 203 ? 25.82800 -21.60200 46.97800 1.000 45.49000 ? 203 ASP A OD2 1 
ATOM   1646 N  N   . PHE A 1 204 ? 26.33900 -21.47600 52.48600 1.000 24.42000 ? 204 PHE A N   1 
ATOM   1647 C  CA  . PHE A 1 204 ? 26.68700 -21.01700 53.81900 1.000 25.27000 ? 204 PHE A CA  1 
ATOM   1648 C  C   . PHE A 1 204 ? 28.15600 -21.29000 54.07100 1.000 25.04000 ? 204 PHE A C   1 
ATOM   1649 O  O   . PHE A 1 204 ? 28.64700 -22.38000 53.77600 1.000 22.33000 ? 204 PHE A O   1 
ATOM   1650 C  CB  . PHE A 1 204 ? 25.84500 -21.72000 54.89300 1.000 23.76000 ? 204 PHE A CB  1 
ATOM   1651 C  CG  . PHE A 1 204 ? 26.23600 -21.35400 56.30400 1.000 28.84000 ? 204 PHE A CG  1 
ATOM   1652 C  CD1 . PHE A 1 204 ? 27.22900 -22.05900 56.98200 1.000 23.84000 ? 204 PHE A CD1 1 
ATOM   1653 C  CD2 . PHE A 1 204 ? 25.61000 -20.30300 56.95100 1.000 26.67000 ? 204 PHE A CD2 1 
ATOM   1654 C  CE1 . PHE A 1 204 ? 27.57700 -21.72200 58.26600 1.000 29.83000 ? 204 PHE A CE1 1 
ATOM   1655 C  CE2 . PHE A 1 204 ? 25.96500 -19.94900 58.23900 1.000 30.57000 ? 204 PHE A CE2 1 
ATOM   1656 C  CZ  . PHE A 1 204 ? 26.93500 -20.66600 58.91000 1.000 29.99000 ? 204 PHE A CZ  1 
ATOM   1657 N  N   . LEU A 1 205 ? 28.85800 -20.31900 54.64300 1.000 21.10000 ? 205 LEU A N   1 
ATOM   1658 C  CA  . LEU A 1 205 ? 30.18900 -20.62200 55.14100 1.000 25.78000 ? 205 LEU A CA  1 
ATOM   1659 C  C   . LEU A 1 205 ? 30.42200 -19.88100 56.44600 1.000 23.65000 ? 205 LEU A C   1 
ATOM   1660 O  O   . LEU A 1 205 ? 29.75900 -18.89300 56.76300 1.000 23.57000 ? 205 LEU A O   1 
ATOM   1661 C  CB  . LEU A 1 205 ? 31.29900 -20.29500 54.12000 1.000 25.42000 ? 205 LEU A CB  1 
ATOM   1662 C  CG  . LEU A 1 205 ? 31.55500 -18.85100 53.69300 1.000 28.53000 ? 205 LEU A CG  1 
ATOM   1663 C  CD1 . LEU A 1 205 ? 32.18300 -17.95300 54.78200 1.000 29.53000 ? 205 LEU A CD1 1 
ATOM   1664 C  CD2 . LEU A 1 205 ? 32.46500 -18.84300 52.43800 1.000 31.04000 ? 205 LEU A CD2 1 
ATOM   1665 N  N   . LYS A 1 206 ? 31.39400 -20.36100 57.20100 1.000 21.38000 ? 206 LYS A N   1 
ATOM   1666 C  CA  . LYS A 1 206 ? 31.75300 -19.71100 58.44700 1.000 21.85000 ? 206 LYS A CA  1 
ATOM   1667 C  C   . LYS A 1 206 ? 33.26000 -19.60300 58.48800 1.000 22.49000 ? 206 LYS A C   1 
ATOM   1668 O  O   . LYS A 1 206 ? 33.96100 -20.59000 58.24800 1.000 22.64000 ? 206 LYS A O   1 
ATOM   1669 C  CB  . LYS A 1 206 ? 31.23200 -20.48800 59.65900 1.000 22.11000 ? 206 LYS A CB  1 
ATOM   1670 C  CG  . LYS A 1 206 ? 31.58300 -19.84900 60.99400 1.000 26.28000 ? 206 LYS A CG  1 
ATOM   1671 C  CD  . LYS A 1 206 ? 30.70600 -20.37000 62.13800 1.000 32.65000 ? 206 LYS A CD  1 
ATOM   1672 C  CE  . LYS A 1 206 ? 30.77200 -21.89000 62.23700 1.000 36.99000 ? 206 LYS A CE  1 
ATOM   1673 N  NZ  . LYS A 1 206 ? 32.16300 -22.42700 62.40300 1.000 42.58000 ? 206 LYS A NZ  1 
ATOM   1674 N  N   . VAL A 1 207 ? 33.74400 -18.40000 58.74800 1.000 24.29000 ? 207 VAL A N   1 
ATOM   1675 C  CA  . VAL A 1 207 ? 35.15200 -18.14900 59.00600 1.000 25.77000 ? 207 VAL A CA  1 
ATOM   1676 C  C   . VAL A 1 207 ? 35.33800 -18.08900 60.51000 1.000 23.98000 ? 207 VAL A C   1 
ATOM   1677 O  O   . VAL A 1 207 ? 34.70300 -17.28000 61.18700 1.000 24.81000 ? 207 VAL A O   1 
ATOM   1678 C  CB  . VAL A 1 207 ? 35.61800 -16.83700 58.36300 1.000 23.98000 ? 207 VAL A CB  1 
ATOM   1679 C  CG1 . VAL A 1 207 ? 37.11300 -16.67200 58.57900 1.000 27.35000 ? 207 VAL A CG1 1 
ATOM   1680 C  CG2 . VAL A 1 207 ? 35.24300 -16.80000 56.89200 1.000 25.88000 ? 207 VAL A CG2 1 
ATOM   1681 N  N   . THR A 1 208 ? 36.18900 -18.94200 61.04400 1.000 25.77000 ? 208 THR A N   1 
ATOM   1682 C  CA  . THR A 1 208 ? 36.58200 -18.82500 62.44800 1.000 29.91000 ? 208 THR A CA  1 
ATOM   1683 C  C   . THR A 1 208 ? 37.87100 -18.02800 62.46600 1.000 24.36000 ? 208 THR A C   1 
ATOM   1684 O  O   . THR A 1 208 ? 38.93600 -18.56600 62.17300 1.000 24.20000 ? 208 THR A O   1 
ATOM   1685 C  CB  . THR A 1 208 ? 36.77900 -20.20000 63.07900 1.000 27.40000 ? 208 THR A CB  1 
ATOM   1686 O  OG1 . THR A 1 208 ? 35.62800 -21.00500 62.81000 1.000 28.98000 ? 208 THR A OG1 1 
ATOM   1687 C  CG2 . THR A 1 208 ? 36.98300 -20.07300 64.57800 1.000 26.84000 ? 208 THR A CG2 1 
ATOM   1688 N  N   . LEU A 1 209 ? 37.78600 -16.73900 62.79300 1.000 24.08000 ? 209 LEU A N   1 
ATOM   1689 C  CA  . LEU A 1 209 ? 38.93400 -15.85800 62.61000 1.000 26.56000 ? 209 LEU A CA  1 
ATOM   1690 C  C   . LEU A 1 209 ? 40.01300 -16.13700 63.64100 1.000 25.66000 ? 209 LEU A C   1 
ATOM   1691 O  O   . LEU A 1 209 ? 39.72200 -16.29600 64.82700 1.000 25.77000 ? 209 LEU A O   1 
ATOM   1692 C  CB  . LEU A 1 209 ? 38.50900 -14.39700 62.71000 1.000 26.58000 ? 209 LEU A CB  1 
ATOM   1693 C  CG  . LEU A 1 209 ? 37.63000 -13.89400 61.57400 1.000 27.27000 ? 209 LEU A CG  1 
ATOM   1694 C  CD1 . LEU A 1 209 ? 37.00100 -12.61800 62.06000 1.000 26.74000 ? 209 LEU A CD1 1 
ATOM   1695 C  CD2 . LEU A 1 209 ? 38.44500 -13.67100 60.28600 1.000 26.98000 ? 209 LEU A CD2 1 
ATOM   1696 N  N   . SER A 1 210 ? 41.26200 -16.18600 63.19400 1.000 24.23000 ? 210 SER A N   1 
ATOM   1697 C  CA  . SER A 1 210 ? 42.37100 -16.17400 64.13600 1.000 24.62000 ? 210 SER A CA  1 
ATOM   1698 C  C   . SER A 1 210 ? 42.74800 -14.73200 64.47600 1.000 24.65000 ? 210 SER A C   1 
ATOM   1699 O  O   . SER A 1 210 ? 42.32600 -13.77400 63.81900 1.000 25.27000 ? 210 SER A O   1 
ATOM   1700 C  CB  . SER A 1 210 ? 43.57200 -16.92900 63.57100 1.000 24.46000 ? 210 SER A CB  1 
ATOM   1701 O  OG  . SER A 1 210 ? 44.24100 -16.16800 62.57100 1.000 26.28000 ? 210 SER A OG  1 
ATOM   1702 N  N   . LEU A 1 211 ? 43.56700 -14.58100 65.51600 1.000 25.54000 ? 211 LEU A N   1 
ATOM   1703 C  CA  . LEU A 1 211 ? 44.07300 -13.26100 65.84800 1.000 21.97000 ? 211 LEU A CA  1 
ATOM   1704 C  C   . LEU A 1 211 ? 44.92300 -12.69800 64.71800 1.000 26.44000 ? 211 LEU A C   1 
ATOM   1705 O  O   . LEU A 1 211 ? 44.93700 -11.48000 64.49800 1.000 27.21000 ? 211 LEU A O   1 
ATOM   1706 C  CB  . LEU A 1 211 ? 44.87500 -13.32400 67.14100 1.000 25.86000 ? 211 LEU A CB  1 
ATOM   1707 C  CG  . LEU A 1 211 ? 45.47700 -12.02200 67.66200 1.000 26.63000 ? 211 LEU A CG  1 
ATOM   1708 C  CD1 . LEU A 1 211 ? 44.41800 -10.90000 67.79900 1.000 22.80000 ? 211 LEU A CD1 1 
ATOM   1709 C  CD2 . LEU A 1 211 ? 46.16900 -12.31800 69.00600 1.000 26.26000 ? 211 LEU A CD2 1 
ATOM   1710 N  N   . GLU A 1 212 ? 45.61900 -13.56400 63.97900 1.000 25.45000 ? 212 GLU A N   1 
ATOM   1711 C  CA  . GLU A 1 212 ? 46.40000 -13.10100 62.84300 1.000 26.49000 ? 212 GLU A CA  1 
ATOM   1712 C  C   . GLU A 1 212 ? 45.51400 -12.38700 61.83200 1.000 31.39000 ? 212 GLU A C   1 
ATOM   1713 O  O   . GLU A 1 212 ? 45.86100 -11.30500 61.33300 1.000 25.76000 ? 212 GLU A O   1 
ATOM   1714 C  CB  . GLU A 1 212 ? 47.11800 -14.28100 62.19600 1.000 28.20000 ? 212 GLU A CB  1 
ATOM   1715 C  CG  . GLU A 1 212 ? 48.01700 -13.90300 61.03000 1.000 29.33000 ? 212 GLU A CG  1 
ATOM   1716 C  CD  . GLU A 1 212 ? 49.27900 -13.15000 61.47000 1.000 42.32000 ? 212 GLU A CD  1 
ATOM   1717 O  OE1 . GLU A 1 212 ? 49.60900 -13.13300 62.68800 1.000 43.84000 ? 212 GLU A OE1 1 
ATOM   1718 O  OE2 . GLU A 1 212 ? 49.95300 -12.58600 60.58200 1.000 45.54000 ? 212 GLU A OE2 1 
ATOM   1719 N  N   . ASP A 1 213 ? 44.36000 -12.98300 61.50800 1.000 26.75000 ? 213 ASP A N   1 
ATOM   1720 C  CA  . ASP A 1 213 ? 43.47600 -12.33900 60.54500 1.000 25.95000 ? 213 ASP A CA  1 
ATOM   1721 C  C   . ASP A 1 213 ? 42.72500 -11.16500 61.17400 1.000 28.23000 ? 213 ASP A C   1 
ATOM   1722 O  O   . ASP A 1 213 ? 42.39500 -10.20800 60.46700 1.000 25.39000 ? 213 ASP A O   1 
ATOM   1723 C  CB  . ASP A 1 213 ? 42.53100 -13.37000 59.92900 1.000 23.63000 ? 213 ASP A CB  1 
ATOM   1724 C  CG  . ASP A 1 213 ? 43.21700 -14.19000 58.81200 1.000 30.80000 ? 213 ASP A CG  1 
ATOM   1725 O  OD1 . ASP A 1 213 ? 44.06600 -13.61800 58.07300 1.000 32.72000 ? 213 ASP A OD1 1 
ATOM   1726 O  OD2 . ASP A 1 213 ? 42.93200 -15.39300 58.66700 1.000 30.55000 ? 213 ASP A OD2 1 
ATOM   1727 N  N   . LYS A 1 214 ? 42.46700 -11.20500 62.49100 1.000 22.38000 ? 214 LYS A N   1 
ATOM   1728 C  CA  . LYS A 1 214 ? 41.89400 -10.03500 63.16100 1.000 23.81000 ? 214 LYS A CA  1 
ATOM   1729 C  C   . LYS A 1 214 ? 42.85700 -8.85300  63.13400 1.000 25.60000 ? 214 LYS A C   1 
ATOM   1730 O  O   . LYS A 1 214 ? 42.43000 -7.70600  62.96500 1.000 26.90000 ? 214 LYS A O   1 
ATOM   1731 C  CB  . LYS A 1 214 ? 41.50300 -10.36000 64.59700 1.000 23.81000 ? 214 LYS A CB  1 
ATOM   1732 C  CG  . LYS A 1 214 ? 40.29500 -11.26800 64.67000 1.000 26.68000 ? 214 LYS A CG  1 
ATOM   1733 C  CD  . LYS A 1 214 ? 39.94400 -11.58000 66.07800 1.000 28.17000 ? 214 LYS A CD  1 
ATOM   1734 C  CE  . LYS A 1 214 ? 38.94100 -12.71400 66.13900 1.000 29.71000 ? 214 LYS A CE  1 
ATOM   1735 N  NZ  . LYS A 1 214 ? 38.40000 -12.81900 67.50900 1.000 22.36000 ? 214 LYS A NZ  1 
ATOM   1736 N  N   . LEU A 1 215 ? 44.16000 -9.10500  63.31000 1.000 25.30000 ? 215 LEU A N   1 
ATOM   1737 C  CA  . LEU A 1 215 ? 45.12900 -8.01400  63.19700 1.000 28.00000 ? 215 LEU A CA  1 
ATOM   1738 C  C   . LEU A 1 215 ? 45.20400 -7.49800  61.76700 1.000 28.71000 ? 215 LEU A C   1 
ATOM   1739 O  O   . LEU A 1 215 ? 45.35700 -6.29100  61.53400 1.000 28.24000 ? 215 LEU A O   1 
ATOM   1740 C  CB  . LEU A 1 215 ? 46.50400 -8.47500  63.67800 1.000 24.47000 ? 215 LEU A CB  1 
ATOM   1741 C  CG  . LEU A 1 215 ? 46.53300 -8.73400  65.18200 1.000 29.87000 ? 215 LEU A CG  1 
ATOM   1742 C  CD1 . LEU A 1 215 ? 47.80100 -9.46300  65.55500 1.000 31.47000 ? 215 LEU A CD1 1 
ATOM   1743 C  CD2 . LEU A 1 215 ? 46.39700 -7.42900  65.96000 1.000 26.03000 ? 215 LEU A CD2 1 
ATOM   1744 N  N   . PHE A 1 216 ? 45.13200 -8.40600  60.79600 1.000 26.90000 ? 216 PHE A N   1 
ATOM   1745 C  CA  . PHE A 1 216 ? 45.04600 -7.99900  59.40000 1.000 28.86000 ? 216 PHE A CA  1 
ATOM   1746 C  C   . PHE A 1 216 ? 43.82900 -7.11700  59.17200 1.000 27.38000 ? 216 PHE A C   1 
ATOM   1747 O  O   . PHE A 1 216 ? 43.90500 -6.11300  58.45600 1.000 29.25000 ? 216 PHE A O   1 
ATOM   1748 C  CB  . PHE A 1 216 ? 44.99800 -9.23800  58.51100 1.000 26.53000 ? 216 PHE A CB  1 
ATOM   1749 C  CG  . PHE A 1 216 ? 44.56800 -8.95400  57.11000 1.000 31.55000 ? 216 PHE A CG  1 
ATOM   1750 C  CD1 . PHE A 1 216 ? 45.32600 -8.13600  56.30000 1.000 34.81000 ? 216 PHE A CD1 1 
ATOM   1751 C  CD2 . PHE A 1 216 ? 43.41700 -9.52600  56.59400 1.000 32.75000 ? 216 PHE A CD2 1 
ATOM   1752 C  CE1 . PHE A 1 216 ? 44.94600 -7.87900  55.00900 1.000 36.19000 ? 216 PHE A CE1 1 
ATOM   1753 C  CE2 . PHE A 1 216 ? 43.02400 -9.26600  55.28500 1.000 36.10000 ? 216 PHE A CE2 1 
ATOM   1754 C  CZ  . PHE A 1 216 ? 43.79600 -8.44300  54.49600 1.000 34.55000 ? 216 PHE A CZ  1 
ATOM   1755 N  N   . LEU A 1 217 ? 42.70200 -7.45200  59.81200 1.000 21.62000 ? 217 LEU A N   1 
ATOM   1756 C  CA  . LEU A 1 217 ? 41.51600 -6.61000  59.68500 1.000 26.50000 ? 217 LEU A CA  1 
ATOM   1757 C  C   . LEU A 1 217 ? 41.68300 -5.28000  60.41800 1.000 24.95000 ? 217 LEU A C   1 
ATOM   1758 O  O   . LEU A 1 217 ? 41.17500 -4.24900  59.95200 1.000 28.80000 ? 217 LEU A O   1 
ATOM   1759 C  CB  . LEU A 1 217 ? 40.27600 -7.36500  60.16700 1.000 26.53000 ? 217 LEU A CB  1 
ATOM   1760 C  CG  . LEU A 1 217 ? 39.88600 -8.59200  59.33500 1.000 24.22000 ? 217 LEU A CG  1 
ATOM   1761 C  CD1 . LEU A 1 217 ? 38.63500 -9.23400  59.91400 1.000 23.90000 ? 217 LEU A CD1 1 
ATOM   1762 C  CD2 . LEU A 1 217 ? 39.67900 -8.25500  57.87100 1.000 23.57000 ? 217 LEU A CD2 1 
ATOM   1763 N  N   . ASP A 1 218 ? 42.37400 -5.27200  61.57100 1.000 25.81000 ? 218 ASP A N   1 
ATOM   1764 C  CA  . ASP A 1 218 ? 42.69900 -4.00300  62.22500 1.000 26.52000 ? 218 ASP A CA  1 
ATOM   1765 C  C   . ASP A 1 218 ? 43.48100 -3.09400  61.27500 1.000 33.03000 ? 218 ASP A C   1 
ATOM   1766 O  O   . ASP A 1 218 ? 43.19700 -1.89500  61.17500 1.000 32.59000 ? 218 ASP A O   1 
ATOM   1767 C  CB  . ASP A 1 218 ? 43.50500 -4.23800  63.51200 1.000 24.42000 ? 218 ASP A CB  1 
ATOM   1768 C  CG  . ASP A 1 218 ? 42.72900 -5.03900  64.59600 1.000 32.89000 ? 218 ASP A CG  1 
ATOM   1769 O  OD1 . ASP A 1 218 ? 41.47000 -4.99100  64.65800 1.000 28.15000 ? 218 ASP A OD1 1 
ATOM   1770 O  OD2 . ASP A 1 218 ? 43.40300 -5.70400  65.42600 1.000 26.02000 ? 218 ASP A OD2 1 
ATOM   1771 N  N   . ASP A 1 219 ? 44.44500 -3.66300  60.54000 1.000 32.27000 ? 219 ASP A N   1 
ATOM   1772 C  CA  . ASP A 1 219 ? 45.22300 -2.90600  59.56300 1.000 28.27000 ? 219 ASP A CA  1 
ATOM   1773 C  C   . ASP A 1 219 ? 44.33900 -2.36600  58.44500 1.000 34.66000 ? 219 ASP A C   1 
ATOM   1774 O  O   . ASP A 1 219 ? 44.45800 -1.20100  58.05400 1.000 33.65000 ? 219 ASP A O   1 
ATOM   1775 C  CB  . ASP A 1 219 ? 46.31200 -3.79300  58.96400 1.000 32.37000 ? 219 ASP A CB  1 
ATOM   1776 C  CG  . ASP A 1 219 ? 47.47600 -4.00900  59.89700 1.000 37.88000 ? 219 ASP A CG  1 
ATOM   1777 O  OD1 . ASP A 1 219 ? 47.60800 -3.25000  60.88900 1.000 41.66000 ? 219 ASP A OD1 1 
ATOM   1778 O  OD2 . ASP A 1 219 ? 48.26400 -4.94700  59.62500 1.000 43.32000 ? 219 ASP A OD2 1 
ATOM   1779 N  N   . ILE A 1 220 ? 43.46900 -3.21800  57.89000 1.000 29.70000 ? 220 ILE A N   1 
ATOM   1780 C  CA  . ILE A 1 220 ? 42.58200 -2.78600  56.81600 1.000 25.77000 ? 220 ILE A CA  1 
ATOM   1781 C  C   . ILE A 1 220 ? 41.68200 -1.65400  57.29900 1.000 32.58000 ? 220 ILE A C   1 
ATOM   1782 O  O   . ILE A 1 220 ? 41.58600 -0.59400  56.66400 1.000 30.54000 ? 220 ILE A O   1 
ATOM   1783 C  CB  . ILE A 1 220 ? 41.76400 -3.97500  56.29500 1.000 24.98000 ? 220 ILE A CB  1 
ATOM   1784 C  CG1 . ILE A 1 220 ? 42.68800 -4.98800  55.59900 1.000 29.64000 ? 220 ILE A CG1 1 
ATOM   1785 C  CG2 . ILE A 1 220 ? 40.66300 -3.48900  55.37600 1.000 26.12000 ? 220 ILE A CG2 1 
ATOM   1786 C  CD1 . ILE A 1 220 ? 43.49900 -4.41500  54.45800 1.000 32.36000 ? 220 ILE A CD1 1 
ATOM   1787 N  N   . ARG A 1 221 ? 41.01600 -1.85900  58.44000 1.000 29.05000 ? 221 ARG A N   1 
ATOM   1788 C  CA  . ARG A 1 221 ? 40.12600 -0.84300  58.97300 1.000 28.55000 ? 221 ARG A CA  1 
ATOM   1789 C  C   . ARG A 1 221 ? 40.86800 0.46400   59.18000 1.000 35.19000 ? 221 ARG A C   1 
ATOM   1790 O  O   . ARG A 1 221 ? 40.28300 1.54500   59.01900 1.000 29.76000 ? 221 ARG A O   1 
ATOM   1791 C  CB  . ARG A 1 221 ? 39.52000 -1.32500  60.29300 1.000 27.46000 ? 221 ARG A CB  1 
ATOM   1792 C  CG  . ARG A 1 221 ? 38.37200 -0.46400  60.81100 1.000 25.59000 ? 221 ARG A CG  1 
ATOM   1793 C  CD  . ARG A 1 221 ? 37.95700 -0.86700  62.21500 1.000 26.45000 ? 221 ARG A CD  1 
ATOM   1794 N  NE  . ARG A 1 221 ? 36.73900 -0.18500  62.62500 1.000 22.47000 ? 221 ARG A NE  1 
ATOM   1795 C  CZ  . ARG A 1 221 ? 36.70400 0.86900   63.43200 1.000 29.56000 ? 221 ARG A CZ  1 
ATOM   1796 N  NH1 . ARG A 1 221 ? 37.82400 1.36900   63.93000 1.000 32.27000 ? 221 ARG A NH1 1 
ATOM   1797 N  NH2 . ARG A 1 221 ? 35.54100 1.41900   63.75700 1.000 35.18000 ? 221 ARG A NH2 1 
ATOM   1798 N  N   . SER A 1 222 ? 42.15800 0.37300   59.52600 1.000 31.64000 ? 222 SER A N   1 
ATOM   1799 C  CA  . SER A 1 222 ? 42.99200 1.54200   59.76300 1.000 34.76000 ? 222 SER A CA  1 
ATOM   1800 C  C   . SER A 1 222 ? 43.10700 2.44600   58.53700 1.000 34.94000 ? 222 SER A C   1 
ATOM   1801 O  O   . SER A 1 222 ? 43.35800 3.64200   58.70600 1.000 40.58000 ? 222 SER A O   1 
ATOM   1802 C  CB  . SER A 1 222 ? 44.37700 1.05600   60.24300 1.000 35.52000 ? 222 SER A CB  1 
ATOM   1803 O  OG  . SER A 1 222 ? 45.42900 1.91700   59.85700 1.000 48.19000 ? 222 SER A OG  1 
ATOM   1804 N  N   . LEU A 1 223 ? 42.92200 1.91000   57.31900 1.000 32.65000 ? 223 LEU A N   1 
ATOM   1805 C  CA  . LEU A 1 223 ? 42.96200 2.69400   56.08200 1.000 28.82000 ? 223 LEU A CA  1 
ATOM   1806 C  C   . LEU A 1 223 ? 41.71700 3.52900   55.85600 1.000 35.72000 ? 223 LEU A C   1 
ATOM   1807 O  O   . LEU A 1 223 ? 41.67500 4.28200   54.87600 1.000 37.86000 ? 223 LEU A O   1 
ATOM   1808 C  CB  . LEU A 1 223 ? 43.12000 1.79800   54.85300 1.000 28.80000 ? 223 LEU A CB  1 
ATOM   1809 C  CG  . LEU A 1 223 ? 44.22800 0.75100   54.90800 1.000 34.84000 ? 223 LEU A CG  1 
ATOM   1810 C  CD1 . LEU A 1 223 ? 44.14300 -0.16000  53.70000 1.000 29.74000 ? 223 LEU A CD1 1 
ATOM   1811 C  CD2 . LEU A 1 223 ? 45.57800 1.44500   54.99500 1.000 34.63000 ? 223 LEU A CD2 1 
ATOM   1812 N  N   . VAL A 1 224 ? 40.69900 3.38200   56.70200 1.000 36.76000 ? 224 VAL A N   1 
ATOM   1813 C  CA  . VAL A 1 224 ? 39.40200 4.02200   56.51200 1.000 42.29000 ? 224 VAL A CA  1 
ATOM   1814 C  C   . VAL A 1 224 ? 39.07900 4.95800   57.66700 1.000 37.38000 ? 224 VAL A C   1 
ATOM   1815 O  O   . VAL A 1 224 ? 38.67800 6.10500   57.45600 1.000 41.06000 ? 224 VAL A O   1 
ATOM   1816 C  CB  . VAL A 1 224 ? 38.27700 2.97400   56.32300 1.000 36.91000 ? 224 VAL A CB  1 
ATOM   1817 C  CG1 . VAL A 1 224 ? 36.94200 3.64100   56.04200 1.000 27.19000 ? 224 VAL A CG1 1 
ATOM   1818 C  CG2 . VAL A 1 224 ? 38.63700 1.99500   55.20800 1.000 35.18000 ? 224 VAL A CG2 1 
ATOM   1819 N  N   . ILE A 1 225 ? 39.27400 4.48800   58.90300 1.000 36.36000 ? 225 ILE A N   1 
ATOM   1820 C  CA  . ILE A 1 225 ? 39.01200 5.26000   60.11400 1.000 34.73000 ? 225 ILE A CA  1 
ATOM   1821 C  C   . ILE A 1 225 ? 40.05500 4.85700   61.16100 1.000 42.45000 ? 225 ILE A C   1 
ATOM   1822 O  O   . ILE A 1 225 ? 40.71600 3.81500   61.04200 1.000 38.31000 ? 225 ILE A O   1 
ATOM   1823 C  CB  . ILE A 1 225 ? 37.55200 5.03400   60.61000 1.000 39.80000 ? 225 ILE A CB  1 
ATOM   1824 C  CG1 . ILE A 1 225 ? 37.26900 5.76100   61.93600 1.000 49.52000 ? 225 ILE A CG1 1 
ATOM   1825 C  CG2 . ILE A 1 225 ? 37.23500 3.53600   60.73500 1.000 34.85000 ? 225 ILE A CG2 1 
ATOM   1826 C  CD1 . ILE A 1 225 ? 35.79500 5.98600   62.25800 1.000 47.60000 ? 225 ILE A CD1 1 
ATOM   1827 N  N   . ASN A 1 226 ? 40.22900 5.71600   62.17400 1.000 42.57000 ? 226 ASN A N   1 
ATOM   1828 C  CA  . ASN A 1 226 ? 41.12000 5.45100   63.30400 1.000 37.94000 ? 226 ASN A CA  1 
ATOM   1829 C  C   . ASN A 1 226 ? 40.85800 4.07800   63.91600 1.000 38.49000 ? 226 ASN A C   1 
ATOM   1830 O  O   . ASN A 1 226 ? 39.72400 3.76600   64.29400 1.000 36.71000 ? 226 ASN A O   1 
ATOM   1831 C  CB  . ASN A 1 226 ? 40.92300 6.52300   64.37700 1.000 39.22000 ? 226 ASN A CB  1 
ATOM   1832 C  CG  . ASN A 1 226 ? 41.28600 7.91500   63.89300 1.000 46.67000 ? 226 ASN A CG  1 
ATOM   1833 O  OD1 . ASN A 1 226 ? 42.10600 8.07500   62.98700 1.000 55.00000 ? 226 ASN A OD1 1 
ATOM   1834 N  ND2 . ASN A 1 226 ? 40.68800 8.93200   64.51000 1.000 45.05000 ? 226 ASN A ND2 1 
ATOM   1835 N  N   . THR A 1 227 ? 41.92300 3.27500   64.03700 1.000 39.86000 ? 227 THR A N   1 
ATOM   1836 C  CA  . THR A 1 227 ? 41.83300 1.88500   64.49300 1.000 38.84000 ? 227 THR A CA  1 
ATOM   1837 C  C   . THR A 1 227 ? 43.06400 1.51000   65.30300 1.000 31.51000 ? 227 THR A C   1 
ATOM   1838 O  O   . THR A 1 227 ? 44.17800 1.52700   64.77500 1.000 37.34000 ? 227 THR A O   1 
ATOM   1839 C  CB  . THR A 1 227 ? 41.71100 0.91800   63.32100 1.000 30.28000 ? 227 THR A CB  1 
ATOM   1840 O  OG1 . THR A 1 227 ? 40.58400 1.28500   62.52600 1.000 31.72000 ? 227 THR A OG1 1 
ATOM   1841 C  CG2 . THR A 1 227 ? 41.54600 -0.52700  63.83700 1.000 27.06000 ? 227 THR A CG2 1 
ATOM   1842 N  N   . MET A 1 228 ? 42.84200 1.11600   66.55100 1.000 31.48000 ? 228 MET A N   1 
ATOM   1843 C  CA  . MET A 1 228 ? 43.86100 0.59600   67.45400 1.000 32.60000 ? 228 MET A CA  1 
ATOM   1844 C  C   . MET A 1 228 ? 44.27600 -0.81900  67.06800 1.000 30.92000 ? 228 MET A C   1 
ATOM   1845 O  O   . MET A 1 228 ? 43.48900 -1.59700  66.53100 1.000 26.39000 ? 228 MET A O   1 
ATOM   1846 C  CB  . MET A 1 228 ? 43.31400 0.48300   68.87300 1.000 32.83000 ? 228 MET A CB  1 
ATOM   1847 C  CG  . MET A 1 228 ? 43.45100 1.64200   69.75500 1.000 40.85000 ? 228 MET A CG  1 
ATOM   1848 S  SD  . MET A 1 228 ? 43.12400 1.03700   71.41900 1.000 42.25000 ? 228 MET A SD  1 
ATOM   1849 C  CE  . MET A 1 228 ? 41.46500 0.37900   71.32700 1.000 30.22000 ? 228 MET A CE  1 
ATOM   1850 N  N   . LYS A 1 229 ? 45.49400 -1.18500  67.44200 1.000 29.34000 ? 229 LYS A N   1 
ATOM   1851 C  CA  . LYS A 1 229 ? 45.82800 -2.59700  67.44200 1.000 30.25000 ? 229 LYS A CA  1 
ATOM   1852 C  C   . LYS A 1 229 ? 44.94600 -3.31500  68.45800 1.000 29.38000 ? 229 LYS A C   1 
ATOM   1853 O  O   . LYS A 1 229 ? 44.63300 -2.77300  69.52400 1.000 25.18000 ? 229 LYS A O   1 
ATOM   1854 C  CB  . LYS A 1 229 ? 47.31000 -2.82800  67.75500 1.000 31.13000 ? 229 LYS A CB  1 
ATOM   1855 C  CG  . LYS A 1 229 ? 47.85600 -4.09000  67.05600 1.000 31.06000 ? 229 LYS A CG  1 
ATOM   1856 C  CD  . LYS A 1 229 ? 49.16300 -4.55500  67.66500 1.000 35.56000 ? 229 LYS A CD  1 
ATOM   1857 C  CE  . LYS A 1 229 ? 49.59800 -5.90400  67.11600 1.000 36.48000 ? 229 LYS A CE  1 
ATOM   1858 N  NZ  . LYS A 1 229 ? 51.05400 -6.13300  67.37300 1.000 46.42000 ? 229 LYS A NZ  1 
ATOM   1859 N  N   . PHE A 1 230 ? 44.50700 -4.52000  68.08000 1.000 25.41000 ? 230 PHE A N   1 
ATOM   1860 C  CA  . PHE A 1 230 ? 43.60200 -5.40000  68.81000 1.000 22.90000 ? 230 PHE A CA  1 
ATOM   1861 C  C   . PHE A 1 230 ? 42.15900 -4.91700  68.78300 1.000 26.05000 ? 230 PHE A C   1 
ATOM   1862 O  O   . PHE A 1 230 ? 41.32500 -5.44300  69.54300 1.000 27.78000 ? 230 PHE A O   1 
ATOM   1863 C  CB  . PHE A 1 230 ? 44.06000 -5.61200  70.25600 1.000 30.02000 ? 230 PHE A CB  1 
ATOM   1864 C  CG  . PHE A 1 230 ? 45.40900 -6.28000  70.36000 1.000 23.36000 ? 230 PHE A CG  1 
ATOM   1865 C  CD1 . PHE A 1 230 ? 45.58200 -7.58100  69.91400 1.000 24.91000 ? 230 PHE A CD1 1 
ATOM   1866 C  CD2 . PHE A 1 230 ? 46.49500 -5.60500  70.89100 1.000 28.56000 ? 230 PHE A CD2 1 
ATOM   1867 C  CE1 . PHE A 1 230 ? 46.81500 -8.19200  70.01200 1.000 25.31000 ? 230 PHE A CE1 1 
ATOM   1868 C  CE2 . PHE A 1 230 ? 47.72500 -6.21200  70.99700 1.000 27.80000 ? 230 PHE A CE2 1 
ATOM   1869 C  CZ  . PHE A 1 230 ? 47.89000 -7.50300  70.55100 1.000 26.82000 ? 230 PHE A CZ  1 
ATOM   1870 N  N   . HIS A 1 231 ? 41.83700 -3.95000  67.91400 1.000 25.25000 ? 231 HIS A N   1 
ATOM   1871 C  CA  . HIS A 1 231 ? 40.47300 -3.43400  67.78900 1.000 27.28000 ? 231 HIS A CA  1 
ATOM   1872 C  C   . HIS A 1 231 ? 39.44100 -4.56000  67.69300 1.000 24.31000 ? 231 HIS A C   1 
ATOM   1873 O  O   . HIS A 1 231 ? 38.52600 -4.65500  68.51600 1.000 27.82000 ? 231 HIS A O   1 
ATOM   1874 C  CB  . HIS A 1 231 ? 40.38100 -2.51900  66.56600 1.000 25.06000 ? 231 HIS A CB  1 
ATOM   1875 C  CG  . HIS A 1 231 ? 38.98400 -2.07900  66.23800 1.000 29.24000 ? 231 HIS A CG  1 
ATOM   1876 N  ND1 . HIS A 1 231 ? 38.46400 -0.87700  66.67300 1.000 28.78000 ? 231 HIS A ND1 1 
ATOM   1877 C  CD2 . HIS A 1 231 ? 38.00200 -2.67300  65.51000 1.000 27.48000 ? 231 HIS A CD2 1 
ATOM   1878 C  CE1 . HIS A 1 231 ? 37.22000 -0.75300  66.23600 1.000 28.94000 ? 231 HIS A CE1 1 
ATOM   1879 N  NE2 . HIS A 1 231 ? 36.91600 -1.82800  65.52700 1.000 27.74000 ? 231 HIS A NE2 1 
ATOM   1880 N  N   . HIS A 1 232 ? 39.57200 -5.43500  66.69900 1.000 25.47000 ? 232 HIS A N   1 
ATOM   1881 C  CA  . HIS A 1 232 ? 38.51300 -6.42400  66.48600 1.000 23.65000 ? 232 HIS A CA  1 
ATOM   1882 C  C   . HIS A 1 232 ? 38.47900 -7.44800  67.61800 1.000 28.50000 ? 232 HIS A C   1 
ATOM   1883 O  O   . HIS A 1 232 ? 37.39500 -7.83900  68.07400 1.000 27.33000 ? 232 HIS A O   1 
ATOM   1884 C  CB  . HIS A 1 232 ? 38.67800 -7.08700  65.12100 1.000 25.06000 ? 232 HIS A CB  1 
ATOM   1885 C  CG  . HIS A 1 232 ? 38.38900 -6.15700  63.98000 1.000 28.94000 ? 232 HIS A CG  1 
ATOM   1886 N  ND1 . HIS A 1 232 ? 39.38300 -5.49400  63.29000 1.000 25.88000 ? 232 HIS A ND1 1 
ATOM   1887 C  CD2 . HIS A 1 232 ? 37.21600 -5.76700  63.41700 1.000 26.14000 ? 232 HIS A CD2 1 
ATOM   1888 C  CE1 . HIS A 1 232 ? 38.83700 -4.74200  62.34700 1.000 28.61000 ? 232 HIS A CE1 1 
ATOM   1889 N  NE2 . HIS A 1 232 ? 37.52300 -4.88400  62.40800 1.000 25.02000 ? 232 HIS A NE2 1 
ATOM   1890 N  N   . MET A 1 233 ? 39.64900 -7.85300  68.13100 1.000 25.65000 ? 233 MET A N   1 
ATOM   1891 C  CA  . MET A 1 233 ? 39.66400 -8.74200  69.29000 1.000 29.75000 ? 233 MET A CA  1 
ATOM   1892 C  C   . MET A 1 233 ? 38.95400 -8.10500  70.48700 1.000 26.03000 ? 233 MET A C   1 
ATOM   1893 O  O   . MET A 1 233 ? 38.12200 -8.74500  71.14500 1.000 22.67000 ? 233 MET A O   1 
ATOM   1894 C  CB  . MET A 1 233 ? 41.10000 -9.12200  69.65700 1.000 25.81000 ? 233 MET A CB  1 
ATOM   1895 C  CG  . MET A 1 233 ? 41.15300 -10.21400 70.69100 1.000 22.70000 ? 233 MET A CG  1 
ATOM   1896 S  SD  . MET A 1 233 ? 42.77900 -10.32800 71.45100 1.000 26.94000 ? 233 MET A SD  1 
ATOM   1897 C  CE  . MET A 1 233 ? 42.72200 -9.01600  72.65100 1.000 19.50000 ? 233 MET A CE  1 
ATOM   1898 N  N   . LEU A 1 234 ? 39.24000 -6.83100  70.75700 1.000 24.34000 ? 234 LEU A N   1 
ATOM   1899 C  CA  . LEU A 1 234 ? 38.57200 -6.15500  71.86900 1.000 25.23000 ? 234 LEU A CA  1 
ATOM   1900 C  C   . LEU A 1 234 ? 37.06900 -6.02500  71.65000 1.000 26.06000 ? 234 LEU A C   1 
ATOM   1901 O  O   . LEU A 1 234 ? 36.30700 -5.97400  72.62400 1.000 27.50000 ? 234 LEU A O   1 
ATOM   1902 C  CB  . LEU A 1 234 ? 39.17700 -4.77700  72.07900 1.000 21.82000 ? 234 LEU A CB  1 
ATOM   1903 C  CG  . LEU A 1 234 ? 40.60800 -4.77400  72.62600 1.000 29.47000 ? 234 LEU A CG  1 
ATOM   1904 C  CD1 . LEU A 1 234 ? 41.18300 -3.36300  72.62800 1.000 24.51000 ? 234 LEU A CD1 1 
ATOM   1905 C  CD2 . LEU A 1 234 ? 40.66400 -5.39600  74.03600 1.000 27.14000 ? 234 LEU A CD2 1 
ATOM   1906 N  N   . LYS A 1 235 ? 36.62200 -5.93700  70.39400 1.000 26.19000 ? 235 LYS A N   1 
ATOM   1907 C  CA  . LYS A 1 235 ? 35.19400 -5.80100  70.10200 1.000 27.22000 ? 235 LYS A CA  1 
ATOM   1908 C  C   . LYS A 1 235 ? 34.41400 -7.06800  70.40400 1.000 29.40000 ? 235 LYS A C   1 
ATOM   1909 O  O   . LYS A 1 235 ? 33.18600 -7.05600  70.30600 1.000 32.92000 ? 235 LYS A O   1 
ATOM   1910 C  CB  . LYS A 1 235 ? 34.98600 -5.38400  68.63700 1.000 29.22000 ? 235 LYS A CB  1 
ATOM   1911 C  CG  . LYS A 1 235 ? 35.44900 -3.94000  68.32000 1.000 29.72000 ? 235 LYS A CG  1 
ATOM   1912 C  CD  . LYS A 1 235 ? 34.57500 -2.91900  69.01600 1.000 27.01000 ? 235 LYS A CD  1 
ATOM   1913 C  CE  . LYS A 1 235 ? 34.41700 -1.66100  68.20500 1.000 36.21000 ? 235 LYS A CE  1 
ATOM   1914 N  NZ  . LYS A 1 235 ? 33.49000 -0.70800  68.88500 1.000 34.43000 ? 235 LYS A NZ  1 
ATOM   1915 N  N   . MET A 1 236 ? 35.08000 -8.15700  70.78900 1.000 29.85000 ? 236 MET A N   1 
ATOM   1916 C  CA  . MET A 1 236 ? 34.35900 -9.30500  71.33500 1.000 29.09000 ? 236 MET A CA  1 
ATOM   1917 C  C   . MET A 1 236 ? 33.89700 -9.09500  72.77300 1.000 31.60000 ? 236 MET A C   1 
ATOM   1918 O  O   . MET A 1 236 ? 33.02200 -9.82500  73.24100 1.000 32.09000 ? 236 MET A O   1 
ATOM   1919 C  CB  . MET A 1 236 ? 35.23300 -10.55000 71.26200 1.000 29.21000 ? 236 MET A CB  1 
ATOM   1920 C  CG  . MET A 1 236 ? 35.37600 -11.04000 69.84900 1.000 36.10000 ? 236 MET A CG  1 
ATOM   1921 S  SD  . MET A 1 236 ? 36.12900 -12.64100 69.82100 1.000 40.87000 ? 236 MET A SD  1 
ATOM   1922 C  CE  . MET A 1 236 ? 37.71100 -12.35000 70.61600 1.000 35.20000 ? 236 MET A CE  1 
ATOM   1923 N  N   . THR A 1 237 ? 34.46300 -8.13500  73.47900 1.000 28.32000 ? 237 THR A N   1 
ATOM   1924 C  CA  . THR A 1 237 ? 34.12800 -7.87700  74.86800 1.000 32.33000 ? 237 THR A CA  1 
ATOM   1925 C  C   . THR A 1 237 ? 33.58600 -6.47800  75.08800 1.000 32.81000 ? 237 THR A C   1 
ATOM   1926 O  O   . THR A 1 237 ? 32.69500 -6.28100  75.90900 1.000 31.91000 ? 237 THR A O   1 
ATOM   1927 C  CB  . THR A 1 237 ? 35.37900 -8.08400  75.73400 1.000 31.38000 ? 237 THR A CB  1 
ATOM   1928 O  OG1 . THR A 1 237 ? 35.79100 -9.46000  75.65400 1.000 32.79000 ? 237 THR A OG1 1 
ATOM   1929 C  CG2 . THR A 1 237 ? 35.10300 -7.70200  77.17800 1.000 30.10000 ? 237 THR A CG2 1 
ATOM   1930 N  N   . TYR A 1 238 ? 34.09500 -5.50800  74.34800 1.000 27.98000 ? 238 TYR A N   1 
ATOM   1931 C  CA  . TYR A 1 238 ? 33.76600 -4.11100  74.52800 1.000 31.91000 ? 238 TYR A CA  1 
ATOM   1932 C  C   . TYR A 1 238 ? 33.03300 -3.59100  73.30000 1.000 31.00000 ? 238 TYR A C   1 
ATOM   1933 O  O   . TYR A 1 238 ? 33.10400 -4.17300  72.21100 1.000 31.59000 ? 238 TYR A O   1 
ATOM   1934 C  CB  . TYR A 1 238 ? 35.03000 -3.29400  74.74900 1.000 26.16000 ? 238 TYR A CB  1 
ATOM   1935 C  CG  . TYR A 1 238 ? 35.84400 -3.67600  75.95800 1.000 27.79000 ? 238 TYR A CG  1 
ATOM   1936 C  CD1 . TYR A 1 238 ? 35.39200 -3.42100  77.24800 1.000 33.97000 ? 238 TYR A CD1 1 
ATOM   1937 C  CD2 . TYR A 1 238 ? 37.09600 -4.25900  75.81100 1.000 33.15000 ? 238 TYR A CD2 1 
ATOM   1938 C  CE1 . TYR A 1 238 ? 36.17900 -3.75200  78.36400 1.000 33.04000 ? 238 TYR A CE1 1 
ATOM   1939 C  CE2 . TYR A 1 238 ? 37.87900 -4.58900  76.90700 1.000 28.72000 ? 238 TYR A CE2 1 
ATOM   1940 C  CZ  . TYR A 1 238 ? 37.42100 -4.33300  78.17100 1.000 30.21000 ? 238 TYR A CZ  1 
ATOM   1941 O  OH  . TYR A 1 238 ? 38.22300 -4.66800  79.23300 1.000 39.17000 ? 238 TYR A OH  1 
ATOM   1942 N  N   . SER A 1 239 ? 32.34800 -2.46200  73.46900 1.000 30.46000 ? 239 SER A N   1 
ATOM   1943 C  CA  . SER A 1 239 ? 31.69800 -1.82800  72.33400 1.000 37.56000 ? 239 SER A CA  1 
ATOM   1944 C  C   . SER A 1 239 ? 32.23200 -0.41000  72.23100 1.000 33.24000 ? 239 SER A C   1 
ATOM   1945 O  O   . SER A 1 239 ? 33.30600 -0.19000  71.64500 1.000 33.89000 ? 239 SER A O   1 
ATOM   1946 C  CB  . SER A 1 239 ? 30.16900 -1.91400  72.46200 1.000 36.17000 ? 239 SER A CB  1 
ATOM   1947 O  OG  . SER A 1 239 ? 29.75200 -1.53700  73.76200 1.000 36.34000 ? 239 SER A OG  1 
ATOM   1948 N  N   . ASN A 1 240 ? 31.53300 0.58100   72.78500 1.000 36.44000 ? 240 ASN A N   1 
ATOM   1949 C  CA  . ASN A 1 240 ? 31.91900 1.97200   72.58400 1.000 39.64000 ? 240 ASN A CA  1 
ATOM   1950 C  C   . ASN A 1 240 ? 33.23800 2.32000   73.25900 1.000 33.97000 ? 240 ASN A C   1 
ATOM   1951 O  O   . ASN A 1 240 ? 33.89000 3.28100   72.83900 1.000 32.40000 ? 240 ASN A O   1 
ATOM   1952 C  CB  . ASN A 1 240 ? 30.80400 2.89500   73.08000 1.000 33.99000 ? 240 ASN A CB  1 
ATOM   1953 C  CG  . ASN A 1 240 ? 29.49100 2.66500   72.33600 1.000 39.15000 ? 240 ASN A CG  1 
ATOM   1954 O  OD1 . ASN A 1 240 ? 28.87300 1.59700   72.45300 1.000 36.75000 ? 240 ASN A OD1 1 
ATOM   1955 N  ND2 . ASN A 1 240 ? 29.06500 3.66100   71.55700 1.000 34.04000 ? 240 ASN A ND2 1 
ATOM   1956 N  N   . GLU A 1 241 ? 33.65100 1.56000   74.27700 1.000 35.75000 ? 241 GLU A N   1 
ATOM   1957 C  CA  . GLU A 1 241 ? 34.94500 1.80300   74.91700 1.000 34.01000 ? 241 GLU A CA  1 
ATOM   1958 C  C   . GLU A 1 241 ? 36.08200 1.81300   73.89900 1.000 35.40000 ? 241 GLU A C   1 
ATOM   1959 O  O   . GLU A 1 241 ? 37.03000 2.60300   74.01200 1.000 32.57000 ? 241 GLU A O   1 
ATOM   1960 C  CB  . GLU A 1 241 ? 35.20400 0.74200   75.99300 1.000 31.32000 ? 241 GLU A CB  1 
ATOM   1961 C  CG  . GLU A 1 241 ? 34.16200 0.69500   77.12000 1.000 32.73000 ? 241 GLU A CG  1 
ATOM   1962 C  CD  . GLU A 1 241 ? 33.08800 -0.37700  76.91200 1.000 40.02000 ? 241 GLU A CD  1 
ATOM   1963 O  OE1 . GLU A 1 241 ? 32.69800 -0.64500  75.74400 1.000 40.70000 ? 241 GLU A OE1 1 
ATOM   1964 O  OE2 . GLU A 1 241 ? 32.62300 -0.94300  77.93100 1.000 48.44000 ? 241 GLU A OE2 1 
ATOM   1965 N  N   . VAL A 1 242 ? 36.01200 0.93000   72.90400 1.000 29.06000 ? 242 VAL A N   1 
ATOM   1966 C  CA  . VAL A 1 242 ? 37.09300 0.83100   71.93600 1.000 32.51000 ? 242 VAL A CA  1 
ATOM   1967 C  C   . VAL A 1 242 ? 37.13200 2.07500   71.06500 1.000 35.80000 ? 242 VAL A C   1 
ATOM   1968 O  O   . VAL A 1 242 ? 38.20800 2.61200   70.76800 1.000 32.05000 ? 242 VAL A O   1 
ATOM   1969 C  CB  . VAL A 1 242 ? 36.94200 -0.45400  71.09600 1.000 33.44000 ? 242 VAL A CB  1 
ATOM   1970 C  CG1 . VAL A 1 242 ? 38.03500 -0.53000  70.04600 1.000 32.88000 ? 242 VAL A CG1 1 
ATOM   1971 C  CG2 . VAL A 1 242 ? 36.96900 -1.69900  71.98800 1.000 24.15000 ? 242 VAL A CG2 1 
ATOM   1972 N  N   . ASP A 1 243 ? 35.95800 2.56600   70.66800 1.000 36.55000 ? 243 ASP A N   1 
ATOM   1973 C  CA  . ASP A 1 243 ? 35.88000 3.74000   69.80400 1.000 40.80000 ? 243 ASP A CA  1 
ATOM   1974 C  C   . ASP A 1 243 ? 36.32400 4.99400   70.54400 1.000 33.31000 ? 243 ASP A C   1 
ATOM   1975 O  O   . ASP A 1 243 ? 36.96800 5.87500   69.95700 1.000 35.45000 ? 243 ASP A O   1 
ATOM   1976 C  CB  . ASP A 1 243 ? 34.45400 3.90300   69.27700 1.000 38.16000 ? 243 ASP A CB  1 
ATOM   1977 C  CG  . ASP A 1 243 ? 33.90000 2.61000   68.69200 1.000 46.98000 ? 243 ASP A CG  1 
ATOM   1978 O  OD1 . ASP A 1 243 ? 34.56300 2.02200   67.79700 1.000 45.47000 ? 243 ASP A OD1 1 
ATOM   1979 O  OD2 . ASP A 1 243 ? 32.80300 2.18300   69.13500 1.000 47.16000 ? 243 ASP A OD2 1 
ATOM   1980 N  N   . ILE A 1 244 ? 36.01200 5.07700   71.83700 1.000 31.38000 ? 244 ILE A N   1 
ATOM   1981 C  CA  . ILE A 1 244 ? 36.45200 6.21700   72.63100 1.000 36.95000 ? 244 ILE A CA  1 
ATOM   1982 C  C   . ILE A 1 244 ? 37.97500 6.29200   72.64200 1.000 41.51000 ? 244 ILE A C   1 
ATOM   1983 O  O   . ILE A 1 244 ? 38.57000 7.31400   72.26600 1.000 33.29000 ? 244 ILE A O   1 
ATOM   1984 C  CB  . ILE A 1 244 ? 35.86700 6.13000   74.05000 1.000 33.15000 ? 244 ILE A CB  1 
ATOM   1985 C  CG1 . ILE A 1 244 ? 34.35100 6.32400   73.99800 1.000 33.52000 ? 244 ILE A CG1 1 
ATOM   1986 C  CG2 . ILE A 1 244 ? 36.50300 7.17100   74.94200 1.000 33.50000 ? 244 ILE A CG2 1 
ATOM   1987 C  CD1 . ILE A 1 244 ? 33.62300 5.89800   75.26800 1.000 36.21000 ? 244 ILE A CD1 1 
ATOM   1988 N  N   . GLU A 1 245 ? 38.62700 5.18400   73.02600 1.000 30.90000 ? 245 GLU A N   1 
ATOM   1989 C  CA  . GLU A 1 245 ? 40.08300 5.14200   73.04100 1.000 30.04000 ? 245 GLU A CA  1 
ATOM   1990 C  C   . GLU A 1 245 ? 40.65800 5.49600   71.68000 1.000 35.27000 ? 245 GLU A C   1 
ATOM   1991 O  O   . GLU A 1 245 ? 41.72200 6.11800   71.59000 1.000 35.54000 ? 245 GLU A O   1 
ATOM   1992 C  CB  . GLU A 1 245 ? 40.56500 3.76000   73.47800 1.000 32.35000 ? 245 GLU A CB  1 
ATOM   1993 C  CG  . GLU A 1 245 ? 42.08300 3.61200   73.45400 1.000 34.84000 ? 245 GLU A CG  1 
ATOM   1994 C  CD  . GLU A 1 245 ? 42.78600 4.52700   74.45500 1.000 41.77000 ? 245 GLU A CD  1 
ATOM   1995 O  OE1 . GLU A 1 245 ? 42.20100 4.79300   75.53100 1.000 44.73000 ? 245 GLU A OE1 1 
ATOM   1996 O  OE2 . GLU A 1 245 ? 43.92400 4.96800   74.16500 1.000 38.62000 ? 245 GLU A OE2 1 
ATOM   1997 N  N   . GLU A 1 246 ? 39.96900 5.12200   70.60400 1.000 32.44000 ? 246 GLU A N   1 
ATOM   1998 C  CA  . GLU A 1 246 ? 40.52100 5.39400   69.28500 1.000 36.78000 ? 246 GLU A CA  1 
ATOM   1999 C  C   . GLU A 1 246 ? 40.36800 6.85000   68.88500 1.000 35.18000 ? 246 GLU A C   1 
ATOM   2000 O  O   . GLU A 1 246 ? 40.99200 7.27400   67.91100 1.000 34.10000 ? 246 GLU A O   1 
ATOM   2001 C  CB  . GLU A 1 246 ? 39.88400 4.46500   68.24800 1.000 32.66000 ? 246 GLU A CB  1 
ATOM   2002 C  CG  . GLU A 1 246 ? 40.30100 3.01100   68.48500 1.000 38.99000 ? 246 GLU A CG  1 
ATOM   2003 C  CD  . GLU A 1 246 ? 39.60000 2.01400   67.57500 1.000 37.97000 ? 246 GLU A CD  1 
ATOM   2004 O  OE1 . GLU A 1 246 ? 38.43300 2.26400   67.19600 1.000 40.46000 ? 246 GLU A OE1 1 
ATOM   2005 O  OE2 . GLU A 1 246 ? 40.22200 0.97500   67.25600 1.000 33.94000 ? 246 GLU A OE2 1 
ATOM   2006 N  N   . GLY A 1 247 ? 39.59100 7.63000   69.62900 1.000 39.23000 ? 247 GLY A N   1 
ATOM   2007 C  CA  . GLY A 1 247 ? 39.58300 9.06400   69.41800 1.000 43.53000 ? 247 GLY A CA  1 
ATOM   2008 C  C   . GLY A 1 247 ? 40.70000 9.84300   70.09700 1.000 41.93000 ? 247 GLY A C   1 
ATOM   2009 O  O   . GLY A 1 247 ? 40.88200 11.02400  69.78100 1.000 40.53000 ? 247 GLY A O   1 
ATOM   2010 N  N   . LYS A 1 248 ? 41.44100 9.22000   71.01400 1.000 39.98000 ? 248 LYS A N   1 
ATOM   2011 C  CA  . LYS A 1 248 ? 42.52000 9.88600   71.74000 1.000 40.73000 ? 248 LYS A CA  1 
ATOM   2012 C  C   . LYS A 1 248 ? 43.74600 10.09300  70.81900 1.000 48.11000 ? 248 LYS A C   1 
ATOM   2013 O  O   . LYS A 1 248 ? 43.77500 9.62900   69.66700 1.000 41.65000 ? 248 LYS A O   1 
ATOM   2014 C  CB  . LYS A 1 248 ? 42.84200 9.09100   73.00900 1.000 38.39000 ? 248 LYS A CB  1 
ATOM   2015 C  CG  . LYS A 1 248 ? 41.67500 9.06100   74.04400 1.000 36.20000 ? 248 LYS A CG  1 
ATOM   2016 C  CD  . LYS A 1 248 ? 42.02700 8.35800   75.37200 1.000 48.60000 ? 248 LYS A CD  1 
ATOM   2017 C  CE  . LYS A 1 248 ? 43.22600 9.03200   76.07400 1.000 54.83000 ? 248 LYS A CE  1 
ATOM   2018 N  NZ  . LYS A 1 248 ? 43.75700 8.28600   77.28200 1.000 54.69000 ? 248 LYS A NZ  1 
ATOM   2019 N  N   . VAL A 1 249 ? 44.75200 10.83600  71.32500 1.000 43.15000 ? 249 VAL A N   1 
ATOM   2020 C  CA  . VAL A 1 249 ? 45.84900 11.31700  70.46900 1.000 46.27000 ? 249 VAL A CA  1 
ATOM   2021 C  C   . VAL A 1 249 ? 46.67900 10.15100  69.94300 1.000 45.87000 ? 249 VAL A C   1 
ATOM   2022 O  O   . VAL A 1 249 ? 46.90100 10.01300  68.73200 1.000 53.42000 ? 249 VAL A O   1 
ATOM   2023 C  CB  . VAL A 1 249 ? 46.75600 12.32200  71.20900 1.000 42.40000 ? 249 VAL A CB  1 
ATOM   2024 C  CG1 . VAL A 1 249 ? 48.02700 12.57600  70.39500 1.000 41.45000 ? 249 VAL A CG1 1 
ATOM   2025 C  CG2 . VAL A 1 249 ? 46.06100 13.63600  71.44400 1.000 42.74000 ? 249 VAL A CG2 1 
ATOM   2026 N  N   . ASN A 1 250 ? 47.19700 9.32500   70.85300 1.000 48.31000 ? 250 ASN A N   1 
ATOM   2027 C  CA  . ASN A 1 250 ? 47.90000 8.09300   70.49800 1.000 52.61000 ? 250 ASN A CA  1 
ATOM   2028 C  C   . ASN A 1 250 ? 47.13100 6.95100   71.14700 1.000 49.44000 ? 250 ASN A C   1 
ATOM   2029 O  O   . ASN A 1 250 ? 47.44500 6.55300   72.27900 1.000 43.47000 ? 250 ASN A O   1 
ATOM   2030 C  CB  . ASN A 1 250 ? 49.36400 8.09800   70.96200 1.000 58.20000 ? 250 ASN A CB  1 
ATOM   2031 C  CG  . ASN A 1 250 ? 50.20900 7.03200   70.23300 1.000 64.37000 ? 250 ASN A CG  1 
ATOM   2032 O  OD1 . ASN A 1 250 ? 49.71000 6.33900   69.33900 1.000 65.98000 ? 250 ASN A OD1 1 
ATOM   2033 N  ND2 . ASN A 1 250 ? 51.50000 6.94500   70.57400 1.000 67.92000 ? 250 ASN A ND2 1 
ATOM   2034 N  N   . PRO A 1 251 ? 46.14900 6.37500   70.45200 1.000 43.95000 ? 251 PRO A N   1 
ATOM   2035 C  CA  . PRO A 1 251 ? 45.31000 5.32300   71.05300 1.000 45.49000 ? 251 PRO A CA  1 
ATOM   2036 C  C   . PRO A 1 251 ? 46.13800 4.08400   71.36500 1.000 38.49000 ? 251 PRO A C   1 
ATOM   2037 O  O   . PRO A 1 251 ? 46.97600 3.65900   70.56300 1.000 41.85000 ? 251 PRO A O   1 
ATOM   2038 C  CB  . PRO A 1 251 ? 44.25200 5.04900   69.97000 1.000 40.83000 ? 251 PRO A CB  1 
ATOM   2039 C  CG  . PRO A 1 251 ? 44.44900 6.12100   68.89500 1.000 42.67000 ? 251 PRO A CG  1 
ATOM   2040 C  CD  . PRO A 1 251 ? 45.87500 6.55400   69.01800 1.000 40.78000 ? 251 PRO A CD  1 
ATOM   2041 N  N   . SER A 1 252 ? 45.89800 3.53300   72.54100 1.000 35.26000 ? 252 SER A N   1 
ATOM   2042 C  CA  . SER A 1 252 ? 46.59000 2.31500   72.99600 1.000 38.03000 ? 252 SER A CA  1 
ATOM   2043 C  C   . SER A 1 252 ? 45.57300 1.32300   73.55200 1.000 33.81000 ? 252 SER A C   1 
ATOM   2044 O  O   . SER A 1 252 ? 44.75200 1.71000   74.33400 1.000 30.23000 ? 252 SER A O   1 
ATOM   2045 C  CB  . SER A 1 252 ? 47.62400 2.63000   74.00600 1.000 36.77000 ? 252 SER A CB  1 
ATOM   2046 O  OG  . SER A 1 252 ? 48.14300 1.46600   74.58500 1.000 37.05000 ? 252 SER A OG  1 
ATOM   2047 N  N   . PRO A 1 253 ? 45.67300 0.03000   73.21200 1.000 31.05000 ? 253 PRO A N   1 
ATOM   2048 C  CA  . PRO A 1 253 ? 44.77900 -0.98700  73.73900 1.000 38.54000 ? 253 PRO A CA  1 
ATOM   2049 C  C   . PRO A 1 253 ? 45.13400 -1.48300  75.14500 1.000 34.54000 ? 253 PRO A C   1 
ATOM   2050 O  O   . PRO A 1 253 ? 44.40800 -2.21300  75.66200 1.000 30.43000 ? 253 PRO A O   1 
ATOM   2051 C  CB  . PRO A 1 253 ? 44.98900 -2.14300  72.76600 1.000 30.14000 ? 253 PRO A CB  1 
ATOM   2052 C  CG  . PRO A 1 253 ? 46.40000 -2.01300  72.37200 1.000 36.43000 ? 253 PRO A CG  1 
ATOM   2053 C  CD  . PRO A 1 253 ? 46.63700 -0.52600  72.30300 1.000 36.08000 ? 253 PRO A CD  1 
ATOM   2054 N  N   . GLU A 1 254 ? 46.22600 -0.98400  75.70400 1.000 32.35000 ? 254 GLU A N   1 
ATOM   2055 C  CA  . GLU A 1 254 ? 46.79900 -1.39600  77.00300 1.000 35.73000 ? 254 GLU A CA  1 
ATOM   2056 C  C   . GLU A 1 254 ? 45.77100 -1.47400  78.13800 1.000 35.45000 ? 254 GLU A C   1 
ATOM   2057 O  O   . GLU A 1 254 ? 45.68000 -2.51200  78.72900 1.000 35.34000 ? 254 GLU A O   1 
ATOM   2058 C  CB  . GLU A 1 254 ? 47.99700 -0.51900  77.34600 1.000 36.82000 ? 254 GLU A CB  1 
ATOM   2059 C  CG  . GLU A 1 254 ? 48.93000 -1.15700  78.34200 1.000 45.09000 ? 254 GLU A CG  1 
ATOM   2060 C  CD  . GLU A 1 254 ? 50.10800 -0.32800  78.81500 1.000 53.43000 ? 254 GLU A CD  1 
ATOM   2061 O  OE1 . GLU A 1 254 ? 50.70400 0.38300   78.00800 1.000 50.84000 ? 254 GLU A OE1 1 
ATOM   2062 O  OE2 . GLU A 1 254 ? 50.40600 -0.41000  79.98000 1.000 47.51000 ? 254 GLU A OE2 1 
ATOM   2063 N  N   . LYS A 1 255 ? 44.99500 -0.42900  78.38000 1.000 33.95000 ? 255 LYS A N   1 
ATOM   2064 C  CA  . LYS A 1 255 ? 44.13400 -0.45600  79.55700 1.000 32.28000 ? 255 LYS A CA  1 
ATOM   2065 C  C   . LYS A 1 255 ? 42.99400 -1.45800  79.39200 1.000 34.55000 ? 255 LYS A C   1 
ATOM   2066 O  O   . LYS A 1 255 ? 42.65800 -2.18600  80.33400 1.000 33.40000 ? 255 LYS A O   1 
ATOM   2067 C  CB  . LYS A 1 255 ? 43.58400 0.94000   79.85500 1.000 41.67000 ? 255 LYS A CB  1 
ATOM   2068 C  CG  . LYS A 1 255 ? 44.56200 1.84400   80.62000 1.000 52.65000 ? 255 LYS A CG  1 
ATOM   2069 C  CD  . LYS A 1 255 ? 44.03000 3.28100   80.75500 1.000 53.24000 ? 255 LYS A CD  1 
ATOM   2070 C  CE  . LYS A 1 255 ? 44.43400 4.17200   79.56400 1.000 55.95000 ? 255 LYS A CE  1 
ATOM   2071 N  NZ  . LYS A 1 255 ? 43.46500 4.20100   78.43000 1.000 50.71000 ? 255 LYS A NZ  1 
ATOM   2072 N  N   . LEU A 1 256 ? 42.38800 -1.51000  78.20400 1.000 31.85000 ? 256 LEU A N   1 
ATOM   2073 C  CA  . LEU A 1 256 ? 41.29600 -2.45100  77.96300 1.000 35.14000 ? 256 LEU A CA  1 
ATOM   2074 C  C   . LEU A 1 256 ? 41.80000 -3.89200  77.93000 1.000 29.70000 ? 256 LEU A C   1 
ATOM   2075 O  O   . LEU A 1 256 ? 41.10700 -4.81000  78.38400 1.000 28.26000 ? 256 LEU A O   1 
ATOM   2076 C  CB  . LEU A 1 256 ? 40.59200 -2.09000  76.65100 1.000 33.10000 ? 256 LEU A CB  1 
ATOM   2077 C  CG  . LEU A 1 256 ? 39.76100 -0.80300  76.64400 1.000 36.50000 ? 256 LEU A CG  1 
ATOM   2078 C  CD1 . LEU A 1 256 ? 39.29300 -0.51500  75.22500 1.000 34.45000 ? 256 LEU A CD1 1 
ATOM   2079 C  CD2 . LEU A 1 256 ? 38.56100 -0.93500  77.57400 1.000 30.50000 ? 256 LEU A CD2 1 
ATOM   2080 N  N   . LEU A 1 257 ? 43.00800 -4.08900  77.44100 1.000 28.19000 ? 257 LEU A N   1 
ATOM   2081 C  CA  . LEU A 1 257 ? 43.63900 -5.42100  77.48300 1.000 29.98000 ? 257 LEU A CA  1 
ATOM   2082 C  C   . LEU A 1 257 ? 43.80800 -5.82900  78.94900 1.000 32.16000 ? 257 LEU A C   1 
ATOM   2083 O  O   . LEU A 1 257 ? 43.36700 -6.87900  79.31300 1.000 26.83000 ? 257 LEU A O   1 
ATOM   2084 C  CB  . LEU A 1 257 ? 44.97300 -5.36400  76.74500 1.000 27.77000 ? 257 LEU A CB  1 
ATOM   2085 C  CG  . LEU A 1 257 ? 44.84700 -5.39700  75.23400 1.000 26.43000 ? 257 LEU A CG  1 
ATOM   2086 C  CD1 . LEU A 1 257 ? 46.18800 -5.34400  74.56700 1.000 29.78000 ? 257 LEU A CD1 1 
ATOM   2087 C  CD2 . LEU A 1 257 ? 44.06900 -6.60600  74.78100 1.000 29.32000 ? 257 LEU A CD2 1 
ATOM   2088 N  N   . THR A 1 258 ? 44.37600 -4.94000  79.75500 1.000 35.17000 ? 258 THR A N   1 
ATOM   2089 C  CA  . THR A 1 258 ? 44.64500 -5.20900  81.18700 1.000 32.04000 ? 258 THR A CA  1 
ATOM   2090 C  C   . THR A 1 258 ? 43.34600 -5.53600  81.91900 1.000 31.36000 ? 258 THR A C   1 
ATOM   2091 O  O   . THR A 1 258 ? 43.35200 -6.43600  82.68600 1.000 31.98000 ? 258 THR A O   1 
ATOM   2092 C  CB  . THR A 1 258 ? 45.42400 -4.05700  81.83500 1.000 32.65000 ? 258 THR A CB  1 
ATOM   2093 O  OG1 . THR A 1 258 ? 46.58700 -3.77600  81.07100 1.000 33.27000 ? 258 THR A OG1 1 
ATOM   2094 C  CG2 . THR A 1 258 ? 45.77700 -4.32800  83.27500 1.000 26.00000 ? 258 THR A CG2 1 
ATOM   2095 N  N   . SER A 1 259 ? 42.27500 -4.82400  81.62100 1.000 30.35000 ? 259 SER A N   1 
ATOM   2096 C  CA  . SER A 1 259 ? 40.94900 -5.01800  82.25400 1.000 36.45000 ? 259 SER A CA  1 
ATOM   2097 C  C   . SER A 1 259 ? 40.39000 -6.42700  82.05700 1.000 31.26000 ? 259 SER A C   1 
ATOM   2098 O  O   . SER A 1 259 ? 39.70000 -6.89000  82.91700 1.000 30.38000 ? 259 SER A O   1 
ATOM   2099 C  CB  . SER A 1 259 ? 39.99300 -4.02300  81.72300 1.000 35.66000 ? 259 SER A CB  1 
ATOM   2100 O  OG  . SER A 1 259 ? 40.38900 -2.74000  82.09700 1.000 52.08000 ? 259 SER A OG  1 
ATOM   2101 N  N   . LEU A 1 260 ? 40.67200 -7.02800  80.91900 1.000 30.49000 ? 260 LEU A N   1 
ATOM   2102 C  CA  . LEU A 1 260 ? 40.18000 -8.38700  80.60500 1.000 29.73000 ? 260 LEU A CA  1 
ATOM   2103 C  C   . LEU A 1 260 ? 40.70600 -9.38400  81.62600 1.000 32.43000 ? 260 LEU A C   1 
ATOM   2104 O  O   . LEU A 1 260 ? 39.94200 -10.17000 82.09100 1.000 37.83000 ? 260 LEU A O   1 
ATOM   2105 C  CB  . LEU A 1 260 ? 40.59900 -8.76000  79.19000 1.000 28.57000 ? 260 LEU A CB  1 
ATOM   2106 C  CG  . LEU A 1 260 ? 39.93600 -7.93800  78.09700 1.000 27.12000 ? 260 LEU A CG  1 
ATOM   2107 C  CD1 . LEU A 1 260 ? 40.34700 -8.41800  76.72800 1.000 24.86000 ? 260 LEU A CD1 1 
ATOM   2108 C  CD2 . LEU A 1 260 ? 38.43800 -8.00900  78.23600 1.000 32.77000 ? 260 LEU A CD2 1 
ATOM   2109 N  N   . ILE A 1 261 ? 41.97000 -9.29100  81.96200 1.000 30.88000 ? 261 ILE A N   1 
ATOM   2110 C  CA  . ILE A 1 261 ? 42.59400 -10.17000 82.97500 1.000 36.30000 ? 261 ILE A CA  1 
ATOM   2111 C  C   . ILE A 1 261 ? 42.91300 -9.21300  84.11600 1.000 48.67000 ? 261 ILE A C   1 
ATOM   2112 O  O   . ILE A 1 261 ? 44.04400 -9.16900  84.53400 1.000 44.95000 ? 261 ILE A O   1 
ATOM   2113 C  CB  . ILE A 1 261 ? 43.88600 -10.75700 82.40900 1.000 39.15000 ? 261 ILE A CB  1 
ATOM   2114 C  CG1 . ILE A 1 261 ? 44.82300 -9.65200  81.91400 1.000 41.10000 ? 261 ILE A CG1 1 
ATOM   2115 C  CG2 . ILE A 1 261 ? 43.56400 -11.76100 81.33100 1.000 37.88000 ? 261 ILE A CG2 1 
ATOM   2116 C  CD1 . ILE A 1 261 ? 45.86200 -10.10600 80.94200 1.000 39.22000 ? 261 ILE A CD1 1 
ATOM   2117 N  N   . GLY A 1 262 ? 41.89100 -8.50700  84.58700 1.000 48.53000 ? 262 GLY A N   1 
ATOM   2118 C  CA  . GLY A 1 262 ? 42.03400 -7.52800  85.67700 1.000 56.18000 ? 262 GLY A CA  1 
ATOM   2119 C  C   . GLY A 1 262 ? 42.60500 -8.12300  86.94400 1.000 53.92000 ? 262 GLY A C   1 
ATOM   2120 O  O   . GLY A 1 262 ? 43.72000 -7.78900  87.31600 1.000 59.81000 ? 262 GLY A O   1 
ATOM   2121 N  N   . ASP A 1 263 ? 41.87800 -9.06900  87.50100 1.000 53.89000 ? 263 ASP A N   1 
ATOM   2122 C  CA  . ASP A 1 263 ? 42.15800 -9.72700  88.79600 1.000 53.69000 ? 263 ASP A CA  1 
ATOM   2123 C  C   . ASP A 1 263 ? 43.16500 -10.87500 88.70000 1.000 44.53000 ? 263 ASP A C   1 
ATOM   2124 O  O   . ASP A 1 263 ? 43.05400 -11.75500 89.50900 1.000 42.92000 ? 263 ASP A O   1 
ATOM   2125 C  CB  . ASP A 1 263 ? 40.85800 -10.31500 89.32000 1.000 57.29000 ? 263 ASP A CB  1 
ATOM   2126 C  CG  . ASP A 1 263 ? 40.01000 -10.76400 88.16500 1.000 71.37000 ? 263 ASP A CG  1 
ATOM   2127 O  OD1 . ASP A 1 263 ? 40.61600 -11.12800 87.16000 1.000 67.78000 ? 263 ASP A OD1 1 
ATOM   2128 O  OD2 . ASP A 1 263 ? 38.79800 -10.64300 88.24800 1.000 73.79000 ? 263 ASP A OD2 1 
ATOM   2129 N  N   . ASN A 1 264 ? 44.02400 -10.91900 87.68800 1.000 44.30000 ? 264 ASN A N   1 
ATOM   2130 C  CA  . ASN A 1 264 ? 45.05500 -11.97700 87.55100 1.000 41.71000 ? 264 ASN A CA  1 
ATOM   2131 C  C   . ASN A 1 264 ? 44.46600 -13.39000 87.62500 1.000 35.04000 ? 264 ASN A C   1 
ATOM   2132 O  O   . ASN A 1 264 ? 45.12400 -14.24000 88.15000 1.000 32.21000 ? 264 ASN A O   1 
ATOM   2133 C  CB  . ASN A 1 264 ? 46.14100 -11.83400 88.61400 1.000 39.53000 ? 264 ASN A CB  1 
ATOM   2134 C  CG  . ASN A 1 264 ? 47.05100 -10.66600 88.35100 1.000 41.15000 ? 264 ASN A CG  1 
ATOM   2135 O  OD1 . ASN A 1 264 ? 47.25500 -10.29500 87.22200 1.000 48.34000 ? 264 ASN A OD1 1 
ATOM   2136 N  ND2 . ASN A 1 264 ? 47.57700 -10.07300 89.39200 1.000 40.89000 ? 264 ASN A ND2 1 
ATOM   2137 N  N   . MET A 1 265 ? 43.29500 -13.62300 87.05400 1.000 33.60000 ? 265 MET A N   1 
ATOM   2138 C  CA  . MET A 1 265 ? 42.69200 -14.96300 87.09400 1.000 31.41000 ? 265 MET A CA  1 
ATOM   2139 C  C   . MET A 1 265 ? 42.16100 -15.33000 85.70700 1.000 33.54000 ? 265 MET A C   1 
ATOM   2140 O  O   . MET A 1 265 ? 41.62300 -14.50000 85.02900 1.000 28.24000 ? 265 MET A O   1 
ATOM   2141 C  CB  . MET A 1 265 ? 41.55500 -15.03300 88.10900 1.000 40.98000 ? 265 MET A CB  1 
ATOM   2142 C  CG  . MET A 1 265 ? 42.00100 -15.30300 89.53000 1.000 51.58000 ? 265 MET A CG  1 
ATOM   2143 S  SD  . MET A 1 265 ? 42.81400 -16.87200 89.86200 1.000 58.23000 ? 265 MET A SD  1 
ATOM   2144 C  CE  . MET A 1 265 ? 41.87000 -17.97400 88.81400 1.000 47.40000 ? 265 MET A CE  1 
ATOM   2145 N  N   . ILE A 1 266 ? 42.40300 -16.55500 85.31100 1.000 26.08000 ? 266 ILE A N   1 
ATOM   2146 C  CA  . ILE A 1 266 ? 41.86300 -17.12100 84.05400 1.000 26.61000 ? 266 ILE A CA  1 
ATOM   2147 C  C   . ILE A 1 266 ? 40.92600 -18.24400 84.47900 1.000 26.42000 ? 266 ILE A C   1 
ATOM   2148 O  O   . ILE A 1 266 ? 41.39000 -19.16400 85.07900 1.000 25.05000 ? 266 ILE A O   1 
ATOM   2149 C  CB  . ILE A 1 266 ? 42.99300 -17.63400 83.15600 1.000 28.05000 ? 266 ILE A CB  1 
ATOM   2150 C  CG1 . ILE A 1 266 ? 43.89300 -16.49500 82.68200 1.000 32.10000 ? 266 ILE A CG1 1 
ATOM   2151 C  CG2 . ILE A 1 266 ? 42.43900 -18.45900 82.01700 1.000 24.15000 ? 266 ILE A CG2 1 
ATOM   2152 C  CD1 . ILE A 1 266 ? 43.16200 -15.39900 81.99500 1.000 24.56000 ? 266 ILE A CD1 1 
ATOM   2153 N  N   . GLU A 1 267 ? 39.65000 -18.11500 84.17300 1.000 24.09000 ? 267 GLU A N   1 
ATOM   2154 C  CA  . GLU A 1 267 ? 38.64800 -19.12600 84.56100 1.000 23.24000 ? 267 GLU A CA  1 
ATOM   2155 C  C   . GLU A 1 267 ? 38.67800 -20.30900 83.58500 1.000 26.22000 ? 267 GLU A C   1 
ATOM   2156 O  O   . GLU A 1 267 ? 38.25700 -21.35900 83.98200 1.000 24.80000 ? 267 GLU A O   1 
ATOM   2157 C  CB  . GLU A 1 267 ? 37.27100 -18.47800 84.69100 1.000 20.16000 ? 267 GLU A CB  1 
ATOM   2158 C  CG  . GLU A 1 267 ? 36.54700 -18.28100 83.38900 1.000 25.99000 ? 267 GLU A CG  1 
ATOM   2159 C  CD  . GLU A 1 267 ? 35.27500 -17.46600 83.47400 1.000 32.28000 ? 267 GLU A CD  1 
ATOM   2160 O  OE1 . GLU A 1 267 ? 35.05600 -16.85300 84.49600 1.000 34.43000 ? 267 GLU A OE1 1 
ATOM   2161 O  OE2 . GLU A 1 267 ? 34.52600 -17.47300 82.54000 1.000 29.94000 ? 267 GLU A OE2 1 
ATOM   2162 N  N   . ALA A 1 268 ? 39.16400 -20.09000 82.36800 1.000 22.52000 ? 268 ALA A N   1 
ATOM   2163 C  CA  . ALA A 1 268 ? 39.25500 -21.13600 81.32300 1.000 21.78000 ? 268 ALA A CA  1 
ATOM   2164 C  C   . ALA A 1 268 ? 40.10500 -20.70900 80.13400 1.000 23.10000 ? 268 ALA A C   1 
ATOM   2165 O  O   . ALA A 1 268 ? 40.16800 -19.55400 79.82700 1.000 22.89000 ? 268 ALA A O   1 
ATOM   2166 C  CB  . ALA A 1 268 ? 37.90100 -21.51000 80.80500 1.000 22.25000 ? 268 ALA A CB  1 
ATOM   2167 N  N   . ILE A 1 269 ? 40.68900 -21.69500 79.49300 1.000 24.48000 ? 269 ILE A N   1 
ATOM   2168 C  CA  . ILE A 1 269 ? 41.40600 -21.50900 78.21700 1.000 21.72000 ? 269 ILE A CA  1 
ATOM   2169 C  C   . ILE A 1 269 ? 40.45600 -22.06100 77.15000 1.000 24.24000 ? 269 ILE A C   1 
ATOM   2170 O  O   . ILE A 1 269 ? 40.06500 -23.20500 77.23500 1.000 21.35000 ? 269 ILE A O   1 
ATOM   2171 C  CB  . ILE A 1 269 ? 42.76900 -22.22200 78.22200 1.000 23.50000 ? 269 ILE A CB  1 
ATOM   2172 C  CG1 . ILE A 1 269 ? 43.67600 -21.69800 79.32700 1.000 25.13000 ? 269 ILE A CG1 1 
ATOM   2173 C  CG2 . ILE A 1 269 ? 43.44400 -22.13400 76.87200 1.000 20.57000 ? 269 ILE A CG2 1 
ATOM   2174 C  CD1 . ILE A 1 269 ? 45.00700 -22.31400 79.30700 1.000 28.75000 ? 269 ILE A CD1 1 
ATOM   2175 N  N   . GLU A 1 270 ? 40.05800 -21.22200 76.22700 1.000 19.90000 ? 270 GLU A N   1 
ATOM   2176 C  CA  . GLU A 1 270 ? 39.19700 -21.70900 75.13700 1.000 21.03000 ? 270 GLU A CA  1 
ATOM   2177 C  C   . GLU A 1 270 ? 40.10300 -22.26700 74.04400 1.000 23.85000 ? 270 GLU A C   1 
ATOM   2178 O  O   . GLU A 1 270 ? 40.74600 -21.50300 73.37100 1.000 21.73000 ? 270 GLU A O   1 
ATOM   2179 C  CB  . GLU A 1 270 ? 38.29700 -20.61100 74.60600 1.000 22.77000 ? 270 GLU A CB  1 
ATOM   2180 C  CG  . GLU A 1 270 ? 37.33100 -20.08600 75.61500 1.000 27.45000 ? 270 GLU A CG  1 
ATOM   2181 C  CD  . GLU A 1 270 ? 36.26500 -19.15700 75.07100 1.000 32.78000 ? 270 GLU A CD  1 
ATOM   2182 O  OE1 . GLU A 1 270 ? 36.36000 -18.77500 73.94500 1.000 30.11000 ? 270 GLU A OE1 1 
ATOM   2183 O  OE2 . GLU A 1 270 ? 35.37600 -18.84200 75.79800 1.000 29.18000 ? 270 GLU A OE2 1 
ATOM   2184 N  N   . HIS A 1 271 ? 40.15100 -23.57800 73.97000 1.000 20.95000 ? 271 HIS A N   1 
ATOM   2185 C  CA  . HIS A 1 271 ? 40.86700 -24.35100 72.93600 1.000 25.28000 ? 271 HIS A CA  1 
ATOM   2186 C  C   . HIS A 1 271 ? 39.92000 -24.50200 71.74100 1.000 24.39000 ? 271 HIS A C   1 
ATOM   2187 O  O   . HIS A 1 271 ? 39.05100 -25.33100 71.78600 1.000 25.20000 ? 271 HIS A O   1 
ATOM   2188 C  CB  . HIS A 1 271 ? 41.28100 -25.68100 73.56000 1.000 27.57000 ? 271 HIS A CB  1 
ATOM   2189 C  CG  . HIS A 1 271 ? 42.03000 -26.61700 72.68900 1.000 26.87000 ? 271 HIS A CG  1 
ATOM   2190 N  ND1 . HIS A 1 271 ? 41.44300 -27.31600 71.71300 1.000 30.48000 ? 271 HIS A ND1 1 
ATOM   2191 C  CD2 . HIS A 1 271 ? 43.29500 -27.04400 72.74400 1.000 27.86000 ? 271 HIS A CD2 1 
ATOM   2192 C  CE1 . HIS A 1 271 ? 42.31700 -28.10800 71.17000 1.000 33.16000 ? 271 HIS A CE1 1 
ATOM   2193 N  NE2 . HIS A 1 271 ? 43.43900 -27.96800 71.78400 1.000 30.79000 ? 271 HIS A NE2 1 
ATOM   2194 N  N   . VAL A 1 272 ? 40.07100 -23.66100 70.74200 1.000 21.65000 ? 272 VAL A N   1 
ATOM   2195 C  CA  . VAL A 1 272 ? 39.16200 -23.75500 69.57300 1.000 24.02000 ? 272 VAL A CA  1 
ATOM   2196 C  C   . VAL A 1 272 ? 39.71700 -24.75200 68.56700 1.000 24.92000 ? 272 VAL A C   1 
ATOM   2197 O  O   . VAL A 1 272 ? 40.75000 -24.55200 68.00900 1.000 23.16000 ? 272 VAL A O   1 
ATOM   2198 C  CB  . VAL A 1 272 ? 38.81700 -22.40400 68.92600 1.000 27.14000 ? 272 VAL A CB  1 
ATOM   2199 C  CG1 . VAL A 1 272 ? 37.73400 -22.54200 67.87700 1.000 21.75000 ? 272 VAL A CG1 1 
ATOM   2200 C  CG2 . VAL A 1 272 ? 38.49200 -21.33700 69.93600 1.000 19.22000 ? 272 VAL A CG2 1 
ATOM   2201 N  N   . LYS A 1 273 ? 38.93600 -25.77100 68.30700 1.000 28.54000 ? 273 LYS A N   1 
ATOM   2202 C  CA  . LYS A 1 273 ? 39.30200 -26.78400 67.30600 1.000 31.35000 ? 273 LYS A CA  1 
ATOM   2203 C  C   . LYS A 1 273 ? 39.16400 -26.17100 65.91700 1.000 30.83000 ? 273 LYS A C   1 
ATOM   2204 O  O   . LYS A 1 273 ? 38.40000 -25.25200 65.72600 1.000 26.93000 ? 273 LYS A O   1 
ATOM   2205 C  CB  . LYS A 1 273 ? 38.39800 -28.00500 67.44500 1.000 28.33000 ? 273 LYS A CB  1 
ATOM   2206 C  CG  . LYS A 1 273 ? 38.65300 -28.86000 68.66700 1.000 29.61000 ? 273 LYS A CG  1 
ATOM   2207 C  CD  . LYS A 1 273 ? 37.59200 -29.84800 68.89000 1.000 39.83000 ? 273 LYS A CD  1 
ATOM   2208 C  CE  . LYS A 1 273 ? 38.11400 -31.25900 68.94500 1.000 49.76000 ? 273 LYS A CE  1 
ATOM   2209 N  NZ  . LYS A 1 273 ? 37.39700 -32.02400 69.98900 1.000 55.05000 ? 273 LYS A NZ  1 
ATOM   2210 N  N   . PRO A 1 274 ? 39.83800 -26.72600 64.90300 1.000 29.92000 ? 274 PRO A N   1 
ATOM   2211 C  CA  . PRO A 1 274 ? 39.70100 -26.27000 63.52700 1.000 31.41000 ? 274 PRO A CA  1 
ATOM   2212 C  C   . PRO A 1 274 ? 38.26300 -26.08900 63.02500 1.000 31.80000 ? 274 PRO A C   1 
ATOM   2213 O  O   . PRO A 1 274 ? 38.03900 -25.18100 62.38400 1.000 34.90000 ? 274 PRO A O   1 
ATOM   2214 C  CB  . PRO A 1 274 ? 40.47900 -27.32100 62.74200 1.000 32.55000 ? 274 PRO A CB  1 
ATOM   2215 C  CG  . PRO A 1 274 ? 41.55300 -27.71000 63.69600 1.000 32.60000 ? 274 PRO A CG  1 
ATOM   2216 C  CD  . PRO A 1 274 ? 40.85100 -27.74500 65.03100 1.000 29.87000 ? 274 PRO A CD  1 
ATOM   2217 N  N   . ASN A 1 275 ? 37.35400 -26.96900 63.41100 1.000 36.39000 ? 275 ASN A N   1 
ATOM   2218 C  CA  . ASN A 1 275 ? 35.91500 -26.92100 63.08300 1.000 30.86000 ? 275 ASN A CA  1 
ATOM   2219 C  C   . ASN A 1 275 ? 35.11500 -25.87200 63.88100 1.000 34.76000 ? 275 ASN A C   1 
ATOM   2220 O  O   . ASN A 1 275 ? 33.93000 -25.87800 63.71700 1.000 33.98000 ? 275 ASN A O   1 
ATOM   2221 C  CB  . ASN A 1 275 ? 35.30900 -28.29700 63.31300 1.000 36.09000 ? 275 ASN A CB  1 
ATOM   2222 C  CG  . ASN A 1 275 ? 35.18100 -28.69700 64.76300 1.000 34.38000 ? 275 ASN A CG  1 
ATOM   2223 O  OD1 . ASN A 1 275 ? 35.35500 -27.91300 65.66900 1.000 36.65000 ? 275 ASN A OD1 1 
ATOM   2224 N  ND2 . ASN A 1 275 ? 34.90200 -29.95000 64.98900 1.000 39.78000 ? 275 ASN A ND2 1 
ATOM   2225 N  N   . GLY A 1 276 ? 35.72400 -25.05800 64.74700 1.000 28.27000 ? 276 GLY A N   1 
ATOM   2226 C  CA  . GLY A 1 276 ? 35.01300 -23.99900 65.48300 1.000 27.15000 ? 276 GLY A CA  1 
ATOM   2227 C  C   . GLY A 1 276 ? 34.56600 -24.36500 66.89100 1.000 32.74000 ? 276 GLY A C   1 
ATOM   2228 O  O   . GLY A 1 276 ? 34.26600 -23.48100 67.64500 1.000 28.93000 ? 276 GLY A O   1 
ATOM   2229 N  N   . LYS A 1 277 ? 34.52400 -25.63900 67.22200 1.000 31.26000 ? 277 LYS A N   1 
ATOM   2230 C  CA  . LYS A 1 277 ? 34.09800 -26.03700 68.57700 1.000 31.73000 ? 277 LYS A CA  1 
ATOM   2231 C  C   . LYS A 1 277 ? 35.04000 -25.44300 69.62500 1.000 26.24000 ? 277 LYS A C   1 
ATOM   2232 O  O   . LYS A 1 277 ? 36.20100 -25.62100 69.52700 1.000 27.26000 ? 277 LYS A O   1 
ATOM   2233 C  CB  . LYS A 1 277 ? 34.01300 -27.55300 68.68400 1.000 30.68000 ? 277 LYS A CB  1 
ATOM   2234 C  CG  . LYS A 1 277 ? 33.51600 -28.08000 70.01200 1.000 31.48000 ? 277 LYS A CG  1 
ATOM   2235 C  CD  . LYS A 1 277 ? 33.50000 -29.56000 70.06300 1.000 34.47000 ? 277 LYS A CD  1 
ATOM   2236 C  CE  . LYS A 1 277 ? 32.77300 -30.12000 71.25400 1.000 41.75000 ? 277 LYS A CE  1 
ATOM   2237 N  NZ  . LYS A 1 277 ? 33.47500 -31.30600 71.77300 1.000 48.16000 ? 277 LYS A NZ  1 
ATOM   2238 N  N   . ARG A 1 278 ? 34.48800 -24.74900 70.59100 1.000 28.80000 ? 278 ARG A N   1 
ATOM   2239 C  CA  . ARG A 1 278 ? 35.30000 -24.15700 71.67000 1.000 24.69000 ? 278 ARG A CA  1 
ATOM   2240 C  C   . ARG A 1 278 ? 35.33100 -25.11400 72.85700 1.000 28.36000 ? 278 ARG A C   1 
ATOM   2241 O  O   . ARG A 1 278 ? 34.32400 -25.31100 73.47900 1.000 32.39000 ? 278 ARG A O   1 
ATOM   2242 C  CB  . ARG A 1 278 ? 34.81600 -22.75500 71.99600 1.000 31.21000 ? 278 ARG A CB  1 
ATOM   2243 C  CG  . ARG A 1 278 ? 34.87000 -21.80500 70.81400 1.000 33.51000 ? 278 ARG A CG  1 
ATOM   2244 C  CD  . ARG A 1 278 ? 34.48800 -20.40100 71.14400 1.000 34.40000 ? 278 ARG A CD  1 
ATOM   2245 N  NE  . ARG A 1 278 ? 33.21300 -20.28100 71.79900 1.000 36.95000 ? 278 ARG A NE  1 
ATOM   2246 C  CZ  . ARG A 1 278 ? 32.05800 -20.15200 71.19800 1.000 44.62000 ? 278 ARG A CZ  1 
ATOM   2247 N  NH1 . ARG A 1 278 ? 31.95900 -20.14200 69.88300 1.000 34.86000 ? 278 ARG A NH1 1 
ATOM   2248 N  NH2 . ARG A 1 278 ? 30.98100 -20.05700 71.93800 1.000 50.88000 ? 278 ARG A NH2 1 
ATOM   2249 N  N   . VAL A 1 279 ? 36.48400 -25.68600 73.11400 1.000 24.64000 ? 279 VAL A N   1 
ATOM   2250 C  CA  . VAL A 1 279 ? 36.66400 -26.65900 74.21500 1.000 28.84000 ? 279 VAL A CA  1 
ATOM   2251 C  C   . VAL A 1 279 ? 37.26400 -25.92500 75.42300 1.000 27.53000 ? 279 VAL A C   1 
ATOM   2252 O  O   . VAL A 1 279 ? 38.31900 -25.35800 75.30200 1.000 23.48000 ? 279 VAL A O   1 
ATOM   2253 C  CB  . VAL A 1 279 ? 37.52800 -27.83700 73.73300 1.000 25.56000 ? 279 VAL A CB  1 
ATOM   2254 C  CG1 . VAL A 1 279 ? 37.87200 -28.79900 74.83500 1.000 26.59000 ? 279 VAL A CG1 1 
ATOM   2255 C  CG2 . VAL A 1 279 ? 36.87500 -28.57700 72.59700 1.000 31.98000 ? 279 VAL A CG2 1 
ATOM   2256 N  N   . LEU A 1 280 ? 36.57600 -25.93900 76.54600 1.000 24.09000 ? 280 LEU A N   1 
ATOM   2257 C  CA  . LEU A 1 280 ? 37.08700 -25.21800 77.73300 1.000 24.79000 ? 280 LEU A CA  1 
ATOM   2258 C  C   . LEU A 1 280 ? 38.10800 -26.07300 78.47700 1.000 25.91000 ? 280 LEU A C   1 
ATOM   2259 O  O   . LEU A 1 280 ? 37.78800 -27.15500 78.85000 1.000 24.54000 ? 280 LEU A O   1 
ATOM   2260 C  CB  . LEU A 1 280 ? 35.93000 -24.82400 78.64300 1.000 25.07000 ? 280 LEU A CB  1 
ATOM   2261 C  CG  . LEU A 1 280 ? 34.83000 -24.01100 77.98000 1.000 24.60000 ? 280 LEU A CG  1 
ATOM   2262 C  CD1 . LEU A 1 280 ? 33.75700 -23.70200 78.97000 1.000 29.12000 ? 280 LEU A CD1 1 
ATOM   2263 C  CD2 . LEU A 1 280 ? 35.37700 -22.74700 77.36700 1.000 27.15000 ? 280 LEU A CD2 1 
ATOM   2264 N  N   . LEU A 1 281 ? 39.29200 -25.53200 78.64400 1.000 22.32000 ? 281 LEU A N   1 
ATOM   2265 C  CA  . LEU A 1 281 ? 40.41200 -26.16400 79.36000 1.000 23.51000 ? 281 LEU A CA  1 
ATOM   2266 C  C   . LEU A 1 281 ? 40.59000 -25.45300 80.69300 1.000 24.43000 ? 281 LEU A C   1 
ATOM   2267 O  O   . LEU A 1 281 ? 40.23000 -24.33300 80.80100 1.000 22.05000 ? 281 LEU A O   1 
ATOM   2268 C  CB  . LEU A 1 281 ? 41.68400 -26.03700 78.52700 1.000 24.52000 ? 281 LEU A CB  1 
ATOM   2269 C  CG  . LEU A 1 281 ? 41.63100 -26.66700 77.14600 1.000 22.08000 ? 281 LEU A CG  1 
ATOM   2270 C  CD1 . LEU A 1 281 ? 42.97800 -26.60400 76.48200 1.000 25.21000 ? 281 LEU A CD1 1 
ATOM   2271 C  CD2 . LEU A 1 281 ? 41.13500 -28.08600 77.21100 1.000 22.36000 ? 281 LEU A CD2 1 
ATOM   2272 N  N   . LYS A 1 282 ? 41.20900 -26.13800 81.62300 1.000 24.27000 ? 282 LYS A N   1 
ATOM   2273 C  CA  . LYS A 1 282 ? 41.40000 -25.62200 82.97800 1.000 26.11000 ? 282 LYS A CA  1 
ATOM   2274 C  C   . LYS A 1 282 ? 42.21700 -24.33000 82.93600 1.000 23.93000 ? 282 LYS A C   1 
ATOM   2275 O  O   . LYS A 1 282 ? 43.14900 -24.24400 82.21200 1.000 24.87000 ? 282 LYS A O   1 
ATOM   2276 C  CB  . LYS A 1 282 ? 41.99600 -26.72700 83.84000 1.000 26.54000 ? 282 LYS A CB  1 
ATOM   2277 C  CG  . LYS A 1 282 ? 42.66100 -26.27700 85.11300 1.000 28.72000 ? 282 LYS A CG  1 
ATOM   2278 C  CD  . LYS A 1 282 ? 43.60200 -27.28300 85.65700 1.000 39.49000 ? 282 LYS A CD  1 
ATOM   2279 C  CE  . LYS A 1 282 ? 42.89900 -28.48500 86.21400 1.000 39.29000 ? 282 LYS A CE  1 
ATOM   2280 N  NZ  . LYS A 1 282 ? 41.90600 -28.03100 87.19000 1.000 36.91000 ? 282 LYS A NZ  1 
ATOM   2281 N  N   . GLY A 1 283 ? 41.77500 -23.34500 83.68400 1.000 22.02000 ? 283 GLY A N   1 
ATOM   2282 C  CA  . GLY A 1 283 ? 42.50000 -22.08200 83.80400 1.000 21.81000 ? 283 GLY A CA  1 
ATOM   2283 C  C   . GLY A 1 283 ? 43.42300 -22.08500 85.01200 1.000 26.87000 ? 283 GLY A C   1 
ATOM   2284 O  O   . GLY A 1 283 ? 43.90800 -23.13600 85.39300 1.000 26.45000 ? 283 GLY A O   1 
ATOM   2285 N  N   . GLY A 1 284 ? 43.64800 -20.91100 85.57900 1.000 27.13000 ? 284 GLY A N   1 
ATOM   2286 C  CA  . GLY A 1 284 ? 44.54400 -20.76700 86.72400 1.000 29.10000 ? 284 GLY A CA  1 
ATOM   2287 C  C   . GLY A 1 284 ? 44.84800 -19.33300 87.04100 1.000 28.92000 ? 284 GLY A C   1 
ATOM   2288 O  O   . GLY A 1 284 ? 44.17500 -18.48100 86.57700 1.000 25.21000 ? 284 GLY A O   1 
ATOM   2289 N  N   . THR A 1 285 ? 45.87300 -19.14700 87.83900 1.000 29.89000 ? 285 THR A N   1 
ATOM   2290 C  CA  . THR A 1 285 ? 46.28800 -17.82300 88.31600 1.000 26.80000 ? 285 THR A CA  1 
ATOM   2291 C  C   . THR A 1 285 ? 47.36800 -17.24000 87.41400 1.000 24.80000 ? 285 THR A C   1 
ATOM   2292 O  O   . THR A 1 285 ? 48.27500 -17.94000 87.06700 1.000 28.43000 ? 285 THR A O   1 
ATOM   2293 C  CB  . THR A 1 285 ? 46.80700 -17.95900 89.74500 1.000 30.65000 ? 285 THR A CB  1 
ATOM   2294 O  OG1 . THR A 1 285 ? 45.74700 -18.47600 90.53800 1.000 34.87000 ? 285 THR A OG1 1 
ATOM   2295 C  CG2 . THR A 1 285 ? 47.31300 -16.65000 90.28500 1.000 24.80000 ? 285 THR A CG2 1 
ATOM   2296 N  N   . ILE A 1 286 ? 47.23900 -15.97300 87.09400 1.000 26.41000 ? 286 ILE A N   1 
ATOM   2297 C  CA  . ILE A 1 286 ? 48.28600 -15.27500 86.31800 1.000 25.99000 ? 286 ILE A CA  1 
ATOM   2298 C  C   . ILE A 1 286 ? 49.37900 -14.90900 87.30700 1.000 26.70000 ? 286 ILE A C   1 
ATOM   2299 O  O   . ILE A 1 286 ? 49.16700 -14.01800 88.08000 1.000 33.28000 ? 286 ILE A O   1 
ATOM   2300 C  CB  . ILE A 1 286 ? 47.75000 -14.01300 85.65100 1.000 23.45000 ? 286 ILE A CB  1 
ATOM   2301 C  CG1 . ILE A 1 286 ? 46.51100 -14.26500 84.79900 1.000 28.70000 ? 286 ILE A CG1 1 
ATOM   2302 C  CG2 . ILE A 1 286 ? 48.85900 -13.29200 84.92400 1.000 29.35000 ? 286 ILE A CG2 1 
ATOM   2303 C  CD1 . ILE A 1 286 ? 46.75900 -14.30200 83.35700 1.000 26.62000 ? 286 ILE A CD1 1 
ATOM   2304 N  N   . VAL A 1 287 ? 50.49600 -15.59900 87.24600 1.000 27.70000 ? 287 VAL A N   1 
ATOM   2305 C  CA  . VAL A 1 287 ? 51.61400 -15.35800 88.19100 1.000 29.18000 ? 287 VAL A CA  1 
ATOM   2306 C  C   . VAL A 1 287 ? 52.50100 -14.22300 87.67900 1.000 31.38000 ? 287 VAL A C   1 
ATOM   2307 O  O   . VAL A 1 287 ? 53.16000 -13.62100 88.45300 1.000 32.87000 ? 287 VAL A O   1 
ATOM   2308 C  CB  . VAL A 1 287 ? 52.36500 -16.66500 88.45900 1.000 36.46000 ? 287 VAL A CB  1 
ATOM   2309 C  CG1 . VAL A 1 287 ? 51.44600 -17.69500 89.05200 1.000 28.73000 ? 287 VAL A CG1 1 
ATOM   2310 C  CG2 . VAL A 1 287 ? 53.04000 -17.20300 87.22100 1.000 32.34000 ? 287 VAL A CG2 1 
ATOM   2311 N  N   . GLN A 1 288 ? 52.44700 -13.92800 86.39800 1.000 28.78000 ? 288 GLN A N   1 
ATOM   2312 C  CA  . GLN A 1 288 ? 53.26300 -12.84100 85.83300 1.000 34.07000 ? 288 GLN A CA  1 
ATOM   2313 C  C   . GLN A 1 288 ? 52.65300 -12.44600 84.50100 1.000 39.26000 ? 288 GLN A C   1 
ATOM   2314 O  O   . GLN A 1 288 ? 52.19100 -13.32000 83.80400 1.000 30.59000 ? 288 GLN A O   1 
ATOM   2315 C  CB  . GLN A 1 288 ? 54.69700 -13.29700 85.57400 1.000 41.15000 ? 288 GLN A CB  1 
ATOM   2316 C  CG  . GLN A 1 288 ? 55.71500 -12.17900 85.74500 1.000 54.10000 ? 288 GLN A CG  1 
ATOM   2317 C  CD  . GLN A 1 288 ? 57.14500 -12.57200 85.47600 1.000 60.93000 ? 288 GLN A CD  1 
ATOM   2318 O  OE1 . GLN A 1 288 ? 57.45700 -13.70800 85.15700 1.000 62.74000 ? 288 GLN A OE1 1 
ATOM   2319 N  NE2 . GLN A 1 288 ? 58.03600 -11.61300 85.59900 1.000 69.35000 ? 288 GLN A NE2 1 
ATOM   2320 N  N   . LYS A 1 289 ? 52.71700 -11.16300 84.19200 1.000 33.86000 ? 289 LYS A N   1 
ATOM   2321 C  CA  . LYS A 1 289 ? 52.17700 -10.68700 82.91200 1.000 37.56000 ? 289 LYS A CA  1 
ATOM   2322 C  C   . LYS A 1 289 ? 52.83800 -9.38000  82.51400 1.000 37.30000 ? 289 LYS A C   1 
ATOM   2323 O  O   . LYS A 1 289 ? 53.43200 -8.75600  83.33000 1.000 38.58000 ? 289 LYS A O   1 
ATOM   2324 C  CB  . LYS A 1 289 ? 50.65200 -10.65700 82.94100 1.000 35.18000 ? 289 LYS A CB  1 
ATOM   2325 C  CG  . LYS A 1 289 ? 50.01100 -9.30500  82.99600 1.000 46.93000 ? 289 LYS A CG  1 
ATOM   2326 C  CD  . LYS A 1 289 ? 48.74600 -9.31900  83.73700 1.000 42.19000 ? 289 LYS A CD  1 
ATOM   2327 C  CE  . LYS A 1 289 ? 49.00800 -8.74100  85.09400 1.000 46.66000 ? 289 LYS A CE  1 
ATOM   2328 N  NZ  . LYS A 1 289 ? 47.90300 -7.88200  85.50200 1.000 45.28000 ? 289 LYS A NZ  1 
ATOM   2329 N  N   . GLU A 1 290 ? 52.72800 -9.06200  81.24500 1.000 37.64000 ? 290 GLU A N   1 
ATOM   2330 C  CA  . GLU A 1 290 ? 53.28400 -7.86100  80.61100 1.000 39.31000 ? 290 GLU A CA  1 
ATOM   2331 C  C   . GLU A 1 290 ? 52.27300 -7.45500  79.55000 1.000 42.06000 ? 290 GLU A C   1 
ATOM   2332 O  O   . GLU A 1 290 ? 52.04000 -8.23600  78.67600 1.000 35.37000 ? 290 GLU A O   1 
ATOM   2333 C  CB  . GLU A 1 290 ? 54.54100 -8.28900  79.87000 1.000 41.69000 ? 290 GLU A CB  1 
ATOM   2334 C  CG  . GLU A 1 290 ? 55.79100 -7.57100  80.28600 1.000 62.72000 ? 290 GLU A CG  1 
ATOM   2335 C  CD  . GLU A 1 290 ? 56.83100 -7.44100  79.18300 1.000 71.14000 ? 290 GLU A CD  1 
ATOM   2336 O  OE1 . GLU A 1 290 ? 57.38200 -8.47000  78.76800 1.000 81.87000 ? 290 GLU A OE1 1 
ATOM   2337 O  OE2 . GLU A 1 290 ? 57.10000 -6.32000  78.76600 1.000 63.20000 ? 290 GLU A OE2 1 
ATOM   2338 N  N   . ILE A 1 291 ? 51.64400 -6.30800  79.71300 1.000 39.34000 ? 291 ILE A N   1 
ATOM   2339 C  CA  . ILE A 1 291 ? 50.66200 -5.79900  78.72800 1.000 34.63000 ? 291 ILE A CA  1 
ATOM   2340 C  C   . ILE A 1 291 ? 51.18900 -4.47500  78.19800 1.000 38.33000 ? 291 ILE A C   1 
ATOM   2341 O  O   . ILE A 1 291 ? 51.31200 -3.56200  78.95900 1.000 43.30000 ? 291 ILE A O   1 
ATOM   2342 C  CB  . ILE A 1 291 ? 49.29000 -5.62800  79.37700 1.000 36.71000 ? 291 ILE A CB  1 
ATOM   2343 C  CG1 . ILE A 1 291 ? 48.90700 -6.81800  80.25000 1.000 37.42000 ? 291 ILE A CG1 1 
ATOM   2344 C  CG2 . ILE A 1 291 ? 48.24900 -5.30400  78.33700 1.000 42.18000 ? 291 ILE A CG2 1 
ATOM   2345 C  CD1 . ILE A 1 291 ? 47.95300 -7.76000  79.63000 1.000 43.70000 ? 291 ILE A CD1 1 
ATOM   2346 N  N   . GLY A 1 292 ? 51.54000 -4.43600  76.92800 1.000 41.69000 ? 292 GLY A N   1 
ATOM   2347 C  CA  . GLY A 1 292 ? 52.02300 -3.21000  76.29000 1.000 38.03000 ? 292 GLY A CA  1 
ATOM   2348 C  C   . GLY A 1 292 ? 51.07500 -2.67000  75.24500 1.000 43.00000 ? 292 GLY A C   1 
ATOM   2349 O  O   . GLY A 1 292 ? 49.94500 -3.11500  75.16000 1.000 38.59000 ? 292 GLY A O   1 
ATOM   2350 N  N   . ARG A 1 293 ? 51.58200 -1.74000  74.45900 1.000 42.54000 ? 293 ARG A N   1 
ATOM   2351 C  CA  . ARG A 1 293 ? 50.81700 -1.07100  73.39800 1.000 39.91000 ? 293 ARG A CA  1 
ATOM   2352 C  C   . ARG A 1 293 ? 50.49100 -2.06300  72.29800 1.000 44.90000 ? 293 ARG A C   1 
ATOM   2353 O  O   . ARG A 1 293 ? 49.46000 -1.88900  71.71100 1.000 39.54000 ? 293 ARG A O   1 
ATOM   2354 C  CB  . ARG A 1 293 ? 51.68500 -0.04000  72.68400 1.000 43.95000 ? 293 ARG A CB  1 
ATOM   2355 C  CG  . ARG A 1 293 ? 52.35500 0.97800   73.58400 1.000 58.80000 ? 293 ARG A CG  1 
ATOM   2356 C  CD  . ARG A 1 293 ? 52.56800 2.28500   72.85900 1.000 57.70000 ? 293 ARG A CD  1 
ATOM   2357 N  NE  . ARG A 1 293 ? 51.95500 3.41000   73.54800 1.000 64.02000 ? 293 ARG A NE  1 
ATOM   2358 C  CZ  . ARG A 1 293 ? 50.93500 4.10600   73.08100 1.000 64.15000 ? 293 ARG A CZ  1 
ATOM   2359 N  NH1 . ARG A 1 293 ? 50.39100 3.78900   71.92200 1.000 68.18000 ? 293 ARG A NH1 1 
ATOM   2360 N  NH2 . ARG A 1 293 ? 50.45900 5.11600   73.77700 1.000 62.66000 ? 293 ARG A NH2 1 
ATOM   2361 N  N   . ASP A 1 294 ? 51.37100 -3.02300  72.03200 1.000 33.80000 ? 294 ASP A N   1 
ATOM   2362 C  CA  . ASP A 1 294 ? 51.12900 -3.87800  70.85800 1.000 39.70000 ? 294 ASP A CA  1 
ATOM   2363 C  C   . ASP A 1 294 ? 51.36300 -5.37000  71.11500 1.000 36.56000 ? 294 ASP A C   1 
ATOM   2364 O  O   . ASP A 1 294 ? 51.46000 -6.08200  70.15300 1.000 31.68000 ? 294 ASP A O   1 
ATOM   2365 C  CB  . ASP A 1 294 ? 51.92700 -3.35600  69.67400 1.000 46.24000 ? 294 ASP A CB  1 
ATOM   2366 C  CG  . ASP A 1 294 ? 53.39900 -3.36500  69.96700 1.000 50.97000 ? 294 ASP A CG  1 
ATOM   2367 O  OD1 . ASP A 1 294 ? 53.77300 -3.00600  71.06100 1.000 50.95000 ? 294 ASP A OD1 1 
ATOM   2368 O  OD2 . ASP A 1 294 ? 54.13200 -3.79900  69.10100 1.000 63.72000 ? 294 ASP A OD2 1 
ATOM   2369 N  N   . TYR A 1 295 ? 51.40000 -5.78600  72.36900 1.000 30.16000 ? 295 TYR A N   1 
ATOM   2370 C  CA  . TYR A 1 295 ? 51.55000 -7.21200  72.70400 1.000 29.58000 ? 295 TYR A CA  1 
ATOM   2371 C  C   . TYR A 1 295 ? 51.22700 -7.42200  74.17300 1.000 31.57000 ? 295 TYR A C   1 
ATOM   2372 O  O   . TYR A 1 295 ? 51.15300 -6.49300  74.92800 1.000 33.09000 ? 295 TYR A O   1 
ATOM   2373 C  CB  . TYR A 1 295 ? 52.95400 -7.73900  72.43000 1.000 29.36000 ? 295 TYR A CB  1 
ATOM   2374 C  CG  . TYR A 1 295 ? 53.93000 -7.28300  73.46200 1.000 40.99000 ? 295 TYR A CG  1 
ATOM   2375 C  CD1 . TYR A 1 295 ? 54.53500 -6.05700  73.34700 1.000 45.31000 ? 295 TYR A CD1 1 
ATOM   2376 C  CD2 . TYR A 1 295 ? 54.16300 -8.02700  74.58900 1.000 41.96000 ? 295 TYR A CD2 1 
ATOM   2377 C  CE1 . TYR A 1 295 ? 55.41900 -5.60500  74.30000 1.000 51.39000 ? 295 TYR A CE1 1 
ATOM   2378 C  CE2 . TYR A 1 295 ? 55.05600 -7.60200  75.55000 1.000 51.21000 ? 295 TYR A CE2 1 
ATOM   2379 C  CZ  . TYR A 1 295 ? 55.67700 -6.38100  75.40400 1.000 48.96000 ? 295 TYR A CZ  1 
ATOM   2380 O  OH  . TYR A 1 295 ? 56.53700 -5.92300  76.33500 1.000 63.65000 ? 295 TYR A OH  1 
ATOM   2381 N  N   . TYR A 1 296 ? 50.97900 -8.66800  74.49800 1.000 30.47000 ? 296 TYR A N   1 
ATOM   2382 C  CA  . TYR A 1 296 ? 50.74200 -9.10900  75.87900 1.000 29.01000 ? 296 TYR A CA  1 
ATOM   2383 C  C   . TYR A 1 296 ? 51.36300 -10.48800 76.03600 1.000 31.08000 ? 296 TYR A C   1 
ATOM   2384 O  O   . TYR A 1 296 ? 51.42500 -11.21500 75.08100 1.000 31.56000 ? 296 TYR A O   1 
ATOM   2385 C  CB  . TYR A 1 296 ? 49.27200 -9.06000  76.26400 1.000 29.37000 ? 296 TYR A CB  1 
ATOM   2386 C  CG  . TYR A 1 296 ? 48.35000 -9.68500  75.26300 1.000 30.71000 ? 296 TYR A CG  1 
ATOM   2387 C  CD1 . TYR A 1 296 ? 48.13800 -11.04800 75.22600 1.000 28.72000 ? 296 TYR A CD1 1 
ATOM   2388 C  CD2 . TYR A 1 296 ? 47.70300 -8.90600  74.33800 1.000 26.54000 ? 296 TYR A CD2 1 
ATOM   2389 C  CE1 . TYR A 1 296 ? 47.30100 -11.62900 74.29500 1.000 22.66000 ? 296 TYR A CE1 1 
ATOM   2390 C  CE2 . TYR A 1 296 ? 46.87000 -9.46700  73.40700 1.000 28.76000 ? 296 TYR A CE2 1 
ATOM   2391 C  CZ  . TYR A 1 296 ? 46.65600 -10.83000 73.38400 1.000 25.62000 ? 296 TYR A CZ  1 
ATOM   2392 O  OH  . TYR A 1 296 ? 45.80700 -11.31000 72.46000 1.000 22.33000 ? 296 TYR A OH  1 
ATOM   2393 N  N   . TRP A 1 297 ? 51.84400 -10.76500 77.22900 1.000 28.55000 ? 297 TRP A N   1 
ATOM   2394 C  CA  . TRP A 1 297 ? 52.47400 -12.04900 77.57800 1.000 29.66000 ? 297 TRP A CA  1 
ATOM   2395 C  C   . TRP A 1 297 ? 52.00600 -12.43600 78.97900 1.000 28.99000 ? 297 TRP A C   1 
ATOM   2396 O  O   . TRP A 1 297 ? 51.86300 -11.57000 79.78800 1.000 30.55000 ? 297 TRP A O   1 
ATOM   2397 C  CB  . TRP A 1 297 ? 53.99000 -11.91600 77.44700 1.000 34.59000 ? 297 TRP A CB  1 
ATOM   2398 C  CG  . TRP A 1 297 ? 54.74400 -13.03000 78.08300 1.000 45.88000 ? 297 TRP A CG  1 
ATOM   2399 C  CD1 . TRP A 1 297 ? 55.10800 -14.22300 77.53500 1.000 47.69000 ? 297 TRP A CD1 1 
ATOM   2400 C  CD2 . TRP A 1 297 ? 55.16900 -13.07700 79.44500 1.000 42.51000 ? 297 TRP A CD2 1 
ATOM   2401 N  NE1 . TRP A 1 297 ? 55.74700 -15.00300 78.45500 1.000 45.93000 ? 297 TRP A NE1 1 
ATOM   2402 C  CE2 . TRP A 1 297 ? 55.81100 -14.31700 79.63200 1.000 48.45000 ? 297 TRP A CE2 1 
ATOM   2403 C  CE3 . TRP A 1 297 ? 55.07100 -12.18700 80.50300 1.000 38.37000 ? 297 TRP A CE3 1 
ATOM   2404 C  CZ2 . TRP A 1 297 ? 56.34800 -14.69100 80.85200 1.000 47.88000 ? 297 TRP A CZ2 1 
ATOM   2405 C  CZ3 . TRP A 1 297 ? 55.62900 -12.54700 81.70100 1.000 46.55000 ? 297 TRP A CZ3 1 
ATOM   2406 C  CH2 . TRP A 1 297 ? 56.23600 -13.78400 81.87500 1.000 53.59000 ? 297 TRP A CH2 1 
ATOM   2407 N  N   . LEU A 1 298 ? 51.71000 -13.69700 79.20600 1.000 30.34000 ? 298 LEU A N   1 
ATOM   2408 C  CA  . LEU A 1 298 ? 51.28000 -14.13300 80.54900 1.000 29.72000 ? 298 LEU A CA  1 
ATOM   2409 C  C   . LEU A 1 298 ? 51.89800 -15.47500 80.87800 1.000 33.37000 ? 298 LEU A C   1 
ATOM   2410 O  O   . LEU A 1 298 ? 52.16500 -16.24200 79.98500 1.000 33.14000 ? 298 LEU A O   1 
ATOM   2411 C  CB  . LEU A 1 298 ? 49.76800 -14.29400 80.69700 1.000 26.76000 ? 298 LEU A CB  1 
ATOM   2412 C  CG  . LEU A 1 298 ? 48.79800 -13.52500 79.81500 1.000 47.03000 ? 298 LEU A CG  1 
ATOM   2413 C  CD1 . LEU A 1 298 ? 47.42200 -14.12900 79.97700 1.000 38.48000 ? 298 LEU A CD1 1 
ATOM   2414 C  CD2 . LEU A 1 298 ? 48.72000 -12.07500 80.21700 1.000 43.27000 ? 298 LEU A CD2 1 
ATOM   2415 N  N   . LYS A 1 299 ? 52.03600 -15.70900 82.16500 1.000 29.76000 ? 299 LYS A N   1 
ATOM   2416 C  CA  . LYS A 1 299 ? 52.47400 -16.99800 82.70800 1.000 29.59000 ? 299 LYS A CA  1 
ATOM   2417 C  C   . LYS A 1 299 ? 51.35400 -17.43100 83.65500 1.000 26.46000 ? 299 LYS A C   1 
ATOM   2418 O  O   . LYS A 1 299 ? 51.07700 -16.73400 84.56800 1.000 30.19000 ? 299 LYS A O   1 
ATOM   2419 C  CB  . LYS A 1 299 ? 53.85500 -16.84700 83.32600 1.000 36.95000 ? 299 LYS A CB  1 
ATOM   2420 C  CG  . LYS A 1 299 ? 54.35600 -18.05200 84.09800 1.000 42.78000 ? 299 LYS A CG  1 
ATOM   2421 C  CD  . LYS A 1 299 ? 55.79000 -17.92400 84.49400 1.000 44.98000 ? 299 LYS A CD  1 
ATOM   2422 C  CE  . LYS A 1 299 ? 56.11500 -18.65300 85.77100 1.000 39.12000 ? 299 LYS A CE  1 
ATOM   2423 N  NZ  . LYS A 1 299 ? 57.53000 -19.08000 85.82400 1.000 56.41000 ? 299 LYS A NZ  1 
ATOM   2424 N  N   . ILE A 1 300 ? 50.66100 -18.48900 83.32500 1.000 23.73000 ? 300 ILE A N   1 
ATOM   2425 C  CA  . ILE A 1 300 ? 49.53900 -18.97500 84.15600 1.000 26.15000 ? 300 ILE A CA  1 
ATOM   2426 C  C   . ILE A 1 300 ? 49.97700 -20.22700 84.90600 1.000 28.08000 ? 300 ILE A C   1 
ATOM   2427 O  O   . ILE A 1 300 ? 50.63400 -21.06700 84.31900 1.000 29.07000 ? 300 ILE A O   1 
ATOM   2428 C  CB  . ILE A 1 300 ? 48.29100 -19.23500 83.29600 1.000 25.79000 ? 300 ILE A CB  1 
ATOM   2429 C  CG1 . ILE A 1 300 ? 47.87100 -17.99800 82.50400 1.000 32.70000 ? 300 ILE A CG1 1 
ATOM   2430 C  CG2 . ILE A 1 300 ? 47.14900 -19.77100 84.11500 1.000 26.15000 ? 300 ILE A CG2 1 
ATOM   2431 C  CD1 . ILE A 1 300 ? 47.18600 -18.28100 81.20800 1.000 28.56000 ? 300 ILE A CD1 1 
ATOM   2432 N  N   . ARG A 1 301 ? 49.59600 -20.30900 86.16400 1.000 24.60000 ? 301 ARG A N   1 
ATOM   2433 C  CA  . ARG A 1 301 ? 49.83500 -21.51100 86.97100 1.000 28.28000 ? 301 ARG A CA  1 
ATOM   2434 C  C   . ARG A 1 301 ? 48.51000 -22.26400 87.10700 1.000 24.68000 ? 301 ARG A C   1 
ATOM   2435 O  O   . ARG A 1 301 ? 47.59200 -21.71200 87.60900 1.000 25.44000 ? 301 ARG A O   1 
ATOM   2436 C  CB  . ARG A 1 301 ? 50.41500 -21.14600 88.33200 1.000 32.26000 ? 301 ARG A CB  1 
ATOM   2437 C  CG  . ARG A 1 301 ? 50.38500 -22.29900 89.31400 1.000 29.91000 ? 301 ARG A CG  1 
ATOM   2438 C  CD  . ARG A 1 301 ? 51.25700 -22.10100 90.52000 1.000 35.45000 ? 301 ARG A CD  1 
ATOM   2439 N  NE  . ARG A 1 301 ? 51.25700 -23.25200 91.37400 1.000 31.26000 ? 301 ARG A NE  1 
ATOM   2440 C  CZ  . ARG A 1 301 ? 52.33800 -23.75400 91.91300 1.000 34.79000 ? 301 ARG A CZ  1 
ATOM   2441 N  NH1 . ARG A 1 301 ? 53.49500 -23.18500 91.68200 1.000 29.52000 ? 301 ARG A NH1 1 
ATOM   2442 N  NH2 . ARG A 1 301 ? 52.25300 -24.81300 92.67800 1.000 32.16000 ? 301 ARG A NH2 1 
ATOM   2443 N  N   . ARG A 1 302 ? 48.46800 -23.49100 86.64000 1.000 22.19000 ? 302 ARG A N   1 
ATOM   2444 C  CA  . ARG A 1 302 ? 47.22900 -24.27800 86.68600 1.000 27.65000 ? 302 ARG A CA  1 
ATOM   2445 C  C   . ARG A 1 302 ? 47.40500 -25.40300 87.68600 1.000 31.03000 ? 302 ARG A C   1 
ATOM   2446 O  O   . ARG A 1 302 ? 48.36500 -26.06900 87.58800 1.000 29.86000 ? 302 ARG A O   1 
ATOM   2447 C  CB  . ARG A 1 302 ? 46.86900 -24.81700 85.30900 1.000 28.51000 ? 302 ARG A CB  1 
ATOM   2448 C  CG  . ARG A 1 302 ? 46.83300 -23.77000 84.21700 1.000 29.02000 ? 302 ARG A CG  1 
ATOM   2449 C  CD  . ARG A 1 302 ? 47.19400 -24.45000 82.93300 1.000 38.65000 ? 302 ARG A CD  1 
ATOM   2450 N  NE  . ARG A 1 302 ? 46.05500 -24.94400 82.25000 1.000 32.11000 ? 302 ARG A NE  1 
ATOM   2451 C  CZ  . ARG A 1 302 ? 46.03100 -25.98700 81.47200 1.000 35.59000 ? 302 ARG A CZ  1 
ATOM   2452 N  NH1 . ARG A 1 302 ? 47.11000 -26.69600 81.25600 1.000 30.36000 ? 302 ARG A NH1 1 
ATOM   2453 N  NH2 . ARG A 1 302 ? 44.90300 -26.33700 80.92700 1.000 27.43000 ? 302 ARG A NH2 1 
ATOM   2454 N  N   . GLU A 1 303 ? 46.44800 -25.56400 88.57700 1.000 31.10000 ? 303 GLU A N   1 
ATOM   2455 C  CA  . GLU A 1 303 ? 46.52300 -26.58000 89.64400 1.000 32.88000 ? 303 GLU A CA  1 
ATOM   2456 C  C   . GLU A 1 303 ? 45.73800 -27.82400 89.23400 1.000 40.02000 ? 303 GLU A C   1 
ATOM   2457 O  O   . GLU A 1 303 ? 44.59000 -27.68700 88.83500 1.000 36.41000 ? 303 GLU A O   1 
ATOM   2458 C  CB  . GLU A 1 303 ? 45.96800 -26.01500 90.94200 1.000 30.32000 ? 303 GLU A CB  1 
ATOM   2459 C  CG  . GLU A 1 303 ? 46.66200 -24.77400 91.41800 1.000 32.27000 ? 303 GLU A CG  1 
ATOM   2460 C  CD  . GLU A 1 303 ? 48.06900 -25.01300 91.89500 1.000 39.99000 ? 303 GLU A CD  1 
ATOM   2461 O  OE1 . GLU A 1 303 ? 48.42000 -26.14500 92.09600 1.000 42.71000 ? 303 GLU A OE1 1 
ATOM   2462 O  OE2 . GLU A 1 303 ? 48.78400 -24.05700 92.06800 1.000 48.53000 ? 303 GLU A OE2 1 
ATOM   2463 N  N   . PHE A 1 304 ? 46.36200 -28.98000 89.36900 1.000 33.15000 ? 304 PHE A N   1 
ATOM   2464 C  CA  . PHE A 1 304 ? 45.72800 -30.26000 89.00600 1.000 33.13000 ? 304 PHE A CA  1 
ATOM   2465 C  C   . PHE A 1 304 ? 45.44500 -31.14000 90.22000 1.000 42.82000 ? 304 PHE A C   1 
ATOM   2466 O  O   . PHE A 1 304 ? 46.16100 -31.15000 91.17800 1.000 38.60000 ? 304 PHE A O   1 
ATOM   2467 C  CB  . PHE A 1 304 ? 46.61100 -31.04500 88.04600 1.000 35.12000 ? 304 PHE A CB  1 
ATOM   2468 C  CG  . PHE A 1 304 ? 46.65400 -30.42500 86.68800 1.000 39.94000 ? 304 PHE A CG  1 
ATOM   2469 C  CD1 . PHE A 1 304 ? 45.72200 -30.75000 85.73500 1.000 40.05000 ? 304 PHE A CD1 1 
ATOM   2470 C  CD2 . PHE A 1 304 ? 47.56600 -29.43700 86.40200 1.000 39.68000 ? 304 PHE A CD2 1 
ATOM   2471 C  CE1 . PHE A 1 304 ? 45.74900 -30.13300 84.50200 1.000 48.78000 ? 304 PHE A CE1 1 
ATOM   2472 C  CE2 . PHE A 1 304 ? 47.59400 -28.83000 85.16800 1.000 38.22000 ? 304 PHE A CE2 1 
ATOM   2473 C  CZ  . PHE A 1 304 ? 46.67900 -29.16900 84.22800 1.000 41.12000 ? 304 PHE A CZ  1 
ATOM   2474 N  N   . LYS A 1 305 ? 44.34800 -31.86100 90.11700 1.000 46.11000 ? 305 LYS A N   1 
ATOM   2475 C  CA  . LYS A 1 305 ? 43.97100 -32.87500 91.11900 1.000 53.58000 ? 305 LYS A CA  1 
ATOM   2476 C  C   . LYS A 1 305 ? 44.17300 -34.24200 90.47500 1.000 50.06000 ? 305 LYS A C   1 
ATOM   2477 O  O   . LYS A 1 305 ? 44.23300 -34.33100 89.26200 1.000 53.39000 ? 305 LYS A O   1 
ATOM   2478 C  CB  . LYS A 1 305 ? 42.52500 -32.68500 91.56300 1.000 44.82000 ? 305 LYS A CB  1 
ATOM   2479 C  CG  . LYS A 1 305 ? 42.29000 -31.46700 92.42800 1.000 52.24000 ? 305 LYS A CG  1 
ATOM   2480 C  CD  . LYS A 1 305 ? 43.39800 -31.19500 93.42600 1.000 60.70000 ? 305 LYS A CD  1 
ATOM   2481 C  CE  . LYS A 1 305 ? 43.52300 -29.73900 93.81300 1.000 64.15000 ? 305 LYS A CE  1 
ATOM   2482 N  NZ  . LYS A 1 305 ? 44.54300 -29.03400 93.00900 1.000 55.96000 ? 305 LYS A NZ  1 
ATOM   2483 N  N   . SER A 1 306 ? 44.22300 -35.28000 91.27900 1.000 46.68000 ? 306 SER A N   1 
ATOM   2484 C  CA  . SER A 1 306 ? 44.40900 -36.65000 90.76100 1.000 52.42000 ? 306 SER A CA  1 
ATOM   2485 C  C   . SER A 1 306 ? 43.34900 -36.98700 89.72600 1.000 56.01000 ? 306 SER A C   1 
ATOM   2486 O  O   . SER A 1 306 ? 42.17100 -36.68300 89.91300 1.000 54.50000 ? 306 SER A O   1 
ATOM   2487 C  CB  . SER A 1 306 ? 44.36800 -37.63700 91.86500 1.000 49.64000 ? 306 SER A CB  1 
ATOM   2488 O  OG  . SER A 1 306 ? 45.55300 -37.52600 92.59600 1.000 64.27000 ? 306 SER A OG  1 
ATOM   2489 N  N   . GLY A 1 307 ? 43.77100 -37.63800 88.66400 1.000 60.52000 ? 307 GLY A N   1 
ATOM   2490 C  CA  . GLY A 1 307 ? 42.74700 -37.97400 87.67900 1.000 59.32000 ? 307 GLY A CA  1 
ATOM   2491 C  C   . GLY A 1 307 ? 43.26100 -38.00800 86.27300 1.000 57.02000 ? 307 GLY A C   1 
ATOM   2492 O  O   . GLY A 1 307 ? 43.47900 -36.97000 85.70100 1.000 62.04000 ? 307 GLY A O   1 
ATOM   2493 N  N   . GLY A 1 308 ? 43.48200 -39.19800 85.76600 1.000 56.07000 ? 308 GLY A N   1 
ATOM   2494 C  CA  . GLY A 1 308 ? 43.79300 -39.26400 84.34200 1.000 62.19000 ? 308 GLY A CA  1 
ATOM   2495 C  C   . GLY A 1 308 ? 45.24400 -39.14200 83.98000 1.000 62.34000 ? 308 GLY A C   1 
ATOM   2496 O  O   . GLY A 1 308 ? 46.11100 -39.25000 84.84800 1.000 56.67000 ? 308 GLY A O   1 
ATOM   2497 N  N   . ILE A 1 309 ? 45.44100 -38.91500 82.69100 1.000 56.70000 ? 309 ILE A N   1 
ATOM   2498 C  CA  . ILE A 1 309 ? 46.79100 -38.86700 82.10300 1.000 55.28000 ? 309 ILE A CA  1 
ATOM   2499 C  C   . ILE A 1 309 ? 46.98900 -37.51100 81.45800 1.000 56.80000 ? 309 ILE A C   1 
ATOM   2500 O  O   . ILE A 1 309 ? 46.04000 -36.97600 80.94800 1.000 62.04000 ? 309 ILE A O   1 
ATOM   2501 C  CB  . ILE A 1 309 ? 46.92500 -39.98500 81.06400 1.000 56.24000 ? 309 ILE A CB  1 
ATOM   2502 C  CG1 . ILE A 1 309 ? 46.32300 -41.29200 81.56900 1.000 61.49000 ? 309 ILE A CG1 1 
ATOM   2503 C  CG2 . ILE A 1 309 ? 48.38000 -40.16400 80.67700 1.000 63.12000 ? 309 ILE A CG2 1 
ATOM   2504 C  CD1 . ILE A 1 309 ? 47.28100 -42.15100 82.34400 1.000 68.86000 ? 309 ILE A CD1 1 
ATOM   2505 N  N   . TYR A 1 310 ? 48.20600 -37.00700 81.51200 1.000 53.09000 ? 310 TYR A N   1 
ATOM   2506 C  CA  . TYR A 1 310 ? 48.53500 -35.73600 80.83500 1.000 57.30000 ? 310 TYR A CA  1 
ATOM   2507 C  C   . TYR A 1 310 ? 48.70300 -36.09900 79.35000 1.000 59.13000 ? 310 TYR A C   1 
ATOM   2508 O  O   . TYR A 1 310 ? 49.43900 -37.02900 79.03100 1.000 50.15000 ? 310 TYR A O   1 
ATOM   2509 C  CB  . TYR A 1 310 ? 49.65700 -35.02300 81.60100 1.000 55.84000 ? 310 TYR A CB  1 
ATOM   2510 C  CG  . TYR A 1 310 ? 49.78700 -33.52700 81.43300 1.000 63.10000 ? 310 TYR A CG  1 
ATOM   2511 C  CD1 . TYR A 1 310 ? 50.51700 -33.00300 80.38500 1.000 78.31000 ? 310 TYR A CD1 1 
ATOM   2512 C  CD2 . TYR A 1 310 ? 49.21600 -32.62100 82.31000 1.000 59.01000 ? 310 TYR A CD2 1 
ATOM   2513 C  CE1 . TYR A 1 310 ? 50.69500 -31.63800 80.21000 1.000 70.83000 ? 310 TYR A CE1 1 
ATOM   2514 C  CE2 . TYR A 1 310 ? 49.36900 -31.24900 82.14000 1.000 60.32000 ? 310 TYR A CE2 1 
ATOM   2515 C  CZ  . TYR A 1 310 ? 50.12400 -30.75400 81.09300 1.000 57.75000 ? 310 TYR A CZ  1 
ATOM   2516 O  OH  . TYR A 1 310 ? 50.30200 -29.44300 80.85700 1.000 42.56000 ? 310 TYR A OH  1 
ATOM   2517 N  N   . ASP A 1 311 ? 47.95300 -35.41800 78.48400 1.000 59.50000 ? 311 ASP A N   1 
ATOM   2518 C  CA  . ASP A 1 311 ? 47.92800 -35.65400 77.02100 1.000 50.80000 ? 311 ASP A CA  1 
ATOM   2519 C  C   . ASP A 1 311 ? 49.30900 -35.41700 76.43700 1.000 57.57000 ? 311 ASP A C   1 
ATOM   2520 O  O   . ASP A 1 311 ? 49.98700 -34.50900 76.88100 1.000 60.81000 ? 311 ASP A O   1 
ATOM   2521 C  CB  . ASP A 1 311 ? 46.86300 -34.80700 76.33500 1.000 61.34000 ? 311 ASP A CB  1 
ATOM   2522 C  CG  . ASP A 1 311 ? 45.52100 -35.52300 76.22400 1.000 70.39000 ? 311 ASP A CG  1 
ATOM   2523 O  OD1 . ASP A 1 311 ? 45.49600 -36.76600 76.33400 1.000 64.15000 ? 311 ASP A OD1 1 
ATOM   2524 O  OD2 . ASP A 1 311 ? 44.51900 -34.83400 76.04500 1.000 70.50000 ? 311 ASP A OD2 1 
ATOM   2525 N  N   . GLY A 1 312 ? 49.78200 -36.31800 75.58200 1.000 55.05000 ? 312 GLY A N   1 
ATOM   2526 C  CA  . GLY A 1 312 ? 51.11800 -36.17700 74.97600 1.000 47.05000 ? 312 GLY A CA  1 
ATOM   2527 C  C   . GLY A 1 312 ? 52.23500 -36.74400 75.83500 1.000 54.79000 ? 312 GLY A C   1 
ATOM   2528 O  O   . GLY A 1 312 ? 53.05200 -37.47300 75.31500 1.000 46.61000 ? 312 GLY A O   1 
ATOM   2529 N  N   . LEU A 1 313 ? 52.29700 -36.33700 77.10000 1.000 54.86000 ? 313 LEU A N   1 
ATOM   2530 C  CA  . LEU A 1 313 ? 53.33000 -36.78200 78.05400 1.000 57.83000 ? 313 LEU A CA  1 
ATOM   2531 C  C   . LEU A 1 313 ? 53.05600 -38.24100 78.41500 1.000 53.60000 ? 313 LEU A C   1 
ATOM   2532 O  O   . LEU A 1 313 ? 54.01700 -38.92200 78.67900 1.000 49.93000 ? 313 LEU A O   1 
ATOM   2533 C  CB  . LEU A 1 313 ? 53.29500 -35.87500 79.28700 1.000 45.75000 ? 313 LEU A CB  1 
ATOM   2534 C  CG  . LEU A 1 313 ? 53.47800 -34.38300 79.02800 1.000 45.68000 ? 313 LEU A CG  1 
ATOM   2535 C  CD1 . LEU A 1 313 ? 53.83600 -33.65100 80.30100 1.000 49.47000 ? 313 LEU A CD1 1 
ATOM   2536 C  CD2 . LEU A 1 313 ? 54.55400 -34.17000 78.01200 1.000 35.98000 ? 313 LEU A CD2 1 
ATOM   2537 N  N   . ASN A 1 314 ? 51.78000 -38.64000 78.43000 1.000 52.45000 ? 314 ASN A N   1 
ATOM   2538 C  CA  . ASN A 1 314 ? 51.30600 -40.00200 78.80100 1.000 54.69000 ? 314 ASN A CA  1 
ATOM   2539 C  C   . ASN A 1 314 ? 51.66700 -40.28600 80.26100 1.000 56.92000 ? 314 ASN A C   1 
ATOM   2540 O  O   . ASN A 1 314 ? 51.97700 -41.41000 80.60100 1.000 49.10000 ? 314 ASN A O   1 
ATOM   2541 C  CB  . ASN A 1 314 ? 51.77800 -41.06200 77.81500 1.000 52.91000 ? 314 ASN A CB  1 
ATOM   2542 C  CG  . ASN A 1 314 ? 51.22700 -40.81700 76.43000 1.000 65.25000 ? 314 ASN A CG  1 
ATOM   2543 O  OD1 . ASN A 1 314 ? 50.02700 -40.62100 76.26300 1.000 65.98000 ? 314 ASN A OD1 1 
ATOM   2544 N  ND2 . ASN A 1 314 ? 52.09100 -40.80900 75.43600 1.000 56.43000 ? 314 ASN A ND2 1 
ATOM   2545 N  N   . LEU A 1 315 ? 51.53700 -39.26300 81.08800 1.000 58.51000 ? 315 LEU A N   1 
ATOM   2546 C  CA  . LEU A 1 315 ? 51.92000 -39.33000 82.50800 1.000 55.30000 ? 315 LEU A CA  1 
ATOM   2547 C  C   . LEU A 1 315 ? 50.66400 -39.19400 83.34000 1.000 53.16000 ? 315 LEU A C   1 
ATOM   2548 O  O   . LEU A 1 315 ? 49.80600 -38.43700 82.96300 1.000 49.58000 ? 315 LEU A O   1 
ATOM   2549 C  CB  . LEU A 1 315 ? 52.86000 -38.16100 82.78000 1.000 53.37000 ? 315 LEU A CB  1 
ATOM   2550 C  CG  . LEU A 1 315 ? 54.19400 -38.24700 82.05600 1.000 52.89000 ? 315 LEU A CG  1 
ATOM   2551 C  CD1 . LEU A 1 315 ? 54.95500 -36.95300 82.19600 1.000 51.12000 ? 315 LEU A CD1 1 
ATOM   2552 C  CD2 . LEU A 1 315 ? 55.02200 -39.37300 82.61600 1.000 51.10000 ? 315 LEU A CD2 1 
ATOM   2553 N  N   . LYS A 1 316 ? 50.61500 -39.92700 84.43900 1.000 55.72000 ? 316 LYS A N   1 
ATOM   2554 C  CA  . LYS A 1 316 ? 49.45400 -39.91800 85.34900 1.000 50.21000 ? 316 LYS A CA  1 
ATOM   2555 C  C   . LYS A 1 316 ? 49.39000 -38.58400 86.08100 1.000 46.34000 ? 316 LYS A C   1 
ATOM   2556 O  O   . LYS A 1 316 ? 50.40300 -38.09400 86.48000 1.000 51.18000 ? 316 LYS A O   1 
ATOM   2557 C  CB  . LYS A 1 316 ? 49.60400 -41.07500 86.33000 1.000 53.88000 ? 316 LYS A CB  1 
ATOM   2558 C  CG  . LYS A 1 316 ? 48.64900 -41.01200 87.50800 1.000 64.54000 ? 316 LYS A CG  1 
ATOM   2559 C  CD  . LYS A 1 316 ? 47.20500 -41.15300 87.13800 1.000 63.16000 ? 316 LYS A CD  1 
ATOM   2560 C  CE  . LYS A 1 316 ? 46.38000 -41.67600 88.29500 1.000 61.18000 ? 316 LYS A CE  1 
ATOM   2561 N  NZ  . LYS A 1 316 ? 46.95800 -42.91900 88.83700 1.000 53.54000 ? 316 LYS A NZ  1 
ATOM   2562 N  N   . ILE A 1 317 ? 48.20100 -38.04800 86.25700 1.000 47.27000 ? 317 ILE A N   1 
ATOM   2563 C  CA  . ILE A 1 317 ? 48.04500 -36.74500 86.94700 1.000 44.08000 ? 317 ILE A CA  1 
ATOM   2564 C  C   . ILE A 1 317 ? 47.91500 -36.98500 88.45000 1.000 42.98000 ? 317 ILE A C   1 
ATOM   2565 O  O   . ILE A 1 317 ? 47.07900 -37.72100 88.85600 1.000 47.25000 ? 317 ILE A O   1 
ATOM   2566 C  CB  . ILE A 1 317 ? 46.86300 -35.99100 86.32400 1.000 47.30000 ? 317 ILE A CB  1 
ATOM   2567 C  CG1 . ILE A 1 317 ? 47.13300 -35.69000 84.85200 1.000 47.85000 ? 317 ILE A CG1 1 
ATOM   2568 C  CG2 . ILE A 1 317 ? 46.58800 -34.74300 87.10900 1.000 49.49000 ? 317 ILE A CG2 1 
ATOM   2569 C  CD1 . ILE A 1 317 ? 46.02200 -35.00500 84.13000 1.000 45.12000 ? 317 ILE A CD1 1 
ATOM   2570 N  N   . GLU A 1 318 ? 48.75300 -36.35800 89.24800 1.000 41.69000 ? 318 GLU A N   1 
ATOM   2571 C  CA  . GLU A 1 318 ? 48.71100 -36.63400 90.69500 1.000 40.21000 ? 318 GLU A CA  1 
ATOM   2572 C  C   . GLU A 1 318 ? 48.30800 -35.38400 91.47000 1.000 45.04000 ? 318 GLU A C   1 
ATOM   2573 O  O   . GLU A 1 318 ? 48.45600 -34.31800 90.93900 1.000 39.46000 ? 318 GLU A O   1 
ATOM   2574 C  CB  . GLU A 1 318 ? 50.06700 -37.16400 91.14300 1.000 44.01000 ? 318 GLU A CB  1 
ATOM   2575 C  CG  . GLU A 1 318 ? 50.48900 -38.41900 90.43300 1.000 45.11000 ? 318 GLU A CG  1 
ATOM   2576 C  CD  . GLU A 1 318 ? 49.83900 -39.70300 90.90500 1.000 59.60000 ? 318 GLU A CD  1 
ATOM   2577 O  OE1 . GLU A 1 318 ? 48.79600 -39.65300 91.55500 1.000 58.43000 ? 318 GLU A OE1 1 
ATOM   2578 O  OE2 . GLU A 1 318 ? 50.37000 -40.75800 90.58200 1.000 66.85000 ? 318 GLU A OE2 1 
ATOM   2579 N  N   . ASP A 1 319 ? 47.85600 -35.56100 92.70700 1.000 44.02000 ? 319 ASP A N   1 
ATOM   2580 C  CA  . ASP A 1 319 ? 47.43600 -34.42200 93.55000 1.000 41.66000 ? 319 ASP A CA  1 
ATOM   2581 C  C   . ASP A 1 319 ? 48.59300 -33.46000 93.72200 1.000 39.51000 ? 319 ASP A C   1 
ATOM   2582 O  O   . ASP A 1 319 ? 49.66300 -33.89200 93.97900 1.000 41.92000 ? 319 ASP A O   1 
ATOM   2583 C  CB  . ASP A 1 319 ? 46.91000 -34.85900 94.90800 1.000 50.23000 ? 319 ASP A CB  1 
ATOM   2584 C  CG  . ASP A 1 319 ? 45.48800 -35.39200 94.88000 1.000 58.82000 ? 319 ASP A CG  1 
ATOM   2585 O  OD1 . ASP A 1 319 ? 44.72100 -34.98900 94.02200 1.000 49.84000 ? 319 ASP A OD1 1 
ATOM   2586 O  OD2 . ASP A 1 319 ? 45.16800 -36.19800 95.73400 1.000 63.69000 ? 319 ASP A OD2 1 
ATOM   2587 N  N   . GLY A 1 320 ? 48.32600 -32.18000 93.54400 1.000 42.98000 ? 320 GLY A N   1 
ATOM   2588 C  CA  . GLY A 1 320 ? 49.35600 -31.15800 93.73500 1.000 39.76000 ? 320 GLY A CA  1 
ATOM   2589 C  C   . GLY A 1 320 ? 50.16500 -30.90600 92.48900 1.000 33.74000 ? 320 GLY A C   1 
ATOM   2590 O  O   . GLY A 1 320 ? 50.96300 -30.03500 92.52400 1.000 32.52000 ? 320 GLY A O   1 
ATOM   2591 N  N   . ASP A 1 321 ? 49.87700 -31.60600 91.40300 1.000 32.36000 ? 321 ASP A N   1 
ATOM   2592 C  CA  . ASP A 1 321 ? 50.58200 -31.35800 90.12600 1.000 35.92000 ? 321 ASP A CA  1 
ATOM   2593 C  C   . ASP A 1 321 ? 50.18900 -29.98000 89.62200 1.000 31.05000 ? 321 ASP A C   1 
ATOM   2594 O  O   . ASP A 1 321 ? 49.06700 -29.57800 89.80900 1.000 37.90000 ? 321 ASP A O   1 
ATOM   2595 C  CB  . ASP A 1 321 ? 50.22800 -32.35100 89.02700 1.000 35.34000 ? 321 ASP A CB  1 
ATOM   2596 C  CG  . ASP A 1 321 ? 50.99600 -33.64500 89.08700 1.000 37.83000 ? 321 ASP A CG  1 
ATOM   2597 O  OD1 . ASP A 1 321 ? 51.77000 -33.80100 89.97300 1.000 41.69000 ? 321 ASP A OD1 1 
ATOM   2598 O  OD2 . ASP A 1 321 ? 50.77500 -34.47700 88.26200 1.000 41.92000 ? 321 ASP A OD2 1 
ATOM   2599 N  N   . TYR A 1 322 ? 51.11500 -29.30000 88.99900 1.000 31.28000 ? 322 TYR A N   1 
ATOM   2600 C  CA  . TYR A 1 322 ? 50.77600 -27.98600 88.44500 1.000 29.98000 ? 322 TYR A CA  1 
ATOM   2601 C  C   . TYR A 1 322 ? 51.46900 -27.77900 87.10800 1.000 32.75000 ? 322 TYR A C   1 
ATOM   2602 O  O   . TYR A 1 322 ? 52.45200 -28.37800 86.82300 1.000 29.03000 ? 322 TYR A O   1 
ATOM   2603 C  CB  . TYR A 1 322 ? 51.05400 -26.87500 89.44000 1.000 31.50000 ? 322 TYR A CB  1 
ATOM   2604 C  CG  . TYR A 1 322 ? 52.50500 -26.62300 89.71500 1.000 28.74000 ? 322 TYR A CG  1 
ATOM   2605 C  CD1 . TYR A 1 322 ? 53.22500 -25.74600 88.94600 1.000 27.47000 ? 322 TYR A CD1 1 
ATOM   2606 C  CD2 . TYR A 1 322 ? 53.14700 -27.26600 90.74400 1.000 30.64000 ? 322 TYR A CD2 1 
ATOM   2607 C  CE1 . TYR A 1 322 ? 54.55300 -25.50000 89.19400 1.000 32.54000 ? 322 TYR A CE1 1 
ATOM   2608 C  CE2 . TYR A 1 322 ? 54.47700 -27.03000 91.01400 1.000 29.03000 ? 322 TYR A CE2 1 
ATOM   2609 C  CZ  . TYR A 1 322 ? 55.17900 -26.14200 90.23900 1.000 28.22000 ? 322 TYR A CZ  1 
ATOM   2610 O  OH  . TYR A 1 322 ? 56.47500 -25.91200 90.47700 1.000 30.13000 ? 322 TYR A OH  1 
ATOM   2611 N  N   . ASP A 1 323 ? 50.92000 -26.84700 86.37100 1.000 27.51000 ? 323 ASP A N   1 
ATOM   2612 C  CA  . ASP A 1 323 ? 51.37400 -26.48000 85.02700 1.000 31.78000 ? 323 ASP A CA  1 
ATOM   2613 C  C   . ASP A 1 323 ? 51.74200 -25.01100 85.04200 1.000 33.42000 ? 323 ASP A C   1 
ATOM   2614 O  O   . ASP A 1 323 ? 50.97600 -24.26100 85.61500 1.000 29.51000 ? 323 ASP A O   1 
ATOM   2615 C  CB  . ASP A 1 323 ? 50.15900 -26.59400 84.11800 1.000 32.83000 ? 323 ASP A CB  1 
ATOM   2616 C  CG  . ASP A 1 323 ? 50.43000 -26.49900 82.64900 1.000 38.77000 ? 323 ASP A CG  1 
ATOM   2617 O  OD1 . ASP A 1 323 ? 51.50800 -26.06300 82.26300 1.000 42.06000 ? 323 ASP A OD1 1 
ATOM   2618 O  OD2 . ASP A 1 323 ? 49.57400 -26.87400 81.92900 1.000 39.90000 ? 323 ASP A OD2 1 
ATOM   2619 N  N   . LEU A 1 324 ? 52.90500 -24.69100 84.49600 1.000 26.09000 ? 324 LEU A N   1 
ATOM   2620 C  CA  . LEU A 1 324 ? 53.32400 -23.29900 84.24700 1.000 28.28000 ? 324 LEU A CA  1 
ATOM   2621 C  C   . LEU A 1 324 ? 53.21200 -23.11100 82.73500 1.000 28.44000 ? 324 LEU A C   1 
ATOM   2622 O  O   . LEU A 1 324 ? 53.92900 -23.76200 82.00400 1.000 28.37000 ? 324 LEU A O   1 
ATOM   2623 C  CB  . LEU A 1 324 ? 54.74100 -23.04500 84.74400 1.000 31.16000 ? 324 LEU A CB  1 
ATOM   2624 C  CG  . LEU A 1 324 ? 54.89000 -22.90900 86.24700 1.000 34.03000 ? 324 LEU A CG  1 
ATOM   2625 C  CD1 . LEU A 1 324 ? 56.33400 -22.76400 86.62400 1.000 28.33000 ? 324 LEU A CD1 1 
ATOM   2626 C  CD2 . LEU A 1 324 ? 54.11100 -21.72100 86.73700 1.000 36.16000 ? 324 LEU A CD2 1 
ATOM   2627 N  N   . VAL A 1 325 ? 52.26100 -22.29500 82.33700 1.000 26.51000 ? 325 VAL A N   1 
ATOM   2628 C  CA  . VAL A 1 325 ? 51.93500 -22.05200 80.91500 1.000 27.60000 ? 325 VAL A CA  1 
ATOM   2629 C  C   . VAL A 1 325 ? 52.34600 -20.65400 80.51700 1.000 26.53000 ? 325 VAL A C   1 
ATOM   2630 O  O   . VAL A 1 325 ? 51.81500 -19.71900 81.05000 1.000 30.04000 ? 325 VAL A O   1 
ATOM   2631 C  CB  . VAL A 1 325 ? 50.44300 -22.21800 80.61100 1.000 29.77000 ? 325 VAL A CB  1 
ATOM   2632 C  CG1 . VAL A 1 325 ? 50.20700 -22.12500 79.12800 1.000 28.97000 ? 325 VAL A CG1 1 
ATOM   2633 C  CG2 . VAL A 1 325 ? 49.90300 -23.50000 81.14400 1.000 33.16000 ? 325 VAL A CG2 1 
ATOM   2634 N  N   . GLU A 1 326 ? 53.20300 -20.58100 79.52900 1.000 29.75000 ? 326 GLU A N   1 
ATOM   2635 C  CA  . GLU A 1 326 ? 53.64800 -19.28900 78.99600 1.000 32.09000 ? 326 GLU A CA  1 
ATOM   2636 C  C   . GLU A 1 326 ? 52.95000 -19.02200 77.67400 1.000 31.15000 ? 326 GLU A C   1 
ATOM   2637 O  O   . GLU A 1 326 ? 53.02100 -19.83000 76.79100 1.000 28.26000 ? 326 GLU A O   1 
ATOM   2638 C  CB  . GLU A 1 326 ? 55.15000 -19.28000 78.79700 1.000 32.78000 ? 326 GLU A CB  1 
ATOM   2639 C  CG  . GLU A 1 326 ? 55.89400 -18.93500 80.05000 1.000 50.53000 ? 326 GLU A CG  1 
ATOM   2640 C  CD  . GLU A 1 326 ? 57.39200 -18.80600 79.89700 1.000 59.45000 ? 326 GLU A CD  1 
ATOM   2641 O  OE1 . GLU A 1 326 ? 57.98700 -19.68300 79.28900 1.000 60.94000 ? 326 GLU A OE1 1 
ATOM   2642 O  OE2 . GLU A 1 326 ? 57.93900 -17.83000 80.40800 1.000 62.52000 ? 326 GLU A OE2 1 
ATOM   2643 N  N   . LEU A 1 327 ? 52.26800 -17.90800 77.59600 1.000 29.34000 ? 327 LEU A N   1 
ATOM   2644 C  CA  . LEU A 1 327 ? 51.65700 -17.55800 76.30800 1.000 33.82000 ? 327 LEU A CA  1 
ATOM   2645 C  C   . LEU A 1 327 ? 51.93900 -16.10700 75.93500 1.000 33.68000 ? 327 LEU A C   1 
ATOM   2646 O  O   . LEU A 1 327 ? 52.17600 -15.30300 76.78600 1.000 32.64000 ? 327 LEU A O   1 
ATOM   2647 C  CB  . LEU A 1 327 ? 50.20100 -17.96700 76.26800 1.000 29.94000 ? 327 LEU A CB  1 
ATOM   2648 C  CG  . LEU A 1 327 ? 49.32400 -17.35700 77.32500 1.000 39.35000 ? 327 LEU A CG  1 
ATOM   2649 C  CD1 . LEU A 1 327 ? 48.58200 -16.19200 76.71300 1.000 38.70000 ? 327 LEU A CD1 1 
ATOM   2650 C  CD2 . LEU A 1 327 ? 48.36600 -18.40800 77.81300 1.000 34.80000 ? 327 LEU A CD2 1 
ATOM   2651 N  N   . ASP A 1 328 ? 51.92600 -15.84400 74.65300 1.000 27.87000 ? 328 ASP A N   1 
ATOM   2652 C  CA  . ASP A 1 328 ? 52.36200 -14.53800 74.13400 1.000 28.74000 ? 328 ASP A CA  1 
ATOM   2653 C  C   . ASP A 1 328 ? 51.59400 -14.27600 72.85100 1.000 25.70000 ? 328 ASP A C   1 
ATOM   2654 O  O   . ASP A 1 328 ? 51.64800 -15.07200 71.96800 1.000 25.77000 ? 328 ASP A O   1 
ATOM   2655 C  CB  . ASP A 1 328 ? 53.87000 -14.58900 73.88900 1.000 27.99000 ? 328 ASP A CB  1 
ATOM   2656 C  CG  . ASP A 1 328 ? 54.56300 -13.27700 73.58500 1.000 33.43000 ? 328 ASP A CG  1 
ATOM   2657 O  OD1 . ASP A 1 328 ? 54.02900 -12.49800 72.84100 1.000 32.46000 ? 328 ASP A OD1 1 
ATOM   2658 O  OD2 . ASP A 1 328 ? 55.63400 -13.08200 74.09200 1.000 33.43000 ? 328 ASP A OD2 1 
ATOM   2659 N  N   . SER A 1 329 ? 51.07100 -13.07200 72.72100 1.000 27.96000 ? 329 SER A N   1 
ATOM   2660 C  CA  . SER A 1 329 ? 50.29700 -12.60500 71.55300 1.000 25.47000 ? 329 SER A CA  1 
ATOM   2661 C  C   . SER A 1 329 ? 51.09300 -12.69600 70.23700 1.000 30.21000 ? 329 SER A C   1 
ATOM   2662 O  O   . SER A 1 329 ? 50.47000 -12.75400 69.24300 1.000 23.37000 ? 329 SER A O   1 
ATOM   2663 C  CB  . SER A 1 329 ? 49.79700 -11.22700 71.80100 1.000 27.07000 ? 329 SER A CB  1 
ATOM   2664 O  OG  . SER A 1 329 ? 50.85800 -10.32800 71.90900 1.000 27.36000 ? 329 SER A OG  1 
ATOM   2665 N  N   . ARG A 1 330 ? 52.41900 -12.60200 70.28600 1.000 24.65000 ? 330 ARG A N   1 
ATOM   2666 C  CA  . ARG A 1 330 ? 53.36000 -12.68200 69.15300 1.000 33.74000 ? 330 ARG A CA  1 
ATOM   2667 C  C   . ARG A 1 330 ? 53.75800 -14.13400 68.87000 1.000 31.70000 ? 330 ARG A C   1 
ATOM   2668 O  O   . ARG A 1 330 ? 54.41600 -14.35200 67.89100 1.000 30.54000 ? 330 ARG A O   1 
ATOM   2669 C  CB  . ARG A 1 330 ? 54.61000 -11.88800 69.53900 1.000 31.52000 ? 330 ARG A CB  1 
ATOM   2670 C  CG  . ARG A 1 330 ? 54.32400 -10.42700 69.82900 1.000 30.54000 ? 330 ARG A CG  1 
ATOM   2671 C  CD  . ARG A 1 330 ? 55.42400 -9.75600  70.58300 1.000 28.94000 ? 330 ARG A CD  1 
ATOM   2672 N  NE  . ARG A 1 330 ? 55.54400 -10.34000 71.89000 1.000 36.38000 ? 330 ARG A NE  1 
ATOM   2673 C  CZ  . ARG A 1 330 ? 56.37100 -9.91800  72.82900 1.000 40.63000 ? 330 ARG A CZ  1 
ATOM   2674 N  NH1 . ARG A 1 330 ? 57.18000 -8.90600  72.59600 1.000 37.17000 ? 330 ARG A NH1 1 
ATOM   2675 N  NH2 . ARG A 1 330 ? 56.39500 -10.51300 73.99400 1.000 34.10000 ? 330 ARG A NH2 1 
ATOM   2676 N  N   . ASN A 1 331 ? 53.37700 -15.06400 69.73100 1.000 25.52000 ? 331 ASN A N   1 
ATOM   2677 C  CA  . ASN A 1 331 ? 53.80600 -16.46100 69.55900 1.000 25.22000 ? 331 ASN A CA  1 
ATOM   2678 C  C   . ASN A 1 331 ? 52.66100 -17.36000 69.10300 1.000 26.75000 ? 331 ASN A C   1 
ATOM   2679 O  O   . ASN A 1 331 ? 51.62100 -17.33700 69.68600 1.000 24.32000 ? 331 ASN A O   1 
ATOM   2680 C  CB  . ASN A 1 331 ? 54.42700 -17.02500 70.82600 1.000 27.55000 ? 331 ASN A CB  1 
ATOM   2681 C  CG  . ASN A 1 331 ? 55.76900 -16.41800 71.16500 1.000 33.97000 ? 331 ASN A CG  1 
ATOM   2682 O  OD1 . ASN A 1 331 ? 56.38200 -15.76100 70.35300 1.000 34.72000 ? 331 ASN A OD1 1 
ATOM   2683 N  ND2 . ASN A 1 331 ? 56.23700 -16.66600 72.36000 1.000 31.28000 ? 331 ASN A ND2 1 
ATOM   2684 N  N   . TRP A 1 332 ? 52.98200 -18.25800 68.19100 1.000 22.92000 ? 332 TRP A N   1 
ATOM   2685 C  CA  . TRP A 1 332 ? 52.07100 -19.29400 67.65500 1.000 25.64000 ? 332 TRP A CA  1 
ATOM   2686 C  C   . TRP A 1 332 ? 52.22100 -20.59600 68.45800 1.000 25.28000 ? 332 TRP A C   1 
ATOM   2687 O  O   . TRP A 1 332 ? 52.07900 -21.63600 67.88900 1.000 24.65000 ? 332 TRP A O   1 
ATOM   2688 C  CB  . TRP A 1 332 ? 52.36100 -19.52700 66.17300 1.000 20.03000 ? 332 TRP A CB  1 
ATOM   2689 C  CG  . TRP A 1 332 ? 51.91500 -18.42400 65.27000 1.000 21.56000 ? 332 TRP A CG  1 
ATOM   2690 C  CD1 . TRP A 1 332 ? 52.41400 -17.16800 65.19500 1.000 22.52000 ? 332 TRP A CD1 1 
ATOM   2691 C  CD2 . TRP A 1 332 ? 50.88900 -18.49300 64.27600 1.000 21.82000 ? 332 TRP A CD2 1 
ATOM   2692 N  NE1 . TRP A 1 332 ? 51.76700 -16.45100 64.24200 1.000 24.49000 ? 332 TRP A NE1 1 
ATOM   2693 C  CE2 . TRP A 1 332 ? 50.83400 -17.23700 63.65600 1.000 22.26000 ? 332 TRP A CE2 1 
ATOM   2694 C  CE3 . TRP A 1 332 ? 50.04600 -19.50500 63.82900 1.000 21.42000 ? 332 TRP A CE3 1 
ATOM   2695 C  CZ2 . TRP A 1 332 ? 49.94300 -16.95700 62.63500 1.000 25.95000 ? 332 TRP A CZ2 1 
ATOM   2696 C  CZ3 . TRP A 1 332 ? 49.15700 -19.22300 62.83000 1.000 22.74000 ? 332 TRP A CZ3 1 
ATOM   2697 C  CH2 . TRP A 1 332 ? 49.10800 -17.96900 62.24800 1.000 26.53000 ? 332 TRP A CH2 1 
ATOM   2698 N  N   . TYR A 1 333 ? 52.50500 -20.49100 69.74900 1.000 26.30000 ? 333 TYR A N   1 
ATOM   2699 C  CA  . TYR A 1 333 ? 52.73100 -21.64100 70.64600 1.000 28.01000 ? 333 TYR A CA  1 
ATOM   2700 C  C   . TYR A 1 333 ? 52.63500 -21.26300 72.12700 1.000 28.84000 ? 333 TYR A C   1 
ATOM   2701 O  O   . TYR A 1 333 ? 52.91100 -20.15600 72.48300 1.000 24.05000 ? 333 TYR A O   1 
ATOM   2702 C  CB  . TYR A 1 333 ? 54.07200 -22.31000 70.35900 1.000 27.94000 ? 333 TYR A CB  1 
ATOM   2703 C  CG  . TYR A 1 333 ? 55.26500 -21.43600 70.62900 1.000 29.06000 ? 333 TYR A CG  1 
ATOM   2704 C  CD1 . TYR A 1 333 ? 55.86900 -21.41900 71.86600 1.000 26.26000 ? 333 TYR A CD1 1 
ATOM   2705 C  CD2 . TYR A 1 333 ? 55.75300 -20.59700 69.66200 1.000 24.56000 ? 333 TYR A CD2 1 
ATOM   2706 C  CE1 . TYR A 1 333 ? 56.95500 -20.61400 72.12900 1.000 28.45000 ? 333 TYR A CE1 1 
ATOM   2707 C  CE2 . TYR A 1 333 ? 56.83500 -19.78100 69.90400 1.000 30.43000 ? 333 TYR A CE2 1 
ATOM   2708 C  CZ  . TYR A 1 333 ? 57.44000 -19.79200 71.14200 1.000 37.05000 ? 333 TYR A CZ  1 
ATOM   2709 O  OH  . TYR A 1 333 ? 58.48600 -18.99000 71.40000 1.000 34.66000 ? 333 TYR A OH  1 
ATOM   2710 N  N   . GLN A 1 334 ? 52.24600 -22.23000 72.94000 1.000 26.85000 ? 334 GLN A N   1 
ATOM   2711 C  CA  . GLN A 1 334 ? 52.23200 -22.10100 74.41400 1.000 27.29000 ? 334 GLN A CA  1 
ATOM   2712 C  C   . GLN A 1 334 ? 53.08400 -23.22100 75.00000 1.000 25.36000 ? 334 GLN A C   1 
ATOM   2713 O  O   . GLN A 1 334 ? 52.88000 -24.34900 74.64700 1.000 26.19000 ? 334 GLN A O   1 
ATOM   2714 C  CB  . GLN A 1 334 ? 50.83700 -22.02700 75.01600 1.000 24.74000 ? 334 GLN A CB  1 
ATOM   2715 C  CG  . GLN A 1 334 ? 49.97700 -20.94300 74.42000 1.000 23.96000 ? 334 GLN A CG  1 
ATOM   2716 C  CD  . GLN A 1 334 ? 49.33900 -21.34900 73.12000 1.000 25.70000 ? 334 GLN A CD  1 
ATOM   2717 O  OE1 . GLN A 1 334 ? 48.88100 -22.44500 72.96400 1.000 27.79000 ? 334 GLN A OE1 1 
ATOM   2718 N  NE2 . GLN A 1 334 ? 49.32300 -20.45000 72.17800 1.000 26.50000 ? 334 GLN A NE2 1 
ATOM   2719 N  N   . ILE A 1 335 ? 54.03900 -22.85100 75.83400 1.000 27.54000 ? 335 ILE A N   1 
ATOM   2720 C  CA  . ILE A 1 335 ? 54.93800 -23.80900 76.52100 1.000 24.49000 ? 335 ILE A CA  1 
ATOM   2721 C  C   . ILE A 1 335 ? 54.33200 -24.15900 77.87300 1.000 31.08000 ? 335 ILE A C   1 
ATOM   2722 O  O   . ILE A 1 335 ? 54.18600 -23.27600 78.68900 1.000 29.70000 ? 335 ILE A O   1 
ATOM   2723 C  CB  . ILE A 1 335 ? 56.34100 -23.22400 76.70300 1.000 30.74000 ? 335 ILE A CB  1 
ATOM   2724 C  CG1 . ILE A 1 335 ? 56.85900 -22.59200 75.42100 1.000 30.39000 ? 335 ILE A CG1 1 
ATOM   2725 C  CG2 . ILE A 1 335 ? 57.29600 -24.26400 77.23900 1.000 30.78000 ? 335 ILE A CG2 1 
ATOM   2726 C  CD1 . ILE A 1 335 ? 58.30500 -22.33200 75.47600 1.000 45.83000 ? 335 ILE A CD1 1 
ATOM   2727 N  N   . HIS A 1 336 ? 53.95800 -25.41400 78.03300 1.000 26.24000 ? 336 HIS A N   1 
ATOM   2728 C  CA  . HIS A 1 336 ? 53.41400 -25.95000 79.29600 1.000 25.47000 ? 336 HIS A CA  1 
ATOM   2729 C  C   . HIS A 1 336 ? 54.52300 -26.72800 80.00400 1.000 27.34000 ? 336 HIS A C   1 
ATOM   2730 O  O   . HIS A 1 336 ? 55.08100 -27.61500 79.41500 1.000 24.94000 ? 336 HIS A O   1 
ATOM   2731 C  CB  . HIS A 1 336 ? 52.23000 -26.86600 79.02200 1.000 27.06000 ? 336 HIS A CB  1 
ATOM   2732 C  CG  . HIS A 1 336 ? 51.06500 -26.22100 78.37700 1.000 24.04000 ? 336 HIS A CG  1 
ATOM   2733 N  ND1 . HIS A 1 336 ? 49.91900 -25.96900 79.03500 1.000 28.65000 ? 336 HIS A ND1 1 
ATOM   2734 C  CD2 . HIS A 1 336 ? 50.85900 -25.79100 77.13100 1.000 25.64000 ? 336 HIS A CD2 1 
ATOM   2735 C  CE1 . HIS A 1 336 ? 49.07300 -25.40500 78.23700 1.000 25.24000 ? 336 HIS A CE1 1 
ATOM   2736 N  NE2 . HIS A 1 336 ? 49.60500 -25.31100 77.08800 1.000 23.64000 ? 336 HIS A NE2 1 
ATOM   2737 N  N   . ARG A 1 337 ? 54.86700 -26.30500 81.20300 1.000 26.34000 ? 337 ARG A N   1 
ATOM   2738 C  CA  . ARG A 1 337 ? 55.86700 -26.99900 82.02700 1.000 29.38000 ? 337 ARG A CA  1 
ATOM   2739 C  C   . ARG A 1 337 ? 55.10400 -27.66000 83.16400 1.000 28.85000 ? 337 ARG A C   1 
ATOM   2740 O  O   . ARG A 1 337 ? 54.59200 -26.97600 84.00000 1.000 26.70000 ? 337 ARG A O   1 
ATOM   2741 C  CB  . ARG A 1 337 ? 56.98000 -26.04300 82.43500 1.000 33.31000 ? 337 ARG A CB  1 
ATOM   2742 C  CG  . ARG A 1 337 ? 57.79200 -25.55100 81.26000 1.000 30.97000 ? 337 ARG A CG  1 
ATOM   2743 C  CD  . ARG A 1 337 ? 58.94600 -24.71400 81.68600 1.000 34.33000 ? 337 ARG A CD  1 
ATOM   2744 N  NE  . ARG A 1 337 ? 59.17100 -23.70600 80.69000 1.000 45.91000 ? 337 ARG A NE  1 
ATOM   2745 C  CZ  . ARG A 1 337 ? 60.16900 -23.75300 79.84900 1.000 52.91000 ? 337 ARG A CZ  1 
ATOM   2746 N  NH1 . ARG A 1 337 ? 61.00900 -24.76200 79.91500 1.000 58.97000 ? 337 ARG A NH1 1 
ATOM   2747 N  NH2 . ARG A 1 337 ? 60.33800 -22.80900 78.95200 1.000 50.07000 ? 337 ARG A NH2 1 
ATOM   2748 N  N   . TYR A 1 338 ? 55.02100 -28.96900 83.09400 1.000 25.28000 ? 338 TYR A N   1 
ATOM   2749 C  CA  . TYR A 1 338 ? 54.24800 -29.78800 84.04600 1.000 27.78000 ? 338 TYR A CA  1 
ATOM   2750 C  C   . TYR A 1 338 ? 55.11900 -30.22000 85.21800 1.000 29.73000 ? 338 TYR A C   1 
ATOM   2751 O  O   . TYR A 1 338 ? 56.09300 -30.89200 85.04000 1.000 27.55000 ? 338 TYR A O   1 
ATOM   2752 C  CB  . TYR A 1 338 ? 53.68100 -30.99100 83.30600 1.000 34.26000 ? 338 TYR A CB  1 
ATOM   2753 C  CG  . TYR A 1 338 ? 52.62000 -31.73800 84.05100 1.000 49.79000 ? 338 TYR A CG  1 
ATOM   2754 C  CD1 . TYR A 1 338 ? 51.61200 -31.04900 84.68200 1.000 54.82000 ? 338 TYR A CD1 1 
ATOM   2755 C  CD2 . TYR A 1 338 ? 52.58800 -33.12100 84.10200 1.000 53.27000 ? 338 TYR A CD2 1 
ATOM   2756 C  CE1 . TYR A 1 338 ? 50.60500 -31.71100 85.35000 1.000 54.00000 ? 338 TYR A CE1 1 
ATOM   2757 C  CE2 . TYR A 1 338 ? 51.58400 -33.80700 84.77300 1.000 53.45000 ? 338 TYR A CE2 1 
ATOM   2758 C  CZ  . TYR A 1 338 ? 50.58700 -33.08300 85.38300 1.000 50.01000 ? 338 TYR A CZ  1 
ATOM   2759 O  OH  . TYR A 1 338 ? 49.57900 -33.65300 86.06400 1.000 56.03000 ? 338 TYR A OH  1 
ATOM   2760 N  N   . HIS A 1 339 ? 54.67000 -29.88300 86.40800 1.000 31.86000 ? 339 HIS A N   1 
ATOM   2761 C  CA  . HIS A 1 339 ? 55.43300 -30.18800 87.63600 1.000 29.37000 ? 339 HIS A CA  1 
ATOM   2762 C  C   . HIS A 1 339 ? 54.62100 -30.98300 88.64800 1.000 32.77000 ? 339 HIS A C   1 
ATOM   2763 O  O   . HIS A 1 339 ? 53.42200 -30.90000 88.63800 1.000 27.23000 ? 339 HIS A O   1 
ATOM   2764 C  CB  . HIS A 1 339 ? 55.77500 -28.88400 88.31200 1.000 28.16000 ? 339 HIS A CB  1 
ATOM   2765 C  CG  . HIS A 1 339 ? 56.77000 -28.06700 87.57700 1.000 30.34000 ? 339 HIS A CG  1 
ATOM   2766 N  ND1 . HIS A 1 339 ? 56.41000 -27.11000 86.69900 1.000 31.46000 ? 339 HIS A ND1 1 
ATOM   2767 C  CD2 . HIS A 1 339 ? 58.10500 -28.06900 87.59200 1.000 32.78000 ? 339 HIS A CD2 1 
ATOM   2768 C  CE1 . HIS A 1 339 ? 57.46300 -26.54000 86.21200 1.000 31.25000 ? 339 HIS A CE1 1 
ATOM   2769 N  NE2 . HIS A 1 339 ? 58.50600 -27.10400 86.74000 1.000 38.60000 ? 339 HIS A NE2 1 
ATOM   2770 N  N   . ASP A 1 340 ? 55.32400 -31.68800 89.53100 1.000 32.43000 ? 340 ASP A N   1 
ATOM   2771 C  CA  . ASP A 1 340 ? 54.66000 -32.35200 90.67600 1.000 29.43000 ? 340 ASP A CA  1 
ATOM   2772 C  C   . ASP A 1 340 ? 54.56200 -31.36000 91.83700 1.000 27.72000 ? 340 ASP A C   1 
ATOM   2773 O  O   . ASP A 1 340 ? 55.08100 -30.28600 91.73900 1.000 27.02000 ? 340 ASP A O   1 
ATOM   2774 C  CB  . ASP A 1 340 ? 55.35900 -33.64800 91.05600 1.000 38.48000 ? 340 ASP A CB  1 
ATOM   2775 C  CG  . ASP A 1 340 ? 56.55400 -33.50000 91.97500 1.000 36.20000 ? 340 ASP A CG  1 
ATOM   2776 O  OD1 . ASP A 1 340 ? 57.15500 -32.44400 91.99600 1.000 37.58000 ? 340 ASP A OD1 1 
ATOM   2777 O  OD2 . ASP A 1 340 ? 56.83700 -34.45400 92.66800 1.000 48.34000 ? 340 ASP A OD2 1 
ATOM   2778 N  N   . ARG A 1 341 ? 53.99200 -31.77700 92.95700 1.000 34.60000 ? 341 ARG A N   1 
ATOM   2779 C  CA  . ARG A 1 341 ? 53.87600 -30.88100 94.13400 1.000 38.43000 ? 341 ARG A CA  1 
ATOM   2780 C  C   . ARG A 1 341 ? 55.23100 -30.42200 94.67100 1.000 36.91000 ? 341 ARG A C   1 
ATOM   2781 O  O   . ARG A 1 341 ? 55.29600 -29.32600 95.14000 1.000 38.47000 ? 341 ARG A O   1 
ATOM   2782 C  CB  . ARG A 1 341 ? 53.05800 -31.47600 95.27100 1.000 37.71000 ? 341 ARG A CB  1 
ATOM   2783 C  CG  . ARG A 1 341 ? 52.37300 -30.37900 96.06400 1.000 63.52000 ? 341 ARG A CG  1 
ATOM   2784 C  CD  . ARG A 1 341 ? 51.88400 -30.80100 97.42800 1.000 65.57000 ? 341 ARG A CD  1 
ATOM   2785 N  NE  . ARG A 1 341 ? 50.56000 -31.36800 97.32600 1.000 69.40000 ? 341 ARG A NE  1 
ATOM   2786 C  CZ  . ARG A 1 341 ? 50.33200 -32.66300 97.33400 1.000 83.84000 ? 341 ARG A CZ  1 
ATOM   2787 N  NH1 . ARG A 1 341 ? 51.34200 -33.51200 97.42300 1.000 74.81000 ? 341 ARG A NH1 1 
ATOM   2788 N  NH2 . ARG A 1 341 ? 49.09800 -33.10300 97.24800 1.000 93.53000 ? 341 ARG A NH2 1 
ATOM   2789 N  N   . ASN A 1 342 ? 56.27700 -31.22500 94.55200 1.000 32.83000 ? 342 ASN A N   1 
ATOM   2790 C  CA  . ASN A 1 342 ? 57.61900 -30.81700 95.02000 1.000 32.30000 ? 342 ASN A CA  1 
ATOM   2791 C  C   . ASN A 1 342 ? 58.42500 -30.06300 93.95800 1.000 30.99000 ? 342 ASN A C   1 
ATOM   2792 O  O   . ASN A 1 342 ? 59.59800 -29.98300 94.13400 1.000 33.14000 ? 342 ASN A O   1 
ATOM   2793 C  CB  . ASN A 1 342 ? 58.36000 -32.01900 95.57200 1.000 36.91000 ? 342 ASN A CB  1 
ATOM   2794 C  CG  . ASN A 1 342 ? 57.70700 -32.53200 96.82800 1.000 37.03000 ? 342 ASN A CG  1 
ATOM   2795 O  OD1 . ASN A 1 342 ? 57.39400 -31.76600 97.71100 1.000 40.38000 ? 342 ASN A OD1 1 
ATOM   2796 N  ND2 . ASN A 1 342 ? 57.48000 -33.81800 96.89300 1.000 34.57000 ? 342 ASN A ND2 1 
ATOM   2797 N  N   . ASN A 1 343 ? 57.78700 -29.53100 92.91900 1.000 29.81000 ? 343 ASN A N   1 
ATOM   2798 C  CA  . ASN A 1 343 ? 58.39200 -28.75400 91.81100 1.000 26.03000 ? 343 ASN A CA  1 
ATOM   2799 C  C   . ASN A 1 343 ? 59.27500 -29.61900 90.90700 1.000 26.68000 ? 343 ASN A C   1 
ATOM   2800 O  O   . ASN A 1 343 ? 60.04800 -29.06200 90.23300 1.000 31.88000 ? 343 ASN A O   1 
ATOM   2801 C  CB  . ASN A 1 343 ? 59.07000 -27.44900 92.24100 1.000 30.45000 ? 343 ASN A CB  1 
ATOM   2802 C  CG  . ASN A 1 343 ? 58.25700 -26.63300 93.21900 1.000 40.04000 ? 343 ASN A CG  1 
ATOM   2803 O  OD1 . ASN A 1 343 ? 57.15000 -26.22700 92.94000 1.000 29.59000 ? 343 ASN A OD1 1 
ATOM   2804 N  ND2 . ASN A 1 343 ? 58.80700 -26.41800 94.39000 1.000 36.77000 ? 343 ASN A ND2 1 
ATOM   2805 N  N   . ASN A 1 344 ? 59.16200 -30.93700 90.93400 1.000 29.12000 ? 344 ASN A N   1 
ATOM   2806 C  CA  . ASN A 1 344 ? 59.94100 -31.79000 90.00700 1.000 27.81000 ? 344 ASN A CA  1 
ATOM   2807 C  C   . ASN A 1 344 ? 59.32900 -31.65100 88.60300 1.000 31.81000 ? 344 ASN A C   1 
ATOM   2808 O  O   . ASN A 1 344 ? 58.12300 -31.73400 88.50100 1.000 27.92000 ? 344 ASN A O   1 
ATOM   2809 C  CB  . ASN A 1 344 ? 59.93600 -33.24100 90.47500 1.000 30.47000 ? 344 ASN A CB  1 
ATOM   2810 C  CG  . ASN A 1 344 ? 60.70300 -33.43900 91.76000 1.000 34.57000 ? 344 ASN A CG  1 
ATOM   2811 O  OD1 . ASN A 1 344 ? 61.85100 -33.06900 91.84900 1.000 35.65000 ? 344 ASN A OD1 1 
ATOM   2812 N  ND2 . ASN A 1 344 ? 60.07700 -34.01800 92.75400 1.000 29.52000 ? 344 ASN A ND2 1 
ATOM   2813 N  N   . LEU A 1 345 ? 60.15000 -31.41400 87.58300 1.000 30.94000 ? 345 LEU A N   1 
ATOM   2814 C  CA  . LEU A 1 345 ? 59.66600 -31.32100 86.18200 1.000 30.14000 ? 345 LEU A CA  1 
ATOM   2815 C  C   . LEU A 1 345 ? 59.21100 -32.68800 85.68400 1.000 32.35000 ? 345 LEU A C   1 
ATOM   2816 O  O   . LEU A 1 345 ? 60.00500 -33.57500 85.65600 1.000 34.18000 ? 345 LEU A O   1 
ATOM   2817 C  CB  . LEU A 1 345 ? 60.73100 -30.77000 85.24100 1.000 30.24000 ? 345 LEU A CB  1 
ATOM   2818 C  CG  . LEU A 1 345 ? 60.23800 -30.54200 83.81500 1.000 32.45000 ? 345 LEU A CG  1 
ATOM   2819 C  CD1 . LEU A 1 345 ? 59.33400 -29.34500 83.74300 1.000 28.53000 ? 345 LEU A CD1 1 
ATOM   2820 C  CD2 . LEU A 1 345 ? 61.37500 -30.39600 82.83000 1.000 30.27000 ? 345 LEU A CD2 1 
ATOM   2821 N  N   . LYS A 1 346 ? 57.95400 -32.81500 85.30500 1.000 30.77000 ? 346 LYS A N   1 
ATOM   2822 C  CA  . LYS A 1 346 ? 57.46600 -34.09500 84.74900 1.000 33.75000 ? 346 LYS A CA  1 
ATOM   2823 C  C   . LYS A 1 346 ? 57.66000 -34.07700 83.22800 1.000 34.38000 ? 346 LYS A C   1 
ATOM   2824 O  O   . LYS A 1 346 ? 58.09200 -35.04400 82.68700 1.000 32.75000 ? 346 LYS A O   1 
ATOM   2825 C  CB  . LYS A 1 346 ? 56.01800 -34.35500 85.14900 1.000 39.04000 ? 346 LYS A CB  1 
ATOM   2826 C  CG  . LYS A 1 346 ? 55.77200 -34.70100 86.60200 1.000 40.73000 ? 346 LYS A CG  1 
ATOM   2827 C  CD  . LYS A 1 346 ? 54.40200 -35.27600 86.76500 1.000 41.93000 ? 346 LYS A CD  1 
ATOM   2828 C  CE  . LYS A 1 346 ? 53.96200 -35.35700 88.20300 1.000 47.12000 ? 346 LYS A CE  1 
ATOM   2829 N  NZ  . LYS A 1 346 ? 52.78800 -36.23400 88.34600 1.000 45.83000 ? 346 LYS A NZ  1 
ATOM   2830 N  N   . GLY A 1 347 ? 57.40800 -32.95100 82.59700 1.000 27.70000 ? 347 GLY A N   1 
ATOM   2831 C  CA  . GLY A 1 347 ? 57.57600 -32.87100 81.15200 1.000 29.16000 ? 347 GLY A CA  1 
ATOM   2832 C  C   . GLY A 1 347 ? 57.16700 -31.52800 80.61900 1.000 35.44000 ? 347 GLY A C   1 
ATOM   2833 O  O   . GLY A 1 347 ? 56.65000 -30.74000 81.38400 1.000 32.48000 ? 347 GLY A O   1 
ATOM   2834 N  N   . LEU A 1 348 ? 57.37600 -31.34600 79.32300 1.000 30.52000 ? 348 LEU A N   1 
ATOM   2835 C  CA  . LEU A 1 348 ? 57.10300 -30.10800 78.57000 1.000 32.31000 ? 348 LEU A CA  1 
ATOM   2836 C  C   . LEU A 1 348 ? 56.19300 -30.40900 77.38900 1.000 34.43000 ? 348 LEU A C   1 
ATOM   2837 O  O   . LEU A 1 348 ? 56.53400 -31.25800 76.60200 1.000 29.65000 ? 348 LEU A O   1 
ATOM   2838 C  CB  . LEU A 1 348 ? 58.41900 -29.64100 77.98100 1.000 39.04000 ? 348 LEU A CB  1 
ATOM   2839 C  CG  . LEU A 1 348 ? 58.96300 -28.34600 78.52400 1.000 40.46000 ? 348 LEU A CG  1 
ATOM   2840 C  CD1 . LEU A 1 348 ? 59.57300 -28.61700 79.86700 1.000 46.14000 ? 348 LEU A CD1 1 
ATOM   2841 C  CD2 . LEU A 1 348 ? 59.99400 -27.78300 77.58100 1.000 34.16000 ? 348 LEU A CD2 1 
ATOM   2842 N  N   . TYR A 1 349 ? 55.11000 -29.67100 77.29100 1.000 29.51000 ? 349 TYR A N   1 
ATOM   2843 C  CA  . TYR A 1 349 ? 54.16300 -29.80300 76.17400 1.000 29.01000 ? 349 TYR A CA  1 
ATOM   2844 C  C   . TYR A 1 349 ? 54.10000 -28.46000 75.47200 1.000 30.08000 ? 349 TYR A C   1 
ATOM   2845 O  O   . TYR A 1 349 ? 53.76100 -27.47100 76.11800 1.000 28.15000 ? 349 TYR A O   1 
ATOM   2846 C  CB  . TYR A 1 349 ? 52.78400 -30.14700 76.71200 1.000 29.49000 ? 349 TYR A CB  1 
ATOM   2847 C  CG  . TYR A 1 349 ? 51.76900 -30.50600 75.67200 1.000 32.08000 ? 349 TYR A CG  1 
ATOM   2848 C  CD1 . TYR A 1 349 ? 51.06300 -29.55000 74.98000 1.000 28.83000 ? 349 TYR A CD1 1 
ATOM   2849 C  CD2 . TYR A 1 349 ? 51.51800 -31.82500 75.39000 1.000 40.92000 ? 349 TYR A CD2 1 
ATOM   2850 C  CE1 . TYR A 1 349 ? 50.10900 -29.89500 74.04600 1.000 32.17000 ? 349 TYR A CE1 1 
ATOM   2851 C  CE2 . TYR A 1 349 ? 50.59200 -32.19800 74.44500 1.000 42.52000 ? 349 TYR A CE2 1 
ATOM   2852 C  CZ  . TYR A 1 349 ? 49.88100 -31.23200 73.77000 1.000 43.34000 ? 349 TYR A CZ  1 
ATOM   2853 O  OH  . TYR A 1 349 ? 48.98700 -31.66900 72.86300 1.000 38.09000 ? 349 TYR A OH  1 
ATOM   2854 N  N   . VAL A 1 350 ? 54.47600 -28.44200 74.21200 1.000 22.15000 ? 350 VAL A N   1 
ATOM   2855 C  CA  . VAL A 1 350 ? 54.34200 -27.18100 73.46200 1.000 23.40000 ? 350 VAL A CA  1 
ATOM   2856 C  C   . VAL A 1 350 ? 53.08400 -27.28400 72.61600 1.000 24.88000 ? 350 VAL A C   1 
ATOM   2857 O  O   . VAL A 1 350 ? 53.03600 -28.09800 71.73800 1.000 24.50000 ? 350 VAL A O   1 
ATOM   2858 C  CB  . VAL A 1 350 ? 55.56500 -26.84000 72.61700 1.000 22.55000 ? 350 VAL A CB  1 
ATOM   2859 C  CG1 . VAL A 1 350 ? 55.38700 -25.49800 71.97200 1.000 25.23000 ? 350 VAL A CG1 1 
ATOM   2860 C  CG2 . VAL A 1 350 ? 56.82800 -26.88100 73.42600 1.000 24.65000 ? 350 VAL A CG2 1 
ATOM   2861 N  N   . ASN A 1 351 ? 52.10200 -26.48700 72.96100 1.000 25.00000 ? 351 ASN A N   1 
ATOM   2862 C  CA  . ASN A 1 351 ? 50.83500 -26.45300 72.22200 1.000 21.20000 ? 351 ASN A CA  1 
ATOM   2863 C  C   . ASN A 1 351 ? 51.02500 -25.52700 71.03200 1.000 27.16000 ? 351 ASN A C   1 
ATOM   2864 O  O   . ASN A 1 351 ? 51.42100 -24.46800 71.25000 1.000 27.88000 ? 351 ASN A O   1 
ATOM   2865 C  CB  . ASN A 1 351 ? 49.74000 -25.82500 73.05400 1.000 23.02000 ? 351 ASN A CB  1 
ATOM   2866 C  CG  . ASN A 1 351 ? 48.40900 -25.97300 72.37800 1.000 26.48000 ? 351 ASN A CG  1 
ATOM   2867 O  OD1 . ASN A 1 351 ? 47.95200 -27.05800 72.30200 1.000 30.11000 ? 351 ASN A OD1 1 
ATOM   2868 N  ND2 . ASN A 1 351 ? 47.79000 -24.91700 71.93300 1.000 25.01000 ? 351 ASN A ND2 1 
ATOM   2869 N  N   . ILE A 1 352 ? 50.75800 -25.97100 69.82500 1.000 23.60000 ? 352 ILE A N   1 
ATOM   2870 C  CA  . ILE A 1 352 ? 50.89600 -25.10400 68.62900 1.000 25.89000 ? 352 ILE A CA  1 
ATOM   2871 C  C   . ILE A 1 352 ? 49.53100 -24.51500 68.28000 1.000 23.47000 ? 352 ILE A C   1 
ATOM   2872 O  O   . ILE A 1 352 ? 48.59500 -25.23900 68.22600 1.000 23.28000 ? 352 ILE A O   1 
ATOM   2873 C  CB  . ILE A 1 352 ? 51.53600 -25.86000 67.46300 1.000 20.28000 ? 352 ILE A CB  1 
ATOM   2874 C  CG1 . ILE A 1 352 ? 53.01800 -26.06200 67.74400 1.000 28.53000 ? 352 ILE A CG1 1 
ATOM   2875 C  CG2 . ILE A 1 352 ? 51.37200 -25.11100 66.17700 1.000 23.90000 ? 352 ILE A CG2 1 
ATOM   2876 C  CD1 . ILE A 1 352 ? 53.60000 -27.20200 67.04100 1.000 24.38000 ? 352 ILE A CD1 1 
ATOM   2877 N  N   . SER A 1 353 ? 49.48100 -23.22500 68.04000 1.000 20.77000 ? 353 SER A N   1 
ATOM   2878 C  CA  . SER A 1 353 ? 48.17100 -22.61000 67.76200 1.000 24.61000 ? 353 SER A CA  1 
ATOM   2879 C  C   . SER A 1 353 ? 48.30800 -21.29900 67.01400 1.000 24.40000 ? 353 SER A C   1 
ATOM   2880 O  O   . SER A 1 353 ? 49.36900 -20.81900 66.81700 1.000 25.69000 ? 353 SER A O   1 
ATOM   2881 C  CB  . SER A 1 353 ? 47.45500 -22.34900 69.06500 1.000 24.47000 ? 353 SER A CB  1 
ATOM   2882 O  OG  . SER A 1 353 ? 48.04300 -21.30200 69.79800 1.000 25.02000 ? 353 SER A OG  1 
ATOM   2883 N  N   . THR A 1 354 ? 47.16700 -20.68700 66.74900 1.000 22.81000 ? 354 THR A N   1 
ATOM   2884 C  CA  . THR A 1 354 ? 47.17600 -19.29000 66.28800 1.000 24.52000 ? 354 THR A CA  1 
ATOM   2885 C  C   . THR A 1 354 ? 47.43100 -18.42500 67.53200 1.000 26.09000 ? 354 THR A C   1 
ATOM   2886 O  O   . THR A 1 354 ? 47.16300 -18.87100 68.64800 1.000 23.21000 ? 354 THR A O   1 
ATOM   2887 C  CB  . THR A 1 354 ? 45.88200 -18.89500 65.57800 1.000 24.67000 ? 354 THR A CB  1 
ATOM   2888 O  OG1 . THR A 1 354 ? 44.84500 -19.06100 66.52700 1.000 25.86000 ? 354 THR A OG1 1 
ATOM   2889 C  CG2 . THR A 1 354 ? 45.61600 -19.67800 64.31700 1.000 23.59000 ? 354 THR A CG2 1 
ATOM   2890 N  N   . PRO A 1 355 ? 47.90800 -17.18300 67.37400 1.000 22.55000 ? 355 PRO A N   1 
ATOM   2891 C  CA  . PRO A 1 355 ? 48.23800 -16.34300 68.49700 1.000 25.93000 ? 355 PRO A CA  1 
ATOM   2892 C  C   . PRO A 1 355 ? 47.07300 -16.17700 69.48400 1.000 23.01000 ? 355 PRO A C   1 
ATOM   2893 O  O   . PRO A 1 355 ? 46.03200 -15.95700 69.07500 1.000 21.56000 ? 355 PRO A O   1 
ATOM   2894 C  CB  . PRO A 1 355 ? 48.73700 -15.05900 67.84300 1.000 28.34000 ? 355 PRO A CB  1 
ATOM   2895 C  CG  . PRO A 1 355 ? 49.22700 -15.49300 66.51000 1.000 28.05000 ? 355 PRO A CG  1 
ATOM   2896 C  CD  . PRO A 1 355 ? 48.24300 -16.56100 66.12100 1.000 28.78000 ? 355 PRO A CD  1 
ATOM   2897 N  N   . PRO A 1 356 ? 47.31600 -16.33100 70.79300 1.000 24.88000 ? 356 PRO A N   1 
ATOM   2898 C  CA  . PRO A 1 356 ? 46.28000 -16.28000 71.81100 1.000 26.72000 ? 356 PRO A CA  1 
ATOM   2899 C  C   . PRO A 1 356 ? 45.57000 -14.93200 71.93800 1.000 22.26000 ? 356 PRO A C   1 
ATOM   2900 O  O   . PRO A 1 356 ? 46.20800 -13.96300 71.97400 1.000 25.50000 ? 356 PRO A O   1 
ATOM   2901 C  CB  . PRO A 1 356 ? 47.02400 -16.59600 73.10800 1.000 23.99000 ? 356 PRO A CB  1 
ATOM   2902 C  CG  . PRO A 1 356 ? 48.39900 -16.11300 72.82600 1.000 28.68000 ? 356 PRO A CG  1 
ATOM   2903 C  CD  . PRO A 1 356 ? 48.61700 -16.50700 71.39300 1.000 23.96000 ? 356 PRO A CD  1 
ATOM   2904 N  N   . GLU A 1 357 ? 44.25500 -14.98400 71.99900 1.000 21.80000 ? 357 GLU A N   1 
ATOM   2905 C  CA  . GLU A 1 357 ? 43.37000 -13.82600 72.18000 1.000 25.01000 ? 357 GLU A CA  1 
ATOM   2906 C  C   . GLU A 1 357 ? 43.00000 -13.69700 73.65900 1.000 24.96000 ? 357 GLU A C   1 
ATOM   2907 O  O   . GLU A 1 357 ? 43.03600 -14.67300 74.36600 1.000 23.92000 ? 357 GLU A O   1 
ATOM   2908 C  CB  . GLU A 1 357 ? 42.05800 -14.02100 71.44100 1.000 22.82000 ? 357 GLU A CB  1 
ATOM   2909 C  CG  . GLU A 1 357 ? 42.17300 -14.05200 69.95000 1.000 27.70000 ? 357 GLU A CG  1 
ATOM   2910 C  CD  . GLU A 1 357 ? 40.83400 -13.94600 69.25500 1.000 31.69000 ? 357 GLU A CD  1 
ATOM   2911 O  OE1 . GLU A 1 357 ? 40.40900 -12.86400 69.01700 1.000 35.78000 ? 357 GLU A OE1 1 
ATOM   2912 O  OE2 . GLU A 1 357 ? 40.24800 -14.94200 68.98300 1.000 30.78000 ? 357 GLU A OE2 1 
ATOM   2913 N  N   . LEU A 1 358 ? 42.65300 -12.49200 74.06600 1.000 25.33000 ? 358 LEU A N   1 
ATOM   2914 C  CA  . LEU A 1 358 ? 42.20800 -12.21000 75.44400 1.000 23.82000 ? 358 LEU A CA  1 
ATOM   2915 C  C   . LEU A 1 358 ? 40.70000 -11.96300 75.45800 1.000 27.40000 ? 358 LEU A C   1 
ATOM   2916 O  O   . LEU A 1 358 ? 40.24200 -11.15200 74.67800 1.000 25.93000 ? 358 LEU A O   1 
ATOM   2917 C  CB  . LEU A 1 358 ? 42.89000 -10.94600 75.94000 1.000 24.87000 ? 358 LEU A CB  1 
ATOM   2918 C  CG  . LEU A 1 358 ? 44.35100 -11.05800 76.31200 1.000 33.23000 ? 358 LEU A CG  1 
ATOM   2919 C  CD1 . LEU A 1 358 ? 44.68300 -9.98500  77.30200 1.000 31.27000 ? 358 LEU A CD1 1 
ATOM   2920 C  CD2 . LEU A 1 358 ? 44.68400 -12.43500 76.84800 1.000 27.20000 ? 358 LEU A CD2 1 
ATOM   2921 N  N   . LEU A 1 359 ? 39.99800 -12.70400 76.29100 1.000 19.80000 ? 359 LEU A N   1 
ATOM   2922 C  CA  . LEU A 1 359 ? 38.57500 -12.47400 76.61400 1.000 27.59000 ? 359 LEU A CA  1 
ATOM   2923 C  C   . LEU A 1 359 ? 38.47900 -12.12800 78.10800 1.000 26.84000 ? 359 LEU A C   1 
ATOM   2924 O  O   . LEU A 1 359 ? 39.49500 -12.12300 78.78300 1.000 26.89000 ? 359 LEU A O   1 
ATOM   2925 C  CB  . LEU A 1 359 ? 37.73100 -13.70300 76.28200 1.000 27.47000 ? 359 LEU A CB  1 
ATOM   2926 C  CG  . LEU A 1 359 ? 37.80500 -14.21200 74.85400 1.000 29.35000 ? 359 LEU A CG  1 
ATOM   2927 C  CD1 . LEU A 1 359 ? 36.99300 -15.48000 74.69500 1.000 34.55000 ? 359 LEU A CD1 1 
ATOM   2928 C  CD2 . LEU A 1 359 ? 37.35200 -13.15200 73.88900 1.000 35.47000 ? 359 LEU A CD2 1 
ATOM   2929 N  N   . LYS A 1 360 ? 37.29500 -11.77900 78.58100 1.000 24.93000 ? 360 LYS A N   1 
ATOM   2930 C  CA  . LYS A 1 360 ? 37.15400 -11.47000 80.01400 1.000 24.40000 ? 360 LYS A CA  1 
ATOM   2931 C  C   . LYS A 1 360 ? 37.50700 -12.72400 80.81600 1.000 27.32000 ? 360 LYS A C   1 
ATOM   2932 O  O   . LYS A 1 360 ? 36.81700 -13.69100 80.63000 1.000 25.76000 ? 360 LYS A O   1 
ATOM   2933 C  CB  . LYS A 1 360 ? 35.73900 -11.00100 80.33800 1.000 34.75000 ? 360 LYS A CB  1 
ATOM   2934 C  CG  . LYS A 1 360 ? 35.58000 -10.47300 81.74300 1.000 33.48000 ? 360 LYS A CG  1 
ATOM   2935 C  CD  . LYS A 1 360 ? 36.58800 -9.42400  82.05800 1.000 35.48000 ? 360 LYS A CD  1 
ATOM   2936 C  CE  . LYS A 1 360 ? 36.09900 -8.38700  83.02900 1.000 35.62000 ? 360 LYS A CE  1 
ATOM   2937 N  NZ  . LYS A 1 360 ? 37.20500 -7.91700  83.88200 1.000 50.24000 ? 360 LYS A NZ  1 
ATOM   2938 N  N   . ASN A 1 361 ? 38.61000 -12.68300 81.56400 1.000 28.05000 ? 361 ASN A N   1 
ATOM   2939 C  CA  . ASN A 1 361 ? 39.06300 -13.81000 82.38000 1.000 28.47000 ? 361 ASN A CA  1 
ATOM   2940 C  C   . ASN A 1 361 ? 39.30700 -15.08700 81.56500 1.000 26.70000 ? 361 ASN A C   1 
ATOM   2941 O  O   . ASN A 1 361 ? 39.23700 -16.19400 82.10700 1.000 27.65000 ? 361 ASN A O   1 
ATOM   2942 C  CB  . ASN A 1 361 ? 38.06300 -14.10300 83.50200 1.000 32.35000 ? 361 ASN A CB  1 
ATOM   2943 C  CG  . ASN A 1 361 ? 37.72100 -12.86700 84.31400 1.000 30.66000 ? 361 ASN A CG  1 
ATOM   2944 O  OD1 . ASN A 1 361 ? 38.59700 -12.09400 84.66900 1.000 39.41000 ? 361 ASN A OD1 1 
ATOM   2945 N  ND2 . ASN A 1 361 ? 36.44300 -12.67200 84.59000 1.000 29.74000 ? 361 ASN A ND2 1 
ATOM   2946 N  N   . ARG A 1 362 ? 39.59600 -14.98300 80.27300 1.000 21.96000 ? 362 ARG A N   1 
ATOM   2947 C  CA  . ARG A 1 362 ? 39.76300 -16.18700 79.47900 1.000 22.14000 ? 362 ARG A CA  1 
ATOM   2948 C  C   . ARG A 1 362 ? 40.80400 -15.94100 78.40700 1.000 26.05000 ? 362 ARG A C   1 
ATOM   2949 O  O   . ARG A 1 362 ? 41.02100 -14.80100 77.98100 1.000 25.05000 ? 362 ARG A O   1 
ATOM   2950 C  CB  . ARG A 1 362 ? 38.44800 -16.62000 78.81700 1.000 21.31000 ? 362 ARG A CB  1 
ATOM   2951 C  CG  . ARG A 1 362 ? 37.38300 -17.11500 79.78800 1.000 25.47000 ? 362 ARG A CG  1 
ATOM   2952 C  CD  . ARG A 1 362 ? 36.32700 -17.88300 79.02900 1.000 25.12000 ? 362 ARG A CD  1 
ATOM   2953 N  NE  . ARG A 1 362 ? 35.21100 -18.30500 79.86800 1.000 30.27000 ? 362 ARG A NE  1 
ATOM   2954 C  CZ  . ARG A 1 362 ? 34.17900 -19.00100 79.40400 1.000 32.75000 ? 362 ARG A CZ  1 
ATOM   2955 N  NH1 . ARG A 1 362 ? 34.14400 -19.34100 78.12200 1.000 26.33000 ? 362 ARG A NH1 1 
ATOM   2956 N  NH2 . ARG A 1 362 ? 33.18300 -19.35000 80.21400 1.000 28.30000 ? 362 ARG A NH2 1 
ATOM   2957 N  N   . ILE A 1 363 ? 41.43300 -17.03100 77.97100 1.000 23.54000 ? 363 ILE A N   1 
ATOM   2958 C  CA  . ILE A 1 363 ? 42.32400 -17.04500 76.81800 1.000 25.54000 ? 363 ILE A CA  1 
ATOM   2959 C  C   . ILE A 1 363 ? 41.60500 -17.83500 75.73300 1.000 23.63000 ? 363 ILE A C   1 
ATOM   2960 O  O   . ILE A 1 363 ? 40.86100 -18.77400 76.03600 1.000 22.52000 ? 363 ILE A O   1 
ATOM   2961 C  CB  . ILE A 1 363 ? 43.67500 -17.70600 77.16100 1.000 28.84000 ? 363 ILE A CB  1 
ATOM   2962 C  CG1 . ILE A 1 363 ? 44.33600 -17.02900 78.37400 1.000 30.45000 ? 363 ILE A CG1 1 
ATOM   2963 C  CG2 . ILE A 1 363 ? 44.60500 -17.73800 75.94800 1.000 28.56000 ? 363 ILE A CG2 1 
ATOM   2964 C  CD1 . ILE A 1 363 ? 44.89200 -15.70500 78.04700 1.000 30.11000 ? 363 ILE A CD1 1 
ATOM   2965 N  N   . ARG A 1 364 ? 41.82200 -17.46200 74.47400 1.000 25.46000 ? 364 ARG A N   1 
ATOM   2966 C  CA  . ARG A 1 364 ? 41.24800 -18.18900 73.34300 1.000 22.70000 ? 364 ARG A CA  1 
ATOM   2967 C  C   . ARG A 1 364 ? 42.31700 -18.35900 72.28200 1.000 19.66000 ? 364 ARG A C   1 
ATOM   2968 O  O   . ARG A 1 364 ? 43.01700 -17.40000 71.95800 1.000 21.71000 ? 364 ARG A O   1 
ATOM   2969 C  CB  . ARG A 1 364 ? 40.04800 -17.45900 72.72700 1.000 18.35000 ? 364 ARG A CB  1 
ATOM   2970 C  CG  . ARG A 1 364 ? 39.51700 -18.18100 71.48500 1.000 25.47000 ? 364 ARG A CG  1 
ATOM   2971 C  CD  . ARG A 1 364 ? 38.33700 -17.45400 70.81300 1.000 25.95000 ? 364 ARG A CD  1 
ATOM   2972 N  NE  . ARG A 1 364 ? 37.12800 -17.48100 71.64600 1.000 25.34000 ? 364 ARG A NE  1 
ATOM   2973 C  CZ  . ARG A 1 364 ? 35.94100 -16.99300 71.28600 1.000 27.88000 ? 364 ARG A CZ  1 
ATOM   2974 N  NH1 . ARG A 1 364 ? 35.78100 -16.43100 70.10000 1.000 24.01000 ? 364 ARG A NH1 1 
ATOM   2975 N  NH2 . ARG A 1 364 ? 34.91100 -17.05900 72.12500 1.000 28.19000 ? 364 ARG A NH2 1 
ATOM   2976 N  N   . TYR A 1 365 ? 42.43900 -19.55700 71.72900 1.000 22.56000 ? 365 TYR A N   1 
ATOM   2977 C  CA  . TYR A 1 365 ? 43.28400 -19.71800 70.55400 1.000 21.54000 ? 365 TYR A CA  1 
ATOM   2978 C  C   . TYR A 1 365 ? 42.67600 -20.76800 69.63900 1.000 25.21000 ? 365 TYR A C   1 
ATOM   2979 O  O   . TYR A 1 365 ? 41.85000 -21.58400 70.05900 1.000 23.12000 ? 365 TYR A O   1 
ATOM   2980 C  CB  . TYR A 1 365 ? 44.72900 -20.09900 70.91300 1.000 19.07000 ? 365 TYR A CB  1 
ATOM   2981 C  CG  . TYR A 1 365 ? 44.85200 -21.30600 71.82500 1.000 24.92000 ? 365 TYR A CG  1 
ATOM   2982 C  CD1 . TYR A 1 365 ? 44.59700 -22.59500 71.35900 1.000 23.33000 ? 365 TYR A CD1 1 
ATOM   2983 C  CD2 . TYR A 1 365 ? 45.23900 -21.14700 73.16000 1.000 26.37000 ? 365 TYR A CD2 1 
ATOM   2984 C  CE1 . TYR A 1 365 ? 44.71600 -23.69400 72.18900 1.000 25.90000 ? 365 TYR A CE1 1 
ATOM   2985 C  CE2 . TYR A 1 365 ? 45.36400 -22.23300 74.00000 1.000 24.63000 ? 365 TYR A CE2 1 
ATOM   2986 C  CZ  . TYR A 1 365 ? 45.10000 -23.50100 73.51900 1.000 24.46000 ? 365 TYR A CZ  1 
ATOM   2987 O  OH  . TYR A 1 365 ? 45.21900 -24.57100 74.36600 1.000 29.95000 ? 365 TYR A OH  1 
ATOM   2988 N  N   . LEU A 1 366 ? 43.11100 -20.74200 68.37800 1.000 24.14000 ? 366 LEU A N   1 
ATOM   2989 C  CA  . LEU A 1 366 ? 42.72200 -21.75000 67.40400 1.000 23.93000 ? 366 LEU A CA  1 
ATOM   2990 C  C   . LEU A 1 366 ? 43.81600 -22.81200 67.41100 1.000 21.19000 ? 366 LEU A C   1 
ATOM   2991 O  O   . LEU A 1 366 ? 44.95900 -22.55400 67.01600 1.000 23.16000 ? 366 LEU A O   1 
ATOM   2992 C  CB  . LEU A 1 366 ? 42.51100 -21.12900 66.02200 1.000 26.97000 ? 366 LEU A CB  1 
ATOM   2993 C  CG  . LEU A 1 366 ? 41.13500 -20.53000 65.64100 1.000 36.23000 ? 366 LEU A CG  1 
ATOM   2994 C  CD1 . LEU A 1 366 ? 40.41000 -19.68200 66.73900 1.000 30.15000 ? 366 LEU A CD1 1 
ATOM   2995 C  CD2 . LEU A 1 366 ? 41.25500 -19.69100 64.36500 1.000 31.22000 ? 366 LEU A CD2 1 
ATOM   2996 N  N   . ASP A 1 367 ? 43.48800 -23.98500 67.93100 1.000 22.48000 ? 367 ASP A N   1 
ATOM   2997 C  CA  . ASP A 1 367 ? 44.47400 -25.04400 68.07000 1.000 21.04000 ? 367 ASP A CA  1 
ATOM   2998 C  C   . ASP A 1 367 ? 44.81500 -25.60500 66.70300 1.000 24.81000 ? 367 ASP A C   1 
ATOM   2999 O  O   . ASP A 1 367 ? 43.93000 -25.79000 65.86400 1.000 23.95000 ? 367 ASP A O   1 
ATOM   3000 C  CB  . ASP A 1 367 ? 43.93400 -26.15200 68.96500 1.000 23.27000 ? 367 ASP A CB  1 
ATOM   3001 C  CG  . ASP A 1 367 ? 44.94500 -27.27900 69.18600 1.000 28.86000 ? 367 ASP A CG  1 
ATOM   3002 O  OD1 . ASP A 1 367 ? 45.85300 -27.13100 70.04700 1.000 23.42000 ? 367 ASP A OD1 1 
ATOM   3003 O  OD2 . ASP A 1 367 ? 44.81200 -28.31800 68.49100 1.000 29.71000 ? 367 ASP A OD2 1 
ATOM   3004 N  N   . LEU A 1 368 ? 46.10200 -25.88000 66.47200 1.000 20.03000 ? 368 LEU A N   1 
ATOM   3005 C  CA  . LEU A 1 368 ? 46.53700 -26.35400 65.16500 1.000 22.36000 ? 368 LEU A CA  1 
ATOM   3006 C  C   . LEU A 1 368 ? 46.91400 -27.83500 65.16300 1.000 23.33000 ? 368 LEU A C   1 
ATOM   3007 O  O   . LEU A 1 368 ? 47.64400 -28.27200 64.27000 1.000 23.68000 ? 368 LEU A O   1 
ATOM   3008 C  CB  . LEU A 1 368 ? 47.69200 -25.49900 64.64500 1.000 22.50000 ? 368 LEU A CB  1 
ATOM   3009 C  CG  . LEU A 1 368 ? 47.24600 -24.07000 64.31000 1.000 24.17000 ? 368 LEU A CG  1 
ATOM   3010 C  CD1 . LEU A 1 368 ? 48.42000 -23.17200 63.99000 1.000 25.12000 ? 368 LEU A CD1 1 
ATOM   3011 C  CD2 . LEU A 1 368 ? 46.19700 -24.06500 63.19000 1.000 19.44000 ? 368 LEU A CD2 1 
ATOM   3012 N  N   . GLU A 1 369 ? 46.42400 -28.60400 66.13800 1.000 21.80000 ? 369 GLU A N   1 
ATOM   3013 C  CA  . GLU A 1 369 ? 46.50700 -30.07000 66.19300 1.000 26.29000 ? 369 GLU A CA  1 
ATOM   3014 C  C   . GLU A 1 369 ? 47.89700 -30.58800 66.53600 1.000 24.98000 ? 369 GLU A C   1 
ATOM   3015 O  O   . GLU A 1 369 ? 48.06200 -31.32200 67.51500 1.000 26.01000 ? 369 GLU A O   1 
ATOM   3016 C  CB  . GLU A 1 369 ? 46.04500 -30.71000 64.87600 1.000 27.15000 ? 369 GLU A CB  1 
ATOM   3017 C  CG  . GLU A 1 369 ? 44.55100 -30.46200 64.54000 1.000 28.08000 ? 369 GLU A CG  1 
ATOM   3018 C  CD  . GLU A 1 369 ? 43.56700 -31.06200 65.57600 1.000 33.79000 ? 369 GLU A CD  1 
ATOM   3019 O  OE1 . GLU A 1 369 ? 43.98000 -31.82000 66.48300 1.000 36.20000 ? 369 GLU A OE1 1 
ATOM   3020 O  OE2 . GLU A 1 369 ? 42.36000 -30.75700 65.49000 1.000 40.41000 ? 369 GLU A OE2 1 
ATOM   3021 N  N   . VAL A 1 370 ? 48.89700 -30.25500 65.72200 1.000 23.44000 ? 370 VAL A N   1 
ATOM   3022 C  CA  . VAL A 1 370 ? 50.24200 -30.74300 65.98200 1.000 22.02000 ? 370 VAL A CA  1 
ATOM   3023 C  C   . VAL A 1 370 ? 50.76200 -30.09800 67.26800 1.000 26.45000 ? 370 VAL A C   1 
ATOM   3024 O  O   . VAL A 1 370 ? 50.45200 -28.94400 67.57600 1.000 24.68000 ? 370 VAL A O   1 
ATOM   3025 C  CB  . VAL A 1 370 ? 51.15100 -30.47200 64.76800 1.000 24.13000 ? 370 VAL A CB  1 
ATOM   3026 C  CG1 . VAL A 1 370 ? 51.28200 -28.98600 64.52600 1.000 21.66000 ? 370 VAL A CG1 1 
ATOM   3027 C  CG2 . VAL A 1 370 ? 52.49300 -31.11000 64.95700 1.000 22.41000 ? 370 VAL A CG2 1 
ATOM   3028 N  N   . ASP A 1 371 ? 51.47800 -30.87800 68.07300 1.000 27.67000 ? 371 ASP A N   1 
ATOM   3029 C  CA  . ASP A 1 371 ? 52.08100 -30.40600 69.31300 1.000 20.63000 ? 371 ASP A CA  1 
ATOM   3030 C  C   . ASP A 1 371 ? 53.50100 -30.95700 69.36200 1.000 27.44000 ? 371 ASP A C   1 
ATOM   3031 O  O   . ASP A 1 371 ? 53.84900 -31.87800 68.61500 1.000 25.15000 ? 371 ASP A O   1 
ATOM   3032 C  CB  . ASP A 1 371 ? 51.29900 -30.86700 70.55600 1.000 25.40000 ? 371 ASP A CB  1 
ATOM   3033 C  CG  . ASP A 1 371 ? 49.79900 -30.51400 70.50700 1.000 35.93000 ? 371 ASP A CG  1 
ATOM   3034 O  OD1 . ASP A 1 371 ? 49.43600 -29.31600 70.52400 1.000 37.44000 ? 371 ASP A OD1 1 
ATOM   3035 O  OD2 . ASP A 1 371 ? 48.96700 -31.45100 70.50900 1.000 43.97000 ? 371 ASP A OD2 1 
ATOM   3036 N  N   . VAL A 1 372 ? 54.32800 -30.41300 70.24700 1.000 24.39000 ? 372 VAL A N   1 
ATOM   3037 C  CA  . VAL A 1 372 ? 55.67400 -30.93900 70.44400 1.000 23.47000 ? 372 VAL A CA  1 
ATOM   3038 C  C   . VAL A 1 372 ? 55.87100 -31.26700 71.92500 1.000 25.90000 ? 372 VAL A C   1 
ATOM   3039 O  O   . VAL A 1 372 ? 55.66500 -30.41500 72.79400 1.000 25.65000 ? 372 VAL A O   1 
ATOM   3040 C  CB  . VAL A 1 372 ? 56.74000 -29.95100 69.94600 1.000 21.71000 ? 372 VAL A CB  1 
ATOM   3041 C  CG1 . VAL A 1 372 ? 58.11500 -30.60300 69.98800 1.000 24.85000 ? 372 VAL A CG1 1 
ATOM   3042 C  CG2 . VAL A 1 372 ? 56.40100 -29.45000 68.53800 1.000 22.22000 ? 372 VAL A CG2 1 
ATOM   3043 N  N   . VAL A 1 373 ? 56.27400 -32.49100 72.21600 1.000 26.23000 ? 373 VAL A N   1 
ATOM   3044 C  CA  . VAL A 1 373 ? 56.38900 -32.94900 73.59400 1.000 28.68000 ? 373 VAL A CA  1 
ATOM   3045 C  C   . VAL A 1 373 ? 57.85400 -33.23000 73.90600 1.000 33.20000 ? 373 VAL A C   1 
ATOM   3046 O  O   . VAL A 1 373 ? 58.57800 -33.79100 73.07300 1.000 33.85000 ? 373 VAL A O   1 
ATOM   3047 C  CB  . VAL A 1 373 ? 55.50200 -34.18200 73.82400 1.000 30.71000 ? 373 VAL A CB  1 
ATOM   3048 C  CG1 . VAL A 1 373 ? 55.95800 -34.95000 75.05600 1.000 40.73000 ? 373 VAL A CG1 1 
ATOM   3049 C  CG2 . VAL A 1 373 ? 54.05400 -33.73300 73.96100 1.000 30.64000 ? 373 VAL A CG2 1 
ATOM   3050 N  N   . LYS A 1 374 ? 58.30200 -32.81000 75.09200 1.000 31.66000 ? 374 LYS A N   1 
ATOM   3051 C  CA  . LYS A 1 374 ? 59.63300 -33.15900 75.58100 1.000 33.53000 ? 374 LYS A CA  1 
ATOM   3052 C  C   . LYS A 1 374 ? 59.52200 -33.76600 76.97200 1.000 34.32000 ? 374 LYS A C   1 
ATOM   3053 O  O   . LYS A 1 374 ? 59.07400 -33.10200 77.91200 1.000 33.98000 ? 374 LYS A O   1 
ATOM   3054 C  CB  . LYS A 1 374 ? 60.56900 -31.94900 75.60700 1.000 27.11000 ? 374 LYS A CB  1 
ATOM   3055 C  CG  . LYS A 1 374 ? 61.88500 -32.20900 76.35800 1.000 33.22000 ? 374 LYS A CG  1 
ATOM   3056 C  CD  . LYS A 1 374 ? 62.94200 -31.21200 75.88600 1.000 34.73000 ? 374 LYS A CD  1 
ATOM   3057 C  CE  . LYS A 1 374 ? 64.17000 -31.16100 76.74400 1.000 37.00000 ? 374 LYS A CE  1 
ATOM   3058 N  NZ  . LYS A 1 374 ? 64.69900 -29.76400 76.73400 1.000 47.43000 ? 374 LYS A NZ  1 
ATOM   3059 N  N   . VAL A 1 375 ? 59.91500 -35.03200 77.09100 1.000 34.02000 ? 375 VAL A N   1 
ATOM   3060 C  CA  . VAL A 1 375 ? 60.09900 -35.71200 78.36400 1.000 33.58000 ? 375 VAL A CA  1 
ATOM   3061 C  C   . VAL A 1 375 ? 61.54900 -36.18000 78.40300 1.000 46.63000 ? 375 VAL A C   1 
ATOM   3062 O  O   . VAL A 1 375 ? 62.00500 -36.87600 77.48100 1.000 46.57000 ? 375 VAL A O   1 
ATOM   3063 C  CB  . VAL A 1 375 ? 59.13900 -36.90000 78.53100 1.000 38.76000 ? 375 VAL A CB  1 
ATOM   3064 C  CG1 . VAL A 1 375 ? 59.42100 -37.62200 79.84500 1.000 34.87000 ? 375 VAL A CG1 1 
ATOM   3065 C  CG2 . VAL A 1 375 ? 57.67700 -36.43600 78.45000 1.000 40.92000 ? 375 VAL A CG2 1 
ATOM   3066 N  N   . ASN A 1 376 ? 62.27700 -35.78600 79.45100 1.000 41.41000 ? 376 ASN A N   1 
ATOM   3067 C  CA  . ASN A 1 376 ? 63.70400 -36.10000 79.60600 1.000 41.85000 ? 376 ASN A CA  1 
ATOM   3068 C  C   . ASN A 1 376 ? 64.43500 -35.51700 78.40500 1.000 44.35000 ? 376 ASN A C   1 
ATOM   3069 O  O   . ASN A 1 376 ? 64.44600 -34.28400 78.24900 1.000 51.16000 ? 376 ASN A O   1 
ATOM   3070 C  CB  . ASN A 1 376 ? 63.87100 -37.60400 79.82800 1.000 45.82000 ? 376 ASN A CB  1 
ATOM   3071 C  CG  . ASN A 1 376 ? 63.39900 -38.03100 81.20100 1.000 44.39000 ? 376 ASN A CG  1 
ATOM   3072 O  OD1 . ASN A 1 376 ? 63.55000 -37.28700 82.17100 1.000 43.82000 ? 376 ASN A OD1 1 
ATOM   3073 N  ND2 . ASN A 1 376 ? 62.80600 -39.21800 81.28900 1.000 51.09000 ? 376 ASN A ND2 1 
ATOM   3074 N  N   . ASN A 1 377 ? 65.05400 -36.31700 77.54300 1.000 39.45000 ? 377 ASN A N   1 
ATOM   3075 C  CA  . ASN A 1 377 ? 65.61000 -35.75400 76.32300 1.000 46.52000 ? 377 ASN A CA  1 
ATOM   3076 C  C   . ASN A 1 377 ? 64.94200 -36.32000 75.07900 1.000 37.13000 ? 377 ASN A C   1 
ATOM   3077 O  O   . ASN A 1 377 ? 65.47100 -36.17600 73.97700 1.000 42.87000 ? 377 ASN A O   1 
ATOM   3078 C  CB  . ASN A 1 377 ? 67.13000 -35.94800 76.27600 1.000 58.43000 ? 377 ASN A CB  1 
ATOM   3079 C  CG  . ASN A 1 377 ? 67.88100 -34.70600 76.76900 1.000 63.34000 ? 377 ASN A CG  1 
ATOM   3080 O  OD1 . ASN A 1 377 ? 67.69200 -34.24200 77.90500 1.000 70.38000 ? 377 ASN A OD1 1 
ATOM   3081 N  ND2 . ASN A 1 377 ? 68.71800 -34.14200 75.89300 1.000 61.01000 ? 377 ASN A ND2 1 
ATOM   3082 N  N   . THR A 1 378 ? 63.76700 -36.92100 75.23600 1.000 40.31000 ? 378 THR A N   1 
ATOM   3083 C  CA  . THR A 1 378 ? 62.92700 -37.31600 74.10800 1.000 38.05000 ? 378 THR A CA  1 
ATOM   3084 C  C   . THR A 1 378 ? 62.09600 -36.11700 73.64600 1.000 34.58000 ? 378 THR A C   1 
ATOM   3085 O  O   . THR A 1 378 ? 61.29900 -35.57700 74.41800 1.000 32.46000 ? 378 THR A O   1 
ATOM   3086 C  CB  . THR A 1 378 ? 62.02700 -38.47700 74.51600 1.000 39.35000 ? 378 THR A CB  1 
ATOM   3087 O  OG1 . THR A 1 378 ? 62.79600 -39.44200 75.24400 1.000 44.61000 ? 378 THR A OG1 1 
ATOM   3088 C  CG2 . THR A 1 378 ? 61.41600 -39.14000 73.29900 1.000 45.36000 ? 378 THR A CG2 1 
ATOM   3089 N  N   . VAL A 1 379 ? 62.30200 -35.69300 72.39600 1.000 35.48000 ? 379 VAL A N   1 
ATOM   3090 C  CA  . VAL A 1 379 ? 61.57800 -34.57700 71.78700 1.000 35.55000 ? 379 VAL A CA  1 
ATOM   3091 C  C   . VAL A 1 379 ? 60.80500 -35.11200 70.58700 1.000 34.90000 ? 379 VAL A C   1 
ATOM   3092 O  O   . VAL A 1 379 ? 61.40600 -35.53200 69.58800 1.000 34.20000 ? 379 VAL A O   1 
ATOM   3093 C  CB  . VAL A 1 379 ? 62.51800 -33.43900 71.35400 1.000 32.03000 ? 379 VAL A CB  1 
ATOM   3094 C  CG1 . VAL A 1 379 ? 61.72500 -32.34900 70.61500 1.000 35.60000 ? 379 VAL A CG1 1 
ATOM   3095 C  CG2 . VAL A 1 379 ? 63.25500 -32.85200 72.54700 1.000 32.19000 ? 379 VAL A CG2 1 
ATOM   3096 N  N   . ASN A 1 380 ? 59.47600 -35.07100 70.66900 1.000 34.56000 ? 380 ASN A N   1 
ATOM   3097 C  CA  . ASN A 1 380 ? 58.62200 -35.66600 69.64400 1.000 34.56000 ? 380 ASN A CA  1 
ATOM   3098 C  C   . ASN A 1 380 ? 57.59000 -34.66300 69.17400 1.000 28.48000 ? 380 ASN A C   1 
ATOM   3099 O  O   . ASN A 1 380 ? 56.87500 -34.07200 69.99300 1.000 27.52000 ? 380 ASN A O   1 
ATOM   3100 C  CB  . ASN A 1 380 ? 57.91000 -36.92100 70.15200 1.000 27.95000 ? 380 ASN A CB  1 
ATOM   3101 C  CG  . ASN A 1 380 ? 58.83000 -38.09900 70.24000 1.000 36.83000 ? 380 ASN A CG  1 
ATOM   3102 O  OD1 . ASN A 1 380 ? 59.70300 -38.28500 69.39100 1.000 47.19000 ? 380 ASN A OD1 1 
ATOM   3103 N  ND2 . ASN A 1 380 ? 58.66400 -38.89400 71.27700 1.000 45.09000 ? 380 ASN A ND2 1 
ATOM   3104 N  N   . ILE A 1 381 ? 57.51600 -34.48700 67.85600 1.000 30.14000 ? 381 ILE A N   1 
ATOM   3105 C  CA  . ILE A 1 381 ? 56.38800 -33.80800 67.22200 1.000 24.40000 ? 381 ILE A CA  1 
ATOM   3106 C  C   . ILE A 1 381 ? 55.26200 -34.82500 67.09000 1.000 26.19000 ? 381 ILE A C   1 
ATOM   3107 O  O   . ILE A 1 381 ? 55.43300 -35.86100 66.43900 1.000 25.28000 ? 381 ILE A O   1 
ATOM   3108 C  CB  . ILE A 1 381 ? 56.78100 -33.24300 65.84800 1.000 28.94000 ? 381 ILE A CB  1 
ATOM   3109 C  CG1 . ILE A 1 381 ? 57.92600 -32.23000 65.95400 1.000 22.28000 ? 381 ILE A CG1 1 
ATOM   3110 C  CG2 . ILE A 1 381 ? 55.56600 -32.60500 65.15000 1.000 22.99000 ? 381 ILE A CG2 1 
ATOM   3111 C  CD1 . ILE A 1 381 ? 58.29600 -31.65500 64.62600 1.000 26.51000 ? 381 ILE A CD1 1 
ATOM   3112 N  N   . ILE A 1 382 ? 54.11800 -34.54200 67.70700 1.000 23.01000 ? 382 ILE A N   1 
ATOM   3113 C  CA  . ILE A 1 382 ? 53.00400 -35.48800 67.73600 1.000 28.65000 ? 382 ILE A CA  1 
ATOM   3114 C  C   . ILE A 1 382 ? 51.77900 -34.92900 67.00500 1.000 23.58000 ? 382 ILE A C   1 
ATOM   3115 O  O   . ILE A 1 382 ? 51.64100 -33.72600 66.79500 1.000 25.51000 ? 382 ILE A O   1 
ATOM   3116 C  CB  . ILE A 1 382 ? 52.64800 -35.87600 69.19200 1.000 26.61000 ? 382 ILE A CB  1 
ATOM   3117 C  CG1 . ILE A 1 382 ? 52.38000 -34.62200 70.02400 1.000 32.25000 ? 382 ILE A CG1 1 
ATOM   3118 C  CG2 . ILE A 1 382 ? 53.77200 -36.73300 69.77900 1.000 27.14000 ? 382 ILE A CG2 1 
ATOM   3119 C  CD1 . ILE A 1 382 ? 51.60100 -34.88200 71.33800 1.000 37.76000 ? 382 ILE A CD1 1 
ATOM   3120 N  N   . ASP A 1 383 ? 50.88700 -35.83800 66.60400 1.000 26.67000 ? 383 ASP A N   1 
ATOM   3121 C  CA  . ASP A 1 383 ? 49.57000 -35.49800 66.03900 1.000 26.03000 ? 383 ASP A CA  1 
ATOM   3122 C  C   . ASP A 1 383 ? 49.66400 -34.82000 64.67200 1.000 27.63000 ? 383 ASP A C   1 
ATOM   3123 O  O   . ASP A 1 383 ? 48.73800 -34.10100 64.25400 1.000 24.36000 ? 383 ASP A O   1 
ATOM   3124 C  CB  . ASP A 1 383 ? 48.75400 -34.62200 67.00700 1.000 29.26000 ? 383 ASP A CB  1 
ATOM   3125 C  CG  . ASP A 1 383 ? 48.43600 -35.33000 68.33700 1.000 47.61000 ? 383 ASP A CG  1 
ATOM   3126 O  OD1 . ASP A 1 383 ? 48.15600 -36.56200 68.32000 1.000 49.85000 ? 383 ASP A OD1 1 
ATOM   3127 O  OD2 . ASP A 1 383 ? 48.43500 -34.65600 69.40800 1.000 52.32000 ? 383 ASP A OD2 1 
ATOM   3128 N  N   . LEU A 1 384 ? 50.77400 -35.04100 63.94800 1.000 28.25000 ? 384 LEU A N   1 
ATOM   3129 C  CA  . LEU A 1 384 ? 50.86000 -34.57700 62.56700 1.000 25.38000 ? 384 LEU A CA  1 
ATOM   3130 C  C   . LEU A 1 384 ? 49.69800 -35.11500 61.74500 1.000 25.19000 ? 384 LEU A C   1 
ATOM   3131 O  O   . LEU A 1 384 ? 49.16400 -34.41300 60.88000 1.000 24.15000 ? 384 LEU A O   1 
ATOM   3132 C  CB  . LEU A 1 384 ? 52.18800 -34.98300 61.93300 1.000 22.34000 ? 384 LEU A CB  1 
ATOM   3133 C  CG  . LEU A 1 384 ? 53.38200 -34.14400 62.37800 1.000 27.52000 ? 384 LEU A CG  1 
ATOM   3134 C  CD1 . LEU A 1 384 ? 54.64600 -34.81200 61.96000 1.000 25.49000 ? 384 LEU A CD1 1 
ATOM   3135 C  CD2 . LEU A 1 384 ? 53.32400 -32.71800 61.81500 1.000 20.42000 ? 384 LEU A CD2 1 
ATOM   3136 N  N   . GLU A 1 385 ? 49.26000 -36.34200 62.02500 1.000 25.29000 ? 385 GLU A N   1 
ATOM   3137 C  CA  . GLU A 1 385 ? 48.18300 -36.90900 61.22400 1.000 24.91000 ? 385 GLU A CA  1 
ATOM   3138 C  C   . GLU A 1 385 ? 46.84900 -36.20000 61.49400 1.000 30.67000 ? 385 GLU A C   1 
ATOM   3139 O  O   . GLU A 1 385 ? 45.95600 -36.20600 60.63400 1.000 25.91000 ? 385 GLU A O   1 
ATOM   3140 C  CB  . GLU A 1 385 ? 48.08700 -38.41200 61.48500 1.000 24.61000 ? 385 GLU A CB  1 
ATOM   3141 C  CG  . GLU A 1 385 ? 47.32700 -38.78300 62.73600 1.000 32.70000 ? 385 GLU A CG  1 
ATOM   3142 C  CD  . GLU A 1 385 ? 48.20200 -38.79800 63.98800 1.000 38.22000 ? 385 GLU A CD  1 
ATOM   3143 O  OE1 . GLU A 1 385 ? 49.36800 -38.33600 63.92000 1.000 35.70000 ? 385 GLU A OE1 1 
ATOM   3144 O  OE2 . GLU A 1 385 ? 47.72100 -39.28400 65.04000 1.000 45.12000 ? 385 GLU A OE2 1 
ATOM   3145 N  N   . GLU A 1 386 ? 46.69700 -35.57700 62.67000 1.000 30.90000 ? 386 GLU A N   1 
ATOM   3146 C  CA  . GLU A 1 386 ? 45.47100 -34.84700 62.96700 1.000 27.98000 ? 386 GLU A CA  1 
ATOM   3147 C  C   . GLU A 1 386 ? 45.47500 -33.46800 62.32200 1.000 31.65000 ? 386 GLU A C   1 
ATOM   3148 O  O   . GLU A 1 386 ? 44.40900 -32.97500 61.91800 1.000 25.18000 ? 386 GLU A O   1 
ATOM   3149 C  CB  . GLU A 1 386 ? 45.26700 -34.73700 64.47800 1.000 36.85000 ? 386 GLU A CB  1 
ATOM   3150 C  CG  . GLU A 1 386 ? 44.90800 -36.06600 65.15200 1.000 40.18000 ? 386 GLU A CG  1 
ATOM   3151 C  CD  . GLU A 1 386 ? 43.70400 -36.74600 64.50000 1.000 54.94000 ? 386 GLU A CD  1 
ATOM   3152 O  OE1 . GLU A 1 386 ? 42.61000 -36.13600 64.49100 1.000 63.12000 ? 386 GLU A OE1 1 
ATOM   3153 O  OE2 . GLU A 1 386 ? 43.84800 -37.88800 63.99400 1.000 62.17000 ? 386 GLU A OE2 1 
ATOM   3154 N  N   . LEU A 1 387 ? 46.65100 -32.83900 62.21600 1.000 20.08000 ? 387 LEU A N   1 
ATOM   3155 C  CA  . LEU A 1 387 ? 46.77500 -31.66000 61.36900 1.000 24.03000 ? 387 LEU A CA  1 
ATOM   3156 C  C   . LEU A 1 387 ? 46.40400 -31.99800 59.92400 1.000 29.43000 ? 387 LEU A C   1 
ATOM   3157 O  O   . LEU A 1 387 ? 45.67000 -31.25000 59.26200 1.000 24.89000 ? 387 LEU A O   1 
ATOM   3158 C  CB  . LEU A 1 387 ? 48.20100 -31.11800 61.45600 1.000 23.51000 ? 387 LEU A CB  1 
ATOM   3159 C  CG  . LEU A 1 387 ? 48.60300 -29.97800 60.51900 1.000 26.70000 ? 387 LEU A CG  1 
ATOM   3160 C  CD1 . LEU A 1 387 ? 47.93600 -28.67400 60.94100 1.000 25.70000 ? 387 LEU A CD1 1 
ATOM   3161 C  CD2 . LEU A 1 387 ? 50.11200 -29.80700 60.48800 1.000 20.97000 ? 387 LEU A CD2 1 
ATOM   3162 N  N   . GLU A 1 388 ? 46.89200 -33.13500 59.42200 1.000 26.54000 ? 388 GLU A N   1 
ATOM   3163 C  CA  . GLU A 1 388 ? 46.54300 -33.55600 58.06900 1.000 28.37000 ? 388 GLU A CA  1 
ATOM   3164 C  C   . GLU A 1 388 ? 45.02900 -33.70500 57.90500 1.000 24.67000 ? 388 GLU A C   1 
ATOM   3165 O  O   . GLU A 1 388 ? 44.44700 -33.17300 56.95500 1.000 30.80000 ? 388 GLU A O   1 
ATOM   3166 C  CB  . GLU A 1 388 ? 47.26400 -34.85400 57.72500 1.000 27.64000 ? 388 GLU A CB  1 
ATOM   3167 C  CG  . GLU A 1 388 ? 47.07900 -35.25700 56.26500 1.000 31.79000 ? 388 GLU A CG  1 
ATOM   3168 C  CD  . GLU A 1 388 ? 47.74000 -34.28400 55.30500 1.000 31.10000 ? 388 GLU A CD  1 
ATOM   3169 O  OE1 . GLU A 1 388 ? 48.91500 -33.91900 55.53700 1.000 30.54000 ? 388 GLU A OE1 1 
ATOM   3170 O  OE2 . GLU A 1 388 ? 47.08100 -33.87800 54.31800 1.000 39.40000 ? 388 GLU A OE2 1 
ATOM   3171 N  N   . ALA A 1 389 ? 44.37300 -34.40300 58.83600 1.000 24.19000 ? 389 ALA A N   1 
ATOM   3172 C  CA  . ALA A 1 389 ? 42.91400 -34.54500 58.79300 1.000 28.90000 ? 389 ALA A CA  1 
ATOM   3173 C  C   . ALA A 1 389 ? 42.17900 -33.21400 58.73100 1.000 25.79000 ? 389 ALA A C   1 
ATOM   3174 O  O   . ALA A 1 389 ? 41.05500 -33.15400 58.23100 1.000 28.69000 ? 389 ALA A O   1 
ATOM   3175 C  CB  . ALA A 1 389 ? 42.41600 -35.31000 60.01700 1.000 29.99000 ? 389 ALA A CB  1 
ATOM   3176 N  N   . ASN A 1 390 ? 42.76900 -32.14100 59.24600 1.000 25.54000 ? 390 ASN A N   1 
ATOM   3177 C  CA  . ASN A 1 390 ? 42.07000 -30.86500 59.30800 1.000 29.61000 ? 390 ASN A CA  1 
ATOM   3178 C  C   . ASN A 1 390 ? 42.50400 -29.89500 58.21700 1.000 26.59000 ? 390 ASN A C   1 
ATOM   3179 O  O   . ASN A 1 390 ? 42.05700 -28.74000 58.21400 1.000 24.63000 ? 390 ASN A O   1 
ATOM   3180 C  CB  . ASN A 1 390 ? 42.26400 -30.24200 60.69300 1.000 27.15000 ? 390 ASN A CB  1 
ATOM   3181 C  CG  . ASN A 1 390 ? 41.42900 -30.94200 61.75700 1.000 29.39000 ? 390 ASN A CG  1 
ATOM   3182 O  OD1 . ASN A 1 390 ? 40.24300 -30.68900 61.87900 1.000 32.56000 ? 390 ASN A OD1 1 
ATOM   3183 N  ND2 . ASN A 1 390 ? 42.03400 -31.85500 62.48900 1.000 31.01000 ? 390 ASN A ND2 1 
ATOM   3184 N  N   . LYS A 1 391 ? 43.34500 -30.33900 57.28700 1.000 22.23000 ? 391 LYS A N   1 
ATOM   3185 C  CA  . LYS A 1 391 ? 43.80500 -29.44900 56.22500 1.000 26.48000 ? 391 LYS A CA  1 
ATOM   3186 C  C   . LYS A 1 391 ? 42.68100 -28.89000 55.34900 1.000 26.80000 ? 391 LYS A C   1 
ATOM   3187 O  O   . LYS A 1 391 ? 42.77100 -27.70700 54.97500 1.000 25.38000 ? 391 LYS A O   1 
ATOM   3188 C  CB  . LYS A 1 391 ? 44.86600 -30.16800 55.38200 1.000 24.64000 ? 391 LYS A CB  1 
ATOM   3189 C  CG  . LYS A 1 391 ? 45.71000 -29.24200 54.53400 1.000 28.02000 ? 391 LYS A CG  1 
ATOM   3190 C  CD  . LYS A 1 391 ? 46.46500 -30.04200 53.48800 1.000 28.76000 ? 391 LYS A CD  1 
ATOM   3191 C  CE  . LYS A 1 391 ? 47.15500 -29.14400 52.48500 1.000 29.47000 ? 391 LYS A CE  1 
ATOM   3192 N  NZ  . LYS A 1 391 ? 48.07300 -29.93500 51.64100 1.000 38.47000 ? 391 LYS A NZ  1 
ATOM   3193 N  N   . PRO A 1 392 ? 41.61000 -29.62500 55.00600 1.000 27.47000 ? 392 PRO A N   1 
ATOM   3194 C  CA  . PRO A 1 392 ? 40.56900 -28.99100 54.17200 1.000 27.53000 ? 392 PRO A CA  1 
ATOM   3195 C  C   . PRO A 1 392 ? 39.96600 -27.72800 54.79100 1.000 27.29000 ? 392 PRO A C   1 
ATOM   3196 O  O   . PRO A 1 392 ? 39.79100 -26.72900 54.08600 1.000 28.29000 ? 392 PRO A O   1 
ATOM   3197 C  CB  . PRO A 1 392 ? 39.52800 -30.10800 54.00100 1.000 28.48000 ? 392 PRO A CB  1 
ATOM   3198 C  CG  . PRO A 1 392 ? 40.29700 -31.38300 54.17200 1.000 24.96000 ? 392 PRO A CG  1 
ATOM   3199 C  CD  . PRO A 1 392 ? 41.30800 -31.05000 55.25300 1.000 27.36000 ? 392 PRO A CD  1 
ATOM   3200 N  N   . ILE A 1 393 ? 39.68200 -27.71800 56.09100 1.000 25.99000 ? 393 ILE A N   1 
ATOM   3201 C  CA  . ILE A 1 393 ? 39.13400 -26.49400 56.69000 1.000 27.23000 ? 393 ILE A CA  1 
ATOM   3202 C  C   . ILE A 1 393 ? 40.22200 -25.49800 57.10100 1.000 22.99000 ? 393 ILE A C   1 
ATOM   3203 O  O   . ILE A 1 393 ? 40.00600 -24.28400 57.01500 1.000 21.09000 ? 393 ILE A O   1 
ATOM   3204 C  CB  . ILE A 1 393 ? 38.21300 -26.81900 57.87700 1.000 27.06000 ? 393 ILE A CB  1 
ATOM   3205 C  CG1 . ILE A 1 393 ? 38.97200 -27.52000 58.99000 1.000 34.86000 ? 393 ILE A CG1 1 
ATOM   3206 C  CG2 . ILE A 1 393 ? 37.07700 -27.68900 57.42200 1.000 32.42000 ? 393 ILE A CG2 1 
ATOM   3207 C  CD1 . ILE A 1 393 ? 38.07900 -27.89900 60.15900 1.000 40.19000 ? 393 ILE A CD1 1 
ATOM   3208 N  N   . LEU A 1 394 ? 41.39300 -25.96600 57.54400 1.000 23.23000 ? 394 LEU A N   1 
ATOM   3209 C  CA  . LEU A 1 394 ? 42.47300 -25.04100 57.88600 1.000 21.90000 ? 394 LEU A CA  1 
ATOM   3210 C  C   . LEU A 1 394 ? 42.95400 -24.26300 56.65900 1.000 28.01000 ? 394 LEU A C   1 
ATOM   3211 O  O   . LEU A 1 394 ? 43.26000 -23.06000 56.75300 1.000 24.38000 ? 394 LEU A O   1 
ATOM   3212 C  CB  . LEU A 1 394 ? 43.64000 -25.80100 58.52800 1.000 22.37000 ? 394 LEU A CB  1 
ATOM   3213 C  CG  . LEU A 1 394 ? 43.53500 -26.29600 59.98100 1.000 23.84000 ? 394 LEU A CG  1 
ATOM   3214 C  CD1 . LEU A 1 394 ? 44.80700 -27.04000 60.34000 1.000 25.50000 ? 394 LEU A CD1 1 
ATOM   3215 C  CD2 . LEU A 1 394 ? 43.28600 -25.13000 60.97100 1.000 23.56000 ? 394 LEU A CD2 1 
ATOM   3216 N  N   . GLY A 1 395 ? 43.02800 -24.92600 55.50100 1.000 23.59000 ? 395 GLY A N   1 
ATOM   3217 C  CA  . GLY A 1 395 ? 43.61600 -24.32700 54.32300 1.000 24.83000 ? 395 GLY A CA  1 
ATOM   3218 C  C   . GLY A 1 395 ? 45.12700 -24.44400 54.33100 1.000 29.73000 ? 395 GLY A C   1 
ATOM   3219 O  O   . GLY A 1 395 ? 45.76300 -24.65900 55.36200 1.000 31.52000 ? 395 GLY A O   1 
ATOM   3220 N  N   . GLU A 1 396 ? 45.71600 -24.28000 53.14900 1.000 31.37000 ? 396 GLU A N   1 
ATOM   3221 C  CA  . GLU A 1 396 ? 47.11200 -24.67100 52.99200 1.000 32.87000 ? 396 GLU A CA  1 
ATOM   3222 C  C   . GLU A 1 396 ? 48.05700 -23.76200 53.76500 1.000 32.53000 ? 396 GLU A C   1 
ATOM   3223 O  O   . GLU A 1 396 ? 49.13300 -24.20900 54.17500 1.000 27.65000 ? 396 GLU A O   1 
ATOM   3224 C  CB  . GLU A 1 396 ? 47.49300 -24.69100 51.51600 1.000 35.75000 ? 396 GLU A CB  1 
ATOM   3225 C  CG  . GLU A 1 396 ? 47.34300 -23.35100 50.82800 1.000 49.48000 ? 396 GLU A CG  1 
ATOM   3226 C  CD  . GLU A 1 396 ? 48.15400 -23.25500 49.54200 1.000 63.23000 ? 396 GLU A CD  1 
ATOM   3227 O  OE1 . GLU A 1 396 ? 48.98300 -24.16000 49.28600 1.000 71.96000 ? 396 GLU A OE1 1 
ATOM   3228 O  OE2 . GLU A 1 396 ? 47.94400 -22.28700 48.77500 1.000 71.24000 ? 396 GLU A OE2 1 
ATOM   3229 N  N   . PHE A 1 397 ? 47.68200 -22.49900 53.98000 1.000 26.92000 ? 397 PHE A N   1 
ATOM   3230 C  CA  . PHE A 1 397 ? 48.61100 -21.57000 54.61500 1.000 30.47000 ? 397 PHE A CA  1 
ATOM   3231 C  C   . PHE A 1 397 ? 48.76600 -21.84700 56.10700 1.000 31.29000 ? 397 PHE A C   1 
ATOM   3232 O  O   . PHE A 1 397 ? 49.88300 -21.79100 56.63800 1.000 28.57000 ? 397 PHE A O   1 
ATOM   3233 C  CB  . PHE A 1 397 ? 48.16100 -20.13700 54.38500 1.000 34.90000 ? 397 PHE A CB  1 
ATOM   3234 C  CG  . PHE A 1 397 ? 48.41500 -19.65600 53.00000 1.000 41.35000 ? 397 PHE A CG  1 
ATOM   3235 C  CD1 . PHE A 1 397 ? 47.48100 -19.87400 51.99600 1.000 49.19000 ? 397 PHE A CD1 1 
ATOM   3236 C  CD2 . PHE A 1 397 ? 49.59700 -18.99600 52.68700 1.000 51.45000 ? 397 PHE A CD2 1 
ATOM   3237 C  CE1 . PHE A 1 397 ? 47.72000 -19.43700 50.69700 1.000 50.41000 ? 397 PHE A CE1 1 
ATOM   3238 C  CE2 . PHE A 1 397 ? 49.84600 -18.55300 51.39000 1.000 52.46000 ? 397 PHE A CE2 1 
ATOM   3239 C  CZ  . PHE A 1 397 ? 48.90500 -18.77700 50.39600 1.000 49.53000 ? 397 PHE A CZ  1 
ATOM   3240 N  N   . LEU A 1 398 ? 47.64900 -22.07800 56.81500 1.000 26.47000 ? 398 LEU A N   1 
ATOM   3241 C  CA  . LEU A 1 398 ? 47.73300 -22.48000 58.21800 1.000 28.61000 ? 398 LEU A CA  1 
ATOM   3242 C  C   . LEU A 1 398 ? 48.42500 -23.82200 58.34800 1.000 26.45000 ? 398 LEU A C   1 
ATOM   3243 O  O   . LEU A 1 398 ? 49.21300 -24.04200 59.27200 1.000 27.63000 ? 398 LEU A O   1 
ATOM   3244 C  CB  . LEU A 1 398 ? 46.33800 -22.58100 58.83200 1.000 24.27000 ? 398 LEU A CB  1 
ATOM   3245 C  CG  . LEU A 1 398 ? 45.67200 -21.31500 59.33300 1.000 29.05000 ? 398 LEU A CG  1 
ATOM   3246 C  CD1 . LEU A 1 398 ? 44.25300 -21.65500 59.84500 1.000 21.63000 ? 398 LEU A CD1 1 
ATOM   3247 C  CD2 . LEU A 1 398 ? 46.55000 -20.68300 60.41000 1.000 24.19000 ? 398 LEU A CD2 1 
ATOM   3248 N  N   . TYR A 1 399 ? 48.08700 -24.74700 57.44900 1.000 26.54000 ? 399 TYR A N   1 
ATOM   3249 C  CA  . TYR A 1 399 ? 48.71400 -26.05600 57.42800 1.000 27.50000 ? 399 TYR A CA  1 
ATOM   3250 C  C   . TYR A 1 399 ? 50.22000 -25.92800 57.32400 1.000 27.47000 ? 399 TYR A C   1 
ATOM   3251 O  O   . TYR A 1 399 ? 50.95600 -26.52400 58.11500 1.000 24.39000 ? 399 TYR A O   1 
ATOM   3252 C  CB  . TYR A 1 399 ? 48.15600 -26.85400 56.26000 1.000 24.64000 ? 399 TYR A CB  1 
ATOM   3253 C  CG  . TYR A 1 399 ? 48.77300 -28.21200 56.06600 1.000 30.57000 ? 399 TYR A CG  1 
ATOM   3254 C  CD1 . TYR A 1 399 ? 48.31000 -29.31600 56.77000 1.000 22.67000 ? 399 TYR A CD1 1 
ATOM   3255 C  CD2 . TYR A 1 399 ? 49.79900 -28.40200 55.14000 1.000 30.28000 ? 399 TYR A CD2 1 
ATOM   3256 C  CE1 . TYR A 1 399 ? 48.87200 -30.55900 56.57300 1.000 28.28000 ? 399 TYR A CE1 1 
ATOM   3257 C  CE2 . TYR A 1 399 ? 50.34900 -29.64700 54.93300 1.000 26.04000 ? 399 TYR A CE2 1 
ATOM   3258 C  CZ  . TYR A 1 399 ? 49.88600 -30.71500 55.64900 1.000 22.11000 ? 399 TYR A CZ  1 
ATOM   3259 O  OH  . TYR A 1 399 ? 50.44700 -31.93800 55.44900 1.000 27.90000 ? 399 TYR A OH  1 
ATOM   3260 N  N   . LYS A 1 400 ? 50.69900 -25.13700 56.35700 1.000 26.78000 ? 400 LYS A N   1 
ATOM   3261 C  CA  . LYS A 1 400 ? 52.13800 -24.98100 56.17700 1.000 26.87000 ? 400 LYS A CA  1 
ATOM   3262 C  C   . LYS A 1 400 ? 52.75800 -24.27400 57.36700 1.000 29.55000 ? 400 LYS A C   1 
ATOM   3263 O  O   . LYS A 1 400 ? 53.85600 -24.63000 57.80900 1.000 24.11000 ? 400 LYS A O   1 
ATOM   3264 C  CB  . LYS A 1 400 ? 52.45100 -24.21100 54.89000 1.000 30.65000 ? 400 LYS A CB  1 
ATOM   3265 C  CG  . LYS A 1 400 ? 52.13000 -25.00000 53.63200 1.000 33.90000 ? 400 LYS A CG  1 
ATOM   3266 C  CD  . LYS A 1 400 ? 53.01300 -24.63400 52.46200 1.000 41.88000 ? 400 LYS A CD  1 
ATOM   3267 C  CE  . LYS A 1 400 ? 52.26700 -23.78200 51.45900 1.000 48.12000 ? 400 LYS A CE  1 
ATOM   3268 N  NZ  . LYS A 1 400 ? 51.77000 -24.60400 50.32400 1.000 61.73000 ? 400 LYS A NZ  1 
ATOM   3269 N  N   . LYS A 1 401 ? 52.07500 -23.25900 57.88900 1.000 29.19000 ? 401 LYS A N   1 
ATOM   3270 C  CA  . LYS A 1 401 ? 52.61000 -22.52800 59.02700 1.000 28.36000 ? 401 LYS A CA  1 
ATOM   3271 C  C   . LYS A 1 401 ? 52.71800 -23.43600 60.25900 1.000 25.05000 ? 401 LYS A C   1 
ATOM   3272 O  O   . LYS A 1 401 ? 53.70900 -23.38900 60.98900 1.000 22.88000 ? 401 LYS A O   1 
ATOM   3273 C  CB  . LYS A 1 401 ? 51.72900 -21.30400 59.27300 1.000 27.79000 ? 401 LYS A CB  1 
ATOM   3274 C  CG  . LYS A 1 401 ? 52.09400 -20.47200 60.46200 1.000 33.31000 ? 401 LYS A CG  1 
ATOM   3275 C  CD  . LYS A 1 401 ? 53.33200 -19.61600 60.21500 1.000 35.97000 ? 401 LYS A CD  1 
ATOM   3276 C  CE  . LYS A 1 401 ? 53.61300 -18.73900 61.44800 1.000 34.85000 ? 401 LYS A CE  1 
ATOM   3277 N  NZ  . LYS A 1 401 ? 54.93600 -18.05800 61.40500 1.000 46.85000 ? 401 LYS A NZ  1 
ATOM   3278 N  N   . ALA A 1 402 ? 51.73900 -24.31300 60.48000 1.000 23.26000 ? 402 ALA A N   1 
ATOM   3279 C  CA  . ALA A 1 402 ? 51.84600 -25.19900 61.64200 1.000 22.94000 ? 402 ALA A CA  1 
ATOM   3280 C  C   . ALA A 1 402 ? 52.99000 -26.19900 61.49300 1.000 27.17000 ? 402 ALA A C   1 
ATOM   3281 O  O   . ALA A 1 402 ? 53.60600 -26.58700 62.49600 1.000 27.78000 ? 402 ALA A O   1 
ATOM   3282 C  CB  . ALA A 1 402 ? 50.52900 -25.93900 61.87900 1.000 26.65000 ? 402 ALA A CB  1 
ATOM   3283 N  N   . LEU A 1 403 ? 53.28500 -26.63000 60.26000 1.000 25.55000 ? 403 LEU A N   1 
ATOM   3284 C  CA  . LEU A 1 403 ? 54.46000 -27.46900 60.02500 1.000 27.76000 ? 403 LEU A CA  1 
ATOM   3285 C  C   . LEU A 1 403 ? 55.76800 -26.70200 60.27500 1.000 28.12000 ? 403 LEU A C   1 
ATOM   3286 O  O   . LEU A 1 403 ? 56.71600 -27.26600 60.84000 1.000 27.70000 ? 403 LEU A O   1 
ATOM   3287 C  CB  . LEU A 1 403 ? 54.42800 -28.04500 58.60500 1.000 26.49000 ? 403 LEU A CB  1 
ATOM   3288 C  CG  . LEU A 1 403 ? 53.35700 -29.09800 58.29200 1.000 30.00000 ? 403 LEU A CG  1 
ATOM   3289 C  CD1 . LEU A 1 403 ? 53.38200 -29.48100 56.79500 1.000 23.83000 ? 403 LEU A CD1 1 
ATOM   3290 C  CD2 . LEU A 1 403 ? 53.50600 -30.34600 59.18500 1.000 25.62000 ? 403 LEU A CD2 1 
ATOM   3291 N  N   . GLU A 1 404 ? 55.84800 -25.42400 59.87900 1.000 26.25000 ? 404 GLU A N   1 
ATOM   3292 C  CA  . GLU A 1 404 ? 57.06900 -24.65100 60.14300 1.000 28.48000 ? 404 GLU A CA  1 
ATOM   3293 C  C   . GLU A 1 404 ? 57.29000 -24.48100 61.63500 1.000 25.34000 ? 404 GLU A C   1 
ATOM   3294 O  O   . GLU A 1 404 ? 58.41600 -24.62100 62.12900 1.000 28.67000 ? 404 GLU A O   1 
ATOM   3295 C  CB  . GLU A 1 404 ? 57.01600 -23.25000 59.53100 1.000 35.02000 ? 404 GLU A CB  1 
ATOM   3296 C  CG  . GLU A 1 404 ? 57.05500 -23.08300 58.04300 1.000 48.51000 ? 404 GLU A CG  1 
ATOM   3297 C  CD  . GLU A 1 404 ? 56.61100 -21.65900 57.66800 1.000 53.76000 ? 404 GLU A CD  1 
ATOM   3298 O  OE1 . GLU A 1 404 ? 57.04600 -20.70200 58.35300 1.000 53.93000 ? 404 GLU A OE1 1 
ATOM   3299 O  OE2 . GLU A 1 404 ? 55.80500 -21.49800 56.72200 1.000 53.61000 ? 404 GLU A OE2 1 
ATOM   3300 N  N   . ILE A 1 405 ? 56.23300 -24.09900 62.35900 1.000 25.64000 ? 405 ILE A N   1 
ATOM   3301 C  CA  . ILE A 1 405 ? 56.34800 -23.87800 63.79800 1.000 29.09000 ? 405 ILE A CA  1 
ATOM   3302 C  C   . ILE A 1 405 ? 56.78700 -25.16000 64.49300 1.000 26.28000 ? 405 ILE A C   1 
ATOM   3303 O  O   . ILE A 1 405 ? 57.71500 -25.15800 65.31300 1.000 21.98000 ? 405 ILE A O   1 
ATOM   3304 C  CB  . ILE A 1 405 ? 55.01800 -23.35700 64.37500 1.000 26.01000 ? 405 ILE A CB  1 
ATOM   3305 C  CG1 . ILE A 1 405 ? 54.69500 -21.95800 63.84500 1.000 31.79000 ? 405 ILE A CG1 1 
ATOM   3306 C  CG2 . ILE A 1 405 ? 55.08700 -23.33200 65.88100 1.000 27.49000 ? 405 ILE A CG2 1 
ATOM   3307 C  CD1 . ILE A 1 405 ? 53.19700 -21.77100 63.64800 1.000 29.86000 ? 405 ILE A CD1 1 
ATOM   3308 N  N   . ALA A 1 406 ? 56.13400 -26.27800 64.15400 1.000 25.86000 ? 406 ALA A N   1 
ATOM   3309 C  CA  . ALA A 1 406 ? 56.47000 -27.57000 64.75000 1.000 28.45000 ? 406 ALA A CA  1 
ATOM   3310 C  C   . ALA A 1 406 ? 57.95500 -27.87800 64.59100 1.000 30.63000 ? 406 ALA A C   1 
ATOM   3311 O  O   . ALA A 1 406 ? 58.64300 -28.21200 65.56600 1.000 28.36000 ? 406 ALA A O   1 
ATOM   3312 C  CB  . ALA A 1 406 ? 55.60900 -28.66900 64.12700 1.000 24.75000 ? 406 ALA A CB  1 
ATOM   3313 N  N   . GLN A 1 407 ? 58.47000 -27.75300 63.36300 1.000 32.22000 ? 407 GLN A N   1 
ATOM   3314 C  CA  . GLN A 1 407 ? 59.89100 -27.98700 63.11700 1.000 27.21000 ? 407 GLN A CA  1 
ATOM   3315 C  C   . GLN A 1 407 ? 60.75600 -27.02600 63.93100 1.000 30.45000 ? 407 GLN A C   1 
ATOM   3316 O  O   . GLN A 1 407 ? 61.74300 -27.44200 64.55200 1.000 29.78000 ? 407 GLN A O   1 
ATOM   3317 C  CB  . GLN A 1 407 ? 60.17300 -27.85600 61.61500 1.000 31.95000 ? 407 GLN A CB  1 
ATOM   3318 C  CG  . GLN A 1 407 ? 61.55900 -28.29000 61.18800 1.000 33.27000 ? 407 GLN A CG  1 
ATOM   3319 C  CD  . GLN A 1 407 ? 61.86700 -29.72500 61.60300 1.000 43.90000 ? 407 GLN A CD  1 
ATOM   3320 O  OE1 . GLN A 1 407 ? 62.74200 -29.95900 62.43600 1.000 46.66000 ? 407 GLN A OE1 1 
ATOM   3321 N  NE2 . GLN A 1 407 ? 61.13200 -30.68700 61.04300 1.000 48.83000 ? 407 GLN A NE2 1 
ATOM   3322 N  N   . ASN A 1 408 ? 60.38200 -25.73900 63.96000 1.000 26.76000 ? 408 ASN A N   1 
ATOM   3323 C  CA  . ASN A 1 408 ? 61.11500 -24.75200 64.74500 1.000 30.24000 ? 408 ASN A CA  1 
ATOM   3324 C  C   . ASN A 1 408 ? 61.17000 -25.14200 66.21400 1.000 30.85000 ? 408 ASN A C   1 
ATOM   3325 O  O   . ASN A 1 408 ? 62.22500 -25.05300 66.85300 1.000 32.79000 ? 408 ASN A O   1 
ATOM   3326 C  CB  . ASN A 1 408 ? 60.47500 -23.36800 64.59700 1.000 25.53000 ? 408 ASN A CB  1 
ATOM   3327 C  CG  . ASN A 1 408 ? 60.71200 -22.76400 63.23300 1.000 33.12000 ? 408 ASN A CG  1 
ATOM   3328 O  OD1 . ASN A 1 408 ? 61.52900 -23.26600 62.45700 1.000 41.64000 ? 408 ASN A OD1 1 
ATOM   3329 N  ND2 . ASN A 1 408 ? 60.00400 -21.68700 62.92700 1.000 35.91000 ? 408 ASN A ND2 1 
ATOM   3330 N  N   . ILE A 1 409 ? 60.03800 -25.54800 66.77600 1.000 25.78000 ? 409 ILE A N   1 
ATOM   3331 C  CA  . ILE A 1 409 ? 59.98900 -25.87900 68.19800 1.000 25.37000 ? 409 ILE A CA  1 
ATOM   3332 C  C   . ILE A 1 409 ? 60.85700 -27.10600 68.48500 1.000 29.17000 ? 409 ILE A C   1 
ATOM   3333 O  O   . ILE A 1 409 ? 61.63800 -27.12700 69.44700 1.000 30.01000 ? 409 ILE A O   1 
ATOM   3334 C  CB  . ILE A 1 409 ? 58.53000 -26.08700 68.64400 1.000 25.16000 ? 409 ILE A CB  1 
ATOM   3335 C  CG1 . ILE A 1 409 ? 57.75100 -24.77200 68.57900 1.000 26.35000 ? 409 ILE A CG1 1 
ATOM   3336 C  CG2 . ILE A 1 409 ? 58.45300 -26.69900 70.05100 1.000 26.20000 ? 409 ILE A CG2 1 
ATOM   3337 C  CD1 . ILE A 1 409 ? 58.19500 -23.77300 69.61000 1.000 29.94000 ? 409 ILE A CD1 1 
ATOM   3338 N  N   . LYS A 1 410 ? 60.74600 -28.14200 67.64200 1.000 29.11000 ? 410 LYS A N   1 
ATOM   3339 C  CA  . LYS A 1 410 ? 61.58500 -29.33100 67.79700 1.000 29.96000 ? 410 LYS A CA  1 
ATOM   3340 C  C   . LYS A 1 410 ? 63.06800 -28.96200 67.80600 1.000 34.76000 ? 410 LYS A C   1 
ATOM   3341 O  O   . LYS A 1 410 ? 63.82400 -29.40200 68.68100 1.000 33.23000 ? 410 LYS A O   1 
ATOM   3342 C  CB  . LYS A 1 410 ? 61.27700 -30.33200 66.68200 1.000 30.63000 ? 410 LYS A CB  1 
ATOM   3343 C  CG  . LYS A 1 410 ? 62.07300 -31.62900 66.72200 1.000 32.50000 ? 410 LYS A CG  1 
ATOM   3344 C  CD  . LYS A 1 410 ? 61.73100 -32.46000 65.48600 1.000 35.02000 ? 410 LYS A CD  1 
ATOM   3345 C  CE  . LYS A 1 410 ? 62.41500 -33.81600 65.44900 1.000 39.07000 ? 410 LYS A CE  1 
ATOM   3346 N  NZ  . LYS A 1 410 ? 62.28100 -34.54300 66.74800 1.000 42.57000 ? 410 LYS A NZ  1 
ATOM   3347 N  N   . ASP A 1 411 ? 63.49600 -28.13700 66.84200 1.000 30.86000 ? 411 ASP A N   1 
ATOM   3348 C  CA  . ASP A 1 411 ? 64.88400 -27.68000 66.79800 1.000 34.17000 ? 411 ASP A CA  1 
ATOM   3349 C  C   . ASP A 1 411 ? 65.27000 -26.92000 68.06900 1.000 32.24000 ? 411 ASP A C   1 
ATOM   3350 O  O   . ASP A 1 411 ? 66.36600 -27.10800 68.59900 1.000 40.63000 ? 411 ASP A O   1 
ATOM   3351 C  CB  . ASP A 1 411 ? 65.12400 -26.78800 65.57000 1.000 32.93000 ? 411 ASP A CB  1 
ATOM   3352 C  CG  . ASP A 1 411 ? 64.96700 -27.52800 64.23900 1.000 42.43000 ? 411 ASP A CG  1 
ATOM   3353 O  OD1 . ASP A 1 411 ? 65.05800 -28.78300 64.21200 1.000 46.52000 ? 411 ASP A OD1 1 
ATOM   3354 O  OD2 . ASP A 1 411 ? 64.74000 -26.84600 63.20600 1.000 44.59000 ? 411 ASP A OD2 1 
ATOM   3355 N  N   . LYS A 1 412 ? 64.40100 -26.03800 68.56100 1.000 31.61000 ? 412 LYS A N   1 
ATOM   3356 C  CA  . LYS A 1 412 ? 64.72600 -25.30700 69.78100 1.000 33.60000 ? 412 LYS A CA  1 
ATOM   3357 C  C   . LYS A 1 412 ? 64.82100 -26.23900 70.98200 1.000 39.24000 ? 412 LYS A C   1 
ATOM   3358 O  O   . LYS A 1 412 ? 65.75900 -26.13300 71.78600 1.000 38.16000 ? 412 LYS A O   1 
ATOM   3359 C  CB  . LYS A 1 412 ? 63.69400 -24.21300 70.04300 1.000 37.69000 ? 412 LYS A CB  1 
ATOM   3360 C  CG  . LYS A 1 412 ? 64.13300 -23.22200 71.11100 1.000 50.76000 ? 412 LYS A CG  1 
ATOM   3361 C  CD  . LYS A 1 412 ? 62.95500 -22.43600 71.69700 1.000 60.79000 ? 412 LYS A CD  1 
ATOM   3362 C  CE  . LYS A 1 412 ? 61.99300 -23.29900 72.52300 1.000 52.71000 ? 412 LYS A CE  1 
ATOM   3363 N  NZ  . LYS A 1 412 ? 60.76500 -22.52000 72.87100 1.000 50.23000 ? 412 LYS A NZ  1 
ATOM   3364 N  N   . LEU A 1 413 ? 63.86000 -27.15800 71.11600 1.000 37.41000 ? 413 LEU A N   1 
ATOM   3365 C  CA  . LEU A 1 413 ? 63.84900 -28.10600 72.22700 1.000 35.55000 ? 413 LEU A CA  1 
ATOM   3366 C  C   . LEU A 1 413 ? 65.02100 -29.07400 72.17100 1.000 39.99000 ? 413 LEU A C   1 
ATOM   3367 O  O   . LEU A 1 413 ? 65.35400 -29.68900 73.18900 1.000 44.05000 ? 413 LEU A O   1 
ATOM   3368 C  CB  . LEU A 1 413 ? 62.54800 -28.90000 72.22700 1.000 27.80000 ? 413 LEU A CB  1 
ATOM   3369 C  CG  . LEU A 1 413 ? 61.29500 -28.11200 72.60100 1.000 34.79000 ? 413 LEU A CG  1 
ATOM   3370 C  CD1 . LEU A 1 413 ? 60.08500 -29.05200 72.63300 1.000 24.40000 ? 413 LEU A CD1 1 
ATOM   3371 C  CD2 . LEU A 1 413 ? 61.49000 -27.43300 73.94200 1.000 28.78000 ? 413 LEU A CD2 1 
ATOM   3372 N  N   . ASN A 1 414 ? 65.64600 -29.22200 71.01000 1.000 38.59000 ? 414 ASN A N   1 
ATOM   3373 C  CA  . ASN A 1 414 ? 66.75800 -30.13800 70.83600 1.000 42.33000 ? 414 ASN A CA  1 
ATOM   3374 C  C   . ASN A 1 414 ? 68.12300 -29.48500 71.00900 1.000 38.88000 ? 414 ASN A C   1 
ATOM   3375 O  O   . ASN A 1 414 ? 69.13000 -30.18600 70.91400 1.000 37.22000 ? 414 ASN A O   1 
ATOM   3376 C  CB  . ASN A 1 414 ? 66.67500 -30.79600 69.46300 1.000 34.58000 ? 414 ASN A CB  1 
ATOM   3377 C  CG  . ASN A 1 414 ? 65.83800 -32.04000 69.49100 1.000 39.25000 ? 414 ASN A CG  1 
ATOM   3378 O  OD1 . ASN A 1 414 ? 65.74300 -32.69800 70.52800 1.000 40.73000 ? 414 ASN A OD1 1 
ATOM   3379 N  ND2 . ASN A 1 414 ? 65.21900 -32.37700 68.36300 1.000 40.96000 ? 414 ASN A ND2 1 
ATOM   3380 N  N   . GLU A 1 415 ? 68.18900 -28.18900 71.29200 1.000 34.16000 ? 415 GLU A N   1 
ATOM   3381 C  CA  . GLU A 1 415 ? 69.47500 -27.48900 71.34600 1.000 40.49000 ? 415 GLU A CA  1 
ATOM   3382 C  C   . GLU A 1 415 ? 70.21900 -27.65200 72.67400 1.000 40.36000 ? 415 GLU A C   1 
ATOM   3383 O  O   . GLU A 1 415 ? 69.69800 -28.23200 73.62800 1.000 52.38000 ? 415 GLU A O   1 
ATOM   3384 C  CB  . GLU A 1 415 ? 69.26500 -26.00300 71.05400 1.000 45.87000 ? 415 GLU A CB  1 
ATOM   3385 C  CG  . GLU A 1 415 ? 69.18100 -25.70400 69.57200 1.000 46.22000 ? 415 GLU A CG  1 
ATOM   3386 C  CD  . GLU A 1 415 ? 68.94400 -24.24900 69.27600 1.000 68.79000 ? 415 GLU A CD  1 
ATOM   3387 O  OE1 . GLU A 1 415 ? 68.69400 -23.48800 70.23500 1.000 64.28000 ? 415 GLU A OE1 1 
ATOM   3388 O  OE2 . GLU A 1 415 ? 69.01000 -23.87000 68.08300 1.000 68.08000 ? 415 GLU A OE2 1 
HETATM 3389 MG MG  . MG  B 2 .   ? 47.46000 -28.60300 70.47400 1.000 30.00000 ? 501 MG  A MG  1 
HETATM 3390 MG MG  . MG  C 2 .   ? 45.82400 -33.74900 70.95200 1.000 30.00000 ? 502 MG  A MG  1 
HETATM 3391 O  O   . HOH D 3 .   ? 47.35100 -32.23900 69.41200 1.000 38.26000 ? 601 HOH A O   1 
HETATM 3392 O  O   . HOH D 3 .   ? 27.11800 9.23600   58.92400 1.000 44.44000 ? 602 HOH A O   1 
HETATM 3393 O  O   . HOH D 3 .   ? 59.08800 -31.50000 61.16700 1.000 53.08000 ? 603 HOH A O   1 
HETATM 3394 O  O   . HOH D 3 .   ? 48.90900 -32.82500 77.95600 1.000 57.93000 ? 604 HOH A O   1 
HETATM 3395 O  O   . HOH D 3 .   ? 61.94600 -37.46900 83.89000 1.000 49.49000 ? 605 HOH A O   1 
HETATM 3396 O  O   . HOH D 3 .   ? 42.24900 -26.05800 88.44000 1.000 41.71000 ? 606 HOH A O   1 
HETATM 3397 O  O   . HOH D 3 .   ? 38.05300 -15.48500 68.29700 1.000 21.40000 ? 607 HOH A O   1 
HETATM 3398 O  O   . HOH D 3 .   ? 33.89700 -17.01300 75.50900 1.000 32.95000 ? 608 HOH A O   1 
HETATM 3399 O  O   . HOH D 3 .   ? 48.51200 -6.22800  57.63900 1.000 40.03000 ? 609 HOH A O   1 
HETATM 3400 O  O   . HOH D 3 .   ? 42.15900 -7.42400  66.50900 1.000 27.35000 ? 610 HOH A O   1 
HETATM 3401 O  O   . HOH D 3 .   ? 46.44100 9.56200   73.11400 1.000 55.33000 ? 611 HOH A O   1 
HETATM 3402 O  O   . HOH D 3 .   ? 50.98600 -2.72000  81.18400 1.000 45.32000 ? 612 HOH A O   1 
HETATM 3403 O  O   . HOH D 3 .   ? 59.21000 -18.47500 73.63400 1.000 41.91000 ? 613 HOH A O   1 
HETATM 3404 O  O   . HOH D 3 .   ? 38.40100 -29.47200 79.09800 1.000 35.45000 ? 614 HOH A O   1 
HETATM 3405 O  O   . HOH D 3 .   ? 8.74500  -23.40700 59.27500 1.000 33.44000 ? 615 HOH A O   1 
HETATM 3406 O  O   . HOH D 3 .   ? 45.17000 -39.79800 64.74600 1.000 47.69000 ? 616 HOH A O   1 
HETATM 3407 O  O   . HOH D 3 .   ? 60.90500 -24.67600 60.55700 1.000 40.60000 ? 617 HOH A O   1 
HETATM 3408 O  O   . HOH D 3 .   ? 31.03800 -8.36400  60.89400 1.000 27.55000 ? 618 HOH A O   1 
HETATM 3409 O  O   . HOH D 3 .   ? 11.93900 -39.80100 55.29900 1.000 38.45000 ? 619 HOH A O   1 
HETATM 3410 O  O   . HOH D 3 .   ? 58.83000 -9.28700  76.95600 1.000 60.81000 ? 620 HOH A O   1 
HETATM 3411 O  O   . HOH D 3 .   ? 36.97300 -10.39300 67.04200 1.000 35.17000 ? 621 HOH A O   1 
HETATM 3412 O  O   . HOH D 3 .   ? 63.97400 -35.07300 68.50100 1.000 44.09000 ? 622 HOH A O   1 
HETATM 3413 O  O   . HOH D 3 .   ? 45.11200 -21.50000 55.62000 1.000 22.68000 ? 623 HOH A O   1 
HETATM 3414 O  O   . HOH D 3 .   ? 33.90100 -20.80100 67.78000 1.000 38.99000 ? 624 HOH A O   1 
HETATM 3415 O  O   . HOH D 3 .   ? 19.61600 -14.69100 50.13000 1.000 51.83000 ? 625 HOH A O   1 
HETATM 3416 O  O   . HOH D 3 .   ? 9.98000  0.66300   50.83000 1.000 52.09000 ? 626 HOH A O   1 
HETATM 3417 O  O   . HOH D 3 .   ? 45.45900 -33.21200 67.95400 1.000 34.63000 ? 627 HOH A O   1 
HETATM 3418 O  O   . HOH D 3 .   ? 47.34900 -6.45500  87.50500 1.000 36.78000 ? 628 HOH A O   1 
HETATM 3419 O  O   . HOH D 3 .   ? 44.63700 -33.60900 53.75500 1.000 44.46000 ? 629 HOH A O   1 
HETATM 3420 O  O   . HOH D 3 .   ? 44.36900 -4.50800  50.49100 1.000 51.04000 ? 630 HOH A O   1 
HETATM 3421 O  O   . HOH D 3 .   ? 44.70200 -13.37700 55.61800 1.000 29.30000 ? 631 HOH A O   1 
HETATM 3422 O  O   . HOH D 3 .   ? 37.90400 9.69700   72.87500 1.000 38.76000 ? 632 HOH A O   1 
HETATM 3423 O  O   . HOH D 3 .   ? 19.67300 -33.45100 69.06900 1.000 42.69000 ? 633 HOH A O   1 
HETATM 3424 O  O   . HOH D 3 .   ? 48.88200 -11.95700 58.34900 1.000 42.65000 ? 634 HOH A O   1 
HETATM 3425 O  O   . HOH D 3 .   ? 6.11300  0.82600   53.45800 1.000 42.12000 ? 635 HOH A O   1 
HETATM 3426 O  O   . HOH D 3 .   ? 57.04100 -19.84100 60.76700 1.000 50.57000 ? 636 HOH A O   1 
HETATM 3427 O  O   . HOH D 3 .   ? 63.48400 -33.03400 89.85800 1.000 40.45000 ? 637 HOH A O   1 
HETATM 3428 O  O   . HOH D 3 .   ? 32.28600 -29.71600 61.15400 1.000 44.15000 ? 638 HOH A O   1 
HETATM 3429 O  O   . HOH D 3 .   ? 36.84600 -32.38000 72.49200 1.000 47.33000 ? 639 HOH A O   1 
HETATM 3430 O  O   . HOH D 3 .   ? 15.19700 -2.93800  43.64000 1.000 37.27000 ? 640 HOH A O   1 
HETATM 3431 O  O   . HOH D 3 .   ? 45.92800 -30.13100 69.97700 1.000 37.00000 ? 641 HOH A O   1 
HETATM 3432 O  O   . HOH D 3 .   ? 52.10900 -33.69300 92.54900 1.000 29.63000 ? 642 HOH A O   1 
HETATM 3433 O  O   . HOH D 3 .   ? 51.07900 -8.98800  69.69000 1.000 33.61000 ? 643 HOH A O   1 
HETATM 3434 O  O   . HOH D 3 .   ? 17.47300 -12.78200 51.26900 1.000 29.64000 ? 644 HOH A O   1 
HETATM 3435 O  O   . HOH D 3 .   ? 5.41700  1.15500   56.80300 1.000 49.99000 ? 645 HOH A O   1 
HETATM 3436 O  O   . HOH D 3 .   ? 23.09400 9.28800   44.16900 1.000 32.67000 ? 646 HOH A O   1 
HETATM 3437 O  O   . HOH D 3 .   ? 13.07400 -33.96000 50.56400 1.000 44.94000 ? 647 HOH A O   1 
HETATM 3438 O  O   . HOH D 3 .   ? 15.40800 -5.29600  42.50700 1.000 42.31000 ? 648 HOH A O   1 
HETATM 3439 O  O   . HOH D 3 .   ? 20.00400 -30.03900 51.49100 1.000 48.57000 ? 649 HOH A O   1 
HETATM 3440 O  O   . HOH D 3 .   ? 27.36700 -0.04400  71.06600 1.000 38.97000 ? 650 HOH A O   1 
HETATM 3441 O  O   . HOH D 3 .   ? 21.17000 -4.46300  41.36400 1.000 44.84000 ? 651 HOH A O   1 
HETATM 3442 O  O   . HOH D 3 .   ? 34.96700 -22.12100 60.52400 1.000 25.67000 ? 652 HOH A O   1 
HETATM 3443 O  O   . HOH D 3 .   ? 57.52200 -14.71500 74.93200 1.000 43.85000 ? 653 HOH A O   1 
HETATM 3444 O  O   . HOH D 3 .   ? 55.54700 -25.66700 56.07500 1.000 33.13000 ? 654 HOH A O   1 
HETATM 3445 O  O   . HOH D 3 .   ? 9.24800  -1.98600  51.36300 1.000 39.87000 ? 655 HOH A O   1 
HETATM 3446 O  O   . HOH D 3 .   ? 59.11600 -37.28300 83.64000 1.000 37.22000 ? 656 HOH A O   1 
HETATM 3447 O  O   . HOH D 3 .   ? 35.00800 -11.40200 77.26500 1.000 38.35000 ? 657 HOH A O   1 
HETATM 3448 O  O   . HOH D 3 .   ? 21.81100 -18.13500 46.38900 1.000 40.46000 ? 658 HOH A O   1 
HETATM 3449 O  O   . HOH D 3 .   ? 41.27300 -36.46700 92.39700 1.000 49.68000 ? 659 HOH A O   1 
HETATM 3450 O  O   . HOH D 3 .   ? 17.64500 -29.09100 44.98300 1.000 40.18000 ? 660 HOH A O   1 
HETATM 3451 O  O   . HOH D 3 .   ? 14.41900 -2.01900  55.49400 1.000 29.78000 ? 661 HOH A O   1 
HETATM 3452 O  O   . HOH D 3 .   ? 52.55800 -32.47000 53.90700 1.000 32.80000 ? 662 HOH A O   1 
HETATM 3453 O  O   . HOH D 3 .   ? 34.45600 -2.58100  64.78500 1.000 24.81000 ? 663 HOH A O   1 
HETATM 3454 O  O   . HOH D 3 .   ? 7.87600  -33.87500 46.94600 1.000 43.52000 ? 664 HOH A O   1 
HETATM 3455 O  O   . HOH D 3 .   ? 44.03000 -16.56600 67.40200 1.000 24.97000 ? 665 HOH A O   1 
HETATM 3456 O  O   . HOH D 3 .   ? 61.90800 -33.55900 80.89700 1.000 40.41000 ? 666 HOH A O   1 
HETATM 3457 O  O   . HOH D 3 .   ? 9.15500  4.78300   60.26700 1.000 41.37000 ? 667 HOH A O   1 
HETATM 3458 O  O   . HOH D 3 .   ? 57.45900 -25.31600 96.43800 1.000 40.62000 ? 668 HOH A O   1 
HETATM 3459 O  O   . HOH D 3 .   ? 23.42300 -20.37800 46.77700 1.000 32.18000 ? 669 HOH A O   1 
HETATM 3460 O  O   . HOH D 3 .   ? 7.34300  -31.11800 52.47000 1.000 46.05000 ? 670 HOH A O   1 
HETATM 3461 O  O   . HOH D 3 .   ? 26.22800 0.25400   43.38400 1.000 43.72000 ? 671 HOH A O   1 
HETATM 3462 O  O   . HOH D 3 .   ? 10.16100 -5.00000  38.73700 1.000 38.90000 ? 672 HOH A O   1 
HETATM 3463 O  O   . HOH D 3 .   ? 33.24000 -20.16500 74.51200 1.000 37.50000 ? 673 HOH A O   1 
HETATM 3464 O  O   . HOH D 3 .   ? 35.71700 3.56600   65.88200 1.000 54.20000 ? 674 HOH A O   1 
HETATM 3465 O  O   . HOH D 3 .   ? 14.89900 -0.17500  45.93200 1.000 40.15000 ? 675 HOH A O   1 
HETATM 3466 O  O   . HOH D 3 .   ? 21.28600 5.10300   45.66200 1.000 45.50000 ? 676 HOH A O   1 
HETATM 3467 O  O   . HOH D 3 .   ? 49.61600 -0.18000  69.59500 1.000 40.23000 ? 677 HOH A O   1 
HETATM 3468 O  O   . HOH D 3 .   ? 48.08900 -38.42700 93.88300 1.000 55.49000 ? 678 HOH A O   1 
HETATM 3469 O  O   . HOH D 3 .   ? 23.63700 7.67800   49.67300 1.000 37.81000 ? 679 HOH A O   1 
HETATM 3470 O  O   . HOH D 3 .   ? 21.60700 -15.29700 47.03100 1.000 37.42000 ? 680 HOH A O   1 
HETATM 3471 O  O   . HOH D 3 .   ? 32.668   -27.477   73.668   1.000 30.46000 ? 681 HOH A O   1 
HETATM 3472 O  O   . HOH D 3 .   ? 27.50100 -17.60600 51.33700 1.000 32.61000 ? 682 HOH A O   1 
HETATM 3473 O  O   . HOH D 3 .   ? 44.46100 -11.32100 52.47600 1.000 38.56000 ? 683 HOH A O   1 
HETATM 3474 O  O   . HOH D 3 .   ? 56.07800 -22.43900 80.93700 1.000 36.97000 ? 684 HOH A O   1 
HETATM 3475 O  O   . HOH D 3 .   ? 48.85800 -2.60200  82.06700 1.000 37.06000 ? 685 HOH A O   1 
HETATM 3476 O  O   . HOH D 3 .   ? 38.31100 -9.34900  73.93100 1.000 25.13000 ? 686 HOH A O   1 
HETATM 3477 O  O   . HOH D 3 .   ? 36.719   -22.800   85.760   1.000 24.81000 ? 687 HOH A O   1 
HETATM 3478 O  O   . HOH D 3 .   ? 37.17500 7.40300   55.40800 1.000 44.66000 ? 688 HOH A O   1 
HETATM 3479 O  O   . HOH D 3 .   ? 22.39100 -2.52000  42.41800 1.000 43.34000 ? 689 HOH A O   1 
HETATM 3480 O  O   . HOH D 3 .   ? 41.61700 -17.34700 69.00300 1.000 28.52000 ? 690 HOH A O   1 
HETATM 3481 O  O   . HOH D 3 .   ? 44.05600 -24.03200 88.00800 1.000 32.88000 ? 691 HOH A O   1 
HETATM 3482 O  O   . HOH D 3 .   ? 27.83000 0.03800   45.43900 1.000 34.20000 ? 692 HOH A O   1 
HETATM 3483 O  O   . HOH D 3 .   ? 57.21400 -29.93700 60.25700 1.000 41.86000 ? 693 HOH A O   1 
HETATM 3484 O  O   . HOH D 3 .   ? 26.42000 -3.40400  53.39600 1.000 20.46000 ? 694 HOH A O   1 
HETATM 3485 O  O   . HOH D 3 .   ? 48.97400 -38.37000 70.27600 1.000 45.75000 ? 695 HOH A O   1 
HETATM 3486 O  O   . HOH D 3 .   ? 18.32100 -35.21700 67.40700 1.000 38.62000 ? 696 HOH A O   1 
HETATM 3487 O  O   . HOH D 3 .   ? 42.35400 -29.61900 68.21600 1.000 40.75000 ? 697 HOH A O   1 
HETATM 3488 O  O   . HOH D 3 .   ? 33.54700 -20.04600 45.91400 1.000 26.83000 ? 698 HOH A O   1 
HETATM 3489 O  O   . HOH D 3 .   ? 27.92000 3.13500   46.43700 1.000 39.76000 ? 699 HOH A O   1 
HETATM 3490 O  O   . HOH D 3 .   ? 35.48500 -16.59200 87.25300 1.000 28.08000 ? 700 HOH A O   1 
HETATM 3491 O  O   . HOH D 3 .   ? 46.98100 3.55500   67.75700 1.000 39.34000 ? 701 HOH A O   1 
HETATM 3492 O  O   . HOH D 3 .   ? 15.65800 -4.46800  54.88800 1.000 31.75000 ? 702 HOH A O   1 
HETATM 3493 O  O   . HOH D 3 .   ? 33.77000 -14.01600 71.44200 1.000 37.84000 ? 703 HOH A O   1 
HETATM 3494 O  O   . HOH D 3 .   ? -0.08700 -9.46100  46.50800 1.000 42.65000 ? 704 HOH A O   1 
HETATM 3495 O  O   . HOH D 3 .   ? 29.68800 -21.60800 50.90500 1.000 36.81000 ? 705 HOH A O   1 
HETATM 3496 O  O   . HOH D 3 .   ? 62.94900 -31.21300 87.87200 1.000 38.23000 ? 706 HOH A O   1 
HETATM 3497 O  O   . HOH D 3 .   ? 5.14200  -27.22500 55.91000 1.000 34.98000 ? 707 HOH A O   1 
HETATM 3498 O  O   . HOH D 3 .   ? 44.56100 -28.84600 79.67900 1.000 35.16000 ? 708 HOH A O   1 
HETATM 3499 O  O   . HOH D 3 .   ? 11.47700 -30.63500 46.60900 1.000 30.54000 ? 709 HOH A O   1 
HETATM 3500 O  O   . HOH D 3 .   ? 65.48000 -31.08600 65.79700 1.000 42.15000 ? 710 HOH A O   1 
HETATM 3501 O  O   . HOH D 3 .   ? 45.32500 2.47500   77.17000 1.000 41.08000 ? 711 HOH A O   1 
HETATM 3502 O  O   . HOH D 3 .   ? 62.22700 -27.07700 81.00600 1.000 43.71000 ? 712 HOH A O   1 
HETATM 3503 O  O   . HOH D 3 .   ? 0.48800  -18.91200 43.00000 1.000 47.73000 ? 713 HOH A O   1 
HETATM 3504 O  O   . HOH D 3 .   ? 15.83500 -28.06100 48.86500 1.000 24.63000 ? 714 HOH A O   1 
HETATM 3505 O  O   . HOH D 3 .   ? 17.14300 -1.84900  43.09900 1.000 45.94000 ? 715 HOH A O   1 
HETATM 3506 O  O   . HOH D 3 .   ? 17.75500 -19.57500 59.88400 1.000 42.88000 ? 716 HOH A O   1 
HETATM 3507 O  O   . HOH D 3 .   ? 38.01000 3.38500   76.56200 1.000 40.66000 ? 717 HOH A O   1 
HETATM 3508 O  O   . HOH D 3 .   ? 16.20100 -35.24500 50.98800 1.000 35.83000 ? 718 HOH A O   1 
HETATM 3509 O  O   . HOH D 3 .   ? 51.17500 -17.93200 72.84300 1.000 21.61000 ? 719 HOH A O   1 
HETATM 3510 O  O   . HOH D 3 .   ? 31.06800 -5.12900  70.46900 1.000 39.07000 ? 720 HOH A O   1 
HETATM 3511 O  O   . HOH D 3 .   ? 42.69100 -1.41700  83.12300 1.000 43.09000 ? 721 HOH A O   1 
HETATM 3512 O  O   . HOH D 3 .   ? 41.82100 -11.93100 46.61500 1.000 42.66000 ? 722 HOH A O   1 
HETATM 3513 O  O   . HOH D 3 .   ? 42.65600 0.52700   76.23100 1.000 34.99000 ? 723 HOH A O   1 
HETATM 3514 O  O   . HOH D 3 .   ? 47.89700 -23.78500 75.39100 1.000 30.51000 ? 724 HOH A O   1 
HETATM 3515 O  O   . HOH D 3 .   ? 33.943   5.780     46.897   1.000 54.28000 ? 725 HOH A O   1 
HETATM 3516 O  O   . HOH D 3 .   ? 21.23600 -14.07300 43.95500 1.000 41.86000 ? 726 HOH A O   1 
HETATM 3517 O  O   . HOH D 3 .   ? 61.55800 -26.75600 89.47900 1.000 41.74000 ? 727 HOH A O   1 
HETATM 3518 O  O   . HOH D 3 .   ? 3.48600  -11.36400 38.51500 1.000 36.51000 ? 728 HOH A O   1 
HETATM 3519 O  O   . HOH D 3 .   ? 27.65800 -23.88800 51.03900 1.000 52.08000 ? 729 HOH A O   1 
HETATM 3520 O  O   . HOH D 3 .   ? 37.46100 -17.16800 66.36100 1.000 33.34000 ? 730 HOH A O   1 
HETATM 3521 O  O   . HOH D 3 .   ? 27.93600 -2.09700  57.05000 1.000 38.83000 ? 731 HOH A O   1 
HETATM 3522 O  O   . HOH D 3 .   ? 31.15300 -2.32400  68.46900 1.000 52.92000 ? 732 HOH A O   1 
HETATM 3523 O  O   . HOH D 3 .   ? 35.75300 -3.42100  60.68000 1.000 23.07000 ? 733 HOH A O   1 
HETATM 3524 O  O   . HOH D 3 .   ? 34.31200 -17.41400 45.64600 1.000 45.18000 ? 734 HOH A O   1 
HETATM 3525 O  O   . HOH D 3 .   ? 27.96200 0.75800   75.06000 1.000 44.46000 ? 735 HOH A O   1 
HETATM 3526 O  O   . HOH D 3 .   ? 31.436   1.077     66.836   1.000 43.06000 ? 736 HOH A O   1 
HETATM 3527 O  O   . HOH D 3 .   ? 25.80800 11.13300  45.06900 1.000 39.26000 ? 737 HOH A O   1 
HETATM 3528 O  O   . HOH D 3 .   ? 24.93100 -11.40500 63.28300 1.000 33.06000 ? 738 HOH A O   1 
HETATM 3529 O  O   . HOH D 3 .   ? 21.14300 -0.33400  42.05700 1.000 41.00000 ? 739 HOH A O   1 
HETATM 3530 O  O   . HOH D 3 .   ? 15.59100 -19.60000 46.82100 1.000 45.13000 ? 740 HOH A O   1 
HETATM 3531 O  O   . HOH D 3 .   ? 10.86300 -5.63200  61.50000 1.000 42.77000 ? 741 HOH A O   1 
HETATM 3532 O  O   . HOH D 3 .   ? 46.36500 -21.48800 90.22900 1.000 41.45000 ? 742 HOH A O   1 
HETATM 3533 O  O   . HOH D 3 .   ? 26.52300 -9.22700  62.55300 1.000 26.21000 ? 743 HOH A O   1 
HETATM 3534 O  O   . HOH D 3 .   ? 32.97000 -26.33100 61.01400 1.000 42.94000 ? 744 HOH A O   1 
HETATM 3535 O  O   . HOH D 3 .   ? 7.32600  -32.51200 58.26600 1.000 40.52000 ? 745 HOH A O   1 
HETATM 3536 O  O   . HOH D 3 .   ? 49.15600 -7.22700  61.20100 1.000 42.12000 ? 746 HOH A O   1 
HETATM 3537 O  O   . HOH D 3 .   ? 50.75000 -12.06700 66.42600 1.000 36.60000 ? 747 HOH A O   1 
HETATM 3538 O  O   . HOH D 3 .   ? 52.33300 -4.36300  81.77500 1.000 35.33000 ? 748 HOH A O   1 
HETATM 3539 O  O   . HOH D 3 .   ? 43.96700 12.49200  73.59700 1.000 42.97000 ? 749 HOH A O   1 
HETATM 3540 O  O   . HOH D 3 .   ? 17.25500 -11.19000 53.51300 1.000 27.36000 ? 750 HOH A O   1 
HETATM 3541 O  O   . HOH D 3 .   ? 16.32200 -11.84200 56.22300 1.000 35.02000 ? 751 HOH A O   1 
HETATM 3542 O  O   . HOH D 3 .   ? 30.18200 -1.00400  45.36300 1.000 38.95000 ? 752 HOH A O   1 
HETATM 3543 O  O   . HOH D 3 .   ? 33.41400 0.80200   80.16300 1.000 53.26000 ? 753 HOH A O   1 
HETATM 3544 O  O   . HOH D 3 .   ? 69.07200 -33.20600 73.12100 1.000 45.89000 ? 754 HOH A O   1 
HETATM 3545 O  O   . HOH D 3 .   ? 21.63600 -13.76800 51.94600 1.000 36.28000 ? 755 HOH A O   1 
HETATM 3546 O  O   . HOH D 3 .   ? 28.73900 -2.10500  53.97600 1.000 27.35000 ? 756 HOH A O   1 
HETATM 3547 O  O   . HOH D 3 .   ? 54.48000 -18.29300 74.14900 1.000 31.24000 ? 757 HOH A O   1 
HETATM 3548 O  O   . HOH D 3 .   ? 52.07600 -20.26700 55.36700 1.000 35.22000 ? 758 HOH A O   1 
HETATM 3549 O  O   . HOH D 3 .   ? 31.55900 -24.34400 70.66300 1.000 33.00000 ? 759 HOH A O   1 
HETATM 3550 O  O   . HOH D 3 .   ? -3.30600 -5.45900  50.86300 1.000 39.79000 ? 760 HOH A O   1 
HETATM 3551 O  O   . HOH D 3 .   ? 3.36200  -2.51800  59.25700 1.000 51.48000 ? 761 HOH A O   1 
HETATM 3552 O  O   . HOH D 3 .   ? 64.48800 -36.85200 70.76500 1.000 39.91000 ? 762 HOH A O   1 
HETATM 3553 O  O   . HOH D 3 .   ? 29.92200 -18.97800 50.67700 1.000 31.24000 ? 763 HOH A O   1 
HETATM 3554 O  O   . HOH D 3 .   ? 4.02100  -21.84800 61.70700 1.000 42.37000 ? 764 HOH A O   1 
HETATM 3555 O  O   . HOH D 3 .   ? 10.25800 -37.97700 54.35200 1.000 40.00000 ? 765 HOH A O   1 
HETATM 3556 O  O   . HOH D 3 .   ? 8.19500  -22.43100 62.16800 1.000 50.66000 ? 766 HOH A O   1 
HETATM 3557 O  O   . HOH D 3 .   ? 37.43600 5.23000   65.52300 1.000 49.44000 ? 767 HOH A O   1 
HETATM 3558 O  O   . HOH D 3 .   ? 56.71800 -38.47200 67.09500 1.000 33.26000 ? 768 HOH A O   1 
HETATM 3559 O  O   . HOH D 3 .   ? 34.93800 -26.60600 54.02300 1.000 31.01000 ? 769 HOH A O   1 
HETATM 3560 O  O   . HOH D 3 .   ? -3.01900 -10.25400 56.87300 1.000 48.82000 ? 770 HOH A O   1 
HETATM 3561 O  O   . HOH D 3 .   ? 18.54600 -26.70700 47.52400 1.000 25.00000 ? 771 HOH A O   1 
HETATM 3562 O  O   . HOH D 3 .   ? 18.46800 -3.74500  54.98400 1.000 36.82000 ? 772 HOH A O   1 
HETATM 3563 O  O   . HOH D 3 .   ? 52.51200 -14.02600 91.36000 1.000 47.34000 ? 773 HOH A O   1 
HETATM 3564 O  O   . HOH D 3 .   ? 36.44200 -24.64500 45.66000 1.000 42.39000 ? 774 HOH A O   1 
HETATM 3565 O  O   . HOH D 3 .   ? 31.57300 -24.61400 65.09200 1.000 42.95000 ? 775 HOH A O   1 
HETATM 3566 O  O   . HOH D 3 .   ? 58.90600 -38.77400 66.53100 1.000 37.19000 ? 776 HOH A O   1 
HETATM 3567 O  O   . HOH D 3 .   ? 19.48700 2.84000   45.35500 1.000 39.40000 ? 777 HOH A O   1 
HETATM 3568 O  O   . HOH D 3 .   ? 56.12300 -28.16800 97.79600 1.000 54.40000 ? 778 HOH A O   1 
HETATM 3569 O  O   . HOH D 3 .   ? 7.53800  -10.78800 62.94300 1.000 35.99000 ? 779 HOH A O   1 
HETATM 3570 O  O   . HOH D 3 .   ? 27.72400 -3.12900  61.42600 1.000 37.50000 ? 780 HOH A O   1 
HETATM 3571 O  O   . HOH D 3 .   ? 39.15800 8.48500   61.53900 1.000 49.16000 ? 781 HOH A O   1 
HETATM 3572 O  O   . HOH D 3 .   ? 41.08800 2.62400   77.38300 1.000 33.73000 ? 782 HOH A O   1 
HETATM 3573 O  O   . HOH D 3 .   ? 30.560   -18.830   78.768   1.000 45.95000 ? 783 HOH A O   1 
HETATM 3574 O  O   . HOH D 3 .   ? 67.44700 -34.51400 72.27800 1.000 47.23000 ? 784 HOH A O   1 
HETATM 3575 O  O   . HOH D 3 .   ? 64.23200 -23.02200 65.78800 1.000 41.87000 ? 785 HOH A O   1 
HETATM 3576 O  O   . HOH D 3 .   ? 21.81400 -28.80400 49.71000 1.000 39.84000 ? 786 HOH A O   1 
HETATM 3577 O  O   . HOH D 3 .   ? 40.87300 -20.86700 87.55600 1.000 37.09000 ? 787 HOH A O   1 
HETATM 3578 O  O   . HOH D 3 .   ? 36.33300 -6.12200  81.13500 1.000 39.44000 ? 788 HOH A O   1 
HETATM 3579 O  O   . HOH D 3 .   ? 57.76700 -13.12500 71.02500 1.000 49.31000 ? 789 HOH A O   1 
HETATM 3580 O  O   . HOH D 3 .   ? 32.45700 -1.08100  61.59700 1.000 23.89000 ? 790 HOH A O   1 
HETATM 3581 O  O   . HOH D 3 .   ? 33.95500 -14.68800 81.01200 1.000 46.73000 ? 791 HOH A O   1 
HETATM 3582 O  O   . HOH D 3 .   ? 10.30000 -32.07600 48.81100 1.000 42.44000 ? 792 HOH A O   1 
HETATM 3583 O  O   . HOH D 3 .   ? 8.49400  -0.75600  43.15000 1.000 43.90000 ? 793 HOH A O   1 
HETATM 3584 O  O   . HOH D 3 .   ? 38.78800 12.46000  68.06600 1.000 48.12000 ? 794 HOH A O   1 
HETATM 3585 O  O   . HOH D 3 .   ? 38.15600 -30.02000 64.03900 1.000 37.39000 ? 795 HOH A O   1 
HETATM 3586 O  O   . HOH D 3 .   ? 51.00600 -36.46700 95.01500 1.000 43.46000 ? 796 HOH A O   1 
HETATM 3587 O  O   . HOH D 3 .   ? 12.47600 -42.83200 60.27100 1.000 45.59000 ? 797 HOH A O   1 
HETATM 3588 O  O   . HOH D 3 .   ? 46.41600 -32.91900 79.48900 1.000 55.10000 ? 798 HOH A O   1 
HETATM 3589 O  O   . HOH D 3 .   ? 7.05700  -2.46100  40.79400 1.000 41.59000 ? 799 HOH A O   1 
HETATM 3590 O  O   . HOH D 3 .   ? 32.01600 -20.99100 76.54700 1.000 45.31000 ? 800 HOH A O   1 
HETATM 3591 O  O   . HOH D 3 .   ? 18.90000 -20.47900 44.32100 1.000 56.28000 ? 801 HOH A O   1 
HETATM 3592 O  O   . HOH D 3 .   ? 63.19100 -29.33100 79.45100 1.000 44.75000 ? 802 HOH A O   1 
HETATM 3593 O  O   . HOH D 3 .   ? 43.46800 -23.47900 51.08800 1.000 40.22000 ? 803 HOH A O   1 
HETATM 3594 O  O   . HOH D 3 .   ? 41.97500 -29.19000 81.25700 1.000 29.15000 ? 804 HOH A O   1 
HETATM 3595 O  O   . HOH D 3 .   ? 38.80700 -30.97900 57.62400 1.000 36.39000 ? 805 HOH A O   1 
HETATM 3596 O  O   . HOH D 3 .   ? 35.749   8.766     69.251   1.000 53.44000 ? 806 HOH A O   1 
HETATM 3597 O  O   . HOH D 3 .   ? 14.81700 -32.87500 39.88000 1.000 43.78000 ? 807 HOH A O   1 
HETATM 3598 O  O   . HOH D 3 .   ? 30.58300 -1.68300  62.68600 1.000 43.28000 ? 808 HOH A O   1 
HETATM 3599 O  O   . HOH D 3 .   ? 27.71400 -19.19400 63.89900 1.000 44.18000 ? 809 HOH A O   1 
HETATM 3600 O  O   . HOH D 3 .   ? 51.99900 -9.32200  66.54100 1.000 44.78000 ? 810 HOH A O   1 
HETATM 3601 O  O   . HOH D 3 .   ? 44.14100 -34.00600 80.95300 1.000 48.92000 ? 811 HOH A O   1 
HETATM 3602 O  O   . HOH D 3 .   ? 38.40500 -1.81100  84.87400 1.000 50.30000 ? 812 HOH A O   1 
HETATM 3603 O  O   . HOH D 3 .   ? 9.56000  -16.74900 61.89600 1.000 54.72000 ? 813 HOH A O   1 
HETATM 3604 O  O   . HOH D 3 .   ? 42.58300 -3.55600  84.91600 1.000 45.88000 ? 814 HOH A O   1 
HETATM 3605 O  O   . HOH D 3 .   ? 25.35200 -6.44000  63.53100 1.000 34.20000 ? 815 HOH A O   1 
HETATM 3606 O  O   . HOH D 3 .   ? 10.50800 -31.46200 44.17700 1.000 48.59000 ? 816 HOH A O   1 
HETATM 3607 O  O   . HOH D 3 .   ? 44.75600 -31.29800 71.60300 1.000 31.78000 ? 817 HOH A O   1 
HETATM 3608 O  O   . HOH D 3 .   ? 7.13000  -18.49000 62.71500 1.000 48.42000 ? 818 HOH A O   1 
HETATM 3609 O  O   . HOH D 3 .   ? 63.24600 -24.84900 59.65000 1.000 41.97000 ? 819 HOH A O   1 
HETATM 3610 O  O   . HOH D 3 .   ? 30.971   -23.526   73.212   1.000 50.50000 ? 820 HOH A O   1 
HETATM 3611 O  O   . HOH D 3 .   ? 36.06100 -26.96300 51.97400 1.000 46.17000 ? 821 HOH A O   1 
HETATM 3612 O  O   . HOH D 3 .   ? 14.33300 -31.21600 47.43500 1.000 39.24000 ? 822 HOH A O   1 
HETATM 3613 O  O   . HOH D 3 .   ? 57.77200 -27.22400 57.22100 1.000 34.63000 ? 823 HOH A O   1 
HETATM 3614 O  O   . HOH D 3 .   ? 14.99200 -14.52000 57.07300 1.000 35.34000 ? 824 HOH A O   1 
HETATM 3615 O  O   . HOH D 3 .   ? 47.38300 -4.18100  86.44700 1.000 44.97000 ? 825 HOH A O   1 
HETATM 3616 O  O   . HOH D 3 .   ? 43.79900 -8.78300  50.89700 1.000 43.49000 ? 826 HOH A O   1 
HETATM 3617 O  O   . HOH D 3 .   ? 8.74400  -4.82500  61.02700 1.000 52.80000 ? 827 HOH A O   1 
HETATM 3618 O  O   . HOH D 3 .   ? 19.18700 -1.17600  54.77700 1.000 34.38000 ? 828 HOH A O   1 
HETATM 3619 O  O   . HOH D 3 .   ? 52.90000 -36.23200 93.76400 1.000 36.32000 ? 829 HOH A O   1 
HETATM 3620 O  O   . HOH D 3 .   ? 44.08000 -37.49700 56.26100 1.000 43.69000 ? 830 HOH A O   1 
HETATM 3621 O  O   . HOH D 3 .   ? 44.15200 -35.80700 69.15100 1.000 53.78000 ? 831 HOH A O   1 
HETATM 3622 O  O   . HOH D 3 .   ? 54.219   -40.137   92.102   1.000 49.54000 ? 832 HOH A O   1 
HETATM 3623 O  O   . HOH D 3 .   ? 43.97600 -22.31400 90.34700 1.000 53.35000 ? 833 HOH A O   1 
HETATM 3624 O  O   . HOH D 3 .   ? 34.90100 -29.71900 60.16300 1.000 41.64000 ? 834 HOH A O   1 
HETATM 3625 O  O   . HOH D 3 .   ? 13.80900 -0.18200  43.21400 1.000 43.79000 ? 835 HOH A O   1 
HETATM 3626 O  O   . HOH D 3 .   ? 46.97300 -12.03000 54.89700 1.000 50.21000 ? 836 HOH A O   1 
HETATM 3627 O  O   . HOH D 3 .   ? 39.54600 -37.32700 58.51000 1.000 53.09000 ? 837 HOH A O   1 
HETATM 3628 O  O   . HOH D 3 .   ? 41.72500 0.98600   84.21100 1.000 45.14000 ? 838 HOH A O   1 
HETATM 3629 O  O   . HOH D 3 .   ? 57.55100 -38.16700 86.03700 1.000 46.23000 ? 839 HOH A O   1 
HETATM 3630 O  O   . HOH D 3 .   ? 45.363   -40.682   59.274   1.000 41.89000 ? 840 HOH A O   1 
HETATM 3631 O  O   . HOH D 3 .   ? 42.00100 -38.26900 57.36000 1.000 39.00000 ? 841 HOH A O   1 
HETATM 3632 O  O   . HOH D 3 .   ? 39.42500 1.90900   79.74700 1.000 53.09000 ? 842 HOH A O   1 
HETATM 3633 O  O   . HOH D 3 .   ? 5.26300  -19.63200 63.60200 1.000 49.89000 ? 843 HOH A O   1 
HETATM 3634 O  O   . HOH D 3 .   ? 45.78700 -31.38500 80.93400 1.000 52.41000 ? 844 HOH A O   1 
HETATM 3635 O  O   . HOH D 3 .   ? 26.04900 -21.35900 62.79000 1.000 51.14000 ? 845 HOH A O   1 
HETATM 3636 O  O   . HOH D 3 .   ? 33.20500 -13.74700 54.87100 1.000 42.29000 ? 846 HOH A O   1 
HETATM 3637 O  O   . HOH D 3 .   ? 39.892   -31.912   76.319   1.000 39.98000 ? 847 HOH A O   1 
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