data_8QNM
# 
_entry.id   8QNM 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8QNM         pdb_00008qnm 10.2210/pdb8qnm/pdb 
WWPDB D_1292133617 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-04-09 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8QNM 
_pdbx_database_status.recvd_initial_deposition_date   2023-09-27 
_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 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB . 8QNA unspecified 
PDB . 8QN1 unspecified 
PDB . 8QN9 unspecified 
PDB . 8QMX unspecified 
PDB . 8QN3 unspecified 
PDB . 8QNE unspecified 
PDB . 8QNK unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              peter.macheroux@tugraz.at 
_pdbx_contact_author.name_first         Peter 
_pdbx_contact_author.name_last          Macheroux 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-0242-454X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Bijelic, A.'      1 ? 
'Macheroux, P.'    2 ? 
'Kerschbaumer, B.' 3 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Crystal structures of OPR3 wildtype and variants in complex with NAD(P)H' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Kerschbaumer, B.' 1 ? 
primary 'Bijelic, A.'      2 ? 
primary 'Macheroux, P.'    3 ? 
# 
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 '12-oxophytodienoate reductase 3' 43768.520 2   ? ? ? ? 
2 non-polymer syn 'FLAVIN MONONUCLEOTIDE' 456.344   2   ? ? ? ? 
3 non-polymer syn 
;[[(2R,3S,4R,5R)-5-(5-aminocarbonyl-3,4-dihydro-2H-pyridin-1-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] [(2R,3R,4R,5R)-5-(6-aminopurin-9-yl)-3-oxidanyl-4-phosphonooxy-oxolan-2-yl]methyl hydrogen phosphate
;
747.437   2   ? ? ? ? 
4 water       nat water 18.015    331 ? ? ? ? 
# 
_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       
;MASHHHHHHMASSAQDGNNPLFSPYKMGKFNLSHRVVLAPMTRCRALNNIPQAALGEYYEQRATAGGFLITEGTMISPTS
AGFPHVPGIFTKEQVREWKKIVDVVHAKGAVIFCQLWHVGRASHEVYQPAGAAPISSTEKPISNRWRILMPDGTHGIYPK
PRAIGTYEISQVVEDYRRSALNAIEAGFDGIEIHGAHGYLIDQFLKDGINDRTDEYGGSLANRCKFITQVVQAVVSAIGA
DRVGVRVSPAIDHLDAMDSNPLSLGLAVVERLNKIQLHSGSKLAYLHVTQPRSDKGGSEEEEARLMRTLRNAYQGTFICS
GGYTRELGIEAVAQGDADLVSYGRLFISNPDLVMRIKLNAPLNKYNRKTFYTQDPVVGYTDYPFLQGNGSNGPLSRL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MASHHHHHHMASSAQDGNNPLFSPYKMGKFNLSHRVVLAPMTRCRALNNIPQAALGEYYEQRATAGGFLITEGTMISPTS
AGFPHVPGIFTKEQVREWKKIVDVVHAKGAVIFCQLWHVGRASHEVYQPAGAAPISSTEKPISNRWRILMPDGTHGIYPK
PRAIGTYEISQVVEDYRRSALNAIEAGFDGIEIHGAHGYLIDQFLKDGINDRTDEYGGSLANRCKFITQVVQAVVSAIGA
DRVGVRVSPAIDHLDAMDSNPLSLGLAVVERLNKIQLHSGSKLAYLHVTQPRSDKGGSEEEEARLMRTLRNAYQGTFICS
GGYTRELGIEAVAQGDADLVSYGRLFISNPDLVMRIKLNAPLNKYNRKTFYTQDPVVGYTDYPFLQGNGSNGPLSRL
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'FLAVIN MONONUCLEOTIDE' FMN 
3 
;[[(2R,3S,4R,5R)-5-(5-aminocarbonyl-3,4-dihydro-2H-pyridin-1-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] [(2R,3R,4R,5R)-5-(6-aminopurin-9-yl)-3-oxidanyl-4-phosphonooxy-oxolan-2-yl]methyl hydrogen phosphate
;
5J8 
4 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   ALA n 
1 3   SER n 
1 4   HIS n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   HIS n 
1 10  MET n 
1 11  ALA n 
1 12  SER n 
1 13  SER n 
1 14  ALA n 
1 15  GLN n 
1 16  ASP n 
1 17  GLY n 
1 18  ASN n 
1 19  ASN n 
1 20  PRO n 
1 21  LEU n 
1 22  PHE n 
1 23  SER n 
1 24  PRO n 
1 25  TYR n 
1 26  LYS n 
1 27  MET n 
1 28  GLY n 
1 29  LYS n 
1 30  PHE n 
1 31  ASN n 
1 32  LEU n 
1 33  SER n 
1 34  HIS n 
1 35  ARG n 
1 36  VAL n 
1 37  VAL n 
1 38  LEU n 
1 39  ALA n 
1 40  PRO n 
1 41  MET n 
1 42  THR n 
1 43  ARG n 
1 44  CYS n 
1 45  ARG n 
1 46  ALA n 
1 47  LEU n 
1 48  ASN n 
1 49  ASN n 
1 50  ILE n 
1 51  PRO n 
1 52  GLN n 
1 53  ALA n 
1 54  ALA n 
1 55  LEU n 
1 56  GLY n 
1 57  GLU n 
1 58  TYR n 
1 59  TYR n 
1 60  GLU n 
1 61  GLN n 
1 62  ARG n 
1 63  ALA n 
1 64  THR n 
1 65  ALA n 
1 66  GLY n 
1 67  GLY n 
1 68  PHE n 
1 69  LEU n 
1 70  ILE n 
1 71  THR n 
1 72  GLU n 
1 73  GLY n 
1 74  THR n 
1 75  MET n 
1 76  ILE n 
1 77  SER n 
1 78  PRO n 
1 79  THR n 
1 80  SER n 
1 81  ALA n 
1 82  GLY n 
1 83  PHE n 
1 84  PRO n 
1 85  HIS n 
1 86  VAL n 
1 87  PRO n 
1 88  GLY n 
1 89  ILE n 
1 90  PHE n 
1 91  THR n 
1 92  LYS n 
1 93  GLU n 
1 94  GLN n 
1 95  VAL n 
1 96  ARG n 
1 97  GLU n 
1 98  TRP n 
1 99  LYS n 
1 100 LYS n 
1 101 ILE n 
1 102 VAL n 
1 103 ASP n 
1 104 VAL n 
1 105 VAL n 
1 106 HIS n 
1 107 ALA n 
1 108 LYS n 
1 109 GLY n 
1 110 ALA n 
1 111 VAL n 
1 112 ILE n 
1 113 PHE n 
1 114 CYS n 
1 115 GLN n 
1 116 LEU n 
1 117 TRP n 
1 118 HIS n 
1 119 VAL n 
1 120 GLY n 
1 121 ARG n 
1 122 ALA n 
1 123 SER n 
1 124 HIS n 
1 125 GLU n 
1 126 VAL n 
1 127 TYR n 
1 128 GLN n 
1 129 PRO n 
1 130 ALA n 
1 131 GLY n 
1 132 ALA n 
1 133 ALA n 
1 134 PRO n 
1 135 ILE n 
1 136 SER n 
1 137 SER n 
1 138 THR n 
1 139 GLU n 
1 140 LYS n 
1 141 PRO n 
1 142 ILE n 
1 143 SER n 
1 144 ASN n 
1 145 ARG n 
1 146 TRP n 
1 147 ARG n 
1 148 ILE n 
1 149 LEU n 
1 150 MET n 
1 151 PRO n 
1 152 ASP n 
1 153 GLY n 
1 154 THR n 
1 155 HIS n 
1 156 GLY n 
1 157 ILE n 
1 158 TYR n 
1 159 PRO n 
1 160 LYS n 
1 161 PRO n 
1 162 ARG n 
1 163 ALA n 
1 164 ILE n 
1 165 GLY n 
1 166 THR n 
1 167 TYR n 
1 168 GLU n 
1 169 ILE n 
1 170 SER n 
1 171 GLN n 
1 172 VAL n 
1 173 VAL n 
1 174 GLU n 
1 175 ASP n 
1 176 TYR n 
1 177 ARG n 
1 178 ARG n 
1 179 SER n 
1 180 ALA n 
1 181 LEU n 
1 182 ASN n 
1 183 ALA n 
1 184 ILE n 
1 185 GLU n 
1 186 ALA n 
1 187 GLY n 
1 188 PHE n 
1 189 ASP n 
1 190 GLY n 
1 191 ILE n 
1 192 GLU n 
1 193 ILE n 
1 194 HIS n 
1 195 GLY n 
1 196 ALA n 
1 197 HIS n 
1 198 GLY n 
1 199 TYR n 
1 200 LEU n 
1 201 ILE n 
1 202 ASP n 
1 203 GLN n 
1 204 PHE n 
1 205 LEU n 
1 206 LYS n 
1 207 ASP n 
1 208 GLY n 
1 209 ILE n 
1 210 ASN n 
1 211 ASP n 
1 212 ARG n 
1 213 THR n 
1 214 ASP n 
1 215 GLU n 
1 216 TYR n 
1 217 GLY n 
1 218 GLY n 
1 219 SER n 
1 220 LEU n 
1 221 ALA n 
1 222 ASN n 
1 223 ARG n 
1 224 CYS n 
1 225 LYS n 
1 226 PHE n 
1 227 ILE n 
1 228 THR n 
1 229 GLN n 
1 230 VAL n 
1 231 VAL n 
1 232 GLN n 
1 233 ALA n 
1 234 VAL n 
1 235 VAL n 
1 236 SER n 
1 237 ALA n 
1 238 ILE n 
1 239 GLY n 
1 240 ALA n 
1 241 ASP n 
1 242 ARG n 
1 243 VAL n 
1 244 GLY n 
1 245 VAL n 
1 246 ARG n 
1 247 VAL n 
1 248 SER n 
1 249 PRO n 
1 250 ALA n 
1 251 ILE n 
1 252 ASP n 
1 253 HIS n 
1 254 LEU n 
1 255 ASP n 
1 256 ALA n 
1 257 MET n 
1 258 ASP n 
1 259 SER n 
1 260 ASN n 
1 261 PRO n 
1 262 LEU n 
1 263 SER n 
1 264 LEU n 
1 265 GLY n 
1 266 LEU n 
1 267 ALA n 
1 268 VAL n 
1 269 VAL n 
1 270 GLU n 
1 271 ARG n 
1 272 LEU n 
1 273 ASN n 
1 274 LYS n 
1 275 ILE n 
1 276 GLN n 
1 277 LEU n 
1 278 HIS n 
1 279 SER n 
1 280 GLY n 
1 281 SER n 
1 282 LYS n 
1 283 LEU n 
1 284 ALA n 
1 285 TYR n 
1 286 LEU n 
1 287 HIS n 
1 288 VAL n 
1 289 THR n 
1 290 GLN n 
1 291 PRO n 
1 292 ARG n 
1 293 SER n 
1 294 ASP n 
1 295 LYS n 
1 296 GLY n 
1 297 GLY n 
1 298 SER n 
1 299 GLU n 
1 300 GLU n 
1 301 GLU n 
1 302 GLU n 
1 303 ALA n 
1 304 ARG n 
1 305 LEU n 
1 306 MET n 
1 307 ARG n 
1 308 THR n 
1 309 LEU n 
1 310 ARG n 
1 311 ASN n 
1 312 ALA n 
1 313 TYR n 
1 314 GLN n 
1 315 GLY n 
1 316 THR n 
1 317 PHE n 
1 318 ILE n 
1 319 CYS n 
1 320 SER n 
1 321 GLY n 
1 322 GLY n 
1 323 TYR n 
1 324 THR n 
1 325 ARG n 
1 326 GLU n 
1 327 LEU n 
1 328 GLY n 
1 329 ILE n 
1 330 GLU n 
1 331 ALA n 
1 332 VAL n 
1 333 ALA n 
1 334 GLN n 
1 335 GLY n 
1 336 ASP n 
1 337 ALA n 
1 338 ASP n 
1 339 LEU n 
1 340 VAL n 
1 341 SER n 
1 342 TYR n 
1 343 GLY n 
1 344 ARG n 
1 345 LEU n 
1 346 PHE n 
1 347 ILE n 
1 348 SER n 
1 349 ASN n 
1 350 PRO n 
1 351 ASP n 
1 352 LEU n 
1 353 VAL n 
1 354 MET n 
1 355 ARG n 
1 356 ILE n 
1 357 LYS n 
1 358 LEU n 
1 359 ASN n 
1 360 ALA n 
1 361 PRO n 
1 362 LEU n 
1 363 ASN n 
1 364 LYS n 
1 365 TYR n 
1 366 ASN n 
1 367 ARG n 
1 368 LYS n 
1 369 THR n 
1 370 PHE n 
1 371 TYR n 
1 372 THR n 
1 373 GLN n 
1 374 ASP n 
1 375 PRO n 
1 376 VAL n 
1 377 VAL n 
1 378 GLY n 
1 379 TYR n 
1 380 THR n 
1 381 ASP n 
1 382 TYR n 
1 383 PRO n 
1 384 PHE n 
1 385 LEU n 
1 386 GLN n 
1 387 GLY n 
1 388 ASN n 
1 389 GLY n 
1 390 SER n 
1 391 ASN n 
1 392 GLY n 
1 393 PRO n 
1 394 LEU n 
1 395 SER n 
1 396 ARG n 
1 397 LEU 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                   397 
_entity_src_gen.gene_src_common_name               tomato 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 OPR3 
_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      'Solanum lycopersicum' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     4081 
_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 
5J8 non-polymer         . 
;[[(2R,3S,4R,5R)-5-(5-aminocarbonyl-3,4-dihydro-2H-pyridin-1-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] [(2R,3R,4R,5R)-5-(6-aminopurin-9-yl)-3-oxidanyl-4-phosphonooxy-oxolan-2-yl]methyl hydrogen phosphate
;
?                          'C21 H32 N7 O17 P3' 747.437 
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 
FMN non-polymer         . 'FLAVIN MONONUCLEOTIDE' 'RIBOFLAVIN MONOPHOSPHATE' 'C17 H21 N4 O9 P'   456.344 
GLN 'L-peptide linking' y GLUTAMINE ?                          'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ?                          'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE ?                          'C2 H5 N O2'        75.067  
HIS 'L-peptide linking' y HISTIDINE ?                          'C6 H10 N3 O2 1'    156.162 
HOH non-polymer         . WATER ?                          'H2 O'              18.015  
ILE 'L-peptide linking' y ISOLEUCINE ?                          'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE ?                          'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE ?                          'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE ?                          'C5 H11 N O2 S'     149.211 
PHE 'L-peptide linking' y PHENYLALANINE ?                          'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE ?                          'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE ?                          'C3 H7 N O3'        105.093 
THR 'L-peptide linking' y THREONINE ?                          'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN ?                          'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE ?                          'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE ?                          'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   -8  ?   ?   ?   A . n 
A 1 2   ALA 2   -7  ?   ?   ?   A . n 
A 1 3   SER 3   -6  ?   ?   ?   A . n 
A 1 4   HIS 4   -5  ?   ?   ?   A . n 
A 1 5   HIS 5   -4  ?   ?   ?   A . n 
A 1 6   HIS 6   -3  ?   ?   ?   A . n 
A 1 7   HIS 7   -2  ?   ?   ?   A . n 
A 1 8   HIS 8   -1  ?   ?   ?   A . n 
A 1 9   HIS 9   0   ?   ?   ?   A . n 
A 1 10  MET 10  1   ?   ?   ?   A . n 
A 1 11  ALA 11  2   ?   ?   ?   A . n 
A 1 12  SER 12  3   ?   ?   ?   A . n 
A 1 13  SER 13  4   ?   ?   ?   A . n 
A 1 14  ALA 14  5   ?   ?   ?   A . n 
A 1 15  GLN 15  6   ?   ?   ?   A . n 
A 1 16  ASP 16  7   ?   ?   ?   A . n 
A 1 17  GLY 17  8   ?   ?   ?   A . n 
A 1 18  ASN 18  9   ?   ?   ?   A . n 
A 1 19  ASN 19  10  10  ASN ASN A . n 
A 1 20  PRO 20  11  11  PRO PRO A . n 
A 1 21  LEU 21  12  12  LEU LEU A . n 
A 1 22  PHE 22  13  13  PHE PHE A . n 
A 1 23  SER 23  14  14  SER SER A . n 
A 1 24  PRO 24  15  15  PRO PRO A . n 
A 1 25  TYR 25  16  16  TYR TYR A . n 
A 1 26  LYS 26  17  17  LYS LYS A . n 
A 1 27  MET 27  18  18  MET MET A . n 
A 1 28  GLY 28  19  19  GLY GLY A . n 
A 1 29  LYS 29  20  20  LYS LYS A . n 
A 1 30  PHE 30  21  21  PHE PHE A . n 
A 1 31  ASN 31  22  22  ASN ASN A . n 
A 1 32  LEU 32  23  23  LEU LEU A . n 
A 1 33  SER 33  24  24  SER SER A . n 
A 1 34  HIS 34  25  25  HIS HIS A . n 
A 1 35  ARG 35  26  26  ARG ARG A . n 
A 1 36  VAL 36  27  27  VAL VAL A . n 
A 1 37  VAL 37  28  28  VAL VAL A . n 
A 1 38  LEU 38  29  29  LEU LEU A . n 
A 1 39  ALA 39  30  30  ALA ALA A . n 
A 1 40  PRO 40  31  31  PRO PRO A . n 
A 1 41  MET 41  32  32  MET MET A . n 
A 1 42  THR 42  33  33  THR THR A . n 
A 1 43  ARG 43  34  34  ARG ARG A . n 
A 1 44  CYS 44  35  35  CYS CYS A . n 
A 1 45  ARG 45  36  36  ARG ARG A . n 
A 1 46  ALA 46  37  37  ALA ALA A . n 
A 1 47  LEU 47  38  38  LEU LEU A . n 
A 1 48  ASN 48  39  39  ASN ASN A . n 
A 1 49  ASN 49  40  40  ASN ASN A . n 
A 1 50  ILE 50  41  41  ILE ILE A . n 
A 1 51  PRO 51  42  42  PRO PRO A . n 
A 1 52  GLN 52  43  43  GLN GLN A . n 
A 1 53  ALA 53  44  44  ALA ALA A . n 
A 1 54  ALA 54  45  45  ALA ALA A . n 
A 1 55  LEU 55  46  46  LEU LEU A . n 
A 1 56  GLY 56  47  47  GLY GLY A . n 
A 1 57  GLU 57  48  48  GLU GLU A . n 
A 1 58  TYR 58  49  49  TYR TYR A . n 
A 1 59  TYR 59  50  50  TYR TYR A . n 
A 1 60  GLU 60  51  51  GLU GLU A . n 
A 1 61  GLN 61  52  52  GLN GLN A . n 
A 1 62  ARG 62  53  53  ARG ARG A . n 
A 1 63  ALA 63  54  54  ALA ALA A . n 
A 1 64  THR 64  55  55  THR THR A . n 
A 1 65  ALA 65  56  56  ALA ALA A . n 
A 1 66  GLY 66  57  57  GLY GLY A . n 
A 1 67  GLY 67  58  58  GLY GLY A . n 
A 1 68  PHE 68  59  59  PHE PHE A . n 
A 1 69  LEU 69  60  60  LEU LEU A . n 
A 1 70  ILE 70  61  61  ILE ILE A . n 
A 1 71  THR 71  62  62  THR THR A . n 
A 1 72  GLU 72  63  63  GLU GLU A . n 
A 1 73  GLY 73  64  64  GLY GLY A . n 
A 1 74  THR 74  65  65  THR THR A . n 
A 1 75  MET 75  66  66  MET MET A . n 
A 1 76  ILE 76  67  67  ILE ILE A . n 
A 1 77  SER 77  68  68  SER SER A . n 
A 1 78  PRO 78  69  69  PRO PRO A . n 
A 1 79  THR 79  70  70  THR THR A . n 
A 1 80  SER 80  71  71  SER SER A . n 
A 1 81  ALA 81  72  72  ALA ALA A . n 
A 1 82  GLY 82  73  73  GLY GLY A . n 
A 1 83  PHE 83  74  74  PHE PHE A . n 
A 1 84  PRO 84  75  75  PRO PRO A . n 
A 1 85  HIS 85  76  76  HIS HIS A . n 
A 1 86  VAL 86  77  77  VAL VAL A . n 
A 1 87  PRO 87  78  78  PRO PRO A . n 
A 1 88  GLY 88  79  79  GLY GLY A . n 
A 1 89  ILE 89  80  80  ILE ILE A . n 
A 1 90  PHE 90  81  81  PHE PHE A . n 
A 1 91  THR 91  82  82  THR THR A . n 
A 1 92  LYS 92  83  83  LYS LYS A . n 
A 1 93  GLU 93  84  84  GLU GLU A . n 
A 1 94  GLN 94  85  85  GLN GLN A . n 
A 1 95  VAL 95  86  86  VAL VAL A . n 
A 1 96  ARG 96  87  87  ARG ARG A . n 
A 1 97  GLU 97  88  88  GLU GLU A . n 
A 1 98  TRP 98  89  89  TRP TRP A . n 
A 1 99  LYS 99  90  90  LYS LYS A . n 
A 1 100 LYS 100 91  91  LYS LYS A . n 
A 1 101 ILE 101 92  92  ILE ILE A . n 
A 1 102 VAL 102 93  93  VAL VAL A . n 
A 1 103 ASP 103 94  94  ASP ASP A . n 
A 1 104 VAL 104 95  95  VAL VAL A . n 
A 1 105 VAL 105 96  96  VAL VAL A . n 
A 1 106 HIS 106 97  97  HIS HIS A . n 
A 1 107 ALA 107 98  98  ALA ALA A . n 
A 1 108 LYS 108 99  99  LYS LYS A . n 
A 1 109 GLY 109 100 100 GLY GLY A . n 
A 1 110 ALA 110 101 101 ALA ALA A . n 
A 1 111 VAL 111 102 102 VAL VAL A . n 
A 1 112 ILE 112 103 103 ILE ILE A . n 
A 1 113 PHE 113 104 104 PHE PHE A . n 
A 1 114 CYS 114 105 105 CYS CYS A . n 
A 1 115 GLN 115 106 106 GLN GLN A . n 
A 1 116 LEU 116 107 107 LEU LEU A . n 
A 1 117 TRP 117 108 108 TRP TRP A . n 
A 1 118 HIS 118 109 109 HIS HIS A . n 
A 1 119 VAL 119 110 110 VAL VAL A . n 
A 1 120 GLY 120 111 111 GLY GLY A . n 
A 1 121 ARG 121 112 112 ARG ARG A . n 
A 1 122 ALA 122 113 113 ALA ALA A . n 
A 1 123 SER 123 114 114 SER SER A . n 
A 1 124 HIS 124 115 115 HIS HIS A . n 
A 1 125 GLU 125 116 116 GLU GLU A . n 
A 1 126 VAL 126 117 117 VAL VAL A . n 
A 1 127 TYR 127 118 118 TYR TYR A . n 
A 1 128 GLN 128 119 119 GLN GLN A . n 
A 1 129 PRO 129 120 120 PRO PRO A . n 
A 1 130 ALA 130 121 121 ALA ALA A . n 
A 1 131 GLY 131 122 122 GLY GLY A . n 
A 1 132 ALA 132 123 123 ALA ALA A . n 
A 1 133 ALA 133 124 124 ALA ALA A . n 
A 1 134 PRO 134 125 125 PRO PRO A . n 
A 1 135 ILE 135 126 126 ILE ILE A . n 
A 1 136 SER 136 127 127 SER SER A . n 
A 1 137 SER 137 128 128 SER SER A . n 
A 1 138 THR 138 129 129 THR THR A . n 
A 1 139 GLU 139 130 130 GLU GLU A . n 
A 1 140 LYS 140 131 131 LYS LYS A . n 
A 1 141 PRO 141 132 132 PRO PRO A . n 
A 1 142 ILE 142 133 133 ILE ILE A . n 
A 1 143 SER 143 134 134 SER SER A . n 
A 1 144 ASN 144 135 135 ASN ASN A . n 
A 1 145 ARG 145 136 136 ARG ARG A . n 
A 1 146 TRP 146 137 137 TRP TRP A . n 
A 1 147 ARG 147 138 138 ARG ARG A . n 
A 1 148 ILE 148 139 139 ILE ILE A . n 
A 1 149 LEU 149 140 140 LEU LEU A . n 
A 1 150 MET 150 141 141 MET MET A . n 
A 1 151 PRO 151 142 142 PRO PRO A . n 
A 1 152 ASP 152 143 143 ASP ASP A . n 
A 1 153 GLY 153 144 144 GLY GLY A . n 
A 1 154 THR 154 145 145 THR THR A . n 
A 1 155 HIS 155 146 146 HIS HIS A . n 
A 1 156 GLY 156 147 147 GLY GLY A . n 
A 1 157 ILE 157 148 148 ILE ILE A . n 
A 1 158 TYR 158 149 149 TYR TYR A . n 
A 1 159 PRO 159 150 150 PRO PRO A . n 
A 1 160 LYS 160 151 151 LYS LYS A . n 
A 1 161 PRO 161 152 152 PRO PRO A . n 
A 1 162 ARG 162 153 153 ARG ARG A . n 
A 1 163 ALA 163 154 154 ALA ALA A . n 
A 1 164 ILE 164 155 155 ILE ILE A . n 
A 1 165 GLY 165 156 156 GLY GLY A . n 
A 1 166 THR 166 157 157 THR THR A . n 
A 1 167 TYR 167 158 158 TYR TYR A . n 
A 1 168 GLU 168 159 159 GLU GLU A . n 
A 1 169 ILE 169 160 160 ILE ILE A . n 
A 1 170 SER 170 161 161 SER SER A . n 
A 1 171 GLN 171 162 162 GLN GLN A . n 
A 1 172 VAL 172 163 163 VAL VAL A . n 
A 1 173 VAL 173 164 164 VAL VAL A . n 
A 1 174 GLU 174 165 165 GLU GLU A . n 
A 1 175 ASP 175 166 166 ASP ASP A . n 
A 1 176 TYR 176 167 167 TYR TYR A . n 
A 1 177 ARG 177 168 168 ARG ARG A . n 
A 1 178 ARG 178 169 169 ARG ARG A . n 
A 1 179 SER 179 170 170 SER SER A . n 
A 1 180 ALA 180 171 171 ALA ALA A . n 
A 1 181 LEU 181 172 172 LEU LEU A . n 
A 1 182 ASN 182 173 173 ASN ASN A . n 
A 1 183 ALA 183 174 174 ALA ALA A . n 
A 1 184 ILE 184 175 175 ILE ILE A . n 
A 1 185 GLU 185 176 176 GLU GLU A . n 
A 1 186 ALA 186 177 177 ALA ALA A . n 
A 1 187 GLY 187 178 178 GLY GLY A . n 
A 1 188 PHE 188 179 179 PHE PHE A . n 
A 1 189 ASP 189 180 180 ASP ASP A . n 
A 1 190 GLY 190 181 181 GLY GLY A . n 
A 1 191 ILE 191 182 182 ILE ILE A . n 
A 1 192 GLU 192 183 183 GLU GLU A . n 
A 1 193 ILE 193 184 184 ILE ILE A . n 
A 1 194 HIS 194 185 185 HIS HIS A . n 
A 1 195 GLY 195 186 186 GLY GLY A . n 
A 1 196 ALA 196 187 187 ALA ALA A . n 
A 1 197 HIS 197 188 188 HIS HIS A . n 
A 1 198 GLY 198 189 189 GLY GLY A . n 
A 1 199 TYR 199 190 190 TYR TYR A . n 
A 1 200 LEU 200 191 191 LEU LEU A . n 
A 1 201 ILE 201 192 192 ILE ILE A . n 
A 1 202 ASP 202 193 193 ASP ASP A . n 
A 1 203 GLN 203 194 194 GLN GLN A . n 
A 1 204 PHE 204 195 195 PHE PHE A . n 
A 1 205 LEU 205 196 196 LEU LEU A . n 
A 1 206 LYS 206 197 197 LYS LYS A . n 
A 1 207 ASP 207 198 198 ASP ASP A . n 
A 1 208 GLY 208 199 199 GLY GLY A . n 
A 1 209 ILE 209 200 200 ILE ILE A . n 
A 1 210 ASN 210 201 201 ASN ASN A . n 
A 1 211 ASP 211 202 202 ASP ASP A . n 
A 1 212 ARG 212 203 203 ARG ARG A . n 
A 1 213 THR 213 204 204 THR THR A . n 
A 1 214 ASP 214 205 205 ASP ASP A . n 
A 1 215 GLU 215 206 206 GLU GLU A . n 
A 1 216 TYR 216 207 207 TYR TYR A . n 
A 1 217 GLY 217 208 208 GLY GLY A . n 
A 1 218 GLY 218 209 209 GLY GLY A . n 
A 1 219 SER 219 210 210 SER SER A . n 
A 1 220 LEU 220 211 211 LEU LEU A . n 
A 1 221 ALA 221 212 212 ALA ALA A . n 
A 1 222 ASN 222 213 213 ASN ASN A . n 
A 1 223 ARG 223 214 214 ARG ARG A . n 
A 1 224 CYS 224 215 215 CYS CYS A . n 
A 1 225 LYS 225 216 216 LYS LYS A . n 
A 1 226 PHE 226 217 217 PHE PHE A . n 
A 1 227 ILE 227 218 218 ILE ILE A . n 
A 1 228 THR 228 219 219 THR THR A . n 
A 1 229 GLN 229 220 220 GLN GLN A . n 
A 1 230 VAL 230 221 221 VAL VAL A . n 
A 1 231 VAL 231 222 222 VAL VAL A . n 
A 1 232 GLN 232 223 223 GLN GLN A . n 
A 1 233 ALA 233 224 224 ALA ALA A . n 
A 1 234 VAL 234 225 225 VAL VAL A . n 
A 1 235 VAL 235 226 226 VAL VAL A . n 
A 1 236 SER 236 227 227 SER SER A . n 
A 1 237 ALA 237 228 228 ALA ALA A . n 
A 1 238 ILE 238 229 229 ILE ILE A . n 
A 1 239 GLY 239 230 230 GLY GLY A . n 
A 1 240 ALA 240 231 231 ALA ALA A . n 
A 1 241 ASP 241 232 232 ASP ASP A . n 
A 1 242 ARG 242 233 233 ARG ARG A . n 
A 1 243 VAL 243 234 234 VAL VAL A . n 
A 1 244 GLY 244 235 235 GLY GLY A . n 
A 1 245 VAL 245 236 236 VAL VAL A . n 
A 1 246 ARG 246 237 237 ARG ARG A . n 
A 1 247 VAL 247 238 238 VAL VAL A . n 
A 1 248 SER 248 239 239 SER SER A . n 
A 1 249 PRO 249 240 240 PRO PRO A . n 
A 1 250 ALA 250 241 241 ALA ALA A . n 
A 1 251 ILE 251 242 242 ILE ILE A . n 
A 1 252 ASP 252 243 243 ASP ASP A . n 
A 1 253 HIS 253 244 244 HIS HIS A . n 
A 1 254 LEU 254 245 245 LEU LEU A . n 
A 1 255 ASP 255 246 246 ASP ASP A . n 
A 1 256 ALA 256 247 247 ALA ALA A . n 
A 1 257 MET 257 248 248 MET MET A . n 
A 1 258 ASP 258 249 249 ASP ASP A . n 
A 1 259 SER 259 250 250 SER SER A . n 
A 1 260 ASN 260 251 251 ASN ASN A . n 
A 1 261 PRO 261 252 252 PRO PRO A . n 
A 1 262 LEU 262 253 253 LEU LEU A . n 
A 1 263 SER 263 254 254 SER SER A . n 
A 1 264 LEU 264 255 255 LEU LEU A . n 
A 1 265 GLY 265 256 256 GLY GLY A . n 
A 1 266 LEU 266 257 257 LEU LEU A . n 
A 1 267 ALA 267 258 258 ALA ALA A . n 
A 1 268 VAL 268 259 259 VAL VAL A . n 
A 1 269 VAL 269 260 260 VAL VAL A . n 
A 1 270 GLU 270 261 261 GLU GLU A . n 
A 1 271 ARG 271 262 262 ARG ARG A . n 
A 1 272 LEU 272 263 263 LEU LEU A . n 
A 1 273 ASN 273 264 264 ASN ASN A . n 
A 1 274 LYS 274 265 265 LYS LYS A . n 
A 1 275 ILE 275 266 266 ILE ILE A . n 
A 1 276 GLN 276 267 267 GLN GLN A . n 
A 1 277 LEU 277 268 268 LEU LEU A . n 
A 1 278 HIS 278 269 269 HIS HIS A . n 
A 1 279 SER 279 270 270 SER SER A . n 
A 1 280 GLY 280 271 271 GLY GLY A . n 
A 1 281 SER 281 272 272 SER SER A . n 
A 1 282 LYS 282 273 273 LYS LYS A . n 
A 1 283 LEU 283 274 274 LEU LEU A . n 
A 1 284 ALA 284 275 275 ALA ALA A . n 
A 1 285 TYR 285 276 276 TYR TYR A . n 
A 1 286 LEU 286 277 277 LEU LEU A . n 
A 1 287 HIS 287 278 278 HIS HIS A . n 
A 1 288 VAL 288 279 279 VAL VAL A . n 
A 1 289 THR 289 280 280 THR THR A . n 
A 1 290 GLN 290 281 281 GLN GLN A . n 
A 1 291 PRO 291 282 282 PRO PRO A . n 
A 1 292 ARG 292 283 283 ARG ARG A . n 
A 1 293 SER 293 284 284 SER SER A . n 
A 1 294 ASP 294 285 ?   ?   ?   A . n 
A 1 295 LYS 295 286 ?   ?   ?   A . n 
A 1 296 GLY 296 287 288 GLY GLY A . n 
A 1 297 GLY 297 288 289 GLY GLY A . n 
A 1 298 SER 298 289 290 SER SER A . n 
A 1 299 GLU 299 290 291 GLU GLU A . n 
A 1 300 GLU 300 291 292 GLU GLU A . n 
A 1 301 GLU 301 292 293 GLU GLU A . n 
A 1 302 GLU 302 293 294 GLU GLU A . n 
A 1 303 ALA 303 294 295 ALA ALA A . n 
A 1 304 ARG 304 295 296 ARG ARG A . n 
A 1 305 LEU 305 296 297 LEU LEU A . n 
A 1 306 MET 306 297 298 MET MET A . n 
A 1 307 ARG 307 298 299 ARG ARG A . n 
A 1 308 THR 308 299 300 THR THR A . n 
A 1 309 LEU 309 300 301 LEU LEU A . n 
A 1 310 ARG 310 301 302 ARG ARG A . n 
A 1 311 ASN 311 302 303 ASN ASN A . n 
A 1 312 ALA 312 303 304 ALA ALA A . n 
A 1 313 TYR 313 304 305 TYR TYR A . n 
A 1 314 GLN 314 305 306 GLN GLN A . n 
A 1 315 GLY 315 306 307 GLY GLY A . n 
A 1 316 THR 316 307 308 THR THR A . n 
A 1 317 PHE 317 308 309 PHE PHE A . n 
A 1 318 ILE 318 309 310 ILE ILE A . n 
A 1 319 CYS 319 310 311 CYS CYS A . n 
A 1 320 SER 320 311 312 SER SER A . n 
A 1 321 GLY 321 312 313 GLY GLY A . n 
A 1 322 GLY 322 313 314 GLY GLY A . n 
A 1 323 TYR 323 314 315 TYR TYR A . n 
A 1 324 THR 324 315 316 THR THR A . n 
A 1 325 ARG 325 316 317 ARG ARG A . n 
A 1 326 GLU 326 317 318 GLU GLU A . n 
A 1 327 LEU 327 318 319 LEU LEU A . n 
A 1 328 GLY 328 319 320 GLY GLY A . n 
A 1 329 ILE 329 320 321 ILE ILE A . n 
A 1 330 GLU 330 321 322 GLU GLU A . n 
A 1 331 ALA 331 322 323 ALA ALA A . n 
A 1 332 VAL 332 323 324 VAL VAL A . n 
A 1 333 ALA 333 324 325 ALA ALA A . n 
A 1 334 GLN 334 325 326 GLN GLN A . n 
A 1 335 GLY 335 326 327 GLY GLY A . n 
A 1 336 ASP 336 327 328 ASP ASP A . n 
A 1 337 ALA 337 328 329 ALA ALA A . n 
A 1 338 ASP 338 329 330 ASP ASP A . n 
A 1 339 LEU 339 330 331 LEU LEU A . n 
A 1 340 VAL 340 331 332 VAL VAL A . n 
A 1 341 SER 341 332 333 SER SER A . n 
A 1 342 TYR 342 333 334 TYR TYR A . n 
A 1 343 GLY 343 334 335 GLY GLY A . n 
A 1 344 ARG 344 335 336 ARG ARG A . n 
A 1 345 LEU 345 336 337 LEU LEU A . n 
A 1 346 PHE 346 337 338 PHE PHE A . n 
A 1 347 ILE 347 338 339 ILE ILE A . n 
A 1 348 SER 348 339 340 SER SER A . n 
A 1 349 ASN 349 340 341 ASN ASN A . n 
A 1 350 PRO 350 341 342 PRO PRO A . n 
A 1 351 ASP 351 342 343 ASP ASP A . n 
A 1 352 LEU 352 343 344 LEU LEU A . n 
A 1 353 VAL 353 344 345 VAL VAL A . n 
A 1 354 MET 354 345 346 MET MET A . n 
A 1 355 ARG 355 346 347 ARG ARG A . n 
A 1 356 ILE 356 347 348 ILE ILE A . n 
A 1 357 LYS 357 348 349 LYS LYS A . n 
A 1 358 LEU 358 349 350 LEU LEU A . n 
A 1 359 ASN 359 350 351 ASN ASN A . n 
A 1 360 ALA 360 351 352 ALA ALA A . n 
A 1 361 PRO 361 352 353 PRO PRO A . n 
A 1 362 LEU 362 353 354 LEU LEU A . n 
A 1 363 ASN 363 354 355 ASN ASN A . n 
A 1 364 LYS 364 355 356 LYS LYS A . n 
A 1 365 TYR 365 356 357 TYR TYR A . n 
A 1 366 ASN 366 357 358 ASN ASN A . n 
A 1 367 ARG 367 358 359 ARG ARG A . n 
A 1 368 LYS 368 359 360 LYS LYS A . n 
A 1 369 THR 369 360 361 THR THR A . n 
A 1 370 PHE 370 361 362 PHE PHE A . n 
A 1 371 TYR 371 362 363 TYR TYR A . n 
A 1 372 THR 372 363 364 THR THR A . n 
A 1 373 GLN 373 364 365 GLN GLN A . n 
A 1 374 ASP 374 365 366 ASP ASP A . n 
A 1 375 PRO 375 366 367 PRO PRO A . n 
A 1 376 VAL 376 367 368 VAL VAL A . n 
A 1 377 VAL 377 368 369 VAL VAL A . n 
A 1 378 GLY 378 369 370 GLY GLY A . n 
A 1 379 TYR 379 370 371 TYR TYR A . n 
A 1 380 THR 380 371 372 THR THR A . n 
A 1 381 ASP 381 372 373 ASP ASP A . n 
A 1 382 TYR 382 373 374 TYR TYR A . n 
A 1 383 PRO 383 374 375 PRO PRO A . n 
A 1 384 PHE 384 375 376 PHE PHE A . n 
A 1 385 LEU 385 376 377 LEU LEU A . n 
A 1 386 GLN 386 377 378 GLN GLN A . n 
A 1 387 GLY 387 378 ?   ?   ?   A . n 
A 1 388 ASN 388 379 ?   ?   ?   A . n 
A 1 389 GLY 389 380 ?   ?   ?   A . n 
A 1 390 SER 390 381 ?   ?   ?   A . n 
A 1 391 ASN 391 382 ?   ?   ?   A . n 
A 1 392 GLY 392 383 ?   ?   ?   A . n 
A 1 393 PRO 393 384 ?   ?   ?   A . n 
A 1 394 LEU 394 385 ?   ?   ?   A . n 
A 1 395 SER 395 386 ?   ?   ?   A . n 
A 1 396 ARG 396 387 ?   ?   ?   A . n 
A 1 397 LEU 397 388 ?   ?   ?   A . n 
B 1 1   MET 1   -8  ?   ?   ?   B . n 
B 1 2   ALA 2   -7  ?   ?   ?   B . n 
B 1 3   SER 3   -6  ?   ?   ?   B . n 
B 1 4   HIS 4   -5  ?   ?   ?   B . n 
B 1 5   HIS 5   -4  ?   ?   ?   B . n 
B 1 6   HIS 6   -3  ?   ?   ?   B . n 
B 1 7   HIS 7   -2  ?   ?   ?   B . n 
B 1 8   HIS 8   -1  ?   ?   ?   B . n 
B 1 9   HIS 9   0   ?   ?   ?   B . n 
B 1 10  MET 10  1   ?   ?   ?   B . n 
B 1 11  ALA 11  2   ?   ?   ?   B . n 
B 1 12  SER 12  3   ?   ?   ?   B . n 
B 1 13  SER 13  4   ?   ?   ?   B . n 
B 1 14  ALA 14  5   ?   ?   ?   B . n 
B 1 15  GLN 15  6   ?   ?   ?   B . n 
B 1 16  ASP 16  7   ?   ?   ?   B . n 
B 1 17  GLY 17  8   ?   ?   ?   B . n 
B 1 18  ASN 18  9   ?   ?   ?   B . n 
B 1 19  ASN 19  10  10  ASN ASN B . n 
B 1 20  PRO 20  11  11  PRO PRO B . n 
B 1 21  LEU 21  12  12  LEU LEU B . n 
B 1 22  PHE 22  13  13  PHE PHE B . n 
B 1 23  SER 23  14  14  SER SER B . n 
B 1 24  PRO 24  15  15  PRO PRO B . n 
B 1 25  TYR 25  16  16  TYR TYR B . n 
B 1 26  LYS 26  17  17  LYS LYS B . n 
B 1 27  MET 27  18  18  MET MET B . n 
B 1 28  GLY 28  19  19  GLY GLY B . n 
B 1 29  LYS 29  20  20  LYS LYS B . n 
B 1 30  PHE 30  21  21  PHE PHE B . n 
B 1 31  ASN 31  22  22  ASN ASN B . n 
B 1 32  LEU 32  23  23  LEU LEU B . n 
B 1 33  SER 33  24  24  SER SER B . n 
B 1 34  HIS 34  25  25  HIS HIS B . n 
B 1 35  ARG 35  26  26  ARG ARG B . n 
B 1 36  VAL 36  27  27  VAL VAL B . n 
B 1 37  VAL 37  28  28  VAL VAL B . n 
B 1 38  LEU 38  29  29  LEU LEU B . n 
B 1 39  ALA 39  30  30  ALA ALA B . n 
B 1 40  PRO 40  31  31  PRO PRO B . n 
B 1 41  MET 41  32  32  MET MET B . n 
B 1 42  THR 42  33  33  THR THR B . n 
B 1 43  ARG 43  34  34  ARG ARG B . n 
B 1 44  CYS 44  35  35  CYS CYS B . n 
B 1 45  ARG 45  36  36  ARG ARG B . n 
B 1 46  ALA 46  37  37  ALA ALA B . n 
B 1 47  LEU 47  38  38  LEU LEU B . n 
B 1 48  ASN 48  39  39  ASN ASN B . n 
B 1 49  ASN 49  40  40  ASN ASN B . n 
B 1 50  ILE 50  41  41  ILE ILE B . n 
B 1 51  PRO 51  42  42  PRO PRO B . n 
B 1 52  GLN 52  43  43  GLN GLN B . n 
B 1 53  ALA 53  44  44  ALA ALA B . n 
B 1 54  ALA 54  45  45  ALA ALA B . n 
B 1 55  LEU 55  46  46  LEU LEU B . n 
B 1 56  GLY 56  47  47  GLY GLY B . n 
B 1 57  GLU 57  48  48  GLU GLU B . n 
B 1 58  TYR 58  49  49  TYR TYR B . n 
B 1 59  TYR 59  50  50  TYR TYR B . n 
B 1 60  GLU 60  51  51  GLU GLU B . n 
B 1 61  GLN 61  52  52  GLN GLN B . n 
B 1 62  ARG 62  53  53  ARG ARG B . n 
B 1 63  ALA 63  54  54  ALA ALA B . n 
B 1 64  THR 64  55  55  THR THR B . n 
B 1 65  ALA 65  56  56  ALA ALA B . n 
B 1 66  GLY 66  57  57  GLY GLY B . n 
B 1 67  GLY 67  58  58  GLY GLY B . n 
B 1 68  PHE 68  59  59  PHE PHE B . n 
B 1 69  LEU 69  60  60  LEU LEU B . n 
B 1 70  ILE 70  61  61  ILE ILE B . n 
B 1 71  THR 71  62  62  THR THR B . n 
B 1 72  GLU 72  63  63  GLU GLU B . n 
B 1 73  GLY 73  64  64  GLY GLY B . n 
B 1 74  THR 74  65  65  THR THR B . n 
B 1 75  MET 75  66  66  MET MET B . n 
B 1 76  ILE 76  67  67  ILE ILE B . n 
B 1 77  SER 77  68  68  SER SER B . n 
B 1 78  PRO 78  69  69  PRO PRO B . n 
B 1 79  THR 79  70  70  THR THR B . n 
B 1 80  SER 80  71  71  SER SER B . n 
B 1 81  ALA 81  72  72  ALA ALA B . n 
B 1 82  GLY 82  73  73  GLY GLY B . n 
B 1 83  PHE 83  74  74  PHE PHE B . n 
B 1 84  PRO 84  75  75  PRO PRO B . n 
B 1 85  HIS 85  76  76  HIS HIS B . n 
B 1 86  VAL 86  77  77  VAL VAL B . n 
B 1 87  PRO 87  78  78  PRO PRO B . n 
B 1 88  GLY 88  79  79  GLY GLY B . n 
B 1 89  ILE 89  80  80  ILE ILE B . n 
B 1 90  PHE 90  81  81  PHE PHE B . n 
B 1 91  THR 91  82  82  THR THR B . n 
B 1 92  LYS 92  83  83  LYS LYS B . n 
B 1 93  GLU 93  84  84  GLU GLU B . n 
B 1 94  GLN 94  85  85  GLN GLN B . n 
B 1 95  VAL 95  86  86  VAL VAL B . n 
B 1 96  ARG 96  87  87  ARG ARG B . n 
B 1 97  GLU 97  88  88  GLU GLU B . n 
B 1 98  TRP 98  89  89  TRP TRP B . n 
B 1 99  LYS 99  90  90  LYS LYS B . n 
B 1 100 LYS 100 91  91  LYS LYS B . n 
B 1 101 ILE 101 92  92  ILE ILE B . n 
B 1 102 VAL 102 93  93  VAL VAL B . n 
B 1 103 ASP 103 94  94  ASP ASP B . n 
B 1 104 VAL 104 95  95  VAL VAL B . n 
B 1 105 VAL 105 96  96  VAL VAL B . n 
B 1 106 HIS 106 97  97  HIS HIS B . n 
B 1 107 ALA 107 98  98  ALA ALA B . n 
B 1 108 LYS 108 99  99  LYS LYS B . n 
B 1 109 GLY 109 100 100 GLY GLY B . n 
B 1 110 ALA 110 101 101 ALA ALA B . n 
B 1 111 VAL 111 102 102 VAL VAL B . n 
B 1 112 ILE 112 103 103 ILE ILE B . n 
B 1 113 PHE 113 104 104 PHE PHE B . n 
B 1 114 CYS 114 105 105 CYS CYS B . n 
B 1 115 GLN 115 106 106 GLN GLN B . n 
B 1 116 LEU 116 107 107 LEU LEU B . n 
B 1 117 TRP 117 108 108 TRP TRP B . n 
B 1 118 HIS 118 109 109 HIS HIS B . n 
B 1 119 VAL 119 110 110 VAL VAL B . n 
B 1 120 GLY 120 111 111 GLY GLY B . n 
B 1 121 ARG 121 112 112 ARG ARG B . n 
B 1 122 ALA 122 113 113 ALA ALA B . n 
B 1 123 SER 123 114 114 SER SER B . n 
B 1 124 HIS 124 115 115 HIS HIS B . n 
B 1 125 GLU 125 116 116 GLU GLU B . n 
B 1 126 VAL 126 117 117 VAL VAL B . n 
B 1 127 TYR 127 118 118 TYR TYR B . n 
B 1 128 GLN 128 119 119 GLN GLN B . n 
B 1 129 PRO 129 120 120 PRO PRO B . n 
B 1 130 ALA 130 121 121 ALA ALA B . n 
B 1 131 GLY 131 122 122 GLY GLY B . n 
B 1 132 ALA 132 123 123 ALA ALA B . n 
B 1 133 ALA 133 124 124 ALA ALA B . n 
B 1 134 PRO 134 125 125 PRO PRO B . n 
B 1 135 ILE 135 126 126 ILE ILE B . n 
B 1 136 SER 136 127 127 SER SER B . n 
B 1 137 SER 137 128 128 SER SER B . n 
B 1 138 THR 138 129 129 THR THR B . n 
B 1 139 GLU 139 130 130 GLU GLU B . n 
B 1 140 LYS 140 131 131 LYS LYS B . n 
B 1 141 PRO 141 132 132 PRO PRO B . n 
B 1 142 ILE 142 133 133 ILE ILE B . n 
B 1 143 SER 143 134 134 SER SER B . n 
B 1 144 ASN 144 135 135 ASN ASN B . n 
B 1 145 ARG 145 136 136 ARG ARG B . n 
B 1 146 TRP 146 137 137 TRP TRP B . n 
B 1 147 ARG 147 138 138 ARG ARG B . n 
B 1 148 ILE 148 139 139 ILE ILE B . n 
B 1 149 LEU 149 140 140 LEU LEU B . n 
B 1 150 MET 150 141 141 MET MET B . n 
B 1 151 PRO 151 142 142 PRO PRO B . n 
B 1 152 ASP 152 143 143 ASP ASP B . n 
B 1 153 GLY 153 144 144 GLY GLY B . n 
B 1 154 THR 154 145 145 THR THR B . n 
B 1 155 HIS 155 146 146 HIS HIS B . n 
B 1 156 GLY 156 147 147 GLY GLY B . n 
B 1 157 ILE 157 148 148 ILE ILE B . n 
B 1 158 TYR 158 149 149 TYR TYR B . n 
B 1 159 PRO 159 150 150 PRO PRO B . n 
B 1 160 LYS 160 151 151 LYS LYS B . n 
B 1 161 PRO 161 152 152 PRO PRO B . n 
B 1 162 ARG 162 153 153 ARG ARG B . n 
B 1 163 ALA 163 154 154 ALA ALA B . n 
B 1 164 ILE 164 155 155 ILE ILE B . n 
B 1 165 GLY 165 156 156 GLY GLY B . n 
B 1 166 THR 166 157 157 THR THR B . n 
B 1 167 TYR 167 158 158 TYR TYR B . n 
B 1 168 GLU 168 159 159 GLU GLU B . n 
B 1 169 ILE 169 160 160 ILE ILE B . n 
B 1 170 SER 170 161 161 SER SER B . n 
B 1 171 GLN 171 162 162 GLN GLN B . n 
B 1 172 VAL 172 163 163 VAL VAL B . n 
B 1 173 VAL 173 164 164 VAL VAL B . n 
B 1 174 GLU 174 165 165 GLU GLU B . n 
B 1 175 ASP 175 166 166 ASP ASP B . n 
B 1 176 TYR 176 167 167 TYR TYR B . n 
B 1 177 ARG 177 168 168 ARG ARG B . n 
B 1 178 ARG 178 169 169 ARG ARG B . n 
B 1 179 SER 179 170 170 SER SER B . n 
B 1 180 ALA 180 171 171 ALA ALA B . n 
B 1 181 LEU 181 172 172 LEU LEU B . n 
B 1 182 ASN 182 173 173 ASN ASN B . n 
B 1 183 ALA 183 174 174 ALA ALA B . n 
B 1 184 ILE 184 175 175 ILE ILE B . n 
B 1 185 GLU 185 176 176 GLU GLU B . n 
B 1 186 ALA 186 177 177 ALA ALA B . n 
B 1 187 GLY 187 178 178 GLY GLY B . n 
B 1 188 PHE 188 179 179 PHE PHE B . n 
B 1 189 ASP 189 180 180 ASP ASP B . n 
B 1 190 GLY 190 181 181 GLY GLY B . n 
B 1 191 ILE 191 182 182 ILE ILE B . n 
B 1 192 GLU 192 183 183 GLU GLU B . n 
B 1 193 ILE 193 184 184 ILE ILE B . n 
B 1 194 HIS 194 185 185 HIS HIS B . n 
B 1 195 GLY 195 186 186 GLY GLY B . n 
B 1 196 ALA 196 187 187 ALA ALA B . n 
B 1 197 HIS 197 188 188 HIS HIS B . n 
B 1 198 GLY 198 189 189 GLY GLY B . n 
B 1 199 TYR 199 190 190 TYR TYR B . n 
B 1 200 LEU 200 191 191 LEU LEU B . n 
B 1 201 ILE 201 192 192 ILE ILE B . n 
B 1 202 ASP 202 193 193 ASP ASP B . n 
B 1 203 GLN 203 194 194 GLN GLN B . n 
B 1 204 PHE 204 195 195 PHE PHE B . n 
B 1 205 LEU 205 196 196 LEU LEU B . n 
B 1 206 LYS 206 197 197 LYS LYS B . n 
B 1 207 ASP 207 198 198 ASP ASP B . n 
B 1 208 GLY 208 199 199 GLY GLY B . n 
B 1 209 ILE 209 200 200 ILE ILE B . n 
B 1 210 ASN 210 201 201 ASN ASN B . n 
B 1 211 ASP 211 202 202 ASP ASP B . n 
B 1 212 ARG 212 203 203 ARG ARG B . n 
B 1 213 THR 213 204 204 THR THR B . n 
B 1 214 ASP 214 205 205 ASP ASP B . n 
B 1 215 GLU 215 206 206 GLU GLU B . n 
B 1 216 TYR 216 207 207 TYR TYR B . n 
B 1 217 GLY 217 208 208 GLY GLY B . n 
B 1 218 GLY 218 209 209 GLY GLY B . n 
B 1 219 SER 219 210 210 SER SER B . n 
B 1 220 LEU 220 211 211 LEU LEU B . n 
B 1 221 ALA 221 212 212 ALA ALA B . n 
B 1 222 ASN 222 213 213 ASN ASN B . n 
B 1 223 ARG 223 214 214 ARG ARG B . n 
B 1 224 CYS 224 215 215 CYS CYS B . n 
B 1 225 LYS 225 216 216 LYS LYS B . n 
B 1 226 PHE 226 217 217 PHE PHE B . n 
B 1 227 ILE 227 218 218 ILE ILE B . n 
B 1 228 THR 228 219 219 THR THR B . n 
B 1 229 GLN 229 220 220 GLN GLN B . n 
B 1 230 VAL 230 221 221 VAL VAL B . n 
B 1 231 VAL 231 222 222 VAL VAL B . n 
B 1 232 GLN 232 223 223 GLN GLN B . n 
B 1 233 ALA 233 224 224 ALA ALA B . n 
B 1 234 VAL 234 225 225 VAL VAL B . n 
B 1 235 VAL 235 226 226 VAL VAL B . n 
B 1 236 SER 236 227 227 SER SER B . n 
B 1 237 ALA 237 228 228 ALA ALA B . n 
B 1 238 ILE 238 229 229 ILE ILE B . n 
B 1 239 GLY 239 230 230 GLY GLY B . n 
B 1 240 ALA 240 231 231 ALA ALA B . n 
B 1 241 ASP 241 232 232 ASP ASP B . n 
B 1 242 ARG 242 233 233 ARG ARG B . n 
B 1 243 VAL 243 234 234 VAL VAL B . n 
B 1 244 GLY 244 235 235 GLY GLY B . n 
B 1 245 VAL 245 236 236 VAL VAL B . n 
B 1 246 ARG 246 237 237 ARG ARG B . n 
B 1 247 VAL 247 238 238 VAL VAL B . n 
B 1 248 SER 248 239 239 SER SER B . n 
B 1 249 PRO 249 240 240 PRO PRO B . n 
B 1 250 ALA 250 241 241 ALA ALA B . n 
B 1 251 ILE 251 242 242 ILE ILE B . n 
B 1 252 ASP 252 243 243 ASP ASP B . n 
B 1 253 HIS 253 244 244 HIS HIS B . n 
B 1 254 LEU 254 245 245 LEU LEU B . n 
B 1 255 ASP 255 246 246 ASP ASP B . n 
B 1 256 ALA 256 247 247 ALA ALA B . n 
B 1 257 MET 257 248 248 MET MET B . n 
B 1 258 ASP 258 249 249 ASP ASP B . n 
B 1 259 SER 259 250 250 SER SER B . n 
B 1 260 ASN 260 251 251 ASN ASN B . n 
B 1 261 PRO 261 252 252 PRO PRO B . n 
B 1 262 LEU 262 253 253 LEU LEU B . n 
B 1 263 SER 263 254 254 SER SER B . n 
B 1 264 LEU 264 255 255 LEU LEU B . n 
B 1 265 GLY 265 256 256 GLY GLY B . n 
B 1 266 LEU 266 257 257 LEU LEU B . n 
B 1 267 ALA 267 258 258 ALA ALA B . n 
B 1 268 VAL 268 259 259 VAL VAL B . n 
B 1 269 VAL 269 260 260 VAL VAL B . n 
B 1 270 GLU 270 261 261 GLU GLU B . n 
B 1 271 ARG 271 262 262 ARG ARG B . n 
B 1 272 LEU 272 263 263 LEU LEU B . n 
B 1 273 ASN 273 264 264 ASN ASN B . n 
B 1 274 LYS 274 265 265 LYS LYS B . n 
B 1 275 ILE 275 266 266 ILE ILE B . n 
B 1 276 GLN 276 267 267 GLN GLN B . n 
B 1 277 LEU 277 268 268 LEU LEU B . n 
B 1 278 HIS 278 269 269 HIS HIS B . n 
B 1 279 SER 279 270 270 SER SER B . n 
B 1 280 GLY 280 271 271 GLY GLY B . n 
B 1 281 SER 281 272 272 SER SER B . n 
B 1 282 LYS 282 273 273 LYS LYS B . n 
B 1 283 LEU 283 274 274 LEU LEU B . n 
B 1 284 ALA 284 275 275 ALA ALA B . n 
B 1 285 TYR 285 276 276 TYR TYR B . n 
B 1 286 LEU 286 277 277 LEU LEU B . n 
B 1 287 HIS 287 278 278 HIS HIS B . n 
B 1 288 VAL 288 279 279 VAL VAL B . n 
B 1 289 THR 289 280 280 THR THR B . n 
B 1 290 GLN 290 281 281 GLN GLN B . n 
B 1 291 PRO 291 282 282 PRO PRO B . n 
B 1 292 ARG 292 283 283 ARG ARG B . n 
B 1 293 SER 293 284 284 SER SER B . n 
B 1 294 ASP 294 285 ?   ?   ?   B . n 
B 1 295 LYS 295 286 ?   ?   ?   B . n 
B 1 296 GLY 296 287 ?   ?   ?   B . n 
B 1 297 GLY 297 288 ?   ?   ?   B . n 
B 1 298 SER 298 289 290 SER SER B . n 
B 1 299 GLU 299 290 291 GLU GLU B . n 
B 1 300 GLU 300 291 292 GLU GLU B . n 
B 1 301 GLU 301 292 293 GLU GLU B . n 
B 1 302 GLU 302 293 294 GLU GLU B . n 
B 1 303 ALA 303 294 295 ALA ALA B . n 
B 1 304 ARG 304 295 296 ARG ARG B . n 
B 1 305 LEU 305 296 297 LEU LEU B . n 
B 1 306 MET 306 297 298 MET MET B . n 
B 1 307 ARG 307 298 299 ARG ARG B . n 
B 1 308 THR 308 299 300 THR THR B . n 
B 1 309 LEU 309 300 301 LEU LEU B . n 
B 1 310 ARG 310 301 302 ARG ARG B . n 
B 1 311 ASN 311 302 303 ASN ASN B . n 
B 1 312 ALA 312 303 304 ALA ALA B . n 
B 1 313 TYR 313 304 305 TYR TYR B . n 
B 1 314 GLN 314 305 306 GLN GLN B . n 
B 1 315 GLY 315 306 307 GLY GLY B . n 
B 1 316 THR 316 307 308 THR THR B . n 
B 1 317 PHE 317 308 309 PHE PHE B . n 
B 1 318 ILE 318 309 310 ILE ILE B . n 
B 1 319 CYS 319 310 311 CYS CYS B . n 
B 1 320 SER 320 311 312 SER SER B . n 
B 1 321 GLY 321 312 313 GLY GLY B . n 
B 1 322 GLY 322 313 314 GLY GLY B . n 
B 1 323 TYR 323 314 315 TYR TYR B . n 
B 1 324 THR 324 315 316 THR THR B . n 
B 1 325 ARG 325 316 317 ARG ARG B . n 
B 1 326 GLU 326 317 318 GLU GLU B . n 
B 1 327 LEU 327 318 319 LEU LEU B . n 
B 1 328 GLY 328 319 320 GLY GLY B . n 
B 1 329 ILE 329 320 321 ILE ILE B . n 
B 1 330 GLU 330 321 322 GLU GLU B . n 
B 1 331 ALA 331 322 323 ALA ALA B . n 
B 1 332 VAL 332 323 324 VAL VAL B . n 
B 1 333 ALA 333 324 325 ALA ALA B . n 
B 1 334 GLN 334 325 326 GLN GLN B . n 
B 1 335 GLY 335 326 327 GLY GLY B . n 
B 1 336 ASP 336 327 328 ASP ASP B . n 
B 1 337 ALA 337 328 329 ALA ALA B . n 
B 1 338 ASP 338 329 330 ASP ASP B . n 
B 1 339 LEU 339 330 331 LEU LEU B . n 
B 1 340 VAL 340 331 332 VAL VAL B . n 
B 1 341 SER 341 332 333 SER SER B . n 
B 1 342 TYR 342 333 334 TYR TYR B . n 
B 1 343 GLY 343 334 335 GLY GLY B . n 
B 1 344 ARG 344 335 336 ARG ARG B . n 
B 1 345 LEU 345 336 337 LEU LEU B . n 
B 1 346 PHE 346 337 338 PHE PHE B . n 
B 1 347 ILE 347 338 339 ILE ILE B . n 
B 1 348 SER 348 339 340 SER SER B . n 
B 1 349 ASN 349 340 341 ASN ASN B . n 
B 1 350 PRO 350 341 342 PRO PRO B . n 
B 1 351 ASP 351 342 343 ASP ASP B . n 
B 1 352 LEU 352 343 344 LEU LEU B . n 
B 1 353 VAL 353 344 345 VAL VAL B . n 
B 1 354 MET 354 345 346 MET MET B . n 
B 1 355 ARG 355 346 347 ARG ARG B . n 
B 1 356 ILE 356 347 348 ILE ILE B . n 
B 1 357 LYS 357 348 349 LYS LYS B . n 
B 1 358 LEU 358 349 350 LEU LEU B . n 
B 1 359 ASN 359 350 351 ASN ASN B . n 
B 1 360 ALA 360 351 352 ALA ALA B . n 
B 1 361 PRO 361 352 353 PRO PRO B . n 
B 1 362 LEU 362 353 354 LEU LEU B . n 
B 1 363 ASN 363 354 355 ASN ASN B . n 
B 1 364 LYS 364 355 356 LYS LYS B . n 
B 1 365 TYR 365 356 357 TYR TYR B . n 
B 1 366 ASN 366 357 358 ASN ASN B . n 
B 1 367 ARG 367 358 359 ARG ARG B . n 
B 1 368 LYS 368 359 360 LYS LYS B . n 
B 1 369 THR 369 360 361 THR THR B . n 
B 1 370 PHE 370 361 362 PHE PHE B . n 
B 1 371 TYR 371 362 363 TYR TYR B . n 
B 1 372 THR 372 363 364 THR THR B . n 
B 1 373 GLN 373 364 365 GLN GLN B . n 
B 1 374 ASP 374 365 366 ASP ASP B . n 
B 1 375 PRO 375 366 367 PRO PRO B . n 
B 1 376 VAL 376 367 368 VAL VAL B . n 
B 1 377 VAL 377 368 369 VAL VAL B . n 
B 1 378 GLY 378 369 370 GLY GLY B . n 
B 1 379 TYR 379 370 371 TYR TYR B . n 
B 1 380 THR 380 371 372 THR THR B . n 
B 1 381 ASP 381 372 373 ASP ASP B . n 
B 1 382 TYR 382 373 374 TYR TYR B . n 
B 1 383 PRO 383 374 375 PRO PRO B . n 
B 1 384 PHE 384 375 376 PHE PHE B . n 
B 1 385 LEU 385 376 377 LEU LEU B . n 
B 1 386 GLN 386 377 ?   ?   ?   B . n 
B 1 387 GLY 387 378 ?   ?   ?   B . n 
B 1 388 ASN 388 379 ?   ?   ?   B . n 
B 1 389 GLY 389 380 ?   ?   ?   B . n 
B 1 390 SER 390 381 ?   ?   ?   B . n 
B 1 391 ASN 391 382 ?   ?   ?   B . n 
B 1 392 GLY 392 383 ?   ?   ?   B . n 
B 1 393 PRO 393 384 ?   ?   ?   B . n 
B 1 394 LEU 394 385 ?   ?   ?   B . n 
B 1 395 SER 395 386 ?   ?   ?   B . n 
B 1 396 ARG 396 387 ?   ?   ?   B . n 
B 1 397 LEU 397 388 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        5J8 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   5J8 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 FMN 1   401 401 FMN FMN A . 
D 3 5J8 1   402 402 5J8 5J8 A . 
E 2 FMN 1   401 401 FMN FMN B . 
F 3 5J8 1   402 402 5J8 5J8 B . 
G 4 HOH 1   501 265 HOH HOH A . 
G 4 HOH 2   502 262 HOH HOH A . 
G 4 HOH 3   503 111 HOH HOH A . 
G 4 HOH 4   504 163 HOH HOH A . 
G 4 HOH 5   505 267 HOH HOH A . 
G 4 HOH 6   506 99  HOH HOH A . 
G 4 HOH 7   507 205 HOH HOH A . 
G 4 HOH 8   508 213 HOH HOH A . 
G 4 HOH 9   509 56  HOH HOH A . 
G 4 HOH 10  510 112 HOH HOH A . 
G 4 HOH 11  511 186 HOH HOH A . 
G 4 HOH 12  512 271 HOH HOH A . 
G 4 HOH 13  513 309 HOH HOH A . 
G 4 HOH 14  514 142 HOH HOH A . 
G 4 HOH 15  515 78  HOH HOH A . 
G 4 HOH 16  516 108 HOH HOH A . 
G 4 HOH 17  517 298 HOH HOH A . 
G 4 HOH 18  518 84  HOH HOH A . 
G 4 HOH 19  519 117 HOH HOH A . 
G 4 HOH 20  520 72  HOH HOH A . 
G 4 HOH 21  521 77  HOH HOH A . 
G 4 HOH 22  522 258 HOH HOH A . 
G 4 HOH 23  523 36  HOH HOH A . 
G 4 HOH 24  524 141 HOH HOH A . 
G 4 HOH 25  525 81  HOH HOH A . 
G 4 HOH 26  526 6   HOH HOH A . 
G 4 HOH 27  527 98  HOH HOH A . 
G 4 HOH 28  528 76  HOH HOH A . 
G 4 HOH 29  529 97  HOH HOH A . 
G 4 HOH 30  530 41  HOH HOH A . 
G 4 HOH 31  531 29  HOH HOH A . 
G 4 HOH 32  532 20  HOH HOH A . 
G 4 HOH 33  533 33  HOH HOH A . 
G 4 HOH 34  534 303 HOH HOH A . 
G 4 HOH 35  535 82  HOH HOH A . 
G 4 HOH 36  536 261 HOH HOH A . 
G 4 HOH 37  537 4   HOH HOH A . 
G 4 HOH 38  538 211 HOH HOH A . 
G 4 HOH 39  539 209 HOH HOH A . 
G 4 HOH 40  540 207 HOH HOH A . 
G 4 HOH 41  541 9   HOH HOH A . 
G 4 HOH 42  542 12  HOH HOH A . 
G 4 HOH 43  543 18  HOH HOH A . 
G 4 HOH 44  544 210 HOH HOH A . 
G 4 HOH 45  545 14  HOH HOH A . 
G 4 HOH 46  546 73  HOH HOH A . 
G 4 HOH 47  547 46  HOH HOH A . 
G 4 HOH 48  548 25  HOH HOH A . 
G 4 HOH 49  549 196 HOH HOH A . 
G 4 HOH 50  550 200 HOH HOH A . 
G 4 HOH 51  551 230 HOH HOH A . 
G 4 HOH 52  552 2   HOH HOH A . 
G 4 HOH 53  553 106 HOH HOH A . 
G 4 HOH 54  554 89  HOH HOH A . 
G 4 HOH 55  555 137 HOH HOH A . 
G 4 HOH 56  556 59  HOH HOH A . 
G 4 HOH 57  557 31  HOH HOH A . 
G 4 HOH 58  558 53  HOH HOH A . 
G 4 HOH 59  559 102 HOH HOH A . 
G 4 HOH 60  560 250 HOH HOH A . 
G 4 HOH 61  561 274 HOH HOH A . 
G 4 HOH 62  562 217 HOH HOH A . 
G 4 HOH 63  563 68  HOH HOH A . 
G 4 HOH 64  564 37  HOH HOH A . 
G 4 HOH 65  565 30  HOH HOH A . 
G 4 HOH 66  566 244 HOH HOH A . 
G 4 HOH 67  567 150 HOH HOH A . 
G 4 HOH 68  568 288 HOH HOH A . 
G 4 HOH 69  569 225 HOH HOH A . 
G 4 HOH 70  570 121 HOH HOH A . 
G 4 HOH 71  571 188 HOH HOH A . 
G 4 HOH 72  572 49  HOH HOH A . 
G 4 HOH 73  573 52  HOH HOH A . 
G 4 HOH 74  574 130 HOH HOH A . 
G 4 HOH 75  575 315 HOH HOH A . 
G 4 HOH 76  576 199 HOH HOH A . 
G 4 HOH 77  577 296 HOH HOH A . 
G 4 HOH 78  578 140 HOH HOH A . 
G 4 HOH 79  579 237 HOH HOH A . 
G 4 HOH 80  580 176 HOH HOH A . 
G 4 HOH 81  581 174 HOH HOH A . 
G 4 HOH 82  582 256 HOH HOH A . 
G 4 HOH 83  583 44  HOH HOH A . 
G 4 HOH 84  584 185 HOH HOH A . 
G 4 HOH 85  585 190 HOH HOH A . 
G 4 HOH 86  586 236 HOH HOH A . 
G 4 HOH 87  587 88  HOH HOH A . 
G 4 HOH 88  588 219 HOH HOH A . 
G 4 HOH 89  589 95  HOH HOH A . 
G 4 HOH 90  590 305 HOH HOH A . 
G 4 HOH 91  591 255 HOH HOH A . 
G 4 HOH 92  592 75  HOH HOH A . 
G 4 HOH 93  593 47  HOH HOH A . 
G 4 HOH 94  594 167 HOH HOH A . 
G 4 HOH 95  595 187 HOH HOH A . 
G 4 HOH 96  596 278 HOH HOH A . 
G 4 HOH 97  597 312 HOH HOH A . 
G 4 HOH 98  598 162 HOH HOH A . 
G 4 HOH 99  599 131 HOH HOH A . 
G 4 HOH 100 600 302 HOH HOH A . 
G 4 HOH 101 601 66  HOH HOH A . 
G 4 HOH 102 602 178 HOH HOH A . 
G 4 HOH 103 603 222 HOH HOH A . 
G 4 HOH 104 604 194 HOH HOH A . 
G 4 HOH 105 605 179 HOH HOH A . 
G 4 HOH 106 606 119 HOH HOH A . 
G 4 HOH 107 607 70  HOH HOH A . 
G 4 HOH 108 608 173 HOH HOH A . 
G 4 HOH 109 609 43  HOH HOH A . 
G 4 HOH 110 610 323 HOH HOH A . 
G 4 HOH 111 611 129 HOH HOH A . 
G 4 HOH 112 612 170 HOH HOH A . 
G 4 HOH 113 613 238 HOH HOH A . 
G 4 HOH 114 614 269 HOH HOH A . 
G 4 HOH 115 615 233 HOH HOH A . 
G 4 HOH 116 616 195 HOH HOH A . 
G 4 HOH 117 617 166 HOH HOH A . 
G 4 HOH 118 618 120 HOH HOH A . 
G 4 HOH 119 619 161 HOH HOH A . 
G 4 HOH 120 620 156 HOH HOH A . 
G 4 HOH 121 621 310 HOH HOH A . 
G 4 HOH 122 622 284 HOH HOH A . 
G 4 HOH 123 623 291 HOH HOH A . 
G 4 HOH 124 624 276 HOH HOH A . 
G 4 HOH 125 625 135 HOH HOH A . 
G 4 HOH 126 626 235 HOH HOH A . 
G 4 HOH 127 627 331 HOH HOH A . 
G 4 HOH 128 628 218 HOH HOH A . 
G 4 HOH 129 629 177 HOH HOH A . 
G 4 HOH 130 630 326 HOH HOH A . 
G 4 HOH 131 631 311 HOH HOH A . 
G 4 HOH 132 632 324 HOH HOH A . 
G 4 HOH 133 633 223 HOH HOH A . 
G 4 HOH 134 634 279 HOH HOH A . 
G 4 HOH 135 635 295 HOH HOH A . 
G 4 HOH 136 636 266 HOH HOH A . 
G 4 HOH 137 637 212 HOH HOH A . 
G 4 HOH 138 638 206 HOH HOH A . 
G 4 HOH 139 639 314 HOH HOH A . 
G 4 HOH 140 640 214 HOH HOH A . 
G 4 HOH 141 641 300 HOH HOH A . 
G 4 HOH 142 642 224 HOH HOH A . 
G 4 HOH 143 643 109 HOH HOH A . 
G 4 HOH 144 644 164 HOH HOH A . 
G 4 HOH 145 645 322 HOH HOH A . 
G 4 HOH 146 646 228 HOH HOH A . 
G 4 HOH 147 647 306 HOH HOH A . 
G 4 HOH 148 648 321 HOH HOH A . 
G 4 HOH 149 649 169 HOH HOH A . 
G 4 HOH 150 650 320 HOH HOH A . 
G 4 HOH 151 651 168 HOH HOH A . 
G 4 HOH 152 652 115 HOH HOH A . 
G 4 HOH 153 653 153 HOH HOH A . 
G 4 HOH 154 654 226 HOH HOH A . 
H 4 HOH 1   501 283 HOH HOH B . 
H 4 HOH 2   502 319 HOH HOH B . 
H 4 HOH 3   503 292 HOH HOH B . 
H 4 HOH 4   504 40  HOH HOH B . 
H 4 HOH 5   505 308 HOH HOH B . 
H 4 HOH 6   506 85  HOH HOH B . 
H 4 HOH 7   507 287 HOH HOH B . 
H 4 HOH 8   508 330 HOH HOH B . 
H 4 HOH 9   509 202 HOH HOH B . 
H 4 HOH 10  510 198 HOH HOH B . 
H 4 HOH 11  511 23  HOH HOH B . 
H 4 HOH 12  512 87  HOH HOH B . 
H 4 HOH 13  513 91  HOH HOH B . 
H 4 HOH 14  514 285 HOH HOH B . 
H 4 HOH 15  515 299 HOH HOH B . 
H 4 HOH 16  516 7   HOH HOH B . 
H 4 HOH 17  517 101 HOH HOH B . 
H 4 HOH 18  518 64  HOH HOH B . 
H 4 HOH 19  519 282 HOH HOH B . 
H 4 HOH 20  520 51  HOH HOH B . 
H 4 HOH 21  521 325 HOH HOH B . 
H 4 HOH 22  522 113 HOH HOH B . 
H 4 HOH 23  523 132 HOH HOH B . 
H 4 HOH 24  524 15  HOH HOH B . 
H 4 HOH 25  525 297 HOH HOH B . 
H 4 HOH 26  526 294 HOH HOH B . 
H 4 HOH 27  527 160 HOH HOH B . 
H 4 HOH 28  528 13  HOH HOH B . 
H 4 HOH 29  529 55  HOH HOH B . 
H 4 HOH 30  530 1   HOH HOH B . 
H 4 HOH 31  531 11  HOH HOH B . 
H 4 HOH 32  532 146 HOH HOH B . 
H 4 HOH 33  533 50  HOH HOH B . 
H 4 HOH 34  534 191 HOH HOH B . 
H 4 HOH 35  535 48  HOH HOH B . 
H 4 HOH 36  536 103 HOH HOH B . 
H 4 HOH 37  537 83  HOH HOH B . 
H 4 HOH 38  538 149 HOH HOH B . 
H 4 HOH 39  539 34  HOH HOH B . 
H 4 HOH 40  540 63  HOH HOH B . 
H 4 HOH 41  541 183 HOH HOH B . 
H 4 HOH 42  542 86  HOH HOH B . 
H 4 HOH 43  543 203 HOH HOH B . 
H 4 HOH 44  544 216 HOH HOH B . 
H 4 HOH 45  545 147 HOH HOH B . 
H 4 HOH 46  546 251 HOH HOH B . 
H 4 HOH 47  547 105 HOH HOH B . 
H 4 HOH 48  548 69  HOH HOH B . 
H 4 HOH 49  549 71  HOH HOH B . 
H 4 HOH 50  550 128 HOH HOH B . 
H 4 HOH 51  551 3   HOH HOH B . 
H 4 HOH 52  552 45  HOH HOH B . 
H 4 HOH 53  553 126 HOH HOH B . 
H 4 HOH 54  554 247 HOH HOH B . 
H 4 HOH 55  555 184 HOH HOH B . 
H 4 HOH 56  556 263 HOH HOH B . 
H 4 HOH 57  557 316 HOH HOH B . 
H 4 HOH 58  558 189 HOH HOH B . 
H 4 HOH 59  559 125 HOH HOH B . 
H 4 HOH 60  560 122 HOH HOH B . 
H 4 HOH 61  561 124 HOH HOH B . 
H 4 HOH 62  562 16  HOH HOH B . 
H 4 HOH 63  563 241 HOH HOH B . 
H 4 HOH 64  564 32  HOH HOH B . 
H 4 HOH 65  565 151 HOH HOH B . 
H 4 HOH 66  566 116 HOH HOH B . 
H 4 HOH 67  567 62  HOH HOH B . 
H 4 HOH 68  568 307 HOH HOH B . 
H 4 HOH 69  569 148 HOH HOH B . 
H 4 HOH 70  570 234 HOH HOH B . 
H 4 HOH 71  571 61  HOH HOH B . 
H 4 HOH 72  572 38  HOH HOH B . 
H 4 HOH 73  573 58  HOH HOH B . 
H 4 HOH 74  574 175 HOH HOH B . 
H 4 HOH 75  575 94  HOH HOH B . 
H 4 HOH 76  576 74  HOH HOH B . 
H 4 HOH 77  577 133 HOH HOH B . 
H 4 HOH 78  578 154 HOH HOH B . 
H 4 HOH 79  579 220 HOH HOH B . 
H 4 HOH 80  580 107 HOH HOH B . 
H 4 HOH 81  581 10  HOH HOH B . 
H 4 HOH 82  582 134 HOH HOH B . 
H 4 HOH 83  583 227 HOH HOH B . 
H 4 HOH 84  584 145 HOH HOH B . 
H 4 HOH 85  585 79  HOH HOH B . 
H 4 HOH 86  586 42  HOH HOH B . 
H 4 HOH 87  587 92  HOH HOH B . 
H 4 HOH 88  588 231 HOH HOH B . 
H 4 HOH 89  589 172 HOH HOH B . 
H 4 HOH 90  590 80  HOH HOH B . 
H 4 HOH 91  591 123 HOH HOH B . 
H 4 HOH 92  592 39  HOH HOH B . 
H 4 HOH 93  593 90  HOH HOH B . 
H 4 HOH 94  594 67  HOH HOH B . 
H 4 HOH 95  595 100 HOH HOH B . 
H 4 HOH 96  596 118 HOH HOH B . 
H 4 HOH 97  597 93  HOH HOH B . 
H 4 HOH 98  598 248 HOH HOH B . 
H 4 HOH 99  599 155 HOH HOH B . 
H 4 HOH 100 600 208 HOH HOH B . 
H 4 HOH 101 601 24  HOH HOH B . 
H 4 HOH 102 602 139 HOH HOH B . 
H 4 HOH 103 603 144 HOH HOH B . 
H 4 HOH 104 604 27  HOH HOH B . 
H 4 HOH 105 605 304 HOH HOH B . 
H 4 HOH 106 606 110 HOH HOH B . 
H 4 HOH 107 607 289 HOH HOH B . 
H 4 HOH 108 608 28  HOH HOH B . 
H 4 HOH 109 609 5   HOH HOH B . 
H 4 HOH 110 610 136 HOH HOH B . 
H 4 HOH 111 611 54  HOH HOH B . 
H 4 HOH 112 612 290 HOH HOH B . 
H 4 HOH 113 613 19  HOH HOH B . 
H 4 HOH 114 614 8   HOH HOH B . 
H 4 HOH 115 615 229 HOH HOH B . 
H 4 HOH 116 616 272 HOH HOH B . 
H 4 HOH 117 617 259 HOH HOH B . 
H 4 HOH 118 618 171 HOH HOH B . 
H 4 HOH 119 619 22  HOH HOH B . 
H 4 HOH 120 620 281 HOH HOH B . 
H 4 HOH 121 621 280 HOH HOH B . 
H 4 HOH 122 622 204 HOH HOH B . 
H 4 HOH 123 623 159 HOH HOH B . 
H 4 HOH 124 624 21  HOH HOH B . 
H 4 HOH 125 625 182 HOH HOH B . 
H 4 HOH 126 626 286 HOH HOH B . 
H 4 HOH 127 627 257 HOH HOH B . 
H 4 HOH 128 628 317 HOH HOH B . 
H 4 HOH 129 629 249 HOH HOH B . 
H 4 HOH 130 630 301 HOH HOH B . 
H 4 HOH 131 631 152 HOH HOH B . 
H 4 HOH 132 632 35  HOH HOH B . 
H 4 HOH 133 633 240 HOH HOH B . 
H 4 HOH 134 634 157 HOH HOH B . 
H 4 HOH 135 635 318 HOH HOH B . 
H 4 HOH 136 636 127 HOH HOH B . 
H 4 HOH 137 637 254 HOH HOH B . 
H 4 HOH 138 638 270 HOH HOH B . 
H 4 HOH 139 639 65  HOH HOH B . 
H 4 HOH 140 640 104 HOH HOH B . 
H 4 HOH 141 641 181 HOH HOH B . 
H 4 HOH 142 642 245 HOH HOH B . 
H 4 HOH 143 643 313 HOH HOH B . 
H 4 HOH 144 644 17  HOH HOH B . 
H 4 HOH 145 645 96  HOH HOH B . 
H 4 HOH 146 646 60  HOH HOH B . 
H 4 HOH 147 647 215 HOH HOH B . 
H 4 HOH 148 648 243 HOH HOH B . 
H 4 HOH 149 649 277 HOH HOH B . 
H 4 HOH 150 650 114 HOH HOH B . 
H 4 HOH 151 651 143 HOH HOH B . 
H 4 HOH 152 652 273 HOH HOH B . 
H 4 HOH 153 653 264 HOH HOH B . 
H 4 HOH 154 654 221 HOH HOH B . 
H 4 HOH 155 655 201 HOH HOH B . 
H 4 HOH 156 656 242 HOH HOH B . 
H 4 HOH 157 657 193 HOH HOH B . 
H 4 HOH 158 658 57  HOH HOH B . 
H 4 HOH 159 659 253 HOH HOH B . 
H 4 HOH 160 660 246 HOH HOH B . 
H 4 HOH 161 661 165 HOH HOH B . 
H 4 HOH 162 662 138 HOH HOH B . 
H 4 HOH 163 663 328 HOH HOH B . 
H 4 HOH 164 664 252 HOH HOH B . 
H 4 HOH 165 665 260 HOH HOH B . 
H 4 HOH 166 666 232 HOH HOH B . 
H 4 HOH 167 667 26  HOH HOH B . 
H 4 HOH 168 668 197 HOH HOH B . 
H 4 HOH 169 669 293 HOH HOH B . 
H 4 HOH 170 670 192 HOH HOH B . 
H 4 HOH 171 671 158 HOH HOH B . 
H 4 HOH 172 672 327 HOH HOH B . 
H 4 HOH 173 673 239 HOH HOH B . 
H 4 HOH 174 674 180 HOH HOH B . 
H 4 HOH 175 675 275 HOH HOH B . 
H 4 HOH 176 676 268 HOH HOH B . 
H 4 HOH 177 677 332 HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 20  ? CG  ? A LYS 29  CG  
2  1 Y 1 A LYS 20  ? CD  ? A LYS 29  CD  
3  1 Y 1 A LYS 20  ? CE  ? A LYS 29  CE  
4  1 Y 1 A LYS 20  ? NZ  ? A LYS 29  NZ  
5  1 Y 1 A LYS 99  ? CG  ? A LYS 108 CG  
6  1 Y 1 A LYS 99  ? CD  ? A LYS 108 CD  
7  1 Y 1 A LYS 99  ? CE  ? A LYS 108 CE  
8  1 Y 1 A LYS 99  ? NZ  ? A LYS 108 NZ  
9  1 Y 1 A GLU 116 ? CG  ? A GLU 125 CG  
10 1 Y 1 A GLU 116 ? CD  ? A GLU 125 CD  
11 1 Y 1 A GLU 116 ? OE1 ? A GLU 125 OE1 
12 1 Y 1 A GLU 116 ? OE2 ? A GLU 125 OE2 
13 1 Y 1 A LYS 131 ? CG  ? A LYS 140 CG  
14 1 Y 1 A LYS 131 ? CD  ? A LYS 140 CD  
15 1 Y 1 A LYS 131 ? CE  ? A LYS 140 CE  
16 1 Y 1 A LYS 131 ? NZ  ? A LYS 140 NZ  
17 1 Y 1 A LYS 216 ? CG  ? A LYS 225 CG  
18 1 Y 1 A LYS 216 ? CD  ? A LYS 225 CD  
19 1 Y 1 A LYS 216 ? CE  ? A LYS 225 CE  
20 1 Y 1 A LYS 216 ? NZ  ? A LYS 225 NZ  
21 1 Y 1 A ASP 243 ? CG  ? A ASP 252 CG  
22 1 Y 1 A ASP 243 ? OD1 ? A ASP 252 OD1 
23 1 Y 1 A ASP 243 ? OD2 ? A ASP 252 OD2 
24 1 Y 1 A LYS 265 ? CG  ? A LYS 274 CG  
25 1 Y 1 A LYS 265 ? CD  ? A LYS 274 CD  
26 1 Y 1 A LYS 265 ? CE  ? A LYS 274 CE  
27 1 Y 1 A LYS 265 ? NZ  ? A LYS 274 NZ  
28 1 Y 1 A HIS 269 ? CG  ? A HIS 278 CG  
29 1 Y 1 A HIS 269 ? ND1 ? A HIS 278 ND1 
30 1 Y 1 A HIS 269 ? CD2 ? A HIS 278 CD2 
31 1 Y 1 A HIS 269 ? CE1 ? A HIS 278 CE1 
32 1 Y 1 A HIS 269 ? NE2 ? A HIS 278 NE2 
33 1 Y 1 A SER 284 ? OG  ? A SER 293 OG  
34 1 Y 1 A GLU 291 ? CG  ? A GLU 300 CG  
35 1 Y 1 A GLU 291 ? CD  ? A GLU 300 CD  
36 1 Y 1 A GLU 291 ? OE1 ? A GLU 300 OE1 
37 1 Y 1 A GLU 291 ? OE2 ? A GLU 300 OE2 
38 1 Y 1 A GLU 293 ? CG  ? A GLU 302 CG  
39 1 Y 1 A GLU 293 ? CD  ? A GLU 302 CD  
40 1 Y 1 A GLU 293 ? OE1 ? A GLU 302 OE1 
41 1 Y 1 A GLU 293 ? OE2 ? A GLU 302 OE2 
42 1 Y 1 A GLU 317 ? CG  ? A GLU 326 CG  
43 1 Y 1 A GLU 317 ? CD  ? A GLU 326 CD  
44 1 Y 1 A GLU 317 ? OE1 ? A GLU 326 OE1 
45 1 Y 1 A GLU 317 ? OE2 ? A GLU 326 OE2 
46 1 Y 1 A LYS 359 ? CG  ? A LYS 368 CG  
47 1 Y 1 A LYS 359 ? CD  ? A LYS 368 CD  
48 1 Y 1 A LYS 359 ? CE  ? A LYS 368 CE  
49 1 Y 1 A LYS 359 ? NZ  ? A LYS 368 NZ  
50 1 Y 1 A GLN 377 ? CG  ? A GLN 386 CG  
51 1 Y 1 A GLN 377 ? CD  ? A GLN 386 CD  
52 1 Y 1 A GLN 377 ? OE1 ? A GLN 386 OE1 
53 1 Y 1 A GLN 377 ? NE2 ? A GLN 386 NE2 
54 1 Y 1 B LYS 17  ? CG  ? B LYS 26  CG  
55 1 Y 1 B LYS 17  ? CD  ? B LYS 26  CD  
56 1 Y 1 B LYS 17  ? CE  ? B LYS 26  CE  
57 1 Y 1 B LYS 17  ? NZ  ? B LYS 26  NZ  
58 1 Y 1 B GLU 51  ? CG  ? B GLU 60  CG  
59 1 Y 1 B GLU 51  ? CD  ? B GLU 60  CD  
60 1 Y 1 B GLU 51  ? OE1 ? B GLU 60  OE1 
61 1 Y 1 B GLU 51  ? OE2 ? B GLU 60  OE2 
62 1 Y 1 B VAL 96  ? CG1 ? B VAL 105 CG1 
63 1 Y 1 B VAL 96  ? CG2 ? B VAL 105 CG2 
64 1 Y 1 B LYS 99  ? CG  ? B LYS 108 CG  
65 1 Y 1 B LYS 99  ? CD  ? B LYS 108 CD  
66 1 Y 1 B LYS 99  ? CE  ? B LYS 108 CE  
67 1 Y 1 B LYS 99  ? NZ  ? B LYS 108 NZ  
68 1 Y 1 B GLU 116 ? CG  ? B GLU 125 CG  
69 1 Y 1 B GLU 116 ? CD  ? B GLU 125 CD  
70 1 Y 1 B GLU 116 ? OE1 ? B GLU 125 OE1 
71 1 Y 1 B GLU 116 ? OE2 ? B GLU 125 OE2 
72 1 Y 1 B GLN 223 ? CG  ? B GLN 232 CG  
73 1 Y 1 B GLN 223 ? CD  ? B GLN 232 CD  
74 1 Y 1 B GLN 223 ? OE1 ? B GLN 232 OE1 
75 1 Y 1 B GLN 223 ? NE2 ? B GLN 232 NE2 
76 1 Y 1 B LYS 265 ? CG  ? B LYS 274 CG  
77 1 Y 1 B LYS 265 ? CD  ? B LYS 274 CD  
78 1 Y 1 B LYS 265 ? CE  ? B LYS 274 CE  
79 1 Y 1 B LYS 265 ? NZ  ? B LYS 274 NZ  
80 1 Y 1 B GLU 290 ? CG  ? B GLU 299 CG  
81 1 Y 1 B GLU 290 ? CD  ? B GLU 299 CD  
82 1 Y 1 B GLU 290 ? OE1 ? B GLU 299 OE1 
83 1 Y 1 B GLU 290 ? OE2 ? B GLU 299 OE2 
84 1 Y 1 B GLU 291 ? CG  ? B GLU 300 CG  
85 1 Y 1 B GLU 291 ? CD  ? B GLU 300 CD  
86 1 Y 1 B GLU 291 ? OE1 ? B GLU 300 OE1 
87 1 Y 1 B GLU 291 ? OE2 ? B GLU 300 OE2 
88 1 Y 1 B GLU 292 ? CG  ? B GLU 301 CG  
89 1 Y 1 B GLU 292 ? CD  ? B GLU 301 CD  
90 1 Y 1 B GLU 292 ? OE1 ? B GLU 301 OE1 
91 1 Y 1 B GLU 292 ? OE2 ? B GLU 301 OE2 
92 1 Y 1 B GLU 317 ? CG  ? B GLU 326 CG  
93 1 Y 1 B GLU 317 ? CD  ? B GLU 326 CD  
94 1 Y 1 B GLU 317 ? OE1 ? B GLU 326 OE1 
95 1 Y 1 B GLU 317 ? OE2 ? B GLU 326 OE2 
96 1 Y 1 B LYS 359 ? CG  ? B LYS 368 CG  
97 1 Y 1 B LYS 359 ? CD  ? B LYS 368 CD  
98 1 Y 1 B LYS 359 ? CE  ? B LYS 368 CE  
99 1 Y 1 B LYS 359 ? NZ  ? B LYS 368 NZ  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX    ? ? ? '(dev_4761)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS       ? ? ? .            2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? pointless ? ? ? .            3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER    ? ? ? '(dev_4761)' 4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   100.38 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8QNM 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     50.200 
_cell.length_a_esd                 ? 
_cell.length_b                     89.950 
_cell.length_b_esd                 ? 
_cell.length_c                     90.520 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_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                         8QNM 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8QNM 
_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             2.30 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          46.44 
_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, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              6.5 
_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    '100 mM MES/Tris, 50 mM ammonium sulfate, 12% PEG8000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-06-30 
_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   1.033202 
_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                        'PETRA III, DESY BEAMLINE P11' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.033202 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   P11 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, DESY' 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8QNM 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.08 
_reflns.d_resolution_low                               44.97 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     304667 
_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                           91.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          1.27 
_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                                   0.618 
_reflns.pdbx_CC_star                                   ? 
_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                                    2.08 
_reflns_shell.d_res_low                                     2.12 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             836 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_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                                  0.0917 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_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                               ? 
_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                                 8QNM 
_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                            2.08 
_refine.ls_d_res_low                             44.97 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     43656 
_refine.ls_number_reflns_R_free                  2098 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    91.26 
_refine.ls_percent_reflns_R_free                 4.81 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2120 
_refine.ls_R_factor_R_free                       0.2427 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2104 
_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       ML 
_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             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_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                 27.22 
_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                            0.25 
_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.pdbx_number_atoms_protein        5586 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         158 
_refine_hist.number_atoms_solvent             332 
_refine_hist.number_atoms_total               6076 
_refine_hist.d_res_high                       2.08 
_refine_hist.d_res_low                        44.97 
# 
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' ? 0.002 ? 5885 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.470 ? 8030 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 8.871 ? 843  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.041 ? 884  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.004 ? 1026 ? f_plane_restr      ? ? 
# 
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' 2.08 2.12  . . 31  630  21.00 . . . . 0.4075 . . . . . . . . . . . 0.4529 
'X-RAY DIFFRACTION' 2.12 2.18  . . 136 2700 88.00 . . . . 0.2792 . . . . . . . . . . . 0.3306 
'X-RAY DIFFRACTION' 2.18 2.24  . . 143 2819 93.00 . . . . 0.2638 . . . . . . . . . . . 0.2960 
'X-RAY DIFFRACTION' 2.24 2.30  . . 148 2940 97.00 . . . . 0.2422 . . . . . . . . . . . 0.2839 
'X-RAY DIFFRACTION' 2.30 2.38  . . 150 2963 98.00 . . . . 0.2375 . . . . . . . . . . . 0.2916 
'X-RAY DIFFRACTION' 2.38 2.46  . . 148 2941 98.00 . . . . 0.2324 . . . . . . . . . . . 0.2979 
'X-RAY DIFFRACTION' 2.46 2.56  . . 150 2975 98.00 . . . . 0.2346 . . . . . . . . . . . 0.2466 
'X-RAY DIFFRACTION' 2.56 2.68  . . 149 2939 98.00 . . . . 0.2326 . . . . . . . . . . . 0.3196 
'X-RAY DIFFRACTION' 2.68 2.82  . . 152 3019 98.00 . . . . 0.2279 . . . . . . . . . . . 0.2728 
'X-RAY DIFFRACTION' 2.82 2.99  . . 150 2966 98.00 . . . . 0.2261 . . . . . . . . . . . 0.2617 
'X-RAY DIFFRACTION' 2.99 3.23  . . 140 2774 92.00 . . . . 0.2292 . . . . . . . . . . . 0.2996 
'X-RAY DIFFRACTION' 3.23 3.55  . . 151 3000 98.00 . . . . 0.2049 . . . . . . . . . . . 0.2254 
'X-RAY DIFFRACTION' 3.55 4.06  . . 151 2976 98.00 . . . . 0.1848 . . . . . . . . . . . 0.2068 
'X-RAY DIFFRACTION' 4.06 5.12  . . 151 3004 97.00 . . . . 0.1712 . . . . . . . . . . . 0.1740 
'X-RAY DIFFRACTION' 5.12 44.97 . . 148 2912 94.00 . . . . 0.2007 . . . . . . . . . . . 0.2332 
# 
_struct.entry_id                     8QNM 
_struct.title                        'OPR3 with redesigned Loop 6 (9aa) in complex with NADPH4' 
_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        8QNM 
_struct_keywords.text            'Old Yellow Enzyme, ene-reductase, flavoenzyme, NADPH, FLAVOPROTEIN' 
_struct_keywords.pdbx_keywords   FLAVOPROTEIN 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 2 ? 
F N N 3 ? 
G N N 4 ? 
H N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    OPR3_SOLLC 
_struct_ref.pdbx_db_accession          Q9FEW9 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MASSAQDGNNPLFSPYKMGKFNLSHRVVLAPMTRCRALNNIPQAALGEYYEQRATAGGFLITEGTMISPTSAGFPHVPGI
FTKEQVREWKKIVDVVHAKGAVIFCQLWHVGRASHEVYQPAGAAPISSTEKPISNRWRILMPDGTHGIYPKPRAIGTYEI
SQVVEDYRRSALNAIEAGFDGIEIHGAHGYLIDQFLKDGINDRTDEYGGSLANRCKFITQVVQAVVSAIGADRVGVRVSP
AIDHLDAMDSNPLSLGLAVVERLNKIQLHSGSKLAYLHVTQPRYVAYGQTEAGRLGSEEEEARLMRTLRNAYQGTFICSG
GYTRELGIEAVAQGDADLVSYGRLFISNPDLVMRIKLNAPLNKYNRKTFYTQDPVVGYTDYPFLQGNGSNGPLSRL
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8QNM A 10 ? 397 ? Q9FEW9 1 ? 396 ? 1 388 
2 1 8QNM B 10 ? 397 ? Q9FEW9 1 ? 396 ? 1 388 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 8QNM MET A 1   ? UNP Q9FEW9 ?   ?   'initiating methionine' -8  1  
1 8QNM ALA A 2   ? UNP Q9FEW9 ?   ?   'expression tag'        -7  2  
1 8QNM SER A 3   ? UNP Q9FEW9 ?   ?   'expression tag'        -6  3  
1 8QNM HIS A 4   ? UNP Q9FEW9 ?   ?   'expression tag'        -5  4  
1 8QNM HIS A 5   ? UNP Q9FEW9 ?   ?   'expression tag'        -4  5  
1 8QNM HIS A 6   ? UNP Q9FEW9 ?   ?   'expression tag'        -3  6  
1 8QNM HIS A 7   ? UNP Q9FEW9 ?   ?   'expression tag'        -2  7  
1 8QNM HIS A 8   ? UNP Q9FEW9 ?   ?   'expression tag'        -1  8  
1 8QNM HIS A 9   ? UNP Q9FEW9 ?   ?   'expression tag'        0   9  
1 8QNM SER A 293 ? UNP Q9FEW9 TYR 284 'engineered mutation'   284 10 
1 8QNM ASP A 294 ? UNP Q9FEW9 VAL 285 'engineered mutation'   285 11 
1 8QNM LYS A 295 ? UNP Q9FEW9 ALA 286 'engineered mutation'   286 12 
1 8QNM GLY A 296 ? UNP Q9FEW9 TYR 287 'engineered mutation'   287 13 
1 8QNM ?   A ?   ? UNP Q9FEW9 GLY 288 deletion                ?   14 
1 8QNM ?   A ?   ? UNP Q9FEW9 GLN 289 deletion                ?   15 
1 8QNM ?   A ?   ? UNP Q9FEW9 THR 290 deletion                ?   16 
1 8QNM ?   A ?   ? UNP Q9FEW9 GLU 291 deletion                ?   17 
1 8QNM ?   A ?   ? UNP Q9FEW9 ALA 292 deletion                ?   18 
1 8QNM ?   A ?   ? UNP Q9FEW9 GLY 293 deletion                ?   19 
1 8QNM ?   A ?   ? UNP Q9FEW9 ARG 294 deletion                ?   20 
1 8QNM ?   A ?   ? UNP Q9FEW9 LEU 295 deletion                ?   21 
2 8QNM MET B 1   ? UNP Q9FEW9 ?   ?   'initiating methionine' -8  22 
2 8QNM ALA B 2   ? UNP Q9FEW9 ?   ?   'expression tag'        -7  23 
2 8QNM SER B 3   ? UNP Q9FEW9 ?   ?   'expression tag'        -6  24 
2 8QNM HIS B 4   ? UNP Q9FEW9 ?   ?   'expression tag'        -5  25 
2 8QNM HIS B 5   ? UNP Q9FEW9 ?   ?   'expression tag'        -4  26 
2 8QNM HIS B 6   ? UNP Q9FEW9 ?   ?   'expression tag'        -3  27 
2 8QNM HIS B 7   ? UNP Q9FEW9 ?   ?   'expression tag'        -2  28 
2 8QNM HIS B 8   ? UNP Q9FEW9 ?   ?   'expression tag'        -1  29 
2 8QNM HIS B 9   ? UNP Q9FEW9 ?   ?   'expression tag'        0   30 
2 8QNM SER B 293 ? UNP Q9FEW9 TYR 284 'engineered mutation'   284 31 
2 8QNM ASP B 294 ? UNP Q9FEW9 VAL 285 'engineered mutation'   285 32 
2 8QNM LYS B 295 ? UNP Q9FEW9 ALA 286 'engineered mutation'   286 33 
2 8QNM GLY B 296 ? UNP Q9FEW9 TYR 287 'engineered mutation'   287 34 
2 8QNM ?   B ?   ? UNP Q9FEW9 GLY 288 deletion                ?   35 
2 8QNM ?   B ?   ? UNP Q9FEW9 GLN 289 deletion                ?   36 
2 8QNM ?   B ?   ? UNP Q9FEW9 THR 290 deletion                ?   37 
2 8QNM ?   B ?   ? UNP Q9FEW9 GLU 291 deletion                ?   38 
2 8QNM ?   B ?   ? UNP Q9FEW9 ALA 292 deletion                ?   39 
2 8QNM ?   B ?   ? UNP Q9FEW9 GLY 293 deletion                ?   40 
2 8QNM ?   B ?   ? UNP Q9FEW9 ARG 294 deletion                ?   41 
2 8QNM ?   B ?   ? UNP Q9FEW9 LEU 295 deletion                ?   42 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,G 
2 1 B,E,F,H 
# 
_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 ASN A 19  ? SER A 23  ? ASN A 10  SER A 14  5 ? 5  
HELX_P HELX_P2  AA2 ALA A 46  ? ILE A 50  ? ALA A 37  ILE A 41  5 ? 5  
HELX_P HELX_P3  AA3 GLN A 52  ? ALA A 63  ? GLN A 43  ALA A 54  1 ? 12 
HELX_P HELX_P4  AA4 THR A 91  ? LYS A 108 ? THR A 82  LYS A 99  1 ? 18 
HELX_P HELX_P5  AA5 HIS A 124 ? ALA A 132 ? HIS A 115 ALA A 123 5 ? 9  
HELX_P HELX_P6  AA6 GLY A 165 ? ALA A 186 ? GLY A 156 ALA A 177 1 ? 22 
HELX_P HELX_P7  AA7 TYR A 199 ? LYS A 206 ? TYR A 190 LYS A 197 1 ? 8  
HELX_P HELX_P8  AA8 SER A 219 ? CYS A 224 ? SER A 210 CYS A 215 1 ? 6  
HELX_P HELX_P9  AA9 CYS A 224 ? GLY A 239 ? CYS A 215 GLY A 230 1 ? 16 
HELX_P HELX_P10 AB1 ASN A 260 ? GLY A 280 ? ASN A 251 GLY A 271 1 ? 21 
HELX_P HELX_P11 AB2 SER A 298 ? TYR A 313 ? SER A 289 TYR A 304 1 ? 16 
HELX_P HELX_P12 AB3 THR A 324 ? GLN A 334 ? THR A 315 GLN A 325 1 ? 11 
HELX_P HELX_P13 AB4 GLY A 343 ? ASN A 349 ? GLY A 334 ASN A 340 1 ? 7  
HELX_P HELX_P14 AB5 ASP A 351 ? ASN A 359 ? ASP A 342 ASN A 350 1 ? 9  
HELX_P HELX_P15 AB6 ASN A 366 ? PHE A 370 ? ASN A 357 PHE A 361 5 ? 5  
HELX_P HELX_P16 AB7 ASN B 19  ? SER B 23  ? ASN B 10  SER B 14  5 ? 5  
HELX_P HELX_P17 AB8 ALA B 46  ? ILE B 50  ? ALA B 37  ILE B 41  5 ? 5  
HELX_P HELX_P18 AB9 GLN B 52  ? ALA B 63  ? GLN B 43  ALA B 54  1 ? 12 
HELX_P HELX_P19 AC1 THR B 91  ? LYS B 108 ? THR B 82  LYS B 99  1 ? 18 
HELX_P HELX_P20 AC2 HIS B 124 ? ALA B 132 ? HIS B 115 ALA B 123 5 ? 9  
HELX_P HELX_P21 AC3 GLY B 165 ? GLY B 187 ? GLY B 156 GLY B 178 1 ? 23 
HELX_P HELX_P22 AC4 TYR B 199 ? LYS B 206 ? TYR B 190 LYS B 197 1 ? 8  
HELX_P HELX_P23 AC5 SER B 219 ? CYS B 224 ? SER B 210 CYS B 215 1 ? 6  
HELX_P HELX_P24 AC6 CYS B 224 ? GLY B 239 ? CYS B 215 GLY B 230 1 ? 16 
HELX_P HELX_P25 AC7 ASP B 252 ? ALA B 256 ? ASP B 243 ALA B 247 5 ? 5  
HELX_P HELX_P26 AC8 ASN B 260 ? GLY B 280 ? ASN B 251 GLY B 271 1 ? 21 
HELX_P HELX_P27 AC9 GLU B 299 ? TYR B 313 ? GLU B 290 TYR B 304 1 ? 15 
HELX_P HELX_P28 AD1 THR B 324 ? GLN B 334 ? THR B 315 GLN B 325 1 ? 11 
HELX_P HELX_P29 AD2 GLY B 343 ? ASN B 349 ? GLY B 334 ASN B 340 1 ? 7  
HELX_P HELX_P30 AD3 ASP B 351 ? ASN B 359 ? ASP B 342 ASN B 350 1 ? 9  
HELX_P HELX_P31 AD4 ASN B 366 ? PHE B 370 ? ASN B 357 PHE B 361 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 9 ? 
AA3 ? 2 ? 
AA4 ? 2 ? 
AA5 ? 2 ? 
AA6 ? 9 ? 
AA7 ? 2 ? 
AA8 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA2 4 5 ? parallel      
AA2 5 6 ? parallel      
AA2 6 7 ? parallel      
AA2 7 8 ? parallel      
AA2 8 9 ? parallel      
AA3 1 2 ? parallel      
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA6 1 2 ? parallel      
AA6 2 3 ? parallel      
AA6 3 4 ? parallel      
AA6 4 5 ? parallel      
AA6 5 6 ? parallel      
AA6 6 7 ? parallel      
AA6 7 8 ? parallel      
AA6 8 9 ? parallel      
AA7 1 2 ? parallel      
AA8 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 TYR A 25  ? MET A 27  ? TYR A 16  MET A 18  
AA1 2 PHE A 30  ? LEU A 32  ? PHE A 21  LEU A 23  
AA2 1 VAL A 36  ? LEU A 38  ? VAL A 27  LEU A 29  
AA2 2 PHE A 68  ? THR A 74  ? PHE A 59  THR A 65  
AA2 3 VAL A 111 ? LEU A 116 ? VAL A 102 LEU A 107 
AA2 4 GLY A 190 ? GLY A 195 ? GLY A 181 GLY A 186 
AA2 5 VAL A 243 ? VAL A 247 ? VAL A 234 VAL A 238 
AA2 6 TYR A 285 ? THR A 289 ? TYR A 276 THR A 280 
AA2 7 PHE A 317 ? SER A 320 ? PHE A 308 SER A 311 
AA2 8 LEU A 339 ? TYR A 342 ? LEU A 330 TYR A 333 
AA2 9 VAL A 36  ? LEU A 38  ? VAL A 27  LEU A 29  
AA3 1 ILE A 135 ? SER A 136 ? ILE A 126 SER A 127 
AA3 2 ARG A 162 ? ALA A 163 ? ARG A 153 ALA A 154 
AA4 1 ILE A 148 ? LEU A 149 ? ILE A 139 LEU A 140 
AA4 2 HIS A 155 ? GLY A 156 ? HIS A 146 GLY A 147 
AA5 1 TYR B 25  ? MET B 27  ? TYR B 16  MET B 18  
AA5 2 PHE B 30  ? LEU B 32  ? PHE B 21  LEU B 23  
AA6 1 VAL B 36  ? LEU B 38  ? VAL B 27  LEU B 29  
AA6 2 PHE B 68  ? ILE B 70  ? PHE B 59  ILE B 61  
AA6 3 VAL B 111 ? LEU B 116 ? VAL B 102 LEU B 107 
AA6 4 GLY B 190 ? GLY B 195 ? GLY B 181 GLY B 186 
AA6 5 VAL B 243 ? VAL B 247 ? VAL B 234 VAL B 238 
AA6 6 TYR B 285 ? THR B 289 ? TYR B 276 THR B 280 
AA6 7 PHE B 317 ? SER B 320 ? PHE B 308 SER B 311 
AA6 8 LEU B 339 ? TYR B 342 ? LEU B 330 TYR B 333 
AA6 9 VAL B 36  ? LEU B 38  ? VAL B 27  LEU B 29  
AA7 1 ILE B 135 ? SER B 136 ? ILE B 126 SER B 127 
AA7 2 ARG B 162 ? ALA B 163 ? ARG B 153 ALA B 154 
AA8 1 ILE B 148 ? LEU B 149 ? ILE B 139 LEU B 140 
AA8 2 HIS B 155 ? GLY B 156 ? HIS B 146 GLY B 147 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N TYR A 25  ? N TYR A 16  O LEU A 32  ? O LEU A 23  
AA2 1 2 N LEU A 38  ? N LEU A 29  O PHE A 68  ? O PHE A 59  
AA2 2 3 N LEU A 69  ? N LEU A 60  O VAL A 111 ? O VAL A 102 
AA2 3 4 N LEU A 116 ? N LEU A 107 O GLU A 192 ? O GLU A 183 
AA2 4 5 N ILE A 191 ? N ILE A 182 O GLY A 244 ? O GLY A 235 
AA2 5 6 N VAL A 245 ? N VAL A 236 O HIS A 287 ? O HIS A 278 
AA2 6 7 N LEU A 286 ? N LEU A 277 O ILE A 318 ? O ILE A 309 
AA2 7 8 N CYS A 319 ? N CYS A 310 O SER A 341 ? O SER A 332 
AA2 8 9 O TYR A 342 ? O TYR A 333 N VAL A 37  ? N VAL A 28  
AA3 1 2 N SER A 136 ? N SER A 127 O ARG A 162 ? O ARG A 153 
AA4 1 2 N ILE A 148 ? N ILE A 139 O GLY A 156 ? O GLY A 147 
AA5 1 2 N TYR B 25  ? N TYR B 16  O LEU B 32  ? O LEU B 23  
AA6 1 2 N LEU B 38  ? N LEU B 29  O PHE B 68  ? O PHE B 59  
AA6 2 3 N LEU B 69  ? N LEU B 60  O VAL B 111 ? O VAL B 102 
AA6 3 4 N LEU B 116 ? N LEU B 107 O GLU B 192 ? O GLU B 183 
AA6 4 5 N ILE B 193 ? N ILE B 184 O GLY B 244 ? O GLY B 235 
AA6 5 6 N VAL B 245 ? N VAL B 236 O HIS B 287 ? O HIS B 278 
AA6 6 7 N LEU B 286 ? N LEU B 277 O ILE B 318 ? O ILE B 309 
AA6 7 8 N CYS B 319 ? N CYS B 310 O SER B 341 ? O SER B 332 
AA6 8 9 O VAL B 340 ? O VAL B 331 N VAL B 37  ? N VAL B 28  
AA7 1 2 N SER B 136 ? N SER B 127 O ARG B 162 ? O ARG B 153 
AA8 1 2 N ILE B 148 ? N ILE B 139 O GLY B 156 ? O GLY B 147 
# 
_pdbx_entry_details.entry_id                   8QNM 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 O   B HOH 659 ? ? O B HOH 664 ? ? 1.92 
2  1 O   B HOH 557 ? ? O B HOH 628 ? ? 1.96 
3  1 O   B LEU 255 ? ? O B HOH 501 ? ? 1.99 
4  1 OE1 A GLU 165 ? ? O A HOH 501 ? ? 2.01 
5  1 OP2 B 5J8 402 ? ? O B HOH 502 ? ? 2.01 
6  1 O   B HOH 612 ? ? O B HOH 638 ? ? 2.02 
7  1 O   A ALA 124 ? ? O A HOH 502 ? ? 2.07 
8  1 O   A HOH 575 ? ? O A HOH 639 ? ? 2.09 
9  1 O   A HOH 645 ? ? O A HOH 650 ? ? 2.09 
10 1 NZ  B LYS 131 ? ? O B HOH 503 ? ? 2.10 
11 1 OE2 B GLU 48  ? ? O B HOH 504 ? ? 2.10 
12 1 N   B GLN 325 ? ? O B HOH 505 ? ? 2.10 
13 1 N   B VAL 259 ? ? O B HOH 501 ? ? 2.13 
14 1 NH1 B ARG 316 ? ? O B HOH 506 ? ? 2.16 
15 1 OE1 A GLN 43  ? ? O A HOH 503 ? ? 2.16 
16 1 O   A ALA 113 ? ? O A HOH 504 ? ? 2.18 
17 1 O   B HOH 507 ? ? O B HOH 556 ? ? 2.18 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O A HOH 606 ? ? 1_555 O A HOH 619 ? ? 2_645 2.07 
2 1 O A HOH 585 ? ? 1_555 O A HOH 617 ? ? 2_645 2.15 
3 1 O A HOH 568 ? ? 1_555 O A HOH 636 ? ? 1_655 2.16 
4 1 O B HOH 533 ? ? 1_555 O B HOH 656 ? ? 1_455 2.18 
# 
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 ILE A 80  ? ? -148.02 22.19   
2  1 SER A 239 ? ? -151.25 72.63   
3  1 ASP A 243 ? ? -99.74  35.15   
4  1 ARG A 283 ? ? 62.27   -126.00 
5  1 ASP A 342 ? ? -92.53  44.94   
6  1 VAL A 367 ? ? -130.57 -40.97  
7  1 TYR A 370 ? ? -124.34 -60.16  
8  1 ILE B 80  ? ? -146.64 23.56   
9  1 ALA B 121 ? ? 57.29   19.80   
10 1 TYR B 190 ? ? -91.78  -159.67 
11 1 ASP B 205 ? ? -105.58 -164.27 
12 1 SER B 239 ? ? -154.10 77.24   
13 1 ASP B 342 ? ? -98.49  45.33   
14 1 VAL B 367 ? ? -125.89 -53.28  
15 1 TYR B 370 ? ? -123.81 -59.74  
# 
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 MET -8  ? A MET 1   
2  1 Y 1 A ALA -7  ? A ALA 2   
3  1 Y 1 A SER -6  ? A SER 3   
4  1 Y 1 A HIS -5  ? A HIS 4   
5  1 Y 1 A HIS -4  ? A HIS 5   
6  1 Y 1 A HIS -3  ? A HIS 6   
7  1 Y 1 A HIS -2  ? A HIS 7   
8  1 Y 1 A HIS -1  ? A HIS 8   
9  1 Y 1 A HIS 0   ? A HIS 9   
10 1 Y 1 A MET 1   ? A MET 10  
11 1 Y 1 A ALA 2   ? A ALA 11  
12 1 Y 1 A SER 3   ? A SER 12  
13 1 Y 1 A SER 4   ? A SER 13  
14 1 Y 1 A ALA 5   ? A ALA 14  
15 1 Y 1 A GLN 6   ? A GLN 15  
16 1 Y 1 A ASP 7   ? A ASP 16  
17 1 Y 1 A GLY 8   ? A GLY 17  
18 1 Y 1 A ASN 9   ? A ASN 18  
19 1 Y 1 A ASP 285 ? A ASP 294 
20 1 Y 1 A LYS 286 ? A LYS 295 
21 1 Y 1 A GLY 378 ? A GLY 387 
22 1 Y 1 A ASN 379 ? A ASN 388 
23 1 Y 1 A GLY 380 ? A GLY 389 
24 1 Y 1 A SER 381 ? A SER 390 
25 1 Y 1 A ASN 382 ? A ASN 391 
26 1 Y 1 A GLY 383 ? A GLY 392 
27 1 Y 1 A PRO 384 ? A PRO 393 
28 1 Y 1 A LEU 385 ? A LEU 394 
29 1 Y 1 A SER 386 ? A SER 395 
30 1 Y 1 A ARG 387 ? A ARG 396 
31 1 Y 1 A LEU 388 ? A LEU 397 
32 1 Y 1 B MET -8  ? B MET 1   
33 1 Y 1 B ALA -7  ? B ALA 2   
34 1 Y 1 B SER -6  ? B SER 3   
35 1 Y 1 B HIS -5  ? B HIS 4   
36 1 Y 1 B HIS -4  ? B HIS 5   
37 1 Y 1 B HIS -3  ? B HIS 6   
38 1 Y 1 B HIS -2  ? B HIS 7   
39 1 Y 1 B HIS -1  ? B HIS 8   
40 1 Y 1 B HIS 0   ? B HIS 9   
41 1 Y 1 B MET 1   ? B MET 10  
42 1 Y 1 B ALA 2   ? B ALA 11  
43 1 Y 1 B SER 3   ? B SER 12  
44 1 Y 1 B SER 4   ? B SER 13  
45 1 Y 1 B ALA 5   ? B ALA 14  
46 1 Y 1 B GLN 6   ? B GLN 15  
47 1 Y 1 B ASP 7   ? B ASP 16  
48 1 Y 1 B GLY 8   ? B GLY 17  
49 1 Y 1 B ASN 9   ? B ASN 18  
50 1 Y 1 B ASP 285 ? B ASP 294 
51 1 Y 1 B LYS 286 ? B LYS 295 
52 1 Y 1 B GLY 287 ? B GLY 296 
53 1 Y 1 B GLY 288 ? B GLY 297 
54 1 Y 1 B GLN 377 ? B GLN 386 
55 1 Y 1 B GLY 378 ? B GLY 387 
56 1 Y 1 B ASN 379 ? B ASN 388 
57 1 Y 1 B GLY 380 ? B GLY 389 
58 1 Y 1 B SER 381 ? B SER 390 
59 1 Y 1 B ASN 382 ? B ASN 391 
60 1 Y 1 B GLY 383 ? B GLY 392 
61 1 Y 1 B PRO 384 ? B PRO 393 
62 1 Y 1 B LEU 385 ? B LEU 394 
63 1 Y 1 B SER 386 ? B SER 395 
64 1 Y 1 B ARG 387 ? B ARG 396 
65 1 Y 1 B LEU 388 ? B LEU 397 
# 
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 
5J8 C4     C Y N 1   
5J8 C5     C Y N 2   
5J8 C6     C Y N 3   
5J8 C8     C Y N 4   
5J8 N1     N Y N 5   
5J8 N3     N Y N 6   
5J8 NBU    N N N 7   
5J8 CBT    C N N 8   
5J8 OBV    O N N 9   
5J8 CBR    C N N 10  
5J8 CBQ    C N N 11  
5J8 CBS    C N N 12  
5J8 CBN    C N N 13  
5J8 CBO    C N N 14  
5J8 NBP    N N N 15  
5J8 CBM    C N R 16  
5J8 OBG    O N N 17  
5J8 CBF    C N R 18  
5J8 OBI    O N N 19  
5J8 CBE    C N S 20  
5J8 OBJ    O N N 21  
5J8 CBH    C N R 22  
5J8 CBK    C N N 23  
5J8 OBL    O N N 24  
5J8 PAA    P N N 25  
5J8 OAC    O N N 26  
5J8 OAB    O N N 27  
5J8 OAD    O N N 28  
5J8 PAE    P N N 29  
5J8 OAG    O N N 30  
5J8 OAF    O N N 31  
5J8 "O5'"  O N N 32  
5J8 "C5'"  C N N 33  
5J8 "C4'"  C N R 34  
5J8 "O4'"  O N N 35  
5J8 "C3'"  C N R 36  
5J8 "O3'"  O N N 37  
5J8 "C2'"  C N R 38  
5J8 "O2'"  O N N 39  
5J8 "P2'"  P N N 40  
5J8 OP1    O N N 41  
5J8 OP3    O N N 42  
5J8 OP2    O N N 43  
5J8 "C1'"  C N R 44  
5J8 N9     N Y N 45  
5J8 N7     N Y N 46  
5J8 C2     C Y N 47  
5J8 N6     N N N 48  
5J8 H1     H N N 49  
5J8 H2     H N N 50  
5J8 H3     H N N 51  
5J8 H5     H N N 52  
5J8 H7     H N N 53  
5J8 H8     H N N 54  
5J8 H9     H N N 55  
5J8 H10    H N N 56  
5J8 H11    H N N 57  
5J8 H12    H N N 58  
5J8 H13    H N N 59  
5J8 H14    H N N 60  
5J8 H15    H N N 61  
5J8 H16    H N N 62  
5J8 H17    H N N 63  
5J8 H18    H N N 64  
5J8 H19    H N N 65  
5J8 H20    H N N 66  
5J8 H21    H N N 67  
5J8 H22    H N N 68  
5J8 H23    H N N 69  
5J8 H24    H N N 70  
5J8 H25    H N N 71  
5J8 H26    H N N 72  
5J8 H27    H N N 73  
5J8 H28    H N N 74  
5J8 H29    H N N 75  
5J8 H30    H N N 76  
5J8 H31    H N N 77  
5J8 H32    H N N 78  
5J8 H4     H N N 79  
5J8 H6     H N N 80  
ALA N      N N N 81  
ALA CA     C N S 82  
ALA C      C N N 83  
ALA O      O N N 84  
ALA CB     C N N 85  
ALA OXT    O N N 86  
ALA H      H N N 87  
ALA H2     H N N 88  
ALA HA     H N N 89  
ALA HB1    H N N 90  
ALA HB2    H N N 91  
ALA HB3    H N N 92  
ALA HXT    H N N 93  
ARG N      N N N 94  
ARG CA     C N S 95  
ARG C      C N N 96  
ARG O      O N N 97  
ARG CB     C N N 98  
ARG CG     C N N 99  
ARG CD     C N N 100 
ARG NE     N N N 101 
ARG CZ     C N N 102 
ARG NH1    N N N 103 
ARG NH2    N N N 104 
ARG OXT    O N N 105 
ARG H      H N N 106 
ARG H2     H N N 107 
ARG HA     H N N 108 
ARG HB2    H N N 109 
ARG HB3    H N N 110 
ARG HG2    H N N 111 
ARG HG3    H N N 112 
ARG HD2    H N N 113 
ARG HD3    H N N 114 
ARG HE     H N N 115 
ARG HH11   H N N 116 
ARG HH12   H N N 117 
ARG HH21   H N N 118 
ARG HH22   H N N 119 
ARG HXT    H N N 120 
ASN N      N N N 121 
ASN CA     C N S 122 
ASN C      C N N 123 
ASN O      O N N 124 
ASN CB     C N N 125 
ASN CG     C N N 126 
ASN OD1    O N N 127 
ASN ND2    N N N 128 
ASN OXT    O N N 129 
ASN H      H N N 130 
ASN H2     H N N 131 
ASN HA     H N N 132 
ASN HB2    H N N 133 
ASN HB3    H N N 134 
ASN HD21   H N N 135 
ASN HD22   H N N 136 
ASN HXT    H N N 137 
ASP N      N N N 138 
ASP CA     C N S 139 
ASP C      C N N 140 
ASP O      O N N 141 
ASP CB     C N N 142 
ASP CG     C N N 143 
ASP OD1    O N N 144 
ASP OD2    O N N 145 
ASP OXT    O N N 146 
ASP H      H N N 147 
ASP H2     H N N 148 
ASP HA     H N N 149 
ASP HB2    H N N 150 
ASP HB3    H N N 151 
ASP HD2    H N N 152 
ASP HXT    H N N 153 
CYS N      N N N 154 
CYS CA     C N R 155 
CYS C      C N N 156 
CYS O      O N N 157 
CYS CB     C N N 158 
CYS SG     S N N 159 
CYS OXT    O N N 160 
CYS H      H N N 161 
CYS H2     H N N 162 
CYS HA     H N N 163 
CYS HB2    H N N 164 
CYS HB3    H N N 165 
CYS HG     H N N 166 
CYS HXT    H N N 167 
FMN N1     N N N 168 
FMN C2     C N N 169 
FMN O2     O N N 170 
FMN N3     N N N 171 
FMN C4     C N N 172 
FMN O4     O N N 173 
FMN C4A    C N N 174 
FMN N5     N N N 175 
FMN C5A    C Y N 176 
FMN C6     C Y N 177 
FMN C7     C Y N 178 
FMN C7M    C N N 179 
FMN C8     C Y N 180 
FMN C8M    C N N 181 
FMN C9     C Y N 182 
FMN C9A    C Y N 183 
FMN N10    N N N 184 
FMN C10    C N N 185 
FMN "C1'"  C N N 186 
FMN "C2'"  C N S 187 
FMN "O2'"  O N N 188 
FMN "C3'"  C N S 189 
FMN "O3'"  O N N 190 
FMN "C4'"  C N R 191 
FMN "O4'"  O N N 192 
FMN "C5'"  C N N 193 
FMN "O5'"  O N N 194 
FMN P      P N N 195 
FMN O1P    O N N 196 
FMN O2P    O N N 197 
FMN O3P    O N N 198 
FMN HN3    H N N 199 
FMN H6     H N N 200 
FMN HM71   H N N 201 
FMN HM72   H N N 202 
FMN HM73   H N N 203 
FMN HM81   H N N 204 
FMN HM82   H N N 205 
FMN HM83   H N N 206 
FMN H9     H N N 207 
FMN "H1'1" H N N 208 
FMN "H1'2" H N N 209 
FMN "H2'"  H N N 210 
FMN "HO2'" H N N 211 
FMN "H3'"  H N N 212 
FMN "HO3'" H N N 213 
FMN "H4'"  H N N 214 
FMN "HO4'" H N N 215 
FMN "H5'1" H N N 216 
FMN "H5'2" H N N 217 
FMN HOP2   H N N 218 
FMN HOP3   H N N 219 
GLN N      N N N 220 
GLN CA     C N S 221 
GLN C      C N N 222 
GLN O      O N N 223 
GLN CB     C N N 224 
GLN CG     C N N 225 
GLN CD     C N N 226 
GLN OE1    O N N 227 
GLN NE2    N N N 228 
GLN OXT    O N N 229 
GLN H      H N N 230 
GLN H2     H N N 231 
GLN HA     H N N 232 
GLN HB2    H N N 233 
GLN HB3    H N N 234 
GLN HG2    H N N 235 
GLN HG3    H N N 236 
GLN HE21   H N N 237 
GLN HE22   H N N 238 
GLN HXT    H N N 239 
GLU N      N N N 240 
GLU CA     C N S 241 
GLU C      C N N 242 
GLU O      O N N 243 
GLU CB     C N N 244 
GLU CG     C N N 245 
GLU CD     C N N 246 
GLU OE1    O N N 247 
GLU OE2    O N N 248 
GLU OXT    O N N 249 
GLU H      H N N 250 
GLU H2     H N N 251 
GLU HA     H N N 252 
GLU HB2    H N N 253 
GLU HB3    H N N 254 
GLU HG2    H N N 255 
GLU HG3    H N N 256 
GLU HE2    H N N 257 
GLU HXT    H N N 258 
GLY N      N N N 259 
GLY CA     C N N 260 
GLY C      C N N 261 
GLY O      O N N 262 
GLY OXT    O N N 263 
GLY H      H N N 264 
GLY H2     H N N 265 
GLY HA2    H N N 266 
GLY HA3    H N N 267 
GLY HXT    H N N 268 
HIS N      N N N 269 
HIS CA     C N S 270 
HIS C      C N N 271 
HIS O      O N N 272 
HIS CB     C N N 273 
HIS CG     C Y N 274 
HIS ND1    N Y N 275 
HIS CD2    C Y N 276 
HIS CE1    C Y N 277 
HIS NE2    N Y N 278 
HIS OXT    O N N 279 
HIS H      H N N 280 
HIS H2     H N N 281 
HIS HA     H N N 282 
HIS HB2    H N N 283 
HIS HB3    H N N 284 
HIS HD1    H N N 285 
HIS HD2    H N N 286 
HIS HE1    H N N 287 
HIS HE2    H N N 288 
HIS HXT    H N N 289 
HOH O      O N N 290 
HOH H1     H N N 291 
HOH H2     H N N 292 
ILE N      N N N 293 
ILE CA     C N S 294 
ILE C      C N N 295 
ILE O      O N N 296 
ILE CB     C N S 297 
ILE CG1    C N N 298 
ILE CG2    C N N 299 
ILE CD1    C N N 300 
ILE OXT    O N N 301 
ILE H      H N N 302 
ILE H2     H N N 303 
ILE HA     H N N 304 
ILE HB     H N N 305 
ILE HG12   H N N 306 
ILE HG13   H N N 307 
ILE HG21   H N N 308 
ILE HG22   H N N 309 
ILE HG23   H N N 310 
ILE HD11   H N N 311 
ILE HD12   H N N 312 
ILE HD13   H N N 313 
ILE HXT    H N N 314 
LEU N      N N N 315 
LEU CA     C N S 316 
LEU C      C N N 317 
LEU O      O N N 318 
LEU CB     C N N 319 
LEU CG     C N N 320 
LEU CD1    C N N 321 
LEU CD2    C N N 322 
LEU OXT    O N N 323 
LEU H      H N N 324 
LEU H2     H N N 325 
LEU HA     H N N 326 
LEU HB2    H N N 327 
LEU HB3    H N N 328 
LEU HG     H N N 329 
LEU HD11   H N N 330 
LEU HD12   H N N 331 
LEU HD13   H N N 332 
LEU HD21   H N N 333 
LEU HD22   H N N 334 
LEU HD23   H N N 335 
LEU HXT    H N N 336 
LYS N      N N N 337 
LYS CA     C N S 338 
LYS C      C N N 339 
LYS O      O N N 340 
LYS CB     C N N 341 
LYS CG     C N N 342 
LYS CD     C N N 343 
LYS CE     C N N 344 
LYS NZ     N N N 345 
LYS OXT    O N N 346 
LYS H      H N N 347 
LYS H2     H N N 348 
LYS HA     H N N 349 
LYS HB2    H N N 350 
LYS HB3    H N N 351 
LYS HG2    H N N 352 
LYS HG3    H N N 353 
LYS HD2    H N N 354 
LYS HD3    H N N 355 
LYS HE2    H N N 356 
LYS HE3    H N N 357 
LYS HZ1    H N N 358 
LYS HZ2    H N N 359 
LYS HZ3    H N N 360 
LYS HXT    H N N 361 
MET N      N N N 362 
MET CA     C N S 363 
MET C      C N N 364 
MET O      O N N 365 
MET CB     C N N 366 
MET CG     C N N 367 
MET SD     S N N 368 
MET CE     C N N 369 
MET OXT    O N N 370 
MET H      H N N 371 
MET H2     H N N 372 
MET HA     H N N 373 
MET HB2    H N N 374 
MET HB3    H N N 375 
MET HG2    H N N 376 
MET HG3    H N N 377 
MET HE1    H N N 378 
MET HE2    H N N 379 
MET HE3    H N N 380 
MET HXT    H N N 381 
PHE N      N N N 382 
PHE CA     C N S 383 
PHE C      C N N 384 
PHE O      O N N 385 
PHE CB     C N N 386 
PHE CG     C Y N 387 
PHE CD1    C Y N 388 
PHE CD2    C Y N 389 
PHE CE1    C Y N 390 
PHE CE2    C Y N 391 
PHE CZ     C Y N 392 
PHE OXT    O N N 393 
PHE H      H N N 394 
PHE H2     H N N 395 
PHE HA     H N N 396 
PHE HB2    H N N 397 
PHE HB3    H N N 398 
PHE HD1    H N N 399 
PHE HD2    H N N 400 
PHE HE1    H N N 401 
PHE HE2    H N N 402 
PHE HZ     H N N 403 
PHE HXT    H N N 404 
PRO N      N N N 405 
PRO CA     C N S 406 
PRO C      C N N 407 
PRO O      O N N 408 
PRO CB     C N N 409 
PRO CG     C N N 410 
PRO CD     C N N 411 
PRO OXT    O N N 412 
PRO H      H N N 413 
PRO HA     H N N 414 
PRO HB2    H N N 415 
PRO HB3    H N N 416 
PRO HG2    H N N 417 
PRO HG3    H N N 418 
PRO HD2    H N N 419 
PRO HD3    H N N 420 
PRO HXT    H N N 421 
SER N      N N N 422 
SER CA     C N S 423 
SER C      C N N 424 
SER O      O N N 425 
SER CB     C N N 426 
SER OG     O N N 427 
SER OXT    O N N 428 
SER H      H N N 429 
SER H2     H N N 430 
SER HA     H N N 431 
SER HB2    H N N 432 
SER HB3    H N N 433 
SER HG     H N N 434 
SER HXT    H N N 435 
THR N      N N N 436 
THR CA     C N S 437 
THR C      C N N 438 
THR O      O N N 439 
THR CB     C N R 440 
THR OG1    O N N 441 
THR CG2    C N N 442 
THR OXT    O N N 443 
THR H      H N N 444 
THR H2     H N N 445 
THR HA     H N N 446 
THR HB     H N N 447 
THR HG1    H N N 448 
THR HG21   H N N 449 
THR HG22   H N N 450 
THR HG23   H N N 451 
THR HXT    H N N 452 
TRP N      N N N 453 
TRP CA     C N S 454 
TRP C      C N N 455 
TRP O      O N N 456 
TRP CB     C N N 457 
TRP CG     C Y N 458 
TRP CD1    C Y N 459 
TRP CD2    C Y N 460 
TRP NE1    N Y N 461 
TRP CE2    C Y N 462 
TRP CE3    C Y N 463 
TRP CZ2    C Y N 464 
TRP CZ3    C Y N 465 
TRP CH2    C Y N 466 
TRP OXT    O N N 467 
TRP H      H N N 468 
TRP H2     H N N 469 
TRP HA     H N N 470 
TRP HB2    H N N 471 
TRP HB3    H N N 472 
TRP HD1    H N N 473 
TRP HE1    H N N 474 
TRP HE3    H N N 475 
TRP HZ2    H N N 476 
TRP HZ3    H N N 477 
TRP HH2    H N N 478 
TRP HXT    H N N 479 
TYR N      N N N 480 
TYR CA     C N S 481 
TYR C      C N N 482 
TYR O      O N N 483 
TYR CB     C N N 484 
TYR CG     C Y N 485 
TYR CD1    C Y N 486 
TYR CD2    C Y N 487 
TYR CE1    C Y N 488 
TYR CE2    C Y N 489 
TYR CZ     C Y N 490 
TYR OH     O N N 491 
TYR OXT    O N N 492 
TYR H      H N N 493 
TYR H2     H N N 494 
TYR HA     H N N 495 
TYR HB2    H N N 496 
TYR HB3    H N N 497 
TYR HD1    H N N 498 
TYR HD2    H N N 499 
TYR HE1    H N N 500 
TYR HE2    H N N 501 
TYR HH     H N N 502 
TYR HXT    H N N 503 
VAL N      N N N 504 
VAL CA     C N S 505 
VAL C      C N N 506 
VAL O      O N N 507 
VAL CB     C N N 508 
VAL CG1    C N N 509 
VAL CG2    C N N 510 
VAL OXT    O N N 511 
VAL H      H N N 512 
VAL H2     H N N 513 
VAL HA     H N N 514 
VAL HB     H N N 515 
VAL HG11   H N N 516 
VAL HG12   H N N 517 
VAL HG13   H N N 518 
VAL HG21   H N N 519 
VAL HG22   H N N 520 
VAL HG23   H N N 521 
VAL HXT    H N N 522 
# 
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 
5J8 OP3   "P2'"  doub N N 1   
5J8 OP2   "P2'"  sing N N 2   
5J8 OP1   "P2'"  sing N N 3   
5J8 "P2'" "O2'"  sing N N 4   
5J8 "O2'" "C2'"  sing N N 5   
5J8 "C2'" "C3'"  sing N N 6   
5J8 "C2'" "C1'"  sing N N 7   
5J8 OAC   PAA    doub N N 8   
5J8 C2    N1     sing Y N 9   
5J8 C2    N3     doub Y N 10  
5J8 N1    C6     doub Y N 11  
5J8 OAG   PAE    doub N N 12  
5J8 "C3'" "O3'"  sing N N 13  
5J8 "C3'" "C4'"  sing N N 14  
5J8 N3    C4     sing Y N 15  
5J8 C6    N6     sing N N 16  
5J8 C6    C5     sing Y N 17  
5J8 OBV   CBT    doub N N 18  
5J8 CBS   CBR    sing N N 19  
5J8 CBS   CBN    sing N N 20  
5J8 CBR   CBT    sing N N 21  
5J8 CBR   CBQ    doub N N 22  
5J8 C4    C5     doub Y N 23  
5J8 C4    N9     sing Y N 24  
5J8 CBN   CBO    sing N N 25  
5J8 C5    N7     sing Y N 26  
5J8 CBT   NBU    sing N N 27  
5J8 CBO   NBP    sing N N 28  
5J8 OBI   CBF    sing N N 29  
5J8 "O5'" PAE    sing N N 30  
5J8 "O5'" "C5'"  sing N N 31  
5J8 N9    "C1'"  sing N N 32  
5J8 N9    C8     sing Y N 33  
5J8 "C1'" "O4'"  sing N N 34  
5J8 N7    C8     doub Y N 35  
5J8 NBP   CBQ    sing N N 36  
5J8 NBP   CBM    sing N N 37  
5J8 PAE   OAD    sing N N 38  
5J8 PAE   OAF    sing N N 39  
5J8 PAA   OAD    sing N N 40  
5J8 PAA   OBL    sing N N 41  
5J8 PAA   OAB    sing N N 42  
5J8 CBF   CBM    sing N N 43  
5J8 CBF   CBE    sing N N 44  
5J8 "C4'" "C5'"  sing N N 45  
5J8 "C4'" "O4'"  sing N N 46  
5J8 OBL   CBK    sing N N 47  
5J8 CBM   OBG    sing N N 48  
5J8 CBE   OBJ    sing N N 49  
5J8 CBE   CBH    sing N N 50  
5J8 OBG   CBH    sing N N 51  
5J8 CBK   CBH    sing N N 52  
5J8 C8    H1     sing N N 53  
5J8 NBU   H2     sing N N 54  
5J8 NBU   H3     sing N N 55  
5J8 CBQ   H5     sing N N 56  
5J8 CBS   H7     sing N N 57  
5J8 CBS   H8     sing N N 58  
5J8 CBN   H9     sing N N 59  
5J8 CBO   H10    sing N N 60  
5J8 CBM   H11    sing N N 61  
5J8 CBF   H12    sing N N 62  
5J8 OBI   H13    sing N N 63  
5J8 CBE   H14    sing N N 64  
5J8 OBJ   H15    sing N N 65  
5J8 CBH   H16    sing N N 66  
5J8 CBK   H17    sing N N 67  
5J8 CBK   H18    sing N N 68  
5J8 OAB   H19    sing N N 69  
5J8 OAF   H20    sing N N 70  
5J8 "C5'" H21    sing N N 71  
5J8 "C5'" H22    sing N N 72  
5J8 "C4'" H23    sing N N 73  
5J8 "C3'" H24    sing N N 74  
5J8 "O3'" H25    sing N N 75  
5J8 "C2'" H26    sing N N 76  
5J8 OP1   H27    sing N N 77  
5J8 OP2   H28    sing N N 78  
5J8 "C1'" H29    sing N N 79  
5J8 C2    H30    sing N N 80  
5J8 N6    H31    sing N N 81  
5J8 N6    H32    sing N N 82  
5J8 CBN   H4     sing N N 83  
5J8 CBO   H6     sing N N 84  
ALA N     CA     sing N N 85  
ALA N     H      sing N N 86  
ALA N     H2     sing N N 87  
ALA CA    C      sing N N 88  
ALA CA    CB     sing N N 89  
ALA CA    HA     sing N N 90  
ALA C     O      doub N N 91  
ALA C     OXT    sing N N 92  
ALA CB    HB1    sing N N 93  
ALA CB    HB2    sing N N 94  
ALA CB    HB3    sing N N 95  
ALA OXT   HXT    sing N N 96  
ARG N     CA     sing N N 97  
ARG N     H      sing N N 98  
ARG N     H2     sing N N 99  
ARG CA    C      sing N N 100 
ARG CA    CB     sing N N 101 
ARG CA    HA     sing N N 102 
ARG C     O      doub N N 103 
ARG C     OXT    sing N N 104 
ARG CB    CG     sing N N 105 
ARG CB    HB2    sing N N 106 
ARG CB    HB3    sing N N 107 
ARG CG    CD     sing N N 108 
ARG CG    HG2    sing N N 109 
ARG CG    HG3    sing N N 110 
ARG CD    NE     sing N N 111 
ARG CD    HD2    sing N N 112 
ARG CD    HD3    sing N N 113 
ARG NE    CZ     sing N N 114 
ARG NE    HE     sing N N 115 
ARG CZ    NH1    sing N N 116 
ARG CZ    NH2    doub N N 117 
ARG NH1   HH11   sing N N 118 
ARG NH1   HH12   sing N N 119 
ARG NH2   HH21   sing N N 120 
ARG NH2   HH22   sing N N 121 
ARG OXT   HXT    sing N N 122 
ASN N     CA     sing N N 123 
ASN N     H      sing N N 124 
ASN N     H2     sing N N 125 
ASN CA    C      sing N N 126 
ASN CA    CB     sing N N 127 
ASN CA    HA     sing N N 128 
ASN C     O      doub N N 129 
ASN C     OXT    sing N N 130 
ASN CB    CG     sing N N 131 
ASN CB    HB2    sing N N 132 
ASN CB    HB3    sing N N 133 
ASN CG    OD1    doub N N 134 
ASN CG    ND2    sing N N 135 
ASN ND2   HD21   sing N N 136 
ASN ND2   HD22   sing N N 137 
ASN OXT   HXT    sing N N 138 
ASP N     CA     sing N N 139 
ASP N     H      sing N N 140 
ASP N     H2     sing N N 141 
ASP CA    C      sing N N 142 
ASP CA    CB     sing N N 143 
ASP CA    HA     sing N N 144 
ASP C     O      doub N N 145 
ASP C     OXT    sing N N 146 
ASP CB    CG     sing N N 147 
ASP CB    HB2    sing N N 148 
ASP CB    HB3    sing N N 149 
ASP CG    OD1    doub N N 150 
ASP CG    OD2    sing N N 151 
ASP OD2   HD2    sing N N 152 
ASP OXT   HXT    sing N N 153 
CYS N     CA     sing N N 154 
CYS N     H      sing N N 155 
CYS N     H2     sing N N 156 
CYS CA    C      sing N N 157 
CYS CA    CB     sing N N 158 
CYS CA    HA     sing N N 159 
CYS C     O      doub N N 160 
CYS C     OXT    sing N N 161 
CYS CB    SG     sing N N 162 
CYS CB    HB2    sing N N 163 
CYS CB    HB3    sing N N 164 
CYS SG    HG     sing N N 165 
CYS OXT   HXT    sing N N 166 
FMN N1    C2     sing N N 167 
FMN N1    C10    doub N N 168 
FMN C2    O2     doub N N 169 
FMN C2    N3     sing N N 170 
FMN N3    C4     sing N N 171 
FMN N3    HN3    sing N N 172 
FMN C4    O4     doub N N 173 
FMN C4    C4A    sing N N 174 
FMN C4A   N5     doub N N 175 
FMN C4A   C10    sing N N 176 
FMN N5    C5A    sing N N 177 
FMN C5A   C6     doub Y N 178 
FMN C5A   C9A    sing Y N 179 
FMN C6    C7     sing Y N 180 
FMN C6    H6     sing N N 181 
FMN C7    C7M    sing N N 182 
FMN C7    C8     doub Y N 183 
FMN C7M   HM71   sing N N 184 
FMN C7M   HM72   sing N N 185 
FMN C7M   HM73   sing N N 186 
FMN C8    C8M    sing N N 187 
FMN C8    C9     sing Y N 188 
FMN C8M   HM81   sing N N 189 
FMN C8M   HM82   sing N N 190 
FMN C8M   HM83   sing N N 191 
FMN C9    C9A    doub Y N 192 
FMN C9    H9     sing N N 193 
FMN C9A   N10    sing N N 194 
FMN N10   C10    sing N N 195 
FMN N10   "C1'"  sing N N 196 
FMN "C1'" "C2'"  sing N N 197 
FMN "C1'" "H1'1" sing N N 198 
FMN "C1'" "H1'2" sing N N 199 
FMN "C2'" "O2'"  sing N N 200 
FMN "C2'" "C3'"  sing N N 201 
FMN "C2'" "H2'"  sing N N 202 
FMN "O2'" "HO2'" sing N N 203 
FMN "C3'" "O3'"  sing N N 204 
FMN "C3'" "C4'"  sing N N 205 
FMN "C3'" "H3'"  sing N N 206 
FMN "O3'" "HO3'" sing N N 207 
FMN "C4'" "O4'"  sing N N 208 
FMN "C4'" "C5'"  sing N N 209 
FMN "C4'" "H4'"  sing N N 210 
FMN "O4'" "HO4'" sing N N 211 
FMN "C5'" "O5'"  sing N N 212 
FMN "C5'" "H5'1" sing N N 213 
FMN "C5'" "H5'2" sing N N 214 
FMN "O5'" P      sing N N 215 
FMN P     O1P    doub N N 216 
FMN P     O2P    sing N N 217 
FMN P     O3P    sing N N 218 
FMN O2P   HOP2   sing N N 219 
FMN O3P   HOP3   sing N N 220 
GLN N     CA     sing N N 221 
GLN N     H      sing N N 222 
GLN N     H2     sing N N 223 
GLN CA    C      sing N N 224 
GLN CA    CB     sing N N 225 
GLN CA    HA     sing N N 226 
GLN C     O      doub N N 227 
GLN C     OXT    sing N N 228 
GLN CB    CG     sing N N 229 
GLN CB    HB2    sing N N 230 
GLN CB    HB3    sing N N 231 
GLN CG    CD     sing N N 232 
GLN CG    HG2    sing N N 233 
GLN CG    HG3    sing N N 234 
GLN CD    OE1    doub N N 235 
GLN CD    NE2    sing N N 236 
GLN NE2   HE21   sing N N 237 
GLN NE2   HE22   sing N N 238 
GLN OXT   HXT    sing N N 239 
GLU N     CA     sing N N 240 
GLU N     H      sing N N 241 
GLU N     H2     sing N N 242 
GLU CA    C      sing N N 243 
GLU CA    CB     sing N N 244 
GLU CA    HA     sing N N 245 
GLU C     O      doub N N 246 
GLU C     OXT    sing N N 247 
GLU CB    CG     sing N N 248 
GLU CB    HB2    sing N N 249 
GLU CB    HB3    sing N N 250 
GLU CG    CD     sing N N 251 
GLU CG    HG2    sing N N 252 
GLU CG    HG3    sing N N 253 
GLU CD    OE1    doub N N 254 
GLU CD    OE2    sing N N 255 
GLU OE2   HE2    sing N N 256 
GLU OXT   HXT    sing N N 257 
GLY N     CA     sing N N 258 
GLY N     H      sing N N 259 
GLY N     H2     sing N N 260 
GLY CA    C      sing N N 261 
GLY CA    HA2    sing N N 262 
GLY CA    HA3    sing N N 263 
GLY C     O      doub N N 264 
GLY C     OXT    sing N N 265 
GLY OXT   HXT    sing N N 266 
HIS N     CA     sing N N 267 
HIS N     H      sing N N 268 
HIS N     H2     sing N N 269 
HIS CA    C      sing N N 270 
HIS CA    CB     sing N N 271 
HIS CA    HA     sing N N 272 
HIS C     O      doub N N 273 
HIS C     OXT    sing N N 274 
HIS CB    CG     sing N N 275 
HIS CB    HB2    sing N N 276 
HIS CB    HB3    sing N N 277 
HIS CG    ND1    sing Y N 278 
HIS CG    CD2    doub Y N 279 
HIS ND1   CE1    doub Y N 280 
HIS ND1   HD1    sing N N 281 
HIS CD2   NE2    sing Y N 282 
HIS CD2   HD2    sing N N 283 
HIS CE1   NE2    sing Y N 284 
HIS CE1   HE1    sing N N 285 
HIS NE2   HE2    sing N N 286 
HIS OXT   HXT    sing N N 287 
HOH O     H1     sing N N 288 
HOH O     H2     sing N N 289 
ILE N     CA     sing N N 290 
ILE N     H      sing N N 291 
ILE N     H2     sing N N 292 
ILE CA    C      sing N N 293 
ILE CA    CB     sing N N 294 
ILE CA    HA     sing N N 295 
ILE C     O      doub N N 296 
ILE C     OXT    sing N N 297 
ILE CB    CG1    sing N N 298 
ILE CB    CG2    sing N N 299 
ILE CB    HB     sing N N 300 
ILE CG1   CD1    sing N N 301 
ILE CG1   HG12   sing N N 302 
ILE CG1   HG13   sing N N 303 
ILE CG2   HG21   sing N N 304 
ILE CG2   HG22   sing N N 305 
ILE CG2   HG23   sing N N 306 
ILE CD1   HD11   sing N N 307 
ILE CD1   HD12   sing N N 308 
ILE CD1   HD13   sing N N 309 
ILE OXT   HXT    sing N N 310 
LEU N     CA     sing N N 311 
LEU N     H      sing N N 312 
LEU N     H2     sing N N 313 
LEU CA    C      sing N N 314 
LEU CA    CB     sing N N 315 
LEU CA    HA     sing N N 316 
LEU C     O      doub N N 317 
LEU C     OXT    sing N N 318 
LEU CB    CG     sing N N 319 
LEU CB    HB2    sing N N 320 
LEU CB    HB3    sing N N 321 
LEU CG    CD1    sing N N 322 
LEU CG    CD2    sing N N 323 
LEU CG    HG     sing N N 324 
LEU CD1   HD11   sing N N 325 
LEU CD1   HD12   sing N N 326 
LEU CD1   HD13   sing N N 327 
LEU CD2   HD21   sing N N 328 
LEU CD2   HD22   sing N N 329 
LEU CD2   HD23   sing N N 330 
LEU OXT   HXT    sing N N 331 
LYS N     CA     sing N N 332 
LYS N     H      sing N N 333 
LYS N     H2     sing N N 334 
LYS CA    C      sing N N 335 
LYS CA    CB     sing N N 336 
LYS CA    HA     sing N N 337 
LYS C     O      doub N N 338 
LYS C     OXT    sing N N 339 
LYS CB    CG     sing N N 340 
LYS CB    HB2    sing N N 341 
LYS CB    HB3    sing N N 342 
LYS CG    CD     sing N N 343 
LYS CG    HG2    sing N N 344 
LYS CG    HG3    sing N N 345 
LYS CD    CE     sing N N 346 
LYS CD    HD2    sing N N 347 
LYS CD    HD3    sing N N 348 
LYS CE    NZ     sing N N 349 
LYS CE    HE2    sing N N 350 
LYS CE    HE3    sing N N 351 
LYS NZ    HZ1    sing N N 352 
LYS NZ    HZ2    sing N N 353 
LYS NZ    HZ3    sing N N 354 
LYS OXT   HXT    sing N N 355 
MET N     CA     sing N N 356 
MET N     H      sing N N 357 
MET N     H2     sing N N 358 
MET CA    C      sing N N 359 
MET CA    CB     sing N N 360 
MET CA    HA     sing N N 361 
MET C     O      doub N N 362 
MET C     OXT    sing N N 363 
MET CB    CG     sing N N 364 
MET CB    HB2    sing N N 365 
MET CB    HB3    sing N N 366 
MET CG    SD     sing N N 367 
MET CG    HG2    sing N N 368 
MET CG    HG3    sing N N 369 
MET SD    CE     sing N N 370 
MET CE    HE1    sing N N 371 
MET CE    HE2    sing N N 372 
MET CE    HE3    sing N N 373 
MET OXT   HXT    sing N N 374 
PHE N     CA     sing N N 375 
PHE N     H      sing N N 376 
PHE N     H2     sing N N 377 
PHE CA    C      sing N N 378 
PHE CA    CB     sing N N 379 
PHE CA    HA     sing N N 380 
PHE C     O      doub N N 381 
PHE C     OXT    sing N N 382 
PHE CB    CG     sing N N 383 
PHE CB    HB2    sing N N 384 
PHE CB    HB3    sing N N 385 
PHE CG    CD1    doub Y N 386 
PHE CG    CD2    sing Y N 387 
PHE CD1   CE1    sing Y N 388 
PHE CD1   HD1    sing N N 389 
PHE CD2   CE2    doub Y N 390 
PHE CD2   HD2    sing N N 391 
PHE CE1   CZ     doub Y N 392 
PHE CE1   HE1    sing N N 393 
PHE CE2   CZ     sing Y N 394 
PHE CE2   HE2    sing N N 395 
PHE CZ    HZ     sing N N 396 
PHE OXT   HXT    sing N N 397 
PRO N     CA     sing N N 398 
PRO N     CD     sing N N 399 
PRO N     H      sing N N 400 
PRO CA    C      sing N N 401 
PRO CA    CB     sing N N 402 
PRO CA    HA     sing N N 403 
PRO C     O      doub N N 404 
PRO C     OXT    sing N N 405 
PRO CB    CG     sing N N 406 
PRO CB    HB2    sing N N 407 
PRO CB    HB3    sing N N 408 
PRO CG    CD     sing N N 409 
PRO CG    HG2    sing N N 410 
PRO CG    HG3    sing N N 411 
PRO CD    HD2    sing N N 412 
PRO CD    HD3    sing N N 413 
PRO OXT   HXT    sing N N 414 
SER N     CA     sing N N 415 
SER N     H      sing N N 416 
SER N     H2     sing N N 417 
SER CA    C      sing N N 418 
SER CA    CB     sing N N 419 
SER CA    HA     sing N N 420 
SER C     O      doub N N 421 
SER C     OXT    sing N N 422 
SER CB    OG     sing N N 423 
SER CB    HB2    sing N N 424 
SER CB    HB3    sing N N 425 
SER OG    HG     sing N N 426 
SER OXT   HXT    sing N N 427 
THR N     CA     sing N N 428 
THR N     H      sing N N 429 
THR N     H2     sing N N 430 
THR CA    C      sing N N 431 
THR CA    CB     sing N N 432 
THR CA    HA     sing N N 433 
THR C     O      doub N N 434 
THR C     OXT    sing N N 435 
THR CB    OG1    sing N N 436 
THR CB    CG2    sing N N 437 
THR CB    HB     sing N N 438 
THR OG1   HG1    sing N N 439 
THR CG2   HG21   sing N N 440 
THR CG2   HG22   sing N N 441 
THR CG2   HG23   sing N N 442 
THR OXT   HXT    sing N N 443 
TRP N     CA     sing N N 444 
TRP N     H      sing N N 445 
TRP N     H2     sing N N 446 
TRP CA    C      sing N N 447 
TRP CA    CB     sing N N 448 
TRP CA    HA     sing N N 449 
TRP C     O      doub N N 450 
TRP C     OXT    sing N N 451 
TRP CB    CG     sing N N 452 
TRP CB    HB2    sing N N 453 
TRP CB    HB3    sing N N 454 
TRP CG    CD1    doub Y N 455 
TRP CG    CD2    sing Y N 456 
TRP CD1   NE1    sing Y N 457 
TRP CD1   HD1    sing N N 458 
TRP CD2   CE2    doub Y N 459 
TRP CD2   CE3    sing Y N 460 
TRP NE1   CE2    sing Y N 461 
TRP NE1   HE1    sing N N 462 
TRP CE2   CZ2    sing Y N 463 
TRP CE3   CZ3    doub Y N 464 
TRP CE3   HE3    sing N N 465 
TRP CZ2   CH2    doub Y N 466 
TRP CZ2   HZ2    sing N N 467 
TRP CZ3   CH2    sing Y N 468 
TRP CZ3   HZ3    sing N N 469 
TRP CH2   HH2    sing N N 470 
TRP OXT   HXT    sing N N 471 
TYR N     CA     sing N N 472 
TYR N     H      sing N N 473 
TYR N     H2     sing N N 474 
TYR CA    C      sing N N 475 
TYR CA    CB     sing N N 476 
TYR CA    HA     sing N N 477 
TYR C     O      doub N N 478 
TYR C     OXT    sing N N 479 
TYR CB    CG     sing N N 480 
TYR CB    HB2    sing N N 481 
TYR CB    HB3    sing N N 482 
TYR CG    CD1    doub Y N 483 
TYR CG    CD2    sing Y N 484 
TYR CD1   CE1    sing Y N 485 
TYR CD1   HD1    sing N N 486 
TYR CD2   CE2    doub Y N 487 
TYR CD2   HD2    sing N N 488 
TYR CE1   CZ     doub Y N 489 
TYR CE1   HE1    sing N N 490 
TYR CE2   CZ     sing Y N 491 
TYR CE2   HE2    sing N N 492 
TYR CZ    OH     sing N N 493 
TYR OH    HH     sing N N 494 
TYR OXT   HXT    sing N N 495 
VAL N     CA     sing N N 496 
VAL N     H      sing N N 497 
VAL N     H2     sing N N 498 
VAL CA    C      sing N N 499 
VAL CA    CB     sing N N 500 
VAL CA    HA     sing N N 501 
VAL C     O      doub N N 502 
VAL C     OXT    sing N N 503 
VAL CB    CG1    sing N N 504 
VAL CB    CG2    sing N N 505 
VAL CB    HB     sing N N 506 
VAL CG1   HG11   sing N N 507 
VAL CG1   HG12   sing N N 508 
VAL CG1   HG13   sing N N 509 
VAL CG2   HG21   sing N N 510 
VAL CG2   HG22   sing N N 511 
VAL CG2   HG23   sing N N 512 
VAL OXT   HXT    sing N N 513 
# 
_pdbx_audit_support.funding_organization   'Austrian Science Fund' 
_pdbx_audit_support.country                Austria 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   2hs6 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8QNM 
_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]   0.019920 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.003649 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011117 
_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]   0.011231 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
P 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N     . ASN A 1 19  ? -0.056 -20.664 8.256   1.00 46.77 ? 10  ASN A N     1 
ATOM   2    C CA    . ASN A 1 19  ? 1.239  -20.132 7.845   1.00 48.12 ? 10  ASN A CA    1 
ATOM   3    C C     . ASN A 1 19  ? 1.390  -18.686 8.299   1.00 48.47 ? 10  ASN A C     1 
ATOM   4    O O     . ASN A 1 19  ? 0.736  -17.792 7.762   1.00 49.24 ? 10  ASN A O     1 
ATOM   5    C CB    . ASN A 1 19  ? 1.407  -20.232 6.327   1.00 52.67 ? 10  ASN A CB    1 
ATOM   6    C CG    . ASN A 1 19  ? 2.854  -20.084 5.885   1.00 50.49 ? 10  ASN A CG    1 
ATOM   7    O OD1   . ASN A 1 19  ? 3.684  -19.526 6.603   1.00 49.84 ? 10  ASN A OD1   1 
ATOM   8    N ND2   . ASN A 1 19  ? 3.160  -20.585 4.695   1.00 50.30 ? 10  ASN A ND2   1 
ATOM   9    N N     . PRO A 1 20  ? 2.259  -18.456 9.289   1.00 49.63 ? 11  PRO A N     1 
ATOM   10   C CA    . PRO A 1 20  ? 2.417  -17.092 9.818   1.00 46.99 ? 11  PRO A CA    1 
ATOM   11   C C     . PRO A 1 20  ? 3.056  -16.133 8.832   1.00 41.34 ? 11  PRO A C     1 
ATOM   12   O O     . PRO A 1 20  ? 2.899  -14.916 8.993   1.00 42.64 ? 11  PRO A O     1 
ATOM   13   C CB    . PRO A 1 20  ? 3.301  -17.295 11.055  1.00 41.69 ? 11  PRO A CB    1 
ATOM   14   C CG    . PRO A 1 20  ? 4.076  -18.532 10.756  1.00 46.72 ? 11  PRO A CG    1 
ATOM   15   C CD    . PRO A 1 20  ? 3.180  -19.413 9.926   1.00 43.22 ? 11  PRO A CD    1 
ATOM   16   N N     . LEU A 1 21  ? 3.763  -16.637 7.818   1.00 44.13 ? 12  LEU A N     1 
ATOM   17   C CA    . LEU A 1 21  ? 4.359  -15.778 6.802   1.00 42.92 ? 12  LEU A CA    1 
ATOM   18   C C     . LEU A 1 21  ? 3.321  -15.038 5.971   1.00 43.66 ? 12  LEU A C     1 
ATOM   19   O O     . LEU A 1 21  ? 3.681  -14.086 5.270   1.00 41.19 ? 12  LEU A O     1 
ATOM   20   C CB    . LEU A 1 21  ? 5.255  -16.601 5.873   1.00 38.21 ? 12  LEU A CB    1 
ATOM   21   C CG    . LEU A 1 21  ? 6.686  -16.863 6.346   1.00 42.05 ? 12  LEU A CG    1 
ATOM   22   C CD1   . LEU A 1 21  ? 7.455  -17.676 5.314   1.00 31.28 ? 12  LEU A CD1   1 
ATOM   23   C CD2   . LEU A 1 21  ? 7.402  -15.557 6.652   1.00 32.79 ? 12  LEU A CD2   1 
ATOM   24   N N     . PHE A 1 22  ? 2.052  -15.445 6.029   1.00 42.09 ? 13  PHE A N     1 
ATOM   25   C CA    . PHE A 1 22  ? 1.008  -14.839 5.212   1.00 47.17 ? 13  PHE A CA    1 
ATOM   26   C C     . PHE A 1 22  ? -0.070 -14.166 6.054   1.00 49.23 ? 13  PHE A C     1 
ATOM   27   O O     . PHE A 1 22  ? -1.179 -13.930 5.564   1.00 53.81 ? 13  PHE A O     1 
ATOM   28   C CB    . PHE A 1 22  ? 0.399  -15.883 4.277   1.00 44.72 ? 13  PHE A CB    1 
ATOM   29   C CG    . PHE A 1 22  ? 1.253  -16.172 3.080   1.00 47.55 ? 13  PHE A CG    1 
ATOM   30   C CD1   . PHE A 1 22  ? 2.290  -17.086 3.158   1.00 48.46 ? 13  PHE A CD1   1 
ATOM   31   C CD2   . PHE A 1 22  ? 1.041  -15.505 1.886   1.00 40.70 ? 13  PHE A CD2   1 
ATOM   32   C CE1   . PHE A 1 22  ? 3.089  -17.343 2.062   1.00 44.64 ? 13  PHE A CE1   1 
ATOM   33   C CE2   . PHE A 1 22  ? 1.835  -15.758 0.786   1.00 49.14 ? 13  PHE A CE2   1 
ATOM   34   C CZ    . PHE A 1 22  ? 2.863  -16.677 0.876   1.00 44.47 ? 13  PHE A CZ    1 
ATOM   35   N N     . SER A 1 23  ? 0.233  -13.855 7.307   1.00 45.22 ? 14  SER A N     1 
ATOM   36   C CA    . SER A 1 23  ? -0.650 -13.006 8.082   1.00 46.80 ? 14  SER A CA    1 
ATOM   37   C C     . SER A 1 23  ? -0.342 -11.540 7.784   1.00 45.87 ? 14  SER A C     1 
ATOM   38   O O     . SER A 1 23  ? 0.810  -11.183 7.522   1.00 42.18 ? 14  SER A O     1 
ATOM   39   C CB    . SER A 1 23  ? -0.487 -13.280 9.573   1.00 42.16 ? 14  SER A CB    1 
ATOM   40   O OG    . SER A 1 23  ? 0.714  -12.716 10.064  1.00 45.14 ? 14  SER A OG    1 
ATOM   41   N N     . PRO A 1 24  ? -1.355 -10.674 7.805   1.00 48.82 ? 15  PRO A N     1 
ATOM   42   C CA    . PRO A 1 24  ? -1.120 -9.263  7.474   1.00 43.95 ? 15  PRO A CA    1 
ATOM   43   C C     . PRO A 1 24  ? -0.187 -8.601  8.478   1.00 46.35 ? 15  PRO A C     1 
ATOM   44   O O     . PRO A 1 24  ? -0.164 -8.943  9.662   1.00 46.46 ? 15  PRO A O     1 
ATOM   45   C CB    . PRO A 1 24  ? -2.523 -8.643  7.524   1.00 46.25 ? 15  PRO A CB    1 
ATOM   46   C CG    . PRO A 1 24  ? -3.473 -9.796  7.472   1.00 53.10 ? 15  PRO A CG    1 
ATOM   47   C CD    . PRO A 1 24  ? -2.769 -10.947 8.109   1.00 48.55 ? 15  PRO A CD    1 
ATOM   48   N N     . TYR A 1 25  ? 0.594  -7.642  7.986   1.00 41.76 ? 16  TYR A N     1 
ATOM   49   C CA    . TYR A 1 25  ? 1.467  -6.847  8.838   1.00 39.33 ? 16  TYR A CA    1 
ATOM   50   C C     . TYR A 1 25  ? 1.514  -5.422  8.314   1.00 44.37 ? 16  TYR A C     1 
ATOM   51   O O     . TYR A 1 25  ? 1.662  -5.205  7.108   1.00 40.25 ? 16  TYR A O     1 
ATOM   52   C CB    . TYR A 1 25  ? 2.887  -7.423  8.904   1.00 39.47 ? 16  TYR A CB    1 
ATOM   53   C CG    . TYR A 1 25  ? 3.780  -6.661  9.856   1.00 40.31 ? 16  TYR A CG    1 
ATOM   54   C CD1   . TYR A 1 25  ? 3.692  -6.861  11.227  1.00 40.45 ? 16  TYR A CD1   1 
ATOM   55   C CD2   . TYR A 1 25  ? 4.694  -5.726  9.387   1.00 37.75 ? 16  TYR A CD2   1 
ATOM   56   C CE1   . TYR A 1 25  ? 4.499  -6.160  12.107  1.00 36.55 ? 16  TYR A CE1   1 
ATOM   57   C CE2   . TYR A 1 25  ? 5.506  -5.019  10.257  1.00 39.89 ? 16  TYR A CE2   1 
ATOM   58   C CZ    . TYR A 1 25  ? 5.403  -5.242  11.618  1.00 40.98 ? 16  TYR A CZ    1 
ATOM   59   O OH    . TYR A 1 25  ? 6.203  -4.544  12.493  1.00 35.88 ? 16  TYR A OH    1 
ATOM   60   N N     . LYS A 1 26  ? 1.397  -4.459  9.225   1.00 43.02 ? 17  LYS A N     1 
ATOM   61   C CA    . LYS A 1 26  ? 1.422  -3.041  8.886   1.00 46.23 ? 17  LYS A CA    1 
ATOM   62   C C     . LYS A 1 26  ? 2.826  -2.507  9.147   1.00 45.69 ? 17  LYS A C     1 
ATOM   63   O O     . LYS A 1 26  ? 3.276  -2.461  10.295  1.00 42.87 ? 17  LYS A O     1 
ATOM   64   C CB    . LYS A 1 26  ? 0.379  -2.276  9.699   1.00 51.27 ? 17  LYS A CB    1 
ATOM   65   C CG    . LYS A 1 26  ? 0.572  -0.771  9.711   1.00 54.49 ? 17  LYS A CG    1 
ATOM   66   C CD    . LYS A 1 26  ? -0.707 -0.059  10.115  1.00 56.64 ? 17  LYS A CD    1 
ATOM   67   C CE    . LYS A 1 26  ? -0.881 1.239   9.347   1.00 58.62 ? 17  LYS A CE    1 
ATOM   68   N NZ    . LYS A 1 26  ? -0.621 2.422   10.214  1.00 69.53 ? 17  LYS A NZ    1 
ATOM   69   N N     . MET A 1 27  ? 3.519  -2.111  8.081   1.00 46.75 ? 18  MET A N     1 
ATOM   70   C CA    . MET A 1 27  ? 4.864  -1.550  8.172   1.00 48.78 ? 18  MET A CA    1 
ATOM   71   C C     . MET A 1 27  ? 4.791  -0.093  7.732   1.00 47.80 ? 18  MET A C     1 
ATOM   72   O O     . MET A 1 27  ? 4.549  0.197   6.555   1.00 41.68 ? 18  MET A O     1 
ATOM   73   C CB    . MET A 1 27  ? 5.850  -2.344  7.318   1.00 45.67 ? 18  MET A CB    1 
ATOM   74   C CG    . MET A 1 27  ? 6.995  -1.522  6.753   1.00 47.99 ? 18  MET A CG    1 
ATOM   75   S SD    . MET A 1 27  ? 8.006  -2.478  5.617   1.00 52.02 ? 18  MET A SD    1 
ATOM   76   C CE    . MET A 1 27  ? 7.809  -1.515  4.118   1.00 34.11 ? 18  MET A CE    1 
ATOM   77   N N     . GLY A 1 28  ? 4.998  0.818   8.677   1.00 49.54 ? 19  GLY A N     1 
ATOM   78   C CA    . GLY A 1 28  ? 4.811  2.227   8.377   1.00 49.15 ? 19  GLY A CA    1 
ATOM   79   C C     . GLY A 1 28  ? 3.352  2.496   8.070   1.00 53.33 ? 19  GLY A C     1 
ATOM   80   O O     . GLY A 1 28  ? 2.452  2.083   8.810   1.00 49.83 ? 19  GLY A O     1 
ATOM   81   N N     . LYS A 1 29  ? 3.106  3.190   6.963   1.00 49.93 ? 20  LYS A N     1 
ATOM   82   C CA    . LYS A 1 29  ? 1.755  3.427   6.479   1.00 56.00 ? 20  LYS A CA    1 
ATOM   83   C C     . LYS A 1 29  ? 1.312  2.390   5.455   1.00 48.57 ? 20  LYS A C     1 
ATOM   84   O O     . LYS A 1 29  ? 0.255  2.557   4.839   1.00 54.99 ? 20  LYS A O     1 
ATOM   85   C CB    . LYS A 1 29  ? 1.649  4.831   5.877   1.00 55.29 ? 20  LYS A CB    1 
ATOM   86   N N     . PHE A 1 30  ? 2.091  1.328   5.263   1.00 48.25 ? 21  PHE A N     1 
ATOM   87   C CA    . PHE A 1 30  ? 1.818  0.313   4.255   1.00 47.47 ? 21  PHE A CA    1 
ATOM   88   C C     . PHE A 1 30  ? 1.308  -0.955  4.924   1.00 44.48 ? 21  PHE A C     1 
ATOM   89   O O     . PHE A 1 30  ? 1.950  -1.481  5.839   1.00 43.87 ? 21  PHE A O     1 
ATOM   90   C CB    . PHE A 1 30  ? 3.072  0.004   3.434   1.00 42.81 ? 21  PHE A CB    1 
ATOM   91   C CG    . PHE A 1 30  ? 3.844  1.225   3.015   1.00 46.20 ? 21  PHE A CG    1 
ATOM   92   C CD1   . PHE A 1 30  ? 3.462  1.956   1.901   1.00 43.71 ? 21  PHE A CD1   1 
ATOM   93   C CD2   . PHE A 1 30  ? 4.959  1.636   3.729   1.00 45.79 ? 21  PHE A CD2   1 
ATOM   94   C CE1   . PHE A 1 30  ? 4.175  3.077   1.511   1.00 41.34 ? 21  PHE A CE1   1 
ATOM   95   C CE2   . PHE A 1 30  ? 5.674  2.755   3.346   1.00 42.51 ? 21  PHE A CE2   1 
ATOM   96   C CZ    . PHE A 1 30  ? 5.283  3.477   2.236   1.00 38.44 ? 21  PHE A CZ    1 
ATOM   97   N N     . ASN A 1 31  ? 0.159  -1.444  4.464   1.00 45.90 ? 22  ASN A N     1 
ATOM   98   C CA    . ASN A 1 31  ? -0.422 -2.691  4.950   1.00 47.89 ? 22  ASN A CA    1 
ATOM   99   C C     . ASN A 1 31  ? -0.015 -3.808  3.996   1.00 43.63 ? 22  ASN A C     1 
ATOM   100  O O     . ASN A 1 31  ? -0.447 -3.834  2.840   1.00 46.09 ? 22  ASN A O     1 
ATOM   101  C CB    . ASN A 1 31  ? -1.941 -2.581  5.058   1.00 44.12 ? 22  ASN A CB    1 
ATOM   102  C CG    . ASN A 1 31  ? -2.379 -1.679  6.195   1.00 53.29 ? 22  ASN A CG    1 
ATOM   103  O OD1   . ASN A 1 31  ? -2.428 -2.100  7.351   1.00 55.34 ? 22  ASN A OD1   1 
ATOM   104  N ND2   . ASN A 1 31  ? -2.695 -0.431  5.872   1.00 42.05 ? 22  ASN A ND2   1 
ATOM   105  N N     . LEU A 1 32  ? 0.820  -4.723  4.479   1.00 41.88 ? 23  LEU A N     1 
ATOM   106  C CA    . LEU A 1 32  ? 1.332  -5.808  3.657   1.00 43.86 ? 23  LEU A CA    1 
ATOM   107  C C     . LEU A 1 32  ? 0.466  -7.050  3.817   1.00 44.03 ? 23  LEU A C     1 
ATOM   108  O O     . LEU A 1 32  ? 0.011  -7.369  4.920   1.00 42.03 ? 23  LEU A O     1 
ATOM   109  C CB    . LEU A 1 32  ? 2.784  -6.120  4.026   1.00 42.64 ? 23  LEU A CB    1 
ATOM   110  C CG    . LEU A 1 32  ? 3.768  -4.949  3.932   1.00 38.37 ? 23  LEU A CG    1 
ATOM   111  C CD1   . LEU A 1 32  ? 5.089  -5.285  4.614   1.00 30.78 ? 23  LEU A CD1   1 
ATOM   112  C CD2   . LEU A 1 32  ? 4.000  -4.550  2.480   1.00 36.71 ? 23  LEU A CD2   1 
ATOM   113  N N     . SER A 1 33  ? 0.238  -7.748  2.702   1.00 41.04 ? 24  SER A N     1 
ATOM   114  C CA    . SER A 1 33  ? -0.564 -8.966  2.730   1.00 40.90 ? 24  SER A CA    1 
ATOM   115  C C     . SER A 1 33  ? 0.223  -10.157 3.261   1.00 42.65 ? 24  SER A C     1 
ATOM   116  O O     . SER A 1 33  ? -0.371 -11.082 3.826   1.00 47.47 ? 24  SER A O     1 
ATOM   117  C CB    . SER A 1 33  ? -1.095 -9.277  1.330   1.00 44.49 ? 24  SER A CB    1 
ATOM   118  O OG    . SER A 1 33  ? -0.064 -9.180  0.363   1.00 47.68 ? 24  SER A OG    1 
ATOM   119  N N     . HIS A 1 34  ? 1.543  -10.154 3.092   1.00 36.55 ? 25  HIS A N     1 
ATOM   120  C CA    . HIS A 1 34  ? 2.382  -11.241 3.572   1.00 38.83 ? 25  HIS A CA    1 
ATOM   121  C C     . HIS A 1 34  ? 3.715  -10.663 4.020   1.00 37.74 ? 25  HIS A C     1 
ATOM   122  O O     . HIS A 1 34  ? 3.989  -9.473  3.853   1.00 35.26 ? 25  HIS A O     1 
ATOM   123  C CB    . HIS A 1 34  ? 2.577  -12.316 2.497   1.00 34.00 ? 25  HIS A CB    1 
ATOM   124  C CG    . HIS A 1 34  ? 3.189  -11.801 1.233   1.00 40.52 ? 25  HIS A CG    1 
ATOM   125  N ND1   . HIS A 1 34  ? 4.548  -11.622 1.083   1.00 36.94 ? 25  HIS A ND1   1 
ATOM   126  C CD2   . HIS A 1 34  ? 2.628  -11.426 0.059   1.00 34.83 ? 25  HIS A CD2   1 
ATOM   127  C CE1   . HIS A 1 34  ? 4.797  -11.158 -0.129  1.00 29.85 ? 25  HIS A CE1   1 
ATOM   128  N NE2   . HIS A 1 34  ? 3.650  -11.030 -0.770  1.00 37.87 ? 25  HIS A NE2   1 
ATOM   129  N N     . ARG A 1 35  ? 4.553  -11.530 4.586   1.00 41.04 ? 26  ARG A N     1 
ATOM   130  C CA    . ARG A 1 35  ? 5.812  -11.111 5.187   1.00 42.08 ? 26  ARG A CA    1 
ATOM   131  C C     . ARG A 1 35  ? 7.033  -11.590 4.413   1.00 32.85 ? 26  ARG A C     1 
ATOM   132  O O     . ARG A 1 35  ? 8.158  -11.442 4.900   1.00 37.50 ? 26  ARG A O     1 
ATOM   133  C CB    . ARG A 1 35  ? 5.881  -11.594 6.637   1.00 40.85 ? 26  ARG A CB    1 
ATOM   134  C CG    . ARG A 1 35  ? 4.776  -11.032 7.512   1.00 38.87 ? 26  ARG A CG    1 
ATOM   135  C CD    . ARG A 1 35  ? 4.387  -12.007 8.603   1.00 43.86 ? 26  ARG A CD    1 
ATOM   136  N NE    . ARG A 1 35  ? 3.261  -11.520 9.390   1.00 50.01 ? 26  ARG A NE    1 
ATOM   137  C CZ    . ARG A 1 35  ? 3.376  -10.822 10.511  1.00 41.02 ? 26  ARG A CZ    1 
ATOM   138  N NH1   . ARG A 1 35  ? 4.560  -10.506 11.010  1.00 38.98 ? 26  ARG A NH1   1 
ATOM   139  N NH2   . ARG A 1 35  ? 2.276  -10.434 11.149  1.00 44.05 ? 26  ARG A NH2   1 
ATOM   140  N N     . VAL A 1 36  ? 6.846  -12.159 3.226   1.00 32.71 ? 27  VAL A N     1 
ATOM   141  C CA    . VAL A 1 36  ? 7.970  -12.524 2.370   1.00 35.74 ? 27  VAL A CA    1 
ATOM   142  C C     . VAL A 1 36  ? 8.462  -11.263 1.669   1.00 36.98 ? 27  VAL A C     1 
ATOM   143  O O     . VAL A 1 36  ? 7.702  -10.603 0.954   1.00 38.99 ? 27  VAL A O     1 
ATOM   144  C CB    . VAL A 1 36  ? 7.571  -13.605 1.356   1.00 35.74 ? 27  VAL A CB    1 
ATOM   145  C CG1   . VAL A 1 36  ? 8.761  -13.980 0.487   1.00 31.39 ? 27  VAL A CG1   1 
ATOM   146  C CG2   . VAL A 1 36  ? 7.020  -14.831 2.075   1.00 35.30 ? 27  VAL A CG2   1 
ATOM   147  N N     . VAL A 1 37  ? 9.732  -10.923 1.879   1.00 32.06 ? 28  VAL A N     1 
ATOM   148  C CA    . VAL A 1 37  ? 10.316 -9.687  1.372   1.00 26.83 ? 28  VAL A CA    1 
ATOM   149  C C     . VAL A 1 37  ? 11.409 -10.030 0.371   1.00 31.61 ? 28  VAL A C     1 
ATOM   150  O O     . VAL A 1 37  ? 12.198 -10.955 0.591   1.00 33.48 ? 28  VAL A O     1 
ATOM   151  C CB    . VAL A 1 37  ? 10.879 -8.818  2.516   1.00 33.03 ? 28  VAL A CB    1 
ATOM   152  C CG1   . VAL A 1 37  ? 11.405 -7.493  1.978   1.00 27.38 ? 28  VAL A CG1   1 
ATOM   153  C CG2   . VAL A 1 37  ? 9.819  -8.589  3.580   1.00 28.93 ? 28  VAL A CG2   1 
ATOM   154  N N     . LEU A 1 38  ? 11.450 -9.286  -0.732  1.00 29.85 ? 29  LEU A N     1 
ATOM   155  C CA    . LEU A 1 38  ? 12.534 -9.412  -1.697  1.00 28.36 ? 29  LEU A CA    1 
ATOM   156  C C     . LEU A 1 38  ? 13.757 -8.663  -1.179  1.00 30.11 ? 29  LEU A C     1 
ATOM   157  O O     . LEU A 1 38  ? 13.725 -7.436  -1.037  1.00 30.18 ? 29  LEU A O     1 
ATOM   158  C CB    . LEU A 1 38  ? 12.105 -8.869  -3.059  1.00 30.35 ? 29  LEU A CB    1 
ATOM   159  C CG    . LEU A 1 38  ? 13.216 -8.707  -4.101  1.00 29.22 ? 29  LEU A CG    1 
ATOM   160  C CD1   . LEU A 1 38  ? 13.842 -10.051 -4.416  1.00 29.43 ? 29  LEU A CD1   1 
ATOM   161  C CD2   . LEU A 1 38  ? 12.689 -8.052  -5.371  1.00 28.64 ? 29  LEU A CD2   1 
ATOM   162  N N     . ALA A 1 39  ? 14.828 -9.399  -0.894  1.00 28.00 ? 30  ALA A N     1 
ATOM   163  C CA    . ALA A 1 39  ? 16.045 -8.775  -0.398  1.00 29.46 ? 30  ALA A CA    1 
ATOM   164  C C     . ALA A 1 39  ? 16.728 -7.983  -1.511  1.00 29.72 ? 30  ALA A C     1 
ATOM   165  O O     . ALA A 1 39  ? 16.687 -8.388  -2.677  1.00 29.26 ? 30  ALA A O     1 
ATOM   166  C CB    . ALA A 1 39  ? 17.004 -9.829  0.154   1.00 31.57 ? 30  ALA A CB    1 
ATOM   167  N N     . PRO A 1 40  ? 17.356 -6.852  -1.186  1.00 35.68 ? 31  PRO A N     1 
ATOM   168  C CA    . PRO A 1 40  ? 18.076 -6.083  -2.208  1.00 32.84 ? 31  PRO A CA    1 
ATOM   169  C C     . PRO A 1 40  ? 19.205 -6.904  -2.808  1.00 34.67 ? 31  PRO A C     1 
ATOM   170  O O     . PRO A 1 40  ? 19.943 -7.588  -2.096  1.00 32.83 ? 31  PRO A O     1 
ATOM   171  C CB    . PRO A 1 40  ? 18.611 -4.875  -1.432  1.00 34.51 ? 31  PRO A CB    1 
ATOM   172  C CG    . PRO A 1 40  ? 18.615 -5.304  -0.004  1.00 30.75 ? 31  PRO A CG    1 
ATOM   173  C CD    . PRO A 1 40  ? 17.447 -6.227  0.143   1.00 30.00 ? 31  PRO A CD    1 
ATOM   174  N N     . MET A 1 41  ? 19.339 -6.839  -4.132  1.00 27.22 ? 32  MET A N     1 
ATOM   175  C CA    . MET A 1 41  ? 20.251 -7.757  -4.807  1.00 26.77 ? 32  MET A CA    1 
ATOM   176  C C     . MET A 1 41  ? 20.830 -7.117  -6.058  1.00 32.49 ? 32  MET A C     1 
ATOM   177  O O     . MET A 1 41  ? 20.140 -6.985  -7.073  1.00 27.01 ? 32  MET A O     1 
ATOM   178  C CB    . MET A 1 41  ? 19.539 -9.054  -5.147  1.00 35.49 ? 32  MET A CB    1 
ATOM   179  C CG    . MET A 1 41  ? 19.828 -10.137 -4.137  1.00 33.04 ? 32  MET A CG    1 
ATOM   180  S SD    . MET A 1 41  ? 18.893 -11.629 -4.446  1.00 45.67 ? 32  MET A SD    1 
ATOM   181  C CE    . MET A 1 41  ? 17.304 -10.977 -4.947  1.00 29.22 ? 32  MET A CE    1 
ATOM   182  N N     . THR A 1 42  ? 22.102 -6.742  -5.972  1.00 29.13 ? 33  THR A N     1 
ATOM   183  C CA    . THR A 1 42  ? 22.860 -6.309  -7.134  1.00 37.41 ? 33  THR A CA    1 
ATOM   184  C C     . THR A 1 42  ? 22.885 -7.408  -8.189  1.00 37.49 ? 33  THR A C     1 
ATOM   185  O O     . THR A 1 42  ? 23.205 -8.562  -7.890  1.00 33.56 ? 33  THR A O     1 
ATOM   186  C CB    . THR A 1 42  ? 24.286 -5.953  -6.711  1.00 34.86 ? 33  THR A CB    1 
ATOM   187  O OG1   . THR A 1 42  ? 24.249 -4.914  -5.723  1.00 33.71 ? 33  THR A OG1   1 
ATOM   188  C CG2   . THR A 1 42  ? 25.112 -5.497  -7.911  1.00 38.55 ? 33  THR A CG2   1 
ATOM   189  N N     . ARG A 1 43  ? 22.531 -7.048  -9.425  1.00 29.95 ? 34  ARG A N     1 
ATOM   190  C CA    . ARG A 1 43  ? 22.569 -7.982  -10.544 1.00 30.00 ? 34  ARG A CA    1 
ATOM   191  C C     . ARG A 1 43  ? 23.314 -7.452  -11.760 1.00 34.97 ? 34  ARG A C     1 
ATOM   192  O O     . ARG A 1 43  ? 23.566 -8.228  -12.689 1.00 32.77 ? 34  ARG A O     1 
ATOM   193  C CB    . ARG A 1 43  ? 21.145 -8.379  -10.970 1.00 26.30 ? 34  ARG A CB    1 
ATOM   194  C CG    . ARG A 1 43  ? 20.254 -8.833  -9.824  1.00 36.28 ? 34  ARG A CG    1 
ATOM   195  C CD    . ARG A 1 43  ? 20.740 -10.146 -9.224  1.00 34.05 ? 34  ARG A CD    1 
ATOM   196  N NE    . ARG A 1 43  ? 21.096 -11.115 -10.253 1.00 29.72 ? 34  ARG A NE    1 
ATOM   197  C CZ    . ARG A 1 43  ? 20.238 -11.953 -10.817 1.00 37.11 ? 34  ARG A CZ    1 
ATOM   198  N NH1   . ARG A 1 43  ? 18.963 -11.977 -10.462 1.00 29.45 ? 34  ARG A NH1   1 
ATOM   199  N NH2   . ARG A 1 43  ? 20.668 -12.782 -11.764 1.00 31.87 ? 34  ARG A NH2   1 
ATOM   200  N N     . CYS A 1 44  ? 23.658 -6.162  -11.795 1.00 30.59 ? 35  CYS A N     1 
ATOM   201  C CA    . CYS A 1 44  ? 24.537 -5.585  -12.810 1.00 31.34 ? 35  CYS A CA    1 
ATOM   202  C C     . CYS A 1 44  ? 23.920 -5.605  -14.207 1.00 30.08 ? 35  CYS A C     1 
ATOM   203  O O     . CYS A 1 44  ? 24.635 -5.730  -15.205 1.00 30.95 ? 35  CYS A O     1 
ATOM   204  C CB    . CYS A 1 44  ? 25.899 -6.285  -12.823 1.00 36.01 ? 35  CYS A CB    1 
ATOM   205  S SG    . CYS A 1 44  ? 26.667 -6.412  -11.196 1.00 34.11 ? 35  CYS A SG    1 
ATOM   206  N N     . ARG A 1 45  ? 22.598 -5.469  -14.295 1.00 31.65 ? 36  ARG A N     1 
ATOM   207  C CA    . ARG A 1 45  ? 21.909 -5.371  -15.574 1.00 37.34 ? 36  ARG A CA    1 
ATOM   208  C C     . ARG A 1 45  ? 21.587 -3.933  -15.963 1.00 38.96 ? 36  ARG A C     1 
ATOM   209  O O     . ARG A 1 45  ? 21.076 -3.704  -17.064 1.00 36.03 ? 36  ARG A O     1 
ATOM   210  C CB    . ARG A 1 45  ? 20.618 -6.198  -15.544 1.00 33.35 ? 36  ARG A CB    1 
ATOM   211  C CG    . ARG A 1 45  ? 20.755 -7.588  -16.152 1.00 34.36 ? 36  ARG A CG    1 
ATOM   212  C CD    . ARG A 1 45  ? 21.556 -8.505  -15.241 1.00 35.02 ? 36  ARG A CD    1 
ATOM   213  N NE    . ARG A 1 45  ? 21.590 -9.880  -15.726 1.00 35.65 ? 36  ARG A NE    1 
ATOM   214  C CZ    . ARG A 1 45  ? 22.017 -10.916 -15.015 1.00 33.95 ? 36  ARG A CZ    1 
ATOM   215  N NH1   . ARG A 1 45  ? 22.461 -10.771 -13.777 1.00 30.45 ? 36  ARG A NH1   1 
ATOM   216  N NH2   . ARG A 1 45  ? 21.996 -12.128 -15.560 1.00 34.62 ? 36  ARG A NH2   1 
ATOM   217  N N     . ALA A 1 46  ? 21.873 -2.962  -15.093 1.00 30.71 ? 37  ALA A N     1 
ATOM   218  C CA    . ALA A 1 46  ? 21.564 -1.557  -15.362 1.00 35.45 ? 37  ALA A CA    1 
ATOM   219  C C     . ALA A 1 46  ? 22.753 -0.923  -16.079 1.00 36.29 ? 37  ALA A C     1 
ATOM   220  O O     . ALA A 1 46  ? 23.584 -0.228  -15.488 1.00 33.73 ? 37  ALA A O     1 
ATOM   221  C CB    . ALA A 1 46  ? 21.223 -0.827  -14.070 1.00 36.18 ? 37  ALA A CB    1 
ATOM   222  N N     . LEU A 1 47  ? 22.818 -1.167  -17.387 1.00 32.07 ? 38  LEU A N     1 
ATOM   223  C CA    . LEU A 1 47  ? 23.964 -0.752  -18.185 1.00 37.61 ? 38  LEU A CA    1 
ATOM   224  C C     . LEU A 1 47  ? 24.171 0.758   -18.120 1.00 35.05 ? 38  LEU A C     1 
ATOM   225  O O     . LEU A 1 47  ? 23.217 1.538   -18.182 1.00 32.66 ? 38  LEU A O     1 
ATOM   226  C CB    . LEU A 1 47  ? 23.778 -1.196  -19.638 1.00 36.21 ? 38  LEU A CB    1 
ATOM   227  C CG    . LEU A 1 47  ? 23.577 -2.700  -19.849 1.00 40.37 ? 38  LEU A CG    1 
ATOM   228  C CD1   . LEU A 1 47  ? 23.562 -3.054  -21.332 1.00 37.20 ? 38  LEU A CD1   1 
ATOM   229  C CD2   . LEU A 1 47  ? 24.651 -3.489  -19.117 1.00 31.99 ? 38  LEU A CD2   1 
ATOM   230  N N     . ASN A 1 48  ? 25.440 1.160   -17.993 1.00 31.06 ? 39  ASN A N     1 
ATOM   231  C CA    . ASN A 1 48  ? 25.837 2.566   -17.892 1.00 34.28 ? 39  ASN A CA    1 
ATOM   232  C C     . ASN A 1 48  ? 25.176 3.260   -16.706 1.00 34.20 ? 39  ASN A C     1 
ATOM   233  O O     . ASN A 1 48  ? 24.931 4.469   -16.744 1.00 24.27 ? 39  ASN A O     1 
ATOM   234  C CB    . ASN A 1 48  ? 25.540 3.330   -19.186 1.00 32.33 ? 39  ASN A CB    1 
ATOM   235  C CG    . ASN A 1 48  ? 26.037 2.604   -20.418 1.00 39.50 ? 39  ASN A CG    1 
ATOM   236  O OD1   . ASN A 1 48  ? 27.191 2.189   -20.485 1.00 36.38 ? 39  ASN A OD1   1 
ATOM   237  N ND2   . ASN A 1 48  ? 25.163 2.446   -21.401 1.00 41.06 ? 39  ASN A ND2   1 
ATOM   238  N N     . ASN A 1 49  ? 24.884 2.496   -15.651 1.00 30.66 ? 40  ASN A N     1 
ATOM   239  C CA    . ASN A 1 49  ? 24.287 3.003   -14.416 1.00 30.31 ? 40  ASN A CA    1 
ATOM   240  C C     . ASN A 1 49  ? 22.888 3.568   -14.635 1.00 38.33 ? 40  ASN A C     1 
ATOM   241  O O     . ASN A 1 49  ? 22.394 4.348   -13.812 1.00 36.96 ? 40  ASN A O     1 
ATOM   242  C CB    . ASN A 1 49  ? 25.181 4.058   -13.751 1.00 30.46 ? 40  ASN A CB    1 
ATOM   243  C CG    . ASN A 1 49  ? 26.611 3.586   -13.577 1.00 33.73 ? 40  ASN A CG    1 
ATOM   244  O OD1   . ASN A 1 49  ? 27.555 4.283   -13.945 1.00 34.44 ? 40  ASN A OD1   1 
ATOM   245  N ND2   . ASN A 1 49  ? 26.778 2.398   -13.007 1.00 33.61 ? 40  ASN A ND2   1 
ATOM   246  N N     . ILE A 1 50  ? 22.241 3.190   -15.726 1.00 36.56 ? 41  ILE A N     1 
ATOM   247  C CA    . ILE A 1 50  ? 20.884 3.626   -16.051 1.00 36.31 ? 41  ILE A CA    1 
ATOM   248  C C     . ILE A 1 50  ? 19.962 2.427   -15.916 1.00 38.30 ? 41  ILE A C     1 
ATOM   249  O O     . ILE A 1 50  ? 20.255 1.366   -16.482 1.00 37.60 ? 41  ILE A O     1 
ATOM   250  C CB    . ILE A 1 50  ? 20.801 4.219   -17.471 1.00 33.50 ? 41  ILE A CB    1 
ATOM   251  C CG1   . ILE A 1 50  ? 21.454 5.602   -17.511 1.00 33.67 ? 41  ILE A CG1   1 
ATOM   252  C CG2   . ILE A 1 50  ? 19.356 4.292   -17.938 1.00 35.99 ? 41  ILE A CG2   1 
ATOM   253  C CD1   . ILE A 1 50  ? 22.137 5.916   -18.824 1.00 45.55 ? 41  ILE A CD1   1 
ATOM   254  N N     . PRO A 1 51  ? 18.859 2.530   -15.174 1.00 35.45 ? 42  PRO A N     1 
ATOM   255  C CA    . PRO A 1 51  ? 17.911 1.413   -15.104 1.00 35.74 ? 42  PRO A CA    1 
ATOM   256  C C     . PRO A 1 51  ? 17.395 1.062   -16.492 1.00 42.71 ? 42  PRO A C     1 
ATOM   257  O O     . PRO A 1 51  ? 17.032 1.940   -17.280 1.00 36.29 ? 42  PRO A O     1 
ATOM   258  C CB    . PRO A 1 51  ? 16.797 1.944   -14.196 1.00 34.60 ? 42  PRO A CB    1 
ATOM   259  C CG    . PRO A 1 51  ? 17.427 3.054   -13.426 1.00 38.28 ? 42  PRO A CG    1 
ATOM   260  C CD    . PRO A 1 51  ? 18.433 3.671   -14.345 1.00 36.88 ? 42  PRO A CD    1 
ATOM   261  N N     . GLN A 1 52  ? 17.389 -0.230  -16.795 1.00 40.01 ? 43  GLN A N     1 
ATOM   262  C CA    . GLN A 1 52  ? 17.005 -0.732  -18.105 1.00 39.69 ? 43  GLN A CA    1 
ATOM   263  C C     . GLN A 1 52  ? 15.658 -1.440  -18.023 1.00 44.00 ? 43  GLN A C     1 
ATOM   264  O O     . GLN A 1 52  ? 15.156 -1.755  -16.940 1.00 42.96 ? 43  GLN A O     1 
ATOM   265  C CB    . GLN A 1 52  ? 18.080 -1.675  -18.658 1.00 36.14 ? 43  GLN A CB    1 
ATOM   266  C CG    . GLN A 1 52  ? 19.454 -1.031  -18.805 1.00 39.62 ? 43  GLN A CG    1 
ATOM   267  C CD    . GLN A 1 52  ? 19.472 0.082   -19.839 1.00 44.28 ? 43  GLN A CD    1 
ATOM   268  O OE1   . GLN A 1 52  ? 18.706 0.063   -20.800 1.00 48.76 ? 43  GLN A OE1   1 
ATOM   269  N NE2   . GLN A 1 52  ? 20.352 1.058   -19.646 1.00 40.97 ? 43  GLN A NE2   1 
ATOM   270  N N     . ALA A 1 53  ? 15.077 -1.690  -19.200 1.00 41.96 ? 44  ALA A N     1 
ATOM   271  C CA    . ALA A 1 53  ? 13.773 -2.344  -19.262 1.00 40.59 ? 44  ALA A CA    1 
ATOM   272  C C     . ALA A 1 53  ? 13.815 -3.745  -18.669 1.00 41.58 ? 44  ALA A C     1 
ATOM   273  O O     . ALA A 1 53  ? 12.785 -4.255  -18.213 1.00 39.40 ? 44  ALA A O     1 
ATOM   274  C CB    . ALA A 1 53  ? 13.279 -2.397  -20.707 1.00 39.31 ? 44  ALA A CB    1 
ATOM   275  N N     . ALA A 1 54  ? 14.988 -4.384  -18.672 1.00 39.51 ? 45  ALA A N     1 
ATOM   276  C CA    . ALA A 1 54  ? 15.111 -5.706  -18.068 1.00 39.74 ? 45  ALA A CA    1 
ATOM   277  C C     . ALA A 1 54  ? 14.808 -5.654  -16.578 1.00 37.48 ? 45  ALA A C     1 
ATOM   278  O O     . ALA A 1 54  ? 14.216 -6.587  -16.022 1.00 41.32 ? 45  ALA A O     1 
ATOM   279  C CB    . ALA A 1 54  ? 16.510 -6.270  -18.314 1.00 36.17 ? 45  ALA A CB    1 
ATOM   280  N N     . LEU A 1 55  ? 15.202 -4.564  -15.915 1.00 39.14 ? 46  LEU A N     1 
ATOM   281  C CA    . LEU A 1 55  ? 14.860 -4.389  -14.508 1.00 38.93 ? 46  LEU A CA    1 
ATOM   282  C C     . LEU A 1 55  ? 13.352 -4.290  -14.320 1.00 42.37 ? 46  LEU A C     1 
ATOM   283  O O     . LEU A 1 55  ? 12.809 -4.783  -13.324 1.00 40.34 ? 46  LEU A O     1 
ATOM   284  C CB    . LEU A 1 55  ? 15.554 -3.146  -13.948 1.00 39.71 ? 46  LEU A CB    1 
ATOM   285  C CG    . LEU A 1 55  ? 16.976 -3.317  -13.410 1.00 33.80 ? 46  LEU A CG    1 
ATOM   286  C CD1   . LEU A 1 55  ? 17.968 -3.514  -14.547 1.00 35.37 ? 46  LEU A CD1   1 
ATOM   287  C CD2   . LEU A 1 55  ? 17.374 -2.123  -12.556 1.00 38.07 ? 46  LEU A CD2   1 
ATOM   288  N N     . GLY A 1 56  ? 12.658 -3.655  -15.268 1.00 34.51 ? 47  GLY A N     1 
ATOM   289  C CA    . GLY A 1 56  ? 11.207 -3.598  -15.191 1.00 32.85 ? 47  GLY A CA    1 
ATOM   290  C C     . GLY A 1 56  ? 10.572 -4.973  -15.266 1.00 37.23 ? 47  GLY A C     1 
ATOM   291  O O     . GLY A 1 56  ? 9.673  -5.303  -14.488 1.00 43.09 ? 47  GLY A O     1 
ATOM   292  N N     . GLU A 1 57  ? 11.035 -5.798  -16.208 1.00 36.12 ? 48  GLU A N     1 
ATOM   293  C CA    . GLU A 1 57  ? 10.525 -7.161  -16.309 1.00 39.69 ? 48  GLU A CA    1 
ATOM   294  C C     . GLU A 1 57  ? 10.908 -7.986  -15.087 1.00 34.85 ? 48  GLU A C     1 
ATOM   295  O O     . GLU A 1 57  ? 10.106 -8.789  -14.595 1.00 36.57 ? 48  GLU A O     1 
ATOM   296  C CB    . GLU A 1 57  ? 11.049 -7.818  -17.586 1.00 42.64 ? 48  GLU A CB    1 
ATOM   297  C CG    . GLU A 1 57  ? 10.212 -8.985  -18.082 1.00 52.90 ? 48  GLU A CG    1 
ATOM   298  C CD    . GLU A 1 57  ? 11.003 -9.926  -18.971 1.00 64.05 ? 48  GLU A CD    1 
ATOM   299  O OE1   . GLU A 1 57  ? 11.671 -9.439  -19.908 1.00 64.31 ? 48  GLU A OE1   1 
ATOM   300  O OE2   . GLU A 1 57  ? 10.959 -11.152 -18.730 1.00 66.89 ? 48  GLU A OE2   1 
ATOM   301  N N     . TYR A 1 58  ? 12.128 -7.794  -14.580 1.00 29.84 ? 49  TYR A N     1 
ATOM   302  C CA    . TYR A 1 58  ? 12.613 -8.597  -13.462 1.00 36.98 ? 49  TYR A CA    1 
ATOM   303  C C     . TYR A 1 58  ? 11.830 -8.310  -12.185 1.00 34.76 ? 49  TYR A C     1 
ATOM   304  O O     . TYR A 1 58  ? 11.413 -9.237  -11.479 1.00 33.95 ? 49  TYR A O     1 
ATOM   305  C CB    . TYR A 1 58  ? 14.108 -8.340  -13.265 1.00 39.11 ? 49  TYR A CB    1 
ATOM   306  C CG    . TYR A 1 58  ? 14.700 -8.843  -11.966 1.00 34.41 ? 49  TYR A CG    1 
ATOM   307  C CD1   . TYR A 1 58  ? 15.232 -10.123 -11.874 1.00 37.66 ? 49  TYR A CD1   1 
ATOM   308  C CD2   . TYR A 1 58  ? 14.776 -8.022  -10.849 1.00 36.19 ? 49  TYR A CD2   1 
ATOM   309  C CE1   . TYR A 1 58  ? 15.793 -10.582 -10.697 1.00 35.26 ? 49  TYR A CE1   1 
ATOM   310  C CE2   . TYR A 1 58  ? 15.334 -8.471  -9.668  1.00 35.55 ? 49  TYR A CE2   1 
ATOM   311  C CZ    . TYR A 1 58  ? 15.841 -9.750  -9.598  1.00 37.52 ? 49  TYR A CZ    1 
ATOM   312  O OH    . TYR A 1 58  ? 16.401 -10.199 -8.424  1.00 40.60 ? 49  TYR A OH    1 
ATOM   313  N N     . TYR A 1 59  ? 11.619 -7.030  -11.865 1.00 31.60 ? 50  TYR A N     1 
ATOM   314  C CA    . TYR A 1 59  ? 10.905 -6.705  -10.633 1.00 33.06 ? 50  TYR A CA    1 
ATOM   315  C C     . TYR A 1 59  ? 9.414  -6.996  -10.752 1.00 37.01 ? 50  TYR A C     1 
ATOM   316  O O     . TYR A 1 59  ? 8.767  -7.314  -9.747  1.00 37.98 ? 50  TYR A O     1 
ATOM   317  C CB    . TYR A 1 59  ? 11.146 -5.243  -10.251 1.00 31.13 ? 50  TYR A CB    1 
ATOM   318  C CG    . TYR A 1 59  ? 12.527 -4.991  -9.682  1.00 36.90 ? 50  TYR A CG    1 
ATOM   319  C CD1   . TYR A 1 59  ? 12.957 -5.644  -8.533  1.00 43.16 ? 50  TYR A CD1   1 
ATOM   320  C CD2   . TYR A 1 59  ? 13.404 -4.108  -10.298 1.00 32.89 ? 50  TYR A CD2   1 
ATOM   321  C CE1   . TYR A 1 59  ? 14.223 -5.421  -8.013  1.00 34.49 ? 50  TYR A CE1   1 
ATOM   322  C CE2   . TYR A 1 59  ? 14.669 -3.880  -9.787  1.00 37.10 ? 50  TYR A CE2   1 
ATOM   323  C CZ    . TYR A 1 59  ? 15.073 -4.539  -8.644  1.00 35.89 ? 50  TYR A CZ    1 
ATOM   324  O OH    . TYR A 1 59  ? 16.334 -4.313  -8.134  1.00 35.33 ? 50  TYR A OH    1 
ATOM   325  N N     . GLU A 1 60  ? 8.854  -6.904  -11.962 1.00 34.01 ? 51  GLU A N     1 
ATOM   326  C CA    . GLU A 1 60  ? 7.445  -7.237  -12.151 1.00 38.99 ? 51  GLU A CA    1 
ATOM   327  C C     . GLU A 1 60  ? 7.195  -8.725  -11.936 1.00 42.03 ? 51  GLU A C     1 
ATOM   328  O O     . GLU A 1 60  ? 6.164  -9.113  -11.371 1.00 33.04 ? 51  GLU A O     1 
ATOM   329  C CB    . GLU A 1 60  ? 6.990  -6.821  -13.549 1.00 36.30 ? 51  GLU A CB    1 
ATOM   330  C CG    . GLU A 1 60  ? 5.564  -7.228  -13.885 1.00 38.93 ? 51  GLU A CG    1 
ATOM   331  C CD    . GLU A 1 60  ? 5.061  -6.589  -15.165 1.00 52.53 ? 51  GLU A CD    1 
ATOM   332  O OE1   . GLU A 1 60  ? 5.500  -7.016  -16.254 1.00 52.28 ? 51  GLU A OE1   1 
ATOM   333  O OE2   . GLU A 1 60  ? 4.233  -5.658  -15.081 1.00 54.51 ? 51  GLU A OE2   1 
ATOM   334  N N     . GLN A 1 61  ? 8.128  -9.571  -12.382 1.00 37.76 ? 52  GLN A N     1 
ATOM   335  C CA    . GLN A 1 61  ? 7.982  -11.010 -12.196 1.00 40.02 ? 52  GLN A CA    1 
ATOM   336  C C     . GLN A 1 61  ? 7.831  -11.376 -10.726 1.00 37.60 ? 52  GLN A C     1 
ATOM   337  O O     . GLN A 1 61  ? 7.153  -12.356 -10.396 1.00 37.92 ? 52  GLN A O     1 
ATOM   338  C CB    . GLN A 1 61  ? 9.184  -11.740 -12.795 1.00 35.57 ? 52  GLN A CB    1 
ATOM   339  C CG    . GLN A 1 61  ? 9.138  -11.911 -14.303 1.00 42.29 ? 52  GLN A CG    1 
ATOM   340  C CD    . GLN A 1 61  ? 10.300 -12.733 -14.822 1.00 43.33 ? 52  GLN A CD    1 
ATOM   341  O OE1   . GLN A 1 61  ? 11.244 -13.023 -14.087 1.00 44.56 ? 52  GLN A OE1   1 
ATOM   342  N NE2   . GLN A 1 61  ? 10.234 -13.121 -16.091 1.00 40.93 ? 52  GLN A NE2   1 
ATOM   343  N N     . ARG A 1 62  ? 8.438  -10.598 -9.831  1.00 37.18 ? 53  ARG A N     1 
ATOM   344  C CA    . ARG A 1 62  ? 8.471  -10.932 -8.415  1.00 42.08 ? 53  ARG A CA    1 
ATOM   345  C C     . ARG A 1 62  ? 7.477  -10.137 -7.579  1.00 42.01 ? 53  ARG A C     1 
ATOM   346  O O     . ARG A 1 62  ? 7.254  -10.488 -6.415  1.00 39.67 ? 53  ARG A O     1 
ATOM   347  C CB    . ARG A 1 62  ? 9.889  -10.727 -7.868  1.00 35.80 ? 53  ARG A CB    1 
ATOM   348  C CG    . ARG A 1 62  ? 10.835 -11.846 -8.259  1.00 37.38 ? 53  ARG A CG    1 
ATOM   349  C CD    . ARG A 1 62  ? 12.210 -11.349 -8.666  1.00 25.63 ? 53  ARG A CD    1 
ATOM   350  N NE    . ARG A 1 62  ? 13.003 -12.446 -9.209  1.00 36.00 ? 53  ARG A NE    1 
ATOM   351  C CZ    . ARG A 1 62  ? 13.050 -12.768 -10.494 1.00 39.90 ? 53  ARG A CZ    1 
ATOM   352  N NH1   . ARG A 1 62  ? 12.427 -12.043 -11.411 1.00 32.28 ? 53  ARG A NH1   1 
ATOM   353  N NH2   . ARG A 1 62  ? 13.737 -13.843 -10.870 1.00 36.67 ? 53  ARG A NH2   1 
ATOM   354  N N     . ALA A 1 63  ? 6.867  -9.096  -8.140  1.00 39.33 ? 54  ALA A N     1 
ATOM   355  C CA    . ALA A 1 63  ? 5.913  -8.290  -7.391  1.00 43.43 ? 54  ALA A CA    1 
ATOM   356  C C     . ALA A 1 63  ? 4.610  -9.050  -7.177  1.00 44.72 ? 54  ALA A C     1 
ATOM   357  O O     . ALA A 1 63  ? 4.107  -9.722  -8.082  1.00 41.99 ? 54  ALA A O     1 
ATOM   358  C CB    . ALA A 1 63  ? 5.637  -6.978  -8.123  1.00 40.88 ? 54  ALA A CB    1 
ATOM   359  N N     . THR A 1 64  ? 4.065  -8.940  -5.967  1.00 38.73 ? 55  THR A N     1 
ATOM   360  C CA    . THR A 1 64  ? 2.790  -9.544  -5.613  1.00 39.12 ? 55  THR A CA    1 
ATOM   361  C C     . THR A 1 64  ? 1.906  -8.499  -4.944  1.00 41.60 ? 55  THR A C     1 
ATOM   362  O O     . THR A 1 64  ? 2.361  -7.417  -4.562  1.00 44.36 ? 55  THR A O     1 
ATOM   363  C CB    . THR A 1 64  ? 2.972  -10.758 -4.689  1.00 40.99 ? 55  THR A CB    1 
ATOM   364  O OG1   . THR A 1 64  ? 3.713  -10.372 -3.524  1.00 39.51 ? 55  THR A OG1   1 
ATOM   365  C CG2   . THR A 1 64  ? 3.714  -11.875 -5.411  1.00 41.92 ? 55  THR A CG2   1 
ATOM   366  N N     . ALA A 1 65  ? 0.623  -8.832  -4.811  1.00 41.77 ? 56  ALA A N     1 
ATOM   367  C CA    . ALA A 1 65  ? -0.349 -7.921  -4.214  1.00 45.99 ? 56  ALA A CA    1 
ATOM   368  C C     . ALA A 1 65  ? -0.041 -7.750  -2.733  1.00 44.08 ? 56  ALA A C     1 
ATOM   369  O O     . ALA A 1 65  ? -0.154 -8.700  -1.951  1.00 30.68 ? 56  ALA A O     1 
ATOM   370  C CB    . ALA A 1 65  ? -1.765 -8.451  -4.422  1.00 41.96 ? 56  ALA A CB    1 
ATOM   371  N N     . GLY A 1 66  ? 0.354  -6.540  -2.344  1.00 38.77 ? 57  GLY A N     1 
ATOM   372  C CA    . GLY A 1 66  ? 0.722  -6.290  -0.966  1.00 45.17 ? 57  GLY A CA    1 
ATOM   373  C C     . GLY A 1 66  ? 2.067  -6.842  -0.558  1.00 44.39 ? 57  GLY A C     1 
ATOM   374  O O     . GLY A 1 66  ? 2.327  -6.984  0.641   1.00 42.61 ? 57  GLY A O     1 
ATOM   375  N N     . GLY A 1 67  ? 2.931  -7.169  -1.516  1.00 40.54 ? 58  GLY A N     1 
ATOM   376  C CA    . GLY A 1 67  ? 4.269  -7.630  -1.202  1.00 35.56 ? 58  GLY A CA    1 
ATOM   377  C C     . GLY A 1 67  ? 5.263  -6.483  -1.141  1.00 38.54 ? 58  GLY A C     1 
ATOM   378  O O     . GLY A 1 67  ? 5.100  -5.459  -1.798  1.00 38.89 ? 58  GLY A O     1 
ATOM   379  N N     . PHE A 1 68  ? 6.304  -6.667  -0.334  1.00 36.41 ? 59  PHE A N     1 
ATOM   380  C CA    . PHE A 1 68  ? 7.340  -5.658  -0.157  1.00 36.39 ? 59  PHE A CA    1 
ATOM   381  C C     . PHE A 1 68  ? 8.581  -6.045  -0.949  1.00 35.30 ? 59  PHE A C     1 
ATOM   382  O O     . PHE A 1 68  ? 9.100  -7.156  -0.796  1.00 35.01 ? 59  PHE A O     1 
ATOM   383  C CB    . PHE A 1 68  ? 7.693  -5.484  1.321   1.00 35.64 ? 59  PHE A CB    1 
ATOM   384  C CG    . PHE A 1 68  ? 8.670  -4.373  1.582   1.00 37.63 ? 59  PHE A CG    1 
ATOM   385  C CD1   . PHE A 1 68  ? 8.639  -3.214  0.824   1.00 32.46 ? 59  PHE A CD1   1 
ATOM   386  C CD2   . PHE A 1 68  ? 9.620  -4.487  2.585   1.00 41.86 ? 59  PHE A CD2   1 
ATOM   387  C CE1   . PHE A 1 68  ? 9.539  -2.190  1.058   1.00 39.58 ? 59  PHE A CE1   1 
ATOM   388  C CE2   . PHE A 1 68  ? 10.523 -3.466  2.825   1.00 40.45 ? 59  PHE A CE2   1 
ATOM   389  C CZ    . PHE A 1 68  ? 10.482 -2.315  2.061   1.00 42.12 ? 59  PHE A CZ    1 
ATOM   390  N N     . LEU A 1 69  ? 9.052  -5.126  -1.790  1.00 35.53 ? 60  LEU A N     1 
ATOM   391  C CA    . LEU A 1 69  ? 10.252 -5.320  -2.591  1.00 36.04 ? 60  LEU A CA    1 
ATOM   392  C C     . LEU A 1 69  ? 11.291 -4.265  -2.235  1.00 33.22 ? 60  LEU A C     1 
ATOM   393  O O     . LEU A 1 69  ? 10.951 -3.106  -1.978  1.00 28.58 ? 60  LEU A O     1 
ATOM   394  C CB    . LEU A 1 69  ? 9.948  -5.239  -4.092  1.00 34.61 ? 60  LEU A CB    1 
ATOM   395  C CG    . LEU A 1 69  ? 8.799  -6.072  -4.659  1.00 43.88 ? 60  LEU A CG    1 
ATOM   396  C CD1   . LEU A 1 69  ? 8.718  -5.887  -6.167  1.00 35.64 ? 60  LEU A CD1   1 
ATOM   397  C CD2   . LEU A 1 69  ? 8.964  -7.540  -4.306  1.00 39.25 ? 60  LEU A CD2   1 
ATOM   398  N N     . ILE A 1 70  ? 12.558 -4.670  -2.223  1.00 31.30 ? 61  ILE A N     1 
ATOM   399  C CA    . ILE A 1 70  ? 13.680 -3.751  -2.069  1.00 28.63 ? 61  ILE A CA    1 
ATOM   400  C C     . ILE A 1 70  ? 14.565 -3.897  -3.296  1.00 31.90 ? 61  ILE A C     1 
ATOM   401  O O     . ILE A 1 70  ? 15.025 -5.004  -3.607  1.00 26.39 ? 61  ILE A O     1 
ATOM   402  C CB    . ILE A 1 70  ? 14.476 -4.014  -0.783  1.00 30.07 ? 61  ILE A CB    1 
ATOM   403  C CG1   . ILE A 1 70  ? 13.550 -3.970  0.435   1.00 30.91 ? 61  ILE A CG1   1 
ATOM   404  C CG2   . ILE A 1 70  ? 15.590 -2.986  -0.634  1.00 27.17 ? 61  ILE A CG2   1 
ATOM   405  C CD1   . ILE A 1 70  ? 14.062 -4.757  1.616   1.00 33.13 ? 61  ILE A CD1   1 
ATOM   406  N N     . THR A 1 71  ? 14.800 -2.788  -3.994  1.00 29.16 ? 62  THR A N     1 
ATOM   407  C CA    . THR A 1 71  ? 15.607 -2.842  -5.200  1.00 35.44 ? 62  THR A CA    1 
ATOM   408  C C     . THR A 1 71  ? 17.062 -3.134  -4.856  1.00 35.20 ? 62  THR A C     1 
ATOM   409  O O     . THR A 1 71  ? 17.494 -3.050  -3.702  1.00 32.18 ? 62  THR A O     1 
ATOM   410  C CB    . THR A 1 71  ? 15.529 -1.528  -5.977  1.00 38.21 ? 62  THR A CB    1 
ATOM   411  O OG1   . THR A 1 71  ? 16.341 -0.541  -5.326  1.00 35.72 ? 62  THR A OG1   1 
ATOM   412  C CG2   . THR A 1 71  ? 14.096 -1.038  -6.059  1.00 33.01 ? 62  THR A CG2   1 
ATOM   413  N N     . GLU A 1 72  ? 17.818 -3.485  -5.891  1.00 31.20 ? 63  GLU A N     1 
ATOM   414  C CA    . GLU A 1 72  ? 19.262 -3.589  -5.787  1.00 27.52 ? 63  GLU A CA    1 
ATOM   415  C C     . GLU A 1 72  ? 19.857 -2.285  -5.262  1.00 33.75 ? 63  GLU A C     1 
ATOM   416  O O     . GLU A 1 72  ? 19.230 -1.220  -5.297  1.00 31.76 ? 63  GLU A O     1 
ATOM   417  C CB    . GLU A 1 72  ? 19.868 -3.902  -7.152  1.00 33.27 ? 63  GLU A CB    1 
ATOM   418  C CG    . GLU A 1 72  ? 19.631 -2.799  -8.170  1.00 30.20 ? 63  GLU A CG    1 
ATOM   419  C CD    . GLU A 1 72  ? 19.257 -3.327  -9.541  1.00 40.76 ? 63  GLU A CD    1 
ATOM   420  O OE1   . GLU A 1 72  ? 18.100 -3.761  -9.721  1.00 41.00 ? 63  GLU A OE1   1 
ATOM   421  O OE2   . GLU A 1 72  ? 20.126 -3.314  -10.436 1.00 36.68 ? 63  GLU A OE2   1 
ATOM   422  N N     . GLY A 1 73  ? 21.090 -2.381  -4.771  1.00 31.96 ? 64  GLY A N     1 
ATOM   423  C CA    . GLY A 1 73  ? 21.839 -1.211  -4.359  1.00 34.27 ? 64  GLY A CA    1 
ATOM   424  C C     . GLY A 1 73  ? 21.949 -0.188  -5.469  1.00 31.97 ? 64  GLY A C     1 
ATOM   425  O O     . GLY A 1 73  ? 22.300 -0.528  -6.603  1.00 30.19 ? 64  GLY A O     1 
ATOM   426  N N     . THR A 1 74  ? 21.647 1.068   -5.151  1.00 31.49 ? 65  THR A N     1 
ATOM   427  C CA    . THR A 1 74  ? 21.544 2.134   -6.138  1.00 27.38 ? 65  THR A CA    1 
ATOM   428  C C     . THR A 1 74  ? 22.490 3.268   -5.768  1.00 36.27 ? 65  THR A C     1 
ATOM   429  O O     . THR A 1 74  ? 22.510 3.713   -4.615  1.00 34.48 ? 65  THR A O     1 
ATOM   430  C CB    . THR A 1 74  ? 20.104 2.641   -6.228  1.00 35.44 ? 65  THR A CB    1 
ATOM   431  O OG1   . THR A 1 74  ? 19.220 1.522   -6.378  1.00 24.50 ? 65  THR A OG1   1 
ATOM   432  C CG2   . THR A 1 74  ? 19.938 3.579   -7.406  1.00 33.35 ? 65  THR A CG2   1 
ATOM   433  N N     . MET A 1 75  ? 23.265 3.732   -6.750  1.00 28.83 ? 66  MET A N     1 
ATOM   434  C CA    . MET A 1 75  ? 24.292 4.736   -6.503  1.00 31.90 ? 66  MET A CA    1 
ATOM   435  C C     . MET A 1 75  ? 23.673 6.061   -6.075  1.00 36.61 ? 66  MET A C     1 
ATOM   436  O O     . MET A 1 75  ? 22.606 6.454   -6.556  1.00 34.53 ? 66  MET A O     1 
ATOM   437  C CB    . MET A 1 75  ? 25.148 4.949   -7.756  1.00 33.84 ? 66  MET A CB    1 
ATOM   438  C CG    . MET A 1 75  ? 25.639 3.668   -8.417  1.00 38.62 ? 66  MET A CG    1 
ATOM   439  S SD    . MET A 1 75  ? 26.435 3.916   -10.025 1.00 40.90 ? 66  MET A SD    1 
ATOM   440  C CE    . MET A 1 75  ? 26.920 5.633   -9.945  1.00 39.78 ? 66  MET A CE    1 
ATOM   441  N N     . ILE A 1 76  ? 24.356 6.753   -5.164  1.00 28.01 ? 67  ILE A N     1 
ATOM   442  C CA    . ILE A 1 76  ? 23.939 8.064   -4.685  1.00 31.50 ? 67  ILE A CA    1 
ATOM   443  C C     . ILE A 1 76  ? 24.792 9.181   -5.252  1.00 38.07 ? 67  ILE A C     1 
ATOM   444  O O     . ILE A 1 76  ? 24.525 10.358  -4.967  1.00 42.04 ? 67  ILE A O     1 
ATOM   445  C CB    . ILE A 1 76  ? 23.943 8.127   -3.146  1.00 31.86 ? 67  ILE A CB    1 
ATOM   446  C CG1   . ILE A 1 76  ? 25.379 8.131   -2.615  1.00 30.57 ? 67  ILE A CG1   1 
ATOM   447  C CG2   . ILE A 1 76  ? 23.150 6.969   -2.560  1.00 30.46 ? 67  ILE A CG2   1 
ATOM   448  C CD1   . ILE A 1 76  ? 25.499 8.571   -1.165  1.00 30.68 ? 67  ILE A CD1   1 
ATOM   449  N N     . SER A 1 77  ? 25.804 8.856   -6.046  1.00 37.10 ? 68  SER A N     1 
ATOM   450  C CA    . SER A 1 77  ? 26.774 9.823   -6.536  1.00 38.82 ? 68  SER A CA    1 
ATOM   451  C C     . SER A 1 77  ? 27.655 9.127   -7.569  1.00 43.25 ? 68  SER A C     1 
ATOM   452  O O     . SER A 1 77  ? 27.686 7.892   -7.624  1.00 40.46 ? 68  SER A O     1 
ATOM   453  C CB    . SER A 1 77  ? 27.629 10.385  -5.390  1.00 35.44 ? 68  SER A CB    1 
ATOM   454  O OG    . SER A 1 77  ? 28.649 9.471   -5.034  1.00 37.47 ? 68  SER A OG    1 
ATOM   455  N N     . PRO A 1 78  ? 28.370 9.895   -8.398  1.00 41.80 ? 69  PRO A N     1 
ATOM   456  C CA    . PRO A 1 78  ? 29.266 9.266   -9.384  1.00 42.71 ? 69  PRO A CA    1 
ATOM   457  C C     . PRO A 1 78  ? 30.411 8.480   -8.765  1.00 44.57 ? 69  PRO A C     1 
ATOM   458  O O     . PRO A 1 78  ? 31.032 7.670   -9.466  1.00 38.67 ? 69  PRO A O     1 
ATOM   459  C CB    . PRO A 1 78  ? 29.790 10.459  -10.198 1.00 41.26 ? 69  PRO A CB    1 
ATOM   460  C CG    . PRO A 1 78  ? 28.795 11.547  -9.981  1.00 40.83 ? 69  PRO A CG    1 
ATOM   461  C CD    . PRO A 1 78  ? 28.260 11.351  -8.597  1.00 38.50 ? 69  PRO A CD    1 
ATOM   462  N N     . THR A 1 79  ? 30.715 8.685   -7.484  1.00 37.60 ? 70  THR A N     1 
ATOM   463  C CA    . THR A 1 79  ? 31.842 8.024   -6.838  1.00 36.11 ? 70  THR A CA    1 
ATOM   464  C C     . THR A 1 79  ? 31.412 6.911   -5.890  1.00 38.51 ? 70  THR A C     1 
ATOM   465  O O     . THR A 1 79  ? 32.241 6.415   -5.119  1.00 37.77 ? 70  THR A O     1 
ATOM   466  C CB    . THR A 1 79  ? 32.693 9.045   -6.081  1.00 42.53 ? 70  THR A CB    1 
ATOM   467  O OG1   . THR A 1 79  ? 32.125 9.270   -4.784  1.00 44.67 ? 70  THR A OG1   1 
ATOM   468  C CG2   . THR A 1 79  ? 32.750 10.360  -6.841  1.00 43.48 ? 70  THR A CG2   1 
ATOM   469  N N     . SER A 1 80  ? 30.148 6.498   -5.931  1.00 31.55 ? 71  SER A N     1 
ATOM   470  C CA    . SER A 1 80  ? 29.619 5.537   -4.974  1.00 38.45 ? 71  SER A CA    1 
ATOM   471  C C     . SER A 1 80  ? 29.573 4.108   -5.503  1.00 33.92 ? 71  SER A C     1 
ATOM   472  O O     . SER A 1 80  ? 29.174 3.205   -4.762  1.00 34.47 ? 71  SER A O     1 
ATOM   473  C CB    . SER A 1 80  ? 28.217 5.962   -4.527  1.00 37.67 ? 71  SER A CB    1 
ATOM   474  O OG    . SER A 1 80  ? 27.295 5.882   -5.597  1.00 34.51 ? 71  SER A OG    1 
ATOM   475  N N     . ALA A 1 81  ? 29.982 3.876   -6.747  1.00 31.22 ? 72  ALA A N     1 
ATOM   476  C CA    . ALA A 1 81  ? 29.865 2.562   -7.361  1.00 25.56 ? 72  ALA A CA    1 
ATOM   477  C C     . ALA A 1 81  ? 31.114 1.722   -7.118  1.00 31.53 ? 72  ALA A C     1 
ATOM   478  O O     . ALA A 1 81  ? 32.234 2.236   -7.053  1.00 25.50 ? 72  ALA A O     1 
ATOM   479  C CB    . ALA A 1 81  ? 29.618 2.688   -8.865  1.00 38.27 ? 72  ALA A CB    1 
ATOM   480  N N     . GLY A 1 82  ? 30.903 0.412   -6.984  1.00 31.71 ? 73  GLY A N     1 
ATOM   481  C CA    . GLY A 1 82  ? 31.985 -0.541  -6.833  1.00 30.38 ? 73  GLY A CA    1 
ATOM   482  C C     . GLY A 1 82  ? 31.735 -1.818  -7.612  1.00 33.34 ? 73  GLY A C     1 
ATOM   483  O O     . GLY A 1 82  ? 32.530 -2.762  -7.557  1.00 34.06 ? 73  GLY A O     1 
ATOM   484  N N     . PHE A 1 83  ? 30.620 -1.857  -8.335  1.00 36.24 ? 74  PHE A N     1 
ATOM   485  C CA    . PHE A 1 83  ? 30.231 -2.959  -9.199  1.00 31.75 ? 74  PHE A CA    1 
ATOM   486  C C     . PHE A 1 83  ? 29.934 -2.419  -10.590 1.00 32.98 ? 74  PHE A C     1 
ATOM   487  O O     . PHE A 1 83  ? 29.593 -1.242  -10.741 1.00 29.81 ? 74  PHE A O     1 
ATOM   488  C CB    . PHE A 1 83  ? 28.993 -3.686  -8.650  1.00 29.24 ? 74  PHE A CB    1 
ATOM   489  C CG    . PHE A 1 83  ? 29.304 -4.737  -7.620  1.00 34.98 ? 74  PHE A CG    1 
ATOM   490  C CD1   . PHE A 1 83  ? 29.666 -4.381  -6.331  1.00 36.80 ? 74  PHE A CD1   1 
ATOM   491  C CD2   . PHE A 1 83  ? 29.220 -6.085  -7.939  1.00 32.83 ? 74  PHE A CD2   1 
ATOM   492  C CE1   . PHE A 1 83  ? 29.945 -5.347  -5.377  1.00 33.28 ? 74  PHE A CE1   1 
ATOM   493  C CE2   . PHE A 1 83  ? 29.498 -7.056  -6.990  1.00 39.95 ? 74  PHE A CE2   1 
ATOM   494  C CZ    . PHE A 1 83  ? 29.860 -6.685  -5.707  1.00 28.91 ? 74  PHE A CZ    1 
ATOM   495  N N     . PRO A 1 84  ? 30.059 -3.246  -11.625 1.00 34.31 ? 75  PRO A N     1 
ATOM   496  C CA    . PRO A 1 84  ? 29.774 -2.758  -12.978 1.00 27.39 ? 75  PRO A CA    1 
ATOM   497  C C     . PRO A 1 84  ? 28.278 -2.702  -13.248 1.00 30.89 ? 75  PRO A C     1 
ATOM   498  O O     . PRO A 1 84  ? 27.526 -3.615  -12.898 1.00 28.61 ? 75  PRO A O     1 
ATOM   499  C CB    . PRO A 1 84  ? 30.463 -3.791  -13.876 1.00 32.38 ? 75  PRO A CB    1 
ATOM   500  C CG    . PRO A 1 84  ? 30.414 -5.050  -13.082 1.00 35.73 ? 75  PRO A CG    1 
ATOM   501  C CD    . PRO A 1 84  ? 30.488 -4.657  -11.626 1.00 29.43 ? 75  PRO A CD    1 
ATOM   502  N N     . HIS A 1 85  ? 27.851 -1.599  -13.862 1.00 34.42 ? 76  HIS A N     1 
ATOM   503  C CA    . HIS A 1 85  ? 26.481 -1.432  -14.348 1.00 28.00 ? 76  HIS A CA    1 
ATOM   504  C C     . HIS A 1 85  ? 25.458 -1.593  -13.224 1.00 37.74 ? 76  HIS A C     1 
ATOM   505  O O     . HIS A 1 85  ? 24.509 -2.374  -13.322 1.00 36.00 ? 76  HIS A O     1 
ATOM   506  C CB    . HIS A 1 85  ? 26.192 -2.400  -15.499 1.00 38.19 ? 76  HIS A CB    1 
ATOM   507  C CG    . HIS A 1 85  ? 27.201 -2.336  -16.602 1.00 36.42 ? 76  HIS A CG    1 
ATOM   508  N ND1   . HIS A 1 85  ? 27.381 -1.212  -17.379 1.00 38.03 ? 76  HIS A ND1   1 
ATOM   509  C CD2   . HIS A 1 85  ? 28.093 -3.251  -17.049 1.00 34.93 ? 76  HIS A CD2   1 
ATOM   510  C CE1   . HIS A 1 85  ? 28.337 -1.439  -18.263 1.00 34.03 ? 76  HIS A CE1   1 
ATOM   511  N NE2   . HIS A 1 85  ? 28.786 -2.669  -18.083 1.00 39.39 ? 76  HIS A NE2   1 
ATOM   512  N N     . VAL A 1 86  ? 25.662 -0.845  -12.145 1.00 33.18 ? 77  VAL A N     1 
ATOM   513  C CA    . VAL A 1 86  ? 24.683 -0.776  -11.063 1.00 35.68 ? 77  VAL A CA    1 
ATOM   514  C C     . VAL A 1 86  ? 23.876 0.500   -11.261 1.00 36.55 ? 77  VAL A C     1 
ATOM   515  O O     . VAL A 1 86  ? 24.440 1.528   -11.660 1.00 37.69 ? 77  VAL A O     1 
ATOM   516  C CB    . VAL A 1 86  ? 25.358 -0.816  -9.683  1.00 32.71 ? 77  VAL A CB    1 
ATOM   517  C CG1   . VAL A 1 86  ? 25.877 -2.213  -9.404  1.00 36.73 ? 77  VAL A CG1   1 
ATOM   518  C CG2   . VAL A 1 86  ? 26.487 0.203   -9.603  1.00 38.87 ? 77  VAL A CG2   1 
ATOM   519  N N     . PRO A 1 87  ? 22.570 0.490   -11.008 1.00 34.00 ? 78  PRO A N     1 
ATOM   520  C CA    . PRO A 1 87  ? 21.753 1.665   -11.324 1.00 28.37 ? 78  PRO A CA    1 
ATOM   521  C C     . PRO A 1 87  ? 22.028 2.817   -10.373 1.00 34.40 ? 78  PRO A C     1 
ATOM   522  O O     . PRO A 1 87  ? 22.487 2.641   -9.241  1.00 32.01 ? 78  PRO A O     1 
ATOM   523  C CB    . PRO A 1 87  ? 20.316 1.152   -11.176 1.00 28.08 ? 78  PRO A CB    1 
ATOM   524  C CG    . PRO A 1 87  ? 20.422 0.026   -10.210 1.00 33.29 ? 78  PRO A CG    1 
ATOM   525  C CD    . PRO A 1 87  ? 21.773 -0.605  -10.429 1.00 30.89 ? 78  PRO A CD    1 
ATOM   526  N N     . GLY A 1 88  ? 21.743 4.023   -10.865 1.00 37.55 ? 79  GLY A N     1 
ATOM   527  C CA    . GLY A 1 88  ? 21.863 5.235   -10.090 1.00 30.27 ? 79  GLY A CA    1 
ATOM   528  C C     . GLY A 1 88  ? 20.507 5.885   -9.855  1.00 30.85 ? 79  GLY A C     1 
ATOM   529  O O     . GLY A 1 88  ? 19.479 5.479   -10.396 1.00 24.62 ? 79  GLY A O     1 
ATOM   530  N N     . ILE A 1 89  ? 20.527 6.916   -9.013  1.00 36.68 ? 80  ILE A N     1 
ATOM   531  C CA    . ILE A 1 89  ? 19.330 7.674   -8.665  1.00 35.69 ? 80  ILE A CA    1 
ATOM   532  C C     . ILE A 1 89  ? 19.745 9.120   -8.403  1.00 34.81 ? 80  ILE A C     1 
ATOM   533  O O     . ILE A 1 89  ? 19.038 9.876   -7.728  1.00 39.55 ? 80  ILE A O     1 
ATOM   534  C CB    . ILE A 1 89  ? 18.609 7.037   -7.457  1.00 37.34 ? 80  ILE A CB    1 
ATOM   535  C CG1   . ILE A 1 89  ? 17.191 7.595   -7.275  1.00 42.28 ? 80  ILE A CG1   1 
ATOM   536  C CG2   . ILE A 1 89  ? 19.430 7.191   -6.183  1.00 35.70 ? 80  ILE A CG2   1 
ATOM   537  C CD1   . ILE A 1 89  ? 16.189 7.105   -8.285  1.00 37.21 ? 80  ILE A CD1   1 
ATOM   538  N N     . PHE A 1 90  ? 20.893 9.522   -8.950  1.00 31.23 ? 81  PHE A N     1 
ATOM   539  C CA    . PHE A 1 90  ? 21.404 10.874  -8.767  1.00 37.77 ? 81  PHE A CA    1 
ATOM   540  C C     . PHE A 1 90  ? 21.305 11.737  -10.020 1.00 38.95 ? 81  PHE A C     1 
ATOM   541  O O     . PHE A 1 90  ? 21.662 12.919  -9.967  1.00 39.74 ? 81  PHE A O     1 
ATOM   542  C CB    . PHE A 1 90  ? 22.859 10.835  -8.275  1.00 37.52 ? 81  PHE A CB    1 
ATOM   543  C CG    . PHE A 1 90  ? 23.816 10.200  -9.245  1.00 41.44 ? 81  PHE A CG    1 
ATOM   544  C CD1   . PHE A 1 90  ? 23.963 8.824   -9.291  1.00 36.41 ? 81  PHE A CD1   1 
ATOM   545  C CD2   . PHE A 1 90  ? 24.578 10.980  -10.101 1.00 38.81 ? 81  PHE A CD2   1 
ATOM   546  C CE1   . PHE A 1 90  ? 24.839 8.236   -10.180 1.00 39.31 ? 81  PHE A CE1   1 
ATOM   547  C CE2   . PHE A 1 90  ? 25.460 10.396  -10.992 1.00 41.57 ? 81  PHE A CE2   1 
ATOM   548  C CZ    . PHE A 1 90  ? 25.591 9.022   -11.032 1.00 37.97 ? 81  PHE A CZ    1 
ATOM   549  N N     . THR A 1 91  ? 20.840 11.189  -11.141 1.00 38.89 ? 82  THR A N     1 
ATOM   550  C CA    . THR A 1 91  ? 20.587 11.973  -12.342 1.00 40.38 ? 82  THR A CA    1 
ATOM   551  C C     . THR A 1 91  ? 19.103 11.936  -12.679 1.00 41.39 ? 82  THR A C     1 
ATOM   552  O O     . THR A 1 91  ? 18.404 10.961  -12.382 1.00 42.37 ? 82  THR A O     1 
ATOM   553  C CB    . THR A 1 91  ? 21.392 11.469  -13.550 1.00 40.69 ? 82  THR A CB    1 
ATOM   554  O OG1   . THR A 1 91  ? 20.683 10.401  -14.188 1.00 37.66 ? 82  THR A OG1   1 
ATOM   555  C CG2   . THR A 1 91  ? 22.761 10.978  -13.125 1.00 47.29 ? 82  THR A CG2   1 
ATOM   556  N N     . LYS A 1 92  ? 18.627 13.017  -13.303 1.00 40.93 ? 83  LYS A N     1 
ATOM   557  C CA    . LYS A 1 92  ? 17.234 13.072  -13.732 1.00 44.48 ? 83  LYS A CA    1 
ATOM   558  C C     . LYS A 1 92  ? 16.926 12.000  -14.768 1.00 40.29 ? 83  LYS A C     1 
ATOM   559  O O     . LYS A 1 92  ? 15.785 11.532  -14.858 1.00 45.77 ? 83  LYS A O     1 
ATOM   560  C CB    . LYS A 1 92  ? 16.911 14.460  -14.288 1.00 47.06 ? 83  LYS A CB    1 
ATOM   561  C CG    . LYS A 1 92  ? 17.791 15.569  -13.732 1.00 49.07 ? 83  LYS A CG    1 
ATOM   562  C CD    . LYS A 1 92  ? 17.950 16.707  -14.731 1.00 62.69 ? 83  LYS A CD    1 
ATOM   563  C CE    . LYS A 1 92  ? 19.104 17.623  -14.347 1.00 59.86 ? 83  LYS A CE    1 
ATOM   564  N NZ    . LYS A 1 92  ? 18.900 19.014  -14.838 1.00 66.48 ? 83  LYS A NZ    1 
ATOM   565  N N     . GLU A 1 93  ? 17.925 11.600  -15.558 1.00 34.24 ? 84  GLU A N     1 
ATOM   566  C CA    . GLU A 1 93  ? 17.725 10.512  -16.509 1.00 42.63 ? 84  GLU A CA    1 
ATOM   567  C C     . GLU A 1 93  ? 17.490 9.190   -15.787 1.00 38.50 ? 84  GLU A C     1 
ATOM   568  O O     . GLU A 1 93  ? 16.666 8.376   -16.221 1.00 43.83 ? 84  GLU A O     1 
ATOM   569  C CB    . GLU A 1 93  ? 18.929 10.413  -17.448 1.00 37.04 ? 84  GLU A CB    1 
ATOM   570  C CG    . GLU A 1 93  ? 18.883 9.231   -18.407 1.00 42.74 ? 84  GLU A CG    1 
ATOM   571  C CD    . GLU A 1 93  ? 20.182 9.045   -19.169 1.00 48.97 ? 84  GLU A CD    1 
ATOM   572  O OE1   . GLU A 1 93  ? 21.231 9.521   -18.685 1.00 56.54 ? 84  GLU A OE1   1 
ATOM   573  O OE2   . GLU A 1 93  ? 20.156 8.424   -20.253 1.00 62.65 ? 84  GLU A OE2   1 
ATOM   574  N N     . GLN A 1 94  ? 18.197 8.962   -14.678 1.00 37.22 ? 85  GLN A N     1 
ATOM   575  C CA    . GLN A 1 94  ? 17.980 7.744   -13.905 1.00 34.88 ? 85  GLN A CA    1 
ATOM   576  C C     . GLN A 1 94  ? 16.610 7.750   -13.239 1.00 39.28 ? 85  GLN A C     1 
ATOM   577  O O     . GLN A 1 94  ? 15.957 6.703   -13.141 1.00 29.60 ? 85  GLN A O     1 
ATOM   578  C CB    . GLN A 1 94  ? 19.084 7.583   -12.862 1.00 35.92 ? 85  GLN A CB    1 
ATOM   579  C CG    . GLN A 1 94  ? 20.457 7.307   -13.453 1.00 33.38 ? 85  GLN A CG    1 
ATOM   580  C CD    . GLN A 1 94  ? 21.582 7.708   -12.523 1.00 34.75 ? 85  GLN A CD    1 
ATOM   581  O OE1   . GLN A 1 94  ? 21.367 8.416   -11.540 1.00 33.64 ? 85  GLN A OE1   1 
ATOM   582  N NE2   . GLN A 1 94  ? 22.793 7.259   -12.831 1.00 39.51 ? 85  GLN A NE2   1 
ATOM   583  N N     . VAL A 1 95  ? 16.158 8.920   -12.780 1.00 35.92 ? 86  VAL A N     1 
ATOM   584  C CA    . VAL A 1 95  ? 14.850 9.021   -12.137 1.00 36.18 ? 86  VAL A CA    1 
ATOM   585  C C     . VAL A 1 95  ? 13.748 8.640   -13.117 1.00 35.53 ? 86  VAL A C     1 
ATOM   586  O O     . VAL A 1 95  ? 12.859 7.838   -12.802 1.00 39.20 ? 86  VAL A O     1 
ATOM   587  C CB    . VAL A 1 95  ? 14.639 10.438  -11.573 1.00 36.88 ? 86  VAL A CB    1 
ATOM   588  C CG1   . VAL A 1 95  ? 13.156 10.724  -11.380 1.00 34.11 ? 86  VAL A CG1   1 
ATOM   589  C CG2   . VAL A 1 95  ? 15.387 10.601  -10.266 1.00 40.54 ? 86  VAL A CG2   1 
ATOM   590  N N     . ARG A 1 96  ? 13.796 9.204   -14.326 1.00 37.53 ? 87  ARG A N     1 
ATOM   591  C CA    . ARG A 1 96  ? 12.761 8.927   -15.316 1.00 38.17 ? 87  ARG A CA    1 
ATOM   592  C C     . ARG A 1 96  ? 12.759 7.456   -15.721 1.00 33.50 ? 87  ARG A C     1 
ATOM   593  O O     . ARG A 1 96  ? 11.693 6.860   -15.919 1.00 36.00 ? 87  ARG A O     1 
ATOM   594  C CB    . ARG A 1 96  ? 12.955 9.839   -16.529 1.00 42.08 ? 87  ARG A CB    1 
ATOM   595  C CG    . ARG A 1 96  ? 12.743 9.181   -17.881 1.00 48.41 ? 87  ARG A CG    1 
ATOM   596  C CD    . ARG A 1 96  ? 12.815 10.209  -19.005 1.00 54.01 ? 87  ARG A CD    1 
ATOM   597  N NE    . ARG A 1 96  ? 14.179 10.662  -19.256 1.00 55.45 ? 87  ARG A NE    1 
ATOM   598  C CZ    . ARG A 1 96  ? 14.690 11.798  -18.798 1.00 56.05 ? 87  ARG A CZ    1 
ATOM   599  N NH1   . ARG A 1 96  ? 13.977 12.625  -18.050 1.00 58.12 ? 87  ARG A NH1   1 
ATOM   600  N NH2   . ARG A 1 96  ? 15.947 12.112  -19.099 1.00 53.18 ? 87  ARG A NH2   1 
ATOM   601  N N     . GLU A 1 97  ? 13.940 6.846   -15.835 1.00 30.96 ? 88  GLU A N     1 
ATOM   602  C CA    . GLU A 1 97  ? 13.996 5.415   -16.120 1.00 39.15 ? 88  GLU A CA    1 
ATOM   603  C C     . GLU A 1 97  ? 13.521 4.597   -14.924 1.00 38.65 ? 88  GLU A C     1 
ATOM   604  O O     . GLU A 1 97  ? 12.865 3.563   -15.092 1.00 36.87 ? 88  GLU A O     1 
ATOM   605  C CB    . GLU A 1 97  ? 15.414 5.013   -16.524 1.00 39.64 ? 88  GLU A CB    1 
ATOM   606  C CG    . GLU A 1 97  ? 15.795 5.421   -17.942 1.00 44.83 ? 88  GLU A CG    1 
ATOM   607  C CD    . GLU A 1 97  ? 14.605 5.455   -18.883 1.00 47.44 ? 88  GLU A CD    1 
ATOM   608  O OE1   . GLU A 1 97  ? 14.045 4.379   -19.183 1.00 53.51 ? 88  GLU A OE1   1 
ATOM   609  O OE2   . GLU A 1 97  ? 14.229 6.561   -19.326 1.00 54.71 ? 88  GLU A OE2   1 
ATOM   610  N N     . TRP A 1 98  ? 13.834 5.051   -13.707 1.00 39.91 ? 89  TRP A N     1 
ATOM   611  C CA    . TRP A 1 98  ? 13.358 4.359   -12.513 1.00 33.84 ? 89  TRP A CA    1 
ATOM   612  C C     . TRP A 1 98  ? 11.841 4.428   -12.388 1.00 36.24 ? 89  TRP A C     1 
ATOM   613  O O     . TRP A 1 98  ? 11.226 3.513   -11.828 1.00 33.65 ? 89  TRP A O     1 
ATOM   614  C CB    . TRP A 1 98  ? 14.008 4.953   -11.264 1.00 29.98 ? 89  TRP A CB    1 
ATOM   615  C CG    . TRP A 1 98  ? 15.222 4.221   -10.777 1.00 30.80 ? 89  TRP A CG    1 
ATOM   616  C CD1   . TRP A 1 98  ? 16.472 4.739   -10.603 1.00 30.23 ? 89  TRP A CD1   1 
ATOM   617  C CD2   . TRP A 1 98  ? 15.302 2.844   -10.389 1.00 30.55 ? 89  TRP A CD2   1 
ATOM   618  N NE1   . TRP A 1 98  ? 17.326 3.773   -10.133 1.00 29.01 ? 89  TRP A NE1   1 
ATOM   619  C CE2   . TRP A 1 98  ? 16.633 2.599   -9.995  1.00 31.55 ? 89  TRP A CE2   1 
ATOM   620  C CE3   . TRP A 1 98  ? 14.380 1.793   -10.342 1.00 28.37 ? 89  TRP A CE3   1 
ATOM   621  C CZ2   . TRP A 1 98  ? 17.064 1.349   -9.557  1.00 30.65 ? 89  TRP A CZ2   1 
ATOM   622  C CZ3   . TRP A 1 98  ? 14.809 0.553   -9.907  1.00 33.95 ? 89  TRP A CZ3   1 
ATOM   623  C CH2   . TRP A 1 98  ? 16.140 0.341   -9.520  1.00 34.84 ? 89  TRP A CH2   1 
ATOM   624  N N     . LYS A 1 99  ? 11.223 5.496   -12.903 1.00 38.69 ? 90  LYS A N     1 
ATOM   625  C CA    . LYS A 1 99  ? 9.786  5.685   -12.724 1.00 36.69 ? 90  LYS A CA    1 
ATOM   626  C C     . LYS A 1 99  ? 8.980  4.626   -13.469 1.00 36.64 ? 90  LYS A C     1 
ATOM   627  O O     . LYS A 1 99  ? 7.967  4.136   -12.956 1.00 38.46 ? 90  LYS A O     1 
ATOM   628  C CB    . LYS A 1 99  ? 9.383  7.088   -13.180 1.00 45.31 ? 90  LYS A CB    1 
ATOM   629  C CG    . LYS A 1 99  ? 7.893  7.253   -13.440 1.00 45.70 ? 90  LYS A CG    1 
ATOM   630  C CD    . LYS A 1 99  ? 7.356  8.532   -12.820 1.00 54.63 ? 90  LYS A CD    1 
ATOM   631  C CE    . LYS A 1 99  ? 5.837  8.567   -12.869 1.00 56.27 ? 90  LYS A CE    1 
ATOM   632  N NZ    . LYS A 1 99  ? 5.329  8.430   -14.261 1.00 62.28 ? 90  LYS A NZ    1 
ATOM   633  N N     . LYS A 1 100 ? 9.410  4.261   -14.680 1.00 40.41 ? 91  LYS A N     1 
ATOM   634  C CA    . LYS A 1 100 ? 8.685  3.253   -15.448 1.00 34.26 ? 91  LYS A CA    1 
ATOM   635  C C     . LYS A 1 100 ? 8.712  1.896   -14.759 1.00 36.70 ? 91  LYS A C     1 
ATOM   636  O O     . LYS A 1 100 ? 7.745  1.133   -14.854 1.00 41.09 ? 91  LYS A O     1 
ATOM   637  C CB    . LYS A 1 100 ? 9.270  3.145   -16.856 1.00 44.10 ? 91  LYS A CB    1 
ATOM   638  C CG    . LYS A 1 100 ? 9.584  4.485   -17.502 1.00 41.65 ? 91  LYS A CG    1 
ATOM   639  C CD    . LYS A 1 100 ? 10.673 4.347   -18.552 1.00 50.23 ? 91  LYS A CD    1 
ATOM   640  C CE    . LYS A 1 100 ? 10.217 4.896   -19.893 1.00 41.93 ? 91  LYS A CE    1 
ATOM   641  N NZ    . LYS A 1 100 ? 11.353 5.449   -20.678 1.00 56.98 ? 91  LYS A NZ    1 
ATOM   642  N N     . ILE A 1 101 ? 9.805  1.578   -14.064 1.00 36.35 ? 92  ILE A N     1 
ATOM   643  C CA    . ILE A 1 101 ? 9.882  0.317   -13.335 1.00 39.35 ? 92  ILE A CA    1 
ATOM   644  C C     . ILE A 1 101 ? 8.979  0.353   -12.109 1.00 34.59 ? 92  ILE A C     1 
ATOM   645  O O     . ILE A 1 101 ? 8.313  -0.637  -11.780 1.00 40.43 ? 92  ILE A O     1 
ATOM   646  C CB    . ILE A 1 101 ? 11.344 0.015   -12.959 1.00 42.93 ? 92  ILE A CB    1 
ATOM   647  C CG1   . ILE A 1 101 ? 12.183 -0.167  -14.224 1.00 41.81 ? 92  ILE A CG1   1 
ATOM   648  C CG2   . ILE A 1 101 ? 11.434 -1.214  -12.065 1.00 41.84 ? 92  ILE A CG2   1 
ATOM   649  C CD1   . ILE A 1 101 ? 13.593 0.350   -14.095 1.00 40.05 ? 92  ILE A CD1   1 
ATOM   650  N N     . VAL A 1 102 ? 8.932  1.494   -11.421 1.00 43.01 ? 93  VAL A N     1 
ATOM   651  C CA    . VAL A 1 102 ? 8.089  1.616   -10.236 1.00 37.58 ? 93  VAL A CA    1 
ATOM   652  C C     . VAL A 1 102 ? 6.615  1.540   -10.618 1.00 39.06 ? 93  VAL A C     1 
ATOM   653  O O     . VAL A 1 102 ? 5.804  0.935   -9.904  1.00 42.42 ? 93  VAL A O     1 
ATOM   654  C CB    . VAL A 1 102 ? 8.422  2.919   -9.485  1.00 43.67 ? 93  VAL A CB    1 
ATOM   655  C CG1   . VAL A 1 102 ? 7.298  3.299   -8.532  1.00 43.22 ? 93  VAL A CG1   1 
ATOM   656  C CG2   . VAL A 1 102 ? 9.739  2.775   -8.740  1.00 37.15 ? 93  VAL A CG2   1 
ATOM   657  N N     . ASP A 1 103 ? 6.245  2.139   -11.753 1.00 41.68 ? 94  ASP A N     1 
ATOM   658  C CA    . ASP A 1 103 ? 4.852  2.108   -12.187 1.00 43.51 ? 94  ASP A CA    1 
ATOM   659  C C     . ASP A 1 103 ? 4.394  0.683   -12.473 1.00 38.59 ? 94  ASP A C     1 
ATOM   660  O O     . ASP A 1 103 ? 3.256  0.312   -12.162 1.00 42.25 ? 94  ASP A O     1 
ATOM   661  C CB    . ASP A 1 103 ? 4.670  2.989   -13.424 1.00 41.22 ? 94  ASP A CB    1 
ATOM   662  C CG    . ASP A 1 103 ? 4.638  4.468   -13.087 1.00 50.96 ? 94  ASP A CG    1 
ATOM   663  O OD1   . ASP A 1 103 ? 4.451  4.804   -11.899 1.00 49.20 ? 94  ASP A OD1   1 
ATOM   664  O OD2   . ASP A 1 103 ? 4.800  5.295   -14.010 1.00 50.27 ? 94  ASP A OD2   1 
ATOM   665  N N     . VAL A 1 104 ? 5.269  -0.131  -13.062 1.00 42.69 ? 95  VAL A N     1 
ATOM   666  C CA    . VAL A 1 104 ? 4.908  -1.510  -13.369 1.00 40.90 ? 95  VAL A CA    1 
ATOM   667  C C     . VAL A 1 104 ? 4.804  -2.332  -12.088 1.00 38.28 ? 95  VAL A C     1 
ATOM   668  O O     . VAL A 1 104 ? 3.916  -3.182  -11.948 1.00 41.14 ? 95  VAL A O     1 
ATOM   669  C CB    . VAL A 1 104 ? 5.924  -2.104  -14.361 1.00 39.63 ? 95  VAL A CB    1 
ATOM   670  C CG1   . VAL A 1 104 ? 5.823  -3.606  -14.392 1.00 46.63 ? 95  VAL A CG1   1 
ATOM   671  C CG2   . VAL A 1 104 ? 5.700  -1.528  -15.750 1.00 41.76 ? 95  VAL A CG2   1 
ATOM   672  N N     . VAL A 1 105 ? 5.694  -2.081  -11.127 1.00 38.39 ? 96  VAL A N     1 
ATOM   673  C CA    . VAL A 1 105 ? 5.631  -2.792  -9.853  1.00 41.44 ? 96  VAL A CA    1 
ATOM   674  C C     . VAL A 1 105 ? 4.372  -2.405  -9.086  1.00 40.24 ? 96  VAL A C     1 
ATOM   675  O O     . VAL A 1 105 ? 3.691  -3.263  -8.509  1.00 38.43 ? 96  VAL A O     1 
ATOM   676  C CB    . VAL A 1 105 ? 6.905  -2.522  -9.031  1.00 39.42 ? 96  VAL A CB    1 
ATOM   677  C CG1   . VAL A 1 105 ? 6.683  -2.862  -7.562  1.00 45.18 ? 96  VAL A CG1   1 
ATOM   678  C CG2   . VAL A 1 105 ? 8.072  -3.312  -9.594  1.00 39.15 ? 96  VAL A CG2   1 
ATOM   679  N N     . HIS A 1 106 ? 4.035  -1.112  -9.076  1.00 40.30 ? 97  HIS A N     1 
ATOM   680  C CA    . HIS A 1 106 ? 2.852  -0.661  -8.350  1.00 35.11 ? 97  HIS A CA    1 
ATOM   681  C C     . HIS A 1 106 ? 1.566  -1.174  -8.986  1.00 38.13 ? 97  HIS A C     1 
ATOM   682  O O     . HIS A 1 106 ? 0.568  -1.370  -8.284  1.00 39.94 ? 97  HIS A O     1 
ATOM   683  C CB    . HIS A 1 106 ? 2.832  0.867   -8.273  1.00 32.97 ? 97  HIS A CB    1 
ATOM   684  C CG    . HIS A 1 106 ? 3.682  1.429   -7.176  1.00 43.47 ? 97  HIS A CG    1 
ATOM   685  N ND1   . HIS A 1 106 ? 4.151  2.725   -7.188  1.00 38.02 ? 97  HIS A ND1   1 
ATOM   686  C CD2   . HIS A 1 106 ? 4.148  0.872   -6.033  1.00 41.25 ? 97  HIS A CD2   1 
ATOM   687  C CE1   . HIS A 1 106 ? 4.867  2.942   -6.099  1.00 45.96 ? 97  HIS A CE1   1 
ATOM   688  N NE2   . HIS A 1 106 ? 4.881  1.833   -5.381  1.00 42.00 ? 97  HIS A NE2   1 
ATOM   689  N N     . ALA A 1 107 ? 1.570  -1.406  -10.303 1.00 37.88 ? 98  ALA A N     1 
ATOM   690  C CA    . ALA A 1 107 ? 0.369  -1.905  -10.968 1.00 37.95 ? 98  ALA A CA    1 
ATOM   691  C C     . ALA A 1 107 ? -0.048 -3.267  -10.428 1.00 40.49 ? 98  ALA A C     1 
ATOM   692  O O     . ALA A 1 107 ? -1.233 -3.615  -10.471 1.00 43.07 ? 98  ALA A O     1 
ATOM   693  C CB    . ALA A 1 107 ? 0.592  -1.977  -12.479 1.00 40.28 ? 98  ALA A CB    1 
ATOM   694  N N     . LYS A 1 108 ? 0.900  -4.045  -9.915  1.00 36.43 ? 99  LYS A N     1 
ATOM   695  C CA    . LYS A 1 108 ? 0.595  -5.327  -9.298  1.00 38.41 ? 99  LYS A CA    1 
ATOM   696  C C     . LYS A 1 108 ? 0.262  -5.204  -7.817  1.00 42.85 ? 99  LYS A C     1 
ATOM   697  O O     . LYS A 1 108 ? 0.021  -6.224  -7.163  1.00 44.06 ? 99  LYS A O     1 
ATOM   698  C CB    . LYS A 1 108 ? 1.766  -6.296  -9.490  1.00 42.19 ? 99  LYS A CB    1 
ATOM   699  N N     . GLY A 1 109 ? 0.245  -3.990  -7.274  1.00 38.01 ? 100 GLY A N     1 
ATOM   700  C CA    . GLY A 1 109 ? -0.131 -3.791  -5.887  1.00 45.33 ? 100 GLY A CA    1 
ATOM   701  C C     . GLY A 1 109 ? 0.949  -4.107  -4.876  1.00 44.85 ? 100 GLY A C     1 
ATOM   702  O O     . GLY A 1 109 ? 0.651  -4.661  -3.810  1.00 54.12 ? 100 GLY A O     1 
ATOM   703  N N     . ALA A 1 110 ? 2.199  -3.761  -5.173  1.00 42.14 ? 101 ALA A N     1 
ATOM   704  C CA    . ALA A 1 110 ? 3.320  -4.041  -4.291  1.00 42.60 ? 101 ALA A CA    1 
ATOM   705  C C     . ALA A 1 110 ? 3.943  -2.743  -3.794  1.00 41.19 ? 101 ALA A C     1 
ATOM   706  O O     . ALA A 1 110 ? 3.775  -1.677  -4.391  1.00 38.98 ? 101 ALA A O     1 
ATOM   707  C CB    . ALA A 1 110 ? 4.387  -4.890  -4.996  1.00 39.61 ? 101 ALA A CB    1 
ATOM   708  N N     . VAL A 1 111 ? 4.667  -2.854  -2.681  1.00 42.29 ? 102 VAL A N     1 
ATOM   709  C CA    . VAL A 1 111 ? 5.421  -1.750  -2.097  1.00 39.15 ? 102 VAL A CA    1 
ATOM   710  C C     . VAL A 1 111 ? 6.892  -1.966  -2.419  1.00 37.87 ? 102 VAL A C     1 
ATOM   711  O O     . VAL A 1 111 ? 7.407  -3.082  -2.272  1.00 38.67 ? 102 VAL A O     1 
ATOM   712  C CB    . VAL A 1 111 ? 5.192  -1.664  -0.577  1.00 40.90 ? 102 VAL A CB    1 
ATOM   713  C CG1   . VAL A 1 111 ? 5.938  -0.476  0.015   1.00 38.47 ? 102 VAL A CG1   1 
ATOM   714  C CG2   . VAL A 1 111 ? 3.706  -1.576  -0.268  1.00 42.33 ? 102 VAL A CG2   1 
ATOM   715  N N     . ILE A 1 112 ? 7.573  -0.910  -2.863  1.00 39.06 ? 103 ILE A N     1 
ATOM   716  C CA    . ILE A 1 112 ? 8.946  -1.021  -3.338  1.00 30.67 ? 103 ILE A CA    1 
ATOM   717  C C     . ILE A 1 112 ? 9.784  0.099   -2.733  1.00 34.98 ? 103 ILE A C     1 
ATOM   718  O O     . ILE A 1 112 ? 9.388  1.270   -2.766  1.00 35.29 ? 103 ILE A O     1 
ATOM   719  C CB    . ILE A 1 112 ? 9.018  -1.003  -4.881  1.00 38.06 ? 103 ILE A CB    1 
ATOM   720  C CG1   . ILE A 1 112 ? 10.461 -1.168  -5.360  1.00 34.10 ? 103 ILE A CG1   1 
ATOM   721  C CG2   . ILE A 1 112 ? 8.381  0.259   -5.459  1.00 35.39 ? 103 ILE A CG2   1 
ATOM   722  C CD1   . ILE A 1 112 ? 10.575 -1.725  -6.771  1.00 36.88 ? 103 ILE A CD1   1 
ATOM   723  N N     . PHE A 1 113 ? 10.933 -0.267  -2.169  1.00 32.95 ? 104 PHE A N     1 
ATOM   724  C CA    . PHE A 1 113 ? 11.896 0.672   -1.610  1.00 32.65 ? 104 PHE A CA    1 
ATOM   725  C C     . PHE A 1 113 ? 13.176 0.639   -2.432  1.00 30.85 ? 104 PHE A C     1 
ATOM   726  O O     . PHE A 1 113 ? 13.616 -0.431  -2.862  1.00 32.21 ? 104 PHE A O     1 
ATOM   727  C CB    . PHE A 1 113 ? 12.224 0.329   -0.152  1.00 31.74 ? 104 PHE A CB    1 
ATOM   728  C CG    . PHE A 1 113 ? 11.301 0.961   0.851   1.00 32.77 ? 104 PHE A CG    1 
ATOM   729  C CD1   . PHE A 1 113 ? 9.981  1.231   0.532   1.00 35.89 ? 104 PHE A CD1   1 
ATOM   730  C CD2   . PHE A 1 113 ? 11.758 1.279   2.120   1.00 36.05 ? 104 PHE A CD2   1 
ATOM   731  C CE1   . PHE A 1 113 ? 9.132  1.807   1.461   1.00 42.61 ? 104 PHE A CE1   1 
ATOM   732  C CE2   . PHE A 1 113 ? 10.916 1.857   3.051   1.00 33.01 ? 104 PHE A CE2   1 
ATOM   733  C CZ    . PHE A 1 113 ? 9.601  2.122   2.721   1.00 38.29 ? 104 PHE A CZ    1 
ATOM   734  N N     . CYS A 1 114 ? 13.777 1.809   -2.641  1.00 24.25 ? 105 CYS A N     1 
ATOM   735  C CA    . CYS A 1 114 ? 15.059 1.906   -3.330  1.00 33.60 ? 105 CYS A CA    1 
ATOM   736  C C     . CYS A 1 114 ? 16.189 1.932   -2.308  1.00 34.19 ? 105 CYS A C     1 
ATOM   737  O O     . CYS A 1 114 ? 16.197 2.776   -1.407  1.00 34.95 ? 105 CYS A O     1 
ATOM   738  C CB    . CYS A 1 114 ? 15.110 3.158   -4.209  1.00 33.13 ? 105 CYS A CB    1 
ATOM   739  S SG    . CYS A 1 114 ? 16.738 3.491   -4.938  1.00 41.14 ? 105 CYS A SG    1 
ATOM   740  N N     . GLN A 1 115 ? 17.142 1.012   -2.448  1.00 30.47 ? 106 GLN A N     1 
ATOM   741  C CA    . GLN A 1 115 ? 18.273 0.936   -1.530  1.00 30.49 ? 106 GLN A CA    1 
ATOM   742  C C     . GLN A 1 115 ? 19.364 1.899   -1.982  1.00 34.49 ? 106 GLN A C     1 
ATOM   743  O O     . GLN A 1 115 ? 19.851 1.810   -3.115  1.00 33.28 ? 106 GLN A O     1 
ATOM   744  C CB    . GLN A 1 115 ? 18.824 -0.487  -1.439  1.00 29.94 ? 106 GLN A CB    1 
ATOM   745  C CG    . GLN A 1 115 ? 19.763 -0.681  -0.248  1.00 34.23 ? 106 GLN A CG    1 
ATOM   746  C CD    . GLN A 1 115 ? 20.600 -1.943  -0.335  1.00 35.92 ? 106 GLN A CD    1 
ATOM   747  O OE1   . GLN A 1 115 ? 21.176 -2.252  -1.378  1.00 34.05 ? 106 GLN A OE1   1 
ATOM   748  N NE2   . GLN A 1 115 ? 20.680 -2.675  0.771   1.00 31.51 ? 106 GLN A NE2   1 
ATOM   749  N N     . LEU A 1 116 ? 19.746 2.815   -1.094  1.00 32.01 ? 107 LEU A N     1 
ATOM   750  C CA    . LEU A 1 116 ? 20.817 3.770   -1.359  1.00 31.33 ? 107 LEU A CA    1 
ATOM   751  C C     . LEU A 1 116 ? 22.134 3.168   -0.885  1.00 33.18 ? 107 LEU A C     1 
ATOM   752  O O     . LEU A 1 116 ? 22.285 2.845   0.298   1.00 28.31 ? 107 LEU A O     1 
ATOM   753  C CB    . LEU A 1 116 ? 20.539 5.100   -0.659  1.00 31.90 ? 107 LEU A CB    1 
ATOM   754  C CG    . LEU A 1 116 ? 19.174 5.721   -0.965  1.00 32.43 ? 107 LEU A CG    1 
ATOM   755  C CD1   . LEU A 1 116 ? 19.058 7.122   -0.378  1.00 28.92 ? 107 LEU A CD1   1 
ATOM   756  C CD2   . LEU A 1 116 ? 18.925 5.742   -2.469  1.00 38.14 ? 107 LEU A CD2   1 
ATOM   757  N N     . TRP A 1 117 ? 23.088 3.029   -1.805  1.00 29.09 ? 108 TRP A N     1 
ATOM   758  C CA    . TRP A 1 117 ? 24.274 2.209   -1.586  1.00 30.47 ? 108 TRP A CA    1 
ATOM   759  C C     . TRP A 1 117 ? 25.514 2.965   -2.040  1.00 36.55 ? 108 TRP A C     1 
ATOM   760  O O     . TRP A 1 117 ? 25.646 3.297   -3.224  1.00 36.89 ? 108 TRP A O     1 
ATOM   761  C CB    . TRP A 1 117 ? 24.141 0.879   -2.335  1.00 34.34 ? 108 TRP A CB    1 
ATOM   762  C CG    . TRP A 1 117 ? 25.343 -0.013  -2.285  1.00 30.54 ? 108 TRP A CG    1 
ATOM   763  C CD1   . TRP A 1 117 ? 26.236 -0.143  -1.261  1.00 33.23 ? 108 TRP A CD1   1 
ATOM   764  C CD2   . TRP A 1 117 ? 25.773 -0.917  -3.310  1.00 38.51 ? 108 TRP A CD2   1 
ATOM   765  N NE1   . TRP A 1 117 ? 27.200 -1.070  -1.589  1.00 30.73 ? 108 TRP A NE1   1 
ATOM   766  C CE2   . TRP A 1 117 ? 26.935 -1.560  -2.841  1.00 34.24 ? 108 TRP A CE2   1 
ATOM   767  C CE3   . TRP A 1 117 ? 25.287 -1.244  -4.581  1.00 32.63 ? 108 TRP A CE3   1 
ATOM   768  C CZ2   . TRP A 1 117 ? 27.620 -2.508  -3.599  1.00 34.91 ? 108 TRP A CZ2   1 
ATOM   769  C CZ3   . TRP A 1 117 ? 25.966 -2.187  -5.330  1.00 36.65 ? 108 TRP A CZ3   1 
ATOM   770  C CH2   . TRP A 1 117 ? 27.119 -2.808  -4.838  1.00 31.86 ? 108 TRP A CH2   1 
ATOM   771  N N     . HIS A 1 118 ? 26.414 3.236   -1.098  1.00 32.79 ? 109 HIS A N     1 
ATOM   772  C CA    . HIS A 1 118 ? 27.731 3.796   -1.377  1.00 32.58 ? 109 HIS A CA    1 
ATOM   773  C C     . HIS A 1 118 ? 28.769 2.770   -0.944  1.00 34.35 ? 109 HIS A C     1 
ATOM   774  O O     . HIS A 1 118 ? 28.793 2.368   0.224   1.00 39.71 ? 109 HIS A O     1 
ATOM   775  C CB    . HIS A 1 118 ? 27.930 5.124   -0.642  1.00 30.99 ? 109 HIS A CB    1 
ATOM   776  C CG    . HIS A 1 118 ? 29.079 5.936   -1.152  1.00 35.60 ? 109 HIS A CG    1 
ATOM   777  N ND1   . HIS A 1 118 ? 30.339 5.410   -1.343  1.00 29.66 ? 109 HIS A ND1   1 
ATOM   778  C CD2   . HIS A 1 118 ? 29.161 7.243   -1.501  1.00 36.31 ? 109 HIS A CD2   1 
ATOM   779  C CE1   . HIS A 1 118 ? 31.146 6.355   -1.792  1.00 34.50 ? 109 HIS A CE1   1 
ATOM   780  N NE2   . HIS A 1 118 ? 30.455 7.477   -1.897  1.00 32.12 ? 109 HIS A NE2   1 
ATOM   781  N N     . VAL A 1 119 ? 29.618 2.344   -1.881  1.00 31.60 ? 110 VAL A N     1 
ATOM   782  C CA    . VAL A 1 119 ? 30.555 1.260   -1.596  1.00 38.16 ? 110 VAL A CA    1 
ATOM   783  C C     . VAL A 1 119 ? 31.756 1.712   -0.779  1.00 35.47 ? 110 VAL A C     1 
ATOM   784  O O     . VAL A 1 119 ? 32.446 0.869   -0.192  1.00 29.69 ? 110 VAL A O     1 
ATOM   785  C CB    . VAL A 1 119 ? 31.055 0.600   -2.892  1.00 36.09 ? 110 VAL A CB    1 
ATOM   786  C CG1   . VAL A 1 119 ? 29.889 0.079   -3.704  1.00 30.10 ? 110 VAL A CG1   1 
ATOM   787  C CG2   . VAL A 1 119 ? 31.879 1.584   -3.706  1.00 35.79 ? 110 VAL A CG2   1 
ATOM   788  N N     . GLY A 1 120 ? 32.035 3.009   -0.727  1.00 36.93 ? 111 GLY A N     1 
ATOM   789  C CA    . GLY A 1 120 ? 33.202 3.461   0.010   1.00 32.80 ? 111 GLY A CA    1 
ATOM   790  C C     . GLY A 1 120 ? 34.477 2.932   -0.616  1.00 35.80 ? 111 GLY A C     1 
ATOM   791  O O     . GLY A 1 120 ? 34.712 3.076   -1.821  1.00 33.37 ? 111 GLY A O     1 
ATOM   792  N N     . ARG A 1 121 ? 35.314 2.303   0.212   1.00 29.33 ? 112 ARG A N     1 
ATOM   793  C CA    . ARG A 1 121 ? 36.610 1.804   -0.235  1.00 29.42 ? 112 ARG A CA    1 
ATOM   794  C C     . ARG A 1 121 ? 36.511 0.527   -1.059  1.00 32.78 ? 112 ARG A C     1 
ATOM   795  O O     . ARG A 1 121 ? 37.515 0.112   -1.647  1.00 30.80 ? 112 ARG A O     1 
ATOM   796  C CB    . ARG A 1 121 ? 37.525 1.561   0.968   1.00 28.14 ? 112 ARG A CB    1 
ATOM   797  C CG    . ARG A 1 121 ? 37.303 0.230   1.670   1.00 33.64 ? 112 ARG A CG    1 
ATOM   798  C CD    . ARG A 1 121 ? 38.066 0.162   2.989   1.00 29.59 ? 112 ARG A CD    1 
ATOM   799  N NE    . ARG A 1 121 ? 37.794 -1.075  3.712   1.00 36.43 ? 112 ARG A NE    1 
ATOM   800  C CZ    . ARG A 1 121 ? 38.611 -1.622  4.602   1.00 28.97 ? 112 ARG A CZ    1 
ATOM   801  N NH1   . ARG A 1 121 ? 39.761 -1.054  4.926   1.00 29.74 ? 112 ARG A NH1   1 
ATOM   802  N NH2   . ARG A 1 121 ? 38.267 -2.769  5.179   1.00 30.49 ? 112 ARG A NH2   1 
ATOM   803  N N     . ALA A 1 122 ? 35.340 -0.105  -1.119  1.00 28.64 ? 113 ALA A N     1 
ATOM   804  C CA    . ALA A 1 122 ? 35.163 -1.329  -1.900  1.00 31.35 ? 113 ALA A CA    1 
ATOM   805  C C     . ALA A 1 122 ? 34.858 -0.962  -3.352  1.00 31.81 ? 113 ALA A C     1 
ATOM   806  O O     . ALA A 1 122 ? 33.773 -1.202  -3.882  1.00 32.97 ? 113 ALA A O     1 
ATOM   807  C CB    . ALA A 1 122 ? 34.067 -2.196  -1.295  1.00 28.64 ? 113 ALA A CB    1 
ATOM   808  N N     . SER A 1 123 ? 35.849 -0.354  -3.991  1.00 33.47 ? 114 SER A N     1 
ATOM   809  C CA    . SER A 1 123 ? 35.701 0.101   -5.367  1.00 37.16 ? 114 SER A CA    1 
ATOM   810  C C     . SER A 1 123 ? 37.039 -0.074  -6.077  1.00 34.09 ? 114 SER A C     1 
ATOM   811  O O     . SER A 1 123 ? 37.926 -0.788  -5.596  1.00 39.65 ? 114 SER A O     1 
ATOM   812  C CB    . SER A 1 123 ? 35.192 1.552   -5.403  1.00 39.52 ? 114 SER A CB    1 
ATOM   813  O OG    . SER A 1 123 ? 34.690 1.877   -6.688  1.00 31.77 ? 114 SER A OG    1 
ATOM   814  N N     . HIS A 1 124 ? 37.182 0.581   -7.224  1.00 36.69 ? 115 HIS A N     1 
ATOM   815  C CA    . HIS A 1 124 ? 38.370 0.467   -8.055  1.00 36.15 ? 115 HIS A CA    1 
ATOM   816  C C     . HIS A 1 124 ? 38.417 1.679   -8.971  1.00 32.09 ? 115 HIS A C     1 
ATOM   817  O O     . HIS A 1 124 ? 37.391 2.305   -9.248  1.00 37.29 ? 115 HIS A O     1 
ATOM   818  C CB    . HIS A 1 124 ? 38.364 -0.836  -8.866  1.00 38.07 ? 115 HIS A CB    1 
ATOM   819  C CG    . HIS A 1 124 ? 39.672 -1.151  -9.526  1.00 39.79 ? 115 HIS A CG    1 
ATOM   820  N ND1   . HIS A 1 124 ? 40.076 -0.555  -10.701 1.00 35.61 ? 115 HIS A ND1   1 
ATOM   821  C CD2   . HIS A 1 124 ? 40.659 -2.013  -9.184  1.00 33.10 ? 115 HIS A CD2   1 
ATOM   822  C CE1   . HIS A 1 124 ? 41.260 -1.028  -11.048 1.00 38.13 ? 115 HIS A CE1   1 
ATOM   823  N NE2   . HIS A 1 124 ? 41.635 -1.916  -10.145 1.00 39.90 ? 115 HIS A NE2   1 
ATOM   824  N N     . GLU A 1 125 ? 39.627 2.008   -9.432  1.00 36.72 ? 116 GLU A N     1 
ATOM   825  C CA    . GLU A 1 125 ? 39.796 3.154   -10.321 1.00 37.58 ? 116 GLU A CA    1 
ATOM   826  C C     . GLU A 1 125 ? 38.936 3.034   -11.572 1.00 34.94 ? 116 GLU A C     1 
ATOM   827  O O     . GLU A 1 125 ? 38.542 4.052   -12.151 1.00 41.43 ? 116 GLU A O     1 
ATOM   828  C CB    . GLU A 1 125 ? 41.268 3.308   -10.705 1.00 38.97 ? 116 GLU A CB    1 
ATOM   829  N N     . VAL A 1 126 ? 38.631 1.806   -12.004 1.00 32.13 ? 117 VAL A N     1 
ATOM   830  C CA    . VAL A 1 126 ? 37.789 1.620   -13.180 1.00 34.46 ? 117 VAL A CA    1 
ATOM   831  C C     . VAL A 1 126 ? 36.346 2.023   -12.907 1.00 37.43 ? 117 VAL A C     1 
ATOM   832  O O     . VAL A 1 126 ? 35.596 2.309   -13.848 1.00 32.63 ? 117 VAL A O     1 
ATOM   833  C CB    . VAL A 1 126 ? 37.871 0.163   -13.678 1.00 38.32 ? 117 VAL A CB    1 
ATOM   834  C CG1   . VAL A 1 126 ? 36.957 -0.743  -12.864 1.00 33.62 ? 117 VAL A CG1   1 
ATOM   835  C CG2   . VAL A 1 126 ? 37.526 0.082   -15.158 1.00 35.10 ? 117 VAL A CG2   1 
ATOM   836  N N     . TYR A 1 127 ? 35.934 2.068   -11.642 1.00 41.57 ? 118 TYR A N     1 
ATOM   837  C CA    . TYR A 1 127 ? 34.583 2.473   -11.279 1.00 36.66 ? 118 TYR A CA    1 
ATOM   838  C C     . TYR A 1 127 ? 34.505 3.918   -10.813 1.00 36.13 ? 118 TYR A C     1 
ATOM   839  O O     . TYR A 1 127 ? 33.411 4.392   -10.494 1.00 36.47 ? 118 TYR A O     1 
ATOM   840  C CB    . TYR A 1 127 ? 34.030 1.547   -10.191 1.00 32.33 ? 118 TYR A CB    1 
ATOM   841  C CG    . TYR A 1 127 ? 33.935 0.105   -10.626 1.00 38.02 ? 118 TYR A CG    1 
ATOM   842  C CD1   . TYR A 1 127 ? 33.260 -0.245  -11.787 1.00 34.00 ? 118 TYR A CD1   1 
ATOM   843  C CD2   . TYR A 1 127 ? 34.529 -0.906  -9.882  1.00 35.71 ? 118 TYR A CD2   1 
ATOM   844  C CE1   . TYR A 1 127 ? 33.172 -1.562  -12.193 1.00 36.08 ? 118 TYR A CE1   1 
ATOM   845  C CE2   . TYR A 1 127 ? 34.445 -2.228  -10.280 1.00 31.49 ? 118 TYR A CE2   1 
ATOM   846  C CZ    . TYR A 1 127 ? 33.765 -2.548  -11.435 1.00 30.98 ? 118 TYR A CZ    1 
ATOM   847  O OH    . TYR A 1 127 ? 33.680 -3.859  -11.837 1.00 31.61 ? 118 TYR A OH    1 
ATOM   848  N N     . GLN A 1 128 ? 35.632 4.629   -10.771 1.00 35.19 ? 119 GLN A N     1 
ATOM   849  C CA    . GLN A 1 128 ? 35.659 5.992   -10.272 1.00 38.96 ? 119 GLN A CA    1 
ATOM   850  C C     . GLN A 1 128 ? 35.905 6.985   -11.402 1.00 44.71 ? 119 GLN A C     1 
ATOM   851  O O     . GLN A 1 128 ? 36.644 6.680   -12.346 1.00 36.98 ? 119 GLN A O     1 
ATOM   852  C CB    . GLN A 1 128 ? 36.746 6.160   -9.207  1.00 36.49 ? 119 GLN A CB    1 
ATOM   853  C CG    . GLN A 1 128 ? 36.557 5.274   -7.987  1.00 37.80 ? 119 GLN A CG    1 
ATOM   854  C CD    . GLN A 1 128 ? 35.336 5.659   -7.179  1.00 37.25 ? 119 GLN A CD    1 
ATOM   855  O OE1   . GLN A 1 128 ? 35.001 6.838   -7.066  1.00 42.16 ? 119 GLN A OE1   1 
ATOM   856  N NE2   . GLN A 1 128 ? 34.663 4.665   -6.610  1.00 38.28 ? 119 GLN A NE2   1 
ATOM   857  N N     . PRO A 1 129 ? 35.300 8.170   -11.337 1.00 45.67 ? 120 PRO A N     1 
ATOM   858  C CA    . PRO A 1 129 ? 35.573 9.194   -12.354 1.00 42.05 ? 120 PRO A CA    1 
ATOM   859  C C     . PRO A 1 129 ? 37.037 9.611   -12.333 1.00 45.31 ? 120 PRO A C     1 
ATOM   860  O O     . PRO A 1 129 ? 37.623 9.834   -11.270 1.00 36.16 ? 120 PRO A O     1 
ATOM   861  C CB    . PRO A 1 129 ? 34.646 10.349  -11.952 1.00 47.78 ? 120 PRO A CB    1 
ATOM   862  C CG    . PRO A 1 129 ? 33.582 9.716   -11.103 1.00 43.41 ? 120 PRO A CG    1 
ATOM   863  C CD    . PRO A 1 129 ? 34.256 8.589   -10.386 1.00 40.62 ? 120 PRO A CD    1 
ATOM   864  N N     . ALA A 1 130 ? 37.627 9.699   -13.527 1.00 37.43 ? 121 ALA A N     1 
ATOM   865  C CA    . ALA A 1 130 ? 39.029 10.063  -13.731 1.00 35.06 ? 121 ALA A CA    1 
ATOM   866  C C     . ALA A 1 130 ? 39.992 9.101   -13.043 1.00 38.20 ? 121 ALA A C     1 
ATOM   867  O O     . ALA A 1 130 ? 41.145 9.459   -12.774 1.00 40.22 ? 121 ALA A O     1 
ATOM   868  C CB    . ALA A 1 130 ? 39.306 11.501  -13.273 1.00 46.43 ? 121 ALA A CB    1 
ATOM   869  N N     . GLY A 1 131 ? 39.547 7.879   -12.758 1.00 42.90 ? 122 GLY A N     1 
ATOM   870  C CA    . GLY A 1 131 ? 40.404 6.908   -12.098 1.00 41.26 ? 122 GLY A CA    1 
ATOM   871  C C     . GLY A 1 131 ? 40.842 7.317   -10.711 1.00 41.35 ? 122 GLY A C     1 
ATOM   872  O O     . GLY A 1 131 ? 41.897 6.875   -10.244 1.00 47.66 ? 122 GLY A O     1 
ATOM   873  N N     . ALA A 1 132 ? 40.060 8.156   -10.037 1.00 36.07 ? 123 ALA A N     1 
ATOM   874  C CA    . ALA A 1 132 ? 40.429 8.631   -8.714  1.00 43.66 ? 123 ALA A CA    1 
ATOM   875  C C     . ALA A 1 132 ? 40.302 7.515   -7.681  1.00 41.95 ? 123 ALA A C     1 
ATOM   876  O O     . ALA A 1 132 ? 39.615 6.511   -7.886  1.00 39.45 ? 123 ALA A O     1 
ATOM   877  C CB    . ALA A 1 132 ? 39.558 9.820   -8.308  1.00 35.40 ? 123 ALA A CB    1 
ATOM   878  N N     . ALA A 1 133 ? 40.981 7.706   -6.556  1.00 43.54 ? 124 ALA A N     1 
ATOM   879  C CA    . ALA A 1 133 ? 40.921 6.728   -5.482  1.00 40.16 ? 124 ALA A CA    1 
ATOM   880  C C     . ALA A 1 133 ? 39.549 6.767   -4.814  1.00 41.61 ? 124 ALA A C     1 
ATOM   881  O O     . ALA A 1 133 ? 38.979 7.847   -4.627  1.00 40.32 ? 124 ALA A O     1 
ATOM   882  C CB    . ALA A 1 133 ? 42.010 6.999   -4.446  1.00 43.82 ? 124 ALA A CB    1 
ATOM   883  N N     . PRO A 1 134 ? 38.992 5.614   -4.447  1.00 40.13 ? 125 PRO A N     1 
ATOM   884  C CA    . PRO A 1 134 ? 37.725 5.614   -3.710  1.00 35.74 ? 125 PRO A CA    1 
ATOM   885  C C     . PRO A 1 134 ? 37.888 6.273   -2.348  1.00 31.74 ? 125 PRO A C     1 
ATOM   886  O O     . PRO A 1 134 ? 38.998 6.473   -1.851  1.00 36.47 ? 125 PRO A O     1 
ATOM   887  C CB    . PRO A 1 134 ? 37.386 4.123   -3.580  1.00 36.31 ? 125 PRO A CB    1 
ATOM   888  C CG    . PRO A 1 134 ? 38.700 3.424   -3.711  1.00 40.30 ? 125 PRO A CG    1 
ATOM   889  C CD    . PRO A 1 134 ? 39.515 4.254   -4.661  1.00 35.88 ? 125 PRO A CD    1 
ATOM   890  N N     . ILE A 1 135 ? 36.755 6.618   -1.743  1.00 28.40 ? 126 ILE A N     1 
ATOM   891  C CA    . ILE A 1 135 ? 36.727 7.364   -0.491  1.00 36.48 ? 126 ILE A CA    1 
ATOM   892  C C     . ILE A 1 135 ? 36.301 6.436   0.638   1.00 36.14 ? 126 ILE A C     1 
ATOM   893  O O     . ILE A 1 135 ? 35.595 5.447   0.421   1.00 34.04 ? 126 ILE A O     1 
ATOM   894  C CB    . ILE A 1 135 ? 35.788 8.583   -0.587  1.00 35.64 ? 126 ILE A CB    1 
ATOM   895  C CG1   . ILE A 1 135 ? 34.354 8.137   -0.879  1.00 34.87 ? 126 ILE A CG1   1 
ATOM   896  C CG2   . ILE A 1 135 ? 36.274 9.543   -1.660  1.00 41.03 ? 126 ILE A CG2   1 
ATOM   897  C CD1   . ILE A 1 135 ? 33.316 8.860   -0.054  1.00 39.67 ? 126 ILE A CD1   1 
ATOM   898  N N     . SER A 1 136 ? 36.730 6.763   1.854   1.00 38.04 ? 127 SER A N     1 
ATOM   899  C CA    . SER A 1 136 ? 36.423 5.930   3.010   1.00 32.30 ? 127 SER A CA    1 
ATOM   900  C C     . SER A 1 136 ? 36.701 6.720   4.282   1.00 35.30 ? 127 SER A C     1 
ATOM   901  O O     . SER A 1 136 ? 37.085 7.892   4.243   1.00 33.16 ? 127 SER A O     1 
ATOM   902  C CB    . SER A 1 136 ? 37.232 4.630   2.983   1.00 33.20 ? 127 SER A CB    1 
ATOM   903  O OG    . SER A 1 136 ? 36.778 3.731   3.978   1.00 39.25 ? 127 SER A OG    1 
ATOM   904  N N     . SER A 1 137 ? 36.499 6.056   5.422   1.00 31.46 ? 128 SER A N     1 
ATOM   905  C CA    . SER A 1 137 ? 36.816 6.661   6.708   1.00 36.24 ? 128 SER A CA    1 
ATOM   906  C C     . SER A 1 137 ? 38.314 6.661   6.979   1.00 37.30 ? 128 SER A C     1 
ATOM   907  O O     . SER A 1 137 ? 38.812 7.540   7.690   1.00 34.97 ? 128 SER A O     1 
ATOM   908  C CB    . SER A 1 137 ? 36.085 5.924   7.830   1.00 37.31 ? 128 SER A CB    1 
ATOM   909  O OG    . SER A 1 137 ? 36.258 4.522   7.713   1.00 35.06 ? 128 SER A OG    1 
ATOM   910  N N     . THR A 1 138 ? 39.038 5.695   6.421   1.00 39.07 ? 129 THR A N     1 
ATOM   911  C CA    . THR A 1 138 ? 40.465 5.529   6.649   1.00 42.25 ? 129 THR A CA    1 
ATOM   912  C C     . THR A 1 138 ? 41.166 5.336   5.311   1.00 42.21 ? 129 THR A C     1 
ATOM   913  O O     . THR A 1 138 ? 40.531 5.250   4.256   1.00 37.71 ? 129 THR A O     1 
ATOM   914  C CB    . THR A 1 138 ? 40.742 4.337   7.574   1.00 44.25 ? 129 THR A CB    1 
ATOM   915  O OG1   . THR A 1 138 ? 42.150 4.228   7.810   1.00 52.47 ? 129 THR A OG1   1 
ATOM   916  C CG2   . THR A 1 138 ? 40.249 3.051   6.935   1.00 42.31 ? 129 THR A CG2   1 
ATOM   917  N N     . GLU A 1 139 ? 42.494 5.272   5.363   1.00 42.49 ? 130 GLU A N     1 
ATOM   918  C CA    . GLU A 1 139 ? 43.315 4.985   4.196   1.00 42.75 ? 130 GLU A CA    1 
ATOM   919  C C     . GLU A 1 139 ? 43.677 3.511   4.083   1.00 45.24 ? 130 GLU A C     1 
ATOM   920  O O     . GLU A 1 139 ? 44.383 3.129   3.145   1.00 45.83 ? 130 GLU A O     1 
ATOM   921  C CB    . GLU A 1 139 ? 44.594 5.828   4.226   1.00 39.12 ? 130 GLU A CB    1 
ATOM   922  C CG    . GLU A 1 139 ? 44.373 7.308   3.964   1.00 45.01 ? 130 GLU A CG    1 
ATOM   923  C CD    . GLU A 1 139 ? 45.533 8.162   4.437   1.00 58.51 ? 130 GLU A CD    1 
ATOM   924  O OE1   . GLU A 1 139 ? 45.286 9.284   4.927   1.00 70.43 ? 130 GLU A OE1   1 
ATOM   925  O OE2   . GLU A 1 139 ? 46.691 7.710   4.320   1.00 63.63 ? 130 GLU A OE2   1 
ATOM   926  N N     . LYS A 1 140 ? 43.216 2.682   5.010   1.00 43.19 ? 131 LYS A N     1 
ATOM   927  C CA    . LYS A 1 140 ? 43.534 1.261   4.984   1.00 40.59 ? 131 LYS A CA    1 
ATOM   928  C C     . LYS A 1 140 ? 42.780 0.576   3.852   1.00 37.82 ? 131 LYS A C     1 
ATOM   929  O O     . LYS A 1 140 ? 41.548 0.677   3.791   1.00 36.78 ? 131 LYS A O     1 
ATOM   930  C CB    . LYS A 1 140 ? 43.185 0.615   6.321   1.00 34.07 ? 131 LYS A CB    1 
ATOM   931  N N     . PRO A 1 141 ? 43.459 -0.116  2.945   1.00 39.44 ? 132 PRO A N     1 
ATOM   932  C CA    . PRO A 1 141 ? 42.757 -0.823  1.874   1.00 37.88 ? 132 PRO A CA    1 
ATOM   933  C C     . PRO A 1 141 ? 42.215 -2.163  2.348   1.00 42.10 ? 132 PRO A C     1 
ATOM   934  O O     . PRO A 1 141 ? 42.634 -2.714  3.368   1.00 38.35 ? 132 PRO A O     1 
ATOM   935  C CB    . PRO A 1 141 ? 43.843 -1.016  0.812   1.00 39.06 ? 132 PRO A CB    1 
ATOM   936  C CG    . PRO A 1 141 ? 45.106 -1.114  1.604   1.00 46.46 ? 132 PRO A CG    1 
ATOM   937  C CD    . PRO A 1 141 ? 44.923 -0.256  2.836   1.00 42.74 ? 132 PRO A CD    1 
ATOM   938  N N     . ILE A 1 142 ? 41.253 -2.679  1.581   1.00 41.72 ? 133 ILE A N     1 
ATOM   939  C CA    . ILE A 1 142 ? 40.760 -4.026  1.828   1.00 43.05 ? 133 ILE A CA    1 
ATOM   940  C C     . ILE A 1 142 ? 41.888 -5.017  1.577   1.00 38.73 ? 133 ILE A C     1 
ATOM   941  O O     . ILE A 1 142 ? 42.672 -4.869  0.630   1.00 45.94 ? 133 ILE A O     1 
ATOM   942  C CB    . ILE A 1 142 ? 39.537 -4.320  0.943   1.00 38.76 ? 133 ILE A CB    1 
ATOM   943  C CG1   . ILE A 1 142 ? 38.424 -3.308  1.224   1.00 39.62 ? 133 ILE A CG1   1 
ATOM   944  C CG2   . ILE A 1 142 ? 39.031 -5.737  1.172   1.00 40.94 ? 133 ILE A CG2   1 
ATOM   945  C CD1   . ILE A 1 142 ? 37.140 -3.584  0.472   1.00 34.60 ? 133 ILE A CD1   1 
ATOM   946  N N     . SER A 1 143 ? 41.988 -6.025  2.442   1.00 42.29 ? 134 SER A N     1 
ATOM   947  C CA    . SER A 1 143 ? 43.071 -6.992  2.348   1.00 43.02 ? 134 SER A CA    1 
ATOM   948  C C     . SER A 1 143 ? 43.029 -7.732  1.014   1.00 43.25 ? 134 SER A C     1 
ATOM   949  O O     . SER A 1 143 ? 41.994 -7.814  0.345   1.00 42.88 ? 134 SER A O     1 
ATOM   950  C CB    . SER A 1 143 ? 42.997 -7.994  3.500   1.00 44.07 ? 134 SER A CB    1 
ATOM   951  O OG    . SER A 1 143 ? 43.401 -9.284  3.080   1.00 49.39 ? 134 SER A OG    1 
ATOM   952  N N     . ASN A 1 144 ? 44.184 -8.278  0.629   1.00 46.14 ? 135 ASN A N     1 
ATOM   953  C CA    . ASN A 1 144 ? 44.305 -9.002  -0.631  1.00 50.82 ? 135 ASN A CA    1 
ATOM   954  C C     . ASN A 1 144 ? 43.575 -10.339 -0.626  1.00 45.71 ? 135 ASN A C     1 
ATOM   955  O O     . ASN A 1 144 ? 43.523 -10.994 -1.673  1.00 47.57 ? 135 ASN A O     1 
ATOM   956  C CB    . ASN A 1 144 ? 45.783 -9.208  -0.976  1.00 51.96 ? 135 ASN A CB    1 
ATOM   957  C CG    . ASN A 1 144 ? 46.339 -10.514 -0.437  1.00 58.93 ? 135 ASN A CG    1 
ATOM   958  O OD1   . ASN A 1 144 ? 46.142 -10.856 0.730   1.00 60.38 ? 135 ASN A OD1   1 
ATOM   959  N ND2   . ASN A 1 144 ? 47.034 -11.254 -1.292  1.00 57.59 ? 135 ASN A ND2   1 
ATOM   960  N N     . ARG A 1 145 ? 43.013 -10.759 0.511   1.00 43.70 ? 136 ARG A N     1 
ATOM   961  C CA    . ARG A 1 145 ? 42.193 -11.965 0.525   1.00 48.24 ? 136 ARG A CA    1 
ATOM   962  C C     . ARG A 1 145 ? 40.927 -11.788 -0.302  1.00 42.25 ? 136 ARG A C     1 
ATOM   963  O O     . ARG A 1 145 ? 40.366 -12.774 -0.793  1.00 42.75 ? 136 ARG A O     1 
ATOM   964  C CB    . ARG A 1 145 ? 41.834 -12.344 1.962   1.00 45.38 ? 136 ARG A CB    1 
ATOM   965  C CG    . ARG A 1 145 ? 43.025 -12.498 2.894   1.00 55.68 ? 136 ARG A CG    1 
ATOM   966  C CD    . ARG A 1 145 ? 42.573 -12.572 4.344   1.00 63.41 ? 136 ARG A CD    1 
ATOM   967  N NE    . ARG A 1 145 ? 43.498 -13.337 5.172   1.00 70.46 ? 136 ARG A NE    1 
ATOM   968  C CZ    . ARG A 1 145 ? 44.130 -12.852 6.232   1.00 70.23 ? 136 ARG A CZ    1 
ATOM   969  N NH1   . ARG A 1 145 ? 43.959 -11.600 6.626   1.00 64.76 ? 136 ARG A NH1   1 
ATOM   970  N NH2   . ARG A 1 145 ? 44.952 -13.643 6.916   1.00 63.39 ? 136 ARG A NH2   1 
ATOM   971  N N     . TRP A 1 146 ? 40.466 -10.551 -0.464  1.00 42.60 ? 137 TRP A N     1 
ATOM   972  C CA    . TRP A 1 146 ? 39.284 -10.240 -1.252  1.00 38.09 ? 137 TRP A CA    1 
ATOM   973  C C     . TRP A 1 146 ? 39.695 -9.548  -2.544  1.00 40.87 ? 137 TRP A C     1 
ATOM   974  O O     . TRP A 1 146 ? 40.606 -8.713  -2.550  1.00 39.65 ? 137 TRP A O     1 
ATOM   975  C CB    . TRP A 1 146 ? 38.316 -9.345  -0.470  1.00 41.38 ? 137 TRP A CB    1 
ATOM   976  C CG    . TRP A 1 146 ? 38.142 -9.736  0.968   1.00 39.75 ? 137 TRP A CG    1 
ATOM   977  C CD1   . TRP A 1 146 ? 38.982 -9.445  2.004   1.00 43.80 ? 137 TRP A CD1   1 
ATOM   978  C CD2   . TRP A 1 146 ? 37.057 -10.485 1.529   1.00 38.04 ? 137 TRP A CD2   1 
ATOM   979  N NE1   . TRP A 1 146 ? 38.489 -9.970  3.174   1.00 45.56 ? 137 TRP A NE1   1 
ATOM   980  C CE2   . TRP A 1 146 ? 37.308 -10.613 2.910   1.00 41.36 ? 137 TRP A CE2   1 
ATOM   981  C CE3   . TRP A 1 146 ? 35.899 -11.060 0.998   1.00 43.17 ? 137 TRP A CE3   1 
ATOM   982  C CZ2   . TRP A 1 146 ? 36.444 -11.292 3.766   1.00 44.74 ? 137 TRP A CZ2   1 
ATOM   983  C CZ3   . TRP A 1 146 ? 35.043 -11.735 1.849   1.00 51.51 ? 137 TRP A CZ3   1 
ATOM   984  C CH2   . TRP A 1 146 ? 35.319 -11.845 3.218   1.00 44.16 ? 137 TRP A CH2   1 
ATOM   985  N N     . ARG A 1 147 ? 39.020 -9.897  -3.634  1.00 41.65 ? 138 ARG A N     1 
ATOM   986  C CA    . ARG A 1 147 ? 39.251 -9.290  -4.935  1.00 39.56 ? 138 ARG A CA    1 
ATOM   987  C C     . ARG A 1 147 ? 37.940 -8.730  -5.472  1.00 38.77 ? 138 ARG A C     1 
ATOM   988  O O     . ARG A 1 147 ? 36.861 -9.268  -5.205  1.00 40.51 ? 138 ARG A O     1 
ATOM   989  C CB    . ARG A 1 147 ? 39.842 -10.300 -5.928  1.00 43.84 ? 138 ARG A CB    1 
ATOM   990  C CG    . ARG A 1 147 ? 40.997 -11.116 -5.369  1.00 43.51 ? 138 ARG A CG    1 
ATOM   991  C CD    . ARG A 1 147 ? 42.307 -10.350 -5.451  1.00 53.28 ? 138 ARG A CD    1 
ATOM   992  N NE    . ARG A 1 147 ? 43.344 -10.947 -4.618  1.00 69.18 ? 138 ARG A NE    1 
ATOM   993  C CZ    . ARG A 1 147 ? 44.627 -11.011 -4.948  1.00 63.27 ? 138 ARG A CZ    1 
ATOM   994  N NH1   . ARG A 1 147 ? 45.072 -10.520 -6.093  1.00 51.42 ? 138 ARG A NH1   1 
ATOM   995  N NH2   . ARG A 1 147 ? 45.485 -11.579 -4.106  1.00 51.05 ? 138 ARG A NH2   1 
ATOM   996  N N     . ILE A 1 148 ? 38.041 -7.643  -6.230  1.00 38.94 ? 139 ILE A N     1 
ATOM   997  C CA    . ILE A 1 148 ? 36.876 -6.936  -6.752  1.00 42.80 ? 139 ILE A CA    1 
ATOM   998  C C     . ILE A 1 148 ? 36.593 -7.409  -8.169  1.00 36.27 ? 139 ILE A C     1 
ATOM   999  O O     . ILE A 1 148 ? 37.511 -7.555  -8.987  1.00 37.69 ? 139 ILE A O     1 
ATOM   1000 C CB    . ILE A 1 148 ? 37.085 -5.409  -6.706  1.00 37.85 ? 139 ILE A CB    1 
ATOM   1001 C CG1   . ILE A 1 148 ? 35.895 -4.685  -7.341  1.00 35.23 ? 139 ILE A CG1   1 
ATOM   1002 C CG2   . ILE A 1 148 ? 38.394 -5.017  -7.382  1.00 36.79 ? 139 ILE A CG2   1 
ATOM   1003 C CD1   . ILE A 1 148 ? 35.893 -3.193  -7.109  1.00 35.03 ? 139 ILE A CD1   1 
ATOM   1004 N N     . LEU A 1 149 ? 35.317 -7.654  -8.461  1.00 35.23 ? 140 LEU A N     1 
ATOM   1005 C CA    . LEU A 1 149 ? 34.911 -8.028  -9.809  1.00 36.23 ? 140 LEU A CA    1 
ATOM   1006 C C     . LEU A 1 149 ? 35.107 -6.854  -10.760 1.00 36.88 ? 140 LEU A C     1 
ATOM   1007 O O     . LEU A 1 149 ? 34.681 -5.731  -10.473 1.00 34.02 ? 140 LEU A O     1 
ATOM   1008 C CB    . LEU A 1 149 ? 33.451 -8.479  -9.815  1.00 35.56 ? 140 LEU A CB    1 
ATOM   1009 C CG    . LEU A 1 149 ? 32.818 -8.757  -11.180 1.00 42.26 ? 140 LEU A CG    1 
ATOM   1010 C CD1   . LEU A 1 149 ? 33.498 -9.935  -11.863 1.00 35.96 ? 140 LEU A CD1   1 
ATOM   1011 C CD2   . LEU A 1 149 ? 31.323 -9.000  -11.039 1.00 41.96 ? 140 LEU A CD2   1 
ATOM   1012 N N     . MET A 1 150 ? 35.751 -7.115  -11.889 1.00 35.97 ? 141 MET A N     1 
ATOM   1013 C CA    . MET A 1 150 ? 36.025 -6.107  -12.901 1.00 37.60 ? 141 MET A CA    1 
ATOM   1014 C C     . MET A 1 150 ? 34.990 -6.169  -14.017 1.00 32.02 ? 141 MET A C     1 
ATOM   1015 O O     . MET A 1 150 ? 34.306 -7.183  -14.189 1.00 34.18 ? 141 MET A O     1 
ATOM   1016 C CB    . MET A 1 150 ? 37.434 -6.303  -13.475 1.00 35.12 ? 141 MET A CB    1 
ATOM   1017 C CG    . MET A 1 150 ? 38.507 -6.469  -12.411 1.00 41.56 ? 141 MET A CG    1 
ATOM   1018 S SD    . MET A 1 150 ? 38.734 -4.975  -11.420 1.00 40.51 ? 141 MET A SD    1 
ATOM   1019 C CE    . MET A 1 150 ? 39.033 -3.766  -12.704 1.00 35.50 ? 141 MET A CE    1 
ATOM   1020 N N     . PRO A 1 151 ? 34.840 -5.091  -14.794 1.00 32.20 ? 142 PRO A N     1 
ATOM   1021 C CA    . PRO A 1 151 ? 33.845 -5.102  -15.883 1.00 38.78 ? 142 PRO A CA    1 
ATOM   1022 C C     . PRO A 1 151 ? 34.065 -6.190  -16.924 1.00 33.12 ? 142 PRO A C     1 
ATOM   1023 O O     . PRO A 1 151 ? 33.114 -6.538  -17.636 1.00 37.24 ? 142 PRO A O     1 
ATOM   1024 C CB    . PRO A 1 151 ? 33.991 -3.704  -16.503 1.00 37.81 ? 142 PRO A CB    1 
ATOM   1025 C CG    . PRO A 1 151 ? 34.545 -2.863  -15.402 1.00 34.47 ? 142 PRO A CG    1 
ATOM   1026 C CD    . PRO A 1 151 ? 35.463 -3.764  -14.636 1.00 32.56 ? 142 PRO A CD    1 
ATOM   1027 N N     . ASP A 1 152 ? 35.272 -6.739  -17.045 1.00 32.39 ? 143 ASP A N     1 
ATOM   1028 C CA    . ASP A 1 152 ? 35.543 -7.792  -18.017 1.00 32.51 ? 143 ASP A CA    1 
ATOM   1029 C C     . ASP A 1 152 ? 35.387 -9.191  -17.437 1.00 36.76 ? 143 ASP A C     1 
ATOM   1030 O O     . ASP A 1 152 ? 35.679 -10.171 -18.128 1.00 35.82 ? 143 ASP A O     1 
ATOM   1031 C CB    . ASP A 1 152 ? 36.950 -7.628  -18.606 1.00 38.27 ? 143 ASP A CB    1 
ATOM   1032 C CG    . ASP A 1 152 ? 38.047 -7.830  -17.575 1.00 38.87 ? 143 ASP A CG    1 
ATOM   1033 O OD1   . ASP A 1 152 ? 37.766 -7.722  -16.364 1.00 44.37 ? 143 ASP A OD1   1 
ATOM   1034 O OD2   . ASP A 1 152 ? 39.198 -8.096  -17.981 1.00 44.61 ? 143 ASP A OD2   1 
ATOM   1035 N N     . GLY A 1 153 ? 34.938 -9.310  -16.190 1.00 37.49 ? 144 GLY A N     1 
ATOM   1036 C CA    . GLY A 1 153 ? 34.772 -10.599 -15.560 1.00 37.02 ? 144 GLY A CA    1 
ATOM   1037 C C     . GLY A 1 153 ? 35.966 -11.082 -14.767 1.00 35.55 ? 144 GLY A C     1 
ATOM   1038 O O     . GLY A 1 153 ? 35.839 -12.068 -14.030 1.00 44.85 ? 144 GLY A O     1 
ATOM   1039 N N     . THR A 1 154 ? 37.118 -10.430 -14.894 1.00 33.13 ? 145 THR A N     1 
ATOM   1040 C CA    . THR A 1 154 ? 38.271 -10.778 -14.080 1.00 40.89 ? 145 THR A CA    1 
ATOM   1041 C C     . THR A 1 154 ? 38.108 -10.194 -12.677 1.00 44.02 ? 145 THR A C     1 
ATOM   1042 O O     . THR A 1 154 ? 37.091 -9.580  -12.342 1.00 43.06 ? 145 THR A O     1 
ATOM   1043 C CB    . THR A 1 154 ? 39.560 -10.283 -14.732 1.00 41.17 ? 145 THR A CB    1 
ATOM   1044 O OG1   . THR A 1 154 ? 39.478 -8.869  -14.950 1.00 41.96 ? 145 THR A OG1   1 
ATOM   1045 C CG2   . THR A 1 154 ? 39.792 -10.986 -16.064 1.00 44.03 ? 145 THR A CG2   1 
ATOM   1046 N N     . HIS A 1 155 ? 39.126 -10.384 -11.843 1.00 40.73 ? 146 HIS A N     1 
ATOM   1047 C CA    . HIS A 1 155 ? 39.123 -9.865  -10.483 1.00 39.45 ? 146 HIS A CA    1 
ATOM   1048 C C     . HIS A 1 155 ? 40.379 -9.039  -10.261 1.00 41.78 ? 146 HIS A C     1 
ATOM   1049 O O     . HIS A 1 155 ? 41.482 -9.475  -10.609 1.00 41.84 ? 146 HIS A O     1 
ATOM   1050 C CB    . HIS A 1 155 ? 39.031 -11.000 -9.459  1.00 41.88 ? 146 HIS A CB    1 
ATOM   1051 C CG    . HIS A 1 155 ? 37.690 -11.662 -9.419  1.00 38.28 ? 146 HIS A CG    1 
ATOM   1052 N ND1   . HIS A 1 155 ? 36.725 -11.335 -8.491  1.00 49.55 ? 146 HIS A ND1   1 
ATOM   1053 C CD2   . HIS A 1 155 ? 37.148 -12.624 -10.201 1.00 39.20 ? 146 HIS A CD2   1 
ATOM   1054 C CE1   . HIS A 1 155 ? 35.649 -12.072 -8.698  1.00 45.70 ? 146 HIS A CE1   1 
ATOM   1055 N NE2   . HIS A 1 155 ? 35.879 -12.863 -9.730  1.00 40.05 ? 146 HIS A NE2   1 
ATOM   1056 N N     . GLY A 1 156 ? 40.209 -7.847  -9.689  1.00 40.97 ? 147 GLY A N     1 
ATOM   1057 C CA    . GLY A 1 156 ? 41.299 -6.936  -9.436  1.00 35.77 ? 147 GLY A CA    1 
ATOM   1058 C C     . GLY A 1 156 ? 41.547 -6.714  -7.951  1.00 38.05 ? 147 GLY A C     1 
ATOM   1059 O O     . GLY A 1 156 ? 40.909 -7.298  -7.079  1.00 38.37 ? 147 GLY A O     1 
ATOM   1060 N N     . ILE A 1 157 ? 42.505 -5.829  -7.683  1.00 44.10 ? 148 ILE A N     1 
ATOM   1061 C CA    . ILE A 1 157 ? 42.963 -5.530  -6.331  1.00 41.04 ? 148 ILE A CA    1 
ATOM   1062 C C     . ILE A 1 157 ? 42.299 -4.250  -5.845  1.00 38.72 ? 148 ILE A C     1 
ATOM   1063 O O     . ILE A 1 157 ? 42.213 -3.260  -6.583  1.00 37.65 ? 148 ILE A O     1 
ATOM   1064 C CB    . ILE A 1 157 ? 44.499 -5.406  -6.291  1.00 39.64 ? 148 ILE A CB    1 
ATOM   1065 C CG1   . ILE A 1 157 ? 45.147 -6.632  -6.934  1.00 38.03 ? 148 ILE A CG1   1 
ATOM   1066 C CG2   . ILE A 1 157 ? 44.992 -5.226  -4.864  1.00 45.84 ? 148 ILE A CG2   1 
ATOM   1067 C CD1   . ILE A 1 157 ? 46.657 -6.584  -6.937  1.00 43.30 ? 148 ILE A CD1   1 
ATOM   1068 N N     . TYR A 1 158 ? 41.826 -4.268  -4.604  1.00 39.70 ? 149 TYR A N     1 
ATOM   1069 C CA    . TYR A 1 158 ? 41.241 -3.072  -4.012  1.00 35.92 ? 149 TYR A CA    1 
ATOM   1070 C C     . TYR A 1 158 ? 42.331 -2.034  -3.771  1.00 40.47 ? 149 TYR A C     1 
ATOM   1071 O O     . TYR A 1 158 ? 43.334 -2.337  -3.113  1.00 37.61 ? 149 TYR A O     1 
ATOM   1072 C CB    . TYR A 1 158 ? 40.537 -3.408  -2.703  1.00 40.71 ? 149 TYR A CB    1 
ATOM   1073 C CG    . TYR A 1 158 ? 39.241 -4.160  -2.881  1.00 39.90 ? 149 TYR A CG    1 
ATOM   1074 C CD1   . TYR A 1 158 ? 38.077 -3.496  -3.244  1.00 33.26 ? 149 TYR A CD1   1 
ATOM   1075 C CD2   . TYR A 1 158 ? 39.178 -5.533  -2.679  1.00 36.17 ? 149 TYR A CD2   1 
ATOM   1076 C CE1   . TYR A 1 158 ? 36.887 -4.180  -3.405  1.00 32.22 ? 149 TYR A CE1   1 
ATOM   1077 C CE2   . TYR A 1 158 ? 37.993 -6.226  -2.838  1.00 35.20 ? 149 TYR A CE2   1 
ATOM   1078 C CZ    . TYR A 1 158 ? 36.852 -5.544  -3.200  1.00 36.46 ? 149 TYR A CZ    1 
ATOM   1079 O OH    . TYR A 1 158 ? 35.670 -6.227  -3.360  1.00 31.99 ? 149 TYR A OH    1 
ATOM   1080 N N     . PRO A 1 159 ? 42.179 -0.815  -4.275  1.00 41.24 ? 150 PRO A N     1 
ATOM   1081 C CA    . PRO A 1 159 ? 43.229 0.195   -4.116  1.00 38.44 ? 150 PRO A CA    1 
ATOM   1082 C C     . PRO A 1 159 ? 43.178 0.849   -2.741  1.00 39.93 ? 150 PRO A C     1 
ATOM   1083 O O     . PRO A 1 159 ? 42.273 0.620   -1.936  1.00 42.51 ? 150 PRO A O     1 
ATOM   1084 C CB    . PRO A 1 159 ? 42.907 1.206   -5.219  1.00 41.69 ? 150 PRO A CB    1 
ATOM   1085 C CG    . PRO A 1 159 ? 41.417 1.120   -5.363  1.00 42.24 ? 150 PRO A CG    1 
ATOM   1086 C CD    . PRO A 1 159 ? 41.032 -0.310  -5.051  1.00 38.81 ? 150 PRO A CD    1 
ATOM   1087 N N     . LYS A 1 160 ? 44.179 1.677   -2.487  1.00 44.84 ? 151 LYS A N     1 
ATOM   1088 C CA    . LYS A 1 160 ? 44.236 2.452   -1.254  1.00 44.55 ? 151 LYS A CA    1 
ATOM   1089 C C     . LYS A 1 160 ? 43.170 3.540   -1.280  1.00 45.66 ? 151 LYS A C     1 
ATOM   1090 O O     . LYS A 1 160 ? 43.168 4.367   -2.201  1.00 45.94 ? 151 LYS A O     1 
ATOM   1091 C CB    . LYS A 1 160 ? 45.624 3.062   -1.088  1.00 43.00 ? 151 LYS A CB    1 
ATOM   1092 C CG    . LYS A 1 160 ? 45.762 3.999   0.097   1.00 49.05 ? 151 LYS A CG    1 
ATOM   1093 C CD    . LYS A 1 160 ? 47.182 3.983   0.640   1.00 50.59 ? 151 LYS A CD    1 
ATOM   1094 C CE    . LYS A 1 160 ? 47.236 4.516   2.060   1.00 53.90 ? 151 LYS A CE    1 
ATOM   1095 N NZ    . LYS A 1 160 ? 47.128 3.418   3.063   1.00 51.09 ? 151 LYS A NZ    1 
ATOM   1096 N N     . PRO A 1 161 ? 42.255 3.582   -0.316  1.00 44.67 ? 152 PRO A N     1 
ATOM   1097 C CA    . PRO A 1 161 ? 41.203 4.601   -0.331  1.00 41.60 ? 152 PRO A CA    1 
ATOM   1098 C C     . PRO A 1 161 ? 41.702 5.927   0.230   1.00 40.38 ? 152 PRO A C     1 
ATOM   1099 O O     . PRO A 1 161 ? 42.746 6.013   0.878   1.00 32.65 ? 152 PRO A O     1 
ATOM   1100 C CB    . PRO A 1 161 ? 40.123 3.997   0.568   1.00 40.28 ? 152 PRO A CB    1 
ATOM   1101 C CG    . PRO A 1 161 ? 40.891 3.103   1.489   1.00 40.74 ? 152 PRO A CG    1 
ATOM   1102 C CD    . PRO A 1 161 ? 42.037 2.541   0.667   1.00 44.65 ? 152 PRO A CD    1 
ATOM   1103 N N     . ARG A 1 162 ? 40.918 6.969   -0.027  1.00 35.32 ? 153 ARG A N     1 
ATOM   1104 C CA    . ARG A 1 162 ? 41.191 8.306   0.482   1.00 41.99 ? 153 ARG A CA    1 
ATOM   1105 C C     . ARG A 1 162 ? 40.298 8.582   1.684   1.00 36.02 ? 153 ARG A C     1 
ATOM   1106 O O     . ARG A 1 162 ? 39.073 8.446   1.598   1.00 37.34 ? 153 ARG A O     1 
ATOM   1107 C CB    . ARG A 1 162 ? 40.963 9.359   -0.604  1.00 40.58 ? 153 ARG A CB    1 
ATOM   1108 C CG    . ARG A 1 162 ? 41.175 10.789  -0.140  1.00 40.11 ? 153 ARG A CG    1 
ATOM   1109 C CD    . ARG A 1 162 ? 41.135 11.760  -1.312  1.00 40.15 ? 153 ARG A CD    1 
ATOM   1110 N NE    . ARG A 1 162 ? 39.819 11.815  -1.939  1.00 41.40 ? 153 ARG A NE    1 
ATOM   1111 C CZ    . ARG A 1 162 ? 38.795 12.517  -1.472  1.00 41.09 ? 153 ARG A CZ    1 
ATOM   1112 N NH1   . ARG A 1 162 ? 38.896 13.232  -0.364  1.00 41.38 ? 153 ARG A NH1   1 
ATOM   1113 N NH2   . ARG A 1 162 ? 37.641 12.502  -2.134  1.00 40.26 ? 153 ARG A NH2   1 
ATOM   1114 N N     . ALA A 1 163 ? 40.912 8.964   2.802   1.00 41.58 ? 154 ALA A N     1 
ATOM   1115 C CA    . ALA A 1 163 ? 40.171 9.269   4.020   1.00 37.19 ? 154 ALA A CA    1 
ATOM   1116 C C     . ALA A 1 163 ? 39.588 10.674  3.922   1.00 32.93 ? 154 ALA A C     1 
ATOM   1117 O O     . ALA A 1 163 ? 40.331 11.654  3.806   1.00 36.30 ? 154 ALA A O     1 
ATOM   1118 C CB    . ALA A 1 163 ? 41.078 9.143   5.241   1.00 43.38 ? 154 ALA A CB    1 
ATOM   1119 N N     . ILE A 1 164 ? 38.267 10.774  3.976   1.00 30.31 ? 155 ILE A N     1 
ATOM   1120 C CA    . ILE A 1 164 ? 37.578 12.044  3.787   1.00 39.91 ? 155 ILE A CA    1 
ATOM   1121 C C     . ILE A 1 164 ? 37.504 12.799  5.107   1.00 35.67 ? 155 ILE A C     1 
ATOM   1122 O O     . ILE A 1 164 ? 37.414 12.209  6.191   1.00 31.09 ? 155 ILE A O     1 
ATOM   1123 C CB    . ILE A 1 164 ? 36.172 11.823  3.190   1.00 37.45 ? 155 ILE A CB    1 
ATOM   1124 C CG1   . ILE A 1 164 ? 35.297 11.014  4.149   1.00 37.43 ? 155 ILE A CG1   1 
ATOM   1125 C CG2   . ILE A 1 164 ? 36.276 11.118  1.852   1.00 42.23 ? 155 ILE A CG2   1 
ATOM   1126 C CD1   . ILE A 1 164 ? 33.905 10.743  3.622   1.00 31.14 ? 155 ILE A CD1   1 
ATOM   1127 N N     . GLY A 1 165 ? 37.549 14.127  5.010   1.00 32.71 ? 156 GLY A N     1 
ATOM   1128 C CA    . GLY A 1 165 ? 37.323 14.988  6.149   1.00 33.20 ? 156 GLY A CA    1 
ATOM   1129 C C     . GLY A 1 165 ? 35.845 15.201  6.409   1.00 34.80 ? 156 GLY A C     1 
ATOM   1130 O O     . GLY A 1 165 ? 34.973 14.662  5.727   1.00 32.83 ? 156 GLY A O     1 
ATOM   1131 N N     . THR A 1 166 ? 35.562 16.025  7.422   1.00 30.64 ? 157 THR A N     1 
ATOM   1132 C CA    . THR A 1 166 ? 34.182 16.178  7.871   1.00 33.92 ? 157 THR A CA    1 
ATOM   1133 C C     . THR A 1 166 ? 33.354 17.013  6.904   1.00 27.81 ? 157 THR A C     1 
ATOM   1134 O O     . THR A 1 166 ? 32.136 16.817  6.812   1.00 33.50 ? 157 THR A O     1 
ATOM   1135 C CB    . THR A 1 166 ? 34.136 16.787  9.273   1.00 34.66 ? 157 THR A CB    1 
ATOM   1136 O OG1   . THR A 1 166 ? 34.731 18.089  9.255   1.00 31.79 ? 157 THR A OG1   1 
ATOM   1137 C CG2   . THR A 1 166 ? 34.887 15.906  10.258  1.00 34.20 ? 157 THR A CG2   1 
ATOM   1138 N N     . TYR A 1 167 ? 33.975 17.943  6.176   1.00 34.61 ? 158 TYR A N     1 
ATOM   1139 C CA    . TYR A 1 167 ? 33.229 18.644  5.137   1.00 32.35 ? 158 TYR A CA    1 
ATOM   1140 C C     . TYR A 1 167 ? 32.753 17.670  4.068   1.00 26.47 ? 158 TYR A C     1 
ATOM   1141 O O     . TYR A 1 167 ? 31.588 17.701  3.655   1.00 26.21 ? 158 TYR A O     1 
ATOM   1142 C CB    . TYR A 1 167 ? 34.071 19.749  4.502   1.00 38.95 ? 158 TYR A CB    1 
ATOM   1143 C CG    . TYR A 1 167 ? 33.407 20.308  3.263   1.00 32.35 ? 158 TYR A CG    1 
ATOM   1144 C CD1   . TYR A 1 167 ? 32.227 21.036  3.359   1.00 38.73 ? 158 TYR A CD1   1 
ATOM   1145 C CD2   . TYR A 1 167 ? 33.932 20.074  1.999   1.00 36.56 ? 158 TYR A CD2   1 
ATOM   1146 C CE1   . TYR A 1 167 ? 31.602 21.538  2.233   1.00 38.58 ? 158 TYR A CE1   1 
ATOM   1147 C CE2   . TYR A 1 167 ? 33.312 20.572  0.866   1.00 34.42 ? 158 TYR A CE2   1 
ATOM   1148 C CZ    . TYR A 1 167 ? 32.149 21.304  0.991   1.00 36.57 ? 158 TYR A CZ    1 
ATOM   1149 O OH    . TYR A 1 167 ? 31.525 21.802  -0.128  1.00 43.60 ? 158 TYR A OH    1 
ATOM   1150 N N     . GLU A 1 168 ? 33.644 16.788  3.610   1.00 31.66 ? 159 GLU A N     1 
ATOM   1151 C CA    . GLU A 1 168 ? 33.241 15.800  2.615   1.00 28.83 ? 159 GLU A CA    1 
ATOM   1152 C C     . GLU A 1 168 ? 32.224 14.819  3.182   1.00 33.03 ? 159 GLU A C     1 
ATOM   1153 O O     . GLU A 1 168 ? 31.385 14.302  2.436   1.00 35.61 ? 159 GLU A O     1 
ATOM   1154 C CB    . GLU A 1 168 ? 34.463 15.057  2.078   1.00 35.38 ? 159 GLU A CB    1 
ATOM   1155 C CG    . GLU A 1 168 ? 34.204 14.308  0.777   1.00 40.25 ? 159 GLU A CG    1 
ATOM   1156 C CD    . GLU A 1 168 ? 35.478 13.991  0.021   1.00 42.77 ? 159 GLU A CD    1 
ATOM   1157 O OE1   . GLU A 1 168 ? 36.554 14.471  0.438   1.00 45.49 ? 159 GLU A OE1   1 
ATOM   1158 O OE2   . GLU A 1 168 ? 35.404 13.269  -0.996  1.00 44.11 ? 159 GLU A OE2   1 
ATOM   1159 N N     . ILE A 1 169 ? 32.273 14.558  4.492   1.00 34.45 ? 160 ILE A N     1 
ATOM   1160 C CA    . ILE A 1 169 ? 31.280 13.686  5.114   1.00 27.17 ? 160 ILE A CA    1 
ATOM   1161 C C     . ILE A 1 169 ? 29.893 14.307  5.006   1.00 33.71 ? 160 ILE A C     1 
ATOM   1162 O O     . ILE A 1 169 ? 28.925 13.649  4.605   1.00 33.07 ? 160 ILE A O     1 
ATOM   1163 C CB    . ILE A 1 169 ? 31.656 13.398  6.580   1.00 32.51 ? 160 ILE A CB    1 
ATOM   1164 C CG1   . ILE A 1 169 ? 32.803 12.388  6.656   1.00 28.24 ? 160 ILE A CG1   1 
ATOM   1165 C CG2   . ILE A 1 169 ? 30.448 12.887  7.350   1.00 30.46 ? 160 ILE A CG2   1 
ATOM   1166 C CD1   . ILE A 1 169 ? 33.472 12.316  8.015   1.00 37.53 ? 160 ILE A CD1   1 
ATOM   1167 N N     . SER A 1 170 ? 29.780 15.594  5.350   1.00 34.37 ? 161 SER A N     1 
ATOM   1168 C CA    . SER A 1 170 ? 28.493 16.275  5.260   1.00 35.14 ? 161 SER A CA    1 
ATOM   1169 C C     . SER A 1 170 ? 28.002 16.363  3.820   1.00 33.23 ? 161 SER A C     1 
ATOM   1170 O O     . SER A 1 170 ? 26.792 16.440  3.580   1.00 38.53 ? 161 SER A O     1 
ATOM   1171 C CB    . SER A 1 170 ? 28.593 17.671  5.881   1.00 36.41 ? 161 SER A CB    1 
ATOM   1172 O OG    . SER A 1 170 ? 29.385 18.539  5.085   1.00 37.09 ? 161 SER A OG    1 
ATOM   1173 N N     . GLN A 1 171 ? 28.917 16.350  2.850   1.00 30.13 ? 162 GLN A N     1 
ATOM   1174 C CA    . GLN A 1 171 ? 28.505 16.358  1.450   1.00 32.26 ? 162 GLN A CA    1 
ATOM   1175 C C     . GLN A 1 171 ? 28.017 14.984  1.003   1.00 35.56 ? 162 GLN A C     1 
ATOM   1176 O O     . GLN A 1 171 ? 27.090 14.886  0.190   1.00 32.12 ? 162 GLN A O     1 
ATOM   1177 C CB    . GLN A 1 171 ? 29.655 16.834  0.566   1.00 32.21 ? 162 GLN A CB    1 
ATOM   1178 C CG    . GLN A 1 171 ? 29.944 18.325  0.679   1.00 41.15 ? 162 GLN A CG    1 
ATOM   1179 C CD    . GLN A 1 171 ? 28.688 19.175  0.592   1.00 43.99 ? 162 GLN A CD    1 
ATOM   1180 O OE1   . GLN A 1 171 ? 28.200 19.689  1.599   1.00 49.35 ? 162 GLN A OE1   1 
ATOM   1181 N NE2   . GLN A 1 171 ? 28.157 19.325  -0.618  1.00 48.32 ? 162 GLN A NE2   1 
ATOM   1182 N N     . VAL A 1 172 ? 28.620 13.912  1.522   1.00 31.74 ? 163 VAL A N     1 
ATOM   1183 C CA    . VAL A 1 172 ? 28.102 12.575  1.245   1.00 29.84 ? 163 VAL A CA    1 
ATOM   1184 C C     . VAL A 1 172 ? 26.719 12.409  1.860   1.00 32.38 ? 163 VAL A C     1 
ATOM   1185 O O     . VAL A 1 172 ? 25.812 11.844  1.237   1.00 32.68 ? 163 VAL A O     1 
ATOM   1186 C CB    . VAL A 1 172 ? 29.082 11.499  1.748   1.00 28.59 ? 163 VAL A CB    1 
ATOM   1187 C CG1   . VAL A 1 172 ? 28.465 10.113  1.613   1.00 29.10 ? 163 VAL A CG1   1 
ATOM   1188 C CG2   . VAL A 1 172 ? 30.389 11.575  0.979   1.00 32.37 ? 163 VAL A CG2   1 
ATOM   1189 N N     . VAL A 1 173 ? 26.535 12.902  3.090   1.00 32.29 ? 164 VAL A N     1 
ATOM   1190 C CA    . VAL A 1 173 ? 25.211 12.922  3.705   1.00 28.93 ? 164 VAL A CA    1 
ATOM   1191 C C     . VAL A 1 173 ? 24.230 13.685  2.824   1.00 30.98 ? 164 VAL A C     1 
ATOM   1192 O O     . VAL A 1 173 ? 23.072 13.280  2.657   1.00 32.71 ? 164 VAL A O     1 
ATOM   1193 C CB    . VAL A 1 173 ? 25.294 13.529  5.120   1.00 35.03 ? 164 VAL A CB    1 
ATOM   1194 C CG1   . VAL A 1 173 ? 23.909 13.803  5.669   1.00 29.67 ? 164 VAL A CG1   1 
ATOM   1195 C CG2   . VAL A 1 173 ? 26.066 12.612  6.055   1.00 24.46 ? 164 VAL A CG2   1 
ATOM   1196 N N     . GLU A 1 174 ? 24.680 14.802  2.246   1.00 36.95 ? 165 GLU A N     1 
ATOM   1197 C CA    . GLU A 1 174 ? 23.858 15.544  1.293   1.00 37.39 ? 165 GLU A CA    1 
ATOM   1198 C C     . GLU A 1 174 ? 23.510 14.700  0.072   1.00 34.97 ? 165 GLU A C     1 
ATOM   1199 O O     . GLU A 1 174 ? 22.412 14.833  -0.484  1.00 33.27 ? 165 GLU A O     1 
ATOM   1200 C CB    . GLU A 1 174 ? 24.587 16.821  0.869   1.00 39.06 ? 165 GLU A CB    1 
ATOM   1201 C CG    . GLU A 1 174 ? 23.701 17.993  0.458   1.00 52.56 ? 165 GLU A CG    1 
ATOM   1202 C CD    . GLU A 1 174 ? 22.342 18.006  1.136   1.00 57.05 ? 165 GLU A CD    1 
ATOM   1203 O OE1   . GLU A 1 174 ? 22.283 17.991  2.383   1.00 56.23 ? 165 GLU A OE1   1 
ATOM   1204 O OE2   . GLU A 1 174 ? 21.328 18.037  0.409   1.00 57.47 ? 165 GLU A OE2   1 
ATOM   1205 N N     . ASP A 1 175 ? 24.425 13.831  -0.364  1.00 34.81 ? 166 ASP A N     1 
ATOM   1206 C CA    . ASP A 1 175 ? 24.127 12.961  -1.498  1.00 33.90 ? 166 ASP A CA    1 
ATOM   1207 C C     . ASP A 1 175 ? 23.035 11.958  -1.149  1.00 34.03 ? 166 ASP A C     1 
ATOM   1208 O O     . ASP A 1 175 ? 22.191 11.633  -1.992  1.00 30.51 ? 166 ASP A O     1 
ATOM   1209 C CB    . ASP A 1 175 ? 25.392 12.238  -1.956  1.00 38.61 ? 166 ASP A CB    1 
ATOM   1210 C CG    . ASP A 1 175 ? 26.380 13.165  -2.634  1.00 39.80 ? 166 ASP A CG    1 
ATOM   1211 O OD1   . ASP A 1 175 ? 25.939 14.067  -3.376  1.00 47.19 ? 166 ASP A OD1   1 
ATOM   1212 O OD2   . ASP A 1 175 ? 27.599 12.991  -2.423  1.00 44.76 ? 166 ASP A OD2   1 
ATOM   1213 N N     . TYR A 1 176 ? 23.036 11.458  0.090   1.00 37.20 ? 167 TYR A N     1 
ATOM   1214 C CA    . TYR A 1 176 ? 21.976 10.555  0.527   1.00 34.49 ? 167 TYR A CA    1 
ATOM   1215 C C     . TYR A 1 176 ? 20.628 11.262  0.522   1.00 29.65 ? 167 TYR A C     1 
ATOM   1216 O O     . TYR A 1 176 ? 19.636 10.737  0.002   1.00 32.08 ? 167 TYR A O     1 
ATOM   1217 C CB    . TYR A 1 176 ? 22.286 10.015  1.924   1.00 32.62 ? 167 TYR A CB    1 
ATOM   1218 C CG    . TYR A 1 176 ? 23.210 8.819   1.948   1.00 33.17 ? 167 TYR A CG    1 
ATOM   1219 C CD1   . TYR A 1 176 ? 22.751 7.555   1.603   1.00 33.32 ? 167 TYR A CD1   1 
ATOM   1220 C CD2   . TYR A 1 176 ? 24.539 8.954   2.328   1.00 29.59 ? 167 TYR A CD2   1 
ATOM   1221 C CE1   . TYR A 1 176 ? 23.593 6.458   1.630   1.00 29.50 ? 167 TYR A CE1   1 
ATOM   1222 C CE2   . TYR A 1 176 ? 25.389 7.863   2.359   1.00 34.65 ? 167 TYR A CE2   1 
ATOM   1223 C CZ    . TYR A 1 176 ? 24.911 6.619   2.008   1.00 31.00 ? 167 TYR A CZ    1 
ATOM   1224 O OH    . TYR A 1 176 ? 25.753 5.532   2.036   1.00 32.57 ? 167 TYR A OH    1 
ATOM   1225 N N     . ARG A 1 177 ? 20.578 12.464  1.104   1.00 34.87 ? 168 ARG A N     1 
ATOM   1226 C CA    . ARG A 1 177 ? 19.331 13.220  1.160   1.00 37.76 ? 168 ARG A CA    1 
ATOM   1227 C C     . ARG A 1 177 ? 18.821 13.550  -0.237  1.00 34.84 ? 168 ARG A C     1 
ATOM   1228 O O     . ARG A 1 177 ? 17.622 13.429  -0.513  1.00 38.33 ? 168 ARG A O     1 
ATOM   1229 C CB    . ARG A 1 177 ? 19.539 14.499  1.971   1.00 39.05 ? 168 ARG A CB    1 
ATOM   1230 C CG    . ARG A 1 177 ? 18.273 15.299  2.220   1.00 34.78 ? 168 ARG A CG    1 
ATOM   1231 C CD    . ARG A 1 177 ? 18.605 16.688  2.742   1.00 46.98 ? 168 ARG A CD    1 
ATOM   1232 N NE    . ARG A 1 177 ? 19.141 17.561  1.705   1.00 55.58 ? 168 ARG A NE    1 
ATOM   1233 C CZ    . ARG A 1 177 ? 18.435 18.058  0.699   1.00 58.86 ? 168 ARG A CZ    1 
ATOM   1234 N NH1   . ARG A 1 177 ? 17.133 17.844  0.594   1.00 52.83 ? 168 ARG A NH1   1 
ATOM   1235 N NH2   . ARG A 1 177 ? 19.046 18.805  -0.216  1.00 57.25 ? 168 ARG A NH2   1 
ATOM   1236 N N     . ARG A 1 178 ? 19.720 13.965  -1.131  1.00 32.92 ? 169 ARG A N     1 
ATOM   1237 C CA    . ARG A 1 178 ? 19.324 14.290  -2.497  1.00 33.48 ? 169 ARG A CA    1 
ATOM   1238 C C     . ARG A 1 178 ? 18.834 13.053  -3.239  1.00 40.33 ? 169 ARG A C     1 
ATOM   1239 O O     . ARG A 1 178 ? 17.906 13.136  -4.053  1.00 36.65 ? 169 ARG A O     1 
ATOM   1240 C CB    . ARG A 1 178 ? 20.497 14.934  -3.237  1.00 37.49 ? 169 ARG A CB    1 
ATOM   1241 C CG    . ARG A 1 178 ? 20.144 15.521  -4.592  1.00 51.32 ? 169 ARG A CG    1 
ATOM   1242 C CD    . ARG A 1 178 ? 21.203 16.511  -5.052  1.00 61.51 ? 169 ARG A CD    1 
ATOM   1243 N NE    . ARG A 1 178 ? 21.793 17.237  -3.933  1.00 66.27 ? 169 ARG A NE    1 
ATOM   1244 C CZ    . ARG A 1 178 ? 22.005 18.546  -3.916  1.00 70.56 ? 169 ARG A CZ    1 
ATOM   1245 N NH1   . ARG A 1 178 ? 21.688 19.311  -4.948  1.00 71.69 ? 169 ARG A NH1   1 
ATOM   1246 N NH2   . ARG A 1 178 ? 22.549 19.101  -2.837  1.00 65.24 ? 169 ARG A NH2   1 
ATOM   1247 N N     . SER A 1 179 ? 19.441 11.895  -2.968  1.00 36.59 ? 170 SER A N     1 
ATOM   1248 C CA    . SER A 1 179 ? 19.013 10.667  -3.629  1.00 31.78 ? 170 SER A CA    1 
ATOM   1249 C C     . SER A 1 179 ? 17.672 10.179  -3.100  1.00 33.00 ? 170 SER A C     1 
ATOM   1250 O O     . SER A 1 179 ? 16.882 9.607   -3.860  1.00 34.55 ? 170 SER A O     1 
ATOM   1251 C CB    . SER A 1 179 ? 20.074 9.583   -3.457  1.00 36.05 ? 170 SER A CB    1 
ATOM   1252 O OG    . SER A 1 179 ? 21.221 9.877   -4.231  1.00 32.78 ? 170 SER A OG    1 
ATOM   1253 N N     . ALA A 1 180 ? 17.402 10.381  -1.806  1.00 32.88 ? 171 ALA A N     1 
ATOM   1254 C CA    . ALA A 1 180 ? 16.123 9.967   -1.240  1.00 35.04 ? 171 ALA A CA    1 
ATOM   1255 C C     . ALA A 1 180 ? 14.971 10.757  -1.846  1.00 30.61 ? 171 ALA A C     1 
ATOM   1256 O O     . ALA A 1 180 ? 13.887 10.209  -2.077  1.00 35.90 ? 171 ALA A O     1 
ATOM   1257 C CB    . ALA A 1 180 ? 16.141 10.128  0.280   1.00 32.91 ? 171 ALA A CB    1 
ATOM   1258 N N     . LEU A 1 181 ? 15.181 12.049  -2.099  1.00 30.96 ? 172 LEU A N     1 
ATOM   1259 C CA    . LEU A 1 181 ? 14.148 12.842  -2.756  1.00 32.09 ? 172 LEU A CA    1 
ATOM   1260 C C     . LEU A 1 181 ? 13.968 12.410  -4.206  1.00 33.21 ? 172 LEU A C     1 
ATOM   1261 O O     . LEU A 1 181 ? 12.841 12.376  -4.714  1.00 38.92 ? 172 LEU A O     1 
ATOM   1262 C CB    . LEU A 1 181 ? 14.496 14.327  -2.676  1.00 32.74 ? 172 LEU A CB    1 
ATOM   1263 C CG    . LEU A 1 181 ? 14.330 14.973  -1.301  1.00 36.56 ? 172 LEU A CG    1 
ATOM   1264 C CD1   . LEU A 1 181 ? 15.026 16.316  -1.272  1.00 39.60 ? 172 LEU A CD1   1 
ATOM   1265 C CD2   . LEU A 1 181 ? 12.857 15.120  -0.952  1.00 35.41 ? 172 LEU A CD2   1 
ATOM   1266 N N     . ASN A 1 182 ? 15.066 12.076  -4.887  1.00 33.26 ? 173 ASN A N     1 
ATOM   1267 C CA    . ASN A 1 182 ? 14.959 11.572  -6.252  1.00 39.38 ? 173 ASN A CA    1 
ATOM   1268 C C     . ASN A 1 182 ? 14.204 10.252  -6.299  1.00 35.26 ? 173 ASN A C     1 
ATOM   1269 O O     . ASN A 1 182 ? 13.489 9.981   -7.271  1.00 35.53 ? 173 ASN A O     1 
ATOM   1270 C CB    . ASN A 1 182 ? 16.349 11.405  -6.864  1.00 32.40 ? 173 ASN A CB    1 
ATOM   1271 C CG    . ASN A 1 182 ? 16.978 12.724  -7.244  1.00 40.23 ? 173 ASN A CG    1 
ATOM   1272 O OD1   . ASN A 1 182 ? 16.285 13.728  -7.412  1.00 34.40 ? 173 ASN A OD1   1 
ATOM   1273 N ND2   . ASN A 1 182 ? 18.300 12.733  -7.378  1.00 39.65 ? 173 ASN A ND2   1 
ATOM   1274 N N     . ALA A 1 183 ? 14.354 9.418   -5.268  1.00 34.30 ? 174 ALA A N     1 
ATOM   1275 C CA    . ALA A 1 183 ? 13.624 8.156   -5.230  1.00 30.26 ? 174 ALA A CA    1 
ATOM   1276 C C     . ALA A 1 183 ? 12.133 8.394   -5.038  1.00 33.27 ? 174 ALA A C     1 
ATOM   1277 O O     . ALA A 1 183 ? 11.305 7.734   -5.677  1.00 29.87 ? 174 ALA A O     1 
ATOM   1278 C CB    . ALA A 1 183 ? 14.175 7.264   -4.120  1.00 31.90 ? 174 ALA A CB    1 
ATOM   1279 N N     . ILE A 1 184 ? 11.774 9.336   -4.164  1.00 32.04 ? 175 ILE A N     1 
ATOM   1280 C CA    . ILE A 1 184 ? 10.372 9.699   -3.998  1.00 31.57 ? 175 ILE A CA    1 
ATOM   1281 C C     . ILE A 1 184 ? 9.838  10.348  -5.268  1.00 32.39 ? 175 ILE A C     1 
ATOM   1282 O O     . ILE A 1 184 ? 8.684  10.129  -5.657  1.00 34.18 ? 175 ILE A O     1 
ATOM   1283 C CB    . ILE A 1 184 ? 10.205 10.616  -2.773  1.00 38.44 ? 175 ILE A CB    1 
ATOM   1284 C CG1   . ILE A 1 184 ? 10.658 9.883   -1.510  1.00 38.49 ? 175 ILE A CG1   1 
ATOM   1285 C CG2   . ILE A 1 184 ? 8.763  11.086  -2.639  1.00 44.47 ? 175 ILE A CG2   1 
ATOM   1286 C CD1   . ILE A 1 184 ? 9.695  8.810   -1.055  1.00 38.33 ? 175 ILE A CD1   1 
ATOM   1287 N N     . GLU A 1 185 ? 10.668 11.149  -5.939  1.00 32.28 ? 176 GLU A N     1 
ATOM   1288 C CA    . GLU A 1 185 ? 10.257 11.737  -7.209  1.00 36.38 ? 176 GLU A CA    1 
ATOM   1289 C C     . GLU A 1 185 ? 9.965  10.659  -8.245  1.00 36.50 ? 176 GLU A C     1 
ATOM   1290 O O     . GLU A 1 185 ? 9.021  10.785  -9.034  1.00 41.23 ? 176 GLU A O     1 
ATOM   1291 C CB    . GLU A 1 185 ? 11.333 12.694  -7.717  1.00 35.83 ? 176 GLU A CB    1 
ATOM   1292 C CG    . GLU A 1 185 ? 11.036 13.288  -9.083  1.00 50.17 ? 176 GLU A CG    1 
ATOM   1293 C CD    . GLU A 1 185 ? 12.115 14.243  -9.544  1.00 50.75 ? 176 GLU A CD    1 
ATOM   1294 O OE1   . GLU A 1 185 ? 13.091 14.444  -8.789  1.00 51.61 ? 176 GLU A OE1   1 
ATOM   1295 O OE2   . GLU A 1 185 ? 11.990 14.794  -10.659 1.00 62.77 ? 176 GLU A OE2   1 
ATOM   1296 N N     . ALA A 1 186 ? 10.753 9.582   -8.251  1.00 38.19 ? 177 ALA A N     1 
ATOM   1297 C CA    . ALA A 1 186 ? 10.507 8.487   -9.180  1.00 37.24 ? 177 ALA A CA    1 
ATOM   1298 C C     . ALA A 1 186 ? 9.299  7.648   -8.790  1.00 39.66 ? 177 ALA A C     1 
ATOM   1299 O O     . ALA A 1 186 ? 8.924  6.747   -9.547  1.00 38.98 ? 177 ALA A O     1 
ATOM   1300 C CB    . ALA A 1 186 ? 11.743 7.592   -9.286  1.00 33.28 ? 177 ALA A CB    1 
ATOM   1301 N N     . GLY A 1 187 ? 8.686  7.916   -7.642  1.00 34.75 ? 178 GLY A N     1 
ATOM   1302 C CA    . GLY A 1 187 ? 7.526  7.175   -7.204  1.00 36.05 ? 178 GLY A CA    1 
ATOM   1303 C C     . GLY A 1 187 ? 7.801  6.051   -6.233  1.00 35.96 ? 178 GLY A C     1 
ATOM   1304 O O     . GLY A 1 187 ? 6.877  5.293   -5.919  1.00 41.25 ? 178 GLY A O     1 
ATOM   1305 N N     . PHE A 1 188 ? 9.037  5.910   -5.758  1.00 32.13 ? 179 PHE A N     1 
ATOM   1306 C CA    . PHE A 1 188 ? 9.337  4.889   -4.764  1.00 38.37 ? 179 PHE A CA    1 
ATOM   1307 C C     . PHE A 1 188 ? 8.546  5.151   -3.490  1.00 35.58 ? 179 PHE A C     1 
ATOM   1308 O O     . PHE A 1 188 ? 8.353  6.301   -3.084  1.00 36.17 ? 179 PHE A O     1 
ATOM   1309 C CB    . PHE A 1 188 ? 10.835 4.867   -4.453  1.00 30.13 ? 179 PHE A CB    1 
ATOM   1310 C CG    . PHE A 1 188 ? 11.659 4.104   -5.453  1.00 33.35 ? 179 PHE A CG    1 
ATOM   1311 C CD1   . PHE A 1 188 ? 11.667 2.719   -5.453  1.00 32.62 ? 179 PHE A CD1   1 
ATOM   1312 C CD2   . PHE A 1 188 ? 12.438 4.771   -6.385  1.00 32.76 ? 179 PHE A CD2   1 
ATOM   1313 C CE1   . PHE A 1 188 ? 12.427 2.017   -6.365  1.00 30.27 ? 179 PHE A CE1   1 
ATOM   1314 C CE2   . PHE A 1 188 ? 13.200 4.073   -7.301  1.00 30.80 ? 179 PHE A CE2   1 
ATOM   1315 C CZ    . PHE A 1 188 ? 13.195 2.693   -7.289  1.00 30.14 ? 179 PHE A CZ    1 
ATOM   1316 N N     . ASP A 1 189 ? 8.077  4.073   -2.858  1.00 42.52 ? 180 ASP A N     1 
ATOM   1317 C CA    . ASP A 1 189 ? 7.380  4.216   -1.586  1.00 36.22 ? 180 ASP A CA    1 
ATOM   1318 C C     . ASP A 1 189 ? 8.318  4.644   -0.468  1.00 38.75 ? 180 ASP A C     1 
ATOM   1319 O O     . ASP A 1 189 ? 7.854  5.179   0.544   1.00 41.46 ? 180 ASP A O     1 
ATOM   1320 C CB    . ASP A 1 189 ? 6.689  2.907   -1.207  1.00 39.49 ? 180 ASP A CB    1 
ATOM   1321 C CG    . ASP A 1 189 ? 5.614  2.506   -2.197  1.00 39.83 ? 180 ASP A CG    1 
ATOM   1322 O OD1   . ASP A 1 189 ? 4.620  3.248   -2.330  1.00 42.65 ? 180 ASP A OD1   1 
ATOM   1323 O OD2   . ASP A 1 189 ? 5.760  1.443   -2.838  1.00 39.45 ? 180 ASP A OD2   1 
ATOM   1324 N N     . GLY A 1 190 ? 9.616  4.423   -0.628  1.00 42.18 ? 181 GLY A N     1 
ATOM   1325 C CA    . GLY A 1 190 ? 10.570 4.792   0.398   1.00 38.25 ? 181 GLY A CA    1 
ATOM   1326 C C     . GLY A 1 190 ? 11.958 4.346   0.001   1.00 38.02 ? 181 GLY A C     1 
ATOM   1327 O O     . GLY A 1 190 ? 12.184 3.888   -1.121  1.00 35.66 ? 181 GLY A O     1 
ATOM   1328 N N     . ILE A 1 191 ? 12.894 4.489   0.936   1.00 32.67 ? 182 ILE A N     1 
ATOM   1329 C CA    . ILE A 1 191 ? 14.283 4.130   0.687   1.00 26.32 ? 182 ILE A CA    1 
ATOM   1330 C C     . ILE A 1 191 ? 14.816 3.305   1.849   1.00 31.76 ? 182 ILE A C     1 
ATOM   1331 O O     . ILE A 1 191 ? 14.347 3.414   2.987   1.00 34.53 ? 182 ILE A O     1 
ATOM   1332 C CB    . ILE A 1 191 ? 15.179 5.372   0.460   1.00 30.69 ? 182 ILE A CB    1 
ATOM   1333 C CG1   . ILE A 1 191 ? 15.285 6.208   1.738   1.00 32.51 ? 182 ILE A CG1   1 
ATOM   1334 C CG2   . ILE A 1 191 ? 14.667 6.212   -0.695  1.00 34.33 ? 182 ILE A CG2   1 
ATOM   1335 C CD1   . ILE A 1 191 ? 16.654 6.168   2.369   1.00 32.55 ? 182 ILE A CD1   1 
ATOM   1336 N N     . GLU A 1 192 ? 15.806 2.470   1.549   1.00 31.45 ? 183 GLU A N     1 
ATOM   1337 C CA    . GLU A 1 192 ? 16.572 1.752   2.556   1.00 26.67 ? 183 GLU A CA    1 
ATOM   1338 C C     . GLU A 1 192 ? 18.001 2.270   2.539   1.00 28.83 ? 183 GLU A C     1 
ATOM   1339 O O     . GLU A 1 192 ? 18.594 2.433   1.467   1.00 34.49 ? 183 GLU A O     1 
ATOM   1340 C CB    . GLU A 1 192 ? 16.557 0.241   2.309   1.00 31.25 ? 183 GLU A CB    1 
ATOM   1341 C CG    . GLU A 1 192 ? 17.391 -0.543  3.321   1.00 34.43 ? 183 GLU A CG    1 
ATOM   1342 C CD    . GLU A 1 192 ? 17.351 -2.044  3.098   1.00 35.11 ? 183 GLU A CD    1 
ATOM   1343 O OE1   . GLU A 1 192 ? 18.186 -2.560  2.325   1.00 37.46 ? 183 GLU A OE1   1 
ATOM   1344 O OE2   . GLU A 1 192 ? 16.489 -2.711  3.703   1.00 35.27 ? 183 GLU A OE2   1 
ATOM   1345 N N     . ILE A 1 193 ? 18.545 2.539   3.719   1.00 30.01 ? 184 ILE A N     1 
ATOM   1346 C CA    . ILE A 1 193 ? 19.934 2.958   3.855   1.00 25.42 ? 184 ILE A CA    1 
ATOM   1347 C C     . ILE A 1 193 ? 20.790 1.706   3.985   1.00 31.72 ? 184 ILE A C     1 
ATOM   1348 O O     . ILE A 1 193 ? 20.602 0.910   4.911   1.00 28.33 ? 184 ILE A O     1 
ATOM   1349 C CB    . ILE A 1 193 ? 20.119 3.888   5.063   1.00 30.86 ? 184 ILE A CB    1 
ATOM   1350 C CG1   . ILE A 1 193 ? 19.471 5.247   4.791   1.00 31.71 ? 184 ILE A CG1   1 
ATOM   1351 C CG2   . ILE A 1 193 ? 21.591 4.063   5.375   1.00 26.68 ? 184 ILE A CG2   1 
ATOM   1352 C CD1   . ILE A 1 193 ? 20.063 5.973   3.604   1.00 35.22 ? 184 ILE A CD1   1 
ATOM   1353 N N     . HIS A 1 194 ? 21.721 1.523   3.050   1.00 27.96 ? 185 HIS A N     1 
ATOM   1354 C CA    . HIS A 1 194 ? 22.601 0.354   3.039   1.00 29.41 ? 185 HIS A CA    1 
ATOM   1355 C C     . HIS A 1 194 ? 23.797 0.646   3.936   1.00 28.30 ? 185 HIS A C     1 
ATOM   1356 O O     . HIS A 1 194 ? 24.751 1.308   3.524   1.00 27.27 ? 185 HIS A O     1 
ATOM   1357 C CB    . HIS A 1 194 ? 23.034 0.025   1.615   1.00 30.61 ? 185 HIS A CB    1 
ATOM   1358 C CG    . HIS A 1 194 ? 23.751 -1.283  1.480   1.00 33.89 ? 185 HIS A CG    1 
ATOM   1359 N ND1   . HIS A 1 194 ? 24.217 -1.996  2.563   1.00 35.13 ? 185 HIS A ND1   1 
ATOM   1360 C CD2   . HIS A 1 194 ? 24.096 -1.998  0.383   1.00 32.98 ? 185 HIS A CD2   1 
ATOM   1361 C CE1   . HIS A 1 194 ? 24.811 -3.098  2.139   1.00 36.09 ? 185 HIS A CE1   1 
ATOM   1362 N NE2   . HIS A 1 194 ? 24.753 -3.122  0.820   1.00 31.89 ? 185 HIS A NE2   1 
ATOM   1363 N N     . GLY A 1 195 ? 23.754 0.146   5.167   1.00 29.45 ? 186 GLY A N     1 
ATOM   1364 C CA    . GLY A 1 195 ? 24.852 0.369   6.089   1.00 36.91 ? 186 GLY A CA    1 
ATOM   1365 C C     . GLY A 1 195 ? 25.497 -0.919  6.554   1.00 37.65 ? 186 GLY A C     1 
ATOM   1366 O O     . GLY A 1 195 ? 25.899 -1.038  7.715   1.00 34.99 ? 186 GLY A O     1 
ATOM   1367 N N     . ALA A 1 196 ? 25.613 -1.887  5.649   1.00 38.12 ? 187 ALA A N     1 
ATOM   1368 C CA    . ALA A 1 196 ? 26.045 -3.234  5.986   1.00 37.23 ? 187 ALA A CA    1 
ATOM   1369 C C     . ALA A 1 196 ? 27.082 -3.714  4.978   1.00 36.28 ? 187 ALA A C     1 
ATOM   1370 O O     . ALA A 1 196 ? 27.477 -2.990  4.059   1.00 31.58 ? 187 ALA A O     1 
ATOM   1371 C CB    . ALA A 1 196 ? 24.850 -4.195  6.026   1.00 35.62 ? 187 ALA A CB    1 
ATOM   1372 N N     . HIS A 1 197 ? 27.531 -4.955  5.179   1.00 36.43 ? 188 HIS A N     1 
ATOM   1373 C CA    . HIS A 1 197 ? 28.381 -5.677  4.232   1.00 35.53 ? 188 HIS A CA    1 
ATOM   1374 C C     . HIS A 1 197 ? 29.700 -4.956  3.963   1.00 38.84 ? 188 HIS A C     1 
ATOM   1375 O O     . HIS A 1 197 ? 30.298 -5.114  2.895   1.00 34.57 ? 188 HIS A O     1 
ATOM   1376 C CB    . HIS A 1 197 ? 27.636 -5.945  2.923   1.00 27.76 ? 188 HIS A CB    1 
ATOM   1377 C CG    . HIS A 1 197 ? 26.354 -6.695  3.108   1.00 30.06 ? 188 HIS A CG    1 
ATOM   1378 N ND1   . HIS A 1 197 ? 25.397 -6.791  2.120   1.00 36.68 ? 188 HIS A ND1   1 
ATOM   1379 C CD2   . HIS A 1 197 ? 25.867 -7.379  4.170   1.00 40.71 ? 188 HIS A CD2   1 
ATOM   1380 C CE1   . HIS A 1 197 ? 24.380 -7.509  2.563   1.00 38.59 ? 188 HIS A CE1   1 
ATOM   1381 N NE2   . HIS A 1 197 ? 24.639 -7.876  3.805   1.00 38.68 ? 188 HIS A NE2   1 
ATOM   1382 N N     . GLY A 1 198 ? 30.166 -4.165  4.926   1.00 26.42 ? 189 GLY A N     1 
ATOM   1383 C CA    . GLY A 1 198 ? 31.489 -3.580  4.826   1.00 26.32 ? 189 GLY A CA    1 
ATOM   1384 C C     . GLY A 1 198 ? 31.638 -2.447  3.839   1.00 28.40 ? 189 GLY A C     1 
ATOM   1385 O O     . GLY A 1 198 ? 32.759 -2.160  3.410   1.00 21.53 ? 189 GLY A O     1 
ATOM   1386 N N     . TYR A 1 199 ? 30.549 -1.786  3.470   1.00 29.68 ? 190 TYR A N     1 
ATOM   1387 C CA    . TYR A 1 199 ? 30.618 -0.659  2.551   1.00 29.96 ? 190 TYR A CA    1 
ATOM   1388 C C     . TYR A 1 199 ? 30.787 0.628   3.366   1.00 31.09 ? 190 TYR A C     1 
ATOM   1389 O O     . TYR A 1 199 ? 31.154 0.572   4.542   1.00 30.09 ? 190 TYR A O     1 
ATOM   1390 C CB    . TYR A 1 199 ? 29.400 -0.695  1.623   1.00 28.46 ? 190 TYR A CB    1 
ATOM   1391 C CG    . TYR A 1 199 ? 29.433 -1.907  0.718   1.00 31.95 ? 190 TYR A CG    1 
ATOM   1392 C CD1   . TYR A 1 199 ? 30.421 -2.040  -0.252  1.00 35.22 ? 190 TYR A CD1   1 
ATOM   1393 C CD2   . TYR A 1 199 ? 28.507 -2.935  0.854   1.00 33.35 ? 190 TYR A CD2   1 
ATOM   1394 C CE1   . TYR A 1 199 ? 30.474 -3.146  -1.075  1.00 30.98 ? 190 TYR A CE1   1 
ATOM   1395 C CE2   . TYR A 1 199 ? 28.554 -4.055  0.031   1.00 29.46 ? 190 TYR A CE2   1 
ATOM   1396 C CZ    . TYR A 1 199 ? 29.542 -4.152  -0.930  1.00 33.26 ? 190 TYR A CZ    1 
ATOM   1397 O OH    . TYR A 1 199 ? 29.605 -5.253  -1.753  1.00 31.95 ? 190 TYR A OH    1 
ATOM   1398 N N     . LEU A 1 200 ? 30.529 1.793   2.757   1.00 30.42 ? 191 LEU A N     1 
ATOM   1399 C CA    . LEU A 1 200 ? 30.969 3.068   3.330   1.00 31.81 ? 191 LEU A CA    1 
ATOM   1400 C C     . LEU A 1 200 ? 30.514 3.240   4.775   1.00 32.42 ? 191 LEU A C     1 
ATOM   1401 O O     . LEU A 1 200 ? 31.327 3.516   5.664   1.00 27.78 ? 191 LEU A O     1 
ATOM   1402 C CB    . LEU A 1 200 ? 30.454 4.235   2.487   1.00 27.57 ? 191 LEU A CB    1 
ATOM   1403 C CG    . LEU A 1 200 ? 30.917 5.642   2.897   1.00 32.77 ? 191 LEU A CG    1 
ATOM   1404 C CD1   . LEU A 1 200 ? 32.343 5.641   3.455   1.00 28.86 ? 191 LEU A CD1   1 
ATOM   1405 C CD2   . LEU A 1 200 ? 30.784 6.630   1.752   1.00 44.06 ? 191 LEU A CD2   1 
ATOM   1406 N N     . ILE A 1 201 ? 29.211 3.099   5.023   1.00 34.03 ? 192 ILE A N     1 
ATOM   1407 C CA    . ILE A 1 201 ? 28.688 3.330   6.366   1.00 29.82 ? 192 ILE A CA    1 
ATOM   1408 C C     . ILE A 1 201 ? 29.287 2.333   7.349   1.00 32.54 ? 192 ILE A C     1 
ATOM   1409 O O     . ILE A 1 201 ? 29.629 2.684   8.487   1.00 32.10 ? 192 ILE A O     1 
ATOM   1410 C CB    . ILE A 1 201 ? 27.150 3.275   6.354   1.00 28.52 ? 192 ILE A CB    1 
ATOM   1411 C CG1   . ILE A 1 201 ? 26.599 4.420   5.503   1.00 28.46 ? 192 ILE A CG1   1 
ATOM   1412 C CG2   . ILE A 1 201 ? 26.598 3.337   7.771   1.00 28.75 ? 192 ILE A CG2   1 
ATOM   1413 C CD1   . ILE A 1 201 ? 25.113 4.634   5.629   1.00 29.50 ? 192 ILE A CD1   1 
ATOM   1414 N N     . ASP A 1 202 ? 29.450 1.083   6.915   1.00 26.72 ? 193 ASP A N     1 
ATOM   1415 C CA    . ASP A 1 202 ? 30.079 0.074   7.759   1.00 31.46 ? 193 ASP A CA    1 
ATOM   1416 C C     . ASP A 1 202 ? 31.555 0.372   7.982   1.00 36.75 ? 193 ASP A C     1 
ATOM   1417 O O     . ASP A 1 202 ? 32.115 -0.012  9.016   1.00 33.49 ? 193 ASP A O     1 
ATOM   1418 C CB    . ASP A 1 202 ? 29.902 -1.310  7.133   1.00 35.76 ? 193 ASP A CB    1 
ATOM   1419 C CG    . ASP A 1 202 ? 29.569 -2.374  8.157   1.00 39.99 ? 193 ASP A CG    1 
ATOM   1420 O OD1   . ASP A 1 202 ? 29.225 -2.011  9.302   1.00 40.32 ? 193 ASP A OD1   1 
ATOM   1421 O OD2   . ASP A 1 202 ? 29.654 -3.575  7.818   1.00 41.06 ? 193 ASP A OD2   1 
ATOM   1422 N N     . GLN A 1 203 ? 32.202 1.054   7.033   1.00 29.06 ? 194 GLN A N     1 
ATOM   1423 C CA    . GLN A 1 203 ? 33.598 1.432   7.212   1.00 31.69 ? 194 GLN A CA    1 
ATOM   1424 C C     . GLN A 1 203 ? 33.773 2.496   8.287   1.00 27.85 ? 194 GLN A C     1 
ATOM   1425 O O     . GLN A 1 203 ? 34.900 2.723   8.739   1.00 31.93 ? 194 GLN A O     1 
ATOM   1426 C CB    . GLN A 1 203 ? 34.187 1.923   5.888   1.00 28.90 ? 194 GLN A CB    1 
ATOM   1427 C CG    . GLN A 1 203 ? 34.325 0.838   4.835   1.00 25.45 ? 194 GLN A CG    1 
ATOM   1428 C CD    . GLN A 1 203 ? 34.302 1.392   3.426   1.00 29.81 ? 194 GLN A CD    1 
ATOM   1429 O OE1   . GLN A 1 203 ? 34.768 2.503   3.177   1.00 35.06 ? 194 GLN A OE1   1 
ATOM   1430 N NE2   . GLN A 1 203 ? 33.759 0.619   2.494   1.00 29.96 ? 194 GLN A NE2   1 
ATOM   1431 N N     . PHE A 1 204 ? 32.692 3.163   8.690   1.00 31.82 ? 195 PHE A N     1 
ATOM   1432 C CA    . PHE A 1 204 ? 32.731 4.063   9.835   1.00 34.42 ? 195 PHE A CA    1 
ATOM   1433 C C     . PHE A 1 204 ? 32.308 3.372   11.124  1.00 32.97 ? 195 PHE A C     1 
ATOM   1434 O O     . PHE A 1 204 ? 32.754 3.769   12.207  1.00 36.20 ? 195 PHE A O     1 
ATOM   1435 C CB    . PHE A 1 204 ? 31.823 5.275   9.596   1.00 27.70 ? 195 PHE A CB    1 
ATOM   1436 C CG    . PHE A 1 204 ? 32.438 6.342   8.734   1.00 32.59 ? 195 PHE A CG    1 
ATOM   1437 C CD1   . PHE A 1 204 ? 32.330 6.284   7.354   1.00 27.45 ? 195 PHE A CD1   1 
ATOM   1438 C CD2   . PHE A 1 204 ? 33.110 7.411   9.304   1.00 37.12 ? 195 PHE A CD2   1 
ATOM   1439 C CE1   . PHE A 1 204 ? 32.890 7.268   6.556   1.00 33.22 ? 195 PHE A CE1   1 
ATOM   1440 C CE2   . PHE A 1 204 ? 33.672 8.399   8.514   1.00 37.23 ? 195 PHE A CE2   1 
ATOM   1441 C CZ    . PHE A 1 204 ? 33.561 8.327   7.137   1.00 36.95 ? 195 PHE A CZ    1 
ATOM   1442 N N     . LEU A 1 205 ? 31.465 2.342   11.028  1.00 31.92 ? 196 LEU A N     1 
ATOM   1443 C CA    . LEU A 1 205 ? 30.920 1.691   12.215  1.00 35.24 ? 196 LEU A CA    1 
ATOM   1444 C C     . LEU A 1 205 ? 31.939 0.773   12.880  1.00 36.30 ? 196 LEU A C     1 
ATOM   1445 O O     . LEU A 1 205 ? 32.091 0.788   14.106  1.00 37.62 ? 196 LEU A O     1 
ATOM   1446 C CB    . LEU A 1 205 ? 29.667 0.896   11.846  1.00 27.24 ? 196 LEU A CB    1 
ATOM   1447 C CG    . LEU A 1 205 ? 28.368 1.655   11.578  1.00 25.43 ? 196 LEU A CG    1 
ATOM   1448 C CD1   . LEU A 1 205 ? 27.308 0.686   11.099  1.00 25.07 ? 196 LEU A CD1   1 
ATOM   1449 C CD2   . LEU A 1 205 ? 27.904 2.393   12.826  1.00 35.19 ? 196 LEU A CD2   1 
ATOM   1450 N N     . LYS A 1 206 ? 32.641 -0.035  12.087  1.00 32.38 ? 197 LYS A N     1 
ATOM   1451 C CA    . LYS A 1 206 ? 33.461 -1.112  12.626  1.00 40.19 ? 197 LYS A CA    1 
ATOM   1452 C C     . LYS A 1 206 ? 34.824 -0.592  13.064  1.00 39.04 ? 197 LYS A C     1 
ATOM   1453 O O     . LYS A 1 206 ? 35.487 0.136   12.320  1.00 30.16 ? 197 LYS A O     1 
ATOM   1454 C CB    . LYS A 1 206 ? 33.627 -2.217  11.584  1.00 41.14 ? 197 LYS A CB    1 
ATOM   1455 C CG    . LYS A 1 206 ? 32.318 -2.690  10.973  1.00 37.59 ? 197 LYS A CG    1 
ATOM   1456 C CD    . LYS A 1 206 ? 31.836 -3.976  11.623  1.00 38.59 ? 197 LYS A CD    1 
ATOM   1457 C CE    . LYS A 1 206 ? 30.395 -4.278  11.251  1.00 34.74 ? 197 LYS A CE    1 
ATOM   1458 N NZ    . LYS A 1 206 ? 30.305 -5.400  10.274  1.00 43.01 ? 197 LYS A NZ    1 
ATOM   1459 N N     . ASP A 1 207 ? 35.246 -0.983  14.272  1.00 35.62 ? 198 ASP A N     1 
ATOM   1460 C CA    . ASP A 1 207 ? 36.541 -0.546  14.786  1.00 34.46 ? 198 ASP A CA    1 
ATOM   1461 C C     . ASP A 1 207 ? 37.701 -1.251  14.098  1.00 32.32 ? 198 ASP A C     1 
ATOM   1462 O O     . ASP A 1 207 ? 38.840 -0.782  14.193  1.00 45.84 ? 198 ASP A O     1 
ATOM   1463 C CB    . ASP A 1 207 ? 36.618 -0.750  16.306  1.00 31.15 ? 198 ASP A CB    1 
ATOM   1464 C CG    . ASP A 1 207 ? 36.379 -2.194  16.733  1.00 39.91 ? 198 ASP A CG    1 
ATOM   1465 O OD1   . ASP A 1 207 ? 36.508 -3.116  15.899  1.00 43.14 ? 198 ASP A OD1   1 
ATOM   1466 O OD2   . ASP A 1 207 ? 36.072 -2.410  17.924  1.00 41.18 ? 198 ASP A OD2   1 
ATOM   1467 N N     . GLY A 1 208 ? 37.443 -2.369  13.417  1.00 33.30 ? 199 GLY A N     1 
ATOM   1468 C CA    . GLY A 1 208 ? 38.470 -2.967  12.583  1.00 34.99 ? 199 GLY A CA    1 
ATOM   1469 C C     . GLY A 1 208 ? 38.867 -2.108  11.402  1.00 38.27 ? 199 GLY A C     1 
ATOM   1470 O O     . GLY A 1 208 ? 39.947 -2.310  10.836  1.00 49.85 ? 199 GLY A O     1 
ATOM   1471 N N     . ILE A 1 209 ? 38.021 -1.153  11.020  1.00 34.82 ? 200 ILE A N     1 
ATOM   1472 C CA    . ILE A 1 209 ? 38.303 -0.222  9.929   1.00 37.16 ? 200 ILE A CA    1 
ATOM   1473 C C     . ILE A 1 209 ? 38.474 1.201   10.451  1.00 43.07 ? 200 ILE A C     1 
ATOM   1474 O O     . ILE A 1 209 ? 39.505 1.837   10.224  1.00 44.65 ? 200 ILE A O     1 
ATOM   1475 C CB    . ILE A 1 209 ? 37.205 -0.288  8.844   1.00 34.48 ? 200 ILE A CB    1 
ATOM   1476 C CG1   . ILE A 1 209 ? 36.996 -1.728  8.373   1.00 38.48 ? 200 ILE A CG1   1 
ATOM   1477 C CG2   . ILE A 1 209 ? 37.555 0.619   7.673   1.00 38.47 ? 200 ILE A CG2   1 
ATOM   1478 C CD1   . ILE A 1 209 ? 35.642 -1.966  7.745   1.00 33.97 ? 200 ILE A CD1   1 
ATOM   1479 N N     . ASN A 1 210 ? 37.470 1.717   11.157  1.00 38.18 ? 201 ASN A N     1 
ATOM   1480 C CA    . ASN A 1 210 ? 37.464 3.107   11.600  1.00 36.36 ? 201 ASN A CA    1 
ATOM   1481 C C     . ASN A 1 210 ? 38.485 3.301   12.714  1.00 41.50 ? 201 ASN A C     1 
ATOM   1482 O O     . ASN A 1 210 ? 38.299 2.809   13.830  1.00 44.70 ? 201 ASN A O     1 
ATOM   1483 C CB    . ASN A 1 210 ? 36.066 3.499   12.068  1.00 38.64 ? 201 ASN A CB    1 
ATOM   1484 C CG    . ASN A 1 210 ? 35.916 4.994   12.282  1.00 35.33 ? 201 ASN A CG    1 
ATOM   1485 O OD1   . ASN A 1 210 ? 36.902 5.723   12.393  1.00 36.48 ? 201 ASN A OD1   1 
ATOM   1486 N ND2   . ASN A 1 210 ? 34.675 5.457   12.343  1.00 32.51 ? 201 ASN A ND2   1 
ATOM   1487 N N     . ASP A 1 211 ? 39.563 4.030   12.413  1.00 49.64 ? 202 ASP A N     1 
ATOM   1488 C CA    . ASP A 1 211 ? 40.565 4.393   13.408  1.00 51.91 ? 202 ASP A CA    1 
ATOM   1489 C C     . ASP A 1 211 ? 40.816 5.899   13.432  1.00 50.60 ? 202 ASP A C     1 
ATOM   1490 O O     . ASP A 1 211 ? 41.883 6.338   13.874  1.00 55.13 ? 202 ASP A O     1 
ATOM   1491 C CB    . ASP A 1 211 ? 41.872 3.632   13.162  1.00 51.09 ? 202 ASP A CB    1 
ATOM   1492 C CG    . ASP A 1 211 ? 42.711 4.248   12.060  1.00 59.35 ? 202 ASP A CG    1 
ATOM   1493 O OD1   . ASP A 1 211 ? 42.166 4.506   10.965  1.00 57.10 ? 202 ASP A OD1   1 
ATOM   1494 O OD2   . ASP A 1 211 ? 43.917 4.478   12.292  1.00 75.79 ? 202 ASP A OD2   1 
ATOM   1495 N N     . ARG A 1 212 ? 39.849 6.696   12.981  1.00 45.40 ? 203 ARG A N     1 
ATOM   1496 C CA    . ARG A 1 212 ? 40.022 8.142   12.942  1.00 41.13 ? 203 ARG A CA    1 
ATOM   1497 C C     . ARG A 1 212 ? 40.180 8.710   14.348  1.00 46.69 ? 203 ARG A C     1 
ATOM   1498 O O     . ARG A 1 212 ? 39.644 8.179   15.325  1.00 45.61 ? 203 ARG A O     1 
ATOM   1499 C CB    . ARG A 1 212 ? 38.830 8.804   12.251  1.00 40.40 ? 203 ARG A CB    1 
ATOM   1500 C CG    . ARG A 1 212 ? 38.452 8.193   10.916  1.00 40.13 ? 203 ARG A CG    1 
ATOM   1501 C CD    . ARG A 1 212 ? 37.066 8.646   10.494  1.00 35.70 ? 203 ARG A CD    1 
ATOM   1502 N NE    . ARG A 1 212 ? 36.975 10.099  10.404  1.00 32.93 ? 203 ARG A NE    1 
ATOM   1503 C CZ    . ARG A 1 212 ? 37.138 10.788  9.283   1.00 41.53 ? 203 ARG A CZ    1 
ATOM   1504 N NH1   . ARG A 1 212 ? 37.411 10.187  8.136   1.00 34.21 ? 203 ARG A NH1   1 
ATOM   1505 N NH2   . ARG A 1 212 ? 37.022 12.113  9.314   1.00 38.50 ? 203 ARG A NH2   1 
ATOM   1506 N N     . THR A 1 213 ? 40.923 9.811   14.441  1.00 47.14 ? 204 THR A N     1 
ATOM   1507 C CA    . THR A 1 213 ? 41.138 10.505  15.702  1.00 49.19 ? 204 THR A CA    1 
ATOM   1508 C C     . THR A 1 213 ? 40.246 11.729  15.862  1.00 48.49 ? 204 THR A C     1 
ATOM   1509 O O     . THR A 1 213 ? 40.389 12.457  16.849  1.00 49.84 ? 204 THR A O     1 
ATOM   1510 C CB    . THR A 1 213 ? 42.609 10.920  15.835  1.00 54.18 ? 204 THR A CB    1 
ATOM   1511 O OG1   . THR A 1 213 ? 42.929 11.890  14.830  1.00 58.50 ? 204 THR A OG1   1 
ATOM   1512 C CG2   . THR A 1 213 ? 43.521 9.711   15.673  1.00 48.86 ? 204 THR A CG2   1 
ATOM   1513 N N     . ASP A 1 214 ? 39.334 11.973  14.926  1.00 48.94 ? 205 ASP A N     1 
ATOM   1514 C CA    . ASP A 1 214 ? 38.410 13.090  15.015  1.00 47.31 ? 205 ASP A CA    1 
ATOM   1515 C C     . ASP A 1 214 ? 37.091 12.615  15.622  1.00 38.84 ? 205 ASP A C     1 
ATOM   1516 O O     . ASP A 1 214 ? 36.997 11.520  16.185  1.00 44.62 ? 205 ASP A O     1 
ATOM   1517 C CB    . ASP A 1 214 ? 38.224 13.738  13.638  1.00 44.86 ? 205 ASP A CB    1 
ATOM   1518 C CG    . ASP A 1 214 ? 37.482 12.844  12.655  1.00 45.38 ? 205 ASP A CG    1 
ATOM   1519 O OD1   . ASP A 1 214 ? 37.340 11.630  12.920  1.00 38.22 ? 205 ASP A OD1   1 
ATOM   1520 O OD2   . ASP A 1 214 ? 37.047 13.362  11.604  1.00 42.95 ? 205 ASP A OD2   1 
ATOM   1521 N N     . GLU A 1 215 ? 36.049 13.439  15.496  1.00 44.61 ? 206 GLU A N     1 
ATOM   1522 C CA    . GLU A 1 215 ? 34.772 13.148  16.137  1.00 44.20 ? 206 GLU A CA    1 
ATOM   1523 C C     . GLU A 1 215 ? 34.005 12.014  15.469  1.00 41.69 ? 206 GLU A C     1 
ATOM   1524 O O     . GLU A 1 215 ? 32.955 11.618  15.987  1.00 37.32 ? 206 GLU A O     1 
ATOM   1525 C CB    . GLU A 1 215 ? 33.904 14.407  16.166  1.00 45.98 ? 206 GLU A CB    1 
ATOM   1526 C CG    . GLU A 1 215 ? 33.325 14.794  14.816  1.00 39.71 ? 206 GLU A CG    1 
ATOM   1527 C CD    . GLU A 1 215 ? 34.007 16.007  14.217  1.00 50.43 ? 206 GLU A CD    1 
ATOM   1528 O OE1   . GLU A 1 215 ? 35.253 16.000  14.113  1.00 55.70 ? 206 GLU A OE1   1 
ATOM   1529 O OE2   . GLU A 1 215 ? 33.299 16.968  13.851  1.00 50.13 ? 206 GLU A OE2   1 
ATOM   1530 N N     . TYR A 1 216 ? 34.486 11.489  14.344  1.00 39.60 ? 207 TYR A N     1 
ATOM   1531 C CA    . TYR A 1 216 ? 33.826 10.389  13.655  1.00 35.68 ? 207 TYR A CA    1 
ATOM   1532 C C     . TYR A 1 216 ? 34.495 9.045   13.914  1.00 37.25 ? 207 TYR A C     1 
ATOM   1533 O O     . TYR A 1 216 ? 34.119 8.048   13.291  1.00 39.92 ? 207 TYR A O     1 
ATOM   1534 C CB    . TYR A 1 216 ? 33.772 10.663  12.149  1.00 38.12 ? 207 TYR A CB    1 
ATOM   1535 C CG    . TYR A 1 216 ? 32.719 11.673  11.748  1.00 35.55 ? 207 TYR A CG    1 
ATOM   1536 C CD1   . TYR A 1 216 ? 31.411 11.280  11.496  1.00 34.71 ? 207 TYR A CD1   1 
ATOM   1537 C CD2   . TYR A 1 216 ? 33.033 13.021  11.624  1.00 37.50 ? 207 TYR A CD2   1 
ATOM   1538 C CE1   . TYR A 1 216 ? 30.445 12.200  11.130  1.00 34.47 ? 207 TYR A CE1   1 
ATOM   1539 C CE2   . TYR A 1 216 ? 32.074 13.948  11.259  1.00 34.21 ? 207 TYR A CE2   1 
ATOM   1540 C CZ    . TYR A 1 216 ? 30.784 13.533  11.012  1.00 40.28 ? 207 TYR A CZ    1 
ATOM   1541 O OH    . TYR A 1 216 ? 29.829 14.456  10.648  1.00 39.44 ? 207 TYR A OH    1 
ATOM   1542 N N     . GLY A 1 217 ? 35.476 8.994   14.813  1.00 36.74 ? 208 GLY A N     1 
ATOM   1543 C CA    . GLY A 1 217 ? 36.165 7.757   15.110  1.00 40.02 ? 208 GLY A CA    1 
ATOM   1544 C C     . GLY A 1 217 ? 36.551 7.686   16.572  1.00 43.92 ? 208 GLY A C     1 
ATOM   1545 O O     . GLY A 1 217 ? 36.353 8.632   17.338  1.00 39.67 ? 208 GLY A O     1 
ATOM   1546 N N     . GLY A 1 218 ? 37.108 6.541   16.956  1.00 40.16 ? 209 GLY A N     1 
ATOM   1547 C CA    . GLY A 1 218 ? 37.564 6.341   18.317  1.00 45.31 ? 209 GLY A CA    1 
ATOM   1548 C C     . GLY A 1 218 ? 36.540 5.666   19.204  1.00 44.72 ? 209 GLY A C     1 
ATOM   1549 O O     . GLY A 1 218 ? 36.550 4.441   19.360  1.00 52.72 ? 209 GLY A O     1 
ATOM   1550 N N     . SER A 1 219 ? 35.648 6.457   19.791  1.00 41.35 ? 210 SER A N     1 
ATOM   1551 C CA    . SER A 1 219 ? 34.639 5.923   20.689  1.00 46.00 ? 210 SER A CA    1 
ATOM   1552 C C     . SER A 1 219 ? 33.505 5.271   19.905  1.00 39.48 ? 210 SER A C     1 
ATOM   1553 O O     . SER A 1 219 ? 33.320 5.507   18.708  1.00 39.60 ? 210 SER A O     1 
ATOM   1554 C CB    . SER A 1 219 ? 34.082 7.026   21.587  1.00 44.41 ? 210 SER A CB    1 
ATOM   1555 O OG    . SER A 1 219 ? 32.940 7.625   21.000  1.00 46.14 ? 210 SER A OG    1 
ATOM   1556 N N     . LEU A 1 220 ? 32.735 4.438   20.609  1.00 38.61 ? 211 LEU A N     1 
ATOM   1557 C CA    . LEU A 1 220 ? 31.602 3.764   19.986  1.00 36.86 ? 211 LEU A CA    1 
ATOM   1558 C C     . LEU A 1 220 ? 30.564 4.765   19.496  1.00 41.97 ? 211 LEU A C     1 
ATOM   1559 O O     . LEU A 1 220 ? 29.997 4.603   18.408  1.00 39.74 ? 211 LEU A O     1 
ATOM   1560 C CB    . LEU A 1 220 ? 30.978 2.781   20.975  1.00 39.14 ? 211 LEU A CB    1 
ATOM   1561 C CG    . LEU A 1 220 ? 29.727 2.024   20.532  1.00 40.36 ? 211 LEU A CG    1 
ATOM   1562 C CD1   . LEU A 1 220 ? 29.969 1.292   19.219  1.00 29.07 ? 211 LEU A CD1   1 
ATOM   1563 C CD2   . LEU A 1 220 ? 29.299 1.054   21.625  1.00 35.31 ? 211 LEU A CD2   1 
ATOM   1564 N N     . ALA A 1 221 ? 30.301 5.810   20.284  1.00 35.93 ? 212 ALA A N     1 
ATOM   1565 C CA    . ALA A 1 221 ? 29.341 6.825   19.867  1.00 38.92 ? 212 ALA A CA    1 
ATOM   1566 C C     . ALA A 1 221 ? 29.846 7.598   18.656  1.00 35.86 ? 212 ALA A C     1 
ATOM   1567 O O     . ALA A 1 221 ? 29.059 7.969   17.778  1.00 40.39 ? 212 ALA A O     1 
ATOM   1568 C CB    . ALA A 1 221 ? 29.045 7.776   21.027  1.00 40.45 ? 212 ALA A CB    1 
ATOM   1569 N N     . ASN A 1 222 ? 31.157 7.844   18.590  1.00 32.09 ? 213 ASN A N     1 
ATOM   1570 C CA    . ASN A 1 222 ? 31.716 8.599   17.474  1.00 40.51 ? 213 ASN A CA    1 
ATOM   1571 C C     . ASN A 1 222 ? 31.610 7.815   16.172  1.00 38.64 ? 213 ASN A C     1 
ATOM   1572 O O     . ASN A 1 222 ? 31.267 8.378   15.126  1.00 39.51 ? 213 ASN A O     1 
ATOM   1573 C CB    . ASN A 1 222 ? 33.171 8.963   17.766  1.00 39.23 ? 213 ASN A CB    1 
ATOM   1574 C CG    . ASN A 1 222 ? 33.296 10.182  18.659  1.00 44.57 ? 213 ASN A CG    1 
ATOM   1575 O OD1   . ASN A 1 222 ? 32.295 10.784  19.045  1.00 38.23 ? 213 ASN A OD1   1 
ATOM   1576 N ND2   . ASN A 1 222 ? 34.529 10.552  18.992  1.00 41.27 ? 213 ASN A ND2   1 
ATOM   1577 N N     . ARG A 1 223 ? 31.890 6.512   16.221  1.00 30.55 ? 214 ARG A N     1 
ATOM   1578 C CA    . ARG A 1 223 ? 31.794 5.676   15.033  1.00 35.18 ? 214 ARG A CA    1 
ATOM   1579 C C     . ARG A 1 223 ? 30.355 5.491   14.568  1.00 30.62 ? 214 ARG A C     1 
ATOM   1580 O O     . ARG A 1 223 ? 30.134 5.092   13.420  1.00 34.63 ? 214 ARG A O     1 
ATOM   1581 C CB    . ARG A 1 223 ? 32.459 4.326   15.309  1.00 24.12 ? 214 ARG A CB    1 
ATOM   1582 C CG    . ARG A 1 223 ? 33.937 4.467   15.645  1.00 33.74 ? 214 ARG A CG    1 
ATOM   1583 C CD    . ARG A 1 223 ? 34.704 3.174   15.452  1.00 39.12 ? 214 ARG A CD    1 
ATOM   1584 N NE    . ARG A 1 223 ? 33.862 1.999   15.634  1.00 40.24 ? 214 ARG A NE    1 
ATOM   1585 C CZ    . ARG A 1 223 ? 33.739 1.336   16.775  1.00 45.09 ? 214 ARG A CZ    1 
ATOM   1586 N NH1   . ARG A 1 223 ? 34.387 1.711   17.866  1.00 44.58 ? 214 ARG A NH1   1 
ATOM   1587 N NH2   . ARG A 1 223 ? 32.946 0.269   16.824  1.00 43.12 ? 214 ARG A NH2   1 
ATOM   1588 N N     . CYS A 1 224 ? 29.377 5.784   15.420  1.00 30.53 ? 215 CYS A N     1 
ATOM   1589 C CA    . CYS A 1 224 ? 27.973 5.741   15.037  1.00 29.74 ? 215 CYS A CA    1 
ATOM   1590 C C     . CYS A 1 224 ? 27.471 7.065   14.476  1.00 31.49 ? 215 CYS A C     1 
ATOM   1591 O O     . CYS A 1 224 ? 26.314 7.142   14.051  1.00 34.54 ? 215 CYS A O     1 
ATOM   1592 C CB    . CYS A 1 224 ? 27.111 5.346   16.239  1.00 39.12 ? 215 CYS A CB    1 
ATOM   1593 S SG    . CYS A 1 224 ? 27.037 3.581   16.602  1.00 37.55 ? 215 CYS A SG    1 
ATOM   1594 N N     . LYS A 1 225 ? 28.306 8.108   14.469  1.00 32.27 ? 216 LYS A N     1 
ATOM   1595 C CA    . LYS A 1 225 ? 27.831 9.426   14.059  1.00 31.72 ? 216 LYS A CA    1 
ATOM   1596 C C     . LYS A 1 225 ? 27.431 9.445   12.590  1.00 34.88 ? 216 LYS A C     1 
ATOM   1597 O O     . LYS A 1 225 ? 26.414 10.049  12.229  1.00 39.96 ? 216 LYS A O     1 
ATOM   1598 C CB    . LYS A 1 225 ? 28.902 10.482  14.335  1.00 32.94 ? 216 LYS A CB    1 
ATOM   1599 N N     . PHE A 1 226 ? 28.209 8.783   11.729  1.00 31.96 ? 217 PHE A N     1 
ATOM   1600 C CA    . PHE A 1 226 ? 27.953 8.863   10.293  1.00 35.79 ? 217 PHE A CA    1 
ATOM   1601 C C     . PHE A 1 226 ? 26.596 8.269   9.941   1.00 37.51 ? 217 PHE A C     1 
ATOM   1602 O O     . PHE A 1 226 ? 25.813 8.878   9.202   1.00 32.95 ? 217 PHE A O     1 
ATOM   1603 C CB    . PHE A 1 226 ? 29.065 8.164   9.512   1.00 27.91 ? 217 PHE A CB    1 
ATOM   1604 C CG    . PHE A 1 226 ? 28.947 8.322   8.018   1.00 35.65 ? 217 PHE A CG    1 
ATOM   1605 C CD1   . PHE A 1 226 ? 29.020 9.575   7.434   1.00 36.78 ? 217 PHE A CD1   1 
ATOM   1606 C CD2   . PHE A 1 226 ? 28.754 7.218   7.201   1.00 24.20 ? 217 PHE A CD2   1 
ATOM   1607 C CE1   . PHE A 1 226 ? 28.909 9.726   6.062   1.00 40.70 ? 217 PHE A CE1   1 
ATOM   1608 C CE2   . PHE A 1 226 ? 28.644 7.361   5.829   1.00 40.43 ? 217 PHE A CE2   1 
ATOM   1609 C CZ    . PHE A 1 226 ? 28.721 8.617   5.258   1.00 36.14 ? 217 PHE A CZ    1 
ATOM   1610 N N     . ILE A 1 227 ? 26.291 7.079   10.467  1.00 36.86 ? 218 ILE A N     1 
ATOM   1611 C CA    . ILE A 1 227 ? 25.000 6.474   10.161  1.00 31.73 ? 218 ILE A CA    1 
ATOM   1612 C C     . ILE A 1 227 ? 23.870 7.281   10.786  1.00 34.07 ? 218 ILE A C     1 
ATOM   1613 O O     . ILE A 1 227 ? 22.776 7.370   10.216  1.00 36.35 ? 218 ILE A O     1 
ATOM   1614 C CB    . ILE A 1 227 ? 24.963 4.997   10.602  1.00 32.69 ? 218 ILE A CB    1 
ATOM   1615 C CG1   . ILE A 1 227 ? 23.768 4.286   9.958   1.00 32.68 ? 218 ILE A CG1   1 
ATOM   1616 C CG2   . ILE A 1 227 ? 24.912 4.869   12.123  1.00 30.52 ? 218 ILE A CG2   1 
ATOM   1617 C CD1   . ILE A 1 227 ? 23.605 2.842   10.386  1.00 35.55 ? 218 ILE A CD1   1 
ATOM   1618 N N     . THR A 1 228 ? 24.113 7.902   11.943  1.00 34.29 ? 219 THR A N     1 
ATOM   1619 C CA    . THR A 1 228 ? 23.083 8.725   12.567  1.00 34.88 ? 219 THR A CA    1 
ATOM   1620 C C     . THR A 1 228 ? 22.756 9.933   11.700  1.00 32.60 ? 219 THR A C     1 
ATOM   1621 O O     . THR A 1 228 ? 21.583 10.253  11.474  1.00 35.04 ? 219 THR A O     1 
ATOM   1622 C CB    . THR A 1 228 ? 23.536 9.169   13.960  1.00 38.60 ? 219 THR A CB    1 
ATOM   1623 O OG1   . THR A 1 228 ? 23.930 8.023   14.723  1.00 31.78 ? 219 THR A OG1   1 
ATOM   1624 C CG2   . THR A 1 228 ? 22.407 9.889   14.683  1.00 35.93 ? 219 THR A CG2   1 
ATOM   1625 N N     . GLN A 1 229 ? 23.787 10.612  11.193  1.00 30.24 ? 220 GLN A N     1 
ATOM   1626 C CA    . GLN A 1 229 ? 23.565 11.800  10.377  1.00 36.03 ? 220 GLN A CA    1 
ATOM   1627 C C     . GLN A 1 229 ? 22.946 11.453  9.029   1.00 41.50 ? 220 GLN A C     1 
ATOM   1628 O O     . GLN A 1 229 ? 22.143 12.231  8.499   1.00 35.86 ? 220 GLN A O     1 
ATOM   1629 C CB    . GLN A 1 229 ? 24.880 12.555  10.184  1.00 33.72 ? 220 GLN A CB    1 
ATOM   1630 C CG    . GLN A 1 229 ? 25.373 13.250  11.443  1.00 40.98 ? 220 GLN A CG    1 
ATOM   1631 C CD    . GLN A 1 229 ? 26.751 13.857  11.278  1.00 44.19 ? 220 GLN A CD    1 
ATOM   1632 O OE1   . GLN A 1 229 ? 27.438 13.611  10.286  1.00 37.31 ? 220 GLN A OE1   1 
ATOM   1633 N NE2   . GLN A 1 229 ? 27.163 14.660  12.253  1.00 46.33 ? 220 GLN A NE2   1 
ATOM   1634 N N     . VAL A 1 230 ? 23.308 10.301  8.459   1.00 36.22 ? 221 VAL A N     1 
ATOM   1635 C CA    . VAL A 1 230 ? 22.691 9.868   7.209   1.00 33.88 ? 221 VAL A CA    1 
ATOM   1636 C C     . VAL A 1 230 ? 21.209 9.588   7.419   1.00 36.42 ? 221 VAL A C     1 
ATOM   1637 O O     . VAL A 1 230 ? 20.359 10.057  6.654   1.00 32.79 ? 221 VAL A O     1 
ATOM   1638 C CB    . VAL A 1 230 ? 23.421 8.636   6.643   1.00 33.11 ? 221 VAL A CB    1 
ATOM   1639 C CG1   . VAL A 1 230 ? 22.648 8.060   5.467   1.00 31.66 ? 221 VAL A CG1   1 
ATOM   1640 C CG2   . VAL A 1 230 ? 24.834 9.002   6.220   1.00 35.45 ? 221 VAL A CG2   1 
ATOM   1641 N N     . VAL A 1 231 ? 20.877 8.827   8.465   1.00 33.98 ? 222 VAL A N     1 
ATOM   1642 C CA    . VAL A 1 231 ? 19.478 8.512   8.739   1.00 38.61 ? 222 VAL A CA    1 
ATOM   1643 C C     . VAL A 1 231 ? 18.709 9.775   9.101   1.00 34.19 ? 222 VAL A C     1 
ATOM   1644 O O     . VAL A 1 231 ? 17.559 9.960   8.682   1.00 35.98 ? 222 VAL A O     1 
ATOM   1645 C CB    . VAL A 1 231 ? 19.374 7.445   9.846   1.00 37.80 ? 222 VAL A CB    1 
ATOM   1646 C CG1   . VAL A 1 231 ? 17.921 7.226   10.237  1.00 37.20 ? 222 VAL A CG1   1 
ATOM   1647 C CG2   . VAL A 1 231 ? 20.000 6.137   9.386   1.00 36.12 ? 222 VAL A CG2   1 
ATOM   1648 N N     . GLN A 1 232 ? 19.330 10.669  9.876   1.00 33.94 ? 223 GLN A N     1 
ATOM   1649 C CA    . GLN A 1 232 ? 18.682 11.932  10.217  1.00 37.13 ? 223 GLN A CA    1 
ATOM   1650 C C     . GLN A 1 232 ? 18.377 12.752  8.968   1.00 37.22 ? 223 GLN A C     1 
ATOM   1651 O O     . GLN A 1 232 ? 17.343 13.427  8.897   1.00 35.79 ? 223 GLN A O     1 
ATOM   1652 C CB    . GLN A 1 232 ? 19.563 12.732  11.178  1.00 40.46 ? 223 GLN A CB    1 
ATOM   1653 C CG    . GLN A 1 232 ? 19.108 12.694  12.630  1.00 45.32 ? 223 GLN A CG    1 
ATOM   1654 C CD    . GLN A 1 232 ? 20.237 12.972  13.609  1.00 50.29 ? 223 GLN A CD    1 
ATOM   1655 O OE1   . GLN A 1 232 ? 21.384 13.182  13.211  1.00 43.61 ? 223 GLN A OE1   1 
ATOM   1656 N NE2   . GLN A 1 232 ? 19.916 12.973  14.900  1.00 46.39 ? 223 GLN A NE2   1 
ATOM   1657 N N     . ALA A 1 233 ? 19.262 12.703  7.970   1.00 41.28 ? 224 ALA A N     1 
ATOM   1658 C CA    . ALA A 1 233 ? 19.071 13.524  6.778   1.00 39.86 ? 224 ALA A CA    1 
ATOM   1659 C C     . ALA A 1 233 ? 17.926 13.004  5.920   1.00 39.21 ? 224 ALA A C     1 
ATOM   1660 O O     . ALA A 1 233 ? 17.099 13.788  5.441   1.00 40.77 ? 224 ALA A O     1 
ATOM   1661 C CB    . ALA A 1 233 ? 20.361 13.585  5.965   1.00 33.91 ? 224 ALA A CB    1 
ATOM   1662 N N     . VAL A 1 234 ? 17.860 11.687  5.709   1.00 37.95 ? 225 VAL A N     1 
ATOM   1663 C CA    . VAL A 1 234 ? 16.799 11.144  4.868   1.00 33.91 ? 225 VAL A CA    1 
ATOM   1664 C C     . VAL A 1 234 ? 15.459 11.200  5.588   1.00 35.52 ? 225 VAL A C     1 
ATOM   1665 O O     . VAL A 1 234 ? 14.414 11.382  4.952   1.00 32.39 ? 225 VAL A O     1 
ATOM   1666 C CB    . VAL A 1 234 ? 17.142 9.712   4.416   1.00 31.98 ? 225 VAL A CB    1 
ATOM   1667 C CG1   . VAL A 1 234 ? 18.309 9.733   3.437   1.00 36.42 ? 225 VAL A CG1   1 
ATOM   1668 C CG2   . VAL A 1 234 ? 17.457 8.826   5.614   1.00 33.54 ? 225 VAL A CG2   1 
ATOM   1669 N N     . VAL A 1 235 ? 15.458 11.051  6.915   1.00 34.89 ? 226 VAL A N     1 
ATOM   1670 C CA    . VAL A 1 235 ? 14.214 11.178  7.667   1.00 31.63 ? 226 VAL A CA    1 
ATOM   1671 C C     . VAL A 1 235 ? 13.684 12.603  7.573   1.00 34.27 ? 226 VAL A C     1 
ATOM   1672 O O     . VAL A 1 235 ? 12.484 12.823  7.373   1.00 35.30 ? 226 VAL A O     1 
ATOM   1673 C CB    . VAL A 1 235 ? 14.424 10.740  9.128   1.00 39.55 ? 226 VAL A CB    1 
ATOM   1674 C CG1   . VAL A 1 235 ? 13.299 11.260  10.014  1.00 39.25 ? 226 VAL A CG1   1 
ATOM   1675 C CG2   . VAL A 1 235 ? 14.516 9.223   9.219   1.00 37.50 ? 226 VAL A CG2   1 
ATOM   1676 N N     . SER A 1 236 ? 14.568 13.595  7.698   1.00 35.65 ? 227 SER A N     1 
ATOM   1677 C CA    . SER A 1 236 ? 14.141 14.983  7.572   1.00 41.03 ? 227 SER A CA    1 
ATOM   1678 C C     . SER A 1 236 ? 13.664 15.319  6.166   1.00 37.61 ? 227 SER A C     1 
ATOM   1679 O O     . SER A 1 236 ? 12.882 16.262  6.000   1.00 42.12 ? 227 SER A O     1 
ATOM   1680 C CB    . SER A 1 236 ? 15.281 15.921  7.970   1.00 39.45 ? 227 SER A CB    1 
ATOM   1681 O OG    . SER A 1 236 ? 15.668 15.706  9.315   1.00 50.72 ? 227 SER A OG    1 
ATOM   1682 N N     . ALA A 1 237 ? 14.103 14.572  5.153   1.00 39.48 ? 228 ALA A N     1 
ATOM   1683 C CA    . ALA A 1 237 ? 13.737 14.884  3.777   1.00 32.48 ? 228 ALA A CA    1 
ATOM   1684 C C     . ALA A 1 237 ? 12.438 14.216  3.346   1.00 40.14 ? 228 ALA A C     1 
ATOM   1685 O O     . ALA A 1 237 ? 11.616 14.845  2.670   1.00 40.01 ? 228 ALA A O     1 
ATOM   1686 C CB    . ALA A 1 237 ? 14.862 14.475  2.825   1.00 40.05 ? 228 ALA A CB    1 
ATOM   1687 N N     . ILE A 1 238 ? 12.232 12.953  3.714   1.00 37.68 ? 229 ILE A N     1 
ATOM   1688 C CA    . ILE A 1 238 ? 11.071 12.194  3.268   1.00 36.02 ? 229 ILE A CA    1 
ATOM   1689 C C     . ILE A 1 238 ? 10.265 11.615  4.418   1.00 38.87 ? 229 ILE A C     1 
ATOM   1690 O O     . ILE A 1 238 ? 9.229  10.991  4.176   1.00 39.13 ? 229 ILE A O     1 
ATOM   1691 C CB    . ILE A 1 238 ? 11.474 11.072  2.289   1.00 39.05 ? 229 ILE A CB    1 
ATOM   1692 C CG1   . ILE A 1 238 ? 12.081 9.892   3.049   1.00 35.11 ? 229 ILE A CG1   1 
ATOM   1693 C CG2   . ILE A 1 238 ? 12.437 11.593  1.232   1.00 37.17 ? 229 ILE A CG2   1 
ATOM   1694 C CD1   . ILE A 1 238 ? 12.311 8.671   2.190   1.00 37.62 ? 229 ILE A CD1   1 
ATOM   1695 N N     . GLY A 1 239 ? 10.698 11.797  5.655   1.00 38.46 ? 230 GLY A N     1 
ATOM   1696 C CA    . GLY A 1 239 ? 9.925  11.226  6.746   1.00 37.54 ? 230 GLY A CA    1 
ATOM   1697 C C     . GLY A 1 239 ? 10.418 9.849   7.142   1.00 40.28 ? 230 GLY A C     1 
ATOM   1698 O O     . GLY A 1 239 ? 10.869 9.052   6.321   1.00 37.82 ? 230 GLY A O     1 
ATOM   1699 N N     . ALA A 1 240 ? 10.319 9.565   8.442   1.00 34.19 ? 231 ALA A N     1 
ATOM   1700 C CA    . ALA A 1 240 ? 10.831 8.305   8.970   1.00 37.76 ? 231 ALA A CA    1 
ATOM   1701 C C     . ALA A 1 240 ? 10.036 7.108   8.465   1.00 39.10 ? 231 ALA A C     1 
ATOM   1702 O O     . ALA A 1 240 ? 10.603 6.026   8.282   1.00 39.35 ? 231 ALA A O     1 
ATOM   1703 C CB    . ALA A 1 240 ? 10.824 8.336   10.498  1.00 37.91 ? 231 ALA A CB    1 
ATOM   1704 N N     . ASP A 1 241 ? 8.732  7.280   8.233   1.00 32.16 ? 232 ASP A N     1 
ATOM   1705 C CA    . ASP A 1 241 ? 7.881  6.183   7.789   1.00 37.13 ? 232 ASP A CA    1 
ATOM   1706 C C     . ASP A 1 241 ? 8.268  5.647   6.418   1.00 43.25 ? 232 ASP A C     1 
ATOM   1707 O O     . ASP A 1 241 ? 7.814  4.558   6.047   1.00 38.58 ? 232 ASP A O     1 
ATOM   1708 C CB    . ASP A 1 241 ? 6.422  6.639   7.769   1.00 45.39 ? 232 ASP A CB    1 
ATOM   1709 C CG    . ASP A 1 241 ? 6.261  8.034   7.197   1.00 47.70 ? 232 ASP A CG    1 
ATOM   1710 O OD1   . ASP A 1 241 ? 6.373  9.011   7.968   1.00 57.76 ? 232 ASP A OD1   1 
ATOM   1711 O OD2   . ASP A 1 241 ? 6.035  8.153   5.975   1.00 54.37 ? 232 ASP A OD2   1 
ATOM   1712 N N     . ARG A 1 242 ? 9.087  6.378   5.659   1.00 34.57 ? 233 ARG A N     1 
ATOM   1713 C CA    . ARG A 1 242 ? 9.533  5.947   4.341   1.00 44.02 ? 233 ARG A CA    1 
ATOM   1714 C C     . ARG A 1 242 ? 11.028 5.636   4.308   1.00 38.48 ? 233 ARG A C     1 
ATOM   1715 O O     . ARG A 1 242 ? 11.637 5.652   3.233   1.00 35.79 ? 233 ARG A O     1 
ATOM   1716 C CB    . ARG A 1 242 ? 9.182  7.008   3.296   1.00 34.69 ? 233 ARG A CB    1 
ATOM   1717 C CG    . ARG A 1 242 ? 7.695  7.066   2.961   1.00 39.48 ? 233 ARG A CG    1 
ATOM   1718 C CD    . ARG A 1 242 ? 7.347  8.197   1.996   1.00 33.60 ? 233 ARG A CD    1 
ATOM   1719 N NE    . ARG A 1 242 ? 7.566  9.517   2.575   1.00 50.64 ? 233 ARG A NE    1 
ATOM   1720 C CZ    . ARG A 1 242 ? 7.595  10.647  1.878   1.00 53.88 ? 233 ARG A CZ    1 
ATOM   1721 N NH1   . ARG A 1 242 ? 7.415  10.656  0.567   1.00 55.96 ? 233 ARG A NH1   1 
ATOM   1722 N NH2   . ARG A 1 242 ? 7.800  11.796  2.516   1.00 52.72 ? 233 ARG A NH2   1 
ATOM   1723 N N     . VAL A 1 243 ? 11.629 5.338   5.459   1.00 34.09 ? 234 VAL A N     1 
ATOM   1724 C CA    . VAL A 1 243 ? 13.071 5.142   5.569   1.00 29.48 ? 234 VAL A CA    1 
ATOM   1725 C C     . VAL A 1 243 ? 13.334 3.833   6.299   1.00 37.22 ? 234 VAL A C     1 
ATOM   1726 O O     . VAL A 1 243 ? 12.923 3.668   7.455   1.00 34.64 ? 234 VAL A O     1 
ATOM   1727 C CB    . VAL A 1 243 ? 13.756 6.307   6.301   1.00 33.77 ? 234 VAL A CB    1 
ATOM   1728 C CG1   . VAL A 1 243 ? 15.169 5.918   6.718   1.00 36.75 ? 234 VAL A CG1   1 
ATOM   1729 C CG2   . VAL A 1 243 ? 13.775 7.548   5.423   1.00 34.71 ? 234 VAL A CG2   1 
ATOM   1730 N N     . GLY A 1 244 ? 14.025 2.912   5.632   1.00 35.25 ? 235 GLY A N     1 
ATOM   1731 C CA    . GLY A 1 244 ? 14.504 1.700   6.268   1.00 31.57 ? 235 GLY A CA    1 
ATOM   1732 C C     . GLY A 1 244 ? 16.012 1.713   6.415   1.00 31.08 ? 235 GLY A C     1 
ATOM   1733 O O     . GLY A 1 244 ? 16.701 2.431   5.686   1.00 33.69 ? 235 GLY A O     1 
ATOM   1734 N N     . VAL A 1 245 ? 16.541 0.934   7.356   1.00 28.13 ? 236 VAL A N     1 
ATOM   1735 C CA    . VAL A 1 245 ? 17.970 0.915   7.648   1.00 29.41 ? 236 VAL A CA    1 
ATOM   1736 C C     . VAL A 1 245 ? 18.439 -0.531  7.695   1.00 30.61 ? 236 VAL A C     1 
ATOM   1737 O O     . VAL A 1 245 ? 17.822 -1.367  8.366   1.00 33.15 ? 236 VAL A O     1 
ATOM   1738 C CB    . VAL A 1 245 ? 18.294 1.629   8.976   1.00 29.42 ? 236 VAL A CB    1 
ATOM   1739 C CG1   . VAL A 1 245 ? 19.797 1.731   9.165   1.00 32.49 ? 236 VAL A CG1   1 
ATOM   1740 C CG2   . VAL A 1 245 ? 17.655 3.013   9.012   1.00 35.65 ? 236 VAL A CG2   1 
ATOM   1741 N N     . ARG A 1 246 ? 19.529 -0.824  6.991   1.00 28.21 ? 237 ARG A N     1 
ATOM   1742 C CA    . ARG A 1 246 ? 20.103 -2.162  6.949   1.00 33.26 ? 237 ARG A CA    1 
ATOM   1743 C C     . ARG A 1 246 ? 21.508 -2.132  7.532   1.00 30.59 ? 237 ARG A C     1 
ATOM   1744 O O     . ARG A 1 246 ? 22.326 -1.294  7.143   1.00 30.19 ? 237 ARG A O     1 
ATOM   1745 C CB    . ARG A 1 246 ? 20.138 -2.708  5.518   1.00 29.07 ? 237 ARG A CB    1 
ATOM   1746 C CG    . ARG A 1 246 ? 20.547 -4.169  5.431   1.00 35.45 ? 237 ARG A CG    1 
ATOM   1747 C CD    . ARG A 1 246 ? 20.438 -4.698  4.009   1.00 38.42 ? 237 ARG A CD    1 
ATOM   1748 N NE    . ARG A 1 246 ? 19.729 -5.971  3.958   1.00 43.95 ? 237 ARG A NE    1 
ATOM   1749 C CZ    . ARG A 1 246 ? 20.175 -7.055  3.337   1.00 38.17 ? 237 ARG A CZ    1 
ATOM   1750 N NH1   . ARG A 1 246 ? 21.332 -7.057  2.697   1.00 41.90 ? 237 ARG A NH1   1 
ATOM   1751 N NH2   . ARG A 1 246 ? 19.440 -8.164  3.356   1.00 40.94 ? 237 ARG A NH2   1 
ATOM   1752 N N     . VAL A 1 247 ? 21.781 -3.041  8.471   1.00 25.10 ? 238 VAL A N     1 
ATOM   1753 C CA    . VAL A 1 247 ? 23.102 -3.197  9.069   1.00 30.44 ? 238 VAL A CA    1 
ATOM   1754 C C     . VAL A 1 247 ? 23.409 -4.685  9.184   1.00 27.91 ? 238 VAL A C     1 
ATOM   1755 O O     . VAL A 1 247 ? 22.528 -5.538  9.067   1.00 28.33 ? 238 VAL A O     1 
ATOM   1756 C CB    . VAL A 1 247 ? 23.210 -2.527  10.458  1.00 32.15 ? 238 VAL A CB    1 
ATOM   1757 C CG1   . VAL A 1 247 ? 22.935 -1.032  10.363  1.00 30.34 ? 238 VAL A CG1   1 
ATOM   1758 C CG2   . VAL A 1 247 ? 22.264 -3.191  11.433  1.00 22.78 ? 238 VAL A CG2   1 
ATOM   1759 N N     . SER A 1 248 ? 24.684 -4.992  9.430   1.00 31.10 ? 239 SER A N     1 
ATOM   1760 C CA    . SER A 1 248 ? 25.129 -6.373  9.628   1.00 36.03 ? 239 SER A CA    1 
ATOM   1761 C C     . SER A 1 248 ? 26.348 -6.374  10.544  1.00 36.70 ? 239 SER A C     1 
ATOM   1762 O O     . SER A 1 248 ? 27.476 -6.620  10.109  1.00 31.81 ? 239 SER A O     1 
ATOM   1763 C CB    . SER A 1 248 ? 25.445 -7.038  8.289   1.00 39.04 ? 239 SER A CB    1 
ATOM   1764 O OG    . SER A 1 248 ? 26.539 -6.401  7.653   1.00 34.34 ? 239 SER A OG    1 
ATOM   1765 N N     . PRO A 1 249 ? 26.148 -6.111  11.838  1.00 34.63 ? 240 PRO A N     1 
ATOM   1766 C CA    . PRO A 1 249 ? 27.300 -6.026  12.751  1.00 33.23 ? 240 PRO A CA    1 
ATOM   1767 C C     . PRO A 1 249 ? 28.055 -7.334  12.916  1.00 38.12 ? 240 PRO A C     1 
ATOM   1768 O O     . PRO A 1 249 ? 29.241 -7.302  13.266  1.00 37.28 ? 240 PRO A O     1 
ATOM   1769 C CB    . PRO A 1 249 ? 26.668 -5.572  14.075  1.00 37.21 ? 240 PRO A CB    1 
ATOM   1770 C CG    . PRO A 1 249 ? 25.237 -5.986  13.976  1.00 34.04 ? 240 PRO A CG    1 
ATOM   1771 C CD    . PRO A 1 249 ? 24.870 -5.865  12.528  1.00 33.50 ? 240 PRO A CD    1 
ATOM   1772 N N     . ALA A 1 250 ? 27.419 -8.477  12.670  1.00 37.99 ? 241 ALA A N     1 
ATOM   1773 C CA    . ALA A 1 250 ? 28.047 -9.777  12.863  1.00 44.38 ? 241 ALA A CA    1 
ATOM   1774 C C     . ALA A 1 250 ? 28.614 -10.363 11.575  1.00 41.73 ? 241 ALA A C     1 
ATOM   1775 O O     . ALA A 1 250 ? 29.021 -11.529 11.565  1.00 47.36 ? 241 ALA A O     1 
ATOM   1776 C CB    . ALA A 1 250 ? 27.049 -10.756 13.486  1.00 32.73 ? 241 ALA A CB    1 
ATOM   1777 N N     . ILE A 1 251 ? 28.654 -9.589  10.494  1.00 37.89 ? 242 ILE A N     1 
ATOM   1778 C CA    . ILE A 1 251 ? 29.193 -10.038 9.215   1.00 40.22 ? 242 ILE A CA    1 
ATOM   1779 C C     . ILE A 1 251 ? 30.515 -9.323  8.974   1.00 38.57 ? 242 ILE A C     1 
ATOM   1780 O O     . ILE A 1 251 ? 30.583 -8.090  9.039   1.00 40.28 ? 242 ILE A O     1 
ATOM   1781 C CB    . ILE A 1 251 ? 28.204 -9.783  8.064   1.00 38.14 ? 242 ILE A CB    1 
ATOM   1782 C CG1   . ILE A 1 251 ? 27.019 -10.746 8.159   1.00 41.28 ? 242 ILE A CG1   1 
ATOM   1783 C CG2   . ILE A 1 251 ? 28.899 -9.932  6.721   1.00 42.06 ? 242 ILE A CG2   1 
ATOM   1784 C CD1   . ILE A 1 251 ? 26.052 -10.647 6.998   1.00 42.42 ? 242 ILE A CD1   1 
ATOM   1785 N N     . ASP A 1 252 ? 31.566 -10.099 8.701   1.00 36.56 ? 243 ASP A N     1 
ATOM   1786 C CA    . ASP A 1 252 ? 32.903 -9.569  8.467   1.00 46.49 ? 243 ASP A CA    1 
ATOM   1787 C C     . ASP A 1 252 ? 33.240 -9.478  6.981   1.00 43.43 ? 243 ASP A C     1 
ATOM   1788 O O     . ASP A 1 252 ? 34.395 -9.684  6.593   1.00 50.01 ? 243 ASP A O     1 
ATOM   1789 C CB    . ASP A 1 252 ? 33.943 -10.420 9.197   1.00 46.83 ? 243 ASP A CB    1 
ATOM   1790 N N     . HIS A 1 253 ? 32.252 -9.167  6.146   1.00 46.19 ? 244 HIS A N     1 
ATOM   1791 C CA    . HIS A 1 253 ? 32.463 -9.099  4.705   1.00 44.34 ? 244 HIS A CA    1 
ATOM   1792 C C     . HIS A 1 253 ? 33.374 -7.927  4.355   1.00 39.59 ? 244 HIS A C     1 
ATOM   1793 O O     . HIS A 1 253 ? 33.145 -6.798  4.800   1.00 46.03 ? 244 HIS A O     1 
ATOM   1794 C CB    . HIS A 1 253 ? 31.117 -8.971  3.990   1.00 40.00 ? 244 HIS A CB    1 
ATOM   1795 C CG    . HIS A 1 253 ? 31.227 -8.736  2.516   1.00 47.12 ? 244 HIS A CG    1 
ATOM   1796 N ND1   . HIS A 1 253 ? 30.650 -7.651  1.892   1.00 40.18 ? 244 HIS A ND1   1 
ATOM   1797 C CD2   . HIS A 1 253 ? 31.840 -9.449  1.542   1.00 48.18 ? 244 HIS A CD2   1 
ATOM   1798 C CE1   . HIS A 1 253 ? 30.902 -7.706  0.596   1.00 50.29 ? 244 HIS A CE1   1 
ATOM   1799 N NE2   . HIS A 1 253 ? 31.624 -8.787  0.358   1.00 50.62 ? 244 HIS A NE2   1 
ATOM   1800 N N     . LEU A 1 254 ? 34.412 -8.203  3.562   1.00 43.92 ? 245 LEU A N     1 
ATOM   1801 C CA    . LEU A 1 254 ? 35.391 -7.195  3.143   1.00 44.22 ? 245 LEU A CA    1 
ATOM   1802 C C     . LEU A 1 254 ? 36.084 -6.553  4.345   1.00 45.87 ? 245 LEU A C     1 
ATOM   1803 O O     . LEU A 1 254 ? 36.232 -5.331  4.427   1.00 40.42 ? 245 LEU A O     1 
ATOM   1804 C CB    . LEU A 1 254 ? 34.743 -6.131  2.252   1.00 37.72 ? 245 LEU A CB    1 
ATOM   1805 C CG    . LEU A 1 254 ? 34.171 -6.608  0.919   1.00 40.61 ? 245 LEU A CG    1 
ATOM   1806 C CD1   . LEU A 1 254 ? 33.454 -5.471  0.214   1.00 38.44 ? 245 LEU A CD1   1 
ATOM   1807 C CD2   . LEU A 1 254 ? 35.277 -7.176  0.042   1.00 33.06 ? 245 LEU A CD2   1 
ATOM   1808 N N     . ASP A 1 255 ? 36.520 -7.399  5.282   1.00 41.87 ? 246 ASP A N     1 
ATOM   1809 C CA    . ASP A 1 255 ? 37.229 -6.960  6.488   1.00 44.81 ? 246 ASP A CA    1 
ATOM   1810 C C     . ASP A 1 255 ? 36.391 -5.985  7.314   1.00 33.24 ? 246 ASP A C     1 
ATOM   1811 O O     . ASP A 1 255 ? 36.894 -4.981  7.822   1.00 45.41 ? 246 ASP A O     1 
ATOM   1812 C CB    . ASP A 1 255 ? 38.586 -6.341  6.144   1.00 53.29 ? 246 ASP A CB    1 
ATOM   1813 C CG    . ASP A 1 255 ? 39.635 -7.381  5.822   1.00 56.88 ? 246 ASP A CG    1 
ATOM   1814 O OD1   . ASP A 1 255 ? 39.347 -8.588  5.967   1.00 57.60 ? 246 ASP A OD1   1 
ATOM   1815 O OD2   . ASP A 1 255 ? 40.752 -6.989  5.427   1.00 64.67 ? 246 ASP A OD2   1 
ATOM   1816 N N     . ALA A 1 256 ? 35.102 -6.283  7.451   1.00 42.05 ? 247 ALA A N     1 
ATOM   1817 C CA    . ALA A 1 256 ? 34.208 -5.477  8.281   1.00 43.20 ? 247 ALA A CA    1 
ATOM   1818 C C     . ALA A 1 256 ? 34.022 -6.158  9.636   1.00 42.35 ? 247 ALA A C     1 
ATOM   1819 O O     . ALA A 1 256 ? 32.960 -6.681  9.974   1.00 44.42 ? 247 ALA A O     1 
ATOM   1820 C CB    . ALA A 1 256 ? 32.875 -5.261  7.574   1.00 39.20 ? 247 ALA A CB    1 
ATOM   1821 N N     . MET A 1 257 ? 35.097 -6.138  10.416  1.00 39.49 ? 248 MET A N     1 
ATOM   1822 C CA    . MET A 1 257 ? 35.146 -6.803  11.710  1.00 45.68 ? 248 MET A CA    1 
ATOM   1823 C C     . MET A 1 257 ? 35.104 -5.769  12.826  1.00 39.55 ? 248 MET A C     1 
ATOM   1824 O O     . MET A 1 257 ? 35.887 -4.814  12.824  1.00 39.78 ? 248 MET A O     1 
ATOM   1825 C CB    . MET A 1 257 ? 36.407 -7.660  11.835  1.00 43.09 ? 248 MET A CB    1 
ATOM   1826 C CG    . MET A 1 257 ? 36.508 -8.430  13.138  1.00 51.19 ? 248 MET A CG    1 
ATOM   1827 S SD    . MET A 1 257 ? 36.855 -10.179 12.877  1.00 72.48 ? 248 MET A SD    1 
ATOM   1828 C CE    . MET A 1 257 ? 38.624 -10.135 12.605  1.00 62.42 ? 248 MET A CE    1 
ATOM   1829 N N     . ASP A 1 258 ? 34.187 -5.960  13.769  1.00 40.92 ? 249 ASP A N     1 
ATOM   1830 C CA    . ASP A 1 258 ? 34.120 -5.161  14.982  1.00 41.23 ? 249 ASP A CA    1 
ATOM   1831 C C     . ASP A 1 258 ? 34.456 -6.042  16.176  1.00 39.13 ? 249 ASP A C     1 
ATOM   1832 O O     . ASP A 1 258 ? 34.052 -7.208  16.232  1.00 44.77 ? 249 ASP A O     1 
ATOM   1833 C CB    . ASP A 1 258 ? 32.734 -4.534  15.162  1.00 40.31 ? 249 ASP A CB    1 
ATOM   1834 C CG    . ASP A 1 258 ? 32.726 -3.425  16.199  1.00 49.00 ? 249 ASP A CG    1 
ATOM   1835 O OD1   . ASP A 1 258 ? 32.453 -3.716  17.383  1.00 41.13 ? 249 ASP A OD1   1 
ATOM   1836 O OD2   . ASP A 1 258 ? 32.993 -2.262  15.830  1.00 39.87 ? 249 ASP A OD2   1 
ATOM   1837 N N     . SER A 1 259 ? 35.203 -5.483  17.130  1.00 42.92 ? 250 SER A N     1 
ATOM   1838 C CA    . SER A 1 259 ? 35.608 -6.245  18.305  1.00 42.59 ? 250 SER A CA    1 
ATOM   1839 C C     . SER A 1 259 ? 34.434 -6.619  19.200  1.00 45.51 ? 250 SER A C     1 
ATOM   1840 O O     . SER A 1 259 ? 34.593 -7.485  20.067  1.00 51.30 ? 250 SER A O     1 
ATOM   1841 C CB    . SER A 1 259 ? 36.643 -5.460  19.112  1.00 37.72 ? 250 SER A CB    1 
ATOM   1842 O OG    . SER A 1 259 ? 36.077 -4.285  19.666  1.00 49.04 ? 250 SER A OG    1 
ATOM   1843 N N     . ASN A 1 260 ? 33.271 -5.999  19.013  1.00 44.68 ? 251 ASN A N     1 
ATOM   1844 C CA    . ASN A 1 260 ? 32.084 -6.306  19.813  1.00 40.63 ? 251 ASN A CA    1 
ATOM   1845 C C     . ASN A 1 260 ? 30.847 -6.097  18.954  1.00 37.58 ? 251 ASN A C     1 
ATOM   1846 O O     . ASN A 1 260 ? 30.194 -5.048  19.015  1.00 36.63 ? 251 ASN A O     1 
ATOM   1847 C CB    . ASN A 1 260 ? 32.030 -5.440  21.074  1.00 38.52 ? 251 ASN A CB    1 
ATOM   1848 C CG    . ASN A 1 260 ? 31.127 -6.021  22.143  1.00 41.35 ? 251 ASN A CG    1 
ATOM   1849 O OD1   . ASN A 1 260 ? 30.252 -6.838  21.857  1.00 41.21 ? 251 ASN A OD1   1 
ATOM   1850 N ND2   . ASN A 1 260 ? 31.334 -5.599  23.386  1.00 46.96 ? 251 ASN A ND2   1 
ATOM   1851 N N     . PRO A 1 261 ? 30.492 -7.088  18.128  1.00 37.36 ? 252 PRO A N     1 
ATOM   1852 C CA    . PRO A 1 261 ? 29.332 -6.913  17.234  1.00 35.47 ? 252 PRO A CA    1 
ATOM   1853 C C     . PRO A 1 261 ? 28.022 -6.671  17.965  1.00 38.26 ? 252 PRO A C     1 
ATOM   1854 O O     . PRO A 1 261 ? 27.189 -5.893  17.484  1.00 32.46 ? 252 PRO A O     1 
ATOM   1855 C CB    . PRO A 1 261 ? 29.305 -8.227  16.439  1.00 39.90 ? 252 PRO A CB    1 
ATOM   1856 C CG    . PRO A 1 261 ? 30.707 -8.743  16.506  1.00 34.46 ? 252 PRO A CG    1 
ATOM   1857 C CD    . PRO A 1 261 ? 31.212 -8.345  17.862  1.00 38.47 ? 252 PRO A CD    1 
ATOM   1858 N N     . LEU A 1 262 ? 27.810 -7.316  19.114  1.00 36.53 ? 253 LEU A N     1 
ATOM   1859 C CA    . LEU A 1 262 ? 26.571 -7.103  19.855  1.00 37.29 ? 253 LEU A CA    1 
ATOM   1860 C C     . LEU A 1 262 ? 26.463 -5.659  20.330  1.00 32.21 ? 253 LEU A C     1 
ATOM   1861 O O     . LEU A 1 262 ? 25.432 -5.005  20.134  1.00 32.68 ? 253 LEU A O     1 
ATOM   1862 C CB    . LEU A 1 262 ? 26.488 -8.069  21.039  1.00 33.44 ? 253 LEU A CB    1 
ATOM   1863 C CG    . LEU A 1 262 ? 25.242 -7.938  21.922  1.00 37.82 ? 253 LEU A CG    1 
ATOM   1864 C CD1   . LEU A 1 262 ? 23.971 -7.921  21.081  1.00 31.69 ? 253 LEU A CD1   1 
ATOM   1865 C CD2   . LEU A 1 262 ? 25.186 -9.058  22.956  1.00 37.82 ? 253 LEU A CD2   1 
ATOM   1866 N N     . SER A 1 263 ? 27.526 -5.142  20.949  1.00 30.65 ? 254 SER A N     1 
ATOM   1867 C CA    . SER A 1 263 ? 27.494 -3.771  21.450  1.00 37.96 ? 254 SER A CA    1 
ATOM   1868 C C     . SER A 1 263 ? 27.386 -2.757  20.319  1.00 26.04 ? 254 SER A C     1 
ATOM   1869 O O     . SER A 1 263 ? 26.742 -1.715  20.486  1.00 31.69 ? 254 SER A O     1 
ATOM   1870 C CB    . SER A 1 263 ? 28.735 -3.491  22.295  1.00 38.70 ? 254 SER A CB    1 
ATOM   1871 O OG    . SER A 1 263 ? 28.568 -3.978  23.615  1.00 43.60 ? 254 SER A OG    1 
ATOM   1872 N N     . LEU A 1 264 ? 28.006 -3.036  19.171  1.00 33.04 ? 255 LEU A N     1 
ATOM   1873 C CA    . LEU A 1 264 ? 27.868 -2.145  18.023  1.00 28.37 ? 255 LEU A CA    1 
ATOM   1874 C C     . LEU A 1 264 ? 26.422 -2.096  17.547  1.00 28.84 ? 255 LEU A C     1 
ATOM   1875 O O     . LEU A 1 264 ? 25.849 -1.015  17.369  1.00 30.33 ? 255 LEU A O     1 
ATOM   1876 C CB    . LEU A 1 264 ? 28.797 -2.592  16.894  1.00 34.59 ? 255 LEU A CB    1 
ATOM   1877 C CG    . LEU A 1 264 ? 28.666 -1.819  15.580  1.00 37.34 ? 255 LEU A CG    1 
ATOM   1878 C CD1   . LEU A 1 264 ? 28.934 -0.335  15.800  1.00 34.43 ? 255 LEU A CD1   1 
ATOM   1879 C CD2   . LEU A 1 264 ? 29.595 -2.389  14.515  1.00 35.54 ? 255 LEU A CD2   1 
ATOM   1880 N N     . GLY A 1 265 ? 25.810 -3.266  17.345  1.00 34.26 ? 256 GLY A N     1 
ATOM   1881 C CA    . GLY A 1 265 ? 24.416 -3.298  16.936  1.00 32.38 ? 256 GLY A CA    1 
ATOM   1882 C C     . GLY A 1 265 ? 23.501 -2.614  17.933  1.00 36.29 ? 256 GLY A C     1 
ATOM   1883 O O     . GLY A 1 265 ? 22.595 -1.869  17.549  1.00 40.04 ? 256 GLY A O     1 
ATOM   1884 N N     . LEU A 1 266 ? 23.727 -2.854  19.228  1.00 33.97 ? 257 LEU A N     1 
ATOM   1885 C CA    . LEU A 1 266 ? 22.922 -2.196  20.252  1.00 33.50 ? 257 LEU A CA    1 
ATOM   1886 C C     . LEU A 1 266 ? 23.105 -0.686  20.207  1.00 27.77 ? 257 LEU A C     1 
ATOM   1887 O O     . LEU A 1 266 ? 22.133 0.068   20.330  1.00 28.06 ? 257 LEU A O     1 
ATOM   1888 C CB    . LEU A 1 266 ? 23.282 -2.739  21.635  1.00 34.41 ? 257 LEU A CB    1 
ATOM   1889 C CG    . LEU A 1 266 ? 22.789 -4.155  21.935  1.00 41.68 ? 257 LEU A CG    1 
ATOM   1890 C CD1   . LEU A 1 266 ? 23.035 -4.513  23.394  1.00 34.72 ? 257 LEU A CD1   1 
ATOM   1891 C CD2   . LEU A 1 266 ? 21.313 -4.297  21.580  1.00 35.82 ? 257 LEU A CD2   1 
ATOM   1892 N N     . ALA A 1 267 ? 24.347 -0.226  20.029  1.00 26.86 ? 258 ALA A N     1 
ATOM   1893 C CA    . ALA A 1 267 ? 24.593 1.208   19.913  1.00 33.65 ? 258 ALA A CA    1 
ATOM   1894 C C     . ALA A 1 267 ? 23.889 1.791   18.696  1.00 30.59 ? 258 ALA A C     1 
ATOM   1895 O O     . ALA A 1 267 ? 23.374 2.914   18.747  1.00 33.09 ? 258 ALA A O     1 
ATOM   1896 C CB    . ALA A 1 267 ? 26.095 1.481   19.845  1.00 38.01 ? 258 ALA A CB    1 
ATOM   1897 N N     . VAL A 1 268 ? 23.852 1.042   17.591  1.00 33.73 ? 259 VAL A N     1 
ATOM   1898 C CA    . VAL A 1 268 ? 23.160 1.519   16.396  1.00 31.01 ? 259 VAL A CA    1 
ATOM   1899 C C     . VAL A 1 268 ? 21.656 1.556   16.632  1.00 32.26 ? 259 VAL A C     1 
ATOM   1900 O O     . VAL A 1 268 ? 20.973 2.507   16.228  1.00 24.27 ? 259 VAL A O     1 
ATOM   1901 C CB    . VAL A 1 268 ? 23.522 0.641   15.184  1.00 34.06 ? 259 VAL A CB    1 
ATOM   1902 C CG1   . VAL A 1 268 ? 22.626 0.974   13.999  1.00 30.18 ? 259 VAL A CG1   1 
ATOM   1903 C CG2   . VAL A 1 268 ? 24.985 0.816   14.818  1.00 34.75 ? 259 VAL A CG2   1 
ATOM   1904 N N     . VAL A 1 269 ? 21.119 0.530   17.297  1.00 27.21 ? 260 VAL A N     1 
ATOM   1905 C CA    . VAL A 1 269 ? 19.685 0.475   17.572  1.00 26.21 ? 260 VAL A CA    1 
ATOM   1906 C C     . VAL A 1 269 ? 19.266 1.640   18.462  1.00 33.46 ? 260 VAL A C     1 
ATOM   1907 O O     . VAL A 1 269 ? 18.255 2.309   18.211  1.00 30.26 ? 260 VAL A O     1 
ATOM   1908 C CB    . VAL A 1 269 ? 19.318 -0.878  18.205  1.00 31.31 ? 260 VAL A CB    1 
ATOM   1909 C CG1   . VAL A 1 269 ? 18.027 -0.768  18.997  1.00 29.86 ? 260 VAL A CG1   1 
ATOM   1910 C CG2   . VAL A 1 269 ? 19.207 -1.952  17.134  1.00 30.46 ? 260 VAL A CG2   1 
ATOM   1911 N N     . GLU A 1 270 ? 20.039 1.898   19.521  1.00 37.47 ? 261 GLU A N     1 
ATOM   1912 C CA    . GLU A 1 270 ? 19.708 2.985   20.438  1.00 36.10 ? 261 GLU A CA    1 
ATOM   1913 C C     . GLU A 1 270 ? 19.651 4.328   19.721  1.00 34.14 ? 261 GLU A C     1 
ATOM   1914 O O     . GLU A 1 270 ? 18.848 5.195   20.088  1.00 36.96 ? 261 GLU A O     1 
ATOM   1915 C CB    . GLU A 1 270 ? 20.724 3.026   21.579  1.00 38.84 ? 261 GLU A CB    1 
ATOM   1916 C CG    . GLU A 1 270 ? 20.509 4.146   22.583  1.00 49.45 ? 261 GLU A CG    1 
ATOM   1917 C CD    . GLU A 1 270 ? 21.804 4.590   23.235  1.00 53.16 ? 261 GLU A CD    1 
ATOM   1918 O OE1   . GLU A 1 270 ? 22.413 5.565   22.746  1.00 62.74 ? 261 GLU A OE1   1 
ATOM   1919 O OE2   . GLU A 1 270 ? 22.211 3.965   24.237  1.00 63.33 ? 261 GLU A OE2   1 
ATOM   1920 N N     . ARG A 1 271 ? 20.478 4.518   18.691  1.00 36.24 ? 262 ARG A N     1 
ATOM   1921 C CA    . ARG A 1 271 ? 20.428 5.767   17.938  1.00 36.31 ? 262 ARG A CA    1 
ATOM   1922 C C     . ARG A 1 271 ? 19.202 5.822   17.037  1.00 32.72 ? 262 ARG A C     1 
ATOM   1923 O O     . ARG A 1 271 ? 18.604 6.890   16.861  1.00 35.14 ? 262 ARG A O     1 
ATOM   1924 C CB    . ARG A 1 271 ? 21.704 5.942   17.120  1.00 28.49 ? 262 ARG A CB    1 
ATOM   1925 C CG    . ARG A 1 271 ? 22.721 6.843   17.789  1.00 39.12 ? 262 ARG A CG    1 
ATOM   1926 C CD    . ARG A 1 271 ? 24.107 6.257   17.696  1.00 40.90 ? 262 ARG A CD    1 
ATOM   1927 N NE    . ARG A 1 271 ? 24.957 6.645   18.816  1.00 44.15 ? 262 ARG A NE    1 
ATOM   1928 C CZ    . ARG A 1 271 ? 24.869 6.137   20.038  1.00 58.47 ? 262 ARG A CZ    1 
ATOM   1929 N NH1   . ARG A 1 271 ? 23.985 5.197   20.336  1.00 42.36 ? 262 ARG A NH1   1 
ATOM   1930 N NH2   . ARG A 1 271 ? 25.700 6.571   20.982  1.00 61.66 ? 262 ARG A NH2   1 
ATOM   1931 N N     . LEU A 1 272 ? 18.817 4.686   16.450  1.00 34.91 ? 263 LEU A N     1 
ATOM   1932 C CA    . LEU A 1 272 ? 17.588 4.649   15.666  1.00 32.22 ? 263 LEU A CA    1 
ATOM   1933 C C     . LEU A 1 272 ? 16.383 4.967   16.538  1.00 30.63 ? 263 LEU A C     1 
ATOM   1934 O O     . LEU A 1 272 ? 15.499 5.733   16.136  1.00 29.95 ? 263 LEU A O     1 
ATOM   1935 C CB    . LEU A 1 272 ? 17.424 3.283   14.999  1.00 29.60 ? 263 LEU A CB    1 
ATOM   1936 C CG    . LEU A 1 272 ? 18.468 2.900   13.948  1.00 35.22 ? 263 LEU A CG    1 
ATOM   1937 C CD1   . LEU A 1 272 ? 18.066 1.612   13.248  1.00 30.39 ? 263 LEU A CD1   1 
ATOM   1938 C CD2   . LEU A 1 272 ? 18.666 4.023   12.941  1.00 34.47 ? 263 LEU A CD2   1 
ATOM   1939 N N     . ASN A 1 273 ? 16.332 4.385   17.738  1.00 33.95 ? 264 ASN A N     1 
ATOM   1940 C CA    . ASN A 1 273 ? 15.289 4.741   18.692  1.00 29.14 ? 264 ASN A CA    1 
ATOM   1941 C C     . ASN A 1 273 ? 15.293 6.242   18.960  1.00 31.85 ? 264 ASN A C     1 
ATOM   1942 O O     . ASN A 1 273 ? 14.268 6.914   18.805  1.00 35.69 ? 264 ASN A O     1 
ATOM   1943 C CB    . ASN A 1 273 ? 15.478 3.957   19.992  1.00 31.49 ? 264 ASN A CB    1 
ATOM   1944 C CG    . ASN A 1 273 ? 15.072 2.498   19.862  1.00 36.05 ? 264 ASN A CG    1 
ATOM   1945 O OD1   . ASN A 1 273 ? 14.399 2.109   18.908  1.00 37.28 ? 264 ASN A OD1   1 
ATOM   1946 N ND2   . ASN A 1 273 ? 15.485 1.682   20.825  1.00 30.79 ? 264 ASN A ND2   1 
ATOM   1947 N N     . LYS A 1 274 ? 16.457 6.789   19.325  1.00 30.37 ? 265 LYS A N     1 
ATOM   1948 C CA    . LYS A 1 274 ? 16.559 8.213   19.636  1.00 31.12 ? 265 LYS A CA    1 
ATOM   1949 C C     . LYS A 1 274 ? 16.068 9.080   18.482  1.00 37.39 ? 265 LYS A C     1 
ATOM   1950 O O     . LYS A 1 274 ? 15.391 10.091  18.703  1.00 39.10 ? 265 LYS A O     1 
ATOM   1951 C CB    . LYS A 1 274 ? 18.004 8.567   19.990  1.00 36.06 ? 265 LYS A CB    1 
ATOM   1952 N N     . ILE A 1 275 ? 16.401 8.706   17.243  1.00 31.39 ? 266 ILE A N     1 
ATOM   1953 C CA    . ILE A 1 275 ? 15.912 9.465   16.094  1.00 36.00 ? 266 ILE A CA    1 
ATOM   1954 C C     . ILE A 1 275 ? 14.395 9.383   16.018  1.00 38.11 ? 266 ILE A C     1 
ATOM   1955 O O     . ILE A 1 275 ? 13.718 10.380  15.739  1.00 36.11 ? 266 ILE A O     1 
ATOM   1956 C CB    . ILE A 1 275 ? 16.572 8.971   14.792  1.00 38.73 ? 266 ILE A CB    1 
ATOM   1957 C CG1   . ILE A 1 275 ? 18.007 9.485   14.686  1.00 40.28 ? 266 ILE A CG1   1 
ATOM   1958 C CG2   . ILE A 1 275 ? 15.769 9.409   13.580  1.00 37.95 ? 266 ILE A CG2   1 
ATOM   1959 C CD1   . ILE A 1 275 ? 19.011 8.409   14.337  1.00 41.53 ? 266 ILE A CD1   1 
ATOM   1960 N N     . GLN A 1 276 ? 13.835 8.200   16.285  1.00 35.72 ? 267 GLN A N     1 
ATOM   1961 C CA    . GLN A 1 276 ? 12.384 8.048   16.263  1.00 40.17 ? 267 GLN A CA    1 
ATOM   1962 C C     . GLN A 1 276 ? 11.719 8.877   17.357  1.00 41.29 ? 267 GLN A C     1 
ATOM   1963 O O     . GLN A 1 276 ? 10.694 9.526   17.114  1.00 41.82 ? 267 GLN A O     1 
ATOM   1964 C CB    . GLN A 1 276 ? 12.008 6.574   16.401  1.00 37.37 ? 267 GLN A CB    1 
ATOM   1965 C CG    . GLN A 1 276 ? 12.420 5.719   15.214  1.00 35.49 ? 267 GLN A CG    1 
ATOM   1966 C CD    . GLN A 1 276 ? 12.107 4.251   15.413  1.00 39.51 ? 267 GLN A CD    1 
ATOM   1967 O OE1   . GLN A 1 276 ? 12.090 3.475   14.457  1.00 34.00 ? 267 GLN A OE1   1 
ATOM   1968 N NE2   . GLN A 1 276 ? 11.858 3.860   16.660  1.00 35.11 ? 267 GLN A NE2   1 
ATOM   1969 N N     . LEU A 1 277 ? 12.281 8.869   18.571  1.00 40.47 ? 268 LEU A N     1 
ATOM   1970 C CA    . LEU A 1 277 ? 11.710 9.688   19.639  1.00 44.95 ? 268 LEU A CA    1 
ATOM   1971 C C     . LEU A 1 277 ? 11.797 11.174  19.306  1.00 42.74 ? 268 LEU A C     1 
ATOM   1972 O O     . LEU A 1 277 ? 10.842 11.924  19.538  1.00 49.11 ? 268 LEU A O     1 
ATOM   1973 C CB    . LEU A 1 277 ? 12.396 9.402   20.980  1.00 40.95 ? 268 LEU A CB    1 
ATOM   1974 C CG    . LEU A 1 277 ? 12.065 8.128   21.776  1.00 44.83 ? 268 LEU A CG    1 
ATOM   1975 C CD1   . LEU A 1 277 ? 10.552 7.956   21.897  1.00 48.03 ? 268 LEU A CD1   1 
ATOM   1976 C CD2   . LEU A 1 277 ? 12.727 6.863   21.259  1.00 52.70 ? 268 LEU A CD2   1 
ATOM   1977 N N     . HIS A 1 278 ? 12.930 11.620  18.759  1.00 43.46 ? 269 HIS A N     1 
ATOM   1978 C CA    . HIS A 1 278 ? 13.087 13.036  18.443  1.00 40.38 ? 269 HIS A CA    1 
ATOM   1979 C C     . HIS A 1 278 ? 12.201 13.440  17.272  1.00 47.58 ? 269 HIS A C     1 
ATOM   1980 O O     . HIS A 1 278 ? 11.489 14.448  17.340  1.00 50.84 ? 269 HIS A O     1 
ATOM   1981 C CB    . HIS A 1 278 ? 14.554 13.348  18.148  1.00 34.46 ? 269 HIS A CB    1 
ATOM   1982 N N     . SER A 1 279 ? 12.226 12.665  16.185  1.00 47.40 ? 270 SER A N     1 
ATOM   1983 C CA    . SER A 1 279 ? 11.427 13.000  15.012  1.00 44.64 ? 270 SER A CA    1 
ATOM   1984 C C     . SER A 1 279 ? 9.940  12.735  15.211  1.00 52.34 ? 270 SER A C     1 
ATOM   1985 O O     . SER A 1 279 ? 9.140  13.138  14.361  1.00 51.61 ? 270 SER A O     1 
ATOM   1986 C CB    . SER A 1 279 ? 11.929 12.223  13.794  1.00 51.08 ? 270 SER A CB    1 
ATOM   1987 O OG    . SER A 1 279 ? 11.773 10.828  13.982  1.00 55.40 ? 270 SER A OG    1 
ATOM   1988 N N     . GLY A 1 280 ? 9.554  12.068  16.297  1.00 48.93 ? 271 GLY A N     1 
ATOM   1989 C CA    . GLY A 1 280 ? 8.152  11.823  16.568  1.00 45.24 ? 271 GLY A CA    1 
ATOM   1990 C C     . GLY A 1 280 ? 7.494  10.768  15.709  1.00 52.55 ? 271 GLY A C     1 
ATOM   1991 O O     . GLY A 1 280 ? 6.267  10.637  15.749  1.00 45.28 ? 271 GLY A O     1 
ATOM   1992 N N     . SER A 1 281 ? 8.264  10.012  14.930  1.00 50.89 ? 272 SER A N     1 
ATOM   1993 C CA    . SER A 1 281 ? 7.715  8.958   14.091  1.00 46.99 ? 272 SER A CA    1 
ATOM   1994 C C     . SER A 1 281 ? 8.680  7.783   14.069  1.00 42.37 ? 272 SER A C     1 
ATOM   1995 O O     . SER A 1 281 ? 9.882  7.935   14.299  1.00 43.69 ? 272 SER A O     1 
ATOM   1996 C CB    . SER A 1 281 ? 7.448  9.452   12.661  1.00 52.35 ? 272 SER A CB    1 
ATOM   1997 O OG    . SER A 1 281 ? 6.453  10.462  12.647  1.00 63.51 ? 272 SER A OG    1 
ATOM   1998 N N     . LYS A 1 282 ? 8.139  6.603   13.786  1.00 40.95 ? 273 LYS A N     1 
ATOM   1999 C CA    . LYS A 1 282 ? 8.936  5.386   13.718  1.00 37.70 ? 273 LYS A CA    1 
ATOM   2000 C C     . LYS A 1 282 ? 9.481  5.187   12.310  1.00 39.97 ? 273 LYS A C     1 
ATOM   2001 O O     . LYS A 1 282 ? 8.814  5.504   11.320  1.00 33.32 ? 273 LYS A O     1 
ATOM   2002 C CB    . LYS A 1 282 ? 8.102  4.171   14.131  1.00 42.32 ? 273 LYS A CB    1 
ATOM   2003 C CG    . LYS A 1 282 ? 8.064  3.918   15.635  1.00 42.91 ? 273 LYS A CG    1 
ATOM   2004 C CD    . LYS A 1 282 ? 6.958  2.940   16.004  1.00 45.81 ? 273 LYS A CD    1 
ATOM   2005 C CE    . LYS A 1 282 ? 7.097  2.453   17.439  1.00 48.88 ? 273 LYS A CE    1 
ATOM   2006 N NZ    . LYS A 1 282 ? 7.656  3.503   18.335  1.00 52.55 ? 273 LYS A NZ    1 
ATOM   2007 N N     . LEU A 1 283 ? 10.702 4.665   12.228  1.00 37.70 ? 274 LEU A N     1 
ATOM   2008 C CA    . LEU A 1 283 ? 11.274 4.304   10.942  1.00 41.14 ? 274 LEU A CA    1 
ATOM   2009 C C     . LEU A 1 283 ? 10.442 3.197   10.296  1.00 36.88 ? 274 LEU A C     1 
ATOM   2010 O O     . LEU A 1 283 ? 9.608  2.552   10.936  1.00 33.35 ? 274 LEU A O     1 
ATOM   2011 C CB    . LEU A 1 283 ? 12.724 3.849   11.105  1.00 41.83 ? 274 LEU A CB    1 
ATOM   2012 C CG    . LEU A 1 283 ? 13.773 4.886   11.520  1.00 38.26 ? 274 LEU A CG    1 
ATOM   2013 C CD1   . LEU A 1 283 ? 14.974 4.197   12.142  1.00 38.48 ? 274 LEU A CD1   1 
ATOM   2014 C CD2   . LEU A 1 283 ? 14.205 5.735   10.335  1.00 27.39 ? 274 LEU A CD2   1 
ATOM   2015 N N     . ALA A 1 284 ? 10.675 2.982   9.001   1.00 36.96 ? 275 ALA A N     1 
ATOM   2016 C CA    . ALA A 1 284 ? 9.964  1.919   8.301   1.00 35.03 ? 275 ALA A CA    1 
ATOM   2017 C C     . ALA A 1 284 ? 10.271 0.560   8.917   1.00 29.83 ? 275 ALA A C     1 
ATOM   2018 O O     . ALA A 1 284 ? 9.359  -0.223  9.205   1.00 32.76 ? 275 ALA A O     1 
ATOM   2019 C CB    . ALA A 1 284 ? 10.322 1.934   6.813   1.00 38.51 ? 275 ALA A CB    1 
ATOM   2020 N N     . TYR A 1 285 ? 11.551 0.269   9.142   1.00 25.60 ? 276 TYR A N     1 
ATOM   2021 C CA    . TYR A 1 285 ? 11.961 -1.028  9.668   1.00 31.41 ? 276 TYR A CA    1 
ATOM   2022 C C     . TYR A 1 285 ? 13.445 -0.982  10.004  1.00 31.79 ? 276 TYR A C     1 
ATOM   2023 O O     . TYR A 1 285 ? 14.158 -0.039  9.648   1.00 30.78 ? 276 TYR A O     1 
ATOM   2024 C CB    . TYR A 1 285 ? 11.681 -2.158  8.671   1.00 32.94 ? 276 TYR A CB    1 
ATOM   2025 C CG    . TYR A 1 285 ? 12.295 -1.942  7.302   1.00 30.92 ? 276 TYR A CG    1 
ATOM   2026 C CD1   . TYR A 1 285 ? 13.633 -2.238  7.061   1.00 34.08 ? 276 TYR A CD1   1 
ATOM   2027 C CD2   . TYR A 1 285 ? 11.535 -1.452  6.249   1.00 35.99 ? 276 TYR A CD2   1 
ATOM   2028 C CE1   . TYR A 1 285 ? 14.196 -2.045  5.813   1.00 36.08 ? 276 TYR A CE1   1 
ATOM   2029 C CE2   . TYR A 1 285 ? 12.090 -1.256  4.996   1.00 39.20 ? 276 TYR A CE2   1 
ATOM   2030 C CZ    . TYR A 1 285 ? 13.421 -1.553  4.784   1.00 32.97 ? 276 TYR A CZ    1 
ATOM   2031 O OH    . TYR A 1 285 ? 13.976 -1.363  3.539   1.00 40.57 ? 276 TYR A OH    1 
ATOM   2032 N N     . LEU A 1 286 ? 13.897 -2.028  10.691  1.00 30.81 ? 277 LEU A N     1 
ATOM   2033 C CA    . LEU A 1 286 ? 15.311 -2.319  10.879  1.00 31.03 ? 277 LEU A CA    1 
ATOM   2034 C C     . LEU A 1 286 ? 15.612 -3.635  10.174  1.00 26.95 ? 277 LEU A C     1 
ATOM   2035 O O     . LEU A 1 286 ? 15.004 -4.664  10.488  1.00 28.50 ? 277 LEU A O     1 
ATOM   2036 C CB    . LEU A 1 286 ? 15.668 -2.402  12.364  1.00 30.49 ? 277 LEU A CB    1 
ATOM   2037 C CG    . LEU A 1 286 ? 17.079 -2.886  12.707  1.00 26.16 ? 277 LEU A CG    1 
ATOM   2038 C CD1   . LEU A 1 286 ? 18.129 -1.993  12.059  1.00 25.13 ? 277 LEU A CD1   1 
ATOM   2039 C CD2   . LEU A 1 286 ? 17.265 -2.929  14.212  1.00 32.47 ? 277 LEU A CD2   1 
ATOM   2040 N N     . HIS A 1 287 ? 16.537 -3.598  9.223   1.00 29.90 ? 278 HIS A N     1 
ATOM   2041 C CA    . HIS A 1 287 ? 16.907 -4.753  8.415   1.00 30.94 ? 278 HIS A CA    1 
ATOM   2042 C C     . HIS A 1 287 ? 18.285 -5.229  8.855   1.00 28.34 ? 278 HIS A C     1 
ATOM   2043 O O     . HIS A 1 287 ? 19.253 -4.465  8.800   1.00 27.74 ? 278 HIS A O     1 
ATOM   2044 C CB    . HIS A 1 287 ? 16.906 -4.383  6.931   1.00 30.77 ? 278 HIS A CB    1 
ATOM   2045 C CG    . HIS A 1 287 ? 16.823 -5.557  6.006   1.00 34.59 ? 278 HIS A CG    1 
ATOM   2046 N ND1   . HIS A 1 287 ? 16.684 -5.416  4.642   1.00 33.52 ? 278 HIS A ND1   1 
ATOM   2047 C CD2   . HIS A 1 287 ? 16.864 -6.889  6.244   1.00 32.35 ? 278 HIS A CD2   1 
ATOM   2048 C CE1   . HIS A 1 287 ? 16.640 -6.611  4.079   1.00 35.12 ? 278 HIS A CE1   1 
ATOM   2049 N NE2   . HIS A 1 287 ? 16.748 -7.522  5.029   1.00 34.02 ? 278 HIS A NE2   1 
ATOM   2050 N N     . VAL A 1 288 ? 18.378 -6.479  9.304   1.00 26.14 ? 279 VAL A N     1 
ATOM   2051 C CA    . VAL A 1 288 ? 19.639 -7.037  9.779   1.00 25.70 ? 279 VAL A CA    1 
ATOM   2052 C C     . VAL A 1 288 ? 19.877 -8.370  9.087   1.00 32.96 ? 279 VAL A C     1 
ATOM   2053 O O     . VAL A 1 288 ? 18.981 -9.219  9.042   1.00 35.83 ? 279 VAL A O     1 
ATOM   2054 C CB    . VAL A 1 288 ? 19.657 -7.221  11.311  1.00 35.88 ? 279 VAL A CB    1 
ATOM   2055 C CG1   . VAL A 1 288 ? 21.059 -7.579  11.775  1.00 29.90 ? 279 VAL A CG1   1 
ATOM   2056 C CG2   . VAL A 1 288 ? 19.179 -5.962  12.013  1.00 26.07 ? 279 VAL A CG2   1 
ATOM   2057 N N     . THR A 1 289 ? 21.081 -8.552  8.553   1.00 33.98 ? 280 THR A N     1 
ATOM   2058 C CA    . THR A 1 289 ? 21.496 -9.807  7.943   1.00 39.84 ? 280 THR A CA    1 
ATOM   2059 C C     . THR A 1 289 ? 22.515 -10.488 8.846   1.00 37.60 ? 280 THR A C     1 
ATOM   2060 O O     . THR A 1 289 ? 23.505 -9.868  9.251   1.00 43.35 ? 280 THR A O     1 
ATOM   2061 C CB    . THR A 1 289 ? 22.096 -9.583  6.553   1.00 34.51 ? 280 THR A CB    1 
ATOM   2062 O OG1   . THR A 1 289 ? 21.147 -8.900  5.725   1.00 43.83 ? 280 THR A OG1   1 
ATOM   2063 C CG2   . THR A 1 289 ? 22.441 -10.916 5.913   1.00 37.53 ? 280 THR A CG2   1 
ATOM   2064 N N     . GLN A 1 290 ? 22.273 -11.753 9.153   1.00 38.20 ? 281 GLN A N     1 
ATOM   2065 C CA    . GLN A 1 290 ? 23.125 -12.536 10.031  1.00 44.11 ? 281 GLN A CA    1 
ATOM   2066 C C     . GLN A 1 290 ? 24.132 -13.346 9.226   1.00 49.00 ? 281 GLN A C     1 
ATOM   2067 O O     . GLN A 1 290 ? 23.902 -13.658 8.053   1.00 41.78 ? 281 GLN A O     1 
ATOM   2068 C CB    . GLN A 1 290 ? 22.271 -13.468 10.900  1.00 43.28 ? 281 GLN A CB    1 
ATOM   2069 C CG    . GLN A 1 290 ? 21.440 -14.468 10.124  1.00 46.09 ? 281 GLN A CG    1 
ATOM   2070 C CD    . GLN A 1 290 ? 20.756 -15.469 11.033  1.00 51.36 ? 281 GLN A CD    1 
ATOM   2071 O OE1   . GLN A 1 290 ? 19.635 -15.245 11.489  1.00 51.83 ? 281 GLN A OE1   1 
ATOM   2072 N NE2   . GLN A 1 290 ? 21.434 -16.578 11.309  1.00 57.79 ? 281 GLN A NE2   1 
ATOM   2073 N N     . PRO A 1 291 ? 25.273 -13.704 9.828   1.00 49.58 ? 282 PRO A N     1 
ATOM   2074 C CA    . PRO A 1 291 ? 26.328 -14.381 9.054   1.00 47.84 ? 282 PRO A CA    1 
ATOM   2075 C C     . PRO A 1 291 ? 26.029 -15.835 8.723   1.00 59.67 ? 282 PRO A C     1 
ATOM   2076 O O     . PRO A 1 291 ? 26.659 -16.375 7.803   1.00 62.91 ? 282 PRO A O     1 
ATOM   2077 C CB    . PRO A 1 291 ? 27.557 -14.266 9.964   1.00 44.42 ? 282 PRO A CB    1 
ATOM   2078 C CG    . PRO A 1 291 ? 26.987 -14.187 11.341  1.00 44.06 ? 282 PRO A CG    1 
ATOM   2079 C CD    . PRO A 1 291 ? 25.703 -13.415 11.209  1.00 41.38 ? 282 PRO A CD    1 
ATOM   2080 N N     . ARG A 1 292 ? 25.107 -16.481 9.435   1.00 48.55 ? 283 ARG A N     1 
ATOM   2081 C CA    . ARG A 1 292 ? 24.766 -17.901 9.237   1.00 59.75 ? 283 ARG A CA    1 
ATOM   2082 C C     . ARG A 1 292 ? 26.019 -18.721 9.539   1.00 68.65 ? 283 ARG A C     1 
ATOM   2083 O O     . ARG A 1 292 ? 26.586 -18.565 10.633  1.00 73.56 ? 283 ARG A O     1 
ATOM   2084 C CB    . ARG A 1 292 ? 24.168 -18.106 7.850   1.00 54.40 ? 283 ARG A CB    1 
ATOM   2085 C CG    . ARG A 1 292 ? 22.715 -17.703 7.738   1.00 57.45 ? 283 ARG A CG    1 
ATOM   2086 C CD    . ARG A 1 292 ? 21.791 -18.827 8.170   1.00 52.89 ? 283 ARG A CD    1 
ATOM   2087 N NE    . ARG A 1 292 ? 20.402 -18.388 8.189   1.00 51.26 ? 283 ARG A NE    1 
ATOM   2088 C CZ    . ARG A 1 292 ? 19.539 -18.668 9.155   1.00 47.40 ? 283 ARG A CZ    1 
ATOM   2089 N NH1   . ARG A 1 292 ? 19.881 -19.413 10.193  1.00 50.17 ? 283 ARG A NH1   1 
ATOM   2090 N NH2   . ARG A 1 292 ? 18.301 -18.189 9.076   1.00 40.15 ? 283 ARG A NH2   1 
ATOM   2091 N N     . SER A 1 293 ? 26.474 -19.583 8.631   1.00 65.98 ? 284 SER A N     1 
ATOM   2092 C CA    . SER A 1 293 ? 27.643 -20.437 8.846   1.00 71.77 ? 284 SER A CA    1 
ATOM   2093 C C     . SER A 1 293 ? 27.502 -21.285 10.109  1.00 65.81 ? 284 SER A C     1 
ATOM   2094 O O     . SER A 1 293 ? 28.448 -21.422 10.885  1.00 71.11 ? 284 SER A O     1 
ATOM   2095 C CB    . SER A 1 293 ? 28.922 -19.596 8.916   1.00 71.05 ? 284 SER A CB    1 
ATOM   2096 N N     . GLY A 1 296 ? 27.773 -26.297 11.015  1.00 58.75 ? 287 GLY A N     1 
ATOM   2097 C CA    . GLY A 1 296 ? 28.412 -25.876 12.248  1.00 69.50 ? 287 GLY A CA    1 
ATOM   2098 C C     . GLY A 1 296 ? 27.503 -25.962 13.459  1.00 72.60 ? 287 GLY A C     1 
ATOM   2099 O O     . GLY A 1 296 ? 26.368 -26.429 13.363  1.00 78.83 ? 287 GLY A O     1 
ATOM   2100 N N     . GLY A 1 297 ? 28.005 -25.508 14.604  1.00 70.06 ? 288 GLY A N     1 
ATOM   2101 C CA    . GLY A 1 297 ? 27.231 -25.531 15.829  1.00 68.04 ? 288 GLY A CA    1 
ATOM   2102 C C     . GLY A 1 297 ? 27.167 -24.187 16.525  1.00 68.50 ? 288 GLY A C     1 
ATOM   2103 O O     . GLY A 1 297 ? 27.357 -24.101 17.742  1.00 65.63 ? 288 GLY A O     1 
ATOM   2104 N N     . SER A 1 298 ? 26.896 -23.125 15.762  1.00 60.37 ? 289 SER A N     1 
ATOM   2105 C CA    . SER A 1 298 ? 26.799 -21.775 16.304  1.00 56.86 ? 289 SER A CA    1 
ATOM   2106 C C     . SER A 1 298 ? 25.468 -21.128 15.939  1.00 60.57 ? 289 SER A C     1 
ATOM   2107 O O     . SER A 1 298 ? 25.358 -19.899 15.892  1.00 57.57 ? 289 SER A O     1 
ATOM   2108 C CB    . SER A 1 298 ? 27.965 -20.910 15.825  1.00 60.84 ? 289 SER A CB    1 
ATOM   2109 O OG    . SER A 1 298 ? 28.072 -20.931 14.412  1.00 66.66 ? 289 SER A OG    1 
ATOM   2110 N N     . GLU A 1 299 ? 24.443 -21.946 15.682  1.00 57.74 ? 290 GLU A N     1 
ATOM   2111 C CA    . GLU A 1 299 ? 23.145 -21.405 15.290  1.00 53.25 ? 290 GLU A CA    1 
ATOM   2112 C C     . GLU A 1 299 ? 22.443 -20.735 16.465  1.00 53.77 ? 290 GLU A C     1 
ATOM   2113 O O     . GLU A 1 299 ? 21.760 -19.719 16.288  1.00 53.51 ? 290 GLU A O     1 
ATOM   2114 C CB    . GLU A 1 299 ? 22.271 -22.514 14.706  1.00 52.89 ? 290 GLU A CB    1 
ATOM   2115 C CG    . GLU A 1 299 ? 22.760 -23.050 13.371  1.00 66.01 ? 290 GLU A CG    1 
ATOM   2116 C CD    . GLU A 1 299 ? 23.474 -24.382 13.502  1.00 68.37 ? 290 GLU A CD    1 
ATOM   2117 O OE1   . GLU A 1 299 ? 23.560 -24.902 14.635  1.00 65.48 ? 290 GLU A OE1   1 
ATOM   2118 O OE2   . GLU A 1 299 ? 23.949 -24.909 12.474  1.00 73.24 ? 290 GLU A OE2   1 
ATOM   2119 N N     . GLU A 1 300 ? 22.597 -21.287 17.671  1.00 46.14 ? 291 GLU A N     1 
ATOM   2120 C CA    . GLU A 1 300 ? 21.929 -20.711 18.834  1.00 43.68 ? 291 GLU A CA    1 
ATOM   2121 C C     . GLU A 1 300 ? 22.537 -19.366 19.214  1.00 40.60 ? 291 GLU A C     1 
ATOM   2122 O O     . GLU A 1 300 ? 21.820 -18.452 19.637  1.00 42.28 ? 291 GLU A O     1 
ATOM   2123 C CB    . GLU A 1 300 ? 21.995 -21.682 20.013  1.00 47.97 ? 291 GLU A CB    1 
ATOM   2124 N N     . GLU A 1 301 ? 23.857 -19.227 19.071  1.00 41.99 ? 292 GLU A N     1 
ATOM   2125 C CA    . GLU A 1 301 ? 24.506 -17.966 19.414  1.00 48.51 ? 292 GLU A CA    1 
ATOM   2126 C C     . GLU A 1 301 ? 24.171 -16.878 18.402  1.00 45.26 ? 292 GLU A C     1 
ATOM   2127 O O     . GLU A 1 301 ? 23.958 -15.718 18.777  1.00 42.64 ? 292 GLU A O     1 
ATOM   2128 C CB    . GLU A 1 301 ? 26.019 -18.162 19.509  1.00 53.38 ? 292 GLU A CB    1 
ATOM   2129 C CG    . GLU A 1 301 ? 26.689 -17.294 20.562  1.00 63.76 ? 292 GLU A CG    1 
ATOM   2130 C CD    . GLU A 1 301 ? 27.763 -18.036 21.334  1.00 68.84 ? 292 GLU A CD    1 
ATOM   2131 O OE1   . GLU A 1 301 ? 27.412 -18.808 22.252  1.00 65.66 ? 292 GLU A OE1   1 
ATOM   2132 O OE2   . GLU A 1 301 ? 28.958 -17.844 21.024  1.00 65.21 ? 292 GLU A OE2   1 
ATOM   2133 N N     . GLU A 1 302 ? 24.122 -17.230 17.115  1.00 43.97 ? 293 GLU A N     1 
ATOM   2134 C CA    . GLU A 1 302 ? 23.781 -16.242 16.098  1.00 45.91 ? 293 GLU A CA    1 
ATOM   2135 C C     . GLU A 1 302 ? 22.319 -15.827 16.188  1.00 44.75 ? 293 GLU A C     1 
ATOM   2136 O O     . GLU A 1 302 ? 21.986 -14.671 15.902  1.00 38.30 ? 293 GLU A O     1 
ATOM   2137 C CB    . GLU A 1 302 ? 24.094 -16.791 14.706  1.00 46.96 ? 293 GLU A CB    1 
ATOM   2138 N N     . ALA A 1 303 ? 21.434 -16.747 16.581  1.00 40.25 ? 294 ALA A N     1 
ATOM   2139 C CA    . ALA A 1 303 ? 20.031 -16.388 16.752  1.00 38.68 ? 294 ALA A CA    1 
ATOM   2140 C C     . ALA A 1 303 ? 19.820 -15.529 17.992  1.00 41.99 ? 294 ALA A C     1 
ATOM   2141 O O     . ALA A 1 303 ? 18.911 -14.692 18.018  1.00 44.77 ? 294 ALA A O     1 
ATOM   2142 C CB    . ALA A 1 303 ? 19.169 -17.648 16.821  1.00 34.66 ? 294 ALA A CB    1 
ATOM   2143 N N     . ARG A 1 304 ? 20.648 -15.715 19.023  1.00 37.59 ? 295 ARG A N     1 
ATOM   2144 C CA    . ARG A 1 304 ? 20.529 -14.890 20.220  1.00 41.95 ? 295 ARG A CA    1 
ATOM   2145 C C     . ARG A 1 304 ? 20.928 -13.446 19.938  1.00 39.33 ? 295 ARG A C     1 
ATOM   2146 O O     . ARG A 1 304 ? 20.320 -12.512 20.475  1.00 36.48 ? 295 ARG A O     1 
ATOM   2147 C CB    . ARG A 1 304 ? 21.385 -15.473 21.344  1.00 35.91 ? 295 ARG A CB    1 
ATOM   2148 C CG    . ARG A 1 304 ? 21.223 -14.771 22.683  1.00 43.95 ? 295 ARG A CG    1 
ATOM   2149 C CD    . ARG A 1 304 ? 22.191 -15.325 23.715  1.00 35.33 ? 295 ARG A CD    1 
ATOM   2150 N NE    . ARG A 1 304 ? 23.575 -15.253 23.260  1.00 54.41 ? 295 ARG A NE    1 
ATOM   2151 C CZ    . ARG A 1 304 ? 24.565 -15.989 23.749  1.00 52.07 ? 295 ARG A CZ    1 
ATOM   2152 N NH1   . ARG A 1 304 ? 24.359 -16.873 24.711  1.00 61.24 ? 295 ARG A NH1   1 
ATOM   2153 N NH2   . ARG A 1 304 ? 25.792 -15.832 23.261  1.00 53.06 ? 295 ARG A NH2   1 
ATOM   2154 N N     . LEU A 1 305 ? 21.946 -13.243 19.099  1.00 39.62 ? 296 LEU A N     1 
ATOM   2155 C CA    . LEU A 1 305 ? 22.358 -11.884 18.763  1.00 39.60 ? 296 LEU A CA    1 
ATOM   2156 C C     . LEU A 1 305 ? 21.277 -11.163 17.966  1.00 38.37 ? 296 LEU A C     1 
ATOM   2157 O O     . LEU A 1 305 ? 20.993 -9.986  18.220  1.00 38.88 ? 296 LEU A O     1 
ATOM   2158 C CB    . LEU A 1 305 ? 23.677 -11.909 17.989  1.00 35.45 ? 296 LEU A CB    1 
ATOM   2159 C CG    . LEU A 1 305 ? 24.386 -10.565 17.794  1.00 40.81 ? 296 LEU A CG    1 
ATOM   2160 C CD1   . LEU A 1 305 ? 25.883 -10.714 18.006  1.00 39.60 ? 296 LEU A CD1   1 
ATOM   2161 C CD2   . LEU A 1 305 ? 24.101 -9.993  16.414  1.00 39.01 ? 296 LEU A CD2   1 
ATOM   2162 N N     . MET A 1 306 ? 20.660 -11.852 17.003  1.00 36.57 ? 297 MET A N     1 
ATOM   2163 C CA    . MET A 1 306 ? 19.598 -11.229 16.218  1.00 39.86 ? 297 MET A CA    1 
ATOM   2164 C C     . MET A 1 306 ? 18.377 -10.927 17.077  1.00 37.00 ? 297 MET A C     1 
ATOM   2165 O O     . MET A 1 306 ? 17.765 -9.860  16.944  1.00 32.64 ? 297 MET A O     1 
ATOM   2166 C CB    . MET A 1 306 ? 19.219 -12.126 15.042  1.00 33.36 ? 297 MET A CB    1 
ATOM   2167 C CG    . MET A 1 306 ? 20.320 -12.267 14.016  1.00 43.83 ? 297 MET A CG    1 
ATOM   2168 S SD    . MET A 1 306 ? 20.265 -10.940 12.793  1.00 40.28 ? 297 MET A SD    1 
ATOM   2169 C CE    . MET A 1 306 ? 18.532 -10.960 12.353  1.00 35.88 ? 297 MET A CE    1 
ATOM   2170 N N     . ARG A 1 307 ? 18.008 -11.856 17.962  1.00 32.33 ? 298 ARG A N     1 
ATOM   2171 C CA    . ARG A 1 307 ? 16.880 -11.618 18.856  1.00 39.65 ? 298 ARG A CA    1 
ATOM   2172 C C     . ARG A 1 307 ? 17.176 -10.479 19.822  1.00 31.77 ? 298 ARG A C     1 
ATOM   2173 O O     . ARG A 1 307 ? 16.282 -9.692  20.153  1.00 32.24 ? 298 ARG A O     1 
ATOM   2174 C CB    . ARG A 1 307 ? 16.535 -12.897 19.621  1.00 33.72 ? 298 ARG A CB    1 
ATOM   2175 C CG    . ARG A 1 307 ? 15.251 -12.801 20.440  1.00 36.16 ? 298 ARG A CG    1 
ATOM   2176 C CD    . ARG A 1 307 ? 14.102 -12.254 19.607  1.00 41.30 ? 298 ARG A CD    1 
ATOM   2177 N NE    . ARG A 1 307 ? 12.900 -12.024 20.400  1.00 40.99 ? 298 ARG A NE    1 
ATOM   2178 C CZ    . ARG A 1 307 ? 11.824 -12.800 20.374  1.00 41.31 ? 298 ARG A CZ    1 
ATOM   2179 N NH1   . ARG A 1 307 ? 11.762 -13.872 19.601  1.00 40.59 ? 298 ARG A NH1   1 
ATOM   2180 N NH2   . ARG A 1 307 ? 10.784 -12.491 21.142  1.00 47.29 ? 298 ARG A NH2   1 
ATOM   2181 N N     . THR A 1 308 ? 18.427 -10.373 20.280  1.00 34.41 ? 299 THR A N     1 
ATOM   2182 C CA    . THR A 1 308 ? 18.801 -9.281  21.175  1.00 34.03 ? 299 THR A CA    1 
ATOM   2183 C C     . THR A 1 308 ? 18.652 -7.927  20.492  1.00 32.97 ? 299 THR A C     1 
ATOM   2184 O O     . THR A 1 308 ? 18.178 -6.961  21.104  1.00 29.00 ? 299 THR A O     1 
ATOM   2185 C CB    . THR A 1 308 ? 20.236 -9.473  21.666  1.00 35.98 ? 299 THR A CB    1 
ATOM   2186 O OG1   . THR A 1 308 ? 20.425 -10.832 22.080  1.00 40.36 ? 299 THR A OG1   1 
ATOM   2187 C CG2   . THR A 1 308 ? 20.527 -8.544  22.836  1.00 33.10 ? 299 THR A CG2   1 
ATOM   2188 N N     . LEU A 1 309 ? 19.059 -7.832  19.223  1.00 31.92 ? 300 LEU A N     1 
ATOM   2189 C CA    . LEU A 1 309 ? 18.889 -6.579  18.494  1.00 32.46 ? 300 LEU A CA    1 
ATOM   2190 C C     . LEU A 1 309 ? 17.414 -6.281  18.254  1.00 30.68 ? 300 LEU A C     1 
ATOM   2191 O O     . LEU A 1 309 ? 16.980 -5.128  18.369  1.00 28.11 ? 300 LEU A O     1 
ATOM   2192 C CB    . LEU A 1 309 ? 19.650 -6.632  17.170  1.00 32.31 ? 300 LEU A CB    1 
ATOM   2193 C CG    . LEU A 1 309 ? 21.165 -6.818  17.276  1.00 43.47 ? 300 LEU A CG    1 
ATOM   2194 C CD1   . LEU A 1 309 ? 21.788 -6.975  15.896  1.00 35.75 ? 300 LEU A CD1   1 
ATOM   2195 C CD2   . LEU A 1 309 ? 21.798 -5.656  18.031  1.00 33.15 ? 300 LEU A CD2   1 
ATOM   2196 N N     . ARG A 1 310 ? 16.632 -7.313  17.922  1.00 31.11 ? 301 ARG A N     1 
ATOM   2197 C CA    . ARG A 1 310 ? 15.200 -7.135  17.706  1.00 29.83 ? 301 ARG A CA    1 
ATOM   2198 C C     . ARG A 1 310 ? 14.512 -6.608  18.959  1.00 34.55 ? 301 ARG A C     1 
ATOM   2199 O O     . ARG A 1 310 ? 13.766 -5.623  18.906  1.00 35.11 ? 301 ARG A O     1 
ATOM   2200 C CB    . ARG A 1 310 ? 14.573 -8.461  17.273  1.00 33.05 ? 301 ARG A CB    1 
ATOM   2201 C CG    . ARG A 1 310 ? 13.155 -8.335  16.743  1.00 35.29 ? 301 ARG A CG    1 
ATOM   2202 C CD    . ARG A 1 310 ? 12.112 -8.664  17.799  1.00 33.88 ? 301 ARG A CD    1 
ATOM   2203 N NE    . ARG A 1 310 ? 10.911 -9.245  17.209  1.00 41.20 ? 301 ARG A NE    1 
ATOM   2204 C CZ    . ARG A 1 310 ? 10.011 -8.564  16.512  1.00 41.15 ? 301 ARG A CZ    1 
ATOM   2205 N NH1   . ARG A 1 310 ? 10.136 -7.263  16.305  1.00 38.04 ? 301 ARG A NH1   1 
ATOM   2206 N NH2   . ARG A 1 310 ? 8.958  -9.205  16.012  1.00 38.06 ? 301 ARG A NH2   1 
ATOM   2207 N N     . ASN A 1 311 ? 14.747 -7.261  20.101  1.00 29.66 ? 302 ASN A N     1 
ATOM   2208 C CA    . ASN A 1 311 ? 14.094 -6.861  21.343  1.00 36.27 ? 302 ASN A CA    1 
ATOM   2209 C C     . ASN A 1 311 ? 14.478 -5.452  21.773  1.00 31.76 ? 302 ASN A C     1 
ATOM   2210 O O     . ASN A 1 311 ? 13.730 -4.822  22.527  1.00 39.08 ? 302 ASN A O     1 
ATOM   2211 C CB    . ASN A 1 311 ? 14.436 -7.849  22.459  1.00 28.95 ? 302 ASN A CB    1 
ATOM   2212 C CG    . ASN A 1 311 ? 13.714 -9.173  22.308  1.00 33.43 ? 302 ASN A CG    1 
ATOM   2213 O OD1   . ASN A 1 311 ? 12.688 -9.261  21.635  1.00 36.60 ? 302 ASN A OD1   1 
ATOM   2214 N ND2   . ASN A 1 311 ? 14.247 -10.213 22.940  1.00 36.36 ? 302 ASN A ND2   1 
ATOM   2215 N N     . ALA A 1 312 ? 15.620 -4.946  21.316  1.00 31.54 ? 303 ALA A N     1 
ATOM   2216 C CA    . ALA A 1 312 ? 16.088 -3.631  21.729  1.00 33.68 ? 303 ALA A CA    1 
ATOM   2217 C C     . ALA A 1 312 ? 15.537 -2.498  20.874  1.00 32.04 ? 303 ALA A C     1 
ATOM   2218 O O     . ALA A 1 312 ? 15.597 -1.338  21.298  1.00 31.74 ? 303 ALA A O     1 
ATOM   2219 C CB    . ALA A 1 312 ? 17.620 -3.587  21.700  1.00 29.60 ? 303 ALA A CB    1 
ATOM   2220 N N     . TYR A 1 313 ? 14.997 -2.797  19.696  1.00 30.68 ? 304 TYR A N     1 
ATOM   2221 C CA    . TYR A 1 313 ? 14.567 -1.773  18.752  1.00 34.62 ? 304 TYR A CA    1 
ATOM   2222 C C     . TYR A 1 313 ? 13.052 -1.622  18.783  1.00 32.03 ? 304 TYR A C     1 
ATOM   2223 O O     . TYR A 1 313 ? 12.321 -2.612  18.672  1.00 33.92 ? 304 TYR A O     1 
ATOM   2224 C CB    . TYR A 1 313 ? 15.032 -2.108  17.334  1.00 33.93 ? 304 TYR A CB    1 
ATOM   2225 C CG    . TYR A 1 313 ? 14.416 -1.214  16.282  1.00 34.28 ? 304 TYR A CG    1 
ATOM   2226 C CD1   . TYR A 1 313 ? 14.610 0.160   16.314  1.00 33.78 ? 304 TYR A CD1   1 
ATOM   2227 C CD2   . TYR A 1 313 ? 13.627 -1.741  15.271  1.00 28.19 ? 304 TYR A CD2   1 
ATOM   2228 C CE1   . TYR A 1 313 ? 14.043 0.984   15.363  1.00 36.05 ? 304 TYR A CE1   1 
ATOM   2229 C CE2   . TYR A 1 313 ? 13.056 -0.925  14.313  1.00 37.37 ? 304 TYR A CE2   1 
ATOM   2230 C CZ    . TYR A 1 313 ? 13.267 0.436   14.365  1.00 38.61 ? 304 TYR A CZ    1 
ATOM   2231 O OH    . TYR A 1 313 ? 12.699 1.250   13.413  1.00 42.46 ? 304 TYR A OH    1 
ATOM   2232 N N     . GLN A 1 314 ? 12.587 -0.380  18.916  1.00 33.58 ? 305 GLN A N     1 
ATOM   2233 C CA    . GLN A 1 314 ? 11.157 -0.072  18.947  1.00 35.19 ? 305 GLN A CA    1 
ATOM   2234 C C     . GLN A 1 314 ? 10.673 0.127   17.516  1.00 39.99 ? 305 GLN A C     1 
ATOM   2235 O O     . GLN A 1 314 ? 10.642 1.244   16.999  1.00 40.32 ? 305 GLN A O     1 
ATOM   2236 C CB    . GLN A 1 314 ? 10.893 1.165   19.797  1.00 37.96 ? 305 GLN A CB    1 
ATOM   2237 C CG    . GLN A 1 314 ? 11.733 1.253   21.063  1.00 42.05 ? 305 GLN A CG    1 
ATOM   2238 C CD    . GLN A 1 314 ? 11.517 2.553   21.821  1.00 41.25 ? 305 GLN A CD    1 
ATOM   2239 O OE1   . GLN A 1 314 ? 10.609 3.326   21.510  1.00 43.67 ? 305 GLN A OE1   1 
ATOM   2240 N NE2   . GLN A 1 314 ? 12.347 2.795   22.829  1.00 35.91 ? 305 GLN A NE2   1 
ATOM   2241 N N     . GLY A 1 315 ? 10.287 -0.963  16.866  1.00 37.76 ? 306 GLY A N     1 
ATOM   2242 C CA    . GLY A 1 315 ? 9.779  -0.873  15.514  1.00 34.81 ? 306 GLY A CA    1 
ATOM   2243 C C     . GLY A 1 315 ? 9.865  -2.208  14.799  1.00 40.03 ? 306 GLY A C     1 
ATOM   2244 O O     . GLY A 1 315 ? 10.088 -3.253  15.410  1.00 34.14 ? 306 GLY A O     1 
ATOM   2245 N N     . THR A 1 316 ? 9.685  -2.139  13.480  1.00 32.54 ? 307 THR A N     1 
ATOM   2246 C CA    . THR A 1 316 ? 9.645  -3.331  12.642  1.00 35.22 ? 307 THR A CA    1 
ATOM   2247 C C     . THR A 1 316 ? 11.048 -3.884  12.420  1.00 31.14 ? 307 THR A C     1 
ATOM   2248 O O     . THR A 1 316 ? 12.001 -3.132  12.197  1.00 31.56 ? 307 THR A O     1 
ATOM   2249 C CB    . THR A 1 316 ? 8.982  -3.007  11.300  1.00 36.37 ? 307 THR A CB    1 
ATOM   2250 O OG1   . THR A 1 316 ? 7.604  -2.681  11.518  1.00 39.08 ? 307 THR A OG1   1 
ATOM   2251 C CG2   . THR A 1 316 ? 9.071  -4.187  10.335  1.00 31.65 ? 307 THR A CG2   1 
ATOM   2252 N N     . PHE A 1 317 ? 11.170 -5.208  12.486  1.00 32.93 ? 308 PHE A N     1 
ATOM   2253 C CA    . PHE A 1 317 ? 12.446 -5.901  12.346  1.00 31.35 ? 308 PHE A CA    1 
ATOM   2254 C C     . PHE A 1 317 ? 12.368 -6.855  11.161  1.00 30.00 ? 308 PHE A C     1 
ATOM   2255 O O     . PHE A 1 317 ? 11.472 -7.704  11.100  1.00 27.70 ? 308 PHE A O     1 
ATOM   2256 C CB    . PHE A 1 317 ? 12.788 -6.660  13.629  1.00 29.75 ? 308 PHE A CB    1 
ATOM   2257 C CG    . PHE A 1 317 ? 14.209 -7.153  13.693  1.00 30.82 ? 308 PHE A CG    1 
ATOM   2258 C CD1   . PHE A 1 317 ? 15.225 -6.324  14.139  1.00 23.45 ? 308 PHE A CD1   1 
ATOM   2259 C CD2   . PHE A 1 317 ? 14.523 -8.451  13.325  1.00 35.20 ? 308 PHE A CD2   1 
ATOM   2260 C CE1   . PHE A 1 317 ? 16.528 -6.777  14.209  1.00 23.80 ? 308 PHE A CE1   1 
ATOM   2261 C CE2   . PHE A 1 317 ? 15.826 -8.909  13.389  1.00 31.09 ? 308 PHE A CE2   1 
ATOM   2262 C CZ    . PHE A 1 317 ? 16.829 -8.072  13.834  1.00 29.75 ? 308 PHE A CZ    1 
ATOM   2263 N N     . ILE A 1 318 ? 13.301 -6.717  10.225  1.00 35.27 ? 309 ILE A N     1 
ATOM   2264 C CA    . ILE A 1 318 ? 13.410 -7.615  9.080   1.00 27.60 ? 309 ILE A CA    1 
ATOM   2265 C C     . ILE A 1 318 ? 14.701 -8.405  9.231   1.00 25.92 ? 309 ILE A C     1 
ATOM   2266 O O     . ILE A 1 318 ? 15.789 -7.823  9.313   1.00 27.72 ? 309 ILE A O     1 
ATOM   2267 C CB    . ILE A 1 318 ? 13.382 -6.852  7.747   1.00 31.64 ? 309 ILE A CB    1 
ATOM   2268 C CG1   . ILE A 1 318 ? 12.139 -5.964  7.661   1.00 33.54 ? 309 ILE A CG1   1 
ATOM   2269 C CG2   . ILE A 1 318 ? 13.412 -7.828  6.576   1.00 24.29 ? 309 ILE A CG2   1 
ATOM   2270 C CD1   . ILE A 1 318 ? 11.960 -5.296  6.311   1.00 37.49 ? 309 ILE A CD1   1 
ATOM   2271 N N     . CYS A 1 319 ? 14.580 -9.727  9.280   1.00 35.68 ? 310 CYS A N     1 
ATOM   2272 C CA    . CYS A 1 319 ? 15.732 -10.613 9.345   1.00 35.73 ? 310 CYS A CA    1 
ATOM   2273 C C     . CYS A 1 319 ? 16.068 -11.130 7.953   1.00 27.37 ? 310 CYS A C     1 
ATOM   2274 O O     . CYS A 1 319 ? 15.183 -11.348 7.123   1.00 36.20 ? 310 CYS A O     1 
ATOM   2275 C CB    . CYS A 1 319 ? 15.469 -11.788 10.289  1.00 28.98 ? 310 CYS A CB    1 
ATOM   2276 S SG    . CYS A 1 319 ? 14.175 -12.917 9.735   1.00 44.66 ? 310 CYS A SG    1 
ATOM   2277 N N     . SER A 1 320 ? 17.362 -11.323 7.703   1.00 33.20 ? 311 SER A N     1 
ATOM   2278 C CA    . SER A 1 320 ? 17.827 -11.774 6.399   1.00 35.30 ? 311 SER A CA    1 
ATOM   2279 C C     . SER A 1 320 ? 19.048 -12.664 6.575   1.00 36.58 ? 311 SER A C     1 
ATOM   2280 O O     . SER A 1 320 ? 19.752 -12.593 7.584   1.00 33.24 ? 311 SER A O     1 
ATOM   2281 C CB    . SER A 1 320 ? 18.171 -10.595 5.482   1.00 33.37 ? 311 SER A CB    1 
ATOM   2282 O OG    . SER A 1 320 ? 18.431 -11.041 4.160   1.00 39.52 ? 311 SER A OG    1 
ATOM   2283 N N     . GLY A 1 321 ? 19.291 -13.503 5.571   1.00 33.45 ? 312 GLY A N     1 
ATOM   2284 C CA    . GLY A 1 321 ? 20.486 -14.324 5.553   1.00 36.09 ? 312 GLY A CA    1 
ATOM   2285 C C     . GLY A 1 321 ? 20.230 -15.808 5.705   1.00 42.46 ? 312 GLY A C     1 
ATOM   2286 O O     . GLY A 1 321 ? 19.983 -16.293 6.814   1.00 36.61 ? 312 GLY A O     1 
ATOM   2287 N N     . GLY A 1 322 ? 20.286 -16.539 4.594   1.00 39.47 ? 313 GLY A N     1 
ATOM   2288 C CA    . GLY A 1 322 ? 20.185 -17.988 4.638   1.00 40.40 ? 313 GLY A CA    1 
ATOM   2289 C C     . GLY A 1 322 ? 18.855 -18.506 5.128   1.00 41.50 ? 313 GLY A C     1 
ATOM   2290 O O     . GLY A 1 322 ? 18.794 -19.601 5.699   1.00 45.72 ? 313 GLY A O     1 
ATOM   2291 N N     . TYR A 1 323 ? 17.780 -17.752 4.921   1.00 41.75 ? 314 TYR A N     1 
ATOM   2292 C CA    . TYR A 1 323 ? 16.470 -18.148 5.412   1.00 38.00 ? 314 TYR A CA    1 
ATOM   2293 C C     . TYR A 1 323 ? 15.752 -19.004 4.378   1.00 40.81 ? 314 TYR A C     1 
ATOM   2294 O O     . TYR A 1 323 ? 15.864 -18.771 3.171   1.00 43.81 ? 314 TYR A O     1 
ATOM   2295 C CB    . TYR A 1 323 ? 15.631 -16.919 5.766   1.00 40.78 ? 314 TYR A CB    1 
ATOM   2296 C CG    . TYR A 1 323 ? 15.905 -16.401 7.162   1.00 37.96 ? 314 TYR A CG    1 
ATOM   2297 C CD1   . TYR A 1 323 ? 15.266 -16.951 8.265   1.00 39.75 ? 314 TYR A CD1   1 
ATOM   2298 C CD2   . TYR A 1 323 ? 16.818 -15.377 7.377   1.00 40.98 ? 314 TYR A CD2   1 
ATOM   2299 C CE1   . TYR A 1 323 ? 15.520 -16.488 9.543   1.00 42.57 ? 314 TYR A CE1   1 
ATOM   2300 C CE2   . TYR A 1 323 ? 17.079 -14.905 8.652   1.00 39.02 ? 314 TYR A CE2   1 
ATOM   2301 C CZ    . TYR A 1 323 ? 16.429 -15.467 9.731   1.00 42.54 ? 314 TYR A CZ    1 
ATOM   2302 O OH    . TYR A 1 323 ? 16.683 -15.004 11.003  1.00 35.35 ? 314 TYR A OH    1 
ATOM   2303 N N     . THR A 1 324 ? 15.029 -20.006 4.864   1.00 42.95 ? 315 THR A N     1 
ATOM   2304 C CA    . THR A 1 324 ? 14.234 -20.906 4.043   1.00 43.48 ? 315 THR A CA    1 
ATOM   2305 C C     . THR A 1 324 ? 12.760 -20.725 4.400   1.00 43.16 ? 315 THR A C     1 
ATOM   2306 O O     . THR A 1 324 ? 12.395 -19.850 5.191   1.00 43.41 ? 315 THR A O     1 
ATOM   2307 C CB    . THR A 1 324 ? 14.685 -22.354 4.242   1.00 41.70 ? 315 THR A CB    1 
ATOM   2308 O OG1   . THR A 1 324 ? 14.548 -22.711 5.624   1.00 47.08 ? 315 THR A OG1   1 
ATOM   2309 C CG2   . THR A 1 324 ? 16.136 -22.526 3.821   1.00 41.37 ? 315 THR A CG2   1 
ATOM   2310 N N     . ARG A 1 325 ? 11.908 -21.566 3.811   1.00 42.69 ? 316 ARG A N     1 
ATOM   2311 C CA    . ARG A 1 325 ? 10.485 -21.501 4.126   1.00 42.65 ? 316 ARG A CA    1 
ATOM   2312 C C     . ARG A 1 325 ? 10.235 -21.847 5.588   1.00 43.88 ? 316 ARG A C     1 
ATOM   2313 O O     . ARG A 1 325 ? 9.531  -21.121 6.299   1.00 41.97 ? 316 ARG A O     1 
ATOM   2314 C CB    . ARG A 1 325 ? 9.695  -22.435 3.212   1.00 39.79 ? 316 ARG A CB    1 
ATOM   2315 C CG    . ARG A 1 325 ? 8.213  -22.479 3.544   1.00 40.80 ? 316 ARG A CG    1 
ATOM   2316 C CD    . ARG A 1 325 ? 7.464  -23.445 2.649   1.00 44.49 ? 316 ARG A CD    1 
ATOM   2317 N NE    . ARG A 1 325 ? 6.051  -23.516 3.001   1.00 42.91 ? 316 ARG A NE    1 
ATOM   2318 C CZ    . ARG A 1 325 ? 5.559  -24.279 3.967   1.00 43.14 ? 316 ARG A CZ    1 
ATOM   2319 N NH1   . ARG A 1 325 ? 6.339  -25.058 4.699   1.00 39.81 ? 316 ARG A NH1   1 
ATOM   2320 N NH2   . ARG A 1 325 ? 4.251  -24.259 4.206   1.00 43.28 ? 316 ARG A NH2   1 
ATOM   2321 N N     . GLU A 1 326 ? 10.816 -22.954 6.056   1.00 45.14 ? 317 GLU A N     1 
ATOM   2322 C CA    . GLU A 1 326 ? 10.612 -23.367 7.440   1.00 45.64 ? 317 GLU A CA    1 
ATOM   2323 C C     . GLU A 1 326 ? 11.308 -22.420 8.412   1.00 42.39 ? 317 GLU A C     1 
ATOM   2324 O O     . GLU A 1 326 ? 10.753 -22.088 9.465   1.00 48.26 ? 317 GLU A O     1 
ATOM   2325 C CB    . GLU A 1 326 ? 11.107 -24.800 7.635   1.00 49.03 ? 317 GLU A CB    1 
ATOM   2326 N N     . LEU A 1 327 ? 12.523 -21.978 8.077   1.00 44.03 ? 318 LEU A N     1 
ATOM   2327 C CA    . LEU A 1 327 ? 13.237 -21.047 8.947   1.00 45.37 ? 318 LEU A CA    1 
ATOM   2328 C C     . LEU A 1 327 ? 12.528 -19.700 9.012   1.00 42.87 ? 318 LEU A C     1 
ATOM   2329 O O     . LEU A 1 327 ? 12.524 -19.045 10.061  1.00 42.11 ? 318 LEU A O     1 
ATOM   2330 C CB    . LEU A 1 327 ? 14.675 -20.873 8.461   1.00 43.50 ? 318 LEU A CB    1 
ATOM   2331 C CG    . LEU A 1 327 ? 15.690 -21.925 8.913   1.00 48.36 ? 318 LEU A CG    1 
ATOM   2332 C CD1   . LEU A 1 327 ? 17.098 -21.347 8.907   1.00 53.58 ? 318 LEU A CD1   1 
ATOM   2333 C CD2   . LEU A 1 327 ? 15.337 -22.465 10.292  1.00 45.79 ? 318 LEU A CD2   1 
ATOM   2334 N N     . GLY A 1 328 ? 11.927 -19.270 7.902   1.00 41.37 ? 319 GLY A N     1 
ATOM   2335 C CA    . GLY A 1 328 ? 11.179 -18.024 7.916   1.00 42.03 ? 319 GLY A CA    1 
ATOM   2336 C C     . GLY A 1 328 ? 9.855  -18.150 8.643   1.00 41.10 ? 319 GLY A C     1 
ATOM   2337 O O     . GLY A 1 328 ? 9.410  -17.209 9.307   1.00 39.75 ? 319 GLY A O     1 
ATOM   2338 N N     . ILE A 1 329 ? 9.204  -19.311 8.525   1.00 41.55 ? 320 ILE A N     1 
ATOM   2339 C CA    . ILE A 1 329 ? 7.963  -19.549 9.257   1.00 44.69 ? 320 ILE A CA    1 
ATOM   2340 C C     . ILE A 1 329 ? 8.213  -19.458 10.756  1.00 42.76 ? 320 ILE A C     1 
ATOM   2341 O O     . ILE A 1 329 ? 7.476  -18.790 11.491  1.00 41.74 ? 320 ILE A O     1 
ATOM   2342 C CB    . ILE A 1 329 ? 7.359  -20.912 8.867   1.00 45.22 ? 320 ILE A CB    1 
ATOM   2343 C CG1   . ILE A 1 329 ? 6.527  -20.789 7.590   1.00 43.60 ? 320 ILE A CG1   1 
ATOM   2344 C CG2   . ILE A 1 329 ? 6.506  -21.470 10.002  1.00 41.95 ? 320 ILE A CG2   1 
ATOM   2345 C CD1   . ILE A 1 329 ? 6.229  -22.121 6.924   1.00 41.44 ? 320 ILE A CD1   1 
ATOM   2346 N N     . GLU A 1 330 ? 9.272  -20.119 11.229  1.00 42.75 ? 321 GLU A N     1 
ATOM   2347 C CA    . GLU A 1 330 ? 9.576  -20.094 12.653  1.00 44.20 ? 321 GLU A CA    1 
ATOM   2348 C C     . GLU A 1 330 ? 10.035 -18.715 13.107  1.00 41.45 ? 321 GLU A C     1 
ATOM   2349 O O     . GLU A 1 330 ? 9.785  -18.332 14.252  1.00 38.76 ? 321 GLU A O     1 
ATOM   2350 C CB    . GLU A 1 330 ? 10.633 -21.147 12.983  1.00 50.41 ? 321 GLU A CB    1 
ATOM   2351 C CG    . GLU A 1 330 ? 10.076 -22.393 13.658  1.00 55.10 ? 321 GLU A CG    1 
ATOM   2352 C CD    . GLU A 1 330 ? 8.922  -23.009 12.888  1.00 59.08 ? 321 GLU A CD    1 
ATOM   2353 O OE1   . GLU A 1 330 ? 9.147  -23.478 11.750  1.00 58.56 ? 321 GLU A OE1   1 
ATOM   2354 O OE2   . GLU A 1 330 ? 7.791  -23.032 13.422  1.00 52.38 ? 321 GLU A OE2   1 
ATOM   2355 N N     . ALA A 1 331 ? 10.695 -17.953 12.230  1.00 43.19 ? 322 ALA A N     1 
ATOM   2356 C CA    . ALA A 1 331 ? 11.140 -16.615 12.611  1.00 38.82 ? 322 ALA A CA    1 
ATOM   2357 C C     . ALA A 1 331 ? 9.962  -15.733 13.005  1.00 40.67 ? 322 ALA A C     1 
ATOM   2358 O O     . ALA A 1 331 ? 10.050 -14.958 13.964  1.00 39.07 ? 322 ALA A O     1 
ATOM   2359 C CB    . ALA A 1 331 ? 11.932 -15.978 11.470  1.00 37.22 ? 322 ALA A CB    1 
ATOM   2360 N N     . VAL A 1 332 ? 8.846  -15.844 12.285  1.00 43.48 ? 323 VAL A N     1 
ATOM   2361 C CA    . VAL A 1 332 ? 7.672  -15.050 12.628  1.00 43.81 ? 323 VAL A CA    1 
ATOM   2362 C C     . VAL A 1 332 ? 6.895  -15.692 13.772  1.00 40.68 ? 323 VAL A C     1 
ATOM   2363 O O     . VAL A 1 332 ? 6.310  -14.986 14.602  1.00 38.87 ? 323 VAL A O     1 
ATOM   2364 C CB    . VAL A 1 332 ? 6.784  -14.851 11.387  1.00 42.32 ? 323 VAL A CB    1 
ATOM   2365 C CG1   . VAL A 1 332 ? 5.575  -13.989 11.722  1.00 43.52 ? 323 VAL A CG1   1 
ATOM   2366 C CG2   . VAL A 1 332 ? 7.587  -14.230 10.258  1.00 39.62 ? 323 VAL A CG2   1 
ATOM   2367 N N     . ALA A 1 333 ? 6.886  -17.025 13.845  1.00 40.26 ? 324 ALA A N     1 
ATOM   2368 C CA    . ALA A 1 333 ? 6.094  -17.712 14.860  1.00 44.16 ? 324 ALA A CA    1 
ATOM   2369 C C     . ALA A 1 333 ? 6.603  -17.406 16.264  1.00 46.22 ? 324 ALA A C     1 
ATOM   2370 O O     . ALA A 1 333 ? 5.823  -17.040 17.151  1.00 49.03 ? 324 ALA A O     1 
ATOM   2371 C CB    . ALA A 1 333 ? 6.102  -19.218 14.597  1.00 41.90 ? 324 ALA A CB    1 
ATOM   2372 N N     . GLN A 1 334 ? 7.907  -17.554 16.489  1.00 46.94 ? 325 GLN A N     1 
ATOM   2373 C CA    . GLN A 1 334 ? 8.484  -17.263 17.796  1.00 45.79 ? 325 GLN A CA    1 
ATOM   2374 C C     . GLN A 1 334 ? 8.715  -15.775 18.025  1.00 46.41 ? 325 GLN A C     1 
ATOM   2375 O O     . GLN A 1 334 ? 9.204  -15.398 19.095  1.00 40.41 ? 325 GLN A O     1 
ATOM   2376 C CB    . GLN A 1 334 ? 9.800  -18.026 17.980  1.00 45.32 ? 325 GLN A CB    1 
ATOM   2377 C CG    . GLN A 1 334 ? 9.948  -19.231 17.070  1.00 47.45 ? 325 GLN A CG    1 
ATOM   2378 C CD    . GLN A 1 334 ? 11.106 -20.130 17.454  1.00 61.99 ? 325 GLN A CD    1 
ATOM   2379 O OE1   . GLN A 1 334 ? 11.273 -20.484 18.621  1.00 73.29 ? 325 GLN A OE1   1 
ATOM   2380 N NE2   . GLN A 1 334 ? 11.924 -20.491 16.470  1.00 60.37 ? 325 GLN A NE2   1 
ATOM   2381 N N     . GLY A 1 335 ? 8.373  -14.925 17.059  1.00 48.53 ? 326 GLY A N     1 
ATOM   2382 C CA    . GLY A 1 335 ? 8.521  -13.495 17.237  1.00 47.03 ? 326 GLY A CA    1 
ATOM   2383 C C     . GLY A 1 335 ? 9.929  -12.974 17.092  1.00 43.44 ? 326 GLY A C     1 
ATOM   2384 O O     . GLY A 1 335 ? 10.228 -11.886 17.594  1.00 39.68 ? 326 GLY A O     1 
ATOM   2385 N N     . ASP A 1 336 ? 10.812 -13.719 16.423  1.00 36.55 ? 327 ASP A N     1 
ATOM   2386 C CA    . ASP A 1 336 ? 12.176 -13.249 16.219  1.00 33.99 ? 327 ASP A CA    1 
ATOM   2387 C C     . ASP A 1 336 ? 12.246 -12.110 15.212  1.00 38.70 ? 327 ASP A C     1 
ATOM   2388 O O     . ASP A 1 336 ? 13.226 -11.358 15.213  1.00 34.60 ? 327 ASP A O     1 
ATOM   2389 C CB    . ASP A 1 336 ? 13.071 -14.400 15.759  1.00 38.67 ? 327 ASP A CB    1 
ATOM   2390 C CG    . ASP A 1 336 ? 13.095 -15.554 16.744  1.00 44.86 ? 327 ASP A CG    1 
ATOM   2391 O OD1   . ASP A 1 336 ? 13.097 -15.297 17.967  1.00 42.97 ? 327 ASP A OD1   1 
ATOM   2392 O OD2   . ASP A 1 336 ? 13.118 -16.719 16.294  1.00 47.08 ? 327 ASP A OD2   1 
ATOM   2393 N N     . ALA A 1 337 ? 11.233 -11.966 14.360  1.00 38.23 ? 328 ALA A N     1 
ATOM   2394 C CA    . ALA A 1 337 ? 11.205 -10.910 13.359  1.00 35.52 ? 328 ALA A CA    1 
ATOM   2395 C C     . ALA A 1 337 ? 9.777  -10.747 12.860  1.00 31.73 ? 328 ALA A C     1 
ATOM   2396 O O     . ALA A 1 337 ? 8.942  -11.643 13.007  1.00 37.12 ? 328 ALA A O     1 
ATOM   2397 C CB    . ALA A 1 337 ? 12.152 -11.212 12.194  1.00 36.07 ? 328 ALA A CB    1 
ATOM   2398 N N     . ASP A 1 338 ? 9.508  -9.585  12.268  1.00 33.07 ? 329 ASP A N     1 
ATOM   2399 C CA    . ASP A 1 338 ? 8.198  -9.321  11.686  1.00 34.45 ? 329 ASP A CA    1 
ATOM   2400 C C     . ASP A 1 338 ? 8.148  -9.629  10.197  1.00 32.86 ? 329 ASP A C     1 
ATOM   2401 O O     . ASP A 1 338 ? 7.104  -10.067 9.698   1.00 37.90 ? 329 ASP A O     1 
ATOM   2402 C CB    . ASP A 1 338 ? 7.801  -7.863  11.922  1.00 34.64 ? 329 ASP A CB    1 
ATOM   2403 C CG    . ASP A 1 338 ? 7.909  -7.464  13.379  1.00 36.10 ? 329 ASP A CG    1 
ATOM   2404 O OD1   . ASP A 1 338 ? 7.115  -7.979  14.195  1.00 38.07 ? 329 ASP A OD1   1 
ATOM   2405 O OD2   . ASP A 1 338 ? 8.792  -6.646  13.708  1.00 38.13 ? 329 ASP A OD2   1 
ATOM   2406 N N     . LEU A 1 339 ? 9.247  -9.410  9.480   1.00 33.94 ? 330 LEU A N     1 
ATOM   2407 C CA    . LEU A 1 339 ? 9.334  -9.707  8.059   1.00 35.43 ? 330 LEU A CA    1 
ATOM   2408 C C     . LEU A 1 339 ? 10.619 -10.476 7.790   1.00 31.21 ? 330 LEU A C     1 
ATOM   2409 O O     . LEU A 1 339 ? 11.605 -10.342 8.519   1.00 35.06 ? 330 LEU A O     1 
ATOM   2410 C CB    . LEU A 1 339 ? 9.291  -8.425  7.211   1.00 30.19 ? 330 LEU A CB    1 
ATOM   2411 C CG    . LEU A 1 339 ? 8.111  -7.484  7.465   1.00 34.92 ? 330 LEU A CG    1 
ATOM   2412 C CD1   . LEU A 1 339 ? 8.403  -6.083  6.946   1.00 34.76 ? 330 LEU A CD1   1 
ATOM   2413 C CD2   . LEU A 1 339 ? 6.842  -8.030  6.840   1.00 33.02 ? 330 LEU A CD2   1 
ATOM   2414 N N     . VAL A 1 340 ? 10.599 -11.291 6.738   1.00 37.30 ? 331 VAL A N     1 
ATOM   2415 C CA    . VAL A 1 340 ? 11.726 -12.146 6.380   1.00 32.10 ? 331 VAL A CA    1 
ATOM   2416 C C     . VAL A 1 340 ? 12.051 -11.912 4.912   1.00 33.12 ? 331 VAL A C     1 
ATOM   2417 O O     . VAL A 1 340 ? 11.198 -12.125 4.043   1.00 32.99 ? 331 VAL A O     1 
ATOM   2418 C CB    . VAL A 1 340 ? 11.428 -13.633 6.639   1.00 36.04 ? 331 VAL A CB    1 
ATOM   2419 C CG1   . VAL A 1 340 ? 12.641 -14.489 6.291   1.00 35.82 ? 331 VAL A CG1   1 
ATOM   2420 C CG2   . VAL A 1 340 ? 11.017 -13.848 8.088   1.00 27.63 ? 331 VAL A CG2   1 
ATOM   2421 N N     . SER A 1 341 ? 13.278 -11.482 4.635   1.00 27.38 ? 332 SER A N     1 
ATOM   2422 C CA    . SER A 1 341 ? 13.701 -11.160 3.281   1.00 32.54 ? 332 SER A CA    1 
ATOM   2423 C C     . SER A 1 341 ? 14.555 -12.286 2.709   1.00 33.60 ? 332 SER A C     1 
ATOM   2424 O O     . SER A 1 341 ? 15.429 -12.827 3.392   1.00 35.97 ? 332 SER A O     1 
ATOM   2425 C CB    . SER A 1 341 ? 14.460 -9.831  3.254   1.00 25.61 ? 332 SER A CB    1 
ATOM   2426 O OG    . SER A 1 341 ? 15.836 -10.008 3.528   1.00 34.84 ? 332 SER A OG    1 
ATOM   2427 N N     . TYR A 1 342 ? 14.284 -12.643 1.453   1.00 32.78 ? 333 TYR A N     1 
ATOM   2428 C CA    . TYR A 1 342 ? 14.928 -13.765 0.783   1.00 29.44 ? 333 TYR A CA    1 
ATOM   2429 C C     . TYR A 1 342 ? 15.759 -13.252 -0.383  1.00 36.30 ? 333 TYR A C     1 
ATOM   2430 O O     . TYR A 1 342 ? 15.280 -12.446 -1.188  1.00 23.85 ? 333 TYR A O     1 
ATOM   2431 C CB    . TYR A 1 342 ? 13.893 -14.780 0.284   1.00 25.66 ? 333 TYR A CB    1 
ATOM   2432 C CG    . TYR A 1 342 ? 13.205 -15.548 1.391   1.00 38.54 ? 333 TYR A CG    1 
ATOM   2433 C CD1   . TYR A 1 342 ? 12.137 -14.995 2.089   1.00 33.60 ? 333 TYR A CD1   1 
ATOM   2434 C CD2   . TYR A 1 342 ? 13.625 -16.825 1.742   1.00 40.24 ? 333 TYR A CD2   1 
ATOM   2435 C CE1   . TYR A 1 342 ? 11.507 -15.693 3.102   1.00 36.68 ? 333 TYR A CE1   1 
ATOM   2436 C CE2   . TYR A 1 342 ? 13.002 -17.530 2.754   1.00 34.90 ? 333 TYR A CE2   1 
ATOM   2437 C CZ    . TYR A 1 342 ? 11.945 -16.961 3.431   1.00 39.63 ? 333 TYR A CZ    1 
ATOM   2438 O OH    . TYR A 1 342 ? 11.324 -17.663 4.439   1.00 37.03 ? 333 TYR A OH    1 
ATOM   2439 N N     . GLY A 1 343 ? 16.997 -13.728 -0.476  1.00 34.58 ? 334 GLY A N     1 
ATOM   2440 C CA    . GLY A 1 343 ? 17.948 -13.302 -1.478  1.00 38.56 ? 334 GLY A CA    1 
ATOM   2441 C C     . GLY A 1 343 ? 17.985 -14.290 -2.629  1.00 36.47 ? 334 GLY A C     1 
ATOM   2442 O O     . GLY A 1 343 ? 17.207 -14.177 -3.593  1.00 33.79 ? 334 GLY A O     1 
ATOM   2443 N N     . ARG A 1 344 ? 18.879 -15.279 -2.551  1.00 34.83 ? 335 ARG A N     1 
ATOM   2444 C CA    . ARG A 1 344 ? 19.174 -16.116 -3.711  1.00 37.74 ? 335 ARG A CA    1 
ATOM   2445 C C     . ARG A 1 344 ? 17.944 -16.876 -4.194  1.00 35.67 ? 335 ARG A C     1 
ATOM   2446 O O     . ARG A 1 344 ? 17.739 -17.027 -5.405  1.00 35.15 ? 335 ARG A O     1 
ATOM   2447 C CB    . ARG A 1 344 ? 20.311 -17.082 -3.378  1.00 32.64 ? 335 ARG A CB    1 
ATOM   2448 C CG    . ARG A 1 344 ? 21.669 -16.408 -3.272  1.00 37.22 ? 335 ARG A CG    1 
ATOM   2449 C CD    . ARG A 1 344 ? 22.665 -17.270 -2.518  1.00 38.27 ? 335 ARG A CD    1 
ATOM   2450 N NE    . ARG A 1 344 ? 22.422 -17.246 -1.081  1.00 37.59 ? 335 ARG A NE    1 
ATOM   2451 C CZ    . ARG A 1 344 ? 22.913 -18.129 -0.223  1.00 41.22 ? 335 ARG A CZ    1 
ATOM   2452 N NH1   . ARG A 1 344 ? 23.692 -19.121 -0.620  1.00 46.41 ? 335 ARG A NH1   1 
ATOM   2453 N NH2   . ARG A 1 344 ? 22.613 -18.014 1.068   1.00 40.19 ? 335 ARG A NH2   1 
ATOM   2454 N N     . LEU A 1 345 ? 17.112 -17.359 -3.268  1.00 28.19 ? 336 LEU A N     1 
ATOM   2455 C CA    . LEU A 1 345 ? 15.919 -18.102 -3.670  1.00 30.84 ? 336 LEU A CA    1 
ATOM   2456 C C     . LEU A 1 345 ? 14.969 -17.240 -4.494  1.00 40.46 ? 336 LEU A C     1 
ATOM   2457 O O     . LEU A 1 345 ? 14.219 -17.765 -5.326  1.00 29.34 ? 336 LEU A O     1 
ATOM   2458 C CB    . LEU A 1 345 ? 15.202 -18.658 -2.440  1.00 32.08 ? 336 LEU A CB    1 
ATOM   2459 C CG    . LEU A 1 345 ? 15.798 -19.933 -1.839  1.00 28.52 ? 336 LEU A CG    1 
ATOM   2460 C CD1   . LEU A 1 345 ? 15.128 -20.281 -0.515  1.00 37.61 ? 336 LEU A CD1   1 
ATOM   2461 C CD2   . LEU A 1 345 ? 15.687 -21.086 -2.822  1.00 36.74 ? 336 LEU A CD2   1 
ATOM   2462 N N     . PHE A 1 346 ? 14.986 -15.923 -4.284  1.00 33.70 ? 337 PHE A N     1 
ATOM   2463 C CA    . PHE A 1 346 ? 14.167 -15.024 -5.085  1.00 31.59 ? 337 PHE A CA    1 
ATOM   2464 C C     . PHE A 1 346 ? 14.752 -14.781 -6.469  1.00 33.48 ? 337 PHE A C     1 
ATOM   2465 O O     . PHE A 1 346 ? 14.026 -14.334 -7.364  1.00 32.89 ? 337 PHE A O     1 
ATOM   2466 C CB    . PHE A 1 346 ? 13.987 -13.688 -4.358  1.00 32.49 ? 337 PHE A CB    1 
ATOM   2467 C CG    . PHE A 1 346 ? 12.549 -13.302 -4.139  1.00 32.26 ? 337 PHE A CG    1 
ATOM   2468 C CD1   . PHE A 1 346 ? 11.619 -13.424 -5.159  1.00 32.26 ? 337 PHE A CD1   1 
ATOM   2469 C CD2   . PHE A 1 346 ? 12.130 -12.807 -2.914  1.00 30.88 ? 337 PHE A CD2   1 
ATOM   2470 C CE1   . PHE A 1 346 ? 10.298 -13.064 -4.960  1.00 35.82 ? 337 PHE A CE1   1 
ATOM   2471 C CE2   . PHE A 1 346 ? 10.810 -12.446 -2.708  1.00 33.53 ? 337 PHE A CE2   1 
ATOM   2472 C CZ    . PHE A 1 346 ? 9.893  -12.574 -3.730  1.00 35.91 ? 337 PHE A CZ    1 
ATOM   2473 N N     . ILE A 1 347 ? 16.044 -15.056 -6.663  1.00 34.21 ? 338 ILE A N     1 
ATOM   2474 C CA    . ILE A 1 347 ? 16.635 -14.950 -7.994  1.00 38.78 ? 338 ILE A CA    1 
ATOM   2475 C C     . ILE A 1 347 ? 16.079 -16.035 -8.906  1.00 35.24 ? 338 ILE A C     1 
ATOM   2476 O O     . ILE A 1 347 ? 15.701 -15.772 -10.054 1.00 32.28 ? 338 ILE A O     1 
ATOM   2477 C CB    . ILE A 1 347 ? 18.170 -15.026 -7.911  1.00 33.24 ? 338 ILE A CB    1 
ATOM   2478 C CG1   . ILE A 1 347 ? 18.746 -13.732 -7.349  1.00 35.42 ? 338 ILE A CG1   1 
ATOM   2479 C CG2   . ILE A 1 347 ? 18.771 -15.312 -9.279  1.00 33.50 ? 338 ILE A CG2   1 
ATOM   2480 C CD1   . ILE A 1 347 ? 20.239 -13.746 -7.303  1.00 32.88 ? 338 ILE A CD1   1 
ATOM   2481 N N     . SER A 1 348 ? 16.012 -17.267 -8.402  1.00 27.86 ? 339 SER A N     1 
ATOM   2482 C CA    . SER A 1 348 ? 15.620 -18.421 -9.198  1.00 32.42 ? 339 SER A CA    1 
ATOM   2483 C C     . SER A 1 348 ? 14.144 -18.768 -9.077  1.00 32.44 ? 339 SER A C     1 
ATOM   2484 O O     . SER A 1 348 ? 13.679 -19.669 -9.781  1.00 28.43 ? 339 SER A O     1 
ATOM   2485 C CB    . SER A 1 348 ? 16.452 -19.642 -8.799  1.00 35.81 ? 339 SER A CB    1 
ATOM   2486 O OG    . SER A 1 348 ? 16.351 -19.883 -7.408  1.00 34.06 ? 339 SER A OG    1 
ATOM   2487 N N     . ASN A 1 349 ? 13.404 -18.095 -8.200  1.00 27.79 ? 340 ASN A N     1 
ATOM   2488 C CA    . ASN A 1 349 ? 11.972 -18.333 -8.035  1.00 30.60 ? 340 ASN A CA    1 
ATOM   2489 C C     . ASN A 1 349 ? 11.268 -16.985 -8.076  1.00 35.05 ? 340 ASN A C     1 
ATOM   2490 O O     . ASN A 1 349 ? 11.113 -16.319 -7.042  1.00 30.85 ? 340 ASN A O     1 
ATOM   2491 C CB    . ASN A 1 349 ? 11.682 -19.088 -6.740  1.00 27.32 ? 340 ASN A CB    1 
ATOM   2492 C CG    . ASN A 1 349 ? 12.417 -20.414 -6.669  1.00 30.67 ? 340 ASN A CG    1 
ATOM   2493 O OD1   . ASN A 1 349 ? 11.904 -21.443 -7.106  1.00 29.37 ? 340 ASN A OD1   1 
ATOM   2494 N ND2   . ASN A 1 349 ? 13.629 -20.392 -6.124  1.00 31.92 ? 340 ASN A ND2   1 
ATOM   2495 N N     . PRO A 1 350 ? 10.844 -16.541 -9.263  1.00 37.85 ? 341 PRO A N     1 
ATOM   2496 C CA    . PRO A 1 350 ? 10.122 -15.260 -9.338  1.00 35.62 ? 341 PRO A CA    1 
ATOM   2497 C C     . PRO A 1 350 ? 8.809  -15.286 -8.580  1.00 38.69 ? 341 PRO A C     1 
ATOM   2498 O O     . PRO A 1 350 ? 8.434  -14.287 -7.954  1.00 39.17 ? 341 PRO A O     1 
ATOM   2499 C CB    . PRO A 1 350 ? 9.916  -15.063 -10.847 1.00 36.32 ? 341 PRO A CB    1 
ATOM   2500 C CG    . PRO A 1 350 ? 9.994  -16.443 -11.429 1.00 40.42 ? 341 PRO A CG    1 
ATOM   2501 C CD    . PRO A 1 350 ? 10.978 -17.191 -10.578 1.00 37.89 ? 341 PRO A CD    1 
ATOM   2502 N N     . ASP A 1 351 ? 8.099  -16.409 -8.612  1.00 31.02 ? 342 ASP A N     1 
ATOM   2503 C CA    . ASP A 1 351 ? 6.906  -16.596 -7.790  1.00 41.12 ? 342 ASP A CA    1 
ATOM   2504 C C     . ASP A 1 351 ? 7.234  -17.260 -6.458  1.00 35.20 ? 342 ASP A C     1 
ATOM   2505 O O     . ASP A 1 351 ? 6.537  -18.179 -6.023  1.00 40.65 ? 342 ASP A O     1 
ATOM   2506 C CB    . ASP A 1 351 ? 5.865  -17.401 -8.562  1.00 40.01 ? 342 ASP A CB    1 
ATOM   2507 C CG    . ASP A 1 351 ? 6.410  -18.722 -9.075  1.00 43.67 ? 342 ASP A CG    1 
ATOM   2508 O OD1   . ASP A 1 351 ? 7.647  -18.914 -9.057  1.00 37.48 ? 342 ASP A OD1   1 
ATOM   2509 O OD2   . ASP A 1 351 ? 5.596  -19.566 -9.509  1.00 44.76 ? 342 ASP A OD2   1 
ATOM   2510 N N     . LEU A 1 352 ? 8.299  -16.803 -5.791  1.00 37.08 ? 343 LEU A N     1 
ATOM   2511 C CA    . LEU A 1 352 ? 8.709  -17.409 -4.528  1.00 37.91 ? 343 LEU A CA    1 
ATOM   2512 C C     . LEU A 1 352 ? 7.638  -17.266 -3.456  1.00 38.41 ? 343 LEU A C     1 
ATOM   2513 O O     . LEU A 1 352 ? 7.474  -18.164 -2.621  1.00 38.82 ? 343 LEU A O     1 
ATOM   2514 C CB    . LEU A 1 352 ? 10.020 -16.787 -4.047  1.00 36.10 ? 343 LEU A CB    1 
ATOM   2515 C CG    . LEU A 1 352 ? 10.502 -17.219 -2.662  1.00 33.95 ? 343 LEU A CG    1 
ATOM   2516 C CD1   . LEU A 1 352 ? 10.924 -18.682 -2.681  1.00 33.05 ? 343 LEU A CD1   1 
ATOM   2517 C CD2   . LEU A 1 352 ? 11.638 -16.332 -2.190  1.00 36.04 ? 343 LEU A CD2   1 
ATOM   2518 N N     . VAL A 1 353 ? 6.906  -16.148 -3.455  1.00 38.39 ? 344 VAL A N     1 
ATOM   2519 C CA    . VAL A 1 353 ? 5.835  -15.960 -2.480  1.00 39.66 ? 344 VAL A CA    1 
ATOM   2520 C C     . VAL A 1 353 ? 4.771  -17.039 -2.648  1.00 40.75 ? 344 VAL A C     1 
ATOM   2521 O O     . VAL A 1 353 ? 4.354  -17.684 -1.679  1.00 38.73 ? 344 VAL A O     1 
ATOM   2522 C CB    . VAL A 1 353 ? 5.231  -14.550 -2.606  1.00 39.20 ? 344 VAL A CB    1 
ATOM   2523 C CG1   . VAL A 1 353 ? 4.224  -14.307 -1.495  1.00 38.06 ? 344 VAL A CG1   1 
ATOM   2524 C CG2   . VAL A 1 353 ? 6.326  -13.496 -2.580  1.00 34.66 ? 344 VAL A CG2   1 
ATOM   2525 N N     . MET A 1 354 ? 4.319  -17.254 -3.886  1.00 38.65 ? 345 MET A N     1 
ATOM   2526 C CA    . MET A 1 354 ? 3.319  -18.288 -4.136  1.00 42.61 ? 345 MET A CA    1 
ATOM   2527 C C     . MET A 1 354 ? 3.861  -19.674 -3.804  1.00 37.97 ? 345 MET A C     1 
ATOM   2528 O O     . MET A 1 354 ? 3.129  -20.527 -3.290  1.00 36.17 ? 345 MET A O     1 
ATOM   2529 C CB    . MET A 1 354 ? 2.854  -18.227 -5.591  1.00 45.92 ? 345 MET A CB    1 
ATOM   2530 C CG    . MET A 1 354 ? 1.717  -19.182 -5.923  1.00 50.04 ? 345 MET A CG    1 
ATOM   2531 S SD    . MET A 1 354 ? 0.105  -18.537 -5.438  1.00 75.86 ? 345 MET A SD    1 
ATOM   2532 C CE    . MET A 1 354 ? -0.980 -19.500 -6.491  1.00 65.79 ? 345 MET A CE    1 
ATOM   2533 N N     . ARG A 1 355 ? 5.146  -19.914 -4.081  1.00 33.85 ? 346 ARG A N     1 
ATOM   2534 C CA    . ARG A 1 355 ? 5.727  -21.223 -3.800  1.00 36.16 ? 346 ARG A CA    1 
ATOM   2535 C C     . ARG A 1 355 ? 5.829  -21.484 -2.303  1.00 40.56 ? 346 ARG A C     1 
ATOM   2536 O O     . ARG A 1 355 ? 5.709  -22.635 -1.868  1.00 34.71 ? 346 ARG A O     1 
ATOM   2537 C CB    . ARG A 1 355 ? 7.102  -21.341 -4.456  1.00 38.54 ? 346 ARG A CB    1 
ATOM   2538 C CG    . ARG A 1 355 ? 7.054  -21.432 -5.975  1.00 36.76 ? 346 ARG A CG    1 
ATOM   2539 C CD    . ARG A 1 355 ? 8.393  -21.858 -6.544  1.00 35.17 ? 346 ARG A CD    1 
ATOM   2540 N NE    . ARG A 1 355 ? 8.529  -21.500 -7.950  1.00 43.51 ? 346 ARG A NE    1 
ATOM   2541 C CZ    . ARG A 1 355 ? 8.934  -22.334 -8.898  1.00 44.96 ? 346 ARG A CZ    1 
ATOM   2542 N NH1   . ARG A 1 355 ? 9.232  -23.595 -8.628  1.00 40.04 ? 346 ARG A NH1   1 
ATOM   2543 N NH2   . ARG A 1 355 ? 9.047  -21.891 -10.147 1.00 39.10 ? 346 ARG A NH2   1 
ATOM   2544 N N     . ILE A 1 356 ? 6.048  -20.437 -1.505  1.00 38.51 ? 347 ILE A N     1 
ATOM   2545 C CA    . ILE A 1 356 ? 6.079  -20.607 -0.056  1.00 38.02 ? 347 ILE A CA    1 
ATOM   2546 C C     . ILE A 1 356 ? 4.678  -20.887 0.476   1.00 40.58 ? 347 ILE A C     1 
ATOM   2547 O O     . ILE A 1 356 ? 4.496  -21.710 1.382   1.00 43.02 ? 347 ILE A O     1 
ATOM   2548 C CB    . ILE A 1 356 ? 6.715  -19.370 0.608   1.00 38.84 ? 347 ILE A CB    1 
ATOM   2549 C CG1   . ILE A 1 356 ? 8.235  -19.392 0.423   1.00 40.49 ? 347 ILE A CG1   1 
ATOM   2550 C CG2   . ILE A 1 356 ? 6.362  -19.303 2.086   1.00 42.99 ? 347 ILE A CG2   1 
ATOM   2551 C CD1   . ILE A 1 356 ? 8.911  -18.054 0.669   1.00 35.16 ? 347 ILE A CD1   1 
ATOM   2552 N N     . LYS A 1 357 ? 3.666  -20.223 -0.089  1.00 42.63 ? 348 LYS A N     1 
ATOM   2553 C CA    . LYS A 1 357 ? 2.290  -20.441 0.347   1.00 38.93 ? 348 LYS A CA    1 
ATOM   2554 C C     . LYS A 1 357 ? 1.861  -21.884 0.117   1.00 41.48 ? 348 LYS A C     1 
ATOM   2555 O O     . LYS A 1 357 ? 1.371  -22.554 1.033   1.00 40.64 ? 348 LYS A O     1 
ATOM   2556 C CB    . LYS A 1 357 ? 1.351  -19.482 -0.387  1.00 41.85 ? 348 LYS A CB    1 
ATOM   2557 C CG    . LYS A 1 357 ? -0.066 -19.450 0.165   1.00 49.49 ? 348 LYS A CG    1 
ATOM   2558 C CD    . LYS A 1 357 ? -0.780 -18.162 -0.216  1.00 56.43 ? 348 LYS A CD    1 
ATOM   2559 C CE    . LYS A 1 357 ? -2.285 -18.288 -0.039  1.00 69.63 ? 348 LYS A CE    1 
ATOM   2560 N NZ    . LYS A 1 357 ? -3.035 -17.484 -1.047  1.00 73.56 ? 348 LYS A NZ    1 
ATOM   2561 N N     . LEU A 1 358 ? 2.044  -22.382 -1.105  1.00 40.96 ? 349 LEU A N     1 
ATOM   2562 C CA    . LEU A 1 358 ? 1.637  -23.734 -1.467  1.00 38.43 ? 349 LEU A CA    1 
ATOM   2563 C C     . LEU A 1 358 ? 2.636  -24.796 -1.032  1.00 39.89 ? 349 LEU A C     1 
ATOM   2564 O O     . LEU A 1 358 ? 2.356  -25.986 -1.211  1.00 46.60 ? 349 LEU A O     1 
ATOM   2565 C CB    . LEU A 1 358 ? 1.427  -23.831 -2.981  1.00 41.11 ? 349 LEU A CB    1 
ATOM   2566 C CG    . LEU A 1 358 ? 0.498  -22.801 -3.627  1.00 42.25 ? 349 LEU A CG    1 
ATOM   2567 C CD1   . LEU A 1 358 ? 0.679  -22.791 -5.138  1.00 41.99 ? 349 LEU A CD1   1 
ATOM   2568 C CD2   . LEU A 1 358 ? -0.948 -23.082 -3.262  1.00 47.60 ? 349 LEU A CD2   1 
ATOM   2569 N N     . ASN A 1 359 ? 3.780  -24.398 -0.469  1.00 40.90 ? 350 ASN A N     1 
ATOM   2570 C CA    . ASN A 1 359 ? 4.861  -25.323 -0.122  1.00 42.54 ? 350 ASN A CA    1 
ATOM   2571 C C     . ASN A 1 359 ? 5.325  -26.109 -1.347  1.00 44.36 ? 350 ASN A C     1 
ATOM   2572 O O     . ASN A 1 359 ? 5.636  -27.299 -1.267  1.00 41.14 ? 350 ASN A O     1 
ATOM   2573 C CB    . ASN A 1 359 ? 4.451  -26.266 1.013   1.00 42.72 ? 350 ASN A CB    1 
ATOM   2574 C CG    . ASN A 1 359 ? 5.645  -26.910 1.695   1.00 48.05 ? 350 ASN A CG    1 
ATOM   2575 O OD1   . ASN A 1 359 ? 6.770  -26.420 1.597   1.00 46.04 ? 350 ASN A OD1   1 
ATOM   2576 N ND2   . ASN A 1 359 ? 5.404  -28.019 2.385   1.00 48.78 ? 350 ASN A ND2   1 
ATOM   2577 N N     . ALA A 1 360 ? 5.368  -25.433 -2.497  1.00 42.12 ? 351 ALA A N     1 
ATOM   2578 C CA    . ALA A 1 360 ? 5.844  -26.042 -3.727  1.00 42.08 ? 351 ALA A CA    1 
ATOM   2579 C C     . ALA A 1 360 ? 7.372  -26.057 -3.757  1.00 43.50 ? 351 ALA A C     1 
ATOM   2580 O O     . ALA A 1 360 ? 8.018  -25.152 -3.221  1.00 41.69 ? 351 ALA A O     1 
ATOM   2581 C CB    . ALA A 1 360 ? 5.310  -25.284 -4.938  1.00 40.04 ? 351 ALA A CB    1 
ATOM   2582 N N     . PRO A 1 361 ? 7.969  -27.077 -4.374  1.00 44.18 ? 352 PRO A N     1 
ATOM   2583 C CA    . PRO A 1 361 ? 9.435  -27.154 -4.419  1.00 41.03 ? 352 PRO A CA    1 
ATOM   2584 C C     . PRO A 1 361 ? 10.038 -25.962 -5.147  1.00 41.36 ? 352 PRO A C     1 
ATOM   2585 O O     . PRO A 1 361 ? 9.498  -25.478 -6.143  1.00 41.20 ? 352 PRO A O     1 
ATOM   2586 C CB    . PRO A 1 361 ? 9.699  -28.464 -5.170  1.00 36.81 ? 352 PRO A CB    1 
ATOM   2587 C CG    . PRO A 1 361 ? 8.448  -29.263 -4.996  1.00 42.11 ? 352 PRO A CG    1 
ATOM   2588 C CD    . PRO A 1 361 ? 7.336  -28.258 -4.984  1.00 44.82 ? 352 PRO A CD    1 
ATOM   2589 N N     . LEU A 1 362 ? 11.172 -25.493 -4.637  1.00 39.43 ? 353 LEU A N     1 
ATOM   2590 C CA    . LEU A 1 362 ? 11.853 -24.340 -5.204  1.00 39.85 ? 353 LEU A CA    1 
ATOM   2591 C C     . LEU A 1 362 ? 12.891 -24.778 -6.228  1.00 39.76 ? 353 LEU A C     1 
ATOM   2592 O O     . LEU A 1 362 ? 13.414 -25.894 -6.176  1.00 33.57 ? 353 LEU A O     1 
ATOM   2593 C CB    . LEU A 1 362 ? 12.524 -23.519 -4.104  1.00 40.24 ? 353 LEU A CB    1 
ATOM   2594 C CG    . LEU A 1 362 ? 11.672 -23.272 -2.860  1.00 37.55 ? 353 LEU A CG    1 
ATOM   2595 C CD1   . LEU A 1 362 ? 12.470 -22.530 -1.806  1.00 36.49 ? 353 LEU A CD1   1 
ATOM   2596 C CD2   . LEU A 1 362 ? 10.411 -22.505 -3.223  1.00 35.54 ? 353 LEU A CD2   1 
ATOM   2597 N N     . ASN A 1 363 ? 13.188 -23.881 -7.161  1.00 35.30 ? 354 ASN A N     1 
ATOM   2598 C CA    . ASN A 1 363 ? 14.186 -24.143 -8.186  1.00 35.51 ? 354 ASN A CA    1 
ATOM   2599 C C     . ASN A 1 363 ? 15.549 -23.618 -7.753  1.00 39.09 ? 354 ASN A C     1 
ATOM   2600 O O     . ASN A 1 363 ? 15.654 -22.646 -6.998  1.00 35.83 ? 354 ASN A O     1 
ATOM   2601 C CB    . ASN A 1 363 ? 13.774 -23.508 -9.515  1.00 35.67 ? 354 ASN A CB    1 
ATOM   2602 C CG    . ASN A 1 363 ? 12.602 -24.221 -10.159 1.00 41.32 ? 354 ASN A CG    1 
ATOM   2603 O OD1   . ASN A 1 363 ? 12.098 -25.211 -9.628  1.00 37.20 ? 354 ASN A OD1   1 
ATOM   2604 N ND2   . ASN A 1 363 ? 12.160 -23.719 -11.306 1.00 39.25 ? 354 ASN A ND2   1 
ATOM   2605 N N     . LYS A 1 364 ? 16.597 -24.279 -8.236  1.00 32.78 ? 355 LYS A N     1 
ATOM   2606 C CA    . LYS A 1 364 ? 17.962 -23.902 -7.907  1.00 31.24 ? 355 LYS A CA    1 
ATOM   2607 C C     . LYS A 1 364 ? 18.384 -22.663 -8.691  1.00 33.34 ? 355 LYS A C     1 
ATOM   2608 O O     . LYS A 1 364 ? 17.854 -22.362 -9.764  1.00 34.72 ? 355 LYS A O     1 
ATOM   2609 C CB    . LYS A 1 364 ? 18.921 -25.055 -8.201  1.00 33.20 ? 355 LYS A CB    1 
ATOM   2610 C CG    . LYS A 1 364 ? 19.077 -25.359 -9.684  1.00 33.34 ? 355 LYS A CG    1 
ATOM   2611 C CD    . LYS A 1 364 ? 19.466 -26.809 -9.912  1.00 41.38 ? 355 LYS A CD    1 
ATOM   2612 C CE    . LYS A 1 364 ? 20.264 -26.971 -11.194 1.00 50.78 ? 355 LYS A CE    1 
ATOM   2613 N NZ    . LYS A 1 364 ? 19.401 -27.402 -12.330 1.00 52.40 ? 355 LYS A NZ    1 
ATOM   2614 N N     . TYR A 1 365 ? 19.358 -21.943 -8.141  1.00 34.40 ? 356 TYR A N     1 
ATOM   2615 C CA    . TYR A 1 365 ? 19.883 -20.732 -8.754  1.00 37.18 ? 356 TYR A CA    1 
ATOM   2616 C C     . TYR A 1 365 ? 21.268 -20.990 -9.333  1.00 32.64 ? 356 TYR A C     1 
ATOM   2617 O O     . TYR A 1 365 ? 22.029 -21.820 -8.828  1.00 36.35 ? 356 TYR A O     1 
ATOM   2618 C CB    . TYR A 1 365 ? 19.948 -19.579 -7.744  1.00 32.32 ? 356 TYR A CB    1 
ATOM   2619 C CG    . TYR A 1 365 ? 20.310 -20.002 -6.338  1.00 35.55 ? 356 TYR A CG    1 
ATOM   2620 C CD1   . TYR A 1 365 ? 21.633 -20.223 -5.978  1.00 39.67 ? 356 TYR A CD1   1 
ATOM   2621 C CD2   . TYR A 1 365 ? 19.330 -20.178 -5.372  1.00 30.73 ? 356 TYR A CD2   1 
ATOM   2622 C CE1   . TYR A 1 365 ? 21.968 -20.609 -4.696  1.00 36.21 ? 356 TYR A CE1   1 
ATOM   2623 C CE2   . TYR A 1 365 ? 19.656 -20.563 -4.087  1.00 36.16 ? 356 TYR A CE2   1 
ATOM   2624 C CZ    . TYR A 1 365 ? 20.976 -20.776 -3.755  1.00 37.31 ? 356 TYR A CZ    1 
ATOM   2625 O OH    . TYR A 1 365 ? 21.305 -21.159 -2.476  1.00 47.34 ? 356 TYR A OH    1 
ATOM   2626 N N     . ASN A 1 366 ? 21.583 -20.267 -10.405 1.00 34.30 ? 357 ASN A N     1 
ATOM   2627 C CA    . ASN A 1 366 ? 22.868 -20.377 -11.085 1.00 33.16 ? 357 ASN A CA    1 
ATOM   2628 C C     . ASN A 1 366 ? 23.727 -19.180 -10.691 1.00 33.44 ? 357 ASN A C     1 
ATOM   2629 O O     . ASN A 1 366 ? 23.473 -18.053 -11.130 1.00 35.23 ? 357 ASN A O     1 
ATOM   2630 C CB    . ASN A 1 366 ? 22.675 -20.447 -12.599 1.00 38.27 ? 357 ASN A CB    1 
ATOM   2631 C CG    . ASN A 1 366 ? 23.980 -20.314 -13.360 1.00 40.24 ? 357 ASN A CG    1 
ATOM   2632 O OD1   . ASN A 1 366 ? 24.051 -19.614 -14.370 1.00 54.31 ? 357 ASN A OD1   1 
ATOM   2633 N ND2   . ASN A 1 366 ? 25.019 -20.990 -12.881 1.00 45.59 ? 357 ASN A ND2   1 
ATOM   2634 N N     . ARG A 1 367 ? 24.749 -19.434 -9.869  1.00 32.36 ? 358 ARG A N     1 
ATOM   2635 C CA    . ARG A 1 367 ? 25.605 -18.362 -9.372  1.00 37.43 ? 358 ARG A CA    1 
ATOM   2636 C C     . ARG A 1 367 ? 26.384 -17.685 -10.497 1.00 38.41 ? 358 ARG A C     1 
ATOM   2637 O O     . ARG A 1 367 ? 26.734 -16.503 -10.388 1.00 32.86 ? 358 ARG A O     1 
ATOM   2638 C CB    . ARG A 1 367 ? 26.552 -18.927 -8.308  1.00 41.18 ? 358 ARG A CB    1 
ATOM   2639 C CG    . ARG A 1 367 ? 27.802 -18.106 -8.040  1.00 45.57 ? 358 ARG A CG    1 
ATOM   2640 C CD    . ARG A 1 367 ? 27.541 -17.036 -7.001  1.00 51.27 ? 358 ARG A CD    1 
ATOM   2641 N NE    . ARG A 1 367 ? 27.007 -17.599 -5.767  1.00 55.47 ? 358 ARG A NE    1 
ATOM   2642 C CZ    . ARG A 1 367 ? 26.827 -16.910 -4.648  1.00 52.73 ? 358 ARG A CZ    1 
ATOM   2643 N NH1   . ARG A 1 367 ? 27.126 -15.623 -4.574  1.00 52.50 ? 358 ARG A NH1   1 
ATOM   2644 N NH2   . ARG A 1 367 ? 26.331 -17.526 -3.579  1.00 54.79 ? 358 ARG A NH2   1 
ATOM   2645 N N     . LYS A 1 368 ? 26.639 -18.404 -11.594 1.00 38.12 ? 359 LYS A N     1 
ATOM   2646 C CA    . LYS A 1 368 ? 27.462 -17.856 -12.668 1.00 31.47 ? 359 LYS A CA    1 
ATOM   2647 C C     . LYS A 1 368 ? 26.810 -16.647 -13.331 1.00 31.14 ? 359 LYS A C     1 
ATOM   2648 O O     . LYS A 1 368 ? 27.513 -15.779 -13.862 1.00 34.29 ? 359 LYS A O     1 
ATOM   2649 C CB    . LYS A 1 368 ? 27.753 -18.939 -13.707 1.00 35.43 ? 359 LYS A CB    1 
ATOM   2650 N N     . THR A 1 369 ? 25.480 -16.565 -13.309 1.00 29.30 ? 360 THR A N     1 
ATOM   2651 C CA    . THR A 1 369 ? 24.752 -15.468 -13.931 1.00 28.95 ? 360 THR A CA    1 
ATOM   2652 C C     . THR A 1 369 ? 24.219 -14.461 -12.914 1.00 36.37 ? 360 THR A C     1 
ATOM   2653 O O     . THR A 1 369 ? 23.298 -13.700 -13.229 1.00 31.90 ? 360 THR A O     1 
ATOM   2654 C CB    . THR A 1 369 ? 23.605 -16.012 -14.783 1.00 34.62 ? 360 THR A CB    1 
ATOM   2655 O OG1   . THR A 1 369 ? 22.855 -16.966 -14.020 1.00 37.80 ? 360 THR A OG1   1 
ATOM   2656 C CG2   . THR A 1 369 ? 24.147 -16.687 -16.038 1.00 32.12 ? 360 THR A CG2   1 
ATOM   2657 N N     . PHE A 1 370 ? 24.777 -14.442 -11.701 1.00 32.02 ? 361 PHE A N     1 
ATOM   2658 C CA    . PHE A 1 370 ? 24.362 -13.450 -10.713 1.00 35.97 ? 361 PHE A CA    1 
ATOM   2659 C C     . PHE A 1 370 ? 24.738 -12.040 -11.160 1.00 36.56 ? 361 PHE A C     1 
ATOM   2660 O O     . PHE A 1 370 ? 23.904 -11.128 -11.138 1.00 36.64 ? 361 PHE A O     1 
ATOM   2661 C CB    . PHE A 1 370 ? 24.991 -13.760 -9.353  1.00 30.46 ? 361 PHE A CB    1 
ATOM   2662 C CG    . PHE A 1 370 ? 24.242 -14.786 -8.546  1.00 32.19 ? 361 PHE A CG    1 
ATOM   2663 C CD1   . PHE A 1 370 ? 23.204 -15.512 -9.105  1.00 37.99 ? 361 PHE A CD1   1 
ATOM   2664 C CD2   . PHE A 1 370 ? 24.584 -15.026 -7.225  1.00 38.52 ? 361 PHE A CD2   1 
ATOM   2665 C CE1   . PHE A 1 370 ? 22.518 -16.457 -8.362  1.00 37.70 ? 361 PHE A CE1   1 
ATOM   2666 C CE2   . PHE A 1 370 ? 23.902 -15.969 -6.475  1.00 36.83 ? 361 PHE A CE2   1 
ATOM   2667 C CZ    . PHE A 1 370 ? 22.868 -16.685 -7.044  1.00 39.50 ? 361 PHE A CZ    1 
ATOM   2668 N N     . TYR A 1 371 ? 25.990 -11.847 -11.583 1.00 28.20 ? 362 TYR A N     1 
ATOM   2669 C CA    . TYR A 1 371 ? 26.541 -10.522 -11.845 1.00 31.18 ? 362 TYR A CA    1 
ATOM   2670 C C     . TYR A 1 371 ? 26.795 -10.260 -13.328 1.00 34.86 ? 362 TYR A C     1 
ATOM   2671 O O     . TYR A 1 371 ? 27.529 -9.327  -13.669 1.00 38.92 ? 362 TYR A O     1 
ATOM   2672 C CB    . TYR A 1 371 ? 27.836 -10.331 -11.056 1.00 30.42 ? 362 TYR A CB    1 
ATOM   2673 C CG    . TYR A 1 371 ? 27.689 -10.541 -9.566  1.00 35.43 ? 362 TYR A CG    1 
ATOM   2674 C CD1   . TYR A 1 371 ? 26.983 -9.637  -8.785  1.00 35.52 ? 362 TYR A CD1   1 
ATOM   2675 C CD2   . TYR A 1 371 ? 28.263 -11.639 -8.940  1.00 35.96 ? 362 TYR A CD2   1 
ATOM   2676 C CE1   . TYR A 1 371 ? 26.849 -9.821  -7.422  1.00 33.54 ? 362 TYR A CE1   1 
ATOM   2677 C CE2   . TYR A 1 371 ? 28.135 -11.832 -7.578  1.00 40.35 ? 362 TYR A CE2   1 
ATOM   2678 C CZ    . TYR A 1 371 ? 27.428 -10.919 -6.824  1.00 38.72 ? 362 TYR A CZ    1 
ATOM   2679 O OH    . TYR A 1 371 ? 27.298 -11.105 -5.467  1.00 38.69 ? 362 TYR A OH    1 
ATOM   2680 N N     . THR A 1 372 ? 26.208 -11.054 -14.217 1.00 31.35 ? 363 THR A N     1 
ATOM   2681 C CA    . THR A 1 372 ? 26.428 -10.857 -15.641 1.00 39.83 ? 363 THR A CA    1 
ATOM   2682 C C     . THR A 1 372 ? 25.532 -9.739  -16.173 1.00 37.42 ? 363 THR A C     1 
ATOM   2683 O O     . THR A 1 372 ? 24.663 -9.211  -15.475 1.00 32.12 ? 363 THR A O     1 
ATOM   2684 C CB    . THR A 1 372 ? 26.179 -12.154 -16.406 1.00 34.61 ? 363 THR A CB    1 
ATOM   2685 O OG1   . THR A 1 372 ? 24.945 -12.738 -15.969 1.00 35.50 ? 363 THR A OG1   1 
ATOM   2686 C CG2   . THR A 1 372 ? 27.313 -13.140 -16.158 1.00 40.20 ? 363 THR A CG2   1 
ATOM   2687 N N     . GLN A 1 373 ? 25.751 -9.380  -17.437 1.00 40.91 ? 364 GLN A N     1 
ATOM   2688 C CA    . GLN A 1 373 ? 25.083 -8.238  -18.047 1.00 38.77 ? 364 GLN A CA    1 
ATOM   2689 C C     . GLN A 1 373 ? 23.935 -8.631  -18.965 1.00 38.34 ? 364 GLN A C     1 
ATOM   2690 O O     . GLN A 1 373 ? 23.263 -7.745  -19.501 1.00 32.49 ? 364 GLN A O     1 
ATOM   2691 C CB    . GLN A 1 373 ? 26.093 -7.393  -18.831 1.00 31.52 ? 364 GLN A CB    1 
ATOM   2692 C CG    . GLN A 1 373 ? 26.924 -6.460  -17.971 1.00 34.21 ? 364 GLN A CG    1 
ATOM   2693 C CD    . GLN A 1 373 ? 27.859 -7.204  -17.039 1.00 37.86 ? 364 GLN A CD    1 
ATOM   2694 O OE1   . GLN A 1 373 ? 28.824 -7.830  -17.477 1.00 35.09 ? 364 GLN A OE1   1 
ATOM   2695 N NE2   . GLN A 1 373 ? 27.574 -7.142  -15.742 1.00 39.96 ? 364 GLN A NE2   1 
ATOM   2696 N N     . ASP A 1 374 ? 23.696 -9.919  -19.162 1.00 41.36 ? 365 ASP A N     1 
ATOM   2697 C CA    . ASP A 1 374 ? 22.648 -10.337 -20.085 1.00 39.43 ? 365 ASP A CA    1 
ATOM   2698 C C     . ASP A 1 374 ? 21.281 -9.969  -19.516 1.00 39.22 ? 365 ASP A C     1 
ATOM   2699 O O     . ASP A 1 374 ? 20.995 -10.272 -18.351 1.00 39.06 ? 365 ASP A O     1 
ATOM   2700 C CB    . ASP A 1 374 ? 22.730 -11.838 -20.348 1.00 34.58 ? 365 ASP A CB    1 
ATOM   2701 C CG    . ASP A 1 374 ? 21.886 -12.266 -21.531 1.00 47.79 ? 365 ASP A CG    1 
ATOM   2702 O OD1   . ASP A 1 374 ? 20.655 -12.385 -21.368 1.00 47.11 ? 365 ASP A OD1   1 
ATOM   2703 O OD2   . ASP A 1 374 ? 22.451 -12.478 -22.624 1.00 53.12 ? 365 ASP A OD2   1 
ATOM   2704 N N     . PRO A 1 375 ? 20.412 -9.323  -20.299 1.00 38.49 ? 366 PRO A N     1 
ATOM   2705 C CA    . PRO A 1 375 ? 19.125 -8.865  -19.759 1.00 36.84 ? 366 PRO A CA    1 
ATOM   2706 C C     . PRO A 1 375 ? 18.091 -9.963  -19.575 1.00 40.55 ? 366 PRO A C     1 
ATOM   2707 O O     . PRO A 1 375 ? 17.020 -9.683  -19.019 1.00 41.58 ? 366 PRO A O     1 
ATOM   2708 C CB    . PRO A 1 375 ? 18.657 -7.846  -20.806 1.00 35.22 ? 366 PRO A CB    1 
ATOM   2709 C CG    . PRO A 1 375 ? 19.262 -8.334  -22.083 1.00 37.88 ? 366 PRO A CG    1 
ATOM   2710 C CD    . PRO A 1 375 ? 20.580 -8.970  -21.721 1.00 36.49 ? 366 PRO A CD    1 
ATOM   2711 N N     . VAL A 1 376 ? 18.356 -11.192 -20.019 1.00 43.30 ? 367 VAL A N     1 
ATOM   2712 C CA    . VAL A 1 376 ? 17.373 -12.261 -19.874 1.00 43.59 ? 367 VAL A CA    1 
ATOM   2713 C C     . VAL A 1 376 ? 18.009 -13.507 -19.270 1.00 41.40 ? 367 VAL A C     1 
ATOM   2714 O O     . VAL A 1 376 ? 17.410 -14.164 -18.412 1.00 40.86 ? 367 VAL A O     1 
ATOM   2715 C CB    . VAL A 1 376 ? 16.695 -12.585 -21.219 1.00 47.85 ? 367 VAL A CB    1 
ATOM   2716 C CG1   . VAL A 1 376 ? 15.585 -11.582 -21.508 1.00 44.03 ? 367 VAL A CG1   1 
ATOM   2717 C CG2   . VAL A 1 376 ? 17.710 -12.591 -22.351 1.00 53.26 ? 367 VAL A CG2   1 
ATOM   2718 N N     . VAL A 1 377 ? 19.225 -13.839 -19.701 1.00 41.91 ? 368 VAL A N     1 
ATOM   2719 C CA    . VAL A 1 377 ? 19.860 -15.084 -19.278 1.00 39.26 ? 368 VAL A CA    1 
ATOM   2720 C C     . VAL A 1 377 ? 20.271 -14.971 -17.814 1.00 40.56 ? 368 VAL A C     1 
ATOM   2721 O O     . VAL A 1 377 ? 21.063 -14.099 -17.439 1.00 38.73 ? 368 VAL A O     1 
ATOM   2722 C CB    . VAL A 1 377 ? 21.062 -15.418 -20.170 1.00 42.23 ? 368 VAL A CB    1 
ATOM   2723 C CG1   . VAL A 1 377 ? 21.834 -16.601 -19.599 1.00 39.38 ? 368 VAL A CG1   1 
ATOM   2724 C CG2   . VAL A 1 377 ? 20.598 -15.712 -21.589 1.00 40.09 ? 368 VAL A CG2   1 
ATOM   2725 N N     . GLY A 1 378 ? 19.741 -15.866 -16.982 1.00 34.19 ? 369 GLY A N     1 
ATOM   2726 C CA    . GLY A 1 378 ? 19.998 -15.812 -15.556 1.00 40.13 ? 369 GLY A CA    1 
ATOM   2727 C C     . GLY A 1 378 ? 19.371 -14.639 -14.842 1.00 31.93 ? 369 GLY A C     1 
ATOM   2728 O O     . GLY A 1 378 ? 19.720 -14.376 -13.687 1.00 37.19 ? 369 GLY A O     1 
ATOM   2729 N N     . TYR A 1 379 ? 18.454 -13.926 -15.494 1.00 37.36 ? 370 TYR A N     1 
ATOM   2730 C CA    . TYR A 1 379 ? 17.816 -12.747 -14.919 1.00 38.24 ? 370 TYR A CA    1 
ATOM   2731 C C     . TYR A 1 379 ? 16.299 -12.873 -14.916 1.00 41.08 ? 370 TYR A C     1 
ATOM   2732 O O     . TYR A 1 379 ? 15.683 -12.842 -13.845 1.00 38.01 ? 370 TYR A O     1 
ATOM   2733 C CB    . TYR A 1 379 ? 18.255 -11.493 -15.688 1.00 32.77 ? 370 TYR A CB    1 
ATOM   2734 C CG    . TYR A 1 379 ? 18.032 -10.198 -14.944 1.00 36.12 ? 370 TYR A CG    1 
ATOM   2735 C CD1   . TYR A 1 379 ? 18.562 -10.002 -13.675 1.00 39.38 ? 370 TYR A CD1   1 
ATOM   2736 C CD2   . TYR A 1 379 ? 17.292 -9.167  -15.511 1.00 37.31 ? 370 TYR A CD2   1 
ATOM   2737 C CE1   . TYR A 1 379 ? 18.361 -8.817  -12.989 1.00 36.02 ? 370 TYR A CE1   1 
ATOM   2738 C CE2   . TYR A 1 379 ? 17.087 -7.976  -14.833 1.00 36.12 ? 370 TYR A CE2   1 
ATOM   2739 C CZ    . TYR A 1 379 ? 17.623 -7.808  -13.572 1.00 32.71 ? 370 TYR A CZ    1 
ATOM   2740 O OH    . TYR A 1 379 ? 17.421 -6.629  -12.893 1.00 34.56 ? 370 TYR A OH    1 
ATOM   2741 N N     . THR A 1 380 ? 15.677 -13.023 -16.086 1.00 30.83 ? 371 THR A N     1 
ATOM   2742 C CA    . THR A 1 380 ? 14.229 -13.121 -16.189 1.00 36.71 ? 371 THR A CA    1 
ATOM   2743 C C     . THR A 1 380 ? 13.752 -14.424 -16.815 1.00 34.61 ? 371 THR A C     1 
ATOM   2744 O O     . THR A 1 380 ? 12.546 -14.578 -17.039 1.00 36.42 ? 371 THR A O     1 
ATOM   2745 C CB    . THR A 1 380 ? 13.667 -11.945 -16.999 1.00 45.36 ? 371 THR A CB    1 
ATOM   2746 O OG1   . THR A 1 380 ? 14.279 -11.923 -18.294 1.00 47.79 ? 371 THR A OG1   1 
ATOM   2747 C CG2   . THR A 1 380 ? 13.939 -10.625 -16.288 1.00 41.26 ? 371 THR A CG2   1 
ATOM   2748 N N     . ASP A 1 381 ? 14.650 -15.363 -17.108 1.00 37.73 ? 372 ASP A N     1 
ATOM   2749 C CA    . ASP A 1 381 ? 14.267 -16.613 -17.748 1.00 38.97 ? 372 ASP A CA    1 
ATOM   2750 C C     . ASP A 1 381 ? 14.096 -17.757 -16.757 1.00 38.99 ? 372 ASP A C     1 
ATOM   2751 O O     . ASP A 1 381 ? 14.055 -18.920 -17.171 1.00 36.93 ? 372 ASP A O     1 
ATOM   2752 C CB    . ASP A 1 381 ? 15.283 -16.991 -18.831 1.00 32.66 ? 372 ASP A CB    1 
ATOM   2753 C CG    . ASP A 1 381 ? 16.692 -17.158 -18.290 1.00 38.93 ? 372 ASP A CG    1 
ATOM   2754 O OD1   . ASP A 1 381 ? 16.932 -16.831 -17.109 1.00 41.36 ? 372 ASP A OD1   1 
ATOM   2755 O OD2   . ASP A 1 381 ? 17.564 -17.617 -19.056 1.00 43.45 ? 372 ASP A OD2   1 
ATOM   2756 N N     . TYR A 1 382 ? 14.002 -17.460 -15.464 1.00 35.39 ? 373 TYR A N     1 
ATOM   2757 C CA    . TYR A 1 382 ? 13.632 -18.476 -14.485 1.00 35.79 ? 373 TYR A CA    1 
ATOM   2758 C C     . TYR A 1 382 ? 12.124 -18.688 -14.537 1.00 40.16 ? 373 TYR A C     1 
ATOM   2759 O O     . TYR A 1 382 ? 11.369 -17.726 -14.356 1.00 45.72 ? 373 TYR A O     1 
ATOM   2760 C CB    . TYR A 1 382 ? 14.049 -18.058 -13.081 1.00 37.37 ? 373 TYR A CB    1 
ATOM   2761 C CG    . TYR A 1 382 ? 15.529 -18.175 -12.790 1.00 33.38 ? 373 TYR A CG    1 
ATOM   2762 C CD1   . TYR A 1 382 ? 16.109 -19.406 -12.506 1.00 36.93 ? 373 TYR A CD1   1 
ATOM   2763 C CD2   . TYR A 1 382 ? 16.341 -17.051 -12.779 1.00 32.86 ? 373 TYR A CD2   1 
ATOM   2764 C CE1   . TYR A 1 382 ? 17.463 -19.510 -12.225 1.00 33.36 ? 373 TYR A CE1   1 
ATOM   2765 C CE2   . TYR A 1 382 ? 17.690 -17.144 -12.500 1.00 27.33 ? 373 TYR A CE2   1 
ATOM   2766 C CZ    . TYR A 1 382 ? 18.246 -18.373 -12.225 1.00 32.13 ? 373 TYR A CZ    1 
ATOM   2767 O OH    . TYR A 1 382 ? 19.591 -18.458 -11.947 1.00 34.60 ? 373 TYR A OH    1 
ATOM   2768 N N     . PRO A 1 383 ? 11.646 -19.904 -14.779 1.00 43.07 ? 374 PRO A N     1 
ATOM   2769 C CA    . PRO A 1 383 ? 10.211 -20.100 -15.012 1.00 34.64 ? 374 PRO A CA    1 
ATOM   2770 C C     . PRO A 1 383 ? 9.387  -19.974 -13.741 1.00 44.41 ? 374 PRO A C     1 
ATOM   2771 O O     . PRO A 1 383 ? 9.871  -20.142 -12.619 1.00 44.67 ? 374 PRO A O     1 
ATOM   2772 C CB    . PRO A 1 383 ? 10.135 -21.522 -15.577 1.00 39.26 ? 374 PRO A CB    1 
ATOM   2773 C CG    . PRO A 1 383 ? 11.363 -22.196 -15.064 1.00 42.34 ? 374 PRO A CG    1 
ATOM   2774 C CD    . PRO A 1 383 ? 12.421 -21.134 -15.018 1.00 42.84 ? 374 PRO A CD    1 
ATOM   2775 N N     . PHE A 1 384 ? 8.107  -19.674 -13.943 1.00 44.37 ? 375 PHE A N     1 
ATOM   2776 C CA    . PHE A 1 384 ? 7.127  -19.677 -12.866 1.00 44.97 ? 375 PHE A CA    1 
ATOM   2777 C C     . PHE A 1 384 ? 6.667  -21.111 -12.613 1.00 52.34 ? 375 PHE A C     1 
ATOM   2778 O O     . PHE A 1 384 ? 7.216  -22.077 -13.151 1.00 50.35 ? 375 PHE A O     1 
ATOM   2779 C CB    . PHE A 1 384 ? 5.949  -18.770 -13.212 1.00 42.54 ? 375 PHE A CB    1 
ATOM   2780 C CG    . PHE A 1 384 ? 6.264  -17.304 -13.152 1.00 45.64 ? 375 PHE A CG    1 
ATOM   2781 C CD1   . PHE A 1 384 ? 6.851  -16.663 -14.232 1.00 43.98 ? 375 PHE A CD1   1 
ATOM   2782 C CD2   . PHE A 1 384 ? 5.958  -16.562 -12.024 1.00 39.39 ? 375 PHE A CD2   1 
ATOM   2783 C CE1   . PHE A 1 384 ? 7.137  -15.311 -14.182 1.00 36.51 ? 375 PHE A CE1   1 
ATOM   2784 C CE2   . PHE A 1 384 ? 6.242  -15.209 -11.968 1.00 40.74 ? 375 PHE A CE2   1 
ATOM   2785 C CZ    . PHE A 1 384 ? 6.831  -14.583 -13.049 1.00 39.85 ? 375 PHE A CZ    1 
ATOM   2786 N N     . LEU A 1 385 ? 5.638  -21.263 -11.785 1.00 55.27 ? 376 LEU A N     1 
ATOM   2787 C CA    . LEU A 1 385 ? 5.014  -22.560 -11.577 1.00 56.70 ? 376 LEU A CA    1 
ATOM   2788 C C     . LEU A 1 385 ? 4.103  -22.891 -12.753 1.00 55.32 ? 376 LEU A C     1 
ATOM   2789 O O     . LEU A 1 385 ? 3.436  -22.012 -13.306 1.00 58.42 ? 376 LEU A O     1 
ATOM   2790 C CB    . LEU A 1 385 ? 4.217  -22.562 -10.273 1.00 54.86 ? 376 LEU A CB    1 
ATOM   2791 C CG    . LEU A 1 385 ? 4.427  -23.740 -9.319  1.00 61.21 ? 376 LEU A CG    1 
ATOM   2792 C CD1   . LEU A 1 385 ? 5.899  -24.108 -9.221  1.00 48.82 ? 376 LEU A CD1   1 
ATOM   2793 C CD2   . LEU A 1 385 ? 3.861  -23.412 -7.945  1.00 56.02 ? 376 LEU A CD2   1 
ATOM   2794 N N     . GLN A 1 386 ? 4.083  -24.162 -13.136 1.00 59.95 ? 377 GLN A N     1 
ATOM   2795 C CA    . GLN A 1 386 ? 3.251  -24.605 -14.249 1.00 58.56 ? 377 GLN A CA    1 
ATOM   2796 C C     . GLN A 1 386 ? 1.840  -24.941 -13.778 1.00 61.58 ? 377 GLN A C     1 
ATOM   2797 O O     . GLN A 1 386 ? 1.658  -25.598 -12.753 1.00 61.54 ? 377 GLN A O     1 
ATOM   2798 C CB    . GLN A 1 386 ? 3.878  -25.817 -14.942 1.00 61.32 ? 377 GLN A CB    1 
ATOM   2799 N N     . ASN B 1 19  ? 54.176 10.986  -27.933 1.00 50.23 ? 10  ASN B N     1 
ATOM   2800 C CA    . ASN B 1 19  ? 53.075 10.473  -28.741 1.00 46.74 ? 10  ASN B CA    1 
ATOM   2801 C C     . ASN B 1 19  ? 52.726 9.047   -28.336 1.00 49.10 ? 10  ASN B C     1 
ATOM   2802 O O     . ASN B 1 19  ? 53.514 8.125   -28.552 1.00 49.53 ? 10  ASN B O     1 
ATOM   2803 C CB    . ASN B 1 19  ? 53.426 10.525  -30.230 1.00 44.14 ? 10  ASN B CB    1 
ATOM   2804 C CG    . ASN B 1 19  ? 52.197 10.506  -31.123 1.00 46.18 ? 10  ASN B CG    1 
ATOM   2805 O OD1   . ASN B 1 19  ? 51.186 9.879   -30.799 1.00 40.32 ? 10  ASN B OD1   1 
ATOM   2806 N ND2   . ASN B 1 19  ? 52.281 11.192  -32.259 1.00 49.48 ? 10  ASN B ND2   1 
ATOM   2807 N N     . PRO B 1 20  ? 51.537 8.863   -27.756 1.00 44.01 ? 11  PRO B N     1 
ATOM   2808 C CA    . PRO B 1 20  ? 51.143 7.518   -27.310 1.00 45.21 ? 11  PRO B CA    1 
ATOM   2809 C C     . PRO B 1 20  ? 50.879 6.553   -28.451 1.00 43.74 ? 11  PRO B C     1 
ATOM   2810 O O     . PRO B 1 20  ? 50.904 5.337   -28.225 1.00 45.09 ? 11  PRO B O     1 
ATOM   2811 C CB    . PRO B 1 20  ? 49.872 7.778   -26.494 1.00 42.07 ? 11  PRO B CB    1 
ATOM   2812 C CG    . PRO B 1 20  ? 49.300 9.019   -27.093 1.00 49.54 ? 11  PRO B CG    1 
ATOM   2813 C CD    . PRO B 1 20  ? 50.473 9.858   -27.533 1.00 50.09 ? 11  PRO B CD    1 
ATOM   2814 N N     . LEU B 1 21  ? 50.631 7.052   -29.666 1.00 42.82 ? 12  LEU B N     1 
ATOM   2815 C CA    . LEU B 1 21  ? 50.404 6.170   -30.805 1.00 43.20 ? 12  LEU B CA    1 
ATOM   2816 C C     . LEU B 1 21  ? 51.658 5.411   -31.207 1.00 38.74 ? 12  LEU B C     1 
ATOM   2817 O O     . LEU B 1 21  ? 51.559 4.414   -31.926 1.00 38.48 ? 12  LEU B O     1 
ATOM   2818 C CB    . LEU B 1 21  ? 49.886 6.967   -32.002 1.00 37.77 ? 12  LEU B CB    1 
ATOM   2819 C CG    . LEU B 1 21  ? 48.397 7.306   -31.993 1.00 36.14 ? 12  LEU B CG    1 
ATOM   2820 C CD1   . LEU B 1 21  ? 48.036 8.158   -33.200 1.00 34.66 ? 12  LEU B CD1   1 
ATOM   2821 C CD2   . LEU B 1 21  ? 47.568 6.033   -31.957 1.00 35.08 ? 12  LEU B CD2   1 
ATOM   2822 N N     . PHE B 1 22  ? 52.829 5.854   -30.764 1.00 35.35 ? 13  PHE B N     1 
ATOM   2823 C CA    . PHE B 1 22  ? 54.093 5.212   -31.095 1.00 35.75 ? 13  PHE B CA    1 
ATOM   2824 C C     . PHE B 1 22  ? 54.743 4.568   -29.873 1.00 45.75 ? 13  PHE B C     1 
ATOM   2825 O O     . PHE B 1 22  ? 55.969 4.462   -29.790 1.00 47.76 ? 13  PHE B O     1 
ATOM   2826 C CB    . PHE B 1 22  ? 55.031 6.221   -31.753 1.00 38.89 ? 13  PHE B CB    1 
ATOM   2827 C CG    . PHE B 1 22  ? 54.586 6.634   -33.126 1.00 40.83 ? 13  PHE B CG    1 
ATOM   2828 C CD1   . PHE B 1 22  ? 53.684 7.670   -33.292 1.00 37.35 ? 13  PHE B CD1   1 
ATOM   2829 C CD2   . PHE B 1 22  ? 55.039 5.957   -34.249 1.00 38.07 ? 13  PHE B CD2   1 
ATOM   2830 C CE1   . PHE B 1 22  ? 53.260 8.043   -34.546 1.00 46.15 ? 13  PHE B CE1   1 
ATOM   2831 C CE2   . PHE B 1 22  ? 54.617 6.325   -35.512 1.00 46.49 ? 13  PHE B CE2   1 
ATOM   2832 C CZ    . PHE B 1 22  ? 53.723 7.370   -35.658 1.00 42.51 ? 13  PHE B CZ    1 
ATOM   2833 N N     . SER B 1 23  ? 53.934 4.139   -28.923 1.00 44.88 ? 14  SER B N     1 
ATOM   2834 C CA    . SER B 1 23  ? 54.413 3.314   -27.823 1.00 44.45 ? 14  SER B CA    1 
ATOM   2835 C C     . SER B 1 23  ? 54.298 1.843   -28.208 1.00 43.90 ? 14  SER B C     1 
ATOM   2836 O O     . SER B 1 23  ? 53.239 1.419   -28.687 1.00 48.10 ? 14  SER B O     1 
ATOM   2837 C CB    . SER B 1 23  ? 53.612 3.587   -26.557 1.00 38.33 ? 14  SER B CB    1 
ATOM   2838 O OG    . SER B 1 23  ? 53.498 2.419   -25.765 1.00 54.60 ? 14  SER B OG    1 
ATOM   2839 N N     . PRO B 1 24  ? 55.351 1.045   -28.025 1.00 44.53 ? 15  PRO B N     1 
ATOM   2840 C CA    . PRO B 1 24  ? 55.303 -0.351  -28.477 1.00 41.38 ? 15  PRO B CA    1 
ATOM   2841 C C     . PRO B 1 24  ? 54.203 -1.129  -27.770 1.00 43.12 ? 15  PRO B C     1 
ATOM   2842 O O     . PRO B 1 24  ? 53.927 -0.921  -26.587 1.00 48.58 ? 15  PRO B O     1 
ATOM   2843 C CB    . PRO B 1 24  ? 56.696 -0.888  -28.122 1.00 44.60 ? 15  PRO B CB    1 
ATOM   2844 C CG    . PRO B 1 24  ? 57.207 0.033   -27.062 1.00 50.14 ? 15  PRO B CG    1 
ATOM   2845 C CD    . PRO B 1 24  ? 56.633 1.380   -27.383 1.00 45.56 ? 15  PRO B CD    1 
ATOM   2846 N N     . TYR B 1 25  ? 53.562 -2.021  -28.519 1.00 36.69 ? 16  TYR B N     1 
ATOM   2847 C CA    . TYR B 1 25  ? 52.462 -2.818  -28.002 1.00 36.91 ? 16  TYR B CA    1 
ATOM   2848 C C     . TYR B 1 25  ? 52.626 -4.257  -28.462 1.00 40.70 ? 16  TYR B C     1 
ATOM   2849 O O     . TYR B 1 25  ? 52.947 -4.513  -29.626 1.00 38.70 ? 16  TYR B O     1 
ATOM   2850 C CB    . TYR B 1 25  ? 51.106 -2.268  -28.465 1.00 35.81 ? 16  TYR B CB    1 
ATOM   2851 C CG    . TYR B 1 25  ? 49.920 -2.978  -27.854 1.00 40.89 ? 16  TYR B CG    1 
ATOM   2852 C CD1   . TYR B 1 25  ? 49.521 -2.709  -26.550 1.00 34.92 ? 16  TYR B CD1   1 
ATOM   2853 C CD2   . TYR B 1 25  ? 49.201 -3.921  -28.580 1.00 34.17 ? 16  TYR B CD2   1 
ATOM   2854 C CE1   . TYR B 1 25  ? 48.436 -3.358  -25.987 1.00 37.51 ? 16  TYR B CE1   1 
ATOM   2855 C CE2   . TYR B 1 25  ? 48.116 -4.575  -28.026 1.00 39.48 ? 16  TYR B CE2   1 
ATOM   2856 C CZ    . TYR B 1 25  ? 47.739 -4.290  -26.729 1.00 39.94 ? 16  TYR B CZ    1 
ATOM   2857 O OH    . TYR B 1 25  ? 46.660 -4.938  -26.174 1.00 34.21 ? 16  TYR B OH    1 
ATOM   2858 N N     . LYS B 1 26  ? 52.399 -5.193  -27.544 1.00 42.71 ? 17  LYS B N     1 
ATOM   2859 C CA    . LYS B 1 26  ? 52.520 -6.622  -27.823 1.00 39.67 ? 17  LYS B CA    1 
ATOM   2860 C C     . LYS B 1 26  ? 51.123 -7.177  -28.078 1.00 44.98 ? 17  LYS B C     1 
ATOM   2861 O O     . LYS B 1 26  ? 50.343 -7.376  -27.144 1.00 47.53 ? 17  LYS B O     1 
ATOM   2862 C CB    . LYS B 1 26  ? 53.208 -7.342  -26.668 1.00 45.26 ? 17  LYS B CB    1 
ATOM   2863 N N     . MET B 1 27  ? 50.810 -7.426  -29.349 1.00 45.47 ? 18  MET B N     1 
ATOM   2864 C CA    . MET B 1 27  ? 49.522 -7.993  -29.750 1.00 47.71 ? 18  MET B CA    1 
ATOM   2865 C C     . MET B 1 27  ? 49.721 -9.499  -29.894 1.00 46.02 ? 18  MET B C     1 
ATOM   2866 O O     . MET B 1 27  ? 50.058 -10.002 -30.967 1.00 45.62 ? 18  MET B O     1 
ATOM   2867 C CB    . MET B 1 27  ? 49.021 -7.355  -31.041 1.00 40.51 ? 18  MET B CB    1 
ATOM   2868 C CG    . MET B 1 27  ? 47.766 -8.002  -31.612 1.00 38.54 ? 18  MET B CG    1 
ATOM   2869 S SD    . MET B 1 27  ? 47.211 -7.225  -33.141 1.00 47.92 ? 18  MET B SD    1 
ATOM   2870 C CE    . MET B 1 27  ? 48.308 -7.996  -34.329 1.00 33.98 ? 18  MET B CE    1 
ATOM   2871 N N     . GLY B 1 28  ? 49.508 -10.220 -28.799 1.00 48.52 ? 19  GLY B N     1 
ATOM   2872 C CA    . GLY B 1 28  ? 49.800 -11.645 -28.803 1.00 47.25 ? 19  GLY B CA    1 
ATOM   2873 C C     . GLY B 1 28  ? 51.298 -11.858 -28.878 1.00 48.28 ? 19  GLY B C     1 
ATOM   2874 O O     . GLY B 1 28  ? 52.068 -11.289 -28.095 1.00 46.97 ? 19  GLY B O     1 
ATOM   2875 N N     . LYS B 1 29  ? 51.729 -12.679 -29.831 1.00 54.26 ? 20  LYS B N     1 
ATOM   2876 C CA    . LYS B 1 29  ? 53.150 -12.872 -30.080 1.00 51.24 ? 20  LYS B CA    1 
ATOM   2877 C C     . LYS B 1 29  ? 53.701 -11.908 -31.123 1.00 49.26 ? 20  LYS B C     1 
ATOM   2878 O O     . LYS B 1 29  ? 54.887 -11.991 -31.457 1.00 50.59 ? 20  LYS B O     1 
ATOM   2879 C CB    . LYS B 1 29  ? 53.426 -14.317 -30.509 1.00 55.85 ? 20  LYS B CB    1 
ATOM   2880 C CG    . LYS B 1 29  ? 52.808 -14.717 -31.834 1.00 56.16 ? 20  LYS B CG    1 
ATOM   2881 C CD    . LYS B 1 29  ? 52.710 -16.230 -31.941 1.00 59.99 ? 20  LYS B CD    1 
ATOM   2882 C CE    . LYS B 1 29  ? 52.144 -16.661 -33.281 1.00 60.16 ? 20  LYS B CE    1 
ATOM   2883 N NZ    . LYS B 1 29  ? 52.546 -15.740 -34.377 1.00 64.04 ? 20  LYS B NZ    1 
ATOM   2884 N N     . PHE B 1 30  ? 52.876 -11.002 -31.640 1.00 47.05 ? 21  PHE B N     1 
ATOM   2885 C CA    . PHE B 1 30  ? 53.332 -9.973  -32.566 1.00 48.86 ? 21  PHE B CA    1 
ATOM   2886 C C     . PHE B 1 30  ? 53.641 -8.702  -31.784 1.00 50.02 ? 21  PHE B C     1 
ATOM   2887 O O     . PHE B 1 30  ? 52.742 -8.105  -31.181 1.00 47.67 ? 21  PHE B O     1 
ATOM   2888 C CB    . PHE B 1 30  ? 52.279 -9.697  -33.639 1.00 46.39 ? 21  PHE B CB    1 
ATOM   2889 C CG    . PHE B 1 30  ? 51.693 -10.935 -34.252 1.00 43.95 ? 21  PHE B CG    1 
ATOM   2890 C CD1   . PHE B 1 30  ? 52.461 -11.754 -35.061 1.00 46.35 ? 21  PHE B CD1   1 
ATOM   2891 C CD2   . PHE B 1 30  ? 50.371 -11.277 -34.024 1.00 45.01 ? 21  PHE B CD2   1 
ATOM   2892 C CE1   . PHE B 1 30  ? 51.923 -12.892 -35.630 1.00 48.81 ? 21  PHE B CE1   1 
ATOM   2893 C CE2   . PHE B 1 30  ? 49.826 -12.414 -34.589 1.00 47.24 ? 21  PHE B CE2   1 
ATOM   2894 C CZ    . PHE B 1 30  ? 50.604 -13.223 -35.393 1.00 43.29 ? 21  PHE B CZ    1 
ATOM   2895 N N     . ASN B 1 31  ? 54.907 -8.292  -31.793 1.00 43.92 ? 22  ASN B N     1 
ATOM   2896 C CA    . ASN B 1 31  ? 55.334 -7.069  -31.121 1.00 47.17 ? 22  ASN B CA    1 
ATOM   2897 C C     . ASN B 1 31  ? 55.235 -5.916  -32.113 1.00 43.79 ? 22  ASN B C     1 
ATOM   2898 O O     . ASN B 1 31  ? 56.008 -5.845  -33.073 1.00 49.69 ? 22  ASN B O     1 
ATOM   2899 C CB    . ASN B 1 31  ? 56.756 -7.216  -30.584 1.00 53.73 ? 22  ASN B CB    1 
ATOM   2900 C CG    . ASN B 1 31  ? 56.873 -8.306  -29.536 1.00 50.04 ? 22  ASN B CG    1 
ATOM   2901 O OD1   . ASN B 1 31  ? 57.786 -9.130  -29.581 1.00 56.31 ? 22  ASN B OD1   1 
ATOM   2902 N ND2   . ASN B 1 31  ? 55.944 -8.317  -28.586 1.00 54.95 ? 22  ASN B ND2   1 
ATOM   2903 N N     . LEU B 1 32  ? 54.283 -5.016  -31.884 1.00 39.46 ? 23  LEU B N     1 
ATOM   2904 C CA    . LEU B 1 32  ? 54.068 -3.884  -32.773 1.00 41.55 ? 23  LEU B CA    1 
ATOM   2905 C C     . LEU B 1 32  ? 54.880 -2.682  -32.308 1.00 42.00 ? 23  LEU B C     1 
ATOM   2906 O O     . LEU B 1 32  ? 54.990 -2.417  -31.107 1.00 35.17 ? 23  LEU B O     1 
ATOM   2907 C CB    . LEU B 1 32  ? 52.583 -3.524  -32.838 1.00 34.39 ? 23  LEU B CB    1 
ATOM   2908 C CG    . LEU B 1 32  ? 51.627 -4.643  -33.258 1.00 39.30 ? 23  LEU B CG    1 
ATOM   2909 C CD1   . LEU B 1 32  ? 50.190 -4.146  -33.265 1.00 30.93 ? 23  LEU B CD1   1 
ATOM   2910 C CD2   . LEU B 1 32  ? 52.008 -5.204  -34.622 1.00 33.38 ? 23  LEU B CD2   1 
ATOM   2911 N N     . SER B 1 33  ? 55.453 -1.957  -33.270 1.00 35.83 ? 24  SER B N     1 
ATOM   2912 C CA    . SER B 1 33  ? 56.246 -0.776  -32.952 1.00 37.64 ? 24  SER B CA    1 
ATOM   2913 C C     . SER B 1 33  ? 55.389 0.462   -32.726 1.00 40.25 ? 24  SER B C     1 
ATOM   2914 O O     . SER B 1 33  ? 55.866 1.429   -32.120 1.00 38.94 ? 24  SER B O     1 
ATOM   2915 C CB    . SER B 1 33  ? 57.255 -0.503  -34.070 1.00 42.20 ? 24  SER B CB    1 
ATOM   2916 O OG    . SER B 1 33  ? 58.485 -1.161  -33.819 1.00 53.82 ? 24  SER B OG    1 
ATOM   2917 N N     . HIS B 1 34  ? 54.144 0.451   -33.196 1.00 34.03 ? 25  HIS B N     1 
ATOM   2918 C CA    . HIS B 1 34  ? 53.247 1.590   -33.071 1.00 32.72 ? 25  HIS B CA    1 
ATOM   2919 C C     . HIS B 1 34  ? 51.818 1.081   -33.191 1.00 39.05 ? 25  HIS B C     1 
ATOM   2920 O O     . HIS B 1 34  ? 51.578 -0.067  -33.572 1.00 38.18 ? 25  HIS B O     1 
ATOM   2921 C CB    . HIS B 1 34  ? 53.547 2.661   -34.124 1.00 36.93 ? 25  HIS B CB    1 
ATOM   2922 C CG    . HIS B 1 34  ? 53.410 2.177   -35.535 1.00 37.31 ? 25  HIS B CG    1 
ATOM   2923 N ND1   . HIS B 1 34  ? 52.192 2.069   -36.169 1.00 37.37 ? 25  HIS B ND1   1 
ATOM   2924 C CD2   . HIS B 1 34  ? 54.339 1.774   -36.433 1.00 37.43 ? 25  HIS B CD2   1 
ATOM   2925 C CE1   . HIS B 1 34  ? 52.375 1.620   -37.398 1.00 36.18 ? 25  HIS B CE1   1 
ATOM   2926 N NE2   . HIS B 1 34  ? 53.669 1.434   -37.584 1.00 35.19 ? 25  HIS B NE2   1 
ATOM   2927 N N     . ARG B 1 35  ? 50.868 1.957   -32.871 1.00 34.99 ? 26  ARG B N     1 
ATOM   2928 C CA    . ARG B 1 35  ? 49.465 1.580   -32.768 1.00 36.67 ? 26  ARG B CA    1 
ATOM   2929 C C     . ARG B 1 35  ? 48.621 2.087   -33.932 1.00 36.25 ? 26  ARG B C     1 
ATOM   2930 O O     . ARG B 1 35  ? 47.388 2.013   -33.869 1.00 39.85 ? 26  ARG B O     1 
ATOM   2931 C CB    . ARG B 1 35  ? 48.895 2.076   -31.438 1.00 38.92 ? 26  ARG B CB    1 
ATOM   2932 C CG    . ARG B 1 35  ? 49.617 1.496   -30.232 1.00 36.67 ? 26  ARG B CG    1 
ATOM   2933 C CD    . ARG B 1 35  ? 49.605 2.448   -29.054 1.00 40.07 ? 26  ARG B CD    1 
ATOM   2934 N NE    . ARG B 1 35  ? 50.383 1.929   -27.936 1.00 40.86 ? 26  ARG B NE    1 
ATOM   2935 C CZ    . ARG B 1 35  ? 49.913 1.096   -27.017 1.00 39.50 ? 26  ARG B CZ    1 
ATOM   2936 N NH1   . ARG B 1 35  ? 48.665 0.656   -27.054 1.00 34.00 ? 26  ARG B NH1   1 
ATOM   2937 N NH2   . ARG B 1 35  ? 50.716 0.696   -26.035 1.00 37.53 ? 26  ARG B NH2   1 
ATOM   2938 N N     . VAL B 1 36  ? 49.246 2.593   -34.990 1.00 33.89 ? 27  VAL B N     1 
ATOM   2939 C CA    . VAL B 1 36  ? 48.518 3.010   -36.183 1.00 37.81 ? 27  VAL B CA    1 
ATOM   2940 C C     . VAL B 1 36  ? 48.299 1.787   -37.066 1.00 34.24 ? 27  VAL B C     1 
ATOM   2941 O O     . VAL B 1 36  ? 49.259 1.188   -37.563 1.00 33.71 ? 27  VAL B O     1 
ATOM   2942 C CB    . VAL B 1 36  ? 49.274 4.113   -36.938 1.00 35.24 ? 27  VAL B CB    1 
ATOM   2943 C CG1   . VAL B 1 36  ? 48.430 4.644   -38.085 1.00 37.12 ? 27  VAL B CG1   1 
ATOM   2944 C CG2   . VAL B 1 36  ? 49.656 5.238   -35.986 1.00 38.83 ? 27  VAL B CG2   1 
ATOM   2945 N N     . VAL B 1 37  ? 47.036 1.412   -37.259 1.00 27.79 ? 28  VAL B N     1 
ATOM   2946 C CA    . VAL B 1 37  ? 46.663 0.212   -37.998 1.00 27.62 ? 28  VAL B CA    1 
ATOM   2947 C C     . VAL B 1 37  ? 46.030 0.620   -39.320 1.00 34.44 ? 28  VAL B C     1 
ATOM   2948 O O     . VAL B 1 37  ? 45.295 1.611   -39.388 1.00 35.55 ? 28  VAL B O     1 
ATOM   2949 C CB    . VAL B 1 37  ? 45.696 -0.668  -37.179 1.00 37.20 ? 28  VAL B CB    1 
ATOM   2950 C CG1   . VAL B 1 37  ? 45.344 -1.941  -37.939 1.00 30.63 ? 28  VAL B CG1   1 
ATOM   2951 C CG2   . VAL B 1 37  ? 46.294 -0.996  -35.819 1.00 33.01 ? 28  VAL B CG2   1 
ATOM   2952 N N     . LEU B 1 38  ? 46.322 -0.139  -40.373 1.00 30.29 ? 29  LEU B N     1 
ATOM   2953 C CA    . LEU B 1 38  ? 45.613 0.019   -41.635 1.00 33.81 ? 29  LEU B CA    1 
ATOM   2954 C C     . LEU B 1 38  ? 44.299 -0.749  -41.561 1.00 32.05 ? 29  LEU B C     1 
ATOM   2955 O O     . LEU B 1 38  ? 44.294 -1.963  -41.323 1.00 30.04 ? 29  LEU B O     1 
ATOM   2956 C CB    . LEU B 1 38  ? 46.464 -0.473  -42.804 1.00 30.68 ? 29  LEU B CB    1 
ATOM   2957 C CG    . LEU B 1 38  ? 45.713 -0.750  -44.109 1.00 34.15 ? 29  LEU B CG    1 
ATOM   2958 C CD1   . LEU B 1 38  ? 45.125 0.537   -44.683 1.00 33.27 ? 29  LEU B CD1   1 
ATOM   2959 C CD2   . LEU B 1 38  ? 46.625 -1.426  -45.125 1.00 31.98 ? 29  LEU B CD2   1 
ATOM   2960 N N     . ALA B 1 39  ? 43.190 -0.041  -41.753 1.00 31.04 ? 30  ALA B N     1 
ATOM   2961 C CA    . ALA B 1 39  ? 41.884 -0.674  -41.712 1.00 27.10 ? 30  ALA B CA    1 
ATOM   2962 C C     . ALA B 1 39  ? 41.642 -1.484  -42.986 1.00 28.30 ? 30  ALA B C     1 
ATOM   2963 O O     . ALA B 1 39  ? 42.154 -1.143  -44.056 1.00 28.01 ? 30  ALA B O     1 
ATOM   2964 C CB    . ALA B 1 39  ? 40.789 0.376   -41.544 1.00 27.64 ? 30  ALA B CB    1 
ATOM   2965 N N     . PRO B 1 40  ? 40.873 -2.570  -42.894 1.00 26.02 ? 31  PRO B N     1 
ATOM   2966 C CA    . PRO B 1 40  ? 40.548 -3.351  -44.097 1.00 30.94 ? 31  PRO B CA    1 
ATOM   2967 C C     . PRO B 1 40  ? 39.682 -2.536  -45.047 1.00 30.90 ? 31  PRO B C     1 
ATOM   2968 O O     . PRO B 1 40  ? 38.706 -1.912  -44.630 1.00 28.53 ? 31  PRO B O     1 
ATOM   2969 C CB    . PRO B 1 40  ? 39.791 -4.561  -43.538 1.00 30.48 ? 31  PRO B CB    1 
ATOM   2970 C CG    . PRO B 1 40  ? 39.253 -4.092  -42.219 1.00 31.23 ? 31  PRO B CG    1 
ATOM   2971 C CD    . PRO B 1 40  ? 40.290 -3.158  -41.676 1.00 29.96 ? 31  PRO B CD    1 
ATOM   2972 N N     . MET B 1 41  ? 40.047 -2.538  -46.331 1.00 33.32 ? 32  MET B N     1 
ATOM   2973 C CA    . MET B 1 41  ? 39.402 -1.651  -47.299 1.00 29.06 ? 32  MET B CA    1 
ATOM   2974 C C     . MET B 1 41  ? 39.323 -2.323  -48.663 1.00 33.01 ? 32  MET B C     1 
ATOM   2975 O O     . MET B 1 41  ? 40.340 -2.458  -49.350 1.00 27.81 ? 32  MET B O     1 
ATOM   2976 C CB    . MET B 1 41  ? 40.152 -0.332  -47.401 1.00 26.87 ? 32  MET B CB    1 
ATOM   2977 C CG    . MET B 1 41  ? 40.158 0.483   -46.131 1.00 33.07 ? 32  MET B CG    1 
ATOM   2978 S SD    . MET B 1 41  ? 40.143 2.221   -46.521 1.00 41.42 ? 32  MET B SD    1 
ATOM   2979 C CE    . MET B 1 41  ? 41.920 2.453   -46.482 1.00 31.32 ? 32  MET B CE    1 
ATOM   2980 N N     . THR B 1 42  ? 38.110 -2.711  -49.049 1.00 26.81 ? 33  THR B N     1 
ATOM   2981 C CA    . THR B 1 42  ? 37.820 -3.158  -50.403 1.00 33.54 ? 33  THR B CA    1 
ATOM   2982 C C     . THR B 1 42  ? 38.148 -2.063  -51.411 1.00 33.52 ? 33  THR B C     1 
ATOM   2983 O O     . THR B 1 42  ? 37.661 -0.935  -51.299 1.00 31.34 ? 33  THR B O     1 
ATOM   2984 C CB    . THR B 1 42  ? 36.341 -3.534  -50.505 1.00 36.89 ? 33  THR B CB    1 
ATOM   2985 O OG1   . THR B 1 42  ? 36.051 -4.601  -49.592 1.00 29.03 ? 33  THR B OG1   1 
ATOM   2986 C CG2   . THR B 1 42  ? 35.978 -3.950  -51.920 1.00 30.47 ? 33  THR B CG2   1 
ATOM   2987 N N     . ARG B 1 43  ? 38.979 -2.398  -52.400 1.00 30.91 ? 34  ARG B N     1 
ATOM   2988 C CA    . ARG B 1 43  ? 39.348 -1.455  -53.447 1.00 32.56 ? 34  ARG B CA    1 
ATOM   2989 C C     . ARG B 1 43  ? 39.076 -1.968  -54.855 1.00 34.72 ? 34  ARG B C     1 
ATOM   2990 O O     . ARG B 1 43  ? 39.142 -1.175  -55.801 1.00 32.28 ? 34  ARG B O     1 
ATOM   2991 C CB    . ARG B 1 43  ? 40.833 -1.068  -53.330 1.00 27.47 ? 34  ARG B CB    1 
ATOM   2992 C CG    . ARG B 1 43  ? 41.272 -0.667  -51.923 1.00 29.63 ? 34  ARG B CG    1 
ATOM   2993 C CD    . ARG B 1 43  ? 40.602 0.624   -51.459 1.00 26.52 ? 34  ARG B CD    1 
ATOM   2994 N NE    . ARG B 1 43  ? 40.627 1.662   -52.484 1.00 29.07 ? 34  ARG B NE    1 
ATOM   2995 C CZ    . ARG B 1 43  ? 41.671 2.436   -52.747 1.00 30.43 ? 34  ARG B CZ    1 
ATOM   2996 N NH1   . ARG B 1 43  ? 42.797 2.334   -52.059 1.00 29.66 ? 34  ARG B NH1   1 
ATOM   2997 N NH2   . ARG B 1 43  ? 41.584 3.334   -53.725 1.00 29.45 ? 34  ARG B NH2   1 
ATOM   2998 N N     . CYS B 1 44  ? 38.796 -3.264  -55.021 1.00 28.01 ? 35  CYS B N     1 
ATOM   2999 C CA    . CYS B 1 44  ? 38.301 -3.828  -56.280 1.00 31.20 ? 35  CYS B CA    1 
ATOM   3000 C C     . CYS B 1 44  ? 39.362 -3.812  -57.382 1.00 29.26 ? 35  CYS B C     1 
ATOM   3001 O O     . CYS B 1 44  ? 39.049 -3.610  -58.557 1.00 31.84 ? 35  CYS B O     1 
ATOM   3002 C CB    . CYS B 1 44  ? 37.028 -3.112  -56.746 1.00 34.43 ? 35  CYS B CB    1 
ATOM   3003 S SG    . CYS B 1 44  ? 35.726 -2.995  -55.493 1.00 40.13 ? 35  CYS B SG    1 
ATOM   3004 N N     . ARG B 1 45  ? 40.621 -4.044  -57.010 1.00 29.21 ? 36  ARG B N     1 
ATOM   3005 C CA    . ARG B 1 45  ? 41.700 -4.137  -57.983 1.00 31.68 ? 36  ARG B CA    1 
ATOM   3006 C C     . ARG B 1 45  ? 42.157 -5.568  -58.236 1.00 37.06 ? 36  ARG B C     1 
ATOM   3007 O O     . ARG B 1 45  ? 42.982 -5.786  -59.130 1.00 36.45 ? 36  ARG B O     1 
ATOM   3008 C CB    . ARG B 1 45  ? 42.898 -3.291  -57.534 1.00 30.79 ? 36  ARG B CB    1 
ATOM   3009 C CG    . ARG B 1 45  ? 42.934 -1.899  -58.146 1.00 31.82 ? 36  ARG B CG    1 
ATOM   3010 C CD    . ARG B 1 45  ? 42.004 -0.959  -57.403 1.00 34.83 ? 36  ARG B CD    1 
ATOM   3011 N NE    . ARG B 1 45  ? 42.145 0.424   -57.840 1.00 28.65 ? 36  ARG B NE    1 
ATOM   3012 C CZ    . ARG B 1 45  ? 41.450 1.437   -57.340 1.00 31.89 ? 36  ARG B CZ    1 
ATOM   3013 N NH1   . ARG B 1 45  ? 40.548 1.254   -56.390 1.00 30.67 ? 36  ARG B NH1   1 
ATOM   3014 N NH2   . ARG B 1 45  ? 41.663 2.665   -57.808 1.00 29.27 ? 36  ARG B NH2   1 
ATOM   3015 N N     . ALA B 1 46  ? 41.643 -6.541  -57.481 1.00 31.05 ? 37  ALA B N     1 
ATOM   3016 C CA    . ALA B 1 46  ? 42.025 -7.944  -57.642 1.00 34.21 ? 37  ALA B CA    1 
ATOM   3017 C C     . ALA B 1 46  ? 41.159 -8.562  -58.736 1.00 32.63 ? 37  ALA B C     1 
ATOM   3018 O O     . ALA B 1 46  ? 40.179 -9.267  -58.482 1.00 29.19 ? 37  ALA B O     1 
ATOM   3019 C CB    . ALA B 1 46  ? 41.889 -8.689  -56.321 1.00 31.15 ? 37  ALA B CB    1 
ATOM   3020 N N     . LEU B 1 47  ? 41.548 -8.292  -59.982 1.00 32.93 ? 38  LEU B N     1 
ATOM   3021 C CA    . LEU B 1 47  ? 40.733 -8.668  -61.129 1.00 34.98 ? 38  LEU B CA    1 
ATOM   3022 C C     . LEU B 1 47  ? 40.500 -10.173 -61.171 1.00 29.93 ? 38  LEU B C     1 
ATOM   3023 O O     . LEU B 1 47  ? 41.411 -10.968 -60.921 1.00 31.09 ? 38  LEU B O     1 
ATOM   3024 C CB    . LEU B 1 47  ? 41.398 -8.201  -62.424 1.00 36.59 ? 38  LEU B CB    1 
ATOM   3025 C CG    . LEU B 1 47  ? 41.869 -6.746  -62.443 1.00 36.56 ? 38  LEU B CG    1 
ATOM   3026 C CD1   . LEU B 1 47  ? 42.572 -6.429  -63.754 1.00 37.29 ? 38  LEU B CD1   1 
ATOM   3027 C CD2   . LEU B 1 47  ? 40.702 -5.797  -62.218 1.00 35.22 ? 38  LEU B CD2   1 
ATOM   3028 N N     . ASN B 1 48  ? 39.258 -10.555 -61.485 1.00 31.95 ? 39  ASN B N     1 
ATOM   3029 C CA    . ASN B 1 48  ? 38.831 -11.954 -61.546 1.00 32.35 ? 39  ASN B CA    1 
ATOM   3030 C C     . ASN B 1 48  ? 39.031 -12.669 -60.213 1.00 33.11 ? 39  ASN B C     1 
ATOM   3031 O O     . ASN B 1 48  ? 39.274 -13.878 -60.178 1.00 27.73 ? 39  ASN B O     1 
ATOM   3032 C CB    . ASN B 1 48  ? 39.544 -12.708 -62.673 1.00 30.97 ? 39  ASN B CB    1 
ATOM   3033 C CG    . ASN B 1 48  ? 39.433 -11.998 -64.012 1.00 36.58 ? 39  ASN B CG    1 
ATOM   3034 O OD1   . ASN B 1 48  ? 40.424 -11.827 -64.719 1.00 39.07 ? 39  ASN B OD1   1 
ATOM   3035 N ND2   . ASN B 1 48  ? 38.222 -11.587 -64.367 1.00 31.50 ? 39  ASN B ND2   1 
ATOM   3036 N N     . ASN B 1 49  ? 38.927 -11.924 -59.110 1.00 28.72 ? 40  ASN B N     1 
ATOM   3037 C CA    . ASN B 1 49  ? 39.064 -12.441 -57.750 1.00 33.22 ? 40  ASN B CA    1 
ATOM   3038 C C     . ASN B 1 49  ? 40.466 -12.957 -57.453 1.00 34.02 ? 40  ASN B C     1 
ATOM   3039 O O     . ASN B 1 49  ? 40.658 -13.714 -56.494 1.00 39.20 ? 40  ASN B O     1 
ATOM   3040 C CB    . ASN B 1 49  ? 38.040 -13.545 -57.457 1.00 25.17 ? 40  ASN B CB    1 
ATOM   3041 C CG    . ASN B 1 49  ? 36.619 -13.118 -57.758 1.00 26.73 ? 40  ASN B CG    1 
ATOM   3042 O OD1   . ASN B 1 49  ? 35.821 -13.901 -58.274 1.00 36.40 ? 40  ASN B OD1   1 
ATOM   3043 N ND2   . ASN B 1 49  ? 36.292 -11.872 -57.433 1.00 31.75 ? 40  ASN B ND2   1 
ATOM   3044 N N     . ILE B 1 50  ? 41.450 -12.569 -58.248 1.00 34.35 ? 41  ILE B N     1 
ATOM   3045 C CA    . ILE B 1 50  ? 42.836 -12.998 -58.078 1.00 37.92 ? 41  ILE B CA    1 
ATOM   3046 C C     . ILE B 1 50  ? 43.644 -11.804 -57.593 1.00 37.44 ? 41  ILE B C     1 
ATOM   3047 O O     . ILE B 1 50  ? 43.615 -10.749 -58.237 1.00 29.41 ? 41  ILE B O     1 
ATOM   3048 C CB    . ILE B 1 50  ? 43.432 -13.553 -59.385 1.00 35.60 ? 41  ILE B CB    1 
ATOM   3049 C CG1   . ILE B 1 50  ? 42.445 -14.507 -60.061 1.00 36.54 ? 41  ILE B CG1   1 
ATOM   3050 C CG2   . ILE B 1 50  ? 44.762 -14.239 -59.109 1.00 39.10 ? 41  ILE B CG2   1 
ATOM   3051 C CD1   . ILE B 1 50  ? 42.419 -15.887 -59.455 1.00 44.30 ? 41  ILE B CD1   1 
ATOM   3052 N N     . PRO B 1 51  ? 44.364 -11.920 -56.479 1.00 33.93 ? 42  PRO B N     1 
ATOM   3053 C CA    . PRO B 1 51  ? 45.243 -10.824 -56.054 1.00 39.67 ? 42  PRO B CA    1 
ATOM   3054 C C     . PRO B 1 51  ? 46.270 -10.513 -57.133 1.00 40.02 ? 42  PRO B C     1 
ATOM   3055 O O     . PRO B 1 51  ? 46.966 -11.402 -57.627 1.00 45.38 ? 42  PRO B O     1 
ATOM   3056 C CB    . PRO B 1 51  ? 45.900 -11.370 -54.781 1.00 31.60 ? 42  PRO B CB    1 
ATOM   3057 C CG    . PRO B 1 51  ? 44.980 -12.451 -54.307 1.00 38.02 ? 42  PRO B CG    1 
ATOM   3058 C CD    . PRO B 1 51  ? 44.390 -13.054 -55.542 1.00 35.65 ? 42  PRO B CD    1 
ATOM   3059 N N     . GLN B 1 52  ? 46.345 -9.241  -57.511 1.00 37.99 ? 43  GLN B N     1 
ATOM   3060 C CA    . GLN B 1 52  ? 47.199 -8.797  -58.601 1.00 40.22 ? 43  GLN B CA    1 
ATOM   3061 C C     . GLN B 1 52  ? 48.460 -8.134  -58.061 1.00 39.64 ? 43  GLN B C     1 
ATOM   3062 O O     . GLN B 1 52  ? 48.578 -7.831  -56.871 1.00 40.46 ? 43  GLN B O     1 
ATOM   3063 C CB    . GLN B 1 52  ? 46.440 -7.830  -59.519 1.00 34.11 ? 43  GLN B CB    1 
ATOM   3064 C CG    . GLN B 1 52  ? 45.168 -8.405  -60.114 1.00 37.33 ? 43  GLN B CG    1 
ATOM   3065 C CD    . GLN B 1 52  ? 45.440 -9.537  -61.084 1.00 40.28 ? 43  GLN B CD    1 
ATOM   3066 O OE1   . GLN B 1 52  ? 46.425 -9.512  -61.821 1.00 48.47 ? 43  GLN B OE1   1 
ATOM   3067 N NE2   . GLN B 1 52  ? 44.568 -10.539 -61.086 1.00 38.81 ? 43  GLN B NE2   1 
ATOM   3068 N N     . ALA B 1 53  ? 49.414 -7.903  -58.967 1.00 39.68 ? 44  ALA B N     1 
ATOM   3069 C CA    . ALA B 1 53  ? 50.650 -7.223  -58.596 1.00 38.31 ? 44  ALA B CA    1 
ATOM   3070 C C     . ALA B 1 53  ? 50.400 -5.817  -58.070 1.00 39.14 ? 44  ALA B C     1 
ATOM   3071 O O     . ALA B 1 53  ? 51.229 -5.293  -57.318 1.00 37.68 ? 44  ALA B O     1 
ATOM   3072 C CB    . ALA B 1 53  ? 51.602 -7.167  -59.793 1.00 34.75 ? 44  ALA B CB    1 
ATOM   3073 N N     . ALA B 1 54  ? 49.282 -5.193  -58.454 1.00 37.43 ? 45  ALA B N     1 
ATOM   3074 C CA    . ALA B 1 54  ? 48.955 -3.868  -57.937 1.00 36.45 ? 45  ALA B CA    1 
ATOM   3075 C C     . ALA B 1 54  ? 48.669 -3.906  -56.443 1.00 34.94 ? 45  ALA B C     1 
ATOM   3076 O O     . ALA B 1 54  ? 48.960 -2.937  -55.733 1.00 36.62 ? 45  ALA B O     1 
ATOM   3077 C CB    . ALA B 1 54  ? 47.757 -3.290  -58.687 1.00 36.79 ? 45  ALA B CB    1 
ATOM   3078 N N     . LEU B 1 55  ? 48.098 -5.009  -55.954 1.00 36.69 ? 46  LEU B N     1 
ATOM   3079 C CA    . LEU B 1 55  ? 47.873 -5.158  -54.521 1.00 34.88 ? 46  LEU B CA    1 
ATOM   3080 C C     . LEU B 1 55  ? 49.193 -5.218  -53.762 1.00 36.95 ? 46  LEU B C     1 
ATOM   3081 O O     . LEU B 1 55  ? 49.312 -4.657  -52.666 1.00 40.12 ? 46  LEU B O     1 
ATOM   3082 C CB    . LEU B 1 55  ? 47.039 -6.410  -54.249 1.00 31.55 ? 46  LEU B CB    1 
ATOM   3083 C CG    . LEU B 1 55  ? 45.516 -6.254  -54.261 1.00 32.87 ? 46  LEU B CG    1 
ATOM   3084 C CD1   . LEU B 1 55  ? 45.002 -5.983  -55.669 1.00 23.94 ? 46  LEU B CD1   1 
ATOM   3085 C CD2   . LEU B 1 55  ? 44.848 -7.488  -53.674 1.00 30.59 ? 46  LEU B CD2   1 
ATOM   3086 N N     . GLY B 1 56  ? 50.195 -5.894  -54.329 1.00 37.98 ? 47  GLY B N     1 
ATOM   3087 C CA    . GLY B 1 56  ? 51.497 -5.944  -53.684 1.00 39.29 ? 47  GLY B CA    1 
ATOM   3088 C C     . GLY B 1 56  ? 52.119 -4.570  -53.532 1.00 38.37 ? 47  GLY B C     1 
ATOM   3089 O O     . GLY B 1 56  ? 52.610 -4.209  -52.460 1.00 42.60 ? 47  GLY B O     1 
ATOM   3090 N N     . GLU B 1 57  ? 52.098 -3.780  -54.606 1.00 36.64 ? 48  GLU B N     1 
ATOM   3091 C CA    . GLU B 1 57  ? 52.631 -2.424  -54.537 1.00 34.45 ? 48  GLU B CA    1 
ATOM   3092 C C     . GLU B 1 57  ? 51.832 -1.571  -53.560 1.00 36.11 ? 48  GLU B C     1 
ATOM   3093 O O     . GLU B 1 57  ? 52.404 -0.777  -52.803 1.00 37.73 ? 48  GLU B O     1 
ATOM   3094 C CB    . GLU B 1 57  ? 52.626 -1.797  -55.932 1.00 39.79 ? 48  GLU B CB    1 
ATOM   3095 C CG    . GLU B 1 57  ? 52.702 -0.283  -55.943 1.00 39.72 ? 48  GLU B CG    1 
ATOM   3096 C CD    . GLU B 1 57  ? 53.555 0.246   -57.077 1.00 50.90 ? 48  GLU B CD    1 
ATOM   3097 O OE1   . GLU B 1 57  ? 53.235 -0.048  -58.248 1.00 51.30 ? 48  GLU B OE1   1 
ATOM   3098 O OE2   . GLU B 1 57  ? 54.544 0.956   -56.798 1.00 58.28 ? 48  GLU B OE2   1 
ATOM   3099 N N     . TYR B 1 58  ? 50.508 -1.735  -53.555 1.00 30.80 ? 49  TYR B N     1 
ATOM   3100 C CA    . TYR B 1 58  ? 49.647 -0.938  -52.689 1.00 34.38 ? 49  TYR B CA    1 
ATOM   3101 C C     . TYR B 1 58  ? 49.901 -1.240  -51.216 1.00 37.11 ? 49  TYR B C     1 
ATOM   3102 O O     . TYR B 1 58  ? 49.973 -0.320  -50.392 1.00 28.49 ? 49  TYR B O     1 
ATOM   3103 C CB    . TYR B 1 58  ? 48.184 -1.190  -53.059 1.00 35.76 ? 49  TYR B CB    1 
ATOM   3104 C CG    . TYR B 1 58  ? 47.163 -0.714  -52.050 1.00 32.61 ? 49  TYR B CG    1 
ATOM   3105 C CD1   . TYR B 1 58  ? 46.739 0.608   -52.031 1.00 33.55 ? 49  TYR B CD1   1 
ATOM   3106 C CD2   . TYR B 1 58  ? 46.602 -1.596  -51.134 1.00 35.63 ? 49  TYR B CD2   1 
ATOM   3107 C CE1   . TYR B 1 58  ? 45.796 1.045   -51.117 1.00 31.33 ? 49  TYR B CE1   1 
ATOM   3108 C CE2   . TYR B 1 58  ? 45.660 -1.169  -50.216 1.00 33.46 ? 49  TYR B CE2   1 
ATOM   3109 C CZ    . TYR B 1 58  ? 45.260 0.151   -50.213 1.00 35.24 ? 49  TYR B CZ    1 
ATOM   3110 O OH    . TYR B 1 58  ? 44.320 0.578   -49.304 1.00 43.83 ? 49  TYR B OH    1 
ATOM   3111 N N     . TYR B 1 59  ? 50.043 -2.519  -50.862 1.00 29.93 ? 50  TYR B N     1 
ATOM   3112 C CA    . TYR B 1 59  ? 50.285 -2.864  -49.466 1.00 33.24 ? 50  TYR B CA    1 
ATOM   3113 C C     . TYR B 1 59  ? 51.730 -2.601  -49.058 1.00 39.18 ? 50  TYR B C     1 
ATOM   3114 O O     . TYR B 1 59  ? 51.995 -2.316  -47.884 1.00 31.12 ? 50  TYR B O     1 
ATOM   3115 C CB    . TYR B 1 59  ? 49.907 -4.326  -49.209 1.00 27.84 ? 50  TYR B CB    1 
ATOM   3116 C CG    . TYR B 1 59  ? 48.409 -4.548  -49.130 1.00 34.48 ? 50  TYR B CG    1 
ATOM   3117 C CD1   . TYR B 1 59  ? 47.655 -3.970  -48.117 1.00 36.50 ? 50  TYR B CD1   1 
ATOM   3118 C CD2   . TYR B 1 59  ? 47.747 -5.320  -50.077 1.00 31.48 ? 50  TYR B CD2   1 
ATOM   3119 C CE1   . TYR B 1 59  ? 46.287 -4.159  -48.045 1.00 30.18 ? 50  TYR B CE1   1 
ATOM   3120 C CE2   . TYR B 1 59  ? 46.379 -5.513  -50.013 1.00 33.28 ? 50  TYR B CE2   1 
ATOM   3121 C CZ    . TYR B 1 59  ? 45.655 -4.929  -48.993 1.00 31.21 ? 50  TYR B CZ    1 
ATOM   3122 O OH    . TYR B 1 59  ? 44.292 -5.116  -48.921 1.00 42.02 ? 50  TYR B OH    1 
ATOM   3123 N N     . GLU B 1 60  ? 52.669 -2.675  -50.005 1.00 35.92 ? 51  GLU B N     1 
ATOM   3124 C CA    . GLU B 1 60  ? 54.061 -2.372  -49.688 1.00 43.34 ? 51  GLU B CA    1 
ATOM   3125 C C     . GLU B 1 60  ? 54.263 -0.888  -49.409 1.00 38.59 ? 51  GLU B C     1 
ATOM   3126 O O     . GLU B 1 60  ? 55.119 -0.524  -48.595 1.00 38.23 ? 51  GLU B O     1 
ATOM   3127 C CB    . GLU B 1 60  ? 54.975 -2.826  -50.826 1.00 34.63 ? 51  GLU B CB    1 
ATOM   3128 N N     . GLN B 1 61  ? 53.489 -0.021  -50.070 1.00 33.87 ? 52  GLN B N     1 
ATOM   3129 C CA    . GLN B 1 61  ? 53.614 1.413   -49.831 1.00 37.68 ? 52  GLN B CA    1 
ATOM   3130 C C     . GLN B 1 61  ? 53.219 1.784   -48.409 1.00 38.48 ? 52  GLN B C     1 
ATOM   3131 O O     . GLN B 1 61  ? 53.782 2.723   -47.836 1.00 41.05 ? 52  GLN B O     1 
ATOM   3132 C CB    . GLN B 1 61  ? 52.757 2.197   -50.827 1.00 34.01 ? 52  GLN B CB    1 
ATOM   3133 C CG    . GLN B 1 61  ? 53.355 2.318   -52.218 1.00 35.20 ? 52  GLN B CG    1 
ATOM   3134 C CD    . GLN B 1 61  ? 52.444 3.061   -53.179 1.00 38.90 ? 52  GLN B CD    1 
ATOM   3135 O OE1   . GLN B 1 61  ? 51.275 3.312   -52.881 1.00 39.84 ? 52  GLN B OE1   1 
ATOM   3136 N NE2   . GLN B 1 61  ? 52.976 3.412   -54.344 1.00 44.46 ? 52  GLN B NE2   1 
ATOM   3137 N N     . ARG B 1 62  ? 52.265 1.062   -47.825 1.00 35.91 ? 53  ARG B N     1 
ATOM   3138 C CA    . ARG B 1 62  ? 51.732 1.401   -46.513 1.00 39.79 ? 53  ARG B CA    1 
ATOM   3139 C C     . ARG B 1 62  ? 52.371 0.611   -45.381 1.00 42.91 ? 53  ARG B C     1 
ATOM   3140 O O     . ARG B 1 62  ? 52.178 0.968   -44.213 1.00 40.07 ? 53  ARG B O     1 
ATOM   3141 C CB    . ARG B 1 62  ? 50.213 1.189   -46.497 1.00 31.82 ? 53  ARG B CB    1 
ATOM   3142 C CG    . ARG B 1 62  ? 49.445 2.356   -47.086 1.00 38.58 ? 53  ARG B CG    1 
ATOM   3143 C CD    . ARG B 1 62  ? 48.400 1.924   -48.101 1.00 32.95 ? 53  ARG B CD    1 
ATOM   3144 N NE    . ARG B 1 62  ? 47.964 3.062   -48.902 1.00 37.52 ? 53  ARG B NE    1 
ATOM   3145 C CZ    . ARG B 1 62  ? 48.414 3.336   -50.118 1.00 36.60 ? 53  ARG B CZ    1 
ATOM   3146 N NH1   . ARG B 1 62  ? 49.263 2.532   -50.738 1.00 26.69 ? 53  ARG B NH1   1 
ATOM   3147 N NH2   . ARG B 1 62  ? 48.003 4.444   -50.728 1.00 30.20 ? 53  ARG B NH2   1 
ATOM   3148 N N     . ALA B 1 63  ? 53.131 -0.435  -45.696 1.00 43.82 ? 54  ALA B N     1 
ATOM   3149 C CA    . ALA B 1 63  ? 53.769 -1.240  -44.665 1.00 41.32 ? 54  ALA B CA    1 
ATOM   3150 C C     . ALA B 1 63  ? 54.903 -0.470  -44.002 1.00 41.65 ? 54  ALA B C     1 
ATOM   3151 O O     . ALA B 1 63  ? 55.659 0.250   -44.661 1.00 42.02 ? 54  ALA B O     1 
ATOM   3152 C CB    . ALA B 1 63  ? 54.301 -2.541  -45.265 1.00 40.89 ? 54  ALA B CB    1 
ATOM   3153 N N     . THR B 1 64  ? 55.012 -0.619  -42.684 1.00 35.44 ? 55  THR B N     1 
ATOM   3154 C CA    . THR B 1 64  ? 56.092 -0.028  -41.910 1.00 37.79 ? 55  THR B CA    1 
ATOM   3155 C C     . THR B 1 64  ? 56.668 -1.081  -40.974 1.00 38.57 ? 55  THR B C     1 
ATOM   3156 O O     . THR B 1 64  ? 56.050 -2.117  -40.716 1.00 39.34 ? 55  THR B O     1 
ATOM   3157 C CB    . THR B 1 64  ? 55.624 1.187   -41.093 1.00 38.92 ? 55  THR B CB    1 
ATOM   3158 O OG1   . THR B 1 64  ? 54.542 0.805   -40.235 1.00 35.11 ? 55  THR B OG1   1 
ATOM   3159 C CG2   . THR B 1 64  ? 55.170 2.312   -42.011 1.00 37.64 ? 55  THR B CG2   1 
ATOM   3160 N N     . ALA B 1 65  ? 57.869 -0.805  -40.469 1.00 41.00 ? 56  ALA B N     1 
ATOM   3161 C CA    . ALA B 1 65  ? 58.516 -1.713  -39.531 1.00 42.79 ? 56  ALA B CA    1 
ATOM   3162 C C     . ALA B 1 65  ? 57.706 -1.803  -38.244 1.00 38.86 ? 56  ALA B C     1 
ATOM   3163 O O     . ALA B 1 65  ? 57.515 -0.802  -37.547 1.00 36.34 ? 56  ALA B O     1 
ATOM   3164 C CB    . ALA B 1 65  ? 59.941 -1.241  -39.242 1.00 36.83 ? 56  ALA B CB    1 
ATOM   3165 N N     . GLY B 1 66  ? 57.223 -3.005  -37.936 1.00 42.69 ? 57  GLY B N     1 
ATOM   3166 C CA    . GLY B 1 66  ? 56.374 -3.198  -36.779 1.00 39.91 ? 57  GLY B CA    1 
ATOM   3167 C C     . GLY B 1 66  ? 54.957 -2.694  -36.934 1.00 40.20 ? 57  GLY B C     1 
ATOM   3168 O O     . GLY B 1 66  ? 54.218 -2.657  -35.944 1.00 36.44 ? 57  GLY B O     1 
ATOM   3169 N N     . GLY B 1 67  ? 54.555 -2.293  -38.140 1.00 39.31 ? 58  GLY B N     1 
ATOM   3170 C CA    . GLY B 1 67  ? 53.189 -1.859  -38.356 1.00 26.45 ? 58  GLY B CA    1 
ATOM   3171 C C     . GLY B 1 67  ? 52.258 -3.025  -38.630 1.00 32.07 ? 58  GLY B C     1 
ATOM   3172 O O     . GLY B 1 67  ? 52.648 -4.054  -39.180 1.00 32.06 ? 58  GLY B O     1 
ATOM   3173 N N     . PHE B 1 68  ? 51.003 -2.853  -38.228 1.00 37.63 ? 59  PHE B N     1 
ATOM   3174 C CA    . PHE B 1 68  ? 49.976 -3.872  -38.393 1.00 35.75 ? 59  PHE B CA    1 
ATOM   3175 C C     . PHE B 1 68  ? 49.062 -3.486  -39.548 1.00 38.30 ? 59  PHE B C     1 
ATOM   3176 O O     . PHE B 1 68  ? 48.519 -2.377  -39.571 1.00 35.28 ? 59  PHE B O     1 
ATOM   3177 C CB    . PHE B 1 68  ? 49.169 -4.043  -37.105 1.00 33.83 ? 59  PHE B CB    1 
ATOM   3178 C CG    . PHE B 1 68  ? 48.075 -5.070  -37.201 1.00 35.01 ? 59  PHE B CG    1 
ATOM   3179 C CD1   . PHE B 1 68  ? 48.244 -6.218  -37.955 1.00 35.92 ? 59  PHE B CD1   1 
ATOM   3180 C CD2   . PHE B 1 68  ? 46.875 -4.886  -36.532 1.00 37.16 ? 59  PHE B CD2   1 
ATOM   3181 C CE1   . PHE B 1 68  ? 47.239 -7.158  -38.047 1.00 33.33 ? 59  PHE B CE1   1 
ATOM   3182 C CE2   . PHE B 1 68  ? 45.865 -5.825  -36.617 1.00 36.40 ? 59  PHE B CE2   1 
ATOM   3183 C CZ    . PHE B 1 68  ? 46.047 -6.962  -37.377 1.00 39.21 ? 59  PHE B CZ    1 
ATOM   3184 N N     . LEU B 1 69  ? 48.900 -4.400  -40.502 1.00 37.41 ? 60  LEU B N     1 
ATOM   3185 C CA    . LEU B 1 69  ? 48.050 -4.189  -41.665 1.00 37.22 ? 60  LEU B CA    1 
ATOM   3186 C C     . LEU B 1 69  ? 46.953 -5.243  -41.700 1.00 34.06 ? 60  LEU B C     1 
ATOM   3187 O O     . LEU B 1 69  ? 47.177 -6.400  -41.332 1.00 31.19 ? 60  LEU B O     1 
ATOM   3188 C CB    . LEU B 1 69  ? 48.854 -4.252  -42.970 1.00 34.12 ? 60  LEU B CB    1 
ATOM   3189 C CG    . LEU B 1 69  ? 50.106 -3.388  -43.122 1.00 38.15 ? 60  LEU B CG    1 
ATOM   3190 C CD1   . LEU B 1 69  ? 50.777 -3.682  -44.453 1.00 38.64 ? 60  LEU B CD1   1 
ATOM   3191 C CD2   . LEU B 1 69  ? 49.769 -1.913  -43.013 1.00 37.75 ? 60  LEU B CD2   1 
ATOM   3192 N N     . ILE B 1 70  ? 45.766 -4.836  -42.136 1.00 32.30 ? 61  ILE B N     1 
ATOM   3193 C CA    . ILE B 1 70  ? 44.667 -5.754  -42.407 1.00 31.98 ? 61  ILE B CA    1 
ATOM   3194 C C     . ILE B 1 70  ? 44.271 -5.585  -43.864 1.00 32.08 ? 61  ILE B C     1 
ATOM   3195 O O     . ILE B 1 70  ? 44.001 -4.464  -44.313 1.00 27.17 ? 61  ILE B O     1 
ATOM   3196 C CB    . ILE B 1 70  ? 43.463 -5.512  -41.482 1.00 28.17 ? 61  ILE B CB    1 
ATOM   3197 C CG1   . ILE B 1 70  ? 43.904 -5.512  -40.017 1.00 31.88 ? 61  ILE B CG1   1 
ATOM   3198 C CG2   . ILE B 1 70  ? 42.403 -6.580  -41.708 1.00 25.83 ? 61  ILE B CG2   1 
ATOM   3199 C CD1   . ILE B 1 70  ? 42.806 -5.121  -39.062 1.00 31.20 ? 61  ILE B CD1   1 
ATOM   3200 N N     . THR B 1 71  ? 44.243 -6.692  -44.601 1.00 31.05 ? 62  THR B N     1 
ATOM   3201 C CA    . THR B 1 71  ? 43.930 -6.631  -46.017 1.00 30.14 ? 62  THR B CA    1 
ATOM   3202 C C     . THR B 1 71  ? 42.451 -6.328  -46.230 1.00 35.06 ? 62  THR B C     1 
ATOM   3203 O O     . THR B 1 71  ? 41.622 -6.430  -45.321 1.00 33.90 ? 62  THR B O     1 
ATOM   3204 C CB    . THR B 1 71  ? 44.278 -7.946  -46.713 1.00 30.71 ? 62  THR B CB    1 
ATOM   3205 O OG1   . THR B 1 71  ? 43.290 -8.930  -46.383 1.00 31.21 ? 62  THR B OG1   1 
ATOM   3206 C CG2   . THR B 1 71  ? 45.645 -8.435  -46.280 1.00 30.83 ? 62  THR B CG2   1 
ATOM   3207 N N     . GLU B 1 72  ? 42.133 -5.957  -47.466 1.00 35.52 ? 63  GLU B N     1 
ATOM   3208 C CA    . GLU B 1 72  ? 40.753 -5.824  -47.901 1.00 24.07 ? 63  GLU B CA    1 
ATOM   3209 C C     . GLU B 1 72  ? 39.980 -7.113  -47.636 1.00 28.62 ? 63  GLU B C     1 
ATOM   3210 O O     . GLU B 1 72  ? 40.553 -8.191  -47.446 1.00 28.77 ? 63  GLU B O     1 
ATOM   3211 C CB    . GLU B 1 72  ? 40.702 -5.501  -49.392 1.00 26.93 ? 63  GLU B CB    1 
ATOM   3212 C CG    . GLU B 1 72  ? 41.312 -6.593  -50.254 1.00 28.79 ? 63  GLU B CG    1 
ATOM   3213 C CD    . GLU B 1 72  ? 42.064 -6.053  -51.452 1.00 37.34 ? 63  GLU B CD    1 
ATOM   3214 O OE1   . GLU B 1 72  ? 43.251 -5.690  -51.297 1.00 38.18 ? 63  GLU B OE1   1 
ATOM   3215 O OE2   . GLU B 1 72  ? 41.466 -5.982  -52.544 1.00 33.84 ? 63  GLU B OE2   1 
ATOM   3216 N N     . GLY B 1 73  ? 38.655 -6.987  -47.623 1.00 26.98 ? 64  GLY B N     1 
ATOM   3217 C CA    . GLY B 1 73  ? 37.780 -8.133  -47.485 1.00 27.70 ? 64  GLY B CA    1 
ATOM   3218 C C     . GLY B 1 73  ? 38.040 -9.179  -48.545 1.00 31.07 ? 64  GLY B C     1 
ATOM   3219 O O     . GLY B 1 73  ? 38.116 -8.861  -49.737 1.00 29.58 ? 64  GLY B O     1 
ATOM   3220 N N     . THR B 1 74  ? 38.178 -10.432 -48.123 1.00 32.40 ? 65  THR B N     1 
ATOM   3221 C CA    . THR B 1 74  ? 38.615 -11.517 -48.991 1.00 33.09 ? 65  THR B CA    1 
ATOM   3222 C C     . THR B 1 74  ? 37.581 -12.632 -48.975 1.00 33.88 ? 65  THR B C     1 
ATOM   3223 O O     . THR B 1 74  ? 37.146 -13.066 -47.902 1.00 30.51 ? 65  THR B O     1 
ATOM   3224 C CB    . THR B 1 74  ? 39.983 -12.042 -48.547 1.00 32.94 ? 65  THR B CB    1 
ATOM   3225 O OG1   . THR B 1 74  ? 40.896 -10.945 -48.436 1.00 27.22 ? 65  THR B OG1   1 
ATOM   3226 C CG2   . THR B 1 74  ? 40.529 -13.046 -49.546 1.00 27.44 ? 65  THR B CG2   1 
ATOM   3227 N N     . MET B 1 75  ? 37.190 -13.092 -50.163 1.00 28.90 ? 66  MET B N     1 
ATOM   3228 C CA    . MET B 1 75  ? 36.158 -14.112 -50.269 1.00 35.71 ? 66  MET B CA    1 
ATOM   3229 C C     . MET B 1 75  ? 36.629 -15.441 -49.691 1.00 35.09 ? 66  MET B C     1 
ATOM   3230 O O     . MET B 1 75  ? 37.809 -15.796 -49.751 1.00 34.86 ? 66  MET B O     1 
ATOM   3231 C CB    . MET B 1 75  ? 35.727 -14.314 -51.725 1.00 33.88 ? 66  MET B CB    1 
ATOM   3232 C CG    . MET B 1 75  ? 35.751 -13.068 -52.592 1.00 34.45 ? 66  MET B CG    1 
ATOM   3233 S SD    . MET B 1 75  ? 35.560 -13.447 -54.349 1.00 34.47 ? 66  MET B SD    1 
ATOM   3234 C CE    . MET B 1 75  ? 34.495 -14.881 -54.307 1.00 32.31 ? 66  MET B CE    1 
ATOM   3235 N N     . ILE B 1 76  ? 35.677 -16.179 -49.124 1.00 30.70 ? 67  ILE B N     1 
ATOM   3236 C CA    . ILE B 1 76  ? 35.934 -17.506 -48.578 1.00 32.19 ? 67  ILE B CA    1 
ATOM   3237 C C     . ILE B 1 76  ? 35.323 -18.607 -49.424 1.00 30.81 ? 67  ILE B C     1 
ATOM   3238 O O     . ILE B 1 76  ? 35.603 -19.790 -49.170 1.00 33.22 ? 67  ILE B O     1 
ATOM   3239 C CB    . ILE B 1 76  ? 35.435 -17.624 -47.122 1.00 29.01 ? 67  ILE B CB    1 
ATOM   3240 C CG1   . ILE B 1 76  ? 33.911 -17.506 -47.068 1.00 23.29 ? 67  ILE B CG1   1 
ATOM   3241 C CG2   . ILE B 1 76  ? 36.087 -16.565 -46.244 1.00 26.95 ? 67  ILE B CG2   1 
ATOM   3242 C CD1   . ILE B 1 76  ? 33.315 -17.991 -45.768 1.00 35.95 ? 67  ILE B CD1   1 
ATOM   3243 N N     . SER B 1 77  ? 34.502 -18.264 -50.411 1.00 36.11 ? 68  SER B N     1 
ATOM   3244 C CA    . SER B 1 77  ? 33.840 -19.238 -51.265 1.00 32.94 ? 68  SER B CA    1 
ATOM   3245 C C     . SER B 1 77  ? 33.344 -18.514 -52.508 1.00 35.34 ? 68  SER B C     1 
ATOM   3246 O O     . SER B 1 77  ? 33.241 -17.281 -52.508 1.00 36.24 ? 68  SER B O     1 
ATOM   3247 C CB    . SER B 1 77  ? 32.674 -19.922 -50.532 1.00 34.66 ? 68  SER B CB    1 
ATOM   3248 O OG    . SER B 1 77  ? 31.496 -19.139 -50.604 1.00 37.26 ? 68  SER B OG    1 
ATOM   3249 N N     . PRO B 1 78  ? 33.045 -19.246 -53.586 1.00 35.45 ? 69  PRO B N     1 
ATOM   3250 C CA    . PRO B 1 78  ? 32.549 -18.585 -54.806 1.00 40.85 ? 69  PRO B CA    1 
ATOM   3251 C C     . PRO B 1 78  ? 31.234 -17.840 -54.622 1.00 39.20 ? 69  PRO B C     1 
ATOM   3252 O O     . PRO B 1 78  ? 30.865 -17.061 -55.509 1.00 37.67 ? 69  PRO B O     1 
ATOM   3253 C CB    . PRO B 1 78  ? 32.393 -19.747 -55.797 1.00 38.76 ? 69  PRO B CB    1 
ATOM   3254 C CG    . PRO B 1 78  ? 33.345 -20.786 -55.309 1.00 39.89 ? 69  PRO B CG    1 
ATOM   3255 C CD    . PRO B 1 78  ? 33.341 -20.672 -53.813 1.00 34.96 ? 69  PRO B CD    1 
ATOM   3256 N N     . THR B 1 79  ? 30.521 -18.043 -53.514 1.00 37.60 ? 70  THR B N     1 
ATOM   3257 C CA    . THR B 1 79  ? 29.242 -17.384 -53.280 1.00 38.22 ? 70  THR B CA    1 
ATOM   3258 C C     . THR B 1 79  ? 29.336 -16.254 -52.261 1.00 30.84 ? 70  THR B C     1 
ATOM   3259 O O     . THR B 1 79  ? 28.305 -15.686 -51.886 1.00 29.63 ? 70  THR B O     1 
ATOM   3260 C CB    . THR B 1 79  ? 28.193 -18.405 -52.829 1.00 44.42 ? 70  THR B CB    1 
ATOM   3261 O OG1   . THR B 1 79  ? 28.450 -18.798 -51.474 1.00 37.44 ? 70  THR B OG1   1 
ATOM   3262 C CG2   . THR B 1 79  ? 28.222 -19.637 -53.725 1.00 36.13 ? 70  THR B CG2   1 
ATOM   3263 N N     . SER B 1 80  ? 30.541 -15.902 -51.817 1.00 30.79 ? 71  SER B N     1 
ATOM   3264 C CA    . SER B 1 80  ? 30.718 -14.931 -50.744 1.00 36.44 ? 71  SER B CA    1 
ATOM   3265 C C     . SER B 1 80  ? 30.978 -13.513 -51.238 1.00 32.93 ? 71  SER B C     1 
ATOM   3266 O O     . SER B 1 80  ? 31.123 -12.606 -50.412 1.00 34.61 ? 71  SER B O     1 
ATOM   3267 C CB    . SER B 1 80  ? 31.865 -15.367 -49.823 1.00 35.25 ? 71  SER B CB    1 
ATOM   3268 O OG    . SER B 1 80  ? 33.072 -15.528 -50.543 1.00 35.75 ? 71  SER B OG    1 
ATOM   3269 N N     . ALA B 1 81  ? 31.033 -13.291 -52.548 1.00 33.07 ? 72  ALA B N     1 
ATOM   3270 C CA    . ALA B 1 81  ? 31.359 -11.978 -53.085 1.00 26.54 ? 72  ALA B CA    1 
ATOM   3271 C C     . ALA B 1 81  ? 30.105 -11.132 -53.277 1.00 32.60 ? 72  ALA B C     1 
ATOM   3272 O O     . ALA B 1 81  ? 29.006 -11.649 -53.503 1.00 25.08 ? 72  ALA B O     1 
ATOM   3273 C CB    . ALA B 1 81  ? 32.102 -12.103 -54.417 1.00 35.91 ? 72  ALA B CB    1 
ATOM   3274 N N     . GLY B 1 82  ? 30.288 -9.815  -53.182 1.00 27.08 ? 73  GLY B N     1 
ATOM   3275 C CA    . GLY B 1 82  ? 29.218 -8.857  -53.383 1.00 23.25 ? 73  GLY B CA    1 
ATOM   3276 C C     . GLY B 1 82  ? 29.733 -7.546  -53.943 1.00 26.61 ? 73  GLY B C     1 
ATOM   3277 O O     . GLY B 1 82  ? 28.983 -6.576  -54.084 1.00 29.12 ? 73  GLY B O     1 
ATOM   3278 N N     . PHE B 1 83  ? 31.023 -7.508  -54.247 1.00 29.09 ? 74  PHE B N     1 
ATOM   3279 C CA    . PHE B 1 83  ? 31.690 -6.402  -54.912 1.00 30.49 ? 74  PHE B CA    1 
ATOM   3280 C C     . PHE B 1 83  ? 32.430 -6.953  -56.120 1.00 34.89 ? 74  PHE B C     1 
ATOM   3281 O O     . PHE B 1 83  ? 32.728 -8.151  -56.178 1.00 28.41 ? 74  PHE B O     1 
ATOM   3282 C CB    . PHE B 1 83  ? 32.675 -5.693  -53.970 1.00 27.58 ? 74  PHE B CB    1 
ATOM   3283 C CG    . PHE B 1 83  ? 32.059 -4.584  -53.160 1.00 35.84 ? 74  PHE B CG    1 
ATOM   3284 C CD1   . PHE B 1 83  ? 31.252 -4.869  -52.071 1.00 30.62 ? 74  PHE B CD1   1 
ATOM   3285 C CD2   . PHE B 1 83  ? 32.300 -3.258  -53.481 1.00 32.82 ? 74  PHE B CD2   1 
ATOM   3286 C CE1   . PHE B 1 83  ? 30.692 -3.852  -51.319 1.00 37.16 ? 74  PHE B CE1   1 
ATOM   3287 C CE2   . PHE B 1 83  ? 31.742 -2.236  -52.734 1.00 37.87 ? 74  PHE B CE2   1 
ATOM   3288 C CZ    . PHE B 1 83  ? 30.937 -2.535  -51.651 1.00 37.30 ? 74  PHE B CZ    1 
ATOM   3289 N N     . PRO B 1 84  ? 32.739 -6.112  -57.106 1.00 30.72 ? 75  PRO B N     1 
ATOM   3290 C CA    . PRO B 1 84  ? 33.469 -6.612  -58.275 1.00 28.50 ? 75  PRO B CA    1 
ATOM   3291 C C     . PRO B 1 84  ? 34.963 -6.699  -58.002 1.00 34.04 ? 75  PRO B C     1 
ATOM   3292 O O     . PRO B 1 84  ? 35.558 -5.817  -57.376 1.00 28.03 ? 75  PRO B O     1 
ATOM   3293 C CB    . PRO B 1 84  ? 33.156 -5.574  -59.359 1.00 29.77 ? 75  PRO B CB    1 
ATOM   3294 C CG    . PRO B 1 84  ? 32.904 -4.312  -58.608 1.00 34.36 ? 75  PRO B CG    1 
ATOM   3295 C CD    . PRO B 1 84  ? 32.427 -4.676  -57.222 1.00 26.23 ? 75  PRO B CD    1 
ATOM   3296 N N     . HIS B 1 85  ? 35.559 -7.800  -58.460 1.00 30.50 ? 76  HIS B N     1 
ATOM   3297 C CA    . HIS B 1 85  ? 37.010 -7.988  -58.448 1.00 27.46 ? 76  HIS B CA    1 
ATOM   3298 C C     . HIS B 1 85  ? 37.593 -7.840  -57.044 1.00 34.01 ? 76  HIS B C     1 
ATOM   3299 O O     . HIS B 1 85  ? 38.576 -7.129  -56.822 1.00 35.04 ? 76  HIS B O     1 
ATOM   3300 C CB    . HIS B 1 85  ? 37.682 -7.032  -59.434 1.00 33.02 ? 76  HIS B CB    1 
ATOM   3301 C CG    . HIS B 1 85  ? 37.140 -7.138  -60.824 1.00 36.17 ? 76  HIS B CG    1 
ATOM   3302 N ND1   . HIS B 1 85  ? 37.292 -8.272  -61.592 1.00 36.84 ? 76  HIS B ND1   1 
ATOM   3303 C CD2   . HIS B 1 85  ? 36.442 -6.260  -61.582 1.00 37.03 ? 76  HIS B CD2   1 
ATOM   3304 C CE1   . HIS B 1 85  ? 36.712 -8.088  -62.764 1.00 39.47 ? 76  HIS B CE1   1 
ATOM   3305 N NE2   . HIS B 1 85  ? 36.189 -6.875  -62.785 1.00 40.81 ? 76  HIS B NE2   1 
ATOM   3306 N N     . VAL B 1 86  ? 36.974 -8.525  -56.088 1.00 30.39 ? 77  VAL B N     1 
ATOM   3307 C CA    . VAL B 1 86  ? 37.511 -8.614  -54.734 1.00 31.33 ? 77  VAL B CA    1 
ATOM   3308 C C     . VAL B 1 86  ? 38.326 -9.898  -54.645 1.00 32.93 ? 77  VAL B C     1 
ATOM   3309 O O     . VAL B 1 86  ? 37.942 -10.913 -55.242 1.00 30.07 ? 77  VAL B O     1 
ATOM   3310 C CB    . VAL B 1 86  ? 36.395 -8.576  -53.680 1.00 32.90 ? 77  VAL B CB    1 
ATOM   3311 C CG1   . VAL B 1 86  ? 35.820 -7.179  -53.593 1.00 33.92 ? 77  VAL B CG1   1 
ATOM   3312 C CG2   . VAL B 1 86  ? 35.305 -9.587  -54.014 1.00 32.38 ? 77  VAL B CG2   1 
ATOM   3313 N N     . PRO B 1 87  ? 39.449 -9.905  -53.930 1.00 29.88 ? 78  PRO B N     1 
ATOM   3314 C CA    . PRO B 1 87  ? 40.301 -11.096 -53.922 1.00 29.88 ? 78  PRO B CA    1 
ATOM   3315 C C     . PRO B 1 87  ? 39.672 -12.230 -53.134 1.00 29.20 ? 78  PRO B C     1 
ATOM   3316 O O     . PRO B 1 87  ? 38.867 -12.020 -52.223 1.00 36.24 ? 78  PRO B O     1 
ATOM   3317 C CB    . PRO B 1 87  ? 41.591 -10.605 -53.254 1.00 30.26 ? 78  PRO B CB    1 
ATOM   3318 C CG    . PRO B 1 87  ? 41.147 -9.491  -52.372 1.00 29.05 ? 78  PRO B CG    1 
ATOM   3319 C CD    . PRO B 1 87  ? 39.978 -8.834  -53.067 1.00 28.53 ? 78  PRO B CD    1 
ATOM   3320 N N     . GLY B 1 88  ? 40.052 -13.452 -53.505 1.00 37.88 ? 79  GLY B N     1 
ATOM   3321 C CA    . GLY B 1 88  ? 39.656 -14.644 -52.793 1.00 26.71 ? 79  GLY B CA    1 
ATOM   3322 C C     . GLY B 1 88  ? 40.849 -15.313 -52.126 1.00 33.21 ? 79  GLY B C     1 
ATOM   3323 O O     . GLY B 1 88  ? 42.006 -14.936 -52.316 1.00 28.01 ? 79  GLY B O     1 
ATOM   3324 N N     . ILE B 1 89  ? 40.538 -16.327 -51.321 1.00 34.06 ? 80  ILE B N     1 
ATOM   3325 C CA    . ILE B 1 89  ? 41.552 -17.094 -50.607 1.00 31.45 ? 80  ILE B CA    1 
ATOM   3326 C C     . ILE B 1 89  ? 41.064 -18.537 -50.500 1.00 34.79 ? 80  ILE B C     1 
ATOM   3327 O O     . ILE B 1 89  ? 41.496 -19.297 -49.625 1.00 43.12 ? 80  ILE B O     1 
ATOM   3328 C CB    . ILE B 1 89  ? 41.849 -16.459 -49.230 1.00 34.42 ? 80  ILE B CB    1 
ATOM   3329 C CG1   . ILE B 1 89  ? 43.126 -17.027 -48.598 1.00 38.39 ? 80  ILE B CG1   1 
ATOM   3330 C CG2   . ILE B 1 89  ? 40.660 -16.596 -48.287 1.00 30.81 ? 80  ILE B CG2   1 
ATOM   3331 C CD1   . ILE B 1 89  ? 44.322 -17.014 -49.507 1.00 38.16 ? 80  ILE B CD1   1 
ATOM   3332 N N     . PHE B 1 90  ? 40.172 -18.935 -51.412 1.00 31.69 ? 81  PHE B N     1 
ATOM   3333 C CA    . PHE B 1 90  ? 39.611 -20.279 -51.405 1.00 36.85 ? 81  PHE B CA    1 
ATOM   3334 C C     . PHE B 1 90  ? 40.156 -21.181 -52.507 1.00 38.23 ? 81  PHE B C     1 
ATOM   3335 O O     . PHE B 1 90  ? 39.904 -22.390 -52.466 1.00 37.26 ? 81  PHE B O     1 
ATOM   3336 C CB    . PHE B 1 90  ? 38.074 -20.224 -51.502 1.00 32.08 ? 81  PHE B CB    1 
ATOM   3337 C CG    . PHE B 1 90  ? 37.561 -19.474 -52.700 1.00 37.10 ? 81  PHE B CG    1 
ATOM   3338 C CD1   . PHE B 1 90  ? 37.383 -18.102 -52.653 1.00 34.48 ? 81  PHE B CD1   1 
ATOM   3339 C CD2   . PHE B 1 90  ? 37.243 -20.145 -53.871 1.00 35.07 ? 81  PHE B CD2   1 
ATOM   3340 C CE1   . PHE B 1 90  ? 36.911 -17.410 -53.752 1.00 32.59 ? 81  PHE B CE1   1 
ATOM   3341 C CE2   . PHE B 1 90  ? 36.770 -19.458 -54.976 1.00 35.63 ? 81  PHE B CE2   1 
ATOM   3342 C CZ    . PHE B 1 90  ? 36.604 -18.089 -54.916 1.00 35.79 ? 81  PHE B CZ    1 
ATOM   3343 N N     . THR B 1 91  ? 40.886 -20.642 -53.480 1.00 39.69 ? 82  THR B N     1 
ATOM   3344 C CA    . THR B 1 91  ? 41.572 -21.452 -54.477 1.00 38.30 ? 82  THR B CA    1 
ATOM   3345 C C     . THR B 1 91  ? 43.072 -21.441 -54.214 1.00 40.10 ? 82  THR B C     1 
ATOM   3346 O O     . THR B 1 91  ? 43.610 -20.531 -53.576 1.00 36.95 ? 82  THR B O     1 
ATOM   3347 C CB    . THR B 1 91  ? 41.305 -20.958 -55.907 1.00 39.66 ? 82  THR B CB    1 
ATOM   3348 O OG1   . THR B 1 91  ? 42.043 -19.754 -56.149 1.00 35.59 ? 82  THR B OG1   1 
ATOM   3349 C CG2   . THR B 1 91  ? 39.826 -20.703 -56.134 1.00 36.56 ? 82  THR B CG2   1 
ATOM   3350 N N     . LYS B 1 92  ? 43.746 -22.477 -54.722 1.00 39.08 ? 83  LYS B N     1 
ATOM   3351 C CA    . LYS B 1 92  ? 45.196 -22.552 -54.585 1.00 39.88 ? 83  LYS B CA    1 
ATOM   3352 C C     . LYS B 1 92  ? 45.891 -21.485 -55.420 1.00 41.08 ? 83  LYS B C     1 
ATOM   3353 O O     . LYS B 1 92  ? 46.959 -20.999 -55.035 1.00 42.78 ? 83  LYS B O     1 
ATOM   3354 C CB    . LYS B 1 92  ? 45.694 -23.943 -54.980 1.00 35.45 ? 83  LYS B CB    1 
ATOM   3355 C CG    . LYS B 1 92  ? 45.435 -25.007 -53.929 1.00 43.13 ? 83  LYS B CG    1 
ATOM   3356 C CD    . LYS B 1 92  ? 46.139 -24.673 -52.620 1.00 40.38 ? 83  LYS B CD    1 
ATOM   3357 C CE    . LYS B 1 92  ? 45.615 -25.536 -51.482 1.00 56.57 ? 83  LYS B CE    1 
ATOM   3358 N NZ    . LYS B 1 92  ? 46.550 -25.574 -50.325 1.00 59.49 ? 83  LYS B NZ    1 
ATOM   3359 N N     . GLU B 1 93  ? 45.305 -21.113 -56.560 1.00 41.11 ? 84  GLU B N     1 
ATOM   3360 C CA    . GLU B 1 93  ? 45.870 -20.035 -57.362 1.00 41.44 ? 84  GLU B CA    1 
ATOM   3361 C C     . GLU B 1 93  ? 45.869 -18.720 -56.593 1.00 42.22 ? 84  GLU B C     1 
ATOM   3362 O O     . GLU B 1 93  ? 46.820 -17.935 -56.686 1.00 44.62 ? 84  GLU B O     1 
ATOM   3363 C CB    . GLU B 1 93  ? 45.092 -19.898 -58.670 1.00 42.97 ? 84  GLU B CB    1 
ATOM   3364 C CG    . GLU B 1 93  ? 45.557 -18.757 -59.560 1.00 50.15 ? 84  GLU B CG    1 
ATOM   3365 C CD    . GLU B 1 93  ? 44.602 -18.492 -60.707 1.00 50.74 ? 84  GLU B CD    1 
ATOM   3366 O OE1   . GLU B 1 93  ? 43.458 -18.991 -60.657 1.00 56.62 ? 84  GLU B OE1   1 
ATOM   3367 O OE2   . GLU B 1 93  ? 44.994 -17.783 -61.657 1.00 69.48 ? 84  GLU B OE2   1 
ATOM   3368 N N     . GLN B 1 94  ? 44.810 -18.465 -55.819 1.00 35.88 ? 85  GLN B N     1 
ATOM   3369 C CA    . GLN B 1 94  ? 44.758 -17.246 -55.018 1.00 40.07 ? 85  GLN B CA    1 
ATOM   3370 C C     . GLN B 1 94  ? 45.802 -17.254 -53.911 1.00 39.47 ? 85  GLN B C     1 
ATOM   3371 O O     . GLN B 1 94  ? 46.344 -16.198 -53.566 1.00 36.48 ? 85  GLN B O     1 
ATOM   3372 C CB    . GLN B 1 94  ? 43.363 -17.067 -54.422 1.00 28.78 ? 85  GLN B CB    1 
ATOM   3373 C CG    . GLN B 1 94  ? 42.327 -16.588 -55.416 1.00 32.70 ? 85  GLN B CG    1 
ATOM   3374 C CD    . GLN B 1 94  ? 40.934 -17.066 -55.074 1.00 29.67 ? 85  GLN B CD    1 
ATOM   3375 O OE1   . GLN B 1 94  ? 40.723 -17.720 -54.053 1.00 36.37 ? 85  GLN B OE1   1 
ATOM   3376 N NE2   . GLN B 1 94  ? 39.970 -16.738 -55.927 1.00 34.41 ? 85  GLN B NE2   1 
ATOM   3377 N N     . VAL B 1 95  ? 46.093 -18.428 -53.345 1.00 39.60 ? 86  VAL B N     1 
ATOM   3378 C CA    . VAL B 1 95  ? 47.074 -18.521 -52.269 1.00 31.28 ? 86  VAL B CA    1 
ATOM   3379 C C     . VAL B 1 95  ? 48.463 -18.160 -52.779 1.00 37.88 ? 86  VAL B C     1 
ATOM   3380 O O     . VAL B 1 95  ? 49.212 -17.429 -52.119 1.00 37.17 ? 86  VAL B O     1 
ATOM   3381 C CB    . VAL B 1 95  ? 47.044 -19.929 -51.647 1.00 36.11 ? 86  VAL B CB    1 
ATOM   3382 C CG1   . VAL B 1 95  ? 48.278 -20.163 -50.789 1.00 38.85 ? 86  VAL B CG1   1 
ATOM   3383 C CG2   . VAL B 1 95  ? 45.779 -20.120 -50.828 1.00 39.47 ? 86  VAL B CG2   1 
ATOM   3384 N N     . ARG B 1 96  ? 48.829 -18.661 -53.962 1.00 34.65 ? 87  ARG B N     1 
ATOM   3385 C CA    . ARG B 1 96  ? 50.144 -18.355 -54.517 1.00 42.94 ? 87  ARG B CA    1 
ATOM   3386 C C     . ARG B 1 96  ? 50.270 -16.873 -54.858 1.00 38.31 ? 87  ARG B C     1 
ATOM   3387 O O     . ARG B 1 96  ? 51.334 -16.275 -54.660 1.00 44.68 ? 87  ARG B O     1 
ATOM   3388 C CB    . ARG B 1 96  ? 50.408 -19.223 -55.749 1.00 41.05 ? 87  ARG B CB    1 
ATOM   3389 C CG    . ARG B 1 96  ? 49.973 -20.672 -55.584 1.00 47.23 ? 87  ARG B CG    1 
ATOM   3390 C CD    . ARG B 1 96  ? 50.507 -21.563 -56.696 1.00 54.25 ? 87  ARG B CD    1 
ATOM   3391 N NE    . ARG B 1 96  ? 49.865 -21.286 -57.975 1.00 50.72 ? 87  ARG B NE    1 
ATOM   3392 C CZ    . ARG B 1 96  ? 48.870 -21.997 -58.489 1.00 49.55 ? 87  ARG B CZ    1 
ATOM   3393 N NH1   . ARG B 1 96  ? 48.368 -23.044 -57.854 1.00 46.87 ? 87  ARG B NH1   1 
ATOM   3394 N NH2   . ARG B 1 96  ? 48.365 -21.648 -59.669 1.00 46.74 ? 87  ARG B NH2   1 
ATOM   3395 N N     . GLU B 1 97  ? 49.198 -16.261 -55.366 1.00 31.13 ? 88  GLU B N     1 
ATOM   3396 C CA    . GLU B 1 97  ? 49.241 -14.829 -55.646 1.00 38.57 ? 88  GLU B CA    1 
ATOM   3397 C C     . GLU B 1 97  ? 49.250 -14.018 -54.356 1.00 37.28 ? 88  GLU B C     1 
ATOM   3398 O O     . GLU B 1 97  ? 49.906 -12.973 -54.279 1.00 35.22 ? 88  GLU B O     1 
ATOM   3399 C CB    . GLU B 1 97  ? 48.061 -14.429 -56.531 1.00 37.25 ? 88  GLU B CB    1 
ATOM   3400 C CG    . GLU B 1 97  ? 48.219 -14.834 -57.990 1.00 43.18 ? 88  GLU B CG    1 
ATOM   3401 C CD    . GLU B 1 97  ? 49.663 -14.804 -58.456 1.00 44.40 ? 88  GLU B CD    1 
ATOM   3402 O OE1   . GLU B 1 97  ? 50.240 -13.699 -58.540 1.00 54.14 ? 88  GLU B OE1   1 
ATOM   3403 O OE2   . GLU B 1 97  ? 50.220 -15.884 -58.745 1.00 49.47 ? 88  GLU B OE2   1 
ATOM   3404 N N     . TRP B 1 98  ? 48.533 -14.487 -53.331 1.00 38.33 ? 89  TRP B N     1 
ATOM   3405 C CA    . TRP B 1 98  ? 48.590 -13.832 -52.028 1.00 36.30 ? 89  TRP B CA    1 
ATOM   3406 C C     . TRP B 1 98  ? 49.977 -13.945 -51.406 1.00 39.81 ? 89  TRP B C     1 
ATOM   3407 O O     . TRP B 1 98  ? 50.411 -13.033 -50.692 1.00 35.12 ? 89  TRP B O     1 
ATOM   3408 C CB    . TRP B 1 98  ? 47.548 -14.436 -51.087 1.00 34.52 ? 89  TRP B CB    1 
ATOM   3409 C CG    . TRP B 1 98  ? 46.216 -13.744 -51.079 1.00 31.02 ? 89  TRP B CG    1 
ATOM   3410 C CD1   . TRP B 1 98  ? 45.004 -14.307 -51.354 1.00 31.30 ? 89  TRP B CD1   1 
ATOM   3411 C CD2   . TRP B 1 98  ? 45.957 -12.371 -50.759 1.00 33.48 ? 89  TRP B CD2   1 
ATOM   3412 N NE1   . TRP B 1 98  ? 44.007 -13.371 -51.230 1.00 29.80 ? 89  TRP B NE1   1 
ATOM   3413 C CE2   . TRP B 1 98  ? 44.565 -12.174 -50.866 1.00 32.32 ? 89  TRP B CE2   1 
ATOM   3414 C CE3   . TRP B 1 98  ? 46.766 -11.288 -50.398 1.00 32.01 ? 89  TRP B CE3   1 
ATOM   3415 C CZ2   . TRP B 1 98  ? 43.964 -10.939 -50.626 1.00 27.61 ? 89  TRP B CZ2   1 
ATOM   3416 C CZ3   . TRP B 1 98  ? 46.167 -10.063 -50.157 1.00 34.98 ? 89  TRP B CZ3   1 
ATOM   3417 C CH2   . TRP B 1 98  ? 44.779 -9.898  -50.273 1.00 31.11 ? 89  TRP B CH2   1 
ATOM   3418 N N     . LYS B 1 99  ? 50.682 -15.051 -51.664 1.00 38.13 ? 90  LYS B N     1 
ATOM   3419 C CA    . LYS B 1 99  ? 51.990 -15.264 -51.052 1.00 39.65 ? 90  LYS B CA    1 
ATOM   3420 C C     . LYS B 1 99  ? 52.987 -14.192 -51.477 1.00 38.35 ? 90  LYS B C     1 
ATOM   3421 O O     . LYS B 1 99  ? 53.781 -13.714 -50.659 1.00 39.92 ? 90  LYS B O     1 
ATOM   3422 C CB    . LYS B 1 99  ? 52.511 -16.658 -51.409 1.00 40.75 ? 90  LYS B CB    1 
ATOM   3423 C CG    . LYS B 1 99  ? 54.027 -16.780 -51.407 1.00 42.01 ? 90  LYS B CG    1 
ATOM   3424 C CD    . LYS B 1 99  ? 54.485 -18.028 -50.668 1.00 50.47 ? 90  LYS B CD    1 
ATOM   3425 C CE    . LYS B 1 99  ? 55.979 -17.986 -50.387 1.00 52.66 ? 90  LYS B CE    1 
ATOM   3426 N NZ    . LYS B 1 99  ? 56.276 -17.378 -49.058 1.00 56.44 ? 90  LYS B NZ    1 
ATOM   3427 N N     . LYS B 1 100 ? 52.956 -13.796 -52.753 1.00 39.47 ? 91  LYS B N     1 
ATOM   3428 C CA    . LYS B 1 100 ? 53.878 -12.772 -53.234 1.00 34.66 ? 91  LYS B CA    1 
ATOM   3429 C C     . LYS B 1 100 ? 53.620 -11.423 -52.575 1.00 38.01 ? 91  LYS B C     1 
ATOM   3430 O O     . LYS B 1 100 ? 54.553 -10.629 -52.408 1.00 40.76 ? 91  LYS B O     1 
ATOM   3431 C CB    . LYS B 1 100 ? 53.772 -12.644 -54.754 1.00 49.52 ? 91  LYS B CB    1 
ATOM   3432 C CG    . LYS B 1 100 ? 53.860 -13.969 -55.495 1.00 46.02 ? 91  LYS B CG    1 
ATOM   3433 C CD    . LYS B 1 100 ? 54.044 -13.749 -56.986 1.00 52.28 ? 91  LYS B CD    1 
ATOM   3434 C CE    . LYS B 1 100 ? 53.235 -14.748 -57.795 1.00 48.51 ? 91  LYS B CE    1 
ATOM   3435 N NZ    . LYS B 1 100 ? 53.737 -14.860 -59.193 1.00 58.13 ? 91  LYS B NZ    1 
ATOM   3436 N N     . ILE B 1 101 ? 52.372 -11.147 -52.198 1.00 38.05 ? 92  ILE B N     1 
ATOM   3437 C CA    . ILE B 1 101 ? 52.054 -9.887  -51.534 1.00 39.22 ? 92  ILE B CA    1 
ATOM   3438 C C     . ILE B 1 101 ? 52.487 -9.919  -50.073 1.00 35.88 ? 92  ILE B C     1 
ATOM   3439 O O     . ILE B 1 101 ? 53.001 -8.928  -49.545 1.00 40.59 ? 92  ILE B O     1 
ATOM   3440 C CB    . ILE B 1 101 ? 50.552 -9.583  -51.682 1.00 37.28 ? 92  ILE B CB    1 
ATOM   3441 C CG1   . ILE B 1 101 ? 50.220 -9.281  -53.144 1.00 34.32 ? 92  ILE B CG1   1 
ATOM   3442 C CG2   . ILE B 1 101 ? 50.140 -8.422  -50.791 1.00 33.67 ? 92  ILE B CG2   1 
ATOM   3443 C CD1   . ILE B 1 101 ? 48.875 -9.799  -53.581 1.00 36.86 ? 92  ILE B CD1   1 
ATOM   3444 N N     . VAL B 1 102 ? 52.293 -11.055 -49.399 1.00 36.54 ? 93  VAL B N     1 
ATOM   3445 C CA    . VAL B 1 102 ? 52.696 -11.165 -47.999 1.00 34.16 ? 93  VAL B CA    1 
ATOM   3446 C C     . VAL B 1 102 ? 54.212 -11.082 -47.863 1.00 37.24 ? 93  VAL B C     1 
ATOM   3447 O O     . VAL B 1 102 ? 54.727 -10.585 -46.853 1.00 41.62 ? 93  VAL B O     1 
ATOM   3448 C CB    . VAL B 1 102 ? 52.141 -12.469 -47.392 1.00 33.84 ? 93  VAL B CB    1 
ATOM   3449 C CG1   . VAL B 1 102 ? 52.572 -12.618 -45.939 1.00 33.98 ? 93  VAL B CG1   1 
ATOM   3450 C CG2   . VAL B 1 102 ? 50.624 -12.502 -47.503 1.00 36.53 ? 93  VAL B CG2   1 
ATOM   3451 N N     . ASP B 1 103 ? 54.952 -11.545 -48.872 1.00 36.27 ? 94  ASP B N     1 
ATOM   3452 C CA    . ASP B 1 103 ? 56.408 -11.548 -48.774 1.00 38.67 ? 94  ASP B CA    1 
ATOM   3453 C C     . ASP B 1 103 ? 56.975 -10.134 -48.812 1.00 37.20 ? 94  ASP B C     1 
ATOM   3454 O O     . ASP B 1 103 ? 57.904 -9.813  -48.061 1.00 42.00 ? 94  ASP B O     1 
ATOM   3455 C CB    . ASP B 1 103 ? 57.010 -12.401 -49.890 1.00 40.26 ? 94  ASP B CB    1 
ATOM   3456 C CG    . ASP B 1 103 ? 56.705 -13.877 -49.721 1.00 47.46 ? 94  ASP B CG    1 
ATOM   3457 O OD1   . ASP B 1 103 ? 56.254 -14.268 -48.623 1.00 45.46 ? 94  ASP B OD1   1 
ATOM   3458 O OD2   . ASP B 1 103 ? 56.919 -14.646 -50.685 1.00 45.26 ? 94  ASP B OD2   1 
ATOM   3459 N N     . VAL B 1 104 ? 56.434 -9.271  -49.675 1.00 35.20 ? 95  VAL B N     1 
ATOM   3460 C CA    . VAL B 1 104 ? 56.953 -7.909  -49.742 1.00 37.56 ? 95  VAL B CA    1 
ATOM   3461 C C     . VAL B 1 104 ? 56.506 -7.100  -48.531 1.00 33.62 ? 95  VAL B C     1 
ATOM   3462 O O     . VAL B 1 104 ? 57.217 -6.190  -48.089 1.00 42.75 ? 95  VAL B O     1 
ATOM   3463 C CB    . VAL B 1 104 ? 56.545 -7.231  -51.065 1.00 37.46 ? 95  VAL B CB    1 
ATOM   3464 C CG1   . VAL B 1 104 ? 57.201 -7.934  -52.242 1.00 37.54 ? 95  VAL B CG1   1 
ATOM   3465 C CG2   . VAL B 1 104 ? 55.034 -7.212  -51.229 1.00 37.08 ? 95  VAL B CG2   1 
ATOM   3466 N N     . VAL B 1 105 ? 55.340 -7.416  -47.964 1.00 35.85 ? 96  VAL B N     1 
ATOM   3467 C CA    . VAL B 1 105 ? 54.910 -6.732  -46.748 1.00 42.95 ? 96  VAL B CA    1 
ATOM   3468 C C     . VAL B 1 105 ? 55.755 -7.176  -45.562 1.00 43.03 ? 96  VAL B C     1 
ATOM   3469 O O     . VAL B 1 105 ? 56.160 -6.357  -44.727 1.00 39.32 ? 96  VAL B O     1 
ATOM   3470 C CB    . VAL B 1 105 ? 53.410 -6.971  -46.498 1.00 48.45 ? 96  VAL B CB    1 
ATOM   3471 N N     . HIS B 1 106 ? 56.036 -8.479  -45.467 1.00 37.64 ? 97  HIS B N     1 
ATOM   3472 C CA    . HIS B 1 106 ? 56.901 -8.970  -44.401 1.00 41.21 ? 97  HIS B CA    1 
ATOM   3473 C C     . HIS B 1 106 ? 58.337 -8.493  -44.583 1.00 43.20 ? 97  HIS B C     1 
ATOM   3474 O O     . HIS B 1 106 ? 59.075 -8.366  -43.599 1.00 41.90 ? 97  HIS B O     1 
ATOM   3475 C CB    . HIS B 1 106 ? 56.850 -10.497 -44.341 1.00 37.93 ? 97  HIS B CB    1 
ATOM   3476 C CG    . HIS B 1 106 ? 55.665 -11.035 -43.600 1.00 43.05 ? 97  HIS B CG    1 
ATOM   3477 N ND1   . HIS B 1 106 ? 55.336 -12.374 -43.593 1.00 42.37 ? 97  HIS B ND1   1 
ATOM   3478 C CD2   . HIS B 1 106 ? 54.731 -10.415 -42.841 1.00 42.80 ? 97  HIS B CD2   1 
ATOM   3479 C CE1   . HIS B 1 106 ? 54.252 -12.555 -42.860 1.00 41.87 ? 97  HIS B CE1   1 
ATOM   3480 N NE2   . HIS B 1 106 ? 53.863 -11.382 -42.393 1.00 38.01 ? 97  HIS B NE2   1 
ATOM   3481 N N     . ALA B 1 107 ? 58.747 -8.219  -45.825 1.00 40.30 ? 98  ALA B N     1 
ATOM   3482 C CA    . ALA B 1 107 ? 60.097 -7.718  -46.067 1.00 43.64 ? 98  ALA B CA    1 
ATOM   3483 C C     . ALA B 1 107 ? 60.309 -6.350  -45.432 1.00 42.61 ? 98  ALA B C     1 
ATOM   3484 O O     . ALA B 1 107 ? 61.445 -5.985  -45.110 1.00 36.94 ? 98  ALA B O     1 
ATOM   3485 C CB    . ALA B 1 107 ? 60.375 -7.656  -47.570 1.00 40.99 ? 98  ALA B CB    1 
ATOM   3486 N N     . LYS B 1 108 ? 59.238 -5.582  -45.248 1.00 43.17 ? 99  LYS B N     1 
ATOM   3487 C CA    . LYS B 1 108 ? 59.312 -4.303  -44.558 1.00 47.31 ? 99  LYS B CA    1 
ATOM   3488 C C     . LYS B 1 108 ? 59.087 -4.431  -43.057 1.00 41.18 ? 99  LYS B C     1 
ATOM   3489 O O     . LYS B 1 108 ? 59.026 -3.410  -42.364 1.00 46.37 ? 99  LYS B O     1 
ATOM   3490 C CB    . LYS B 1 108 ? 58.296 -3.321  -45.152 1.00 44.03 ? 99  LYS B CB    1 
ATOM   3491 N N     . GLY B 1 109 ? 58.958 -5.652  -42.542 1.00 40.47 ? 100 GLY B N     1 
ATOM   3492 C CA    . GLY B 1 109 ? 58.799 -5.854  -41.115 1.00 42.87 ? 100 GLY B CA    1 
ATOM   3493 C C     . GLY B 1 109 ? 57.407 -5.610  -40.580 1.00 40.88 ? 100 GLY B C     1 
ATOM   3494 O O     . GLY B 1 109 ? 57.253 -5.305  -39.393 1.00 36.47 ? 100 GLY B O     1 
ATOM   3495 N N     . ALA B 1 110 ? 56.382 -5.743  -41.415 1.00 41.30 ? 101 ALA B N     1 
ATOM   3496 C CA    . ALA B 1 110 ? 55.009 -5.500  -41.002 1.00 37.39 ? 101 ALA B CA    1 
ATOM   3497 C C     . ALA B 1 110 ? 54.286 -6.811  -40.716 1.00 37.08 ? 101 ALA B C     1 
ATOM   3498 O O     . ALA B 1 110 ? 54.596 -7.855  -41.293 1.00 42.08 ? 101 ALA B O     1 
ATOM   3499 C CB    . ALA B 1 110 ? 54.247 -4.715  -42.071 1.00 34.21 ? 101 ALA B CB    1 
ATOM   3500 N N     . VAL B 1 111 ? 53.321 -6.742  -39.804 1.00 35.66 ? 102 VAL B N     1 
ATOM   3501 C CA    . VAL B 1 111 ? 52.401 -7.838  -39.523 1.00 35.14 ? 102 VAL B CA    1 
ATOM   3502 C C     . VAL B 1 111 ? 51.135 -7.595  -40.330 1.00 36.35 ? 102 VAL B C     1 
ATOM   3503 O O     . VAL B 1 111 ? 50.607 -6.476  -40.344 1.00 37.94 ? 102 VAL B O     1 
ATOM   3504 C CB    . VAL B 1 111 ? 52.091 -7.933  -38.019 1.00 38.76 ? 102 VAL B CB    1 
ATOM   3505 C CG1   . VAL B 1 111 ? 51.126 -9.073  -37.739 1.00 40.65 ? 102 VAL B CG1   1 
ATOM   3506 C CG2   . VAL B 1 111 ? 53.377 -8.107  -37.228 1.00 37.50 ? 102 VAL B CG2   1 
ATOM   3507 N N     . ILE B 1 112 ? 50.651 -8.628  -41.015 1.00 34.29 ? 103 ILE B N     1 
ATOM   3508 C CA    . ILE B 1 112 ? 49.522 -8.485  -41.924 1.00 33.96 ? 103 ILE B CA    1 
ATOM   3509 C C     . ILE B 1 112 ? 48.534 -9.620  -41.685 1.00 29.23 ? 103 ILE B C     1 
ATOM   3510 O O     . ILE B 1 112 ? 48.927 -10.789 -41.592 1.00 34.18 ? 103 ILE B O     1 
ATOM   3511 C CB    . ILE B 1 112 ? 49.982 -8.437  -43.397 1.00 32.82 ? 103 ILE B CB    1 
ATOM   3512 C CG1   . ILE B 1 112 ? 48.796 -8.182  -44.325 1.00 31.79 ? 103 ILE B CG1   1 
ATOM   3513 C CG2   . ILE B 1 112 ? 50.748 -9.700  -43.796 1.00 31.71 ? 103 ILE B CG2   1 
ATOM   3514 C CD1   . ILE B 1 112 ? 49.164 -7.389  -45.562 1.00 33.54 ? 103 ILE B CD1   1 
ATOM   3515 N N     . PHE B 1 113 ? 47.255 -9.269  -41.574 1.00 30.44 ? 104 PHE B N     1 
ATOM   3516 C CA    . PHE B 1 113 ? 46.165 -10.215 -41.396 1.00 36.92 ? 104 PHE B CA    1 
ATOM   3517 C C     . PHE B 1 113 ? 45.246 -10.155 -42.609 1.00 30.38 ? 104 PHE B C     1 
ATOM   3518 O O     . PHE B 1 113 ? 45.060 -9.093  -43.210 1.00 33.16 ? 104 PHE B O     1 
ATOM   3519 C CB    . PHE B 1 113 ? 45.352 -9.903  -40.128 1.00 33.23 ? 104 PHE B CB    1 
ATOM   3520 C CG    . PHE B 1 113 ? 45.926 -10.484 -38.865 1.00 35.17 ? 104 PHE B CG    1 
ATOM   3521 C CD1   . PHE B 1 113 ? 47.295 -10.497 -38.645 1.00 37.08 ? 104 PHE B CD1   1 
ATOM   3522 C CD2   . PHE B 1 113 ? 45.090 -10.983 -37.879 1.00 32.71 ? 104 PHE B CD2   1 
ATOM   3523 C CE1   . PHE B 1 113 ? 47.819 -11.021 -37.474 1.00 43.72 ? 104 PHE B CE1   1 
ATOM   3524 C CE2   . PHE B 1 113 ? 45.607 -11.507 -36.707 1.00 36.67 ? 104 PHE B CE2   1 
ATOM   3525 C CZ    . PHE B 1 113 ? 46.972 -11.525 -36.503 1.00 38.19 ? 104 PHE B CZ    1 
ATOM   3526 N N     . CYS B 1 114 ? 44.656 -11.295 -42.955 1.00 30.17 ? 105 CYS B N     1 
ATOM   3527 C CA    . CYS B 1 114 ? 43.715 -11.381 -44.066 1.00 36.73 ? 105 CYS B CA    1 
ATOM   3528 C C     . CYS B 1 114 ? 42.290 -11.418 -43.525 1.00 28.57 ? 105 CYS B C     1 
ATOM   3529 O O     . CYS B 1 114 ? 41.930 -12.338 -42.786 1.00 34.46 ? 105 CYS B O     1 
ATOM   3530 C CB    . CYS B 1 114 ? 43.991 -12.618 -44.920 1.00 32.71 ? 105 CYS B CB    1 
ATOM   3531 S SG    . CYS B 1 114 ? 42.776 -12.880 -46.237 1.00 38.82 ? 105 CYS B SG    1 
ATOM   3532 N N     . GLN B 1 115 ? 41.480 -10.431 -43.905 1.00 22.97 ? 106 GLN B N     1 
ATOM   3533 C CA    . GLN B 1 115 ? 40.091 -10.378 -43.461 1.00 31.79 ? 106 GLN B CA    1 
ATOM   3534 C C     . GLN B 1 115 ? 39.245 -11.339 -44.288 1.00 30.58 ? 106 GLN B C     1 
ATOM   3535 O O     . GLN B 1 115 ? 39.213 -11.244 -45.520 1.00 29.99 ? 106 GLN B O     1 
ATOM   3536 C CB    . GLN B 1 115 ? 39.541 -8.957  -43.568 1.00 29.15 ? 106 GLN B CB    1 
ATOM   3537 C CG    . GLN B 1 115 ? 38.142 -8.800  -42.980 1.00 32.42 ? 106 GLN B CG    1 
ATOM   3538 C CD    . GLN B 1 115 ? 37.549 -7.426  -43.225 1.00 32.46 ? 106 GLN B CD    1 
ATOM   3539 O OE1   . GLN B 1 115 ? 37.402 -6.995  -44.369 1.00 33.33 ? 106 GLN B OE1   1 
ATOM   3540 N NE2   . GLN B 1 115 ? 37.201 -6.731  -42.148 1.00 26.45 ? 106 GLN B NE2   1 
ATOM   3541 N N     . LEU B 1 116 ? 38.557 -12.257 -43.611 1.00 30.25 ? 107 LEU B N     1 
ATOM   3542 C CA    . LEU B 1 116 ? 37.676 -13.219 -44.264 1.00 31.25 ? 107 LEU B CA    1 
ATOM   3543 C C     . LEU B 1 116 ? 36.265 -12.641 -44.313 1.00 29.25 ? 107 LEU B C     1 
ATOM   3544 O O     . LEU B 1 116 ? 35.663 -12.368 -43.268 1.00 31.18 ? 107 LEU B O     1 
ATOM   3545 C CB    . LEU B 1 116 ? 37.693 -14.558 -43.526 1.00 30.45 ? 107 LEU B CB    1 
ATOM   3546 C CG    . LEU B 1 116 ? 39.068 -15.165 -43.230 1.00 29.72 ? 107 LEU B CG    1 
ATOM   3547 C CD1   . LEU B 1 116 ? 38.940 -16.623 -42.815 1.00 29.90 ? 107 LEU B CD1   1 
ATOM   3548 C CD2   . LEU B 1 116 ? 40.000 -15.034 -44.432 1.00 32.68 ? 107 LEU B CD2   1 
ATOM   3549 N N     . TRP B 1 117 ? 35.736 -12.468 -45.523 1.00 25.92 ? 108 TRP B N     1 
ATOM   3550 C CA    . TRP B 1 117 ? 34.554 -11.645 -45.750 1.00 30.68 ? 108 TRP B CA    1 
ATOM   3551 C C     . TRP B 1 117 ? 33.528 -12.413 -46.568 1.00 33.39 ? 108 TRP B C     1 
ATOM   3552 O O     . TRP B 1 117 ? 33.818 -12.838 -47.691 1.00 33.95 ? 108 TRP B O     1 
ATOM   3553 C CB    . TRP B 1 117 ? 34.951 -10.347 -46.459 1.00 33.83 ? 108 TRP B CB    1 
ATOM   3554 C CG    . TRP B 1 117 ? 33.824 -9.424  -46.786 1.00 32.06 ? 108 TRP B CG    1 
ATOM   3555 C CD1   . TRP B 1 117 ? 32.669 -9.246  -46.081 1.00 30.48 ? 108 TRP B CD1   1 
ATOM   3556 C CD2   . TRP B 1 117 ? 33.760 -8.521  -47.897 1.00 34.60 ? 108 TRP B CD2   1 
ATOM   3557 N NE1   . TRP B 1 117 ? 31.885 -8.295  -46.693 1.00 30.93 ? 108 TRP B NE1   1 
ATOM   3558 C CE2   . TRP B 1 117 ? 32.533 -7.836  -47.810 1.00 36.75 ? 108 TRP B CE2   1 
ATOM   3559 C CE3   . TRP B 1 117 ? 34.619 -8.234  -48.963 1.00 29.63 ? 108 TRP B CE3   1 
ATOM   3560 C CZ2   . TRP B 1 117 ? 32.145 -6.879  -48.747 1.00 35.43 ? 108 TRP B CZ2   1 
ATOM   3561 C CZ3   . TRP B 1 117 ? 34.234 -7.285  -49.889 1.00 30.79 ? 108 TRP B CZ3   1 
ATOM   3562 C CH2   . TRP B 1 117 ? 33.009 -6.618  -49.775 1.00 26.27 ? 108 TRP B CH2   1 
ATOM   3563 N N     . HIS B 1 118 ? 32.330 -12.580 -46.010 1.00 31.91 ? 109 HIS B N     1 
ATOM   3564 C CA    . HIS B 1 118 ? 31.185 -13.140 -46.720 1.00 35.04 ? 109 HIS B CA    1 
ATOM   3565 C C     . HIS B 1 118 ? 30.064 -12.110 -46.681 1.00 34.84 ? 109 HIS B C     1 
ATOM   3566 O O     . HIS B 1 118 ? 29.638 -11.695 -45.598 1.00 34.40 ? 109 HIS B O     1 
ATOM   3567 C CB    . HIS B 1 118 ? 30.737 -14.464 -46.093 1.00 33.45 ? 109 HIS B CB    1 
ATOM   3568 C CG    . HIS B 1 118 ? 29.791 -15.253 -46.947 1.00 34.48 ? 109 HIS B CG    1 
ATOM   3569 N ND1   . HIS B 1 118 ? 28.624 -14.724 -47.454 1.00 31.60 ? 109 HIS B ND1   1 
ATOM   3570 C CD2   . HIS B 1 118 ? 29.840 -16.536 -47.378 1.00 34.11 ? 109 HIS B CD2   1 
ATOM   3571 C CE1   . HIS B 1 118 ? 27.996 -15.644 -48.164 1.00 35.02 ? 109 HIS B CE1   1 
ATOM   3572 N NE2   . HIS B 1 118 ? 28.714 -16.753 -48.135 1.00 43.33 ? 109 HIS B NE2   1 
ATOM   3573 N N     . VAL B 1 119 ? 29.592 -11.695 -47.860 1.00 28.02 ? 110 VAL B N     1 
ATOM   3574 C CA    . VAL B 1 119 ? 28.624 -10.604 -47.931 1.00 34.59 ? 110 VAL B CA    1 
ATOM   3575 C C     . VAL B 1 119 ? 27.215 -11.040 -47.560 1.00 30.68 ? 110 VAL B C     1 
ATOM   3576 O O     . VAL B 1 119 ? 26.383 -10.189 -47.225 1.00 32.27 ? 110 VAL B O     1 
ATOM   3577 C CB    . VAL B 1 119 ? 28.580 -9.975  -49.334 1.00 31.60 ? 110 VAL B CB    1 
ATOM   3578 C CG1   . VAL B 1 119 ? 29.889 -9.271  -49.643 1.00 28.49 ? 110 VAL B CG1   1 
ATOM   3579 C CG2   . VAL B 1 119 ? 28.255 -11.028 -50.383 1.00 28.84 ? 110 VAL B CG2   1 
ATOM   3580 N N     . GLY B 1 120 ? 26.916 -12.331 -47.621 1.00 36.05 ? 111 GLY B N     1 
ATOM   3581 C CA    . GLY B 1 120 ? 25.564 -12.769 -47.325 1.00 30.64 ? 111 GLY B CA    1 
ATOM   3582 C C     . GLY B 1 120 ? 24.589 -12.234 -48.357 1.00 32.07 ? 111 GLY B C     1 
ATOM   3583 O O     . GLY B 1 120 ? 24.808 -12.346 -49.569 1.00 33.60 ? 111 GLY B O     1 
ATOM   3584 N N     . ARG B 1 121 ? 23.496 -11.637 -47.874 1.00 33.05 ? 112 ARG B N     1 
ATOM   3585 C CA    . ARG B 1 121 ? 22.452 -11.128 -48.757 1.00 32.86 ? 112 ARG B CA    1 
ATOM   3586 C C     . ARG B 1 121 ? 22.862 -9.862  -49.496 1.00 33.34 ? 112 ARG B C     1 
ATOM   3587 O O     . ARG B 1 121 ? 22.144 -9.444  -50.409 1.00 31.46 ? 112 ARG B O     1 
ATOM   3588 C CB    . ARG B 1 121 ? 21.173 -10.862 -47.963 1.00 27.14 ? 112 ARG B CB    1 
ATOM   3589 C CG    . ARG B 1 121 ? 21.226 -9.606  -47.105 1.00 34.60 ? 112 ARG B CG    1 
ATOM   3590 C CD    . ARG B 1 121 ? 19.931 -9.389  -46.331 1.00 30.89 ? 112 ARG B CD    1 
ATOM   3591 N NE    . ARG B 1 121 ? 19.987 -8.179  -45.517 1.00 32.84 ? 112 ARG B NE    1 
ATOM   3592 C CZ    . ARG B 1 121 ? 18.941 -7.618  -44.927 1.00 29.76 ? 112 ARG B CZ    1 
ATOM   3593 N NH1   . ARG B 1 121 ? 17.728 -8.139  -45.028 1.00 31.83 ? 112 ARG B NH1   1 
ATOM   3594 N NH2   . ARG B 1 121 ? 19.115 -6.508  -44.216 1.00 38.77 ? 112 ARG B NH2   1 
ATOM   3595 N N     . ALA B 1 122 ? 23.986 -9.244  -49.129 1.00 32.16 ? 113 ALA B N     1 
ATOM   3596 C CA    . ALA B 1 122 ? 24.457 -8.024  -49.783 1.00 37.21 ? 113 ALA B CA    1 
ATOM   3597 C C     . ALA B 1 122 ? 25.221 -8.367  -51.063 1.00 27.57 ? 113 ALA B C     1 
ATOM   3598 O O     . ALA B 1 122 ? 26.418 -8.113  -51.205 1.00 34.12 ? 113 ALA B O     1 
ATOM   3599 C CB    . ALA B 1 122 ? 25.317 -7.211  -48.825 1.00 27.12 ? 113 ALA B CB    1 
ATOM   3600 N N     . SER B 1 123 ? 24.497 -8.955  -52.010 1.00 34.53 ? 114 SER B N     1 
ATOM   3601 C CA    . SER B 1 123 ? 25.099 -9.445  -53.241 1.00 27.64 ? 114 SER B CA    1 
ATOM   3602 C C     . SER B 1 123 ? 24.105 -9.255  -54.381 1.00 34.36 ? 114 SER B C     1 
ATOM   3603 O O     . SER B 1 123 ? 23.113 -8.531  -54.251 1.00 30.09 ? 114 SER B O     1 
ATOM   3604 C CB    . SER B 1 123 ? 25.528 -10.910 -53.081 1.00 30.65 ? 114 SER B CB    1 
ATOM   3605 O OG    . SER B 1 123 ? 26.365 -11.321 -54.147 1.00 31.25 ? 114 SER B OG    1 
ATOM   3606 N N     . HIS B 1 124 ? 24.374 -9.919  -55.501 1.00 35.13 ? 115 HIS B N     1 
ATOM   3607 C CA    . HIS B 1 124 ? 23.588 -9.767  -56.716 1.00 35.77 ? 115 HIS B CA    1 
ATOM   3608 C C     . HIS B 1 124 ? 23.859 -10.972 -57.602 1.00 34.04 ? 115 HIS B C     1 
ATOM   3609 O O     . HIS B 1 124 ? 24.937 -11.569 -57.536 1.00 33.19 ? 115 HIS B O     1 
ATOM   3610 C CB    . HIS B 1 124 ? 23.940 -8.464  -57.444 1.00 35.88 ? 115 HIS B CB    1 
ATOM   3611 C CG    . HIS B 1 124 ? 22.958 -8.071  -58.505 1.00 42.87 ? 115 HIS B CG    1 
ATOM   3612 N ND1   . HIS B 1 124 ? 22.992 -8.592  -59.781 1.00 39.23 ? 115 HIS B ND1   1 
ATOM   3613 C CD2   . HIS B 1 124 ? 21.926 -7.195  -58.483 1.00 35.99 ? 115 HIS B CD2   1 
ATOM   3614 C CE1   . HIS B 1 124 ? 22.015 -8.061  -60.496 1.00 39.38 ? 115 HIS B CE1   1 
ATOM   3615 N NE2   . HIS B 1 124 ? 21.355 -7.210  -59.732 1.00 36.60 ? 115 HIS B NE2   1 
ATOM   3616 N N     . GLU B 1 125 ? 22.870 -11.323 -58.431 1.00 38.77 ? 116 GLU B N     1 
ATOM   3617 C CA    . GLU B 1 125 ? 23.013 -12.484 -59.307 1.00 39.24 ? 116 GLU B CA    1 
ATOM   3618 C C     . GLU B 1 125 ? 24.254 -12.381 -60.184 1.00 34.06 ? 116 GLU B C     1 
ATOM   3619 O O     . GLU B 1 125 ? 24.863 -13.405 -60.516 1.00 35.78 ? 116 GLU B O     1 
ATOM   3620 C CB    . GLU B 1 125 ? 21.766 -12.650 -60.176 1.00 37.34 ? 116 GLU B CB    1 
ATOM   3621 N N     . VAL B 1 126 ? 24.649 -11.161 -60.559 1.00 36.49 ? 117 VAL B N     1 
ATOM   3622 C CA    . VAL B 1 126 ? 25.852 -10.973 -61.361 1.00 36.62 ? 117 VAL B CA    1 
ATOM   3623 C C     . VAL B 1 126 ? 27.106 -11.371 -60.595 1.00 33.95 ? 117 VAL B C     1 
ATOM   3624 O O     . VAL B 1 126 ? 28.130 -11.688 -61.208 1.00 31.06 ? 117 VAL B O     1 
ATOM   3625 C CB    . VAL B 1 126 ? 25.947 -9.513  -61.847 1.00 39.51 ? 117 VAL B CB    1 
ATOM   3626 C CG1   . VAL B 1 126 ? 26.395 -8.598  -60.716 1.00 33.42 ? 117 VAL B CG1   1 
ATOM   3627 C CG2   . VAL B 1 126 ? 26.887 -9.400  -63.039 1.00 39.98 ? 117 VAL B CG2   1 
ATOM   3628 N N     . TYR B 1 127 ? 27.052 -11.377 -59.265 1.00 40.15 ? 118 TYR B N     1 
ATOM   3629 C CA    . TYR B 1 127 ? 28.188 -11.754 -58.438 1.00 32.18 ? 118 TYR B CA    1 
ATOM   3630 C C     . TYR B 1 127 ? 28.125 -13.203 -57.973 1.00 33.81 ? 118 TYR B C     1 
ATOM   3631 O O     . TYR B 1 127 ? 29.074 -13.678 -57.343 1.00 40.78 ? 118 TYR B O     1 
ATOM   3632 C CB    . TYR B 1 127 ? 28.286 -10.822 -57.223 1.00 32.90 ? 118 TYR B CB    1 
ATOM   3633 C CG    . TYR B 1 127 ? 28.638 -9.394  -57.579 1.00 36.11 ? 118 TYR B CG    1 
ATOM   3634 C CD1   . TYR B 1 127 ? 29.737 -9.112  -58.381 1.00 30.00 ? 118 TYR B CD1   1 
ATOM   3635 C CD2   . TYR B 1 127 ? 27.873 -8.330  -57.117 1.00 35.13 ? 118 TYR B CD2   1 
ATOM   3636 C CE1   . TYR B 1 127 ? 30.067 -7.814  -58.712 1.00 29.59 ? 118 TYR B CE1   1 
ATOM   3637 C CE2   . TYR B 1 127 ? 28.196 -7.023  -57.444 1.00 35.58 ? 118 TYR B CE2   1 
ATOM   3638 C CZ    . TYR B 1 127 ? 29.295 -6.774  -58.244 1.00 36.28 ? 118 TYR B CZ    1 
ATOM   3639 O OH    . TYR B 1 127 ? 29.628 -5.481  -58.581 1.00 35.49 ? 118 TYR B OH    1 
ATOM   3640 N N     . GLN B 1 128 ? 27.041 -13.917 -58.276 1.00 36.54 ? 119 GLN B N     1 
ATOM   3641 C CA    . GLN B 1 128 ? 26.835 -15.270 -57.786 1.00 38.68 ? 119 GLN B CA    1 
ATOM   3642 C C     . GLN B 1 128 ? 27.009 -16.297 -58.903 1.00 42.85 ? 119 GLN B C     1 
ATOM   3643 O O     . GLN B 1 128 ? 26.706 -16.016 -60.067 1.00 38.70 ? 119 GLN B O     1 
ATOM   3644 C CB    . GLN B 1 128 ? 25.435 -15.417 -57.180 1.00 34.94 ? 119 GLN B CB    1 
ATOM   3645 C CG    . GLN B 1 128 ? 25.243 -14.644 -55.888 1.00 34.51 ? 119 GLN B CG    1 
ATOM   3646 C CD    . GLN B 1 128 ? 26.106 -15.178 -54.767 1.00 37.72 ? 119 GLN B CD    1 
ATOM   3647 O OE1   . GLN B 1 128 ? 26.483 -16.351 -54.766 1.00 41.19 ? 119 GLN B OE1   1 
ATOM   3648 N NE2   . GLN B 1 128 ? 26.431 -14.320 -53.805 1.00 37.28 ? 119 GLN B NE2   1 
ATOM   3649 N N     . PRO B 1 129 ? 27.496 -17.496 -58.582 1.00 39.76 ? 120 PRO B N     1 
ATOM   3650 C CA    . PRO B 1 129 ? 27.621 -18.536 -59.611 1.00 43.49 ? 120 PRO B CA    1 
ATOM   3651 C C     . PRO B 1 129 ? 26.255 -18.970 -60.120 1.00 42.23 ? 120 PRO B C     1 
ATOM   3652 O O     . PRO B 1 129 ? 25.299 -19.099 -59.351 1.00 41.09 ? 120 PRO B O     1 
ATOM   3653 C CB    . PRO B 1 129 ? 28.337 -19.682 -58.883 1.00 42.17 ? 120 PRO B CB    1 
ATOM   3654 C CG    . PRO B 1 129 ? 28.918 -19.065 -57.642 1.00 51.34 ? 120 PRO B CG    1 
ATOM   3655 C CD    . PRO B 1 129 ? 27.999 -17.947 -57.275 1.00 43.03 ? 120 PRO B CD    1 
ATOM   3656 N N     . ALA B 1 130 ? 26.172 -19.179 -61.435 1.00 40.47 ? 121 ALA B N     1 
ATOM   3657 C CA    . ALA B 1 130 ? 24.938 -19.556 -62.124 1.00 33.17 ? 121 ALA B CA    1 
ATOM   3658 C C     . ALA B 1 130 ? 23.815 -18.550 -61.902 1.00 39.54 ? 121 ALA B C     1 
ATOM   3659 O O     . ALA B 1 130 ? 22.638 -18.877 -62.094 1.00 40.16 ? 121 ALA B O     1 
ATOM   3660 C CB    . ALA B 1 130 ? 24.475 -20.959 -61.712 1.00 40.73 ? 121 ALA B CB    1 
ATOM   3661 N N     . GLY B 1 131 ? 24.153 -17.325 -61.502 1.00 41.52 ? 122 GLY B N     1 
ATOM   3662 C CA    . GLY B 1 131 ? 23.142 -16.328 -61.210 1.00 40.00 ? 122 GLY B CA    1 
ATOM   3663 C C     . GLY B 1 131 ? 22.211 -16.694 -60.079 1.00 39.89 ? 122 GLY B C     1 
ATOM   3664 O O     . GLY B 1 131 ? 21.092 -16.180 -60.018 1.00 43.24 ? 122 GLY B O     1 
ATOM   3665 N N     . ALA B 1 132 ? 22.640 -17.573 -59.177 1.00 38.57 ? 123 ALA B N     1 
ATOM   3666 C CA    . ALA B 1 132 ? 21.789 -18.003 -58.080 1.00 38.92 ? 123 ALA B CA    1 
ATOM   3667 C C     . ALA B 1 132 ? 21.598 -16.870 -57.072 1.00 38.97 ? 123 ALA B C     1 
ATOM   3668 O O     . ALA B 1 132 ? 22.312 -15.863 -57.076 1.00 41.24 ? 123 ALA B O     1 
ATOM   3669 C CB    . ALA B 1 132 ? 22.382 -19.231 -57.391 1.00 32.40 ? 123 ALA B CB    1 
ATOM   3670 N N     . ALA B 1 133 ? 20.611 -17.046 -56.199 1.00 36.74 ? 124 ALA B N     1 
ATOM   3671 C CA    . ALA B 1 133 ? 20.338 -16.052 -55.177 1.00 40.96 ? 124 ALA B CA    1 
ATOM   3672 C C     . ALA B 1 133 ? 21.404 -16.107 -54.084 1.00 40.83 ? 124 ALA B C     1 
ATOM   3673 O O     . ALA B 1 133 ? 21.950 -17.174 -53.788 1.00 32.20 ? 124 ALA B O     1 
ATOM   3674 C CB    . ALA B 1 133 ? 18.957 -16.277 -54.566 1.00 37.67 ? 124 ALA B CB    1 
ATOM   3675 N N     . PRO B 1 134 ? 21.729 -14.969 -53.478 1.00 39.38 ? 125 PRO B N     1 
ATOM   3676 C CA    . PRO B 1 134 ? 22.676 -14.975 -52.359 1.00 35.71 ? 125 PRO B CA    1 
ATOM   3677 C C     . PRO B 1 134 ? 22.078 -15.659 -51.140 1.00 31.44 ? 125 PRO B C     1 
ATOM   3678 O O     . PRO B 1 134 ? 20.863 -15.826 -51.016 1.00 28.28 ? 125 PRO B O     1 
ATOM   3679 C CB    . PRO B 1 134 ? 22.933 -13.486 -52.094 1.00 35.60 ? 125 PRO B CB    1 
ATOM   3680 C CG    . PRO B 1 134 ? 22.417 -12.771 -53.311 1.00 37.71 ? 125 PRO B CG    1 
ATOM   3681 C CD    . PRO B 1 134 ? 21.294 -13.607 -53.824 1.00 35.73 ? 125 PRO B CD    1 
ATOM   3682 N N     . ILE B 1 135 ? 22.961 -16.065 -50.234 1.00 31.68 ? 126 ILE B N     1 
ATOM   3683 C CA    . ILE B 1 135 ? 22.566 -16.767 -49.021 1.00 32.24 ? 126 ILE B CA    1 
ATOM   3684 C C     . ILE B 1 135 ? 22.509 -15.775 -47.866 1.00 35.63 ? 126 ILE B C     1 
ATOM   3685 O O     . ILE B 1 135 ? 23.154 -14.725 -47.885 1.00 36.81 ? 126 ILE B O     1 
ATOM   3686 C CB    . ILE B 1 135 ? 23.527 -17.932 -48.705 1.00 33.45 ? 126 ILE B CB    1 
ATOM   3687 C CG1   . ILE B 1 135 ? 24.929 -17.406 -48.391 1.00 35.96 ? 126 ILE B CG1   1 
ATOM   3688 C CG2   . ILE B 1 135 ? 23.581 -18.913 -49.871 1.00 35.33 ? 126 ILE B CG2   1 
ATOM   3689 C CD1   . ILE B 1 135 ? 25.592 -18.095 -47.222 1.00 43.37 ? 126 ILE B CD1   1 
ATOM   3690 N N     . SER B 1 136 ? 21.718 -16.106 -46.847 1.00 36.50 ? 127 SER B N     1 
ATOM   3691 C CA    . SER B 1 136 ? 21.567 -15.248 -45.671 1.00 35.00 ? 127 SER B CA    1 
ATOM   3692 C C     . SER B 1 136 ? 20.887 -16.059 -44.571 1.00 35.50 ? 127 SER B C     1 
ATOM   3693 O O     . SER B 1 136 ? 20.652 -17.265 -44.720 1.00 37.88 ? 127 SER B O     1 
ATOM   3694 C CB    . SER B 1 136 ? 20.784 -13.976 -46.009 1.00 38.26 ? 127 SER B CB    1 
ATOM   3695 O OG    . SER B 1 136 ? 20.484 -13.231 -44.841 1.00 38.41 ? 127 SER B OG    1 
ATOM   3696 N N     . SER B 1 137 ? 20.571 -15.388 -43.458 1.00 34.47 ? 128 SER B N     1 
ATOM   3697 C CA    . SER B 1 137 ? 19.852 -16.040 -42.366 1.00 31.49 ? 128 SER B CA    1 
ATOM   3698 C C     . SER B 1 137 ? 18.350 -16.091 -42.620 1.00 36.64 ? 128 SER B C     1 
ATOM   3699 O O     . SER B 1 137 ? 17.670 -16.999 -42.125 1.00 36.08 ? 128 SER B O     1 
ATOM   3700 C CB    . SER B 1 137 ? 20.128 -15.325 -41.040 1.00 36.62 ? 128 SER B CB    1 
ATOM   3701 O OG    . SER B 1 137 ? 19.734 -13.962 -41.089 1.00 33.45 ? 128 SER B OG    1 
ATOM   3702 N N     . THR B 1 138 ? 17.820 -15.137 -43.381 1.00 33.73 ? 129 THR B N     1 
ATOM   3703 C CA    . THR B 1 138 ? 16.399 -15.052 -43.686 1.00 38.68 ? 129 THR B CA    1 
ATOM   3704 C C     . THR B 1 138 ? 16.222 -14.817 -45.181 1.00 41.29 ? 129 THR B C     1 
ATOM   3705 O O     . THR B 1 138 ? 17.193 -14.702 -45.935 1.00 30.81 ? 129 THR B O     1 
ATOM   3706 C CB    . THR B 1 138 ? 15.722 -13.930 -42.888 1.00 41.72 ? 129 THR B CB    1 
ATOM   3707 O OG1   . THR B 1 138 ? 14.384 -13.740 -43.366 1.00 53.11 ? 129 THR B OG1   1 
ATOM   3708 C CG2   . THR B 1 138 ? 16.485 -12.636 -43.059 1.00 41.56 ? 129 THR B CG2   1 
ATOM   3709 N N     . GLU B 1 139 ? 14.962 -14.742 -45.606 1.00 41.59 ? 130 GLU B N     1 
ATOM   3710 C CA    . GLU B 1 139 ? 14.609 -14.426 -46.983 1.00 36.96 ? 130 GLU B CA    1 
ATOM   3711 C C     . GLU B 1 139 ? 14.398 -12.935 -47.211 1.00 39.51 ? 130 GLU B C     1 
ATOM   3712 O O     . GLU B 1 139 ? 14.047 -12.539 -48.327 1.00 40.98 ? 130 GLU B O     1 
ATOM   3713 C CB    . GLU B 1 139 ? 13.342 -15.187 -47.391 1.00 42.49 ? 130 GLU B CB    1 
ATOM   3714 C CG    . GLU B 1 139 ? 13.603 -16.538 -48.042 1.00 50.58 ? 130 GLU B CG    1 
ATOM   3715 C CD    . GLU B 1 139 ? 12.401 -17.463 -47.970 1.00 55.66 ? 130 GLU B CD    1 
ATOM   3716 O OE1   . GLU B 1 139 ? 11.299 -17.044 -48.384 1.00 60.00 ? 130 GLU B OE1   1 
ATOM   3717 O OE2   . GLU B 1 139 ? 12.558 -18.611 -47.504 1.00 58.12 ? 130 GLU B OE2   1 
ATOM   3718 N N     . LYS B 1 140 ? 14.599 -12.107 -46.194 1.00 40.42 ? 131 LYS B N     1 
ATOM   3719 C CA    . LYS B 1 140 ? 14.363 -10.675 -46.334 1.00 37.45 ? 131 LYS B CA    1 
ATOM   3720 C C     . LYS B 1 140 ? 15.494 -10.031 -47.126 1.00 38.56 ? 131 LYS B C     1 
ATOM   3721 O O     . LYS B 1 140 ? 16.668 -10.257 -46.816 1.00 34.79 ? 131 LYS B O     1 
ATOM   3722 C CB    . LYS B 1 140 ? 14.250 -10.011 -44.968 1.00 42.45 ? 131 LYS B CB    1 
ATOM   3723 C CG    . LYS B 1 140 ? 13.169 -10.597 -44.091 1.00 49.42 ? 131 LYS B CG    1 
ATOM   3724 C CD    . LYS B 1 140 ? 12.840 -9.664  -42.946 1.00 57.38 ? 131 LYS B CD    1 
ATOM   3725 C CE    . LYS B 1 140 ? 13.338 -10.227 -41.630 1.00 55.50 ? 131 LYS B CE    1 
ATOM   3726 N NZ    . LYS B 1 140 ? 12.626 -9.611  -40.483 1.00 61.47 ? 131 LYS B NZ    1 
ATOM   3727 N N     . PRO B 1 141 ? 15.188 -9.233  -48.140 1.00 40.04 ? 132 PRO B N     1 
ATOM   3728 C CA    . PRO B 1 141 ? 16.231 -8.519  -48.871 1.00 39.42 ? 132 PRO B CA    1 
ATOM   3729 C C     . PRO B 1 141 ? 16.505 -7.157  -48.241 1.00 42.11 ? 132 PRO B C     1 
ATOM   3730 O O     . PRO B 1 141 ? 15.744 -6.658  -47.410 1.00 40.15 ? 132 PRO B O     1 
ATOM   3731 C CB    . PRO B 1 141 ? 15.629 -8.359  -50.276 1.00 42.76 ? 132 PRO B CB    1 
ATOM   3732 C CG    . PRO B 1 141 ? 14.129 -8.529  -50.099 1.00 41.71 ? 132 PRO B CG    1 
ATOM   3733 C CD    . PRO B 1 141 ? 13.848 -8.945  -48.676 1.00 45.61 ? 132 PRO B CD    1 
ATOM   3734 N N     . ILE B 1 142 ? 17.631 -6.571  -48.645 1.00 40.96 ? 133 ILE B N     1 
ATOM   3735 C CA    . ILE B 1 142 ? 17.887 -5.175  -48.327 1.00 41.35 ? 133 ILE B CA    1 
ATOM   3736 C C     . ILE B 1 142 ? 16.892 -4.312  -49.090 1.00 36.79 ? 133 ILE B C     1 
ATOM   3737 O O     . ILE B 1 142 ? 16.602 -4.562  -50.268 1.00 44.36 ? 133 ILE B O     1 
ATOM   3738 C CB    . ILE B 1 142 ? 19.342 -4.809  -48.665 1.00 36.09 ? 133 ILE B CB    1 
ATOM   3739 C CG1   . ILE B 1 142 ? 20.295 -5.832  -48.041 1.00 36.60 ? 133 ILE B CG1   1 
ATOM   3740 C CG2   . ILE B 1 142 ? 19.670 -3.408  -48.179 1.00 39.98 ? 133 ILE B CG2   1 
ATOM   3741 C CD1   . ILE B 1 142 ? 21.762 -5.520  -48.244 1.00 38.54 ? 133 ILE B CD1   1 
ATOM   3742 N N     . SER B 1 143 ? 16.350 -3.298  -48.419 1.00 39.43 ? 134 SER B N     1 
ATOM   3743 C CA    . SER B 1 143 ? 15.253 -2.522  -48.982 1.00 43.89 ? 134 SER B CA    1 
ATOM   3744 C C     . SER B 1 143 ? 15.738 -1.657  -50.147 1.00 46.53 ? 134 SER B C     1 
ATOM   3745 O O     . SER B 1 143 ? 16.914 -1.660  -50.523 1.00 42.42 ? 134 SER B O     1 
ATOM   3746 C CB    . SER B 1 143 ? 14.606 -1.660  -47.902 1.00 41.40 ? 134 SER B CB    1 
ATOM   3747 O OG    . SER B 1 143 ? 15.365 -0.486  -47.673 1.00 38.47 ? 134 SER B OG    1 
ATOM   3748 N N     . ASN B 1 144 ? 14.802 -0.895  -50.719 1.00 50.93 ? 135 ASN B N     1 
ATOM   3749 C CA    . ASN B 1 144 ? 15.083 -0.021  -51.853 1.00 50.00 ? 135 ASN B CA    1 
ATOM   3750 C C     . ASN B 1 144 ? 15.967 1.165   -51.491 1.00 45.13 ? 135 ASN B C     1 
ATOM   3751 O O     . ASN B 1 144 ? 16.366 1.911   -52.391 1.00 45.91 ? 135 ASN B O     1 
ATOM   3752 C CB    . ASN B 1 144 ? 13.773 0.496   -52.456 1.00 51.60 ? 135 ASN B CB    1 
ATOM   3753 C CG    . ASN B 1 144 ? 13.036 -0.562  -53.253 1.00 61.58 ? 135 ASN B CG    1 
ATOM   3754 O OD1   . ASN B 1 144 ? 12.623 -1.589  -52.712 1.00 64.30 ? 135 ASN B OD1   1 
ATOM   3755 N ND2   . ASN B 1 144 ? 12.861 -0.314  -54.547 1.00 64.65 ? 135 ASN B ND2   1 
ATOM   3756 N N     . ARG B 1 145 ? 16.272 1.364   -50.207 1.00 44.24 ? 136 ARG B N     1 
ATOM   3757 C CA    . ARG B 1 145 ? 17.087 2.506   -49.809 1.00 49.78 ? 136 ARG B CA    1 
ATOM   3758 C C     . ARG B 1 145 ? 18.530 2.363   -50.275 1.00 46.90 ? 136 ARG B C     1 
ATOM   3759 O O     . ARG B 1 145 ? 19.184 3.366   -50.580 1.00 50.07 ? 136 ARG B O     1 
ATOM   3760 C CB    . ARG B 1 145 ? 17.045 2.683   -48.292 1.00 46.84 ? 136 ARG B CB    1 
ATOM   3761 C CG    . ARG B 1 145 ? 17.321 4.101   -47.833 1.00 55.88 ? 136 ARG B CG    1 
ATOM   3762 C CD    . ARG B 1 145 ? 18.087 4.119   -46.516 1.00 59.92 ? 136 ARG B CD    1 
ATOM   3763 N NE    . ARG B 1 145 ? 18.479 5.459   -46.087 1.00 68.48 ? 136 ARG B NE    1 
ATOM   3764 C CZ    . ARG B 1 145 ? 19.247 6.294   -46.779 1.00 77.10 ? 136 ARG B CZ    1 
ATOM   3765 N NH1   . ARG B 1 145 ? 19.797 5.943   -47.931 1.00 76.86 ? 136 ARG B NH1   1 
ATOM   3766 N NH2   . ARG B 1 145 ? 19.495 7.504   -46.285 1.00 69.38 ? 136 ARG B NH2   1 
ATOM   3767 N N     . TRP B 1 146 ? 19.043 1.139   -50.329 1.00 41.88 ? 137 TRP B N     1 
ATOM   3768 C CA    . TRP B 1 146 ? 20.424 0.883   -50.707 1.00 38.50 ? 137 TRP B CA    1 
ATOM   3769 C C     . TRP B 1 146 ? 20.478 0.228   -52.079 1.00 39.13 ? 137 TRP B C     1 
ATOM   3770 O O     . TRP B 1 146 ? 19.606 -0.571  -52.434 1.00 37.54 ? 137 TRP B O     1 
ATOM   3771 C CB    . TRP B 1 146 ? 21.121 -0.006  -49.675 1.00 42.99 ? 137 TRP B CB    1 
ATOM   3772 C CG    . TRP B 1 146 ? 20.924 0.456   -48.264 1.00 43.26 ? 137 TRP B CG    1 
ATOM   3773 C CD1   . TRP B 1 146 ? 19.864 0.180   -47.450 1.00 43.91 ? 137 TRP B CD1   1 
ATOM   3774 C CD2   . TRP B 1 146 ? 21.814 1.278   -47.498 1.00 49.47 ? 137 TRP B CD2   1 
ATOM   3775 N NE1   . TRP B 1 146 ? 20.038 0.779   -46.225 1.00 47.24 ? 137 TRP B NE1   1 
ATOM   3776 C CE2   . TRP B 1 146 ? 21.227 1.459   -46.229 1.00 48.51 ? 137 TRP B CE2   1 
ATOM   3777 C CE3   . TRP B 1 146 ? 23.049 1.878   -47.762 1.00 48.39 ? 137 TRP B CE3   1 
ATOM   3778 C CZ2   . TRP B 1 146 ? 21.834 2.213   -45.227 1.00 50.57 ? 137 TRP B CZ2   1 
ATOM   3779 C CZ3   . TRP B 1 146 ? 23.649 2.630   -46.765 1.00 54.04 ? 137 TRP B CZ3   1 
ATOM   3780 C CH2   . TRP B 1 146 ? 23.041 2.789   -45.513 1.00 52.70 ? 137 TRP B CH2   1 
ATOM   3781 N N     . ARG B 1 147 ? 21.499 0.583   -52.851 1.00 37.15 ? 138 ARG B N     1 
ATOM   3782 C CA    . ARG B 1 147 ? 21.765 -0.024  -54.144 1.00 38.74 ? 138 ARG B CA    1 
ATOM   3783 C C     . ARG B 1 147 ? 23.166 -0.614  -54.134 1.00 37.04 ? 138 ARG B C     1 
ATOM   3784 O O     . ARG B 1 147 ? 24.058 -0.123  -53.435 1.00 36.06 ? 138 ARG B O     1 
ATOM   3785 C CB    . ARG B 1 147 ? 21.629 0.995   -55.281 1.00 40.26 ? 138 ARG B CB    1 
ATOM   3786 C CG    . ARG B 1 147 ? 20.376 1.848   -55.205 1.00 44.13 ? 138 ARG B CG    1 
ATOM   3787 C CD    . ARG B 1 147 ? 19.148 1.059   -55.622 1.00 49.64 ? 138 ARG B CD    1 
ATOM   3788 N NE    . ARG B 1 147 ? 18.060 1.932   -56.045 1.00 59.03 ? 138 ARG B NE    1 
ATOM   3789 C CZ    . ARG B 1 147 ? 16.807 1.824   -55.624 1.00 60.47 ? 138 ARG B CZ    1 
ATOM   3790 N NH1   . ARG B 1 147 ? 16.443 0.879   -54.772 1.00 59.14 ? 138 ARG B NH1   1 
ATOM   3791 N NH2   . ARG B 1 147 ? 15.896 2.685   -56.068 1.00 56.12 ? 138 ARG B NH2   1 
ATOM   3792 N N     . ILE B 1 148 ? 23.356 -1.674  -54.911 1.00 37.25 ? 139 ILE B N     1 
ATOM   3793 C CA    . ILE B 1 148 ? 24.629 -2.380  -54.971 1.00 38.43 ? 139 ILE B CA    1 
ATOM   3794 C C     . ILE B 1 148 ? 25.390 -1.913  -56.203 1.00 36.11 ? 139 ILE B C     1 
ATOM   3795 O O     . ILE B 1 148 ? 24.814 -1.789  -57.291 1.00 39.25 ? 139 ILE B O     1 
ATOM   3796 C CB    . ILE B 1 148 ? 24.422 -3.906  -54.985 1.00 33.42 ? 139 ILE B CB    1 
ATOM   3797 C CG1   . ILE B 1 148 ? 25.760 -4.630  -55.157 1.00 34.38 ? 139 ILE B CG1   1 
ATOM   3798 C CG2   . ILE B 1 148 ? 23.429 -4.310  -56.065 1.00 33.14 ? 139 ILE B CG2   1 
ATOM   3799 C CD1   . ILE B 1 148 ? 25.686 -6.117  -54.894 1.00 34.28 ? 139 ILE B CD1   1 
ATOM   3800 N N     . LEU B 1 149 ? 26.679 -1.632  -56.028 1.00 26.99 ? 140 LEU B N     1 
ATOM   3801 C CA    . LEU B 1 149 ? 27.527 -1.287  -57.159 1.00 35.94 ? 140 LEU B CA    1 
ATOM   3802 C C     . LEU B 1 149 ? 27.622 -2.467  -58.117 1.00 37.34 ? 140 LEU B C     1 
ATOM   3803 O O     . LEU B 1 149 ? 27.855 -3.605  -57.699 1.00 28.95 ? 140 LEU B O     1 
ATOM   3804 C CB    . LEU B 1 149 ? 28.919 -0.883  -56.673 1.00 36.16 ? 140 LEU B CB    1 
ATOM   3805 C CG    . LEU B 1 149 ? 29.769 -0.048  -57.637 1.00 47.19 ? 140 LEU B CG    1 
ATOM   3806 C CD1   . LEU B 1 149 ? 28.924 0.994   -58.354 1.00 42.96 ? 140 LEU B CD1   1 
ATOM   3807 C CD2   . LEU B 1 149 ? 30.933 0.608   -56.910 1.00 52.62 ? 140 LEU B CD2   1 
ATOM   3808 N N     . MET B 1 150 ? 27.433 -2.193  -59.403 1.00 34.87 ? 141 MET B N     1 
ATOM   3809 C CA    . MET B 1 150 ? 27.481 -3.197  -60.453 1.00 30.05 ? 141 MET B CA    1 
ATOM   3810 C C     . MET B 1 150 ? 28.853 -3.213  -61.113 1.00 29.70 ? 141 MET B C     1 
ATOM   3811 O O     . MET B 1 150 ? 29.622 -2.255  -60.992 1.00 35.35 ? 141 MET B O     1 
ATOM   3812 C CB    . MET B 1 150 ? 26.396 -2.920  -61.500 1.00 32.37 ? 141 MET B CB    1 
ATOM   3813 C CG    . MET B 1 150 ? 24.981 -2.952  -60.946 1.00 34.24 ? 141 MET B CG    1 
ATOM   3814 S SD    . MET B 1 150 ? 24.582 -4.518  -60.138 1.00 34.69 ? 141 MET B SD    1 
ATOM   3815 C CE    . MET B 1 150 ? 24.353 -5.571  -61.570 1.00 40.00 ? 141 MET B CE    1 
ATOM   3816 N N     . PRO B 1 151 ? 29.204 -4.299  -61.811 1.00 30.16 ? 142 PRO B N     1 
ATOM   3817 C CA    . PRO B 1 151 ? 30.530 -4.356  -62.449 1.00 35.87 ? 142 PRO B CA    1 
ATOM   3818 C C     . PRO B 1 151 ? 30.769 -3.267  -63.482 1.00 32.42 ? 142 PRO B C     1 
ATOM   3819 O O     . PRO B 1 151 ? 31.929 -2.906  -63.723 1.00 36.39 ? 142 PRO B O     1 
ATOM   3820 C CB    . PRO B 1 151 ? 30.550 -5.752  -63.087 1.00 32.00 ? 142 PRO B CB    1 
ATOM   3821 C CG    . PRO B 1 151 ? 29.586 -6.547  -62.278 1.00 32.43 ? 142 PRO B CG    1 
ATOM   3822 C CD    . PRO B 1 151 ? 28.499 -5.591  -61.900 1.00 28.31 ? 142 PRO B CD    1 
ATOM   3823 N N     . ASP B 1 152 ? 29.722 -2.724  -64.100 1.00 29.70 ? 143 ASP B N     1 
ATOM   3824 C CA    . ASP B 1 152 ? 29.895 -1.684  -65.108 1.00 36.41 ? 143 ASP B CA    1 
ATOM   3825 C C     . ASP B 1 152 ? 29.861 -0.274  -64.525 1.00 36.56 ? 143 ASP B C     1 
ATOM   3826 O O     . ASP B 1 152 ? 29.860 0.698   -65.289 1.00 36.14 ? 143 ASP B O     1 
ATOM   3827 C CB    . ASP B 1 152 ? 28.838 -1.824  -66.211 1.00 38.36 ? 143 ASP B CB    1 
ATOM   3828 C CG    . ASP B 1 152 ? 27.414 -1.744  -65.685 1.00 39.19 ? 143 ASP B CG    1 
ATOM   3829 O OD1   . ASP B 1 152 ? 27.222 -1.517  -64.471 1.00 39.91 ? 143 ASP B OD1   1 
ATOM   3830 O OD2   . ASP B 1 152 ? 26.481 -1.908  -66.500 1.00 43.39 ? 143 ASP B OD2   1 
ATOM   3831 N N     . GLY B 1 153 ? 29.841 -0.137  -63.200 1.00 36.78 ? 144 GLY B N     1 
ATOM   3832 C CA    . GLY B 1 153 ? 29.848 1.162   -62.561 1.00 32.68 ? 144 GLY B CA    1 
ATOM   3833 C C     . GLY B 1 153 ? 28.484 1.699   -62.185 1.00 32.66 ? 144 GLY B C     1 
ATOM   3834 O O     . GLY B 1 153 ? 28.410 2.692   -61.450 1.00 41.38 ? 144 GLY B O     1 
ATOM   3835 N N     . THR B 1 154 ? 27.409 1.084   -62.667 1.00 35.32 ? 145 THR B N     1 
ATOM   3836 C CA    . THR B 1 154 ? 26.064 1.485   -62.290 1.00 33.82 ? 145 THR B CA    1 
ATOM   3837 C C     . THR B 1 154 ? 25.695 0.867   -60.942 1.00 41.35 ? 145 THR B C     1 
ATOM   3838 O O     . THR B 1 154 ? 26.481 0.145   -60.321 1.00 36.25 ? 145 THR B O     1 
ATOM   3839 C CB    . THR B 1 154 ? 25.063 1.074   -63.366 1.00 38.48 ? 145 THR B CB    1 
ATOM   3840 O OG1   . THR B 1 154 ? 24.912 -0.351  -63.353 1.00 40.79 ? 145 THR B OG1   1 
ATOM   3841 C CG2   . THR B 1 154 ? 25.549 1.510   -64.741 1.00 40.58 ? 145 THR B CG2   1 
ATOM   3842 N N     . HIS B 1 155 ? 24.477 1.143   -60.485 1.00 33.33 ? 146 HIS B N     1 
ATOM   3843 C CA    . HIS B 1 155 ? 23.969 0.597   -59.235 1.00 40.07 ? 146 HIS B CA    1 
ATOM   3844 C C     . HIS B 1 155 ? 22.711 -0.217  -59.503 1.00 37.73 ? 146 HIS B C     1 
ATOM   3845 O O     . HIS B 1 155 ? 21.894 0.148   -60.353 1.00 41.30 ? 146 HIS B O     1 
ATOM   3846 C CB    . HIS B 1 155 ? 23.687 1.713   -58.223 1.00 39.25 ? 146 HIS B CB    1 
ATOM   3847 C CG    . HIS B 1 155 ? 24.926 2.321   -57.645 1.00 39.58 ? 146 HIS B CG    1 
ATOM   3848 N ND1   . HIS B 1 155 ? 25.471 1.906   -56.449 1.00 46.67 ? 146 HIS B ND1   1 
ATOM   3849 C CD2   . HIS B 1 155 ? 25.737 3.301   -58.107 1.00 44.12 ? 146 HIS B CD2   1 
ATOM   3850 C CE1   . HIS B 1 155 ? 26.560 2.610   -56.195 1.00 45.39 ? 146 HIS B CE1   1 
ATOM   3851 N NE2   . HIS B 1 155 ? 26.743 3.464   -57.186 1.00 40.44 ? 146 HIS B NE2   1 
ATOM   3852 N N     . GLY B 1 156 ? 22.566 -1.327  -58.780 1.00 39.39 ? 147 GLY B N     1 
ATOM   3853 C CA    . GLY B 1 156 ? 21.461 -2.238  -59.004 1.00 30.86 ? 147 GLY B CA    1 
ATOM   3854 C C     . GLY B 1 156 ? 20.655 -2.548  -57.760 1.00 37.64 ? 147 GLY B C     1 
ATOM   3855 O O     . GLY B 1 156 ? 20.884 -1.963  -56.698 1.00 33.78 ? 147 GLY B O     1 
ATOM   3856 N N     . ILE B 1 157 ? 19.709 -3.476  -57.880 1.00 37.84 ? 148 ILE B N     1 
ATOM   3857 C CA    . ILE B 1 157 ? 18.783 -3.809  -56.803 1.00 39.29 ? 148 ILE B CA    1 
ATOM   3858 C C     . ILE B 1 157 ? 19.274 -5.070  -56.104 1.00 34.49 ? 148 ILE B C     1 
ATOM   3859 O O     . ILE B 1 157 ? 19.640 -6.051  -56.761 1.00 36.31 ? 148 ILE B O     1 
ATOM   3860 C CB    . ILE B 1 157 ? 17.354 -3.996  -57.345 1.00 34.41 ? 148 ILE B CB    1 
ATOM   3861 C CG1   . ILE B 1 157 ? 16.836 -2.686  -57.943 1.00 41.23 ? 148 ILE B CG1   1 
ATOM   3862 C CG2   . ILE B 1 157 ? 16.417 -4.486  -56.253 1.00 41.10 ? 148 ILE B CG2   1 
ATOM   3863 C CD1   . ILE B 1 157 ? 16.401 -1.674  -56.909 1.00 49.37 ? 148 ILE B CD1   1 
ATOM   3864 N N     . TYR B 1 158 ? 19.298 -5.044  -54.782 1.00 38.35 ? 149 TYR B N     1 
ATOM   3865 C CA    . TYR B 1 158 ? 19.607 -6.243  -54.014 1.00 35.34 ? 149 TYR B CA    1 
ATOM   3866 C C     . TYR B 1 158 ? 18.495 -7.266  -54.204 1.00 37.62 ? 149 TYR B C     1 
ATOM   3867 O O     . TYR B 1 158 ? 17.343 -6.986  -53.840 1.00 31.27 ? 149 TYR B O     1 
ATOM   3868 C CB    . TYR B 1 158 ? 19.761 -5.914  -52.536 1.00 30.81 ? 149 TYR B CB    1 
ATOM   3869 C CG    . TYR B 1 158 ? 21.006 -5.131  -52.206 1.00 38.40 ? 149 TYR B CG    1 
ATOM   3870 C CD1   . TYR B 1 158 ? 22.249 -5.749  -52.170 1.00 31.79 ? 149 TYR B CD1   1 
ATOM   3871 C CD2   . TYR B 1 158 ? 20.940 -3.769  -51.940 1.00 37.31 ? 149 TYR B CD2   1 
ATOM   3872 C CE1   . TYR B 1 158 ? 23.387 -5.033  -51.868 1.00 31.39 ? 149 TYR B CE1   1 
ATOM   3873 C CE2   . TYR B 1 158 ? 22.069 -3.047  -51.642 1.00 33.74 ? 149 TYR B CE2   1 
ATOM   3874 C CZ    . TYR B 1 158 ? 23.290 -3.680  -51.606 1.00 37.52 ? 149 TYR B CZ    1 
ATOM   3875 O OH    . TYR B 1 158 ? 24.420 -2.955  -51.306 1.00 35.53 ? 149 TYR B OH    1 
ATOM   3876 N N     . PRO B 1 159 ? 18.779 -8.453  -54.770 1.00 42.58 ? 150 PRO B N     1 
ATOM   3877 C CA    . PRO B 1 159 ? 17.722 -9.465  -54.917 1.00 41.12 ? 150 PRO B CA    1 
ATOM   3878 C C     . PRO B 1 159 ? 17.340 -10.106 -53.592 1.00 41.16 ? 150 PRO B C     1 
ATOM   3879 O O     . PRO B 1 159 ? 17.961 -9.839  -52.560 1.00 39.55 ? 150 PRO B O     1 
ATOM   3880 C CB    . PRO B 1 159 ? 18.351 -10.495 -55.866 1.00 41.68 ? 150 PRO B CB    1 
ATOM   3881 C CG    . PRO B 1 159 ? 19.817 -10.355 -55.630 1.00 42.32 ? 150 PRO B CG    1 
ATOM   3882 C CD    . PRO B 1 159 ? 20.059 -8.901  -55.348 1.00 41.28 ? 150 PRO B CD    1 
ATOM   3883 N N     . LYS B 1 160 ? 16.335 -10.975 -53.621 1.00 45.64 ? 151 LYS B N     1 
ATOM   3884 C CA    . LYS B 1 160 ? 15.897 -11.721 -52.447 1.00 39.07 ? 151 LYS B CA    1 
ATOM   3885 C C     . LYS B 1 160 ? 16.891 -12.838 -52.136 1.00 40.41 ? 151 LYS B C     1 
ATOM   3886 O O     . LYS B 1 160 ? 17.302 -13.572 -53.039 1.00 41.00 ? 151 LYS B O     1 
ATOM   3887 C CB    . LYS B 1 160 ? 14.513 -12.316 -52.678 1.00 47.29 ? 151 LYS B CB    1 
ATOM   3888 C CG    . LYS B 1 160 ? 13.373 -11.392 -52.297 1.00 53.62 ? 151 LYS B CG    1 
ATOM   3889 C CD    . LYS B 1 160 ? 12.033 -12.104 -52.387 1.00 56.19 ? 151 LYS B CD    1 
ATOM   3890 C CE    . LYS B 1 160 ? 12.123 -13.517 -51.840 1.00 56.69 ? 151 LYS B CE    1 
ATOM   3891 N NZ    . LYS B 1 160 ? 12.509 -13.529 -50.400 1.00 55.33 ? 151 LYS B NZ    1 
ATOM   3892 N N     . PRO B 1 161 ? 17.295 -12.985 -50.880 1.00 40.70 ? 152 PRO B N     1 
ATOM   3893 C CA    . PRO B 1 161 ? 18.213 -14.064 -50.514 1.00 36.47 ? 152 PRO B CA    1 
ATOM   3894 C C     . PRO B 1 161 ? 17.484 -15.360 -50.183 1.00 36.61 ? 152 PRO B C     1 
ATOM   3895 O O     . PRO B 1 161 ? 16.275 -15.394 -49.941 1.00 33.44 ? 152 PRO B O     1 
ATOM   3896 C CB    . PRO B 1 161 ? 18.921 -13.504 -49.273 1.00 32.17 ? 152 PRO B CB    1 
ATOM   3897 C CG    . PRO B 1 161 ? 17.889 -12.626 -48.633 1.00 34.61 ? 152 PRO B CG    1 
ATOM   3898 C CD    . PRO B 1 161 ? 16.996 -12.098 -49.741 1.00 36.09 ? 152 PRO B CD    1 
ATOM   3899 N N     . ARG B 1 162 ? 18.260 -16.442 -50.172 1.00 32.35 ? 153 ARG B N     1 
ATOM   3900 C CA    . ARG B 1 162 ? 17.779 -17.764 -49.795 1.00 35.15 ? 153 ARG B CA    1 
ATOM   3901 C C     . ARG B 1 162 ? 18.166 -18.040 -48.349 1.00 30.46 ? 153 ARG B C     1 
ATOM   3902 O O     . ARG B 1 162 ? 19.328 -17.860 -47.971 1.00 32.34 ? 153 ARG B O     1 
ATOM   3903 C CB    . ARG B 1 162 ? 18.367 -18.831 -50.720 1.00 34.43 ? 153 ARG B CB    1 
ATOM   3904 C CG    . ARG B 1 162 ? 17.993 -20.255 -50.366 1.00 37.86 ? 153 ARG B CG    1 
ATOM   3905 C CD    . ARG B 1 162 ? 18.451 -21.215 -51.455 1.00 39.15 ? 153 ARG B CD    1 
ATOM   3906 N NE    . ARG B 1 162 ? 19.896 -21.174 -51.654 1.00 37.62 ? 153 ARG B NE    1 
ATOM   3907 C CZ    . ARG B 1 162 ? 20.783 -21.755 -50.855 1.00 40.55 ? 153 ARG B CZ    1 
ATOM   3908 N NH1   . ARG B 1 162 ? 20.409 -22.430 -49.781 1.00 36.85 ? 153 ARG B NH1   1 
ATOM   3909 N NH2   . ARG B 1 162 ? 22.078 -21.657 -51.142 1.00 34.25 ? 153 ARG B NH2   1 
ATOM   3910 N N     . ALA B 1 163 ? 17.193 -18.467 -47.543 1.00 36.34 ? 154 ALA B N     1 
ATOM   3911 C CA    . ALA B 1 163 ? 17.432 -18.748 -46.131 1.00 33.90 ? 154 ALA B CA    1 
ATOM   3912 C C     . ALA B 1 163 ? 18.019 -20.146 -45.980 1.00 36.10 ? 154 ALA B C     1 
ATOM   3913 O O     . ALA B 1 163 ? 17.369 -21.140 -46.325 1.00 38.75 ? 154 ALA B O     1 
ATOM   3914 C CB    . ALA B 1 163 ? 16.139 -18.615 -45.331 1.00 37.63 ? 154 ALA B CB    1 
ATOM   3915 N N     . ILE B 1 164 ? 19.241 -20.222 -45.453 1.00 30.96 ? 155 ILE B N     1 
ATOM   3916 C CA    . ILE B 1 164 ? 19.990 -21.471 -45.386 1.00 35.74 ? 155 ILE B CA    1 
ATOM   3917 C C     . ILE B 1 164 ? 19.665 -22.214 -44.097 1.00 39.84 ? 155 ILE B C     1 
ATOM   3918 O O     . ILE B 1 164 ? 19.433 -21.617 -43.040 1.00 27.65 ? 155 ILE B O     1 
ATOM   3919 C CB    . ILE B 1 164 ? 21.505 -21.205 -45.506 1.00 39.86 ? 155 ILE B CB    1 
ATOM   3920 C CG1   . ILE B 1 164 ? 21.970 -20.232 -44.419 1.00 40.33 ? 155 ILE B CG1   1 
ATOM   3921 C CG2   . ILE B 1 164 ? 21.843 -20.662 -46.885 1.00 40.71 ? 155 ILE B CG2   1 
ATOM   3922 C CD1   . ILE B 1 164 ? 23.473 -20.128 -44.291 1.00 31.66 ? 155 ILE B CD1   1 
ATOM   3923 N N     . GLY B 1 165 ? 19.651 -23.543 -44.191 1.00 37.43 ? 156 GLY B N     1 
ATOM   3924 C CA    . GLY B 1 165 ? 19.464 -24.385 -43.033 1.00 27.06 ? 156 GLY B CA    1 
ATOM   3925 C C     . GLY B 1 165 ? 20.752 -24.577 -42.256 1.00 35.95 ? 156 GLY B C     1 
ATOM   3926 O O     . GLY B 1 165 ? 21.815 -24.060 -42.602 1.00 33.16 ? 156 GLY B O     1 
ATOM   3927 N N     . THR B 1 166 ? 20.647 -25.356 -41.176 1.00 34.47 ? 157 THR B N     1 
ATOM   3928 C CA    . THR B 1 166 ? 21.782 -25.507 -40.272 1.00 34.98 ? 157 THR B CA    1 
ATOM   3929 C C     . THR B 1 166 ? 22.920 -26.290 -40.911 1.00 29.20 ? 157 THR B C     1 
ATOM   3930 O O     . THR B 1 166 ? 24.092 -26.013 -40.629 1.00 32.79 ? 157 THR B O     1 
ATOM   3931 C CB    . THR B 1 166 ? 21.345 -26.181 -38.971 1.00 36.02 ? 157 THR B CB    1 
ATOM   3932 O OG1   . THR B 1 166 ? 20.906 -27.516 -39.248 1.00 33.43 ? 157 THR B OG1   1 
ATOM   3933 C CG2   . THR B 1 166 ? 20.214 -25.398 -38.318 1.00 37.42 ? 157 THR B CG2   1 
ATOM   3934 N N     . TYR B 1 167 ? 22.609 -27.268 -41.764 1.00 33.42 ? 158 TYR B N     1 
ATOM   3935 C CA    . TYR B 1 167 ? 23.675 -28.007 -42.432 1.00 30.72 ? 158 TYR B CA    1 
ATOM   3936 C C     . TYR B 1 167 ? 24.509 -27.081 -43.305 1.00 30.35 ? 158 TYR B C     1 
ATOM   3937 O O     . TYR B 1 167 ? 25.745 -27.129 -43.281 1.00 30.12 ? 158 TYR B O     1 
ATOM   3938 C CB    . TYR B 1 167 ? 23.101 -29.152 -43.265 1.00 37.16 ? 158 TYR B CB    1 
ATOM   3939 C CG    . TYR B 1 167 ? 24.114 -29.717 -44.233 1.00 30.17 ? 158 TYR B CG    1 
ATOM   3940 C CD1   . TYR B 1 167 ? 25.256 -30.358 -43.771 1.00 32.17 ? 158 TYR B CD1   1 
ATOM   3941 C CD2   . TYR B 1 167 ? 23.944 -29.586 -45.605 1.00 40.26 ? 158 TYR B CD2   1 
ATOM   3942 C CE1   . TYR B 1 167 ? 26.192 -30.867 -44.646 1.00 40.52 ? 158 TYR B CE1   1 
ATOM   3943 C CE2   . TYR B 1 167 ? 24.877 -30.093 -46.491 1.00 36.53 ? 158 TYR B CE2   1 
ATOM   3944 C CZ    . TYR B 1 167 ? 25.998 -30.732 -46.004 1.00 39.86 ? 158 TYR B CZ    1 
ATOM   3945 O OH    . TYR B 1 167 ? 26.932 -31.238 -46.875 1.00 43.29 ? 158 TYR B OH    1 
ATOM   3946 N N     . GLU B 1 168 ? 23.848 -26.219 -44.082 1.00 33.47 ? 159 GLU B N     1 
ATOM   3947 C CA    . GLU B 1 168 ? 24.586 -25.273 -44.911 1.00 34.90 ? 159 GLU B CA    1 
ATOM   3948 C C     . GLU B 1 168 ? 25.336 -24.256 -44.062 1.00 36.35 ? 159 GLU B C     1 
ATOM   3949 O O     . GLU B 1 168 ? 26.369 -23.731 -44.494 1.00 36.41 ? 159 GLU B O     1 
ATOM   3950 C CB    . GLU B 1 168 ? 23.637 -24.567 -45.879 1.00 35.96 ? 159 GLU B CB    1 
ATOM   3951 C CG    . GLU B 1 168 ? 24.341 -23.691 -46.903 1.00 44.03 ? 159 GLU B CG    1 
ATOM   3952 C CD    . GLU B 1 168 ? 23.503 -23.444 -48.141 1.00 44.06 ? 159 GLU B CD    1 
ATOM   3953 O OE1   . GLU B 1 168 ? 22.374 -23.978 -48.216 1.00 45.13 ? 159 GLU B OE1   1 
ATOM   3954 O OE2   . GLU B 1 168 ? 23.971 -22.711 -49.038 1.00 49.20 ? 159 GLU B OE2   1 
ATOM   3955 N N     . ILE B 1 169 ? 24.837 -23.967 -42.857 1.00 34.17 ? 160 ILE B N     1 
ATOM   3956 C CA    . ILE B 1 169 ? 25.567 -23.099 -41.936 1.00 30.88 ? 160 ILE B CA    1 
ATOM   3957 C C     . ILE B 1 169 ? 26.894 -23.738 -41.550 1.00 35.29 ? 160 ILE B C     1 
ATOM   3958 O O     . ILE B 1 169 ? 27.939 -23.074 -41.526 1.00 38.08 ? 160 ILE B O     1 
ATOM   3959 C CB    . ILE B 1 169 ? 24.703 -22.788 -40.698 1.00 36.75 ? 160 ILE B CB    1 
ATOM   3960 C CG1   . ILE B 1 169 ? 23.643 -21.735 -41.029 1.00 29.89 ? 160 ILE B CG1   1 
ATOM   3961 C CG2   . ILE B 1 169 ? 25.566 -22.333 -39.531 1.00 34.83 ? 160 ILE B CG2   1 
ATOM   3962 C CD1   . ILE B 1 169 ? 22.477 -21.717 -40.055 1.00 36.74 ? 160 ILE B CD1   1 
ATOM   3963 N N     . SER B 1 170 ? 26.879 -25.041 -41.254 1.00 33.67 ? 161 SER B N     1 
ATOM   3964 C CA    . SER B 1 170 ? 28.108 -25.739 -40.896 1.00 33.12 ? 161 SER B CA    1 
ATOM   3965 C C     . SER B 1 170 ? 29.084 -25.824 -42.061 1.00 33.37 ? 161 SER B C     1 
ATOM   3966 O O     . SER B 1 170 ? 30.292 -25.947 -41.830 1.00 37.08 ? 161 SER B O     1 
ATOM   3967 C CB    . SER B 1 170 ? 27.784 -27.143 -40.374 1.00 35.40 ? 161 SER B CB    1 
ATOM   3968 O OG    . SER B 1 170 ? 27.229 -27.958 -41.392 1.00 37.55 ? 161 SER B OG    1 
ATOM   3969 N N     . GLN B 1 171 ? 28.594 -25.758 -43.301 1.00 31.75 ? 162 GLN B N     1 
ATOM   3970 C CA    . GLN B 1 171 ? 29.485 -25.720 -44.455 1.00 32.51 ? 162 GLN B CA    1 
ATOM   3971 C C     . GLN B 1 171 ? 30.099 -24.335 -44.641 1.00 34.95 ? 162 GLN B C     1 
ATOM   3972 O O     . GLN B 1 171 ? 31.275 -24.218 -45.005 1.00 27.42 ? 162 GLN B O     1 
ATOM   3973 C CB    . GLN B 1 171 ? 28.731 -26.148 -45.713 1.00 32.42 ? 162 GLN B CB    1 
ATOM   3974 C CG    . GLN B 1 171 ? 28.042 -27.496 -45.583 1.00 43.09 ? 162 GLN B CG    1 
ATOM   3975 C CD    . GLN B 1 171 ? 28.933 -28.546 -44.946 1.00 44.45 ? 162 GLN B CD    1 
ATOM   3976 O OE1   . GLN B 1 171 ? 29.915 -28.988 -45.543 1.00 45.93 ? 162 GLN B OE1   1 
ATOM   3977 N NE2   . GLN B 1 171 ? 28.600 -28.945 -43.722 1.00 44.25 ? 162 GLN B NE2   1 
ATOM   3978 N N     . VAL B 1 172 ? 29.323 -23.277 -44.396 1.00 35.34 ? 163 VAL B N     1 
ATOM   3979 C CA    . VAL B 1 172 ? 29.892 -21.933 -44.422 1.00 34.03 ? 163 VAL B CA    1 
ATOM   3980 C C     . VAL B 1 172 ? 30.956 -21.792 -43.343 1.00 30.06 ? 163 VAL B C     1 
ATOM   3981 O O     . VAL B 1 172 ? 32.007 -21.178 -43.563 1.00 32.33 ? 163 VAL B O     1 
ATOM   3982 C CB    . VAL B 1 172 ? 28.783 -20.875 -44.274 1.00 34.22 ? 163 VAL B CB    1 
ATOM   3983 C CG1   . VAL B 1 172 ? 29.385 -19.482 -44.141 1.00 28.95 ? 163 VAL B CG1   1 
ATOM   3984 C CG2   . VAL B 1 172 ? 27.838 -20.935 -45.464 1.00 39.22 ? 163 VAL B CG2   1 
ATOM   3985 N N     . VAL B 1 173 ? 30.708 -22.372 -42.163 1.00 35.86 ? 164 VAL B N     1 
ATOM   3986 C CA    . VAL B 1 173 ? 31.720 -22.385 -41.110 1.00 29.65 ? 164 VAL B CA    1 
ATOM   3987 C C     . VAL B 1 173 ? 32.975 -23.105 -41.591 1.00 31.17 ? 164 VAL B C     1 
ATOM   3988 O O     . VAL B 1 173 ? 34.102 -22.654 -41.349 1.00 30.94 ? 164 VAL B O     1 
ATOM   3989 C CB    . VAL B 1 173 ? 31.148 -23.024 -39.828 1.00 37.11 ? 164 VAL B CB    1 
ATOM   3990 C CG1   . VAL B 1 173 ? 32.258 -23.361 -38.854 1.00 31.09 ? 164 VAL B CG1   1 
ATOM   3991 C CG2   . VAL B 1 173 ? 30.131 -22.101 -39.168 1.00 26.37 ? 164 VAL B CG2   1 
ATOM   3992 N N     . GLU B 1 174 ? 32.801 -24.228 -42.295 1.00 34.16 ? 165 GLU B N     1 
ATOM   3993 C CA    . GLU B 1 174 ? 33.945 -24.934 -42.864 1.00 34.86 ? 165 GLU B CA    1 
ATOM   3994 C C     . GLU B 1 174 ? 34.673 -24.086 -43.900 1.00 36.85 ? 165 GLU B C     1 
ATOM   3995 O O     . GLU B 1 174 ? 35.899 -24.185 -44.031 1.00 34.03 ? 165 GLU B O     1 
ATOM   3996 C CB    . GLU B 1 174 ? 33.493 -26.252 -43.492 1.00 39.27 ? 165 GLU B CB    1 
ATOM   3997 C CG    . GLU B 1 174 ? 33.750 -27.477 -42.631 1.00 50.84 ? 165 GLU B CG    1 
ATOM   3998 C CD    . GLU B 1 174 ? 35.211 -27.623 -42.246 1.00 54.63 ? 165 GLU B CD    1 
ATOM   3999 O OE1   . GLU B 1 174 ? 36.050 -27.841 -43.147 1.00 54.51 ? 165 GLU B OE1   1 
ATOM   4000 O OE2   . GLU B 1 174 ? 35.518 -27.522 -41.039 1.00 51.62 ? 165 GLU B OE2   1 
ATOM   4001 N N     . ASP B 1 175 ? 33.941 -23.260 -44.653 1.00 30.18 ? 166 ASP B N     1 
ATOM   4002 C CA    . ASP B 1 175 ? 34.592 -22.361 -45.601 1.00 34.09 ? 166 ASP B CA    1 
ATOM   4003 C C     . ASP B 1 175 ? 35.503 -21.375 -44.881 1.00 29.97 ? 166 ASP B C     1 
ATOM   4004 O O     . ASP B 1 175 ? 36.619 -21.102 -45.338 1.00 30.09 ? 166 ASP B O     1 
ATOM   4005 C CB    . ASP B 1 175 ? 33.547 -21.613 -46.429 1.00 31.47 ? 166 ASP B CB    1 
ATOM   4006 C CG    . ASP B 1 175 ? 32.839 -22.507 -47.425 1.00 33.50 ? 166 ASP B CG    1 
ATOM   4007 O OD1   . ASP B 1 175 ? 33.436 -23.515 -47.856 1.00 38.74 ? 166 ASP B OD1   1 
ATOM   4008 O OD2   . ASP B 1 175 ? 31.682 -22.197 -47.778 1.00 39.37 ? 166 ASP B OD2   1 
ATOM   4009 N N     . TYR B 1 176 ? 35.041 -20.830 -43.751 1.00 34.95 ? 167 TYR B N     1 
ATOM   4010 C CA    . TYR B 1 176 ? 35.875 -19.937 -42.953 1.00 29.85 ? 167 TYR B CA    1 
ATOM   4011 C C     . TYR B 1 176 ? 37.118 -20.660 -42.451 1.00 26.49 ? 167 TYR B C     1 
ATOM   4012 O O     . TYR B 1 176 ? 38.233 -20.129 -42.516 1.00 33.80 ? 167 TYR B O     1 
ATOM   4013 C CB    . TYR B 1 176 ? 35.075 -19.387 -41.771 1.00 26.09 ? 167 TYR B CB    1 
ATOM   4014 C CG    . TYR B 1 176 ? 34.246 -18.156 -42.059 1.00 28.02 ? 167 TYR B CG    1 
ATOM   4015 C CD1   . TYR B 1 176 ? 34.842 -16.909 -42.207 1.00 25.57 ? 167 TYR B CD1   1 
ATOM   4016 C CD2   . TYR B 1 176 ? 32.861 -18.236 -42.153 1.00 20.26 ? 167 TYR B CD2   1 
ATOM   4017 C CE1   . TYR B 1 176 ? 34.082 -15.781 -42.458 1.00 24.08 ? 167 TYR B CE1   1 
ATOM   4018 C CE2   . TYR B 1 176 ? 32.094 -17.114 -42.401 1.00 29.98 ? 167 TYR B CE2   1 
ATOM   4019 C CZ    . TYR B 1 176 ? 32.709 -15.890 -42.553 1.00 25.48 ? 167 TYR B CZ    1 
ATOM   4020 O OH    . TYR B 1 176 ? 31.947 -14.774 -42.802 1.00 30.94 ? 167 TYR B OH    1 
ATOM   4021 N N     . ARG B 1 177 ? 36.937 -21.876 -41.932 1.00 35.70 ? 168 ARG B N     1 
ATOM   4022 C CA    . ARG B 1 177 ? 38.068 -22.653 -41.435 1.00 40.81 ? 168 ARG B CA    1 
ATOM   4023 C C     . ARG B 1 177 ? 39.059 -22.960 -42.550 1.00 28.22 ? 168 ARG B C     1 
ATOM   4024 O O     . ARG B 1 177 ? 40.276 -22.861 -42.354 1.00 31.22 ? 168 ARG B O     1 
ATOM   4025 C CB    . ARG B 1 177 ? 37.568 -23.946 -40.790 1.00 38.69 ? 168 ARG B CB    1 
ATOM   4026 C CG    . ARG B 1 177 ? 38.664 -24.800 -40.182 1.00 37.98 ? 168 ARG B CG    1 
ATOM   4027 C CD    . ARG B 1 177 ? 38.112 -26.115 -39.648 1.00 45.14 ? 168 ARG B CD    1 
ATOM   4028 N NE    . ARG B 1 177 ? 38.592 -27.259 -40.414 1.00 48.09 ? 168 ARG B NE    1 
ATOM   4029 C CZ    . ARG B 1 177 ? 39.809 -27.776 -40.307 1.00 60.71 ? 168 ARG B CZ    1 
ATOM   4030 N NH1   . ARG B 1 177 ? 40.700 -27.282 -39.461 1.00 53.82 ? 168 ARG B NH1   1 
ATOM   4031 N NH2   . ARG B 1 177 ? 40.142 -28.816 -41.066 1.00 60.27 ? 168 ARG B NH2   1 
ATOM   4032 N N     . ARG B 1 178 ? 38.554 -23.336 -43.728 1.00 32.48 ? 169 ARG B N     1 
ATOM   4033 C CA    . ARG B 1 178 ? 39.428 -23.660 -44.851 1.00 31.76 ? 169 ARG B CA    1 
ATOM   4034 C C     . ARG B 1 178 ? 40.192 -22.433 -45.331 1.00 32.59 ? 169 ARG B C     1 
ATOM   4035 O O     . ARG B 1 178 ? 41.389 -22.515 -45.631 1.00 30.72 ? 169 ARG B O     1 
ATOM   4036 C CB    . ARG B 1 178 ? 38.608 -24.252 -45.996 1.00 37.42 ? 169 ARG B CB    1 
ATOM   4037 C CG    . ARG B 1 178 ? 38.473 -25.761 -45.965 1.00 53.88 ? 169 ARG B CG    1 
ATOM   4038 C CD    . ARG B 1 178 ? 37.640 -26.245 -47.140 1.00 67.40 ? 169 ARG B CD    1 
ATOM   4039 N NE    . ARG B 1 178 ? 38.133 -27.503 -47.687 1.00 71.66 ? 169 ARG B NE    1 
ATOM   4040 C CZ    . ARG B 1 178 ? 37.854 -28.698 -47.186 1.00 78.29 ? 169 ARG B CZ    1 
ATOM   4041 N NH1   . ARG B 1 178 ? 37.082 -28.839 -46.121 1.00 72.96 ? 169 ARG B NH1   1 
ATOM   4042 N NH2   . ARG B 1 178 ? 38.359 -29.780 -47.773 1.00 75.98 ? 169 ARG B NH2   1 
ATOM   4043 N N     . SER B 1 179 ? 39.513 -21.287 -45.418 1.00 35.14 ? 170 SER B N     1 
ATOM   4044 C CA    . SER B 1 179 ? 40.174 -20.066 -45.863 1.00 36.14 ? 170 SER B CA    1 
ATOM   4045 C C     . SER B 1 179 ? 41.255 -19.632 -44.882 1.00 32.17 ? 170 SER B C     1 
ATOM   4046 O O     . SER B 1 179 ? 42.297 -19.108 -45.291 1.00 35.81 ? 170 SER B O     1 
ATOM   4047 C CB    . SER B 1 179 ? 39.142 -18.956 -46.052 1.00 33.66 ? 170 SER B CB    1 
ATOM   4048 O OG    . SER B 1 179 ? 38.157 -19.349 -46.988 1.00 36.20 ? 170 SER B OG    1 
ATOM   4049 N N     . ALA B 1 180 ? 41.026 -19.846 -43.584 1.00 38.26 ? 171 ALA B N     1 
ATOM   4050 C CA    . ALA B 1 180 ? 42.023 -19.475 -42.585 1.00 32.23 ? 171 ALA B CA    1 
ATOM   4051 C C     . ALA B 1 180 ? 43.301 -20.282 -42.764 1.00 33.12 ? 171 ALA B C     1 
ATOM   4052 O O     . ALA B 1 180 ? 44.409 -19.733 -42.724 1.00 32.18 ? 171 ALA B O     1 
ATOM   4053 C CB    . ALA B 1 180 ? 41.452 -19.670 -41.181 1.00 32.23 ? 171 ALA B CB    1 
ATOM   4054 N N     . LEU B 1 181 ? 43.165 -21.596 -42.965 1.00 34.69 ? 172 LEU B N     1 
ATOM   4055 C CA    . LEU B 1 181 ? 44.333 -22.429 -43.229 1.00 32.71 ? 172 LEU B CA    1 
ATOM   4056 C C     . LEU B 1 181 ? 45.033 -22.001 -44.511 1.00 34.03 ? 172 LEU B C     1 
ATOM   4057 O O     . LEU B 1 181 ? 46.267 -22.036 -44.597 1.00 32.94 ? 172 LEU B O     1 
ATOM   4058 C CB    . LEU B 1 181 ? 43.920 -23.899 -43.304 1.00 31.95 ? 172 LEU B CB    1 
ATOM   4059 C CG    . LEU B 1 181 ? 43.494 -24.510 -41.967 1.00 37.17 ? 172 LEU B CG    1 
ATOM   4060 C CD1   . LEU B 1 181 ? 42.688 -25.783 -42.179 1.00 38.33 ? 172 LEU B CD1   1 
ATOM   4061 C CD2   . LEU B 1 181 ? 44.715 -24.773 -41.101 1.00 34.22 ? 172 LEU B CD2   1 
ATOM   4062 N N     . ASN B 1 182 ? 44.261 -21.592 -45.519 1.00 31.98 ? 173 ASN B N     1 
ATOM   4063 C CA    . ASN B 1 182 ? 44.862 -21.085 -46.748 1.00 34.53 ? 173 ASN B CA    1 
ATOM   4064 C C     . ASN B 1 182 ? 45.633 -19.798 -46.491 1.00 31.79 ? 173 ASN B C     1 
ATOM   4065 O O     . ASN B 1 182 ? 46.705 -19.582 -47.067 1.00 32.39 ? 173 ASN B O     1 
ATOM   4066 C CB    . ASN B 1 182 ? 43.780 -20.861 -47.804 1.00 31.17 ? 173 ASN B CB    1 
ATOM   4067 C CG    . ASN B 1 182 ? 43.394 -22.137 -48.516 1.00 38.60 ? 173 ASN B CG    1 
ATOM   4068 O OD1   . ASN B 1 182 ? 43.938 -23.204 -48.236 1.00 37.48 ? 173 ASN B OD1   1 
ATOM   4069 N ND2   . ASN B 1 182 ? 42.446 -22.036 -49.441 1.00 35.85 ? 173 ASN B ND2   1 
ATOM   4070 N N     . ALA B 1 183 ? 45.103 -18.930 -45.623 1.00 29.76 ? 174 ALA B N     1 
ATOM   4071 C CA    . ALA B 1 183 ? 45.784 -17.674 -45.327 1.00 27.69 ? 174 ALA B CA    1 
ATOM   4072 C C     . ALA B 1 183 ? 47.112 -17.920 -44.625 1.00 29.35 ? 174 ALA B C     1 
ATOM   4073 O O     . ALA B 1 183 ? 48.108 -17.249 -44.917 1.00 32.25 ? 174 ALA B O     1 
ATOM   4074 C CB    . ALA B 1 183 ? 44.883 -16.778 -44.479 1.00 28.46 ? 174 ALA B CB    1 
ATOM   4075 N N     . ILE B 1 184 ? 47.146 -18.879 -43.698 1.00 33.97 ? 175 ILE B N     1 
ATOM   4076 C CA    . ILE B 1 184 ? 48.405 -19.260 -43.066 1.00 33.17 ? 175 ILE B CA    1 
ATOM   4077 C C     . ILE B 1 184 ? 49.342 -19.888 -44.090 1.00 29.20 ? 175 ILE B C     1 
ATOM   4078 O O     . ILE B 1 184 ? 50.556 -19.649 -44.071 1.00 32.78 ? 175 ILE B O     1 
ATOM   4079 C CB    . ILE B 1 184 ? 48.136 -20.204 -41.879 1.00 37.34 ? 175 ILE B CB    1 
ATOM   4080 C CG1   . ILE B 1 184 ? 47.442 -19.442 -40.751 1.00 31.27 ? 175 ILE B CG1   1 
ATOM   4081 C CG2   . ILE B 1 184 ? 49.431 -20.825 -41.375 1.00 39.18 ? 175 ILE B CG2   1 
ATOM   4082 C CD1   . ILE B 1 184 ? 48.309 -18.378 -40.118 1.00 40.36 ? 175 ILE B CD1   1 
ATOM   4083 N N     . GLU B 1 185 ? 48.795 -20.689 -45.008 1.00 34.38 ? 176 GLU B N     1 
ATOM   4084 C CA    . GLU B 1 185 ? 49.611 -21.251 -46.079 1.00 35.10 ? 176 GLU B CA    1 
ATOM   4085 C C     . GLU B 1 185 ? 50.213 -20.152 -46.946 1.00 34.50 ? 176 GLU B C     1 
ATOM   4086 O O     . GLU B 1 185 ? 51.367 -20.254 -47.379 1.00 37.59 ? 176 GLU B O     1 
ATOM   4087 C CB    . GLU B 1 185 ? 48.775 -22.211 -46.927 1.00 36.50 ? 176 GLU B CB    1 
ATOM   4088 C CG    . GLU B 1 185 ? 49.550 -22.895 -48.041 1.00 46.88 ? 176 GLU B CG    1 
ATOM   4089 C CD    . GLU B 1 185 ? 48.682 -23.824 -48.871 1.00 50.50 ? 176 GLU B CD    1 
ATOM   4090 O OE1   . GLU B 1 185 ? 47.553 -24.132 -48.434 1.00 53.15 ? 176 GLU B OE1   1 
ATOM   4091 O OE2   . GLU B 1 185 ? 49.130 -24.250 -49.957 1.00 45.39 ? 176 GLU B OE2   1 
ATOM   4092 N N     . ALA B 1 186 ? 49.455 -19.083 -47.197 1.00 36.66 ? 177 ALA B N     1 
ATOM   4093 C CA    . ALA B 1 186 ? 49.979 -17.959 -47.962 1.00 31.25 ? 177 ALA B CA    1 
ATOM   4094 C C     . ALA B 1 186 ? 51.037 -17.173 -47.201 1.00 34.59 ? 177 ALA B C     1 
ATOM   4095 O O     . ALA B 1 186 ? 51.740 -16.362 -47.813 1.00 32.67 ? 177 ALA B O     1 
ATOM   4096 C CB    . ALA B 1 186 ? 48.843 -17.021 -48.372 1.00 32.47 ? 177 ALA B CB    1 
ATOM   4097 N N     . GLY B 1 187 ? 51.165 -17.390 -45.894 1.00 26.73 ? 178 GLY B N     1 
ATOM   4098 C CA    . GLY B 1 187 ? 52.126 -16.676 -45.084 1.00 31.09 ? 178 GLY B CA    1 
ATOM   4099 C C     . GLY B 1 187 ? 51.545 -15.590 -44.208 1.00 35.22 ? 178 GLY B C     1 
ATOM   4100 O O     . GLY B 1 187 ? 52.311 -14.893 -43.532 1.00 39.76 ? 178 GLY B O     1 
ATOM   4101 N N     . PHE B 1 188 ? 50.223 -15.420 -44.197 1.00 25.90 ? 179 PHE B N     1 
ATOM   4102 C CA    . PHE B 1 188 ? 49.610 -14.402 -43.354 1.00 34.77 ? 179 PHE B CA    1 
ATOM   4103 C C     . PHE B 1 188 ? 49.898 -14.682 -41.883 1.00 36.75 ? 179 PHE B C     1 
ATOM   4104 O O     . PHE B 1 188 ? 49.937 -15.836 -41.449 1.00 33.23 ? 179 PHE B O     1 
ATOM   4105 C CB    . PHE B 1 188 ? 48.098 -14.353 -43.590 1.00 29.20 ? 179 PHE B CB    1 
ATOM   4106 C CG    . PHE B 1 188 ? 47.698 -13.584 -44.817 1.00 29.90 ? 179 PHE B CG    1 
ATOM   4107 C CD1   . PHE B 1 188 ? 47.706 -12.198 -44.817 1.00 33.16 ? 179 PHE B CD1   1 
ATOM   4108 C CD2   . PHE B 1 188 ? 47.308 -14.246 -45.971 1.00 33.62 ? 179 PHE B CD2   1 
ATOM   4109 C CE1   . PHE B 1 188 ? 47.336 -11.487 -45.946 1.00 28.93 ? 179 PHE B CE1   1 
ATOM   4110 C CE2   . PHE B 1 188 ? 46.938 -13.541 -47.103 1.00 33.96 ? 179 PHE B CE2   1 
ATOM   4111 C CZ    . PHE B 1 188 ? 46.951 -12.159 -47.090 1.00 32.88 ? 179 PHE B CZ    1 
ATOM   4112 N N     . ASP B 1 189 ? 50.111 -13.613 -41.113 1.00 33.97 ? 180 ASP B N     1 
ATOM   4113 C CA    . ASP B 1 189 ? 50.311 -13.778 -39.677 1.00 40.20 ? 180 ASP B CA    1 
ATOM   4114 C C     . ASP B 1 189 ? 49.027 -14.212 -38.985 1.00 36.87 ? 180 ASP B C     1 
ATOM   4115 O O     . ASP B 1 189 ? 49.075 -14.897 -37.958 1.00 42.30 ? 180 ASP B O     1 
ATOM   4116 C CB    . ASP B 1 189 ? 50.836 -12.479 -39.064 1.00 38.56 ? 180 ASP B CB    1 
ATOM   4117 C CG    . ASP B 1 189 ? 52.164 -12.044 -39.661 1.00 38.90 ? 180 ASP B CG    1 
ATOM   4118 O OD1   . ASP B 1 189 ? 53.195 -12.680 -39.357 1.00 43.32 ? 180 ASP B OD1   1 
ATOM   4119 O OD2   . ASP B 1 189 ? 52.178 -11.058 -40.428 1.00 40.59 ? 180 ASP B OD2   1 
ATOM   4120 N N     . GLY B 1 190 ? 47.882 -13.826 -39.530 1.00 36.75 ? 181 GLY B N     1 
ATOM   4121 C CA    . GLY B 1 190 ? 46.611 -14.242 -38.981 1.00 36.85 ? 181 GLY B CA    1 
ATOM   4122 C C     . GLY B 1 190 ? 45.479 -13.817 -39.887 1.00 38.50 ? 181 GLY B C     1 
ATOM   4123 O O     . GLY B 1 190 ? 45.695 -13.373 -41.015 1.00 34.03 ? 181 GLY B O     1 
ATOM   4124 N N     . ILE B 1 191 ? 44.257 -13.961 -39.376 1.00 35.72 ? 182 ILE B N     1 
ATOM   4125 C CA    . ILE B 1 191 ? 43.064 -13.560 -40.108 1.00 32.36 ? 182 ILE B CA    1 
ATOM   4126 C C     . ILE B 1 191 ? 42.162 -12.738 -39.197 1.00 35.40 ? 182 ILE B C     1 
ATOM   4127 O O     . ILE B 1 191 ? 42.256 -12.791 -37.969 1.00 36.45 ? 182 ILE B O     1 
ATOM   4128 C CB    . ILE B 1 191 ? 42.283 -14.765 -40.678 1.00 33.41 ? 182 ILE B CB    1 
ATOM   4129 C CG1   . ILE B 1 191 ? 41.651 -15.576 -39.549 1.00 29.03 ? 182 ILE B CG1   1 
ATOM   4130 C CG2   . ILE B 1 191 ? 43.180 -15.639 -41.531 1.00 34.57 ? 182 ILE B CG2   1 
ATOM   4131 C CD1   . ILE B 1 191 ? 40.150 -15.478 -39.512 1.00 36.62 ? 182 ILE B CD1   1 
ATOM   4132 N N     . GLU B 1 192 ? 41.276 -11.971 -39.826 1.00 31.67 ? 183 GLU B N     1 
ATOM   4133 C CA    . GLU B 1 192 ? 40.231 -11.233 -39.132 1.00 25.83 ? 183 GLU B CA    1 
ATOM   4134 C C     . GLU B 1 192 ? 38.881 -11.699 -39.652 1.00 27.92 ? 183 GLU B C     1 
ATOM   4135 O O     . GLU B 1 192 ? 38.685 -11.811 -40.867 1.00 35.27 ? 183 GLU B O     1 
ATOM   4136 C CB    . GLU B 1 192 ? 40.384 -9.721  -39.326 1.00 33.74 ? 183 GLU B CB    1 
ATOM   4137 C CG    . GLU B 1 192 ? 39.168 -8.923  -38.879 1.00 28.81 ? 183 GLU B CG    1 
ATOM   4138 C CD    . GLU B 1 192 ? 39.392 -7.427  -38.941 1.00 33.05 ? 183 GLU B CD    1 
ATOM   4139 O OE1   . GLU B 1 192 ? 40.141 -6.902  -38.093 1.00 36.41 ? 183 GLU B OE1   1 
ATOM   4140 O OE2   . GLU B 1 192 ? 38.818 -6.775  -39.836 1.00 39.57 ? 183 GLU B OE2   1 
ATOM   4141 N N     . ILE B 1 193 ? 37.963 -11.986 -38.737 1.00 29.38 ? 184 ILE B N     1 
ATOM   4142 C CA    . ILE B 1 193 ? 36.618 -12.420 -39.094 1.00 29.88 ? 184 ILE B CA    1 
ATOM   4143 C C     . ILE B 1 193 ? 35.755 -11.179 -39.282 1.00 33.60 ? 184 ILE B C     1 
ATOM   4144 O O     . ILE B 1 193 ? 35.554 -10.408 -38.339 1.00 23.19 ? 184 ILE B O     1 
ATOM   4145 C CB    . ILE B 1 193 ? 36.031 -13.349 -38.021 1.00 30.78 ? 184 ILE B CB    1 
ATOM   4146 C CG1   . ILE B 1 193 ? 36.694 -14.727 -38.084 1.00 28.87 ? 184 ILE B CG1   1 
ATOM   4147 C CG2   . ILE B 1 193 ? 34.523 -13.469 -38.179 1.00 27.60 ? 184 ILE B CG2   1 
ATOM   4148 C CD1   . ILE B 1 193 ? 36.541 -15.423 -39.430 1.00 30.76 ? 184 ILE B CD1   1 
ATOM   4149 N N     . HIS B 1 194 ? 35.255 -10.978 -40.500 1.00 27.79 ? 185 HIS B N     1 
ATOM   4150 C CA    . HIS B 1 194 ? 34.409 -9.823  -40.801 1.00 30.53 ? 185 HIS B CA    1 
ATOM   4151 C C     . HIS B 1 194 ? 32.988 -10.135 -40.351 1.00 32.24 ? 185 HIS B C     1 
ATOM   4152 O O     . HIS B 1 194 ? 32.243 -10.830 -41.043 1.00 30.12 ? 185 HIS B O     1 
ATOM   4153 C CB    . HIS B 1 194 ? 34.455 -9.491  -42.288 1.00 30.71 ? 185 HIS B CB    1 
ATOM   4154 C CG    . HIS B 1 194 ? 33.819 -8.181  -42.640 1.00 35.87 ? 185 HIS B CG    1 
ATOM   4155 N ND1   . HIS B 1 194 ? 32.778 -7.635  -41.919 1.00 30.78 ? 185 HIS B ND1   1 
ATOM   4156 C CD2   . HIS B 1 194 ? 34.069 -7.315  -43.651 1.00 34.79 ? 185 HIS B CD2   1 
ATOM   4157 C CE1   . HIS B 1 194 ? 32.421 -6.486  -42.465 1.00 37.98 ? 185 HIS B CE1   1 
ATOM   4158 N NE2   . HIS B 1 194 ? 33.189 -6.269  -43.518 1.00 29.75 ? 185 HIS B NE2   1 
ATOM   4159 N N     . GLY B 1 195 ? 32.605 -9.610  -39.190 1.00 33.23 ? 186 GLY B N     1 
ATOM   4160 C CA    . GLY B 1 195 ? 31.256 -9.798  -38.692 1.00 36.82 ? 186 GLY B CA    1 
ATOM   4161 C C     . GLY B 1 195 ? 30.539 -8.483  -38.470 1.00 32.21 ? 186 GLY B C     1 
ATOM   4162 O O     . GLY B 1 195 ? 29.782 -8.333  -37.506 1.00 32.58 ? 186 GLY B O     1 
ATOM   4163 N N     . ALA B 1 196 ? 30.762 -7.526  -39.366 1.00 30.72 ? 187 ALA B N     1 
ATOM   4164 C CA    . ALA B 1 196 ? 30.288 -6.162  -39.200 1.00 36.48 ? 187 ALA B CA    1 
ATOM   4165 C C     . ALA B 1 196 ? 29.627 -5.680  -40.487 1.00 33.70 ? 187 ALA B C     1 
ATOM   4166 O O     . ALA B 1 196 ? 29.532 -6.409  -41.480 1.00 27.42 ? 187 ALA B O     1 
ATOM   4167 C CB    . ALA B 1 196 ? 31.442 -5.231  -38.806 1.00 32.12 ? 187 ALA B CB    1 
ATOM   4168 N N     . HIS B 1 197 ? 29.152 -4.434  -40.445 1.00 31.58 ? 188 HIS B N     1 
ATOM   4169 C CA    . HIS B 1 197 ? 28.661 -3.690  -41.605 1.00 34.27 ? 188 HIS B CA    1 
ATOM   4170 C C     . HIS B 1 197 ? 27.484 -4.370  -42.303 1.00 35.89 ? 188 HIS B C     1 
ATOM   4171 O O     . HIS B 1 197 ? 27.228 -4.115  -43.483 1.00 33.54 ? 188 HIS B O     1 
ATOM   4172 C CB    . HIS B 1 197 ? 29.793 -3.426  -42.603 1.00 28.25 ? 188 HIS B CB    1 
ATOM   4173 C CG    . HIS B 1 197 ? 30.952 -2.679  -42.016 1.00 27.02 ? 188 HIS B CG    1 
ATOM   4174 N ND1   . HIS B 1 197 ? 32.249 -2.854  -42.450 1.00 34.85 ? 188 HIS B ND1   1 
ATOM   4175 C CD2   . HIS B 1 197 ? 31.010 -1.757  -41.025 1.00 40.08 ? 188 HIS B CD2   1 
ATOM   4176 C CE1   . HIS B 1 197 ? 33.054 -2.070  -41.755 1.00 33.31 ? 188 HIS B CE1   1 
ATOM   4177 N NE2   . HIS B 1 197 ? 32.327 -1.394  -40.883 1.00 36.50 ? 188 HIS B NE2   1 
ATOM   4178 N N     . GLY B 1 198 ? 26.749 -5.227  -41.598 1.00 28.80 ? 189 GLY B N     1 
ATOM   4179 C CA    . GLY B 1 198 ? 25.541 -5.798  -42.160 1.00 26.66 ? 189 GLY B CA    1 
ATOM   4180 C C     . GLY B 1 198 ? 25.747 -6.907  -43.162 1.00 34.10 ? 189 GLY B C     1 
ATOM   4181 O O     . GLY B 1 198 ? 24.864 -7.147  -43.991 1.00 26.79 ? 189 GLY B O     1 
ATOM   4182 N N     . TYR B 1 199 ? 26.878 -7.598  -43.115 1.00 33.42 ? 190 TYR B N     1 
ATOM   4183 C CA    . TYR B 1 199 ? 27.128 -8.707  -44.023 1.00 27.69 ? 190 TYR B CA    1 
ATOM   4184 C C     . TYR B 1 199 ? 26.653 -10.003 -43.355 1.00 30.28 ? 190 TYR B C     1 
ATOM   4185 O O     . TYR B 1 199 ? 25.839 -9.961  -42.429 1.00 27.49 ? 190 TYR B O     1 
ATOM   4186 C CB    . TYR B 1 199 ? 28.600 -8.689  -44.442 1.00 30.11 ? 190 TYR B CB    1 
ATOM   4187 C CG    . TYR B 1 199 ? 28.922 -7.485  -45.306 1.00 32.15 ? 190 TYR B CG    1 
ATOM   4188 C CD1   . TYR B 1 199 ? 28.328 -7.326  -46.551 1.00 34.59 ? 190 TYR B CD1   1 
ATOM   4189 C CD2   . TYR B 1 199 ? 29.790 -6.496  -44.865 1.00 31.41 ? 190 TYR B CD2   1 
ATOM   4190 C CE1   . TYR B 1 199 ? 28.602 -6.230  -47.341 1.00 36.13 ? 190 TYR B CE1   1 
ATOM   4191 C CE2   . TYR B 1 199 ? 30.069 -5.388  -45.650 1.00 33.70 ? 190 TYR B CE2   1 
ATOM   4192 C CZ    . TYR B 1 199 ? 29.472 -5.262  -46.887 1.00 36.58 ? 190 TYR B CZ    1 
ATOM   4193 O OH    . TYR B 1 199 ? 29.741 -4.169  -47.677 1.00 36.02 ? 190 TYR B OH    1 
ATOM   4194 N N     . LEU B 1 200 ? 27.150 -11.158 -43.812 1.00 31.47 ? 191 LEU B N     1 
ATOM   4195 C CA    . LEU B 1 200 ? 26.521 -12.437 -43.476 1.00 33.94 ? 191 LEU B CA    1 
ATOM   4196 C C     . LEU B 1 200 ? 26.448 -12.661 -41.969 1.00 30.47 ? 191 LEU B C     1 
ATOM   4197 O O     . LEU B 1 200 ? 25.393 -13.022 -41.435 1.00 27.19 ? 191 LEU B O     1 
ATOM   4198 C CB    . LEU B 1 200 ? 27.275 -13.589 -44.140 1.00 29.16 ? 191 LEU B CB    1 
ATOM   4199 C CG    . LEU B 1 200 ? 26.719 -14.965 -43.760 1.00 32.10 ? 191 LEU B CG    1 
ATOM   4200 C CD1   . LEU B 1 200 ? 25.325 -15.155 -44.344 1.00 25.95 ? 191 LEU B CD1   1 
ATOM   4201 C CD2   . LEU B 1 200 ? 27.647 -16.088 -44.194 1.00 28.27 ? 191 LEU B CD2   1 
ATOM   4202 N N     . ILE B 1 201 ? 27.566 -12.474 -41.269 1.00 33.19 ? 192 ILE B N     1 
ATOM   4203 C CA    . ILE B 1 201 ? 27.577 -12.714 -39.830 1.00 31.87 ? 192 ILE B CA    1 
ATOM   4204 C C     . ILE B 1 201 ? 26.697 -11.698 -39.112 1.00 33.80 ? 192 ILE B C     1 
ATOM   4205 O O     . ILE B 1 201 ? 25.979 -12.037 -38.164 1.00 38.56 ? 192 ILE B O     1 
ATOM   4206 C CB    . ILE B 1 201 ? 29.024 -12.698 -39.309 1.00 31.89 ? 192 ILE B CB    1 
ATOM   4207 C CG1   . ILE B 1 201 ? 29.817 -13.833 -39.958 1.00 29.59 ? 192 ILE B CG1   1 
ATOM   4208 C CG2   . ILE B 1 201 ? 29.051 -12.802 -37.788 1.00 32.61 ? 192 ILE B CG2   1 
ATOM   4209 C CD1   . ILE B 1 201 ? 31.215 -13.995 -39.419 1.00 34.15 ? 192 ILE B CD1   1 
ATOM   4210 N N     . ASP B 1 202 ? 26.730 -10.442 -39.559 1.00 33.73 ? 193 ASP B N     1 
ATOM   4211 C CA    . ASP B 1 202 ? 25.855 -9.420  -38.995 1.00 32.23 ? 193 ASP B CA    1 
ATOM   4212 C C     . ASP B 1 202 ? 24.388 -9.714  -39.287 1.00 37.04 ? 193 ASP B C     1 
ATOM   4213 O O     . ASP B 1 202 ? 23.514 -9.374  -38.480 1.00 30.08 ? 193 ASP B O     1 
ATOM   4214 C CB    . ASP B 1 202 ? 26.251 -8.049  -39.548 1.00 33.14 ? 193 ASP B CB    1 
ATOM   4215 C CG    . ASP B 1 202 ? 26.249 -6.962  -38.493 1.00 36.95 ? 193 ASP B CG    1 
ATOM   4216 O OD1   . ASP B 1 202 ? 26.268 -7.285  -37.285 1.00 41.79 ? 193 ASP B OD1   1 
ATOM   4217 O OD2   . ASP B 1 202 ? 26.232 -5.773  -38.878 1.00 39.33 ? 193 ASP B OD2   1 
ATOM   4218 N N     . GLN B 1 203 ? 24.100 -10.346 -40.429 1.00 27.20 ? 194 GLN B N     1 
ATOM   4219 C CA    . GLN B 1 203 ? 22.730 -10.722 -40.758 1.00 26.76 ? 194 GLN B CA    1 
ATOM   4220 C C     . GLN B 1 203 ? 22.174 -11.763 -39.795 1.00 30.15 ? 194 GLN B C     1 
ATOM   4221 O O     . GLN B 1 203 ? 20.951 -11.900 -39.687 1.00 32.72 ? 194 GLN B O     1 
ATOM   4222 C CB    . GLN B 1 203 ? 22.657 -11.246 -42.196 1.00 25.83 ? 194 GLN B CB    1 
ATOM   4223 C CG    . GLN B 1 203 ? 22.745 -10.162 -43.263 1.00 22.42 ? 194 GLN B CG    1 
ATOM   4224 C CD    . GLN B 1 203 ? 23.340 -10.668 -44.566 1.00 29.42 ? 194 GLN B CD    1 
ATOM   4225 O OE1   . GLN B 1 203 ? 23.153 -11.826 -44.938 1.00 24.66 ? 194 GLN B OE1   1 
ATOM   4226 N NE2   . GLN B 1 203 ? 24.060 -9.799  -45.267 1.00 31.93 ? 194 GLN B NE2   1 
ATOM   4227 N N     . PHE B 1 204 ? 23.039 -12.504 -39.105 1.00 27.86 ? 195 PHE B N     1 
ATOM   4228 C CA    . PHE B 1 204 ? 22.601 -13.424 -38.064 1.00 29.91 ? 195 PHE B CA    1 
ATOM   4229 C C     . PHE B 1 204 ? 22.521 -12.757 -36.697 1.00 33.10 ? 195 PHE B C     1 
ATOM   4230 O O     . PHE B 1 204 ? 21.750 -13.205 -35.841 1.00 30.84 ? 195 PHE B O     1 
ATOM   4231 C CB    . PHE B 1 204 ? 23.550 -14.625 -37.984 1.00 25.09 ? 195 PHE B CB    1 
ATOM   4232 C CG    . PHE B 1 204 ? 23.220 -15.731 -38.946 1.00 34.61 ? 195 PHE B CG    1 
ATOM   4233 C CD1   . PHE B 1 204 ? 23.675 -15.689 -40.255 1.00 32.49 ? 195 PHE B CD1   1 
ATOM   4234 C CD2   . PHE B 1 204 ? 22.461 -16.816 -38.540 1.00 33.52 ? 195 PHE B CD2   1 
ATOM   4235 C CE1   . PHE B 1 204 ? 23.373 -16.706 -41.144 1.00 28.41 ? 195 PHE B CE1   1 
ATOM   4236 C CE2   . PHE B 1 204 ? 22.156 -17.838 -39.420 1.00 35.92 ? 195 PHE B CE2   1 
ATOM   4237 C CZ    . PHE B 1 204 ? 22.613 -17.783 -40.726 1.00 37.88 ? 195 PHE B CZ    1 
ATOM   4238 N N     . LEU B 1 205 ? 23.290 -11.688 -36.481 1.00 34.95 ? 196 LEU B N     1 
ATOM   4239 C CA    . LEU B 1 205 ? 23.385 -11.081 -35.157 1.00 36.72 ? 196 LEU B CA    1 
ATOM   4240 C C     . LEU B 1 205 ? 22.232 -10.126 -34.874 1.00 34.07 ? 196 LEU B C     1 
ATOM   4241 O O     . LEU B 1 205 ? 21.666 -10.143 -33.776 1.00 34.33 ? 196 LEU B O     1 
ATOM   4242 C CB    . LEU B 1 205 ? 24.715 -10.342 -35.017 1.00 31.77 ? 196 LEU B CB    1 
ATOM   4243 C CG    . LEU B 1 205 ? 25.988 -11.175 -34.907 1.00 34.46 ? 196 LEU B CG    1 
ATOM   4244 C CD1   . LEU B 1 205 ? 27.194 -10.299 -35.185 1.00 30.27 ? 196 LEU B CD1   1 
ATOM   4245 C CD2   . LEU B 1 205 ? 26.084 -11.815 -33.532 1.00 39.53 ? 196 LEU B CD2   1 
ATOM   4246 N N     . LYS B 1 206 ? 21.884 -9.276  -35.834 1.00 35.26 ? 197 LYS B N     1 
ATOM   4247 C CA    . LYS B 1 206 ? 20.932 -8.203  -35.583 1.00 41.27 ? 197 LYS B CA    1 
ATOM   4248 C C     . LYS B 1 206 ? 19.505 -8.722  -35.679 1.00 37.20 ? 197 LYS B C     1 
ATOM   4249 O O     . LYS B 1 206 ? 19.148 -9.410  -36.640 1.00 31.08 ? 197 LYS B O     1 
ATOM   4250 C CB    . LYS B 1 206 ? 21.155 -7.061  -36.573 1.00 39.79 ? 197 LYS B CB    1 
ATOM   4251 C CG    . LYS B 1 206 ? 22.615 -6.673  -36.722 1.00 41.95 ? 197 LYS B CG    1 
ATOM   4252 C CD    . LYS B 1 206 ? 22.814 -5.177  -36.560 1.00 44.17 ? 197 LYS B CD    1 
ATOM   4253 C CE    . LYS B 1 206 ? 24.289 -4.832  -36.440 1.00 40.04 ? 197 LYS B CE    1 
ATOM   4254 N NZ    . LYS B 1 206 ? 24.537 -3.385  -36.681 1.00 38.57 ? 197 LYS B NZ    1 
ATOM   4255 N N     . ASP B 1 207 ? 18.687 -8.389  -34.675 1.00 37.97 ? 198 ASP B N     1 
ATOM   4256 C CA    . ASP B 1 207 ? 17.301 -8.843  -34.655 1.00 41.01 ? 198 ASP B CA    1 
ATOM   4257 C C     . ASP B 1 207 ? 16.426 -8.100  -35.655 1.00 36.52 ? 198 ASP B C     1 
ATOM   4258 O O     . ASP B 1 207 ? 15.279 -8.507  -35.869 1.00 40.37 ? 198 ASP B O     1 
ATOM   4259 C CB    . ASP B 1 207 ? 16.716 -8.719  -33.242 1.00 42.33 ? 198 ASP B CB    1 
ATOM   4260 C CG    . ASP B 1 207 ? 16.746 -7.297  -32.709 1.00 43.57 ? 198 ASP B CG    1 
ATOM   4261 O OD1   . ASP B 1 207 ? 17.189 -6.384  -33.434 1.00 39.27 ? 198 ASP B OD1   1 
ATOM   4262 O OD2   . ASP B 1 207 ? 16.322 -7.094  -31.552 1.00 42.45 ? 198 ASP B OD2   1 
ATOM   4263 N N     . GLY B 1 208 ? 16.931 -7.026  -36.264 1.00 36.62 ? 199 GLY B N     1 
ATOM   4264 C CA    . GLY B 1 208 ? 16.229 -6.423  -37.381 1.00 41.30 ? 199 GLY B CA    1 
ATOM   4265 C C     . GLY B 1 208 ? 16.206 -7.293  -38.621 1.00 42.03 ? 199 GLY B C     1 
ATOM   4266 O O     . GLY B 1 208 ? 15.338 -7.106  -39.480 1.00 44.71 ? 199 GLY B O     1 
ATOM   4267 N N     . ILE B 1 209 ? 17.135 -8.241  -38.730 1.00 38.12 ? 200 ILE B N     1 
ATOM   4268 C CA    . ILE B 1 209 ? 17.203 -9.165  -39.855 1.00 36.50 ? 200 ILE B CA    1 
ATOM   4269 C C     . ILE B 1 209 ? 16.869 -10.590 -39.427 1.00 40.95 ? 200 ILE B C     1 
ATOM   4270 O O     . ILE B 1 209 ? 16.064 -11.267 -40.067 1.00 46.36 ? 200 ILE B O     1 
ATOM   4271 C CB    . ILE B 1 209 ? 18.588 -9.108  -40.538 1.00 40.70 ? 200 ILE B CB    1 
ATOM   4272 C CG1   . ILE B 1 209 ? 18.943 -7.674  -40.924 1.00 37.13 ? 200 ILE B CG1   1 
ATOM   4273 C CG2   . ILE B 1 209 ? 18.611 -10.006 -41.764 1.00 34.67 ? 200 ILE B CG2   1 
ATOM   4274 C CD1   . ILE B 1 209 ? 20.410 -7.485  -41.228 1.00 38.34 ? 200 ILE B CD1   1 
ATOM   4275 N N     . ASN B 1 210 ? 17.479 -11.060 -38.340 1.00 38.78 ? 201 ASN B N     1 
ATOM   4276 C CA    . ASN B 1 210 ? 17.358 -12.458 -37.930 1.00 35.70 ? 201 ASN B CA    1 
ATOM   4277 C C     . ASN B 1 210 ? 16.055 -12.659 -37.168 1.00 38.46 ? 201 ASN B C     1 
ATOM   4278 O O     . ASN B 1 210 ? 15.940 -12.294 -35.997 1.00 36.13 ? 201 ASN B O     1 
ATOM   4279 C CB    . ASN B 1 210 ? 18.554 -12.877 -37.083 1.00 38.33 ? 201 ASN B CB    1 
ATOM   4280 C CG    . ASN B 1 210 ? 18.605 -14.380 -36.845 1.00 39.87 ? 201 ASN B CG    1 
ATOM   4281 O OD1   . ASN B 1 210 ? 17.667 -15.106 -37.174 1.00 36.37 ? 201 ASN B OD1   1 
ATOM   4282 N ND2   . ASN B 1 210 ? 19.703 -14.851 -36.268 1.00 34.82 ? 201 ASN B ND2   1 
ATOM   4283 N N     . ASP B 1 211 ? 15.072 -13.261 -37.833 1.00 42.58 ? 202 ASP B N     1 
ATOM   4284 C CA    . ASP B 1 211 ? 13.856 -13.734 -37.184 1.00 48.15 ? 202 ASP B CA    1 
ATOM   4285 C C     . ASP B 1 211 ? 13.679 -15.236 -37.385 1.00 46.62 ? 202 ASP B C     1 
ATOM   4286 O O     . ASP B 1 211 ? 12.556 -15.725 -37.526 1.00 52.81 ? 202 ASP B O     1 
ATOM   4287 C CB    . ASP B 1 211 ? 12.633 -12.970 -37.691 1.00 49.31 ? 202 ASP B CB    1 
ATOM   4288 C CG    . ASP B 1 211 ? 12.536 -12.962 -39.201 1.00 53.89 ? 202 ASP B CG    1 
ATOM   4289 O OD1   . ASP B 1 211 ? 13.502 -13.395 -39.864 1.00 55.16 ? 202 ASP B OD1   1 
ATOM   4290 O OD2   . ASP B 1 211 ? 11.494 -12.517 -39.725 1.00 67.26 ? 202 ASP B OD2   1 
ATOM   4291 N N     . ARG B 1 212 ? 14.788 -15.976 -37.410 1.00 40.90 ? 203 ARG B N     1 
ATOM   4292 C CA    . ARG B 1 212 ? 14.729 -17.423 -37.568 1.00 41.86 ? 203 ARG B CA    1 
ATOM   4293 C C     . ARG B 1 212 ? 14.015 -18.065 -36.383 1.00 42.30 ? 203 ARG B C     1 
ATOM   4294 O O     . ARG B 1 212 ? 14.084 -17.582 -35.251 1.00 40.80 ? 203 ARG B O     1 
ATOM   4295 C CB    . ARG B 1 212 ? 16.136 -18.007 -37.690 1.00 41.14 ? 203 ARG B CB    1 
ATOM   4296 C CG    . ARG B 1 212 ? 16.853 -17.702 -38.989 1.00 41.13 ? 203 ARG B CG    1 
ATOM   4297 C CD    . ARG B 1 212 ? 18.306 -18.155 -38.913 1.00 32.34 ? 203 ARG B CD    1 
ATOM   4298 N NE    . ARG B 1 212 ? 18.435 -19.595 -39.101 1.00 30.56 ? 203 ARG B NE    1 
ATOM   4299 C CZ    . ARG B 1 212 ? 18.645 -20.179 -40.273 1.00 38.90 ? 203 ARG B CZ    1 
ATOM   4300 N NH1   . ARG B 1 212 ? 18.760 -19.473 -41.388 1.00 29.27 ? 203 ARG B NH1   1 
ATOM   4301 N NH2   . ARG B 1 212 ? 18.740 -21.504 -40.330 1.00 35.73 ? 203 ARG B NH2   1 
ATOM   4302 N N     . THR B 1 213 ? 13.335 -19.177 -36.653 1.00 48.68 ? 204 THR B N     1 
ATOM   4303 C CA    . THR B 1 213 ? 12.605 -19.914 -35.631 1.00 48.70 ? 204 THR B CA    1 
ATOM   4304 C C     . THR B 1 213 ? 13.359 -21.144 -35.140 1.00 43.41 ? 204 THR B C     1 
ATOM   4305 O O     . THR B 1 213 ? 12.797 -21.938 -34.379 1.00 51.54 ? 204 THR B O     1 
ATOM   4306 C CB    . THR B 1 213 ? 11.227 -20.326 -36.157 1.00 50.63 ? 204 THR B CB    1 
ATOM   4307 O OG1   . THR B 1 213 ? 11.370 -20.969 -37.430 1.00 53.20 ? 204 THR B OG1   1 
ATOM   4308 C CG2   . THR B 1 213 ? 10.328 -19.109 -36.308 1.00 49.17 ? 204 THR B CG2   1 
ATOM   4309 N N     . ASP B 1 214 ? 14.615 -21.319 -35.550 1.00 44.19 ? 205 ASP B N     1 
ATOM   4310 C CA    . ASP B 1 214 ? 15.415 -22.463 -35.154 1.00 42.29 ? 205 ASP B CA    1 
ATOM   4311 C C     . ASP B 1 214 ? 16.457 -22.035 -34.116 1.00 38.51 ? 205 ASP B C     1 
ATOM   4312 O O     . ASP B 1 214 ? 16.355 -20.947 -33.529 1.00 41.80 ? 205 ASP B O     1 
ATOM   4313 C CB    . ASP B 1 214 ? 16.033 -23.098 -36.404 1.00 49.23 ? 205 ASP B CB    1 
ATOM   4314 C CG    . ASP B 1 214 ? 17.031 -22.188 -37.096 1.00 42.83 ? 205 ASP B CG    1 
ATOM   4315 O OD1   . ASP B 1 214 ? 17.033 -20.972 -36.813 1.00 44.09 ? 205 ASP B OD1   1 
ATOM   4316 O OD2   . ASP B 1 214 ? 17.811 -22.691 -37.932 1.00 36.20 ? 205 ASP B OD2   1 
ATOM   4317 N N     . GLU B 1 215 ? 17.465 -22.887 -33.899 1.00 42.75 ? 206 GLU B N     1 
ATOM   4318 C CA    . GLU B 1 215 ? 18.467 -22.642 -32.868 1.00 40.47 ? 206 GLU B CA    1 
ATOM   4319 C C     . GLU B 1 215 ? 19.407 -21.491 -33.207 1.00 39.76 ? 206 GLU B C     1 
ATOM   4320 O O     . GLU B 1 215 ? 20.212 -21.105 -32.352 1.00 39.99 ? 206 GLU B O     1 
ATOM   4321 C CB    . GLU B 1 215 ? 19.289 -23.912 -32.607 1.00 44.94 ? 206 GLU B CB    1 
ATOM   4322 C CG    . GLU B 1 215 ? 20.459 -24.127 -33.564 1.00 49.99 ? 206 GLU B CG    1 
ATOM   4323 C CD    . GLU B 1 215 ? 20.657 -25.579 -33.963 1.00 57.70 ? 206 GLU B CD    1 
ATOM   4324 O OE1   . GLU B 1 215 ? 19.768 -26.149 -34.625 1.00 59.46 ? 206 GLU B OE1   1 
ATOM   4325 O OE2   . GLU B 1 215 ? 21.712 -26.150 -33.618 1.00 56.63 ? 206 GLU B OE2   1 
ATOM   4326 N N     . TYR B 1 216 ? 19.326 -20.931 -34.413 1.00 42.70 ? 207 TYR B N     1 
ATOM   4327 C CA    . TYR B 1 216 ? 20.214 -19.855 -34.833 1.00 40.44 ? 207 TYR B CA    1 
ATOM   4328 C C     . TYR B 1 216 ? 19.545 -18.487 -34.832 1.00 36.10 ? 207 TYR B C     1 
ATOM   4329 O O     . TYR B 1 216 ? 20.194 -17.497 -35.184 1.00 41.17 ? 207 TYR B O     1 
ATOM   4330 C CB    . TYR B 1 216 ? 20.775 -20.150 -36.229 1.00 37.33 ? 207 TYR B CB    1 
ATOM   4331 C CG    . TYR B 1 216 ? 21.913 -21.144 -36.230 1.00 33.22 ? 207 TYR B CG    1 
ATOM   4332 C CD1   . TYR B 1 216 ? 23.212 -20.741 -35.957 1.00 32.51 ? 207 TYR B CD1   1 
ATOM   4333 C CD2   . TYR B 1 216 ? 21.688 -22.486 -36.505 1.00 39.21 ? 207 TYR B CD2   1 
ATOM   4334 C CE1   . TYR B 1 216 ? 24.256 -21.646 -35.955 1.00 36.25 ? 207 TYR B CE1   1 
ATOM   4335 C CE2   . TYR B 1 216 ? 22.726 -23.400 -36.506 1.00 34.08 ? 207 TYR B CE2   1 
ATOM   4336 C CZ    . TYR B 1 216 ? 24.006 -22.975 -36.232 1.00 35.88 ? 207 TYR B CZ    1 
ATOM   4337 O OH    . TYR B 1 216 ? 25.041 -23.881 -36.232 1.00 35.92 ? 207 TYR B OH    1 
ATOM   4338 N N     . GLY B 1 217 ? 18.270 -18.401 -34.447 1.00 40.72 ? 208 GLY B N     1 
ATOM   4339 C CA    . GLY B 1 217 ? 17.570 -17.136 -34.444 1.00 40.40 ? 208 GLY B CA    1 
ATOM   4340 C C     . GLY B 1 217 ? 16.640 -17.022 -33.254 1.00 43.86 ? 208 GLY B C     1 
ATOM   4341 O O     . GLY B 1 217 ? 16.405 -17.986 -32.521 1.00 43.07 ? 208 GLY B O     1 
ATOM   4342 N N     . GLY B 1 218 ? 16.111 -15.814 -33.076 1.00 46.29 ? 209 GLY B N     1 
ATOM   4343 C CA    . GLY B 1 218 ? 15.193 -15.542 -31.990 1.00 43.56 ? 209 GLY B CA    1 
ATOM   4344 C C     . GLY B 1 218 ? 15.852 -14.853 -30.815 1.00 50.67 ? 209 GLY B C     1 
ATOM   4345 O O     . GLY B 1 218 ? 16.038 -13.631 -30.824 1.00 54.14 ? 209 GLY B O     1 
ATOM   4346 N N     . SER B 1 219 ? 16.213 -15.629 -29.797 1.00 40.59 ? 210 SER B N     1 
ATOM   4347 C CA    . SER B 1 219 ? 16.837 -15.073 -28.608 1.00 41.51 ? 210 SER B CA    1 
ATOM   4348 C C     . SER B 1 219 ? 18.212 -14.497 -28.936 1.00 41.46 ? 210 SER B C     1 
ATOM   4349 O O     . SER B 1 219 ? 18.810 -14.788 -29.976 1.00 49.22 ? 210 SER B O     1 
ATOM   4350 C CB    . SER B 1 219 ? 16.965 -16.140 -27.522 1.00 41.94 ? 210 SER B CB    1 
ATOM   4351 O OG    . SER B 1 219 ? 18.127 -16.927 -27.722 1.00 44.22 ? 210 SER B OG    1 
ATOM   4352 N N     . LEU B 1 220 ? 18.712 -13.664 -28.021 1.00 42.30 ? 211 LEU B N     1 
ATOM   4353 C CA    . LEU B 1 220 ? 20.026 -13.056 -28.207 1.00 41.42 ? 211 LEU B CA    1 
ATOM   4354 C C     . LEU B 1 220 ? 21.120 -14.112 -28.265 1.00 41.16 ? 211 LEU B C     1 
ATOM   4355 O O     . LEU B 1 220 ? 22.054 -14.005 -29.068 1.00 43.81 ? 211 LEU B O     1 
ATOM   4356 C CB    . LEU B 1 220 ? 20.302 -12.058 -27.083 1.00 44.96 ? 211 LEU B CB    1 
ATOM   4357 C CG    . LEU B 1 220 ? 21.657 -11.346 -27.078 1.00 41.44 ? 211 LEU B CG    1 
ATOM   4358 C CD1   . LEU B 1 220 ? 21.937 -10.683 -28.420 1.00 36.32 ? 211 LEU B CD1   1 
ATOM   4359 C CD2   . LEU B 1 220 ? 21.712 -10.329 -25.947 1.00 44.61 ? 211 LEU B CD2   1 
ATOM   4360 N N     . ALA B 1 221 ? 21.021 -15.143 -27.422 1.00 37.35 ? 212 ALA B N     1 
ATOM   4361 C CA    . ALA B 1 221 ? 22.025 -16.201 -27.428 1.00 39.86 ? 212 ALA B CA    1 
ATOM   4362 C C     . ALA B 1 221 ? 22.007 -16.971 -28.742 1.00 39.98 ? 212 ALA B C     1 
ATOM   4363 O O     . ALA B 1 221 ? 23.060 -17.396 -29.232 1.00 35.98 ? 212 ALA B O     1 
ATOM   4364 C CB    . ALA B 1 221 ? 21.799 -17.148 -26.250 1.00 38.98 ? 212 ALA B CB    1 
ATOM   4365 N N     . ASN B 1 222 ? 20.820 -17.162 -29.325 1.00 33.82 ? 213 ASN B N     1 
ATOM   4366 C CA    . ASN B 1 222 ? 20.725 -17.888 -30.586 1.00 42.59 ? 213 ASN B CA    1 
ATOM   4367 C C     . ASN B 1 222 ? 21.303 -17.073 -31.736 1.00 38.06 ? 213 ASN B C     1 
ATOM   4368 O O     . ASN B 1 222 ? 21.956 -17.625 -32.628 1.00 37.42 ? 213 ASN B O     1 
ATOM   4369 C CB    . ASN B 1 222 ? 19.269 -18.264 -30.867 1.00 40.43 ? 213 ASN B CB    1 
ATOM   4370 C CG    . ASN B 1 222 ? 18.813 -19.472 -30.067 1.00 44.76 ? 213 ASN B CG    1 
ATOM   4371 O OD1   . ASN B 1 222 ? 19.545 -19.981 -29.219 1.00 45.03 ? 213 ASN B OD1   1 
ATOM   4372 N ND2   . ASN B 1 222 ? 17.596 -19.935 -30.332 1.00 38.57 ? 213 ASN B ND2   1 
ATOM   4373 N N     . ARG B 1 223 ? 21.084 -15.756 -31.727 1.00 37.36 ? 214 ARG B N     1 
ATOM   4374 C CA    . ARG B 1 223 ? 21.618 -14.902 -32.782 1.00 41.30 ? 214 ARG B CA    1 
ATOM   4375 C C     . ARG B 1 223 ? 23.138 -14.814 -32.743 1.00 39.08 ? 214 ARG B C     1 
ATOM   4376 O O     . ARG B 1 223 ? 23.754 -14.502 -33.768 1.00 42.89 ? 214 ARG B O     1 
ATOM   4377 C CB    . ARG B 1 223 ? 21.008 -13.502 -32.684 1.00 37.70 ? 214 ARG B CB    1 
ATOM   4378 C CG    . ARG B 1 223 ? 19.564 -13.420 -33.158 1.00 35.01 ? 214 ARG B CG    1 
ATOM   4379 C CD    . ARG B 1 223 ? 19.043 -11.992 -33.094 1.00 42.55 ? 214 ARG B CD    1 
ATOM   4380 N NE    . ARG B 1 223 ? 18.300 -11.735 -31.865 1.00 47.32 ? 214 ARG B NE    1 
ATOM   4381 C CZ    . ARG B 1 223 ? 18.609 -10.793 -30.984 1.00 48.69 ? 214 ARG B CZ    1 
ATOM   4382 N NH1   . ARG B 1 223 ? 19.650 -9.996  -31.160 1.00 50.35 ? 214 ARG B NH1   1 
ATOM   4383 N NH2   . ARG B 1 223 ? 17.854 -10.647 -29.899 1.00 55.13 ? 214 ARG B NH2   1 
ATOM   4384 N N     . CYS B 1 224 ? 23.753 -15.082 -31.594 1.00 35.55 ? 215 CYS B N     1 
ATOM   4385 C CA    . CYS B 1 224 ? 25.203 -15.105 -31.468 1.00 32.08 ? 215 CYS B CA    1 
ATOM   4386 C C     . CYS B 1 224 ? 25.801 -16.471 -31.772 1.00 31.89 ? 215 CYS B C     1 
ATOM   4387 O O     . CYS B 1 224 ? 27.016 -16.643 -31.628 1.00 34.43 ? 215 CYS B O     1 
ATOM   4388 C CB    . CYS B 1 224 ? 25.621 -14.677 -30.056 1.00 43.27 ? 215 CYS B CB    1 
ATOM   4389 S SG    . CYS B 1 224 ? 25.149 -12.997 -29.591 1.00 42.39 ? 215 CYS B SG    1 
ATOM   4390 N N     . LYS B 1 225 ? 24.985 -17.446 -32.178 1.00 32.47 ? 216 LYS B N     1 
ATOM   4391 C CA    . LYS B 1 225 ? 25.505 -18.790 -32.408 1.00 36.31 ? 216 LYS B CA    1 
ATOM   4392 C C     . LYS B 1 225 ? 26.442 -18.829 -33.607 1.00 32.67 ? 216 LYS B C     1 
ATOM   4393 O O     . LYS B 1 225 ? 27.501 -19.466 -33.554 1.00 33.46 ? 216 LYS B O     1 
ATOM   4394 C CB    . LYS B 1 225 ? 24.355 -19.778 -32.603 1.00 38.93 ? 216 LYS B CB    1 
ATOM   4395 C CG    . LYS B 1 225 ? 24.212 -20.790 -31.479 1.00 49.63 ? 216 LYS B CG    1 
ATOM   4396 C CD    . LYS B 1 225 ? 23.467 -22.032 -31.943 1.00 47.29 ? 216 LYS B CD    1 
ATOM   4397 C CE    . LYS B 1 225 ? 23.203 -22.974 -30.782 1.00 51.77 ? 216 LYS B CE    1 
ATOM   4398 N NZ    . LYS B 1 225 ? 22.026 -22.532 -29.983 1.00 48.49 ? 216 LYS B NZ    1 
ATOM   4399 N N     . PHE B 1 226 ? 26.074 -18.151 -34.696 1.00 31.03 ? 217 PHE B N     1 
ATOM   4400 C CA    . PHE B 1 226 ? 26.854 -18.249 -35.925 1.00 35.04 ? 217 PHE B CA    1 
ATOM   4401 C C     . PHE B 1 226 ? 28.254 -17.674 -35.741 1.00 32.51 ? 217 PHE B C     1 
ATOM   4402 O O     . PHE B 1 226 ? 29.248 -18.296 -36.134 1.00 32.26 ? 217 PHE B O     1 
ATOM   4403 C CB    . PHE B 1 226 ? 26.123 -17.544 -37.068 1.00 30.69 ? 217 PHE B CB    1 
ATOM   4404 C CG    . PHE B 1 226 ? 26.766 -17.743 -38.411 1.00 35.64 ? 217 PHE B CG    1 
ATOM   4405 C CD1   . PHE B 1 226 ? 27.041 -19.017 -38.879 1.00 36.08 ? 217 PHE B CD1   1 
ATOM   4406 C CD2   . PHE B 1 226 ? 27.099 -16.656 -39.202 1.00 34.32 ? 217 PHE B CD2   1 
ATOM   4407 C CE1   . PHE B 1 226 ? 27.633 -19.205 -40.115 1.00 36.97 ? 217 PHE B CE1   1 
ATOM   4408 C CE2   . PHE B 1 226 ? 27.693 -16.836 -40.439 1.00 37.53 ? 217 PHE B CE2   1 
ATOM   4409 C CZ    . PHE B 1 226 ? 27.960 -18.112 -40.896 1.00 33.89 ? 217 PHE B CZ    1 
ATOM   4410 N N     . ILE B 1 227 ? 28.357 -16.486 -35.138 1.00 33.02 ? 218 ILE B N     1 
ATOM   4411 C CA    . ILE B 1 227 ? 29.672 -15.877 -34.966 1.00 32.50 ? 218 ILE B CA    1 
ATOM   4412 C C     . ILE B 1 227 ? 30.524 -16.689 -33.998 1.00 30.30 ? 218 ILE B C     1 
ATOM   4413 O O     . ILE B 1 227 ? 31.753 -16.728 -34.128 1.00 30.79 ? 218 ILE B O     1 
ATOM   4414 C CB    . ILE B 1 227 ? 29.541 -14.409 -34.514 1.00 37.18 ? 218 ILE B CB    1 
ATOM   4415 C CG1   . ILE B 1 227 ? 30.894 -13.696 -34.622 1.00 33.01 ? 218 ILE B CG1   1 
ATOM   4416 C CG2   . ILE B 1 227 ? 28.996 -14.319 -33.094 1.00 25.93 ? 218 ILE B CG2   1 
ATOM   4417 C CD1   . ILE B 1 227 ? 30.823 -12.200 -34.380 1.00 33.03 ? 218 ILE B CD1   1 
ATOM   4418 N N     . THR B 1 228 ? 29.901 -17.360 -33.027 1.00 31.18 ? 219 THR B N     1 
ATOM   4419 C CA    . THR B 1 228 ? 30.666 -18.176 -32.091 1.00 32.36 ? 219 THR B CA    1 
ATOM   4420 C C     . THR B 1 228 ? 31.239 -19.405 -32.784 1.00 26.62 ? 219 THR B C     1 
ATOM   4421 O O     . THR B 1 228 ? 32.424 -19.722 -32.628 1.00 30.99 ? 219 THR B O     1 
ATOM   4422 C CB    . THR B 1 228 ? 29.786 -18.584 -30.908 1.00 35.98 ? 219 THR B CB    1 
ATOM   4423 O OG1   . THR B 1 228 ? 29.141 -17.422 -30.373 1.00 30.04 ? 219 THR B OG1   1 
ATOM   4424 C CG2   . THR B 1 228 ? 30.623 -19.243 -29.817 1.00 32.85 ? 219 THR B CG2   1 
ATOM   4425 N N     . GLN B 1 229 ? 30.413 -20.103 -33.565 1.00 30.27 ? 220 GLN B N     1 
ATOM   4426 C CA    . GLN B 1 229 ? 30.891 -21.280 -34.282 1.00 32.58 ? 220 GLN B CA    1 
ATOM   4427 C C     . GLN B 1 229 ? 31.917 -20.913 -35.345 1.00 35.49 ? 220 GLN B C     1 
ATOM   4428 O O     . GLN B 1 229 ? 32.838 -21.694 -35.609 1.00 38.74 ? 220 GLN B O     1 
ATOM   4429 C CB    . GLN B 1 229 ? 29.713 -22.025 -34.909 1.00 34.21 ? 220 GLN B CB    1 
ATOM   4430 C CG    . GLN B 1 229 ? 28.990 -22.952 -33.941 1.00 38.21 ? 220 GLN B CG    1 
ATOM   4431 C CD    . GLN B 1 229 ? 27.574 -23.267 -34.378 1.00 39.56 ? 220 GLN B CD    1 
ATOM   4432 O OE1   . GLN B 1 229 ? 27.226 -23.123 -35.551 1.00 42.23 ? 220 GLN B OE1   1 
ATOM   4433 N NE2   . GLN B 1 229 ? 26.748 -23.700 -33.434 1.00 45.48 ? 220 GLN B NE2   1 
ATOM   4434 N N     . VAL B 1 230 ? 31.778 -19.739 -35.964 1.00 31.49 ? 221 VAL B N     1 
ATOM   4435 C CA    . VAL B 1 230 ? 32.787 -19.281 -36.915 1.00 29.85 ? 221 VAL B CA    1 
ATOM   4436 C C     . VAL B 1 230 ? 34.101 -19.004 -36.196 1.00 28.72 ? 221 VAL B C     1 
ATOM   4437 O O     . VAL B 1 230 ? 35.169 -19.457 -36.622 1.00 28.06 ? 221 VAL B O     1 
ATOM   4438 C CB    . VAL B 1 230 ? 32.288 -18.039 -37.677 1.00 33.67 ? 221 VAL B CB    1 
ATOM   4439 C CG1   . VAL B 1 230 ? 33.450 -17.335 -38.354 1.00 29.12 ? 221 VAL B CG1   1 
ATOM   4440 C CG2   . VAL B 1 230 ? 31.226 -18.426 -38.700 1.00 29.36 ? 221 VAL B CG2   1 
ATOM   4441 N N     . VAL B 1 231 ? 34.038 -18.263 -35.086 1.00 31.53 ? 222 VAL B N     1 
ATOM   4442 C CA    . VAL B 1 231 ? 35.249 -17.928 -34.341 1.00 32.55 ? 222 VAL B CA    1 
ATOM   4443 C C     . VAL B 1 231 ? 35.883 -19.184 -33.755 1.00 31.77 ? 222 VAL B C     1 
ATOM   4444 O O     . VAL B 1 231 ? 37.110 -19.344 -33.773 1.00 30.95 ? 222 VAL B O     1 
ATOM   4445 C CB    . VAL B 1 231 ? 34.932 -16.886 -33.252 1.00 31.90 ? 222 VAL B CB    1 
ATOM   4446 C CG1   . VAL B 1 231 ? 36.067 -16.799 -32.243 1.00 29.70 ? 222 VAL B CG1   1 
ATOM   4447 C CG2   . VAL B 1 231 ? 34.674 -15.525 -33.878 1.00 29.46 ? 222 VAL B CG2   1 
ATOM   4448 N N     . GLN B 1 232 ? 35.061 -20.098 -33.232 1.00 32.69 ? 223 GLN B N     1 
ATOM   4449 C CA    . GLN B 1 232 ? 35.602 -21.322 -32.650 1.00 29.76 ? 223 GLN B CA    1 
ATOM   4450 C C     . GLN B 1 232 ? 36.294 -22.176 -33.706 1.00 33.95 ? 223 GLN B C     1 
ATOM   4451 O O     . GLN B 1 232 ? 37.335 -22.787 -33.436 1.00 36.53 ? 223 GLN B O     1 
ATOM   4452 C CB    . GLN B 1 232 ? 34.489 -22.113 -31.962 1.00 32.42 ? 223 GLN B CB    1 
ATOM   4453 N N     . ALA B 1 233 ? 35.737 -22.225 -34.918 1.00 35.51 ? 224 ALA B N     1 
ATOM   4454 C CA    . ALA B 1 233 ? 36.326 -23.056 -35.962 1.00 36.08 ? 224 ALA B CA    1 
ATOM   4455 C C     . ALA B 1 233 ? 37.688 -22.529 -36.394 1.00 37.92 ? 224 ALA B C     1 
ATOM   4456 O O     . ALA B 1 233 ? 38.637 -23.305 -36.549 1.00 41.66 ? 224 ALA B O     1 
ATOM   4457 C CB    . ALA B 1 233 ? 35.385 -23.147 -37.160 1.00 29.52 ? 224 ALA B CB    1 
ATOM   4458 N N     . VAL B 1 234 ? 37.807 -21.214 -36.596 1.00 33.02 ? 225 VAL B N     1 
ATOM   4459 C CA    . VAL B 1 234 ? 39.089 -20.668 -37.027 1.00 35.73 ? 225 VAL B CA    1 
ATOM   4460 C C     . VAL B 1 234 ? 40.105 -20.712 -35.891 1.00 34.32 ? 225 VAL B C     1 
ATOM   4461 O O     . VAL B 1 234 ? 41.298 -20.939 -36.129 1.00 36.54 ? 225 VAL B O     1 
ATOM   4462 C CB    . VAL B 1 234 ? 38.915 -19.241 -37.585 1.00 33.29 ? 225 VAL B CB    1 
ATOM   4463 C CG1   . VAL B 1 234 ? 38.243 -18.332 -36.567 1.00 34.72 ? 225 VAL B CG1   1 
ATOM   4464 C CG2   . VAL B 1 234 ? 40.256 -18.673 -37.994 1.00 37.41 ? 225 VAL B CG2   1 
ATOM   4465 N N     . VAL B 1 235 ? 39.663 -20.510 -34.647 1.00 32.09 ? 226 VAL B N     1 
ATOM   4466 C CA    . VAL B 1 235 ? 40.571 -20.631 -33.508 1.00 31.38 ? 226 VAL B CA    1 
ATOM   4467 C C     . VAL B 1 235 ? 41.150 -22.038 -33.446 1.00 33.46 ? 226 VAL B C     1 
ATOM   4468 O O     . VAL B 1 235 ? 42.368 -22.225 -33.333 1.00 33.03 ? 226 VAL B O     1 
ATOM   4469 C CB    . VAL B 1 235 ? 39.850 -20.261 -32.199 1.00 36.43 ? 226 VAL B CB    1 
ATOM   4470 C CG1   . VAL B 1 235 ? 40.564 -20.880 -31.002 1.00 33.29 ? 226 VAL B CG1   1 
ATOM   4471 C CG2   . VAL B 1 235 ? 39.762 -18.751 -32.044 1.00 32.44 ? 226 VAL B CG2   1 
ATOM   4472 N N     . SER B 1 236 ? 40.285 -23.049 -33.538 1.00 32.86 ? 227 SER B N     1 
ATOM   4473 C CA    . SER B 1 236 ? 40.749 -24.430 -33.486 1.00 43.58 ? 227 SER B CA    1 
ATOM   4474 C C     . SER B 1 236 ? 41.671 -24.776 -34.647 1.00 36.06 ? 227 SER B C     1 
ATOM   4475 O O     . SER B 1 236 ? 42.472 -25.709 -34.530 1.00 43.56 ? 227 SER B O     1 
ATOM   4476 C CB    . SER B 1 236 ? 39.553 -25.384 -33.469 1.00 40.09 ? 227 SER B CB    1 
ATOM   4477 O OG    . SER B 1 236 ? 38.821 -25.256 -32.262 1.00 50.47 ? 227 SER B OG    1 
ATOM   4478 N N     . ALA B 1 237 ? 41.591 -24.042 -35.756 1.00 42.30 ? 228 ALA B N     1 
ATOM   4479 C CA    . ALA B 1 237 ? 42.365 -24.385 -36.943 1.00 33.27 ? 228 ALA B CA    1 
ATOM   4480 C C     . ALA B 1 237 ? 43.744 -23.733 -36.964 1.00 37.32 ? 228 ALA B C     1 
ATOM   4481 O O     . ALA B 1 237 ? 44.718 -24.370 -37.379 1.00 43.71 ? 228 ALA B O     1 
ATOM   4482 C CB    . ALA B 1 237 ? 41.592 -23.998 -38.205 1.00 38.39 ? 228 ALA B CB    1 
ATOM   4483 N N     . ILE B 1 238 ? 43.854 -22.475 -36.534 1.00 34.71 ? 229 ILE B N     1 
ATOM   4484 C CA    . ILE B 1 238 ? 45.107 -21.735 -36.629 1.00 35.10 ? 229 ILE B CA    1 
ATOM   4485 C C     . ILE B 1 238 ? 45.567 -21.165 -35.296 1.00 30.13 ? 229 ILE B C     1 
ATOM   4486 O O     . ILE B 1 238 ? 46.652 -20.587 -35.230 1.00 32.27 ? 229 ILE B O     1 
ATOM   4487 C CB    . ILE B 1 238 ? 45.012 -20.607 -37.678 1.00 36.36 ? 229 ILE B CB    1 
ATOM   4488 C CG1   . ILE B 1 238 ? 44.093 -19.491 -37.177 1.00 25.83 ? 229 ILE B CG1   1 
ATOM   4489 C CG2   . ILE B 1 238 ? 44.528 -21.154 -39.013 1.00 34.60 ? 229 ILE B CG2   1 
ATOM   4490 C CD1   . ILE B 1 238 ? 44.033 -18.288 -38.096 1.00 32.77 ? 229 ILE B CD1   1 
ATOM   4491 N N     . GLY B 1 239 ? 44.783 -21.301 -34.232 1.00 37.22 ? 230 GLY B N     1 
ATOM   4492 C CA    . GLY B 1 239 ? 45.155 -20.724 -32.955 1.00 31.08 ? 230 GLY B CA    1 
ATOM   4493 C C     . GLY B 1 239 ? 44.497 -19.383 -32.714 1.00 33.66 ? 230 GLY B C     1 
ATOM   4494 O O     . GLY B 1 239 ? 44.324 -18.595 -33.648 1.00 35.75 ? 230 GLY B O     1 
ATOM   4495 N N     . ALA B 1 240 ? 44.128 -19.109 -31.461 1.00 34.44 ? 231 ALA B N     1 
ATOM   4496 C CA    . ALA B 1 240 ? 43.401 -17.881 -31.154 1.00 36.54 ? 231 ALA B CA    1 
ATOM   4497 C C     . ALA B 1 240 ? 44.261 -16.646 -31.388 1.00 32.65 ? 231 ALA B C     1 
ATOM   4498 O O     . ALA B 1 240 ? 43.764 -15.623 -31.873 1.00 36.31 ? 231 ALA B O     1 
ATOM   4499 C CB    . ALA B 1 240 ? 42.897 -17.917 -29.711 1.00 31.11 ? 231 ALA B CB    1 
ATOM   4500 N N     . ASP B 1 241 ? 45.553 -16.721 -31.060 1.00 32.95 ? 232 ASP B N     1 
ATOM   4501 C CA    . ASP B 1 241 ? 46.433 -15.563 -31.162 1.00 35.29 ? 232 ASP B CA    1 
ATOM   4502 C C     . ASP B 1 241 ? 46.611 -15.066 -32.593 1.00 39.37 ? 232 ASP B C     1 
ATOM   4503 O O     . ASP B 1 241 ? 47.145 -13.967 -32.784 1.00 37.31 ? 232 ASP B O     1 
ATOM   4504 C CB    . ASP B 1 241 ? 47.792 -15.894 -30.540 1.00 37.15 ? 232 ASP B CB    1 
ATOM   4505 C CG    . ASP B 1 241 ? 48.533 -16.980 -31.295 1.00 53.16 ? 232 ASP B CG    1 
ATOM   4506 O OD1   . ASP B 1 241 ? 47.878 -17.761 -32.015 1.00 58.83 ? 232 ASP B OD1   1 
ATOM   4507 O OD2   . ASP B 1 241 ? 49.772 -17.057 -31.163 1.00 55.86 ? 232 ASP B OD2   1 
ATOM   4508 N N     . ARG B 1 242 ? 46.176 -15.831 -33.595 1.00 35.96 ? 233 ARG B N     1 
ATOM   4509 C CA    . ARG B 1 242 ? 46.201 -15.395 -34.986 1.00 41.82 ? 233 ARG B CA    1 
ATOM   4510 C C     . ARG B 1 242 ? 44.805 -15.077 -35.515 1.00 37.73 ? 233 ARG B C     1 
ATOM   4511 O O     . ARG B 1 242 ? 44.589 -15.087 -36.731 1.00 34.21 ? 233 ARG B O     1 
ATOM   4512 C CB    . ARG B 1 242 ? 46.871 -16.455 -35.863 1.00 34.27 ? 233 ARG B CB    1 
ATOM   4513 C CG    . ARG B 1 242 ? 47.861 -17.344 -35.129 1.00 44.40 ? 233 ARG B CG    1 
ATOM   4514 C CD    . ARG B 1 242 ? 48.650 -18.218 -36.094 1.00 43.75 ? 233 ARG B CD    1 
ATOM   4515 N NE    . ARG B 1 242 ? 49.583 -17.437 -36.896 1.00 51.08 ? 233 ARG B NE    1 
ATOM   4516 C CZ    . ARG B 1 242 ? 50.902 -17.553 -36.839 1.00 54.57 ? 233 ARG B CZ    1 
ATOM   4517 N NH1   . ARG B 1 242 ? 51.485 -18.425 -36.033 1.00 55.51 ? 233 ARG B NH1   1 
ATOM   4518 N NH2   . ARG B 1 242 ? 51.656 -16.773 -37.609 1.00 55.39 ? 233 ARG B NH2   1 
ATOM   4519 N N     . VAL B 1 243 ? 43.854 -14.793 -34.629 1.00 28.66 ? 234 VAL B N     1 
ATOM   4520 C CA    . VAL B 1 243 ? 42.461 -14.584 -35.010 1.00 29.00 ? 234 VAL B CA    1 
ATOM   4521 C C     . VAL B 1 243 ? 41.979 -13.275 -34.402 1.00 38.38 ? 234 VAL B C     1 
ATOM   4522 O O     . VAL B 1 243 ? 41.949 -13.130 -33.173 1.00 31.39 ? 234 VAL B O     1 
ATOM   4523 C CB    . VAL B 1 243 ? 41.560 -15.744 -34.557 1.00 28.44 ? 234 VAL B CB    1 
ATOM   4524 C CG1   . VAL B 1 243 ? 40.097 -15.419 -34.839 1.00 31.65 ? 234 VAL B CG1   1 
ATOM   4525 C CG2   . VAL B 1 243 ? 41.969 -17.041 -35.238 1.00 24.90 ? 234 VAL B CG2   1 
ATOM   4526 N N     . GLY B 1 244 ? 41.599 -12.330 -35.259 1.00 33.69 ? 235 GLY B N     1 
ATOM   4527 C CA    . GLY B 1 244 ? 40.919 -11.127 -34.823 1.00 30.63 ? 235 GLY B CA    1 
ATOM   4528 C C     . GLY B 1 244 ? 39.472 -11.140 -35.269 1.00 33.50 ? 235 GLY B C     1 
ATOM   4529 O O     . GLY B 1 244 ? 39.126 -11.834 -36.230 1.00 30.35 ? 235 GLY B O     1 
ATOM   4530 N N     . VAL B 1 245 ? 38.611 -10.391 -34.582 1.00 23.64 ? 236 VAL B N     1 
ATOM   4531 C CA    . VAL B 1 245 ? 37.178 -10.381 -34.859 1.00 28.77 ? 236 VAL B CA    1 
ATOM   4532 C C     . VAL B 1 245 ? 36.717 -8.935  -34.952 1.00 32.16 ? 236 VAL B C     1 
ATOM   4533 O O     . VAL B 1 245 ? 36.978 -8.139  -34.043 1.00 34.13 ? 236 VAL B O     1 
ATOM   4534 C CB    . VAL B 1 245 ? 36.374 -11.131 -33.777 1.00 32.00 ? 236 VAL B CB    1 
ATOM   4535 C CG1   . VAL B 1 245 ? 34.906 -11.225 -34.170 1.00 32.61 ? 236 VAL B CG1   1 
ATOM   4536 C CG2   . VAL B 1 245 ? 36.953 -12.520 -33.530 1.00 34.59 ? 236 VAL B CG2   1 
ATOM   4537 N N     . ARG B 1 246 ? 36.027 -8.599  -36.039 1.00 30.42 ? 237 ARG B N     1 
ATOM   4538 C CA    . ARG B 1 246 ? 35.508 -7.255  -36.258 1.00 34.41 ? 237 ARG B CA    1 
ATOM   4539 C C     . ARG B 1 246 ? 33.986 -7.279  -36.232 1.00 31.02 ? 237 ARG B C     1 
ATOM   4540 O O     . ARG B 1 246 ? 33.361 -8.067  -36.948 1.00 29.17 ? 237 ARG B O     1 
ATOM   4541 C CB    . ARG B 1 246 ? 36.005 -6.676  -37.585 1.00 31.03 ? 237 ARG B CB    1 
ATOM   4542 C CG    . ARG B 1 246 ? 35.730 -5.186  -37.744 1.00 34.01 ? 237 ARG B CG    1 
ATOM   4543 C CD    . ARG B 1 246 ? 36.437 -4.608  -38.964 1.00 38.96 ? 237 ARG B CD    1 
ATOM   4544 N NE    . ARG B 1 246 ? 36.874 -3.235  -38.736 1.00 38.74 ? 237 ARG B NE    1 
ATOM   4545 C CZ    . ARG B 1 246 ? 36.763 -2.255  -39.622 1.00 37.98 ? 237 ARG B CZ    1 
ATOM   4546 N NH1   . ARG B 1 246 ? 36.233 -2.460  -40.816 1.00 34.36 ? 237 ARG B NH1   1 
ATOM   4547 N NH2   . ARG B 1 246 ? 37.199 -1.040  -39.304 1.00 39.39 ? 237 ARG B NH2   1 
ATOM   4548 N N     . VAL B 1 247 ? 33.395 -6.417  -35.402 1.00 28.06 ? 238 VAL B N     1 
ATOM   4549 C CA    . VAL B 1 247 ? 31.947 -6.295  -35.273 1.00 29.92 ? 238 VAL B CA    1 
ATOM   4550 C C     . VAL B 1 247 ? 31.585 -4.814  -35.252 1.00 30.92 ? 238 VAL B C     1 
ATOM   4551 O O     . VAL B 1 247 ? 32.435 -3.943  -35.055 1.00 30.66 ? 238 VAL B O     1 
ATOM   4552 C CB    . VAL B 1 247 ? 31.407 -6.995  -34.005 1.00 32.53 ? 238 VAL B CB    1 
ATOM   4553 C CG1   . VAL B 1 247 ? 31.698 -8.492  -34.045 1.00 25.60 ? 238 VAL B CG1   1 
ATOM   4554 C CG2   . VAL B 1 247 ? 32.001 -6.363  -32.759 1.00 29.84 ? 238 VAL B CG2   1 
ATOM   4555 N N     . SER B 1 248 ? 30.299 -4.534  -35.454 1.00 28.49 ? 239 SER B N     1 
ATOM   4556 C CA    . SER B 1 248 ? 29.787 -3.162  -35.429 1.00 35.91 ? 239 SER B CA    1 
ATOM   4557 C C     . SER B 1 248 ? 28.316 -3.188  -35.050 1.00 37.51 ? 239 SER B C     1 
ATOM   4558 O O     . SER B 1 248 ? 27.430 -3.038  -35.900 1.00 32.84 ? 239 SER B O     1 
ATOM   4559 C CB    . SER B 1 248 ? 29.991 -2.468  -36.777 1.00 33.16 ? 239 SER B CB    1 
ATOM   4560 O OG    . SER B 1 248 ? 29.247 -3.109  -37.797 1.00 34.89 ? 239 SER B OG    1 
ATOM   4561 N N     . PRO B 1 249 ? 28.012 -3.373  -33.762 1.00 34.57 ? 240 PRO B N     1 
ATOM   4562 C CA    . PRO B 1 249 ? 26.602 -3.448  -33.350 1.00 35.14 ? 240 PRO B CA    1 
ATOM   4563 C C     . PRO B 1 249 ? 25.855 -2.130  -33.464 1.00 35.04 ? 240 PRO B C     1 
ATOM   4564 O O     . PRO B 1 249 ? 24.625 -2.151  -33.593 1.00 37.34 ? 240 PRO B O     1 
ATOM   4565 C CB    . PRO B 1 249 ? 26.685 -3.919  -31.890 1.00 37.74 ? 240 PRO B CB    1 
ATOM   4566 C CG    . PRO B 1 249 ? 28.056 -3.535  -31.438 1.00 34.56 ? 240 PRO B CG    1 
ATOM   4567 C CD    . PRO B 1 249 ? 28.937 -3.636  -32.645 1.00 32.02 ? 240 PRO B CD    1 
ATOM   4568 N N     . ALA B 1 250 ? 26.544 -0.991  -33.434 1.00 33.22 ? 241 ALA B N     1 
ATOM   4569 C CA    . ALA B 1 250 ? 25.892 0.312   -33.445 1.00 37.49 ? 241 ALA B CA    1 
ATOM   4570 C C     . ALA B 1 250 ? 25.823 0.938   -34.835 1.00 35.69 ? 241 ALA B C     1 
ATOM   4571 O O     . ALA B 1 250 ? 25.491 2.122   -34.950 1.00 47.47 ? 241 ALA B O     1 
ATOM   4572 C CB    . ALA B 1 250 ? 26.601 1.264   -32.479 1.00 29.34 ? 241 ALA B CB    1 
ATOM   4573 N N     . ILE B 1 251 ? 26.120 0.181   -35.888 1.00 40.97 ? 242 ILE B N     1 
ATOM   4574 C CA    . ILE B 1 251 ? 26.069 0.678   -37.259 1.00 41.11 ? 242 ILE B CA    1 
ATOM   4575 C C     . ILE B 1 251 ? 24.895 0.015   -37.967 1.00 42.88 ? 242 ILE B C     1 
ATOM   4576 O O     . ILE B 1 251 ? 24.799 -1.218  -38.005 1.00 39.33 ? 242 ILE B O     1 
ATOM   4577 C CB    . ILE B 1 251 ? 27.390 0.418   -38.003 1.00 41.51 ? 242 ILE B CB    1 
ATOM   4578 C CG1   . ILE B 1 251 ? 28.451 1.430   -37.561 1.00 41.28 ? 242 ILE B CG1   1 
ATOM   4579 C CG2   . ILE B 1 251 ? 27.182 0.486   -39.509 1.00 39.98 ? 242 ILE B CG2   1 
ATOM   4580 C CD1   . ILE B 1 251 ? 29.810 1.219   -38.199 1.00 37.97 ? 242 ILE B CD1   1 
ATOM   4581 N N     . ASP B 1 252 ? 24.004 0.834   -38.530 1.00 35.29 ? 243 ASP B N     1 
ATOM   4582 C CA    . ASP B 1 252 ? 22.789 0.360   -39.181 1.00 48.09 ? 243 ASP B CA    1 
ATOM   4583 C C     . ASP B 1 252 ? 22.950 0.210   -40.692 1.00 47.94 ? 243 ASP B C     1 
ATOM   4584 O O     . ASP B 1 252 ? 21.952 0.262   -41.419 1.00 53.02 ? 243 ASP B O     1 
ATOM   4585 C CB    . ASP B 1 252 ? 21.623 1.302   -38.875 1.00 52.30 ? 243 ASP B CB    1 
ATOM   4586 C CG    . ASP B 1 252 ? 21.521 1.647   -37.402 1.00 61.52 ? 243 ASP B CG    1 
ATOM   4587 O OD1   . ASP B 1 252 ? 21.957 0.829   -36.564 1.00 63.95 ? 243 ASP B OD1   1 
ATOM   4588 O OD2   . ASP B 1 252 ? 21.007 2.741   -37.084 1.00 65.50 ? 243 ASP B OD2   1 
ATOM   4589 N N     . HIS B 1 253 ? 24.177 0.019   -41.172 1.00 46.37 ? 244 HIS B N     1 
ATOM   4590 C CA    . HIS B 1 253 ? 24.431 -0.042  -42.607 1.00 45.93 ? 244 HIS B CA    1 
ATOM   4591 C C     . HIS B 1 253 ? 23.732 -1.240  -43.241 1.00 45.07 ? 244 HIS B C     1 
ATOM   4592 O O     . HIS B 1 253 ? 23.629 -2.311  -42.637 1.00 42.50 ? 244 HIS B O     1 
ATOM   4593 C CB    . HIS B 1 253 ? 25.937 -0.118  -42.870 1.00 48.60 ? 244 HIS B CB    1 
ATOM   4594 C CG    . HIS B 1 253 ? 26.304 -0.143  -44.322 1.00 54.11 ? 244 HIS B CG    1 
ATOM   4595 N ND1   . HIS B 1 253 ? 25.737 0.705   -45.250 1.00 52.77 ? 244 HIS B ND1   1 
ATOM   4596 C CD2   . HIS B 1 253 ? 27.189 -0.908  -45.005 1.00 49.97 ? 244 HIS B CD2   1 
ATOM   4597 C CE1   . HIS B 1 253 ? 26.253 0.461   -46.442 1.00 46.07 ? 244 HIS B CE1   1 
ATOM   4598 N NE2   . HIS B 1 253 ? 27.137 -0.513  -46.321 1.00 53.64 ? 244 HIS B NE2   1 
ATOM   4599 N N     . LEU B 1 254 ? 23.246 -1.044  -44.470 1.00 42.14 ? 245 LEU B N     1 
ATOM   4600 C CA    . LEU B 1 254 ? 22.627 -2.109  -45.264 1.00 43.58 ? 245 LEU B CA    1 
ATOM   4601 C C     . LEU B 1 254 ? 21.465 -2.765  -44.521 1.00 48.69 ? 245 LEU B C     1 
ATOM   4602 O O     . LEU B 1 254 ? 21.307 -3.988  -44.537 1.00 50.50 ? 245 LEU B O     1 
ATOM   4603 C CB    . LEU B 1 254 ? 23.659 -3.156  -45.686 1.00 41.44 ? 245 LEU B CB    1 
ATOM   4604 C CG    . LEU B 1 254 ? 24.692 -2.695  -46.714 1.00 42.59 ? 245 LEU B CG    1 
ATOM   4605 C CD1   . LEU B 1 254 ? 25.631 -3.834  -47.081 1.00 44.95 ? 245 LEU B CD1   1 
ATOM   4606 C CD2   . LEU B 1 254 ? 24.006 -2.131  -47.953 1.00 38.28 ? 245 LEU B CD2   1 
ATOM   4607 N N     . ASP B 1 255 ? 20.650 -1.941  -43.861 1.00 44.98 ? 246 ASP B N     1 
ATOM   4608 C CA    . ASP B 1 255 ? 19.440 -2.399  -43.175 1.00 47.53 ? 246 ASP B CA    1 
ATOM   4609 C C     . ASP B 1 255 ? 19.759 -3.430  -42.095 1.00 42.58 ? 246 ASP B C     1 
ATOM   4610 O O     . ASP B 1 255 ? 19.043 -4.419  -41.925 1.00 35.24 ? 246 ASP B O     1 
ATOM   4611 C CB    . ASP B 1 255 ? 18.417 -2.956  -44.168 1.00 40.84 ? 246 ASP B CB    1 
ATOM   4612 C CG    . ASP B 1 255 ? 17.729 -1.870  -44.965 1.00 48.56 ? 246 ASP B CG    1 
ATOM   4613 O OD1   . ASP B 1 255 ? 18.186 -0.708  -44.913 1.00 51.09 ? 246 ASP B OD1   1 
ATOM   4614 O OD2   . ASP B 1 255 ? 16.728 -2.179  -45.642 1.00 47.82 ? 246 ASP B OD2   1 
ATOM   4615 N N     . ALA B 1 256 ? 20.833 -3.193  -41.347 1.00 38.96 ? 247 ALA B N     1 
ATOM   4616 C CA    . ALA B 1 256 ? 21.264 -4.082  -40.271 1.00 44.68 ? 247 ALA B CA    1 
ATOM   4617 C C     . ALA B 1 256 ? 21.181 -3.317  -38.954 1.00 41.30 ? 247 ALA B C     1 
ATOM   4618 O O     . ALA B 1 256 ? 22.153 -2.690  -38.526 1.00 41.95 ? 247 ALA B O     1 
ATOM   4619 C CB    . ALA B 1 256 ? 22.670 -4.607  -40.523 1.00 36.58 ? 247 ALA B CB    1 
ATOM   4620 N N     . MET B 1 257 ? 20.023 -3.378  -38.305 1.00 40.45 ? 248 MET B N     1 
ATOM   4621 C CA    . MET B 1 257 ? 19.816 -2.709  -37.031 1.00 42.46 ? 248 MET B CA    1 
ATOM   4622 C C     . MET B 1 257 ? 19.458 -3.726  -35.957 1.00 38.94 ? 248 MET B C     1 
ATOM   4623 O O     . MET B 1 257 ? 18.865 -4.771  -36.237 1.00 42.10 ? 248 MET B O     1 
ATOM   4624 C CB    . MET B 1 257 ? 18.705 -1.655  -37.112 1.00 41.12 ? 248 MET B CB    1 
ATOM   4625 C CG    . MET B 1 257 ? 17.366 -2.198  -37.597 1.00 49.53 ? 248 MET B CG    1 
ATOM   4626 S SD    . MET B 1 257 ? 17.482 -3.223  -39.071 1.00 62.88 ? 248 MET B SD    1 
ATOM   4627 C CE    . MET B 1 257 ? 17.462 -1.946  -40.330 1.00 46.66 ? 248 MET B CE    1 
ATOM   4628 N N     . ASP B 1 258 ? 19.826 -3.406  -34.721 1.00 38.50 ? 249 ASP B N     1 
ATOM   4629 C CA    . ASP B 1 258 ? 19.444 -4.187  -33.556 1.00 44.11 ? 249 ASP B CA    1 
ATOM   4630 C C     . ASP B 1 258 ? 18.669 -3.304  -32.588 1.00 38.90 ? 249 ASP B C     1 
ATOM   4631 O O     . ASP B 1 258 ? 18.931 -2.104  -32.475 1.00 43.52 ? 249 ASP B O     1 
ATOM   4632 C CB    . ASP B 1 258 ? 20.667 -4.784  -32.848 1.00 38.56 ? 249 ASP B CB    1 
ATOM   4633 C CG    . ASP B 1 258 ? 20.292 -5.848  -31.827 1.00 46.53 ? 249 ASP B CG    1 
ATOM   4634 O OD1   . ASP B 1 258 ? 20.167 -5.510  -30.631 1.00 45.16 ? 249 ASP B OD1   1 
ATOM   4635 O OD2   . ASP B 1 258 ? 20.115 -7.022  -32.223 1.00 44.07 ? 249 ASP B OD2   1 
ATOM   4636 N N     . SER B 1 259 ? 17.704 -3.909  -31.891 1.00 41.54 ? 250 SER B N     1 
ATOM   4637 C CA    . SER B 1 259 ? 16.899 -3.156  -30.936 1.00 47.77 ? 250 SER B CA    1 
ATOM   4638 C C     . SER B 1 259 ? 17.692 -2.748  -29.703 1.00 49.34 ? 250 SER B C     1 
ATOM   4639 O O     . SER B 1 259 ? 17.254 -1.858  -28.966 1.00 51.03 ? 250 SER B O     1 
ATOM   4640 C CB    . SER B 1 259 ? 15.674 -3.971  -30.518 1.00 44.54 ? 250 SER B CB    1 
ATOM   4641 O OG    . SER B 1 259 ? 16.020 -5.321  -30.269 1.00 47.69 ? 250 SER B OG    1 
ATOM   4642 N N     . ASN B 1 260 ? 18.841 -3.374  -29.461 1.00 41.46 ? 251 ASN B N     1 
ATOM   4643 C CA    . ASN B 1 260 ? 19.686 -3.043  -28.313 1.00 40.76 ? 251 ASN B CA    1 
ATOM   4644 C C     . ASN B 1 260 ? 21.138 -3.236  -28.713 1.00 41.45 ? 251 ASN B C     1 
ATOM   4645 O O     . ASN B 1 260 ? 21.743 -4.284  -28.453 1.00 38.93 ? 251 ASN B O     1 
ATOM   4646 C CB    . ASN B 1 260 ? 19.330 -3.901  -27.098 1.00 43.84 ? 251 ASN B CB    1 
ATOM   4647 C CG    . ASN B 1 260 ? 19.816 -3.298  -25.795 1.00 38.00 ? 251 ASN B CG    1 
ATOM   4648 O OD1   . ASN B 1 260 ? 20.674 -2.416  -25.787 1.00 40.68 ? 251 ASN B OD1   1 
ATOM   4649 N ND2   . ASN B 1 260 ? 19.267 -3.773  -24.683 1.00 44.45 ? 251 ASN B ND2   1 
ATOM   4650 N N     . PRO B 1 261 ? 21.737 -2.234  -29.366 1.00 43.42 ? 252 PRO B N     1 
ATOM   4651 C CA    . PRO B 1 261 ? 23.119 -2.402  -29.851 1.00 35.45 ? 252 PRO B CA    1 
ATOM   4652 C C     . PRO B 1 261 ? 24.128 -2.660  -28.746 1.00 37.33 ? 252 PRO B C     1 
ATOM   4653 O O     . PRO B 1 261 ? 25.078 -3.426  -28.951 1.00 40.36 ? 252 PRO B O     1 
ATOM   4654 C CB    . PRO B 1 261 ? 23.396 -1.076  -30.574 1.00 40.61 ? 252 PRO B CB    1 
ATOM   4655 C CG    . PRO B 1 261 ? 22.045 -0.552  -30.939 1.00 36.42 ? 252 PRO B CG    1 
ATOM   4656 C CD    . PRO B 1 261 ? 21.142 -0.964  -29.815 1.00 43.41 ? 252 PRO B CD    1 
ATOM   4657 N N     . LEU B 1 262 ? 23.953 -2.042  -27.577 1.00 36.87 ? 253 LEU B N     1 
ATOM   4658 C CA    . LEU B 1 262 ? 24.898 -2.258  -26.487 1.00 34.43 ? 253 LEU B CA    1 
ATOM   4659 C C     . LEU B 1 262 ? 24.803 -3.681  -25.953 1.00 37.26 ? 253 LEU B C     1 
ATOM   4660 O O     . LEU B 1 262 ? 25.821 -4.368  -25.807 1.00 33.07 ? 253 LEU B O     1 
ATOM   4661 C CB    . LEU B 1 262 ? 24.658 -1.245  -25.368 1.00 38.17 ? 253 LEU B CB    1 
ATOM   4662 C CG    . LEU B 1 262 ? 25.541 -1.434  -24.134 1.00 38.03 ? 253 LEU B CG    1 
ATOM   4663 C CD1   . LEU B 1 262 ? 27.004 -1.490  -24.535 1.00 34.38 ? 253 LEU B CD1   1 
ATOM   4664 C CD2   . LEU B 1 262 ? 25.304 -0.328  -23.121 1.00 32.64 ? 253 LEU B CD2   1 
ATOM   4665 N N     . SER B 1 263 ? 23.587 -4.140  -25.649 1.00 30.75 ? 254 SER B N     1 
ATOM   4666 C CA    . SER B 1 263 ? 23.420 -5.508  -25.169 1.00 36.75 ? 254 SER B CA    1 
ATOM   4667 C C     . SER B 1 263 ? 23.797 -6.522  -26.239 1.00 36.59 ? 254 SER B C     1 
ATOM   4668 O O     . SER B 1 263 ? 24.320 -7.596  -25.916 1.00 39.78 ? 254 SER B O     1 
ATOM   4669 C CB    . SER B 1 263 ? 21.983 -5.734  -24.701 1.00 33.06 ? 254 SER B CB    1 
ATOM   4670 O OG    . SER B 1 263 ? 21.803 -7.057  -24.230 1.00 57.12 ? 254 SER B OG    1 
ATOM   4671 N N     . LEU B 1 264 ? 23.542 -6.206  -27.511 1.00 36.09 ? 255 LEU B N     1 
ATOM   4672 C CA    . LEU B 1 264 ? 24.058 -7.049  -28.583 1.00 37.34 ? 255 LEU B CA    1 
ATOM   4673 C C     . LEU B 1 264 ? 25.576 -6.977  -28.652 1.00 41.39 ? 255 LEU B C     1 
ATOM   4674 O O     . LEU B 1 264 ? 26.223 -7.954  -29.040 1.00 37.37 ? 255 LEU B O     1 
ATOM   4675 C CB    . LEU B 1 264 ? 23.445 -6.649  -29.926 1.00 28.31 ? 255 LEU B CB    1 
ATOM   4676 C CG    . LEU B 1 264 ? 24.092 -7.280  -31.164 1.00 40.04 ? 255 LEU B CG    1 
ATOM   4677 C CD1   . LEU B 1 264 ? 23.731 -8.757  -31.261 1.00 42.34 ? 255 LEU B CD1   1 
ATOM   4678 C CD2   . LEU B 1 264 ? 23.720 -6.545  -32.441 1.00 30.90 ? 255 LEU B CD2   1 
ATOM   4679 N N     . GLY B 1 265 ? 26.162 -5.836  -28.276 1.00 38.65 ? 256 GLY B N     1 
ATOM   4680 C CA    . GLY B 1 265 ? 27.607 -5.716  -28.253 1.00 34.73 ? 256 GLY B CA    1 
ATOM   4681 C C     . GLY B 1 265 ? 28.274 -6.411  -27.089 1.00 43.30 ? 256 GLY B C     1 
ATOM   4682 O O     . GLY B 1 265 ? 29.453 -6.766  -27.189 1.00 44.83 ? 256 GLY B O     1 
ATOM   4683 N N     . LEU B 1 266 ? 27.544 -6.635  -25.995 1.00 35.40 ? 257 LEU B N     1 
ATOM   4684 C CA    . LEU B 1 266 ? 28.103 -7.308  -24.833 1.00 37.33 ? 257 LEU B CA    1 
ATOM   4685 C C     . LEU B 1 266 ? 27.985 -8.822  -24.908 1.00 35.20 ? 257 LEU B C     1 
ATOM   4686 O O     . LEU B 1 266 ? 28.731 -9.519  -24.214 1.00 33.81 ? 257 LEU B O     1 
ATOM   4687 C CB    . LEU B 1 266 ? 27.422 -6.807  -23.556 1.00 34.46 ? 257 LEU B CB    1 
ATOM   4688 C CG    . LEU B 1 266 ? 27.651 -5.340  -23.188 1.00 31.03 ? 257 LEU B CG    1 
ATOM   4689 C CD1   . LEU B 1 266 ? 26.879 -4.964  -21.933 1.00 36.66 ? 257 LEU B CD1   1 
ATOM   4690 C CD2   . LEU B 1 266 ? 29.136 -5.077  -23.003 1.00 32.61 ? 257 LEU B CD2   1 
ATOM   4691 N N     . ALA B 1 267 ? 27.073 -9.346  -25.730 1.00 35.85 ? 258 ALA B N     1 
ATOM   4692 C CA    . ALA B 1 267 ? 26.880 -10.790 -25.809 1.00 41.91 ? 258 ALA B CA    1 
ATOM   4693 C C     . ALA B 1 267 ? 27.996 -11.470 -26.595 1.00 39.42 ? 258 ALA B C     1 
ATOM   4694 O O     . ALA B 1 267 ? 28.502 -12.516 -26.174 1.00 34.57 ? 258 ALA B O     1 
ATOM   4695 C CB    . ALA B 1 267 ? 25.520 -11.104 -26.431 1.00 42.05 ? 258 ALA B CB    1 
ATOM   4696 N N     . VAL B 1 268 ? 28.382 -10.902 -27.740 1.00 37.76 ? 259 VAL B N     1 
ATOM   4697 C CA    . VAL B 1 268 ? 29.492 -11.452 -28.513 1.00 39.43 ? 259 VAL B CA    1 
ATOM   4698 C C     . VAL B 1 268 ? 30.793 -11.328 -27.732 1.00 35.11 ? 259 VAL B C     1 
ATOM   4699 O O     . VAL B 1 268 ? 31.616 -12.251 -27.722 1.00 36.07 ? 259 VAL B O     1 
ATOM   4700 C CB    . VAL B 1 268 ? 29.585 -10.757 -29.884 1.00 40.00 ? 259 VAL B CB    1 
ATOM   4701 C CG1   . VAL B 1 268 ? 30.845 -11.190 -30.620 1.00 38.33 ? 259 VAL B CG1   1 
ATOM   4702 C CG2   . VAL B 1 268 ? 28.342 -11.046 -30.712 1.00 40.23 ? 259 VAL B CG2   1 
ATOM   4703 N N     . VAL B 1 269 ? 30.999 -10.187 -27.067 1.00 32.50 ? 260 VAL B N     1 
ATOM   4704 C CA    . VAL B 1 269 ? 32.149 -10.038 -26.178 1.00 35.74 ? 260 VAL B CA    1 
ATOM   4705 C C     . VAL B 1 269 ? 32.150 -11.144 -25.132 1.00 32.32 ? 260 VAL B C     1 
ATOM   4706 O O     . VAL B 1 269 ? 33.200 -11.711 -24.802 1.00 32.82 ? 260 VAL B O     1 
ATOM   4707 C CB    . VAL B 1 269 ? 32.145 -8.639  -25.532 1.00 39.59 ? 260 VAL B CB    1 
ATOM   4708 C CG1   . VAL B 1 269 ? 33.003 -8.620  -24.276 1.00 31.81 ? 260 VAL B CG1   1 
ATOM   4709 C CG2   . VAL B 1 269 ? 32.624 -7.593  -26.527 1.00 38.81 ? 260 VAL B CG2   1 
ATOM   4710 N N     . GLU B 1 270 ? 30.969 -11.482 -24.609 1.00 33.80 ? 261 GLU B N     1 
ATOM   4711 C CA    . GLU B 1 270 ? 30.861 -12.610 -23.689 1.00 44.15 ? 261 GLU B CA    1 
ATOM   4712 C C     . GLU B 1 270 ? 31.233 -13.917 -24.378 1.00 34.95 ? 261 GLU B C     1 
ATOM   4713 O O     . GLU B 1 270 ? 31.916 -14.765 -23.790 1.00 38.60 ? 261 GLU B O     1 
ATOM   4714 C CB    . GLU B 1 270 ? 29.444 -12.683 -23.122 1.00 45.19 ? 261 GLU B CB    1 
ATOM   4715 C CG    . GLU B 1 270 ? 29.384 -12.889 -21.622 1.00 53.10 ? 261 GLU B CG    1 
ATOM   4716 C CD    . GLU B 1 270 ? 29.468 -14.350 -21.236 1.00 58.65 ? 261 GLU B CD    1 
ATOM   4717 O OE1   . GLU B 1 270 ? 30.324 -14.693 -20.392 1.00 76.56 ? 261 GLU B OE1   1 
ATOM   4718 O OE2   . GLU B 1 270 ? 28.681 -15.154 -21.775 1.00 58.10 ? 261 GLU B OE2   1 
ATOM   4719 N N     . ARG B 1 271 ? 30.796 -14.096 -25.627 1.00 39.58 ? 262 ARG B N     1 
ATOM   4720 C CA    . ARG B 1 271 ? 31.181 -15.284 -26.381 1.00 34.63 ? 262 ARG B CA    1 
ATOM   4721 C C     . ARG B 1 271 ? 32.684 -15.314 -26.625 1.00 31.68 ? 262 ARG B C     1 
ATOM   4722 O O     . ARG B 1 271 ? 33.317 -16.371 -26.520 1.00 36.34 ? 262 ARG B O     1 
ATOM   4723 C CB    . ARG B 1 271 ? 30.427 -15.336 -27.709 1.00 36.03 ? 262 ARG B CB    1 
ATOM   4724 C CG    . ARG B 1 271 ? 28.912 -15.382 -27.579 1.00 43.72 ? 262 ARG B CG    1 
ATOM   4725 C CD    . ARG B 1 271 ? 28.462 -16.380 -26.528 1.00 31.51 ? 262 ARG B CD    1 
ATOM   4726 N NE    . ARG B 1 271 ? 27.009 -16.446 -26.439 1.00 45.01 ? 262 ARG B NE    1 
ATOM   4727 C CZ    . ARG B 1 271 ? 26.257 -15.578 -25.773 1.00 54.63 ? 262 ARG B CZ    1 
ATOM   4728 N NH1   . ARG B 1 271 ? 26.792 -14.562 -25.114 1.00 40.31 ? 262 ARG B NH1   1 
ATOM   4729 N NH2   . ARG B 1 271 ? 24.936 -15.734 -25.768 1.00 54.53 ? 262 ARG B NH2   1 
ATOM   4730 N N     . LEU B 1 272 ? 33.273 -14.161 -26.952 1.00 31.76 ? 263 LEU B N     1 
ATOM   4731 C CA    . LEU B 1 272 ? 34.714 -14.110 -27.181 1.00 32.17 ? 263 LEU B CA    1 
ATOM   4732 C C     . LEU B 1 272 ? 35.487 -14.404 -25.902 1.00 33.00 ? 263 LEU B C     1 
ATOM   4733 O O     . LEU B 1 272 ? 36.506 -15.102 -25.933 1.00 31.19 ? 263 LEU B O     1 
ATOM   4734 C CB    . LEU B 1 272 ? 35.110 -12.746 -27.749 1.00 31.44 ? 263 LEU B CB    1 
ATOM   4735 C CG    . LEU B 1 272 ? 34.484 -12.339 -29.087 1.00 40.88 ? 263 LEU B CG    1 
ATOM   4736 C CD1   . LEU B 1 272 ? 35.157 -11.087 -29.632 1.00 29.66 ? 263 LEU B CD1   1 
ATOM   4737 C CD2   . LEU B 1 272 ? 34.542 -13.476 -30.104 1.00 33.39 ? 263 LEU B CD2   1 
ATOM   4738 N N     . ASN B 1 273 ? 35.019 -13.874 -24.768 1.00 38.25 ? 264 ASN B N     1 
ATOM   4739 C CA    . ASN B 1 273 ? 35.664 -14.169 -23.493 1.00 31.92 ? 264 ASN B CA    1 
ATOM   4740 C C     . ASN B 1 273 ? 35.596 -15.658 -23.174 1.00 34.52 ? 264 ASN B C     1 
ATOM   4741 O O     . ASN B 1 273 ? 36.591 -16.257 -22.750 1.00 39.66 ? 264 ASN B O     1 
ATOM   4742 C CB    . ASN B 1 273 ? 35.012 -13.355 -22.373 1.00 37.48 ? 264 ASN B CB    1 
ATOM   4743 C CG    . ASN B 1 273 ? 35.489 -11.914 -22.339 1.00 38.44 ? 264 ASN B CG    1 
ATOM   4744 O OD1   . ASN B 1 273 ? 36.434 -11.539 -23.035 1.00 36.50 ? 264 ASN B OD1   1 
ATOM   4745 N ND2   . ASN B 1 273 ? 34.836 -11.098 -21.521 1.00 39.84 ? 264 ASN B ND2   1 
ATOM   4746 N N     . LYS B 1 274 ? 34.429 -16.274 -23.381 1.00 37.14 ? 265 LYS B N     1 
ATOM   4747 C CA    . LYS B 1 274 ? 34.264 -17.689 -23.063 1.00 39.63 ? 265 LYS B CA    1 
ATOM   4748 C C     . LYS B 1 274 ? 35.097 -18.570 -23.986 1.00 42.97 ? 265 LYS B C     1 
ATOM   4749 O O     . LYS B 1 274 ? 35.616 -19.609 -23.559 1.00 40.11 ? 265 LYS B O     1 
ATOM   4750 C CB    . LYS B 1 274 ? 32.787 -18.075 -23.140 1.00 39.19 ? 265 LYS B CB    1 
ATOM   4751 N N     . ILE B 1 275 ? 35.230 -18.180 -25.257 1.00 39.10 ? 266 ILE B N     1 
ATOM   4752 C CA    . ILE B 1 275 ? 36.082 -18.935 -26.172 1.00 37.75 ? 266 ILE B CA    1 
ATOM   4753 C C     . ILE B 1 275 ? 37.533 -18.865 -25.718 1.00 43.67 ? 266 ILE B C     1 
ATOM   4754 O O     . ILE B 1 275 ? 38.257 -19.868 -25.743 1.00 45.21 ? 266 ILE B O     1 
ATOM   4755 C CB    . ILE B 1 275 ? 35.917 -18.418 -27.613 1.00 39.60 ? 266 ILE B CB    1 
ATOM   4756 C CG1   . ILE B 1 275 ? 34.571 -18.856 -28.188 1.00 40.50 ? 266 ILE B CG1   1 
ATOM   4757 C CG2   . ILE B 1 275 ? 37.054 -18.916 -28.495 1.00 35.98 ? 266 ILE B CG2   1 
ATOM   4758 C CD1   . ILE B 1 275 ? 34.145 -18.063 -29.401 1.00 32.96 ? 266 ILE B CD1   1 
ATOM   4759 N N     . GLN B 1 276 ? 37.977 -17.682 -25.285 1.00 36.05 ? 267 GLN B N     1 
ATOM   4760 C CA    . GLN B 1 276 ? 39.355 -17.526 -24.835 1.00 35.75 ? 267 GLN B CA    1 
ATOM   4761 C C     . GLN B 1 276 ? 39.632 -18.372 -23.598 1.00 41.17 ? 267 GLN B C     1 
ATOM   4762 O O     . GLN B 1 276 ? 40.703 -18.979 -23.478 1.00 41.77 ? 267 GLN B O     1 
ATOM   4763 C CB    . GLN B 1 276 ? 39.653 -16.052 -24.559 1.00 34.52 ? 267 GLN B CB    1 
ATOM   4764 C CG    . GLN B 1 276 ? 39.726 -15.190 -25.813 1.00 38.09 ? 267 GLN B CG    1 
ATOM   4765 C CD    . GLN B 1 276 ? 39.915 -13.717 -25.506 1.00 40.21 ? 267 GLN B CD    1 
ATOM   4766 O OE1   . GLN B 1 276 ? 40.197 -12.915 -26.401 1.00 31.25 ? 267 GLN B OE1   1 
ATOM   4767 N NE2   . GLN B 1 276 ? 39.764 -13.351 -24.236 1.00 34.74 ? 267 GLN B NE2   1 
ATOM   4768 N N     . LEU B 1 277 ? 38.673 -18.432 -22.671 1.00 40.05 ? 268 LEU B N     1 
ATOM   4769 C CA    . LEU B 1 277 ? 38.869 -19.214 -21.454 1.00 49.60 ? 268 LEU B CA    1 
ATOM   4770 C C     . LEU B 1 277 ? 38.837 -20.709 -21.742 1.00 48.63 ? 268 LEU B C     1 
ATOM   4771 O O     . LEU B 1 277 ? 39.612 -21.476 -21.158 1.00 55.20 ? 268 LEU B O     1 
ATOM   4772 C CB    . LEU B 1 277 ? 37.807 -18.844 -20.419 1.00 41.82 ? 268 LEU B CB    1 
ATOM   4773 C CG    . LEU B 1 277 ? 37.862 -17.407 -19.896 1.00 48.74 ? 268 LEU B CG    1 
ATOM   4774 C CD1   . LEU B 1 277 ? 36.604 -17.069 -19.114 1.00 42.63 ? 268 LEU B CD1   1 
ATOM   4775 C CD2   . LEU B 1 277 ? 39.103 -17.193 -19.041 1.00 42.02 ? 268 LEU B CD2   1 
ATOM   4776 N N     . HIS B 1 278 ? 37.946 -21.143 -22.638 1.00 46.57 ? 269 HIS B N     1 
ATOM   4777 C CA    . HIS B 1 278 ? 37.834 -22.567 -22.939 1.00 52.29 ? 269 HIS B CA    1 
ATOM   4778 C C     . HIS B 1 278 ? 39.063 -23.075 -23.683 1.00 56.75 ? 269 HIS B C     1 
ATOM   4779 O O     . HIS B 1 278 ? 39.510 -24.205 -23.454 1.00 59.60 ? 269 HIS B O     1 
ATOM   4780 C CB    . HIS B 1 278 ? 36.565 -22.832 -23.750 1.00 49.56 ? 269 HIS B CB    1 
ATOM   4781 C CG    . HIS B 1 278 ? 36.130 -24.265 -23.742 1.00 63.77 ? 269 HIS B CG    1 
ATOM   4782 N ND1   . HIS B 1 278 ? 35.766 -24.926 -22.588 1.00 67.26 ? 269 HIS B ND1   1 
ATOM   4783 C CD2   . HIS B 1 278 ? 35.998 -25.162 -24.747 1.00 65.38 ? 269 HIS B CD2   1 
ATOM   4784 C CE1   . HIS B 1 278 ? 35.430 -26.169 -22.883 1.00 65.93 ? 269 HIS B CE1   1 
ATOM   4785 N NE2   . HIS B 1 278 ? 35.562 -26.338 -24.186 1.00 73.01 ? 269 HIS B NE2   1 
ATOM   4786 N N     . SER B 1 279 ? 39.624 -22.258 -24.571 1.00 46.75 ? 270 SER B N     1 
ATOM   4787 C CA    . SER B 1 279 ? 40.798 -22.642 -25.343 1.00 48.14 ? 270 SER B CA    1 
ATOM   4788 C C     . SER B 1 279 ? 42.106 -22.261 -24.664 1.00 50.23 ? 270 SER B C     1 
ATOM   4789 O O     . SER B 1 279 ? 43.176 -22.544 -25.214 1.00 50.89 ? 270 SER B O     1 
ATOM   4790 C CB    . SER B 1 279 ? 40.740 -22.010 -26.737 1.00 44.95 ? 270 SER B CB    1 
ATOM   4791 O OG    . SER B 1 279 ? 41.013 -20.622 -26.671 1.00 48.52 ? 270 SER B OG    1 
ATOM   4792 N N     . GLY B 1 280 ? 42.049 -21.628 -23.494 1.00 47.86 ? 271 GLY B N     1 
ATOM   4793 C CA    . GLY B 1 280 ? 43.256 -21.291 -22.761 1.00 44.60 ? 271 GLY B CA    1 
ATOM   4794 C C     . GLY B 1 280 ? 44.176 -20.319 -23.460 1.00 46.43 ? 271 GLY B C     1 
ATOM   4795 O O     . GLY B 1 280 ? 45.376 -20.300 -23.174 1.00 44.76 ? 271 GLY B O     1 
ATOM   4796 N N     . SER B 1 281 ? 43.650 -19.504 -24.373 1.00 46.01 ? 272 SER B N     1 
ATOM   4797 C CA    . SER B 1 281 ? 44.467 -18.553 -25.111 1.00 45.42 ? 272 SER B CA    1 
ATOM   4798 C C     . SER B 1 281 ? 43.610 -17.354 -25.486 1.00 44.73 ? 272 SER B C     1 
ATOM   4799 O O     . SER B 1 281 ? 42.383 -17.446 -25.569 1.00 40.00 ? 272 SER B O     1 
ATOM   4800 C CB    . SER B 1 281 ? 45.074 -19.191 -26.366 1.00 51.52 ? 272 SER B CB    1 
ATOM   4801 O OG    . SER B 1 281 ? 44.097 -19.930 -27.079 1.00 53.45 ? 272 SER B OG    1 
ATOM   4802 N N     . LYS B 1 282 ? 44.271 -16.225 -25.717 1.00 41.58 ? 273 LYS B N     1 
ATOM   4803 C CA    . LYS B 1 282 ? 43.592 -14.982 -26.053 1.00 36.89 ? 273 LYS B CA    1 
ATOM   4804 C C     . LYS B 1 282 ? 43.640 -14.740 -27.556 1.00 36.27 ? 273 LYS B C     1 
ATOM   4805 O O     . LYS B 1 282 ? 44.652 -15.011 -28.208 1.00 35.09 ? 273 LYS B O     1 
ATOM   4806 C CB    . LYS B 1 282 ? 44.221 -13.800 -25.315 1.00 45.12 ? 273 LYS B CB    1 
ATOM   4807 C CG    . LYS B 1 282 ? 43.371 -13.261 -24.174 1.00 47.79 ? 273 LYS B CG    1 
ATOM   4808 C CD    . LYS B 1 282 ? 44.024 -12.052 -23.521 1.00 49.46 ? 273 LYS B CD    1 
ATOM   4809 C CE    . LYS B 1 282 ? 43.451 -11.804 -22.136 1.00 47.16 ? 273 LYS B CE    1 
ATOM   4810 N NZ    . LYS B 1 282 ? 43.513 -13.028 -21.289 1.00 54.11 ? 273 LYS B NZ    1 
ATOM   4811 N N     . LEU B 1 283 ? 42.539 -14.225 -28.098 1.00 38.91 ? 274 LEU B N     1 
ATOM   4812 C CA    . LEU B 1 283 ? 42.496 -13.858 -29.503 1.00 35.17 ? 274 LEU B CA    1 
ATOM   4813 C C     . LEU B 1 283 ? 43.492 -12.736 -29.789 1.00 35.66 ? 274 LEU B C     1 
ATOM   4814 O O     . LEU B 1 283 ? 44.059 -12.117 -28.885 1.00 33.18 ? 274 LEU B O     1 
ATOM   4815 C CB    . LEU B 1 283 ? 41.089 -13.416 -29.903 1.00 36.32 ? 274 LEU B CB    1 
ATOM   4816 C CG    . LEU B 1 283 ? 39.959 -14.439 -29.795 1.00 36.70 ? 274 LEU B CG    1 
ATOM   4817 C CD1   . LEU B 1 283 ? 38.640 -13.732 -29.539 1.00 38.75 ? 274 LEU B CD1   1 
ATOM   4818 C CD2   . LEU B 1 283 ? 39.879 -15.271 -31.060 1.00 34.36 ? 274 LEU B CD2   1 
ATOM   4819 N N     . ALA B 1 284 ? 43.700 -12.475 -31.079 1.00 35.31 ? 275 ALA B N     1 
ATOM   4820 C CA    . ALA B 1 284 ? 44.570 -11.372 -31.469 1.00 34.72 ? 275 ALA B CA    1 
ATOM   4821 C C     . ALA B 1 284 ? 44.012 -10.041 -30.981 1.00 30.51 ? 275 ALA B C     1 
ATOM   4822 O O     . ALA B 1 284 ? 44.733 -9.239  -30.375 1.00 29.48 ? 275 ALA B O     1 
ATOM   4823 C CB    . ALA B 1 284 ? 44.757 -11.361 -32.988 1.00 30.96 ? 275 ALA B CB    1 
ATOM   4824 N N     . TYR B 1 285 ? 42.724 -9.795  -31.217 1.00 24.72 ? 276 TYR B N     1 
ATOM   4825 C CA    . TYR B 1 285 ? 42.115 -8.521  -30.853 1.00 28.88 ? 276 TYR B CA    1 
ATOM   4826 C C     . TYR B 1 285 ? 40.611 -8.598  -31.070 1.00 30.81 ? 276 TYR B C     1 
ATOM   4827 O O     . TYR B 1 285 ? 40.085 -9.569  -31.620 1.00 31.77 ? 276 TYR B O     1 
ATOM   4828 C CB    . TYR B 1 285 ? 42.696 -7.362  -31.668 1.00 30.03 ? 276 TYR B CB    1 
ATOM   4829 C CG    . TYR B 1 285 ? 42.639 -7.575  -33.167 1.00 31.28 ? 276 TYR B CG    1 
ATOM   4830 C CD1   . TYR B 1 285 ? 41.493 -7.268  -33.894 1.00 32.69 ? 276 TYR B CD1   1 
ATOM   4831 C CD2   . TYR B 1 285 ? 43.734 -8.078  -33.857 1.00 34.78 ? 276 TYR B CD2   1 
ATOM   4832 C CE1   . TYR B 1 285 ? 41.441 -7.462  -35.267 1.00 31.65 ? 276 TYR B CE1   1 
ATOM   4833 C CE2   . TYR B 1 285 ? 43.690 -8.274  -35.227 1.00 35.80 ? 276 TYR B CE2   1 
ATOM   4834 C CZ    . TYR B 1 285 ? 42.544 -7.963  -35.927 1.00 32.29 ? 276 TYR B CZ    1 
ATOM   4835 O OH    . TYR B 1 285 ? 42.505 -8.158  -37.291 1.00 31.85 ? 276 TYR B OH    1 
ATOM   4836 N N     . LEU B 1 286 ? 39.930 -7.540  -30.636 1.00 30.02 ? 277 LEU B N     1 
ATOM   4837 C CA    . LEU B 1 286 ? 38.540 -7.276  -30.982 1.00 28.41 ? 277 LEU B CA    1 
ATOM   4838 C C     . LEU B 1 286 ? 38.484 -5.918  -31.667 1.00 32.92 ? 277 LEU B C     1 
ATOM   4839 O O     . LEU B 1 286 ? 38.893 -4.907  -31.085 1.00 30.61 ? 277 LEU B O     1 
ATOM   4840 C CB    . LEU B 1 286 ? 37.641 -7.302  -29.745 1.00 33.96 ? 277 LEU B CB    1 
ATOM   4841 C CG    . LEU B 1 286 ? 36.277 -6.617  -29.859 1.00 28.04 ? 277 LEU B CG    1 
ATOM   4842 C CD1   . LEU B 1 286 ? 35.369 -7.377  -30.813 1.00 27.06 ? 277 LEU B CD1   1 
ATOM   4843 C CD2   . LEU B 1 286 ? 35.639 -6.508  -28.483 1.00 29.92 ? 277 LEU B CD2   1 
ATOM   4844 N N     . HIS B 1 287 ? 37.991 -5.901  -32.900 1.00 31.20 ? 278 HIS B N     1 
ATOM   4845 C CA    . HIS B 1 287 ? 37.942 -4.708  -33.735 1.00 27.00 ? 278 HIS B CA    1 
ATOM   4846 C C     . HIS B 1 287 ? 36.499 -4.232  -33.809 1.00 30.57 ? 278 HIS B C     1 
ATOM   4847 O O     . HIS B 1 287 ? 35.616 -4.986  -34.226 1.00 26.47 ? 278 HIS B O     1 
ATOM   4848 C CB    . HIS B 1 287 ? 38.485 -5.017  -35.131 1.00 35.05 ? 278 HIS B CB    1 
ATOM   4849 C CG    . HIS B 1 287 ? 38.899 -3.808  -35.911 1.00 34.28 ? 278 HIS B CG    1 
ATOM   4850 N ND1   . HIS B 1 287 ? 39.497 -3.895  -37.149 1.00 38.34 ? 278 HIS B ND1   1 
ATOM   4851 C CD2   . HIS B 1 287 ? 38.797 -2.487  -35.634 1.00 27.41 ? 278 HIS B CD2   1 
ATOM   4852 C CE1   . HIS B 1 287 ? 39.750 -2.680  -37.601 1.00 36.65 ? 278 HIS B CE1   1 
ATOM   4853 N NE2   . HIS B 1 287 ? 39.335 -1.807  -36.701 1.00 37.30 ? 278 HIS B NE2   1 
ATOM   4854 N N     . VAL B 1 288 ? 36.250 -2.992  -33.396 1.00 28.63 ? 279 VAL B N     1 
ATOM   4855 C CA    . VAL B 1 288 ? 34.901 -2.440  -33.398 1.00 28.86 ? 279 VAL B CA    1 
ATOM   4856 C C     . VAL B 1 288 ? 34.905 -1.133  -34.174 1.00 34.95 ? 279 VAL B C     1 
ATOM   4857 O O     . VAL B 1 288 ? 35.758 -0.269  -33.942 1.00 32.46 ? 279 VAL B O     1 
ATOM   4858 C CB    . VAL B 1 288 ? 34.364 -2.215  -31.972 1.00 34.47 ? 279 VAL B CB    1 
ATOM   4859 C CG1   . VAL B 1 288 ? 32.933 -1.700  -32.031 1.00 33.83 ? 279 VAL B CG1   1 
ATOM   4860 C CG2   . VAL B 1 288 ? 34.432 -3.504  -31.171 1.00 26.50 ? 279 VAL B CG2   1 
ATOM   4861 N N     . THR B 1 289 ? 33.951 -0.985  -35.086 1.00 30.97 ? 280 THR B N     1 
ATOM   4862 C CA    . THR B 1 289 ? 33.777 0.252   -35.834 1.00 36.37 ? 280 THR B CA    1 
ATOM   4863 C C     . THR B 1 289 ? 32.571 1.005   -35.293 1.00 36.84 ? 280 THR B C     1 
ATOM   4864 O O     . THR B 1 289 ? 31.481 0.436   -35.168 1.00 41.47 ? 280 THR B O     1 
ATOM   4865 C CB    . THR B 1 289 ? 33.590 -0.013  -37.327 1.00 33.23 ? 280 THR B CB    1 
ATOM   4866 O OG1   . THR B 1 289 ? 34.539 -0.991  -37.765 1.00 43.03 ? 280 THR B OG1   1 
ATOM   4867 C CG2   . THR B 1 289 ? 33.808 1.274   -38.106 1.00 36.25 ? 280 THR B CG2   1 
ATOM   4868 N N     . GLN B 1 290 ? 32.766 2.247   -34.986 1.00 40.96 ? 281 GLN B N     1 
ATOM   4869 C CA    . GLN B 1 290 ? 31.711 3.075   -34.436 1.00 43.93 ? 281 GLN B CA    1 
ATOM   4870 C C     . GLN B 1 290 ? 31.121 3.980   -35.510 1.00 54.32 ? 281 GLN B C     1 
ATOM   4871 O O     . GLN B 1 290 ? 31.799 4.329   -36.484 1.00 42.15 ? 281 GLN B O     1 
ATOM   4872 C CB    . GLN B 1 290 ? 32.246 3.936   -33.288 1.00 43.52 ? 281 GLN B CB    1 
ATOM   4873 C CG    . GLN B 1 290 ? 33.339 4.913   -33.702 1.00 42.95 ? 281 GLN B CG    1 
ATOM   4874 C CD    . GLN B 1 290 ? 33.714 5.878   -32.591 1.00 48.16 ? 281 GLN B CD    1 
ATOM   4875 O OE1   . GLN B 1 290 ? 34.626 5.616   -31.807 1.00 51.35 ? 281 GLN B OE1   1 
ATOM   4876 N NE2   . GLN B 1 290 ? 33.014 7.005   -32.524 1.00 48.63 ? 281 GLN B NE2   1 
ATOM   4877 N N     . PRO B 1 291 ? 29.855 4.354   -35.369 1.00 50.64 ? 282 PRO B N     1 
ATOM   4878 C CA    . PRO B 1 291 ? 29.296 5.397   -36.230 1.00 47.77 ? 282 PRO B CA    1 
ATOM   4879 C C     . PRO B 1 291 ? 29.709 6.776   -35.743 1.00 53.25 ? 282 PRO B C     1 
ATOM   4880 O O     . PRO B 1 291 ? 29.945 7.000   -34.553 1.00 49.88 ? 282 PRO B O     1 
ATOM   4881 C CB    . PRO B 1 291 ? 27.784 5.189   -36.093 1.00 48.59 ? 282 PRO B CB    1 
ATOM   4882 C CG    . PRO B 1 291 ? 27.624 4.633   -34.715 1.00 48.41 ? 282 PRO B CG    1 
ATOM   4883 C CD    . PRO B 1 291 ? 28.845 3.780   -34.462 1.00 44.95 ? 282 PRO B CD    1 
ATOM   4884 N N     . ARG B 1 292 ? 29.803 7.707   -36.689 1.00 53.17 ? 283 ARG B N     1 
ATOM   4885 C CA    . ARG B 1 292 ? 30.210 9.077   -36.400 1.00 57.65 ? 283 ARG B CA    1 
ATOM   4886 C C     . ARG B 1 292 ? 29.207 10.029  -37.029 1.00 59.71 ? 283 ARG B C     1 
ATOM   4887 O O     . ARG B 1 292 ? 29.083 10.080  -38.258 1.00 64.40 ? 283 ARG B O     1 
ATOM   4888 C CB    . ARG B 1 292 ? 31.622 9.357   -36.923 1.00 52.40 ? 283 ARG B CB    1 
ATOM   4889 C CG    . ARG B 1 292 ? 32.718 8.625   -36.165 1.00 50.91 ? 283 ARG B CG    1 
ATOM   4890 C CD    . ARG B 1 292 ? 33.327 9.500   -35.081 1.00 43.97 ? 283 ARG B CD    1 
ATOM   4891 N NE    . ARG B 1 292 ? 34.631 9.005   -34.655 1.00 49.31 ? 283 ARG B NE    1 
ATOM   4892 C CZ    . ARG B 1 292 ? 35.312 9.479   -33.620 1.00 53.25 ? 283 ARG B CZ    1 
ATOM   4893 N NH1   . ARG B 1 292 ? 34.845 10.472  -32.881 1.00 49.01 ? 283 ARG B NH1   1 
ATOM   4894 N NH2   . ARG B 1 292 ? 36.492 8.943   -33.320 1.00 46.36 ? 283 ARG B NH2   1 
ATOM   4895 N N     . SER B 1 293 ? 28.495 10.778  -36.193 1.00 63.02 ? 284 SER B N     1 
ATOM   4896 C CA    . SER B 1 293 ? 27.501 11.728  -36.674 1.00 67.60 ? 284 SER B CA    1 
ATOM   4897 C C     . SER B 1 293 ? 27.768 13.126  -36.126 1.00 75.55 ? 284 SER B C     1 
ATOM   4898 O O     . SER B 1 293 ? 27.937 13.308  -34.920 1.00 70.37 ? 284 SER B O     1 
ATOM   4899 C CB    . SER B 1 293 ? 26.093 11.271  -36.289 1.00 64.45 ? 284 SER B CB    1 
ATOM   4900 O OG    . SER B 1 293 ? 25.115 12.177  -36.768 1.00 74.29 ? 284 SER B OG    1 
ATOM   4901 N N     . SER B 1 298 ? 25.523 12.369  -30.996 1.00 52.48 ? 289 SER B N     1 
ATOM   4902 C CA    . SER B 1 298 ? 26.184 12.689  -29.736 1.00 50.86 ? 289 SER B CA    1 
ATOM   4903 C C     . SER B 1 298 ? 27.520 11.964  -29.620 1.00 51.84 ? 289 SER B C     1 
ATOM   4904 O O     . SER B 1 298 ? 27.566 10.734  -29.565 1.00 54.01 ? 289 SER B O     1 
ATOM   4905 C CB    . SER B 1 298 ? 25.285 12.328  -28.551 1.00 53.35 ? 289 SER B CB    1 
ATOM   4906 O OG    . SER B 1 298 ? 25.730 12.954  -27.361 1.00 59.15 ? 289 SER B OG    1 
ATOM   4907 N N     . GLU B 1 299 ? 28.609 12.736  -29.581 1.00 42.86 ? 290 GLU B N     1 
ATOM   4908 C CA    . GLU B 1 299 ? 29.934 12.135  -29.466 1.00 44.54 ? 290 GLU B CA    1 
ATOM   4909 C C     . GLU B 1 299 ? 30.124 11.438  -28.125 1.00 49.00 ? 290 GLU B C     1 
ATOM   4910 O O     . GLU B 1 299 ? 30.888 10.471  -28.035 1.00 47.96 ? 290 GLU B O     1 
ATOM   4911 C CB    . GLU B 1 299 ? 31.013 13.198  -29.670 1.00 45.05 ? 290 GLU B CB    1 
ATOM   4912 N N     . GLU B 1 300 ? 29.440 11.907  -27.077 1.00 47.60 ? 291 GLU B N     1 
ATOM   4913 C CA    . GLU B 1 300 ? 29.595 11.294  -25.761 1.00 47.29 ? 291 GLU B CA    1 
ATOM   4914 C C     . GLU B 1 300 ? 28.917 9.931   -25.699 1.00 44.35 ? 291 GLU B C     1 
ATOM   4915 O O     . GLU B 1 300 ? 29.441 9.000   -25.076 1.00 40.91 ? 291 GLU B O     1 
ATOM   4916 C CB    . GLU B 1 300 ? 29.034 12.220  -24.682 1.00 43.62 ? 291 GLU B CB    1 
ATOM   4917 N N     . GLU B 1 301 ? 27.749 9.795   -26.330 1.00 43.68 ? 292 GLU B N     1 
ATOM   4918 C CA    . GLU B 1 301 ? 27.039 8.520   -26.310 1.00 49.10 ? 292 GLU B CA    1 
ATOM   4919 C C     . GLU B 1 301 ? 27.775 7.468   -27.130 1.00 44.94 ? 292 GLU B C     1 
ATOM   4920 O O     . GLU B 1 301 ? 27.935 6.323   -26.689 1.00 42.12 ? 292 GLU B O     1 
ATOM   4921 C CB    . GLU B 1 301 ? 25.612 8.706   -26.827 1.00 51.16 ? 292 GLU B CB    1 
ATOM   4922 N N     . GLU B 1 302 ? 28.229 7.839   -28.330 1.00 41.92 ? 293 GLU B N     1 
ATOM   4923 C CA    . GLU B 1 302 ? 28.976 6.902   -29.163 1.00 41.56 ? 293 GLU B CA    1 
ATOM   4924 C C     . GLU B 1 302 ? 30.271 6.472   -28.486 1.00 45.68 ? 293 GLU B C     1 
ATOM   4925 O O     . GLU B 1 302 ? 30.653 5.297   -28.550 1.00 36.88 ? 293 GLU B O     1 
ATOM   4926 C CB    . GLU B 1 302 ? 29.272 7.527   -30.527 1.00 51.95 ? 293 GLU B CB    1 
ATOM   4927 C CG    . GLU B 1 302 ? 28.102 8.268   -31.153 1.00 53.09 ? 293 GLU B CG    1 
ATOM   4928 C CD    . GLU B 1 302 ? 28.478 8.959   -32.453 1.00 52.23 ? 293 GLU B CD    1 
ATOM   4929 O OE1   . GLU B 1 302 ? 29.609 9.482   -32.546 1.00 51.75 ? 293 GLU B OE1   1 
ATOM   4930 O OE2   . GLU B 1 302 ? 27.641 8.980   -33.382 1.00 58.27 ? 293 GLU B OE2   1 
ATOM   4931 N N     . ALA B 1 303 ? 30.960 7.410   -27.830 1.00 42.20 ? 294 ALA B N     1 
ATOM   4932 C CA    . ALA B 1 303 ? 32.212 7.067   -27.164 1.00 42.64 ? 294 ALA B CA    1 
ATOM   4933 C C     . ALA B 1 303 ? 31.977 6.198   -25.936 1.00 40.89 ? 294 ALA B C     1 
ATOM   4934 O O     . ALA B 1 303 ? 32.830 5.371   -25.593 1.00 34.70 ? 294 ALA B O     1 
ATOM   4935 C CB    . ALA B 1 303 ? 32.973 8.334   -26.780 1.00 41.61 ? 294 ALA B CB    1 
ATOM   4936 N N     . ARG B 1 304 ? 30.837 6.368   -25.265 1.00 39.78 ? 295 ARG B N     1 
ATOM   4937 C CA    . ARG B 1 304 ? 30.547 5.553   -24.090 1.00 45.74 ? 295 ARG B CA    1 
ATOM   4938 C C     . ARG B 1 304 ? 30.347 4.093   -24.474 1.00 38.51 ? 295 ARG B C     1 
ATOM   4939 O O     . ARG B 1 304 ? 30.925 3.195   -23.854 1.00 32.82 ? 295 ARG B O     1 
ATOM   4940 C CB    . ARG B 1 304 ? 29.317 6.094   -23.361 1.00 44.55 ? 295 ARG B CB    1 
ATOM   4941 C CG    . ARG B 1 304 ? 29.064 5.438   -22.012 1.00 45.92 ? 295 ARG B CG    1 
ATOM   4942 C CD    . ARG B 1 304 ? 27.790 5.961   -21.370 1.00 42.36 ? 295 ARG B CD    1 
ATOM   4943 N NE    . ARG B 1 304 ? 26.600 5.563   -22.113 1.00 53.28 ? 295 ARG B NE    1 
ATOM   4944 C CZ    . ARG B 1 304 ? 25.445 6.215   -22.082 1.00 50.61 ? 295 ARG B CZ    1 
ATOM   4945 N NH1   . ARG B 1 304 ? 25.289 7.309   -21.356 1.00 50.17 ? 295 ARG B NH1   1 
ATOM   4946 N NH2   . ARG B 1 304 ? 24.422 5.757   -22.799 1.00 52.95 ? 295 ARG B NH2   1 
ATOM   4947 N N     . LEU B 1 305 ? 29.534 3.839   -25.504 1.00 40.43 ? 296 LEU B N     1 
ATOM   4948 C CA    . LEU B 1 305 ? 29.279 2.466   -25.931 1.00 42.10 ? 296 LEU B CA    1 
ATOM   4949 C C     . LEU B 1 305 ? 30.575 1.745   -26.280 1.00 39.57 ? 296 LEU B C     1 
ATOM   4950 O O     . LEU B 1 305 ? 30.764 0.580   -25.912 1.00 35.15 ? 296 LEU B O     1 
ATOM   4951 C CB    . LEU B 1 305 ? 28.324 2.456   -27.124 1.00 33.48 ? 296 LEU B CB    1 
ATOM   4952 C CG    . LEU B 1 305 ? 27.688 1.108   -27.479 1.00 40.42 ? 296 LEU B CG    1 
ATOM   4953 C CD1   . LEU B 1 305 ? 26.193 1.266   -27.704 1.00 47.12 ? 296 LEU B CD1   1 
ATOM   4954 C CD2   . LEU B 1 305 ? 28.348 0.500   -28.704 1.00 37.48 ? 296 LEU B CD2   1 
ATOM   4955 N N     . MET B 1 306 ? 31.483 2.426   -26.984 1.00 36.56 ? 297 MET B N     1 
ATOM   4956 C CA    . MET B 1 306 ? 32.767 1.821   -27.322 1.00 38.77 ? 297 MET B CA    1 
ATOM   4957 C C     . MET B 1 306 ? 33.558 1.465   -26.070 1.00 37.75 ? 297 MET B C     1 
ATOM   4958 O O     . MET B 1 306 ? 34.168 0.392   -25.995 1.00 34.33 ? 297 MET B O     1 
ATOM   4959 C CB    . MET B 1 306 ? 33.574 2.766   -28.211 1.00 34.61 ? 297 MET B CB    1 
ATOM   4960 C CG    . MET B 1 306 ? 33.008 2.936   -29.612 1.00 46.28 ? 297 MET B CG    1 
ATOM   4961 S SD    . MET B 1 306 ? 33.333 1.500   -30.654 1.00 38.34 ? 297 MET B SD    1 
ATOM   4962 C CE    . MET B 1 306 ? 35.122 1.468   -30.635 1.00 27.93 ? 297 MET B CE    1 
ATOM   4963 N N     . ARG B 1 307 ? 33.553 2.352   -25.072 1.00 35.61 ? 298 ARG B N     1 
ATOM   4964 C CA    . ARG B 1 307 ? 34.312 2.094   -23.852 1.00 38.90 ? 298 ARG B CA    1 
ATOM   4965 C C     . ARG B 1 307 ? 33.723 0.931   -23.066 1.00 32.24 ? 298 ARG B C     1 
ATOM   4966 O O     . ARG B 1 307 ? 34.466 0.137   -22.476 1.00 38.05 ? 298 ARG B O     1 
ATOM   4967 C CB    . ARG B 1 307 ? 34.360 3.354   -22.989 1.00 42.47 ? 298 ARG B CB    1 
ATOM   4968 C CG    . ARG B 1 307 ? 35.249 3.229   -21.765 1.00 39.47 ? 298 ARG B CG    1 
ATOM   4969 C CD    . ARG B 1 307 ? 36.708 3.443   -22.128 1.00 48.27 ? 298 ARG B CD    1 
ATOM   4970 N NE    . ARG B 1 307 ? 37.609 2.719   -21.239 1.00 43.87 ? 298 ARG B NE    1 
ATOM   4971 C CZ    . ARG B 1 307 ? 38.646 3.267   -20.621 1.00 45.27 ? 298 ARG B CZ    1 
ATOM   4972 N NH1   . ARG B 1 307 ? 38.955 4.542   -20.788 1.00 41.19 ? 298 ARG B NH1   1 
ATOM   4973 N NH2   . ARG B 1 307 ? 39.391 2.517   -19.816 1.00 44.80 ? 298 ARG B NH2   1 
ATOM   4974 N N     . THR B 1 308 ? 32.392 0.814   -23.042 1.00 30.42 ? 299 THR B N     1 
ATOM   4975 C CA    . THR B 1 308 ? 31.760 -0.293  -22.329 1.00 39.90 ? 299 THR B CA    1 
ATOM   4976 C C     . THR B 1 308 ? 32.102 -1.630  -22.970 1.00 33.39 ? 299 THR B C     1 
ATOM   4977 O O     . THR B 1 308 ? 32.338 -2.619  -22.267 1.00 29.93 ? 299 THR B O     1 
ATOM   4978 C CB    . THR B 1 308 ? 30.245 -0.105  -22.291 1.00 40.44 ? 299 THR B CB    1 
ATOM   4979 O OG1   . THR B 1 308 ? 29.723 -0.199  -23.620 1.00 47.21 ? 299 THR B OG1   1 
ATOM   4980 C CG2   . THR B 1 308 ? 29.892 1.244   -21.713 1.00 42.24 ? 299 THR B CG2   1 
ATOM   4981 N N     . LEU B 1 309 ? 32.114 -1.685  -24.305 1.00 31.72 ? 300 LEU B N     1 
ATOM   4982 C CA    . LEU B 1 309 ? 32.551 -2.899  -24.987 1.00 30.57 ? 300 LEU B CA    1 
ATOM   4983 C C     . LEU B 1 309 ? 34.019 -3.177  -24.698 1.00 29.91 ? 300 LEU B C     1 
ATOM   4984 O O     . LEU B 1 309 ? 34.397 -4.310  -24.377 1.00 31.65 ? 300 LEU B O     1 
ATOM   4985 C CB    . LEU B 1 309 ? 32.310 -2.775  -26.493 1.00 35.22 ? 300 LEU B CB    1 
ATOM   4986 C CG    . LEU B 1 309 ? 30.858 -2.578  -26.932 1.00 38.46 ? 300 LEU B CG    1 
ATOM   4987 C CD1   . LEU B 1 309 ? 30.733 -2.637  -28.450 1.00 40.70 ? 300 LEU B CD1   1 
ATOM   4988 C CD2   . LEU B 1 309 ? 29.963 -3.611  -26.274 1.00 31.45 ? 300 LEU B CD2   1 
ATOM   4989 N N     . ARG B 1 310 ? 34.861 -2.146  -24.806 1.00 29.35 ? 301 ARG B N     1 
ATOM   4990 C CA    . ARG B 1 310 ? 36.279 -2.299  -24.499 1.00 32.11 ? 301 ARG B CA    1 
ATOM   4991 C C     . ARG B 1 310 ? 36.483 -2.813  -23.079 1.00 30.53 ? 301 ARG B C     1 
ATOM   4992 O O     . ARG B 1 310 ? 37.239 -3.764  -22.853 1.00 36.57 ? 301 ARG B O     1 
ATOM   4993 C CB    . ARG B 1 310 ? 36.999 -0.964  -24.695 1.00 35.17 ? 301 ARG B CB    1 
ATOM   4994 C CG    . ARG B 1 310 ? 38.513 -1.065  -24.688 1.00 30.14 ? 301 ARG B CG    1 
ATOM   4995 C CD    . ARG B 1 310 ? 39.103 -0.786  -23.314 1.00 34.37 ? 301 ARG B CD    1 
ATOM   4996 N NE    . ARG B 1 310 ? 40.423 -0.176  -23.405 1.00 37.69 ? 301 ARG B NE    1 
ATOM   4997 C CZ    . ARG B 1 310 ? 41.534 -0.828  -23.718 1.00 35.76 ? 301 ARG B CZ    1 
ATOM   4998 N NH1   . ARG B 1 310 ? 41.528 -2.129  -23.962 1.00 35.58 ? 301 ARG B NH1   1 
ATOM   4999 N NH2   . ARG B 1 310 ? 42.680 -0.159  -23.786 1.00 36.64 ? 301 ARG B NH2   1 
ATOM   5000 N N     . ASN B 1 311 ? 35.814 -2.191  -22.105 1.00 35.61 ? 302 ASN B N     1 
ATOM   5001 C CA    . ASN B 1 311 ? 35.978 -2.591  -20.711 1.00 35.91 ? 302 ASN B CA    1 
ATOM   5002 C C     . ASN B 1 311 ? 35.455 -3.994  -20.443 1.00 34.35 ? 302 ASN B C     1 
ATOM   5003 O O     . ASN B 1 311 ? 35.896 -4.633  -19.482 1.00 33.20 ? 302 ASN B O     1 
ATOM   5004 C CB    . ASN B 1 311 ? 35.270 -1.598  -19.788 1.00 33.56 ? 302 ASN B CB    1 
ATOM   5005 C CG    . ASN B 1 311 ? 35.983 -0.265  -19.709 1.00 34.97 ? 302 ASN B CG    1 
ATOM   5006 O OD1   . ASN B 1 311 ? 37.166 -0.159  -20.031 1.00 41.75 ? 302 ASN B OD1   1 
ATOM   5007 N ND2   . ASN B 1 311 ? 35.263 0.765   -19.277 1.00 44.27 ? 302 ASN B ND2   1 
ATOM   5008 N N     . ALA B 1 312 ? 34.529 -4.487  -21.264 1.00 29.55 ? 303 ALA B N     1 
ATOM   5009 C CA    . ALA B 1 312 ? 33.975 -5.816  -21.056 1.00 35.55 ? 303 ALA B CA    1 
ATOM   5010 C C     . ALA B 1 312 ? 34.840 -6.920  -21.652 1.00 30.70 ? 303 ALA B C     1 
ATOM   5011 O O     . ALA B 1 312 ? 34.754 -8.066  -21.199 1.00 30.56 ? 303 ALA B O     1 
ATOM   5012 C CB    . ALA B 1 312 ? 32.561 -5.891  -21.640 1.00 31.04 ? 303 ALA B CB    1 
ATOM   5013 N N     . TYR B 1 313 ? 35.677 -6.608  -22.640 1.00 38.27 ? 304 TYR B N     1 
ATOM   5014 C CA    . TYR B 1 313 ? 36.463 -7.623  -23.331 1.00 31.21 ? 304 TYR B CA    1 
ATOM   5015 C C     . TYR B 1 313 ? 37.840 -7.766  -22.693 1.00 34.11 ? 304 TYR B C     1 
ATOM   5016 O O     . TYR B 1 313 ? 38.543 -6.772  -22.485 1.00 35.11 ? 304 TYR B O     1 
ATOM   5017 C CB    . TYR B 1 313 ? 36.607 -7.278  -24.815 1.00 36.04 ? 304 TYR B CB    1 
ATOM   5018 C CG    . TYR B 1 313 ? 37.545 -8.213  -25.540 1.00 33.35 ? 304 TYR B CG    1 
ATOM   5019 C CD1   . TYR B 1 313 ? 37.311 -9.581  -25.556 1.00 35.41 ? 304 TYR B CD1   1 
ATOM   5020 C CD2   . TYR B 1 313 ? 38.676 -7.734  -26.190 1.00 34.34 ? 304 TYR B CD2   1 
ATOM   5021 C CE1   . TYR B 1 313 ? 38.166 -10.445 -26.208 1.00 36.58 ? 304 TYR B CE1   1 
ATOM   5022 C CE2   . TYR B 1 313 ? 39.538 -8.593  -26.848 1.00 29.69 ? 304 TYR B CE2   1 
ATOM   5023 C CZ    . TYR B 1 313 ? 39.277 -9.948  -26.849 1.00 29.40 ? 304 TYR B CZ    1 
ATOM   5024 O OH    . TYR B 1 313 ? 40.128 -10.814 -27.494 1.00 36.38 ? 304 TYR B OH    1 
ATOM   5025 N N     . GLN B 1 314 ? 38.225 -9.009  -22.393 1.00 28.06 ? 305 GLN B N     1 
ATOM   5026 C CA    . GLN B 1 314 ? 39.542 -9.311  -21.832 1.00 35.56 ? 305 GLN B CA    1 
ATOM   5027 C C     . GLN B 1 314 ? 40.510 -9.540  -22.986 1.00 41.48 ? 305 GLN B C     1 
ATOM   5028 O O     . GLN B 1 314 ? 40.695 -10.662 -23.460 1.00 35.83 ? 305 GLN B O     1 
ATOM   5029 C CB    . GLN B 1 314 ? 39.478 -10.522 -20.905 1.00 37.61 ? 305 GLN B CB    1 
ATOM   5030 C CG    . GLN B 1 314 ? 38.086 -10.839 -20.364 1.00 41.38 ? 305 GLN B CG    1 
ATOM   5031 C CD    . GLN B 1 314 ? 38.075 -11.999 -19.373 1.00 41.81 ? 305 GLN B CD    1 
ATOM   5032 O OE1   . GLN B 1 314 ? 38.989 -12.826 -19.348 1.00 39.55 ? 305 GLN B OE1   1 
ATOM   5033 N NE2   . GLN B 1 314 ? 37.028 -12.068 -18.558 1.00 41.32 ? 305 GLN B NE2   1 
ATOM   5034 N N     . GLY B 1 315 ? 41.139 -8.465  -23.445 1.00 35.46 ? 306 GLY B N     1 
ATOM   5035 C CA    . GLY B 1 315 ? 42.105 -8.585  -24.521 1.00 29.10 ? 306 GLY B CA    1 
ATOM   5036 C C     . GLY B 1 315 ? 42.275 -7.262  -25.248 1.00 34.68 ? 306 GLY B C     1 
ATOM   5037 O O     . GLY B 1 315 ? 41.867 -6.210  -24.759 1.00 34.99 ? 306 GLY B O     1 
ATOM   5038 N N     . THR B 1 316 ? 42.881 -7.357  -26.429 1.00 32.37 ? 307 THR B N     1 
ATOM   5039 C CA    . THR B 1 316 ? 43.240 -6.182  -27.212 1.00 37.45 ? 307 THR B CA    1 
ATOM   5040 C C     . THR B 1 316 ? 42.027 -5.623  -27.947 1.00 32.92 ? 307 THR B C     1 
ATOM   5041 O O     . THR B 1 316 ? 41.248 -6.366  -28.549 1.00 32.07 ? 307 THR B O     1 
ATOM   5042 C CB    . THR B 1 316 ? 44.343 -6.534  -28.210 1.00 33.62 ? 307 THR B CB    1 
ATOM   5043 O OG1   . THR B 1 316 ? 45.526 -6.913  -27.496 1.00 34.72 ? 307 THR B OG1   1 
ATOM   5044 C CG2   . THR B 1 316 ? 44.659 -5.350  -29.115 1.00 33.47 ? 307 THR B CG2   1 
ATOM   5045 N N     . PHE B 1 317 ? 41.880 -4.302  -27.899 1.00 30.24 ? 308 PHE B N     1 
ATOM   5046 C CA    . PHE B 1 317 ? 40.750 -3.602  -28.490 1.00 30.95 ? 308 PHE B CA    1 
ATOM   5047 C C     . PHE B 1 317 ? 41.248 -2.668  -29.584 1.00 35.22 ? 308 PHE B C     1 
ATOM   5048 O O     . PHE B 1 317 ? 42.190 -1.898  -29.367 1.00 35.30 ? 308 PHE B O     1 
ATOM   5049 C CB    . PHE B 1 317 ? 39.991 -2.817  -27.419 1.00 30.01 ? 308 PHE B CB    1 
ATOM   5050 C CG    . PHE B 1 317 ? 38.649 -2.313  -27.863 1.00 27.32 ? 308 PHE B CG    1 
ATOM   5051 C CD1   . PHE B 1 317 ? 37.541 -3.142  -27.844 1.00 23.25 ? 308 PHE B CD1   1 
ATOM   5052 C CD2   . PHE B 1 317 ? 38.492 -1.001  -28.280 1.00 28.67 ? 308 PHE B CD2   1 
ATOM   5053 C CE1   . PHE B 1 317 ? 36.303 -2.677  -28.241 1.00 23.60 ? 308 PHE B CE1   1 
ATOM   5054 C CE2   . PHE B 1 317 ? 37.259 -0.531  -28.682 1.00 33.57 ? 308 PHE B CE2   1 
ATOM   5055 C CZ    . PHE B 1 317 ? 36.161 -1.369  -28.661 1.00 29.84 ? 308 PHE B CZ    1 
ATOM   5056 N N     . ILE B 1 318 ? 40.618 -2.738  -30.754 1.00 32.17 ? 309 ILE B N     1 
ATOM   5057 C CA    . ILE B 1 318 ? 40.926 -1.854  -31.874 1.00 30.88 ? 309 ILE B CA    1 
ATOM   5058 C C     . ILE B 1 318 ? 39.681 -1.036  -32.178 1.00 29.13 ? 309 ILE B C     1 
ATOM   5059 O O     . ILE B 1 318 ? 38.621 -1.599  -32.482 1.00 31.59 ? 309 ILE B O     1 
ATOM   5060 C CB    . ILE B 1 318 ? 41.380 -2.633  -33.118 1.00 31.06 ? 309 ILE B CB    1 
ATOM   5061 C CG1   . ILE B 1 318 ? 42.471 -3.643  -32.751 1.00 37.14 ? 309 ILE B CG1   1 
ATOM   5062 C CG2   . ILE B 1 318 ? 41.875 -1.670  -34.192 1.00 35.94 ? 309 ILE B CG2   1 
ATOM   5063 C CD1   . ILE B 1 318 ? 43.248 -4.169  -33.945 1.00 37.69 ? 309 ILE B CD1   1 
ATOM   5064 N N     . CYS B 1 319 ? 39.804 0.285   -32.096 1.00 33.27 ? 310 CYS B N     1 
ATOM   5065 C CA    . CYS B 1 319 ? 38.713 1.188   -32.425 1.00 34.54 ? 310 CYS B CA    1 
ATOM   5066 C C     . CYS B 1 319 ? 38.856 1.681   -33.860 1.00 33.25 ? 310 CYS B C     1 
ATOM   5067 O O     . CYS B 1 319 ? 39.966 1.839   -34.373 1.00 32.63 ? 310 CYS B O     1 
ATOM   5068 C CB    . CYS B 1 319 ? 38.677 2.380   -31.466 1.00 37.34 ? 310 CYS B CB    1 
ATOM   5069 S SG    . CYS B 1 319 ? 40.161 3.400   -31.506 1.00 43.32 ? 310 CYS B SG    1 
ATOM   5070 N N     . SER B 1 320 ? 37.715 1.925   -34.505 1.00 35.12 ? 311 SER B N     1 
ATOM   5071 C CA    . SER B 1 320 ? 37.707 2.323   -35.904 1.00 30.72 ? 311 SER B CA    1 
ATOM   5072 C C     . SER B 1 320 ? 36.503 3.211   -36.179 1.00 34.21 ? 311 SER B C     1 
ATOM   5073 O O     . SER B 1 320 ? 35.450 3.068   -35.551 1.00 33.93 ? 311 SER B O     1 
ATOM   5074 C CB    . SER B 1 320 ? 37.673 1.107   -36.835 1.00 34.98 ? 311 SER B CB    1 
ATOM   5075 O OG    . SER B 1 320 ? 37.621 1.505   -38.197 1.00 39.14 ? 311 SER B OG    1 
ATOM   5076 N N     . GLY B 1 321 ? 36.668 4.122   -37.133 1.00 35.68 ? 312 GLY B N     1 
ATOM   5077 C CA    . GLY B 1 321 ? 35.572 4.965   -37.563 1.00 38.94 ? 312 GLY B CA    1 
ATOM   5078 C C     . GLY B 1 321 ? 35.799 6.441   -37.314 1.00 42.27 ? 312 GLY B C     1 
ATOM   5079 O O     . GLY B 1 321 ? 35.627 6.918   -36.190 1.00 34.25 ? 312 GLY B O     1 
ATOM   5080 N N     . GLY B 1 322 ? 36.190 7.169   -38.358 1.00 37.45 ? 313 GLY B N     1 
ATOM   5081 C CA    . GLY B 1 322 ? 36.321 8.611   -38.268 1.00 41.02 ? 313 GLY B CA    1 
ATOM   5082 C C     . GLY B 1 322 ? 37.400 9.102   -37.331 1.00 44.72 ? 313 GLY B C     1 
ATOM   5083 O O     . GLY B 1 322 ? 37.279 10.201  -36.782 1.00 42.10 ? 313 GLY B O     1 
ATOM   5084 N N     . TYR B 1 323 ? 38.459 8.325   -37.136 1.00 41.15 ? 314 TYR B N     1 
ATOM   5085 C CA    . TYR B 1 323 ? 39.517 8.711   -36.216 1.00 44.56 ? 314 TYR B CA    1 
ATOM   5086 C C     . TYR B 1 323 ? 40.544 9.585   -36.921 1.00 44.38 ? 314 TYR B C     1 
ATOM   5087 O O     . TYR B 1 323 ? 40.838 9.397   -38.104 1.00 46.59 ? 314 TYR B O     1 
ATOM   5088 C CB    . TYR B 1 323 ? 40.191 7.478   -35.614 1.00 40.83 ? 314 TYR B CB    1 
ATOM   5089 C CG    . TYR B 1 323 ? 39.453 6.942   -34.412 1.00 38.03 ? 314 TYR B CG    1 
ATOM   5090 C CD1   . TYR B 1 323 ? 39.690 7.455   -33.142 1.00 41.17 ? 314 TYR B CD1   1 
ATOM   5091 C CD2   . TYR B 1 323 ? 38.502 5.938   -34.548 1.00 40.66 ? 314 TYR B CD2   1 
ATOM   5092 C CE1   . TYR B 1 323 ? 39.010 6.975   -32.039 1.00 41.99 ? 314 TYR B CE1   1 
ATOM   5093 C CE2   . TYR B 1 323 ? 37.816 5.450   -33.450 1.00 38.96 ? 314 TYR B CE2   1 
ATOM   5094 C CZ    . TYR B 1 323 ? 38.073 5.973   -32.199 1.00 44.34 ? 314 TYR B CZ    1 
ATOM   5095 O OH    . TYR B 1 323 ? 37.392 5.490   -31.105 1.00 36.26 ? 314 TYR B OH    1 
ATOM   5096 N N     . THR B 1 324 ? 41.069 10.555  -36.186 1.00 43.72 ? 315 THR B N     1 
ATOM   5097 C CA    . THR B 1 324 ? 42.098 11.462  -36.665 1.00 42.84 ? 315 THR B CA    1 
ATOM   5098 C C     . THR B 1 324 ? 43.375 11.231  -35.868 1.00 39.21 ? 315 THR B C     1 
ATOM   5099 O O     . THR B 1 324 ? 43.453 10.341  -35.016 1.00 39.24 ? 315 THR B O     1 
ATOM   5100 C CB    . THR B 1 324 ? 41.632 12.916  -36.554 1.00 46.33 ? 315 THR B CB    1 
ATOM   5101 O OG1   . THR B 1 324 ? 41.498 13.272  -35.172 1.00 39.33 ? 315 THR B OG1   1 
ATOM   5102 C CG2   . THR B 1 324 ? 40.292 13.102  -37.251 1.00 45.57 ? 315 THR B CG2   1 
ATOM   5103 N N     . ARG B 1 325 ? 44.390 12.047  -36.153 1.00 38.05 ? 316 ARG B N     1 
ATOM   5104 C CA    . ARG B 1 325 ? 45.621 11.976  -35.375 1.00 42.52 ? 316 ARG B CA    1 
ATOM   5105 C C     . ARG B 1 325 ? 45.358 12.331  -33.917 1.00 43.06 ? 316 ARG B C     1 
ATOM   5106 O O     . ARG B 1 325 ? 45.772 11.607  -33.003 1.00 40.31 ? 316 ARG B O     1 
ATOM   5107 C CB    . ARG B 1 325 ? 46.678 12.903  -35.974 1.00 43.90 ? 316 ARG B CB    1 
ATOM   5108 C CG    . ARG B 1 325 ? 47.830 13.201  -35.034 1.00 39.23 ? 316 ARG B CG    1 
ATOM   5109 C CD    . ARG B 1 325 ? 48.947 13.953  -35.737 1.00 38.44 ? 316 ARG B CD    1 
ATOM   5110 N NE    . ARG B 1 325 ? 50.236 13.715  -35.100 1.00 41.56 ? 316 ARG B NE    1 
ATOM   5111 C CZ    . ARG B 1 325 ? 50.639 14.304  -33.982 1.00 40.73 ? 316 ARG B CZ    1 
ATOM   5112 N NH1   . ARG B 1 325 ? 49.884 15.194  -33.358 1.00 41.82 ? 316 ARG B NH1   1 
ATOM   5113 N NH2   . ARG B 1 325 ? 51.830 13.992  -33.478 1.00 43.68 ? 316 ARG B NH2   1 
ATOM   5114 N N     . GLU B 1 326 ? 44.651 13.440  -33.684 1.00 44.63 ? 317 GLU B N     1 
ATOM   5115 C CA    . GLU B 1 326 ? 44.347 13.858  -32.320 1.00 40.42 ? 317 GLU B CA    1 
ATOM   5116 C C     . GLU B 1 326 ? 43.363 12.904  -31.653 1.00 39.82 ? 317 GLU B C     1 
ATOM   5117 O O     . GLU B 1 326 ? 43.552 12.526  -30.491 1.00 43.07 ? 317 GLU B O     1 
ATOM   5118 C CB    . GLU B 1 326 ? 43.795 15.284  -32.322 1.00 48.92 ? 317 GLU B CB    1 
ATOM   5119 N N     . LEU B 1 327 ? 42.305 12.509  -32.367 1.00 41.12 ? 318 LEU B N     1 
ATOM   5120 C CA    . LEU B 1 327 ? 41.349 11.563  -31.799 1.00 44.31 ? 318 LEU B CA    1 
ATOM   5121 C C     . LEU B 1 327 ? 42.005 10.216  -31.530 1.00 41.93 ? 318 LEU B C     1 
ATOM   5122 O O     . LEU B 1 327 ? 41.694 9.552   -30.534 1.00 45.05 ? 318 LEU B O     1 
ATOM   5123 C CB    . LEU B 1 327 ? 40.149 11.399  -32.732 1.00 39.15 ? 318 LEU B CB    1 
ATOM   5124 C CG    . LEU B 1 327 ? 39.184 12.583  -32.818 1.00 45.52 ? 318 LEU B CG    1 
ATOM   5125 C CD1   . LEU B 1 327 ? 37.966 12.225  -33.657 1.00 46.17 ? 318 LEU B CD1   1 
ATOM   5126 C CD2   . LEU B 1 327 ? 38.766 13.037  -31.426 1.00 43.24 ? 318 LEU B CD2   1 
ATOM   5127 N N     . GLY B 1 328 ? 42.920 9.798   -32.407 1.00 37.06 ? 319 GLY B N     1 
ATOM   5128 C CA    . GLY B 1 328 ? 43.641 8.559   -32.172 1.00 43.80 ? 319 GLY B CA    1 
ATOM   5129 C C     . GLY B 1 328 ? 44.592 8.657   -30.995 1.00 40.17 ? 319 GLY B C     1 
ATOM   5130 O O     . GLY B 1 328 ? 44.702 7.724   -30.196 1.00 38.75 ? 319 GLY B O     1 
ATOM   5131 N N     . ILE B 1 329 ? 45.299 9.785   -30.877 1.00 42.41 ? 320 ILE B N     1 
ATOM   5132 C CA    . ILE B 1 329 ? 46.137 10.012  -29.703 1.00 44.13 ? 320 ILE B CA    1 
ATOM   5133 C C     . ILE B 1 329 ? 45.288 9.973   -28.440 1.00 43.15 ? 320 ILE B C     1 
ATOM   5134 O O     . ILE B 1 329 ? 45.649 9.330   -27.447 1.00 39.22 ? 320 ILE B O     1 
ATOM   5135 C CB    . ILE B 1 329 ? 46.897 11.346  -29.836 1.00 46.11 ? 320 ILE B CB    1 
ATOM   5136 C CG1   . ILE B 1 329 ? 48.133 11.171  -30.717 1.00 38.68 ? 320 ILE B CG1   1 
ATOM   5137 C CG2   . ILE B 1 329 ? 47.300 11.880  -28.463 1.00 38.62 ? 320 ILE B CG2   1 
ATOM   5138 C CD1   . ILE B 1 329 ? 48.609 12.457  -31.356 1.00 45.21 ? 320 ILE B CD1   1 
ATOM   5139 N N     . GLU B 1 330 ? 44.133 10.644  -28.468 1.00 47.27 ? 321 GLU B N     1 
ATOM   5140 C CA    . GLU B 1 330 ? 43.214 10.630  -27.336 1.00 50.01 ? 321 GLU B CA    1 
ATOM   5141 C C     . GLU B 1 330 ? 42.522 9.286   -27.152 1.00 47.90 ? 321 GLU B C     1 
ATOM   5142 O O     . GLU B 1 330 ? 41.885 9.079   -26.112 1.00 47.42 ? 321 GLU B O     1 
ATOM   5143 C CB    . GLU B 1 330 ? 42.159 11.729  -27.489 1.00 47.18 ? 321 GLU B CB    1 
ATOM   5144 C CG    . GLU B 1 330 ? 42.716 13.143  -27.451 1.00 57.12 ? 321 GLU B CG    1 
ATOM   5145 C CD    . GLU B 1 330 ? 43.642 13.379  -26.271 1.00 62.38 ? 321 GLU B CD    1 
ATOM   5146 O OE1   . GLU B 1 330 ? 44.735 13.956  -26.469 1.00 67.72 ? 321 GLU B OE1   1 
ATOM   5147 O OE2   . GLU B 1 330 ? 43.275 12.988  -25.143 1.00 69.59 ? 321 GLU B OE2   1 
ATOM   5148 N N     . ALA B 1 331 ? 42.646 8.364   -28.108 1.00 45.57 ? 322 ALA B N     1 
ATOM   5149 C CA    . ALA B 1 331 ? 42.097 7.027   -27.921 1.00 39.66 ? 322 ALA B CA    1 
ATOM   5150 C C     . ALA B 1 331 ? 43.049 6.125   -27.144 1.00 41.43 ? 322 ALA B C     1 
ATOM   5151 O O     . ALA B 1 331 ? 42.595 5.260   -26.390 1.00 41.85 ? 322 ALA B O     1 
ATOM   5152 C CB    . ALA B 1 331 ? 41.763 6.396   -29.275 1.00 41.47 ? 322 ALA B CB    1 
ATOM   5153 N N     . VAL B 1 332 ? 44.357 6.329   -27.285 1.00 38.50 ? 323 VAL B N     1 
ATOM   5154 C CA    . VAL B 1 332 ? 45.342 5.474   -26.623 1.00 41.43 ? 323 VAL B CA    1 
ATOM   5155 C C     . VAL B 1 332 ? 45.721 6.013   -25.246 1.00 44.48 ? 323 VAL B C     1 
ATOM   5156 O O     . VAL B 1 332 ? 45.908 5.241   -24.304 1.00 40.34 ? 323 VAL B O     1 
ATOM   5157 C CB    . VAL B 1 332 ? 46.581 5.312   -27.529 1.00 38.80 ? 323 VAL B CB    1 
ATOM   5158 C CG1   . VAL B 1 332 ? 47.749 4.716   -26.758 1.00 35.29 ? 323 VAL B CG1   1 
ATOM   5159 C CG2   . VAL B 1 332 ? 46.247 4.446   -28.740 1.00 36.01 ? 323 VAL B CG2   1 
ATOM   5160 N N     . ALA B 1 333 ? 45.814 7.337   -25.093 1.00 41.44 ? 324 ALA B N     1 
ATOM   5161 C CA    . ALA B 1 333 ? 46.286 7.907   -23.831 1.00 43.30 ? 324 ALA B CA    1 
ATOM   5162 C C     . ALA B 1 333 ? 45.285 7.684   -22.701 1.00 46.73 ? 324 ALA B C     1 
ATOM   5163 O O     . ALA B 1 333 ? 45.670 7.318   -21.585 1.00 49.41 ? 324 ALA B O     1 
ATOM   5164 C CB    . ALA B 1 333 ? 46.571 9.398   -24.005 1.00 39.78 ? 324 ALA B CB    1 
ATOM   5165 N N     . GLN B 1 334 ? 43.996 7.904   -22.970 1.00 49.56 ? 325 GLN B N     1 
ATOM   5166 C CA    . GLN B 1 334 ? 42.944 7.679   -21.987 1.00 48.58 ? 325 GLN B CA    1 
ATOM   5167 C C     . GLN B 1 334 ? 42.627 6.205   -21.783 1.00 47.85 ? 325 GLN B C     1 
ATOM   5168 O O     . GLN B 1 334 ? 41.815 5.879   -20.911 1.00 49.80 ? 325 GLN B O     1 
ATOM   5169 C CB    . GLN B 1 334 ? 41.666 8.411   -22.406 1.00 45.35 ? 325 GLN B CB    1 
ATOM   5170 C CG    . GLN B 1 334 ? 41.853 9.884   -22.719 1.00 49.72 ? 325 GLN B CG    1 
ATOM   5171 C CD    . GLN B 1 334 ? 40.644 10.478  -23.415 1.00 56.24 ? 325 GLN B CD    1 
ATOM   5172 O OE1   . GLN B 1 334 ? 39.690 10.909  -22.769 1.00 67.10 ? 325 GLN B OE1   1 
ATOM   5173 N NE2   . GLN B 1 334 ? 40.678 10.500  -24.743 1.00 62.11 ? 325 GLN B NE2   1 
ATOM   5174 N N     . GLY B 1 335 ? 43.231 5.315   -22.567 1.00 47.59 ? 326 GLY B N     1 
ATOM   5175 C CA    . GLY B 1 335 ? 42.990 3.895   -22.417 1.00 41.20 ? 326 GLY B CA    1 
ATOM   5176 C C     . GLY B 1 335 ? 41.706 3.385   -23.028 1.00 45.42 ? 326 GLY B C     1 
ATOM   5177 O O     . GLY B 1 335 ? 41.267 2.284   -22.682 1.00 45.36 ? 326 GLY B O     1 
ATOM   5178 N N     . ASP B 1 336 ? 41.081 4.149   -23.925 1.00 37.94 ? 327 ASP B N     1 
ATOM   5179 C CA    . ASP B 1 336 ? 39.859 3.694   -24.576 1.00 36.52 ? 327 ASP B CA    1 
ATOM   5180 C C     . ASP B 1 336 ? 40.113 2.646   -25.652 1.00 40.31 ? 327 ASP B C     1 
ATOM   5181 O O     . ASP B 1 336 ? 39.163 1.985   -26.083 1.00 35.11 ? 327 ASP B O     1 
ATOM   5182 C CB    . ASP B 1 336 ? 39.106 4.882   -25.183 1.00 43.87 ? 327 ASP B CB    1 
ATOM   5183 C CG    . ASP B 1 336 ? 38.561 5.827   -24.128 1.00 49.65 ? 327 ASP B CG    1 
ATOM   5184 O OD1   . ASP B 1 336 ? 37.477 6.407   -24.349 1.00 54.83 ? 327 ASP B OD1   1 
ATOM   5185 O OD2   . ASP B 1 336 ? 39.216 5.992   -23.078 1.00 53.56 ? 327 ASP B OD2   1 
ATOM   5186 N N     . ALA B 1 337 ? 41.359 2.480   -26.091 1.00 28.44 ? 328 ALA B N     1 
ATOM   5187 C CA    . ALA B 1 337 ? 41.705 1.445   -27.054 1.00 36.30 ? 328 ALA B CA    1 
ATOM   5188 C C     . ALA B 1 337 ? 43.202 1.188   -26.977 1.00 40.29 ? 328 ALA B C     1 
ATOM   5189 O O     . ALA B 1 337 ? 43.964 2.000   -26.446 1.00 39.20 ? 328 ALA B O     1 
ATOM   5190 C CB    . ALA B 1 337 ? 41.300 1.836   -28.480 1.00 36.33 ? 328 ALA B CB    1 
ATOM   5191 N N     . ASP B 1 338 ? 43.611 0.042   -27.517 1.00 35.63 ? 329 ASP B N     1 
ATOM   5192 C CA    . ASP B 1 338 ? 45.020 -0.313  -27.631 1.00 31.95 ? 329 ASP B CA    1 
ATOM   5193 C C     . ASP B 1 338 ? 45.597 0.016   -28.999 1.00 35.30 ? 329 ASP B C     1 
ATOM   5194 O O     . ASP B 1 338 ? 46.749 0.450   -29.092 1.00 38.26 ? 329 ASP B O     1 
ATOM   5195 C CB    . ASP B 1 338 ? 45.215 -1.803  -27.344 1.00 33.77 ? 329 ASP B CB    1 
ATOM   5196 C CG    . ASP B 1 338 ? 44.645 -2.213  -26.002 1.00 35.72 ? 329 ASP B CG    1 
ATOM   5197 O OD1   . ASP B 1 338 ? 45.187 -1.771  -24.969 1.00 38.11 ? 329 ASP B OD1   1 
ATOM   5198 O OD2   . ASP B 1 338 ? 43.655 -2.975  -25.980 1.00 41.81 ? 329 ASP B OD2   1 
ATOM   5199 N N     . LEU B 1 339 ? 44.823 -0.184  -30.062 1.00 34.27 ? 330 LEU B N     1 
ATOM   5200 C CA    . LEU B 1 339 ? 45.243 0.139   -31.415 1.00 36.28 ? 330 LEU B CA    1 
ATOM   5201 C C     . LEU B 1 339 ? 44.147 0.938   -32.105 1.00 32.11 ? 330 LEU B C     1 
ATOM   5202 O O     . LEU B 1 339 ? 42.966 0.824   -31.767 1.00 34.76 ? 330 LEU B O     1 
ATOM   5203 C CB    . LEU B 1 339 ? 45.569 -1.129  -32.220 1.00 37.83 ? 330 LEU B CB    1 
ATOM   5204 C CG    . LEU B 1 339 ? 46.534 -2.110  -31.547 1.00 38.97 ? 330 LEU B CG    1 
ATOM   5205 C CD1   . LEU B 1 339 ? 46.504 -3.469  -32.231 1.00 39.77 ? 330 LEU B CD1   1 
ATOM   5206 C CD2   . LEU B 1 339 ? 47.945 -1.550  -31.529 1.00 36.25 ? 330 LEU B CD2   1 
ATOM   5207 N N     . VAL B 1 340 ? 44.553 1.759   -33.070 1.00 33.76 ? 331 VAL B N     1 
ATOM   5208 C CA    . VAL B 1 340 ? 43.643 2.624   -33.813 1.00 32.72 ? 331 VAL B CA    1 
ATOM   5209 C C     . VAL B 1 340 ? 43.840 2.350   -35.296 1.00 32.44 ? 331 VAL B C     1 
ATOM   5210 O O     . VAL B 1 340 ? 44.958 2.471   -35.809 1.00 36.16 ? 331 VAL B O     1 
ATOM   5211 C CB    . VAL B 1 340 ? 43.876 4.113   -33.503 1.00 32.68 ? 331 VAL B CB    1 
ATOM   5212 C CG1   . VAL B 1 340 ? 42.820 4.972   -34.189 1.00 33.39 ? 331 VAL B CG1   1 
ATOM   5213 C CG2   . VAL B 1 340 ? 43.868 4.352   -31.999 1.00 33.57 ? 331 VAL B CG2   1 
ATOM   5214 N N     . SER B 1 341 ? 42.765 1.975   -35.981 1.00 26.94 ? 332 SER B N     1 
ATOM   5215 C CA    . SER B 1 341 ? 42.823 1.686   -37.405 1.00 35.16 ? 332 SER B CA    1 
ATOM   5216 C C     . SER B 1 341 ? 42.271 2.866   -38.190 1.00 29.60 ? 332 SER B C     1 
ATOM   5217 O O     . SER B 1 341 ? 41.266 3.470   -37.806 1.00 34.26 ? 332 SER B O     1 
ATOM   5218 C CB    . SER B 1 341 ? 42.057 0.404   -37.745 1.00 25.95 ? 332 SER B CB    1 
ATOM   5219 O OG    . SER B 1 341 ? 40.656 0.600   -37.686 1.00 36.73 ? 332 SER B OG    1 
ATOM   5220 N N     . TYR B 1 342 ? 42.949 3.198   -39.281 1.00 33.08 ? 333 TYR B N     1 
ATOM   5221 C CA    . TYR B 1 342 ? 42.585 4.323   -40.128 1.00 31.27 ? 333 TYR B CA    1 
ATOM   5222 C C     . TYR B 1 342 ? 42.233 3.796   -41.511 1.00 34.97 ? 333 TYR B C     1 
ATOM   5223 O O     . TYR B 1 342 ? 42.983 3.000   -42.081 1.00 32.32 ? 333 TYR B O     1 
ATOM   5224 C CB    . TYR B 1 342 ? 43.722 5.344   -40.217 1.00 28.08 ? 333 TYR B CB    1 
ATOM   5225 C CG    . TYR B 1 342 ? 43.979 6.102   -38.931 1.00 36.98 ? 333 TYR B CG    1 
ATOM   5226 C CD1   . TYR B 1 342 ? 44.853 5.602   -37.973 1.00 38.55 ? 333 TYR B CD1   1 
ATOM   5227 C CD2   . TYR B 1 342 ? 43.353 7.318   -38.676 1.00 34.41 ? 333 TYR B CD2   1 
ATOM   5228 C CE1   . TYR B 1 342 ? 45.096 6.286   -36.800 1.00 38.39 ? 333 TYR B CE1   1 
ATOM   5229 C CE2   . TYR B 1 342 ? 43.591 8.013   -37.499 1.00 37.96 ? 333 TYR B CE2   1 
ATOM   5230 C CZ    . TYR B 1 342 ? 44.463 7.490   -36.566 1.00 40.91 ? 333 TYR B CZ    1 
ATOM   5231 O OH    . TYR B 1 342 ? 44.705 8.172   -35.397 1.00 35.74 ? 333 TYR B OH    1 
ATOM   5232 N N     . GLY B 1 343 ? 41.106 4.244   -42.049 1.00 31.30 ? 334 GLY B N     1 
ATOM   5233 C CA    . GLY B 1 343 ? 40.601 3.856   -43.349 1.00 32.26 ? 334 GLY B CA    1 
ATOM   5234 C C     . GLY B 1 343 ? 40.931 4.912   -44.378 1.00 32.94 ? 334 GLY B C     1 
ATOM   5235 O O     . GLY B 1 343 ? 42.059 4.958   -44.910 1.00 32.25 ? 334 GLY B O     1 
ATOM   5236 N N     . ARG B 1 344 ? 39.973 5.801   -44.678 1.00 32.84 ? 335 ARG B N     1 
ATOM   5237 C CA    . ARG B 1 344 ? 40.091 6.691   -45.829 1.00 39.12 ? 335 ARG B CA    1 
ATOM   5238 C C     . ARG B 1 344 ? 41.397 7.482   -45.838 1.00 33.59 ? 335 ARG B C     1 
ATOM   5239 O O     . ARG B 1 344 ? 41.952 7.750   -46.912 1.00 34.64 ? 335 ARG B O     1 
ATOM   5240 C CB    . ARG B 1 344 ? 38.895 7.638   -45.874 1.00 40.07 ? 335 ARG B CB    1 
ATOM   5241 C CG    . ARG B 1 344 ? 37.599 6.946   -46.275 1.00 38.65 ? 335 ARG B CG    1 
ATOM   5242 C CD    . ARG B 1 344 ? 36.381 7.789   -45.947 1.00 35.70 ? 335 ARG B CD    1 
ATOM   5243 N NE    . ARG B 1 344 ? 36.120 7.844   -44.513 1.00 39.84 ? 335 ARG B NE    1 
ATOM   5244 C CZ    . ARG B 1 344 ? 35.352 8.754   -43.931 1.00 42.66 ? 335 ARG B CZ    1 
ATOM   5245 N NH1   . ARG B 1 344 ? 34.765 9.712   -44.630 1.00 41.87 ? 335 ARG B NH1   1 
ATOM   5246 N NH2   . ARG B 1 344 ? 35.163 8.699   -42.616 1.00 44.83 ? 335 ARG B NH2   1 
ATOM   5247 N N     . LEU B 1 345 ? 41.914 7.854   -44.665 1.00 25.41 ? 336 LEU B N     1 
ATOM   5248 C CA    . LEU B 1 345 ? 43.164 8.605   -44.626 1.00 28.00 ? 336 LEU B CA    1 
ATOM   5249 C C     . LEU B 1 345 ? 44.358 7.763   -45.057 1.00 34.79 ? 336 LEU B C     1 
ATOM   5250 O O     . LEU B 1 345 ? 45.367 8.322   -45.502 1.00 31.70 ? 336 LEU B O     1 
ATOM   5251 C CB    . LEU B 1 345 ? 43.403 9.171   -43.225 1.00 31.19 ? 336 LEU B CB    1 
ATOM   5252 C CG    . LEU B 1 345 ? 42.681 10.483  -42.916 1.00 34.26 ? 336 LEU B CG    1 
ATOM   5253 C CD1   . LEU B 1 345 ? 42.879 10.881  -41.458 1.00 28.69 ? 336 LEU B CD1   1 
ATOM   5254 C CD2   . LEU B 1 345 ? 43.142 11.596  -43.856 1.00 26.81 ? 336 LEU B CD2   1 
ATOM   5255 N N     . PHE B 1 346 ? 44.268 6.439   -44.933 1.00 31.02 ? 337 PHE B N     1 
ATOM   5256 C CA    . PHE B 1 346 ? 45.320 5.560   -45.425 1.00 32.19 ? 337 PHE B CA    1 
ATOM   5257 C C     . PHE B 1 346 ? 45.256 5.363   -46.934 1.00 33.59 ? 337 PHE B C     1 
ATOM   5258 O O     . PHE B 1 346 ? 46.263 4.974   -47.535 1.00 34.49 ? 337 PHE B O     1 
ATOM   5259 C CB    . PHE B 1 346 ? 45.240 4.202   -44.722 1.00 31.63 ? 337 PHE B CB    1 
ATOM   5260 C CG    . PHE B 1 346 ? 46.479 3.843   -43.950 1.00 28.01 ? 337 PHE B CG    1 
ATOM   5261 C CD1   . PHE B 1 346 ? 47.732 3.978   -44.522 1.00 29.56 ? 337 PHE B CD1   1 
ATOM   5262 C CD2   . PHE B 1 346 ? 46.388 3.365   -42.651 1.00 33.28 ? 337 PHE B CD2   1 
ATOM   5263 C CE1   . PHE B 1 346 ? 48.874 3.643   -43.815 1.00 37.91 ? 337 PHE B CE1   1 
ATOM   5264 C CE2   . PHE B 1 346 ? 47.527 3.028   -41.938 1.00 30.39 ? 337 PHE B CE2   1 
ATOM   5265 C CZ    . PHE B 1 346 ? 48.770 3.167   -42.520 1.00 34.97 ? 337 PHE B CZ    1 
ATOM   5266 N N     . ILE B 1 347 ? 44.100 5.615   -47.555 1.00 29.16 ? 338 ILE B N     1 
ATOM   5267 C CA    . ILE B 1 347 ? 44.008 5.557   -49.013 1.00 40.08 ? 338 ILE B CA    1 
ATOM   5268 C C     . ILE B 1 347 ? 44.911 6.611   -49.639 1.00 34.23 ? 338 ILE B C     1 
ATOM   5269 O O     . ILE B 1 347 ? 45.727 6.315   -50.520 1.00 39.08 ? 338 ILE B O     1 
ATOM   5270 C CB    . ILE B 1 347 ? 42.549 5.734   -49.473 1.00 34.48 ? 338 ILE B CB    1 
ATOM   5271 C CG1   . ILE B 1 347 ? 41.749 4.452   -49.255 1.00 34.23 ? 338 ILE B CG1   1 
ATOM   5272 C CG2   . ILE B 1 347 ? 42.495 6.141   -50.943 1.00 33.95 ? 338 ILE B CG2   1 
ATOM   5273 C CD1   . ILE B 1 347 ? 40.305 4.549   -49.703 1.00 34.35 ? 338 ILE B CD1   1 
ATOM   5274 N N     . SER B 1 348 ? 44.785 7.857   -49.180 1.00 31.03 ? 339 SER B N     1 
ATOM   5275 C CA    . SER B 1 348 ? 45.464 8.986   -49.800 1.00 34.35 ? 339 SER B CA    1 
ATOM   5276 C C     . SER B 1 348 ? 46.832 9.278   -49.200 1.00 37.95 ? 339 SER B C     1 
ATOM   5277 O O     . SER B 1 348 ? 47.612 10.020  -49.807 1.00 34.38 ? 339 SER B O     1 
ATOM   5278 C CB    . SER B 1 348 ? 44.597 10.241  -49.692 1.00 34.45 ? 339 SER B CB    1 
ATOM   5279 O OG    . SER B 1 348 ? 44.291 10.520  -48.339 1.00 37.51 ? 339 SER B OG    1 
ATOM   5280 N N     . ASN B 1 349 ? 47.141 8.729   -48.026 1.00 31.06 ? 340 ASN B N     1 
ATOM   5281 C CA    . ASN B 1 349 ? 48.439 8.920   -47.381 1.00 32.38 ? 340 ASN B CA    1 
ATOM   5282 C C     . ASN B 1 349 ? 49.078 7.552   -47.192 1.00 35.19 ? 340 ASN B C     1 
ATOM   5283 O O     . ASN B 1 349 ? 48.884 6.904   -46.151 1.00 36.65 ? 340 ASN B O     1 
ATOM   5284 C CB    . ASN B 1 349 ? 48.292 9.654   -46.051 1.00 30.07 ? 340 ASN B CB    1 
ATOM   5285 C CG    . ASN B 1 349 ? 47.579 10.982  -46.196 1.00 32.97 ? 340 ASN B CG    1 
ATOM   5286 O OD1   . ASN B 1 349 ? 48.216 12.029  -46.321 1.00 31.47 ? 340 ASN B OD1   1 
ATOM   5287 N ND2   . ASN B 1 349 ? 46.249 10.947  -46.179 1.00 24.44 ? 340 ASN B ND2   1 
ATOM   5288 N N     . PRO B 1 350 ? 49.841 7.069   -48.175 1.00 37.15 ? 341 PRO B N     1 
ATOM   5289 C CA    . PRO B 1 350 ? 50.492 5.760   -48.015 1.00 34.15 ? 341 PRO B CA    1 
ATOM   5290 C C     . PRO B 1 350 ? 51.478 5.728   -46.866 1.00 40.47 ? 341 PRO B C     1 
ATOM   5291 O O     . PRO B 1 350 ? 51.660 4.676   -46.239 1.00 38.19 ? 341 PRO B O     1 
ATOM   5292 C CB    . PRO B 1 350 ? 51.189 5.547   -49.366 1.00 32.89 ? 341 PRO B CB    1 
ATOM   5293 C CG    . PRO B 1 350 ? 51.371 6.930   -49.922 1.00 36.94 ? 341 PRO B CG    1 
ATOM   5294 C CD    . PRO B 1 350 ? 50.187 7.717   -49.453 1.00 36.58 ? 341 PRO B CD    1 
ATOM   5295 N N     . ASP B 1 351 ? 52.123 6.849   -46.570 1.00 33.50 ? 342 ASP B N     1 
ATOM   5296 C CA    . ASP B 1 351 ? 52.990 6.967   -45.399 1.00 41.61 ? 342 ASP B CA    1 
ATOM   5297 C C     . ASP B 1 351 ? 52.254 7.639   -44.247 1.00 37.14 ? 342 ASP B C     1 
ATOM   5298 O O     . ASP B 1 351 ? 52.778 8.536   -43.587 1.00 41.61 ? 342 ASP B O     1 
ATOM   5299 C CB    . ASP B 1 351 ? 54.258 7.729   -45.762 1.00 41.08 ? 342 ASP B CB    1 
ATOM   5300 C CG    . ASP B 1 351 ? 53.967 9.069   -46.406 1.00 40.17 ? 342 ASP B CG    1 
ATOM   5301 O OD1   . ASP B 1 351 ? 52.786 9.352   -46.700 1.00 38.02 ? 342 ASP B OD1   1 
ATOM   5302 O OD2   . ASP B 1 351 ? 54.924 9.841   -46.615 1.00 40.71 ? 342 ASP B OD2   1 
ATOM   5303 N N     . LEU B 1 352 ? 51.012 7.203   -44.009 1.00 30.89 ? 343 LEU B N     1 
ATOM   5304 C CA    . LEU B 1 352 ? 50.189 7.813   -42.969 1.00 35.81 ? 343 LEU B CA    1 
ATOM   5305 C C     . LEU B 1 352 ? 50.843 7.690   -41.599 1.00 38.57 ? 343 LEU B C     1 
ATOM   5306 O O     . LEU B 1 352 ? 50.737 8.602   -40.771 1.00 36.32 ? 343 LEU B O     1 
ATOM   5307 C CB    . LEU B 1 352 ? 48.801 7.172   -42.956 1.00 34.45 ? 343 LEU B CB    1 
ATOM   5308 C CG    . LEU B 1 352 ? 47.823 7.704   -41.907 1.00 35.94 ? 343 LEU B CG    1 
ATOM   5309 C CD1   . LEU B 1 352 ? 47.677 9.215   -42.022 1.00 29.95 ? 343 LEU B CD1   1 
ATOM   5310 C CD2   . LEU B 1 352 ? 46.470 7.018   -42.029 1.00 35.16 ? 343 LEU B CD2   1 
ATOM   5311 N N     . VAL B 1 353 ? 51.527 6.573   -41.344 1.00 41.36 ? 344 VAL B N     1 
ATOM   5312 C CA    . VAL B 1 353 ? 52.178 6.376   -40.051 1.00 39.68 ? 344 VAL B CA    1 
ATOM   5313 C C     . VAL B 1 353 ? 53.269 7.417   -39.837 1.00 42.86 ? 344 VAL B C     1 
ATOM   5314 O O     . VAL B 1 353 ? 53.406 7.980   -38.743 1.00 40.48 ? 344 VAL B O     1 
ATOM   5315 C CB    . VAL B 1 353 ? 52.733 4.944   -39.945 1.00 38.57 ? 344 VAL B CB    1 
ATOM   5316 C CG1   . VAL B 1 353 ? 53.411 4.737   -38.597 1.00 38.52 ? 344 VAL B CG1   1 
ATOM   5317 C CG2   . VAL B 1 353 ? 51.620 3.926   -40.151 1.00 35.06 ? 344 VAL B CG2   1 
ATOM   5318 N N     . MET B 1 354 ? 54.064 7.693   -40.874 1.00 39.24 ? 345 MET B N     1 
ATOM   5319 C CA    . MET B 1 354 ? 55.115 8.695   -40.739 1.00 41.55 ? 345 MET B CA    1 
ATOM   5320 C C     . MET B 1 354 ? 54.537 10.102  -40.643 1.00 43.36 ? 345 MET B C     1 
ATOM   5321 O O     . MET B 1 354 ? 55.089 10.952  -39.934 1.00 36.63 ? 345 MET B O     1 
ATOM   5322 C CB    . MET B 1 354 ? 56.092 8.591   -41.912 1.00 47.23 ? 345 MET B CB    1 
ATOM   5323 C CG    . MET B 1 354 ? 57.184 9.652   -41.919 1.00 59.81 ? 345 MET B CG    1 
ATOM   5324 S SD    . MET B 1 354 ? 58.342 9.503   -40.539 1.00 65.82 ? 345 MET B SD    1 
ATOM   5325 C CE    . MET B 1 354 ? 58.103 7.795   -40.056 1.00 55.41 ? 345 MET B CE    1 
ATOM   5326 N N     . ARG B 1 355 ? 53.427 10.363  -41.339 1.00 40.37 ? 346 ARG B N     1 
ATOM   5327 C CA    . ARG B 1 355 ? 52.789 11.674  -41.255 1.00 39.59 ? 346 ARG B CA    1 
ATOM   5328 C C     . ARG B 1 355 ? 52.255 11.939  -39.854 1.00 42.26 ? 346 ARG B C     1 
ATOM   5329 O O     . ARG B 1 355 ? 52.362 13.061  -39.344 1.00 39.21 ? 346 ARG B O     1 
ATOM   5330 C CB    . ARG B 1 355 ? 51.669 11.776  -42.290 1.00 36.83 ? 346 ARG B CB    1 
ATOM   5331 C CG    . ARG B 1 355 ? 52.156 11.637  -43.723 1.00 40.60 ? 346 ARG B CG    1 
ATOM   5332 C CD    . ARG B 1 355 ? 51.153 12.187  -44.719 1.00 35.45 ? 346 ARG B CD    1 
ATOM   5333 N NE    . ARG B 1 355 ? 51.587 11.955  -46.091 1.00 38.39 ? 346 ARG B NE    1 
ATOM   5334 C CZ    . ARG B 1 355 ? 51.428 12.816  -47.086 1.00 42.00 ? 346 ARG B CZ    1 
ATOM   5335 N NH1   . ARG B 1 355 ? 50.844 13.990  -46.899 1.00 40.36 ? 346 ARG B NH1   1 
ATOM   5336 N NH2   . ARG B 1 355 ? 51.863 12.492  -48.299 1.00 39.55 ? 346 ARG B NH2   1 
ATOM   5337 N N     . ILE B 1 356 ? 51.672 10.920  -39.220 1.00 40.72 ? 347 ILE B N     1 
ATOM   5338 C CA    . ILE B 1 356 ? 51.216 11.067  -37.841 1.00 41.46 ? 347 ILE B CA    1 
ATOM   5339 C C     . ILE B 1 356 ? 52.403 11.299  -36.912 1.00 39.09 ? 347 ILE B C     1 
ATOM   5340 O O     . ILE B 1 356 ? 52.324 12.093  -35.966 1.00 43.35 ? 347 ILE B O     1 
ATOM   5341 C CB    . ILE B 1 356 ? 50.392 9.834   -37.425 1.00 39.15 ? 347 ILE B CB    1 
ATOM   5342 C CG1   . ILE B 1 356 ? 49.093 9.775   -38.230 1.00 36.87 ? 347 ILE B CG1   1 
ATOM   5343 C CG2   . ILE B 1 356 ? 50.095 9.854   -35.934 1.00 40.03 ? 347 ILE B CG2   1 
ATOM   5344 C CD1   . ILE B 1 356 ? 48.336 8.476   -38.076 1.00 33.63 ? 347 ILE B CD1   1 
ATOM   5345 N N     . LYS B 1 357 ? 53.525 10.626  -37.178 1.00 41.35 ? 348 LYS B N     1 
ATOM   5346 C CA    . LYS B 1 357 ? 54.712 10.780  -36.340 1.00 45.35 ? 348 LYS B CA    1 
ATOM   5347 C C     . LYS B 1 357 ? 55.217 12.218  -36.351 1.00 44.70 ? 348 LYS B C     1 
ATOM   5348 O O     . LYS B 1 357 ? 55.491 12.801  -35.296 1.00 42.84 ? 348 LYS B O     1 
ATOM   5349 C CB    . LYS B 1 357 ? 55.811 9.826   -36.811 1.00 44.58 ? 348 LYS B CB    1 
ATOM   5350 C CG    . LYS B 1 357 ? 57.140 10.009  -36.101 1.00 46.45 ? 348 LYS B CG    1 
ATOM   5351 C CD    . LYS B 1 357 ? 57.874 8.685   -35.962 1.00 53.68 ? 348 LYS B CD    1 
ATOM   5352 C CE    . LYS B 1 357 ? 58.509 8.554   -34.587 1.00 61.36 ? 348 LYS B CE    1 
ATOM   5353 N NZ    . LYS B 1 357 ? 57.508 8.742   -33.502 1.00 59.04 ? 348 LYS B NZ    1 
ATOM   5354 N N     . LEU B 1 358 ? 55.347 12.806  -37.538 1.00 43.12 ? 349 LEU B N     1 
ATOM   5355 C CA    . LEU B 1 358 ? 55.882 14.152  -37.690 1.00 45.92 ? 349 LEU B CA    1 
ATOM   5356 C C     . LEU B 1 358 ? 54.811 15.234  -37.638 1.00 40.91 ? 349 LEU B C     1 
ATOM   5357 O O     . LEU B 1 358 ? 55.146 16.416  -37.764 1.00 42.14 ? 349 LEU B O     1 
ATOM   5358 C CB    . LEU B 1 358 ? 56.651 14.266  -39.011 1.00 40.81 ? 349 LEU B CB    1 
ATOM   5359 C CG    . LEU B 1 358 ? 57.687 13.178  -39.293 1.00 39.26 ? 349 LEU B CG    1 
ATOM   5360 C CD1   . LEU B 1 358 ? 57.956 13.066  -40.785 1.00 33.79 ? 349 LEU B CD1   1 
ATOM   5361 C CD2   . LEU B 1 358 ? 58.971 13.465  -38.536 1.00 38.64 ? 349 LEU B CD2   1 
ATOM   5362 N N     . ASN B 1 359 ? 53.543 14.859  -37.454 1.00 39.85 ? 350 ASN B N     1 
ATOM   5363 C CA    . ASN B 1 359 ? 52.419 15.795  -37.532 1.00 38.48 ? 350 ASN B CA    1 
ATOM   5364 C C     . ASN B 1 359 ? 52.426 16.550  -38.860 1.00 43.36 ? 350 ASN B C     1 
ATOM   5365 O O     . ASN B 1 359 ? 52.105 17.739  -38.931 1.00 41.90 ? 350 ASN B O     1 
ATOM   5366 C CB    . ASN B 1 359 ? 52.414 16.767  -36.350 1.00 41.28 ? 350 ASN B CB    1 
ATOM   5367 C CG    . ASN B 1 359 ? 51.061 17.423  -36.144 1.00 43.18 ? 350 ASN B CG    1 
ATOM   5368 O OD1   . ASN B 1 359 ? 50.029 16.878  -36.538 1.00 43.07 ? 350 ASN B OD1   1 
ATOM   5369 N ND2   . ASN B 1 359 ? 51.059 18.604  -35.536 1.00 45.29 ? 350 ASN B ND2   1 
ATOM   5370 N N     . ALA B 1 360 ? 52.801 15.848  -39.925 1.00 38.21 ? 351 ALA B N     1 
ATOM   5371 C CA    . ALA B 1 360 ? 52.811 16.441  -41.249 1.00 44.30 ? 351 ALA B CA    1 
ATOM   5372 C C     . ALA B 1 360 ? 51.389 16.530  -41.801 1.00 45.42 ? 351 ALA B C     1 
ATOM   5373 O O     . ALA B 1 360 ? 50.531 15.710  -41.460 1.00 43.78 ? 351 ALA B O     1 
ATOM   5374 C CB    . ALA B 1 360 ? 53.685 15.621  -42.192 1.00 38.56 ? 351 ALA B CB    1 
ATOM   5375 N N     . PRO B 1 361 ? 51.111 17.526  -42.642 1.00 42.76 ? 352 PRO B N     1 
ATOM   5376 C CA    . PRO B 1 361 ? 49.764 17.652  -43.211 1.00 40.09 ? 352 PRO B CA    1 
ATOM   5377 C C     . PRO B 1 361 ? 49.380 16.416  -44.012 1.00 39.98 ? 352 PRO B C     1 
ATOM   5378 O O     . PRO B 1 361 ? 50.216 15.788  -44.663 1.00 39.86 ? 352 PRO B O     1 
ATOM   5379 C CB    . PRO B 1 361 ? 49.869 18.894  -44.104 1.00 44.06 ? 352 PRO B CB    1 
ATOM   5380 C CG    . PRO B 1 361 ? 51.015 19.669  -43.541 1.00 49.41 ? 352 PRO B CG    1 
ATOM   5381 C CD    . PRO B 1 361 ? 51.987 18.642  -43.040 1.00 45.02 ? 352 PRO B CD    1 
ATOM   5382 N N     . LEU B 1 362 ? 48.101 16.064  -43.944 1.00 39.56 ? 353 LEU B N     1 
ATOM   5383 C CA    . LEU B 1 362 ? 47.582 14.915  -44.666 1.00 35.92 ? 353 LEU B CA    1 
ATOM   5384 C C     . LEU B 1 362 ? 46.992 15.355  -45.998 1.00 37.84 ? 353 LEU B C     1 
ATOM   5385 O O     . LEU B 1 362 ? 46.539 16.492  -46.155 1.00 31.74 ? 353 LEU B O     1 
ATOM   5386 C CB    . LEU B 1 362 ? 46.521 14.190  -43.836 1.00 34.61 ? 353 LEU B CB    1 
ATOM   5387 C CG    . LEU B 1 362 ? 46.889 13.899  -42.378 1.00 36.29 ? 353 LEU B CG    1 
ATOM   5388 C CD1   . LEU B 1 362 ? 45.799 13.085  -41.706 1.00 36.78 ? 353 LEU B CD1   1 
ATOM   5389 C CD2   . LEU B 1 362 ? 48.227 13.180  -42.286 1.00 33.75 ? 353 LEU B CD2   1 
ATOM   5390 N N     . ASN B 1 363 ? 47.005 14.442  -46.962 1.00 30.82 ? 354 ASN B N     1 
ATOM   5391 C CA    . ASN B 1 363 ? 46.465 14.701  -48.287 1.00 33.55 ? 354 ASN B CA    1 
ATOM   5392 C C     . ASN B 1 363 ? 45.026 14.209  -48.376 1.00 38.18 ? 354 ASN B C     1 
ATOM   5393 O O     . ASN B 1 363 ? 44.620 13.284  -47.667 1.00 32.28 ? 354 ASN B O     1 
ATOM   5394 C CB    . ASN B 1 363 ? 47.318 14.026  -49.365 1.00 37.64 ? 354 ASN B CB    1 
ATOM   5395 C CG    . ASN B 1 363 ? 48.622 14.758  -49.618 1.00 44.11 ? 354 ASN B CG    1 
ATOM   5396 O OD1   . ASN B 1 363 ? 48.912 15.775  -48.985 1.00 42.03 ? 354 ASN B OD1   1 
ATOM   5397 N ND2   . ASN B 1 363 ? 49.419 14.242  -50.548 1.00 40.97 ? 354 ASN B ND2   1 
ATOM   5398 N N     . LYS B 1 364 ? 44.256 14.844  -49.255 1.00 35.44 ? 355 LYS B N     1 
ATOM   5399 C CA    . LYS B 1 364 ? 42.856 14.494  -49.439 1.00 34.05 ? 355 LYS B CA    1 
ATOM   5400 C C     . LYS B 1 364 ? 42.715 13.230  -50.281 1.00 31.91 ? 355 LYS B C     1 
ATOM   5401 O O     . LYS B 1 364 ? 43.558 12.923  -51.128 1.00 33.53 ? 355 LYS B O     1 
ATOM   5402 C CB    . LYS B 1 364 ? 42.103 15.647  -50.107 1.00 34.80 ? 355 LYS B CB    1 
ATOM   5403 C CG    . LYS B 1 364 ? 42.599 15.968  -51.515 1.00 33.23 ? 355 LYS B CG    1 
ATOM   5404 C CD    . LYS B 1 364 ? 41.908 17.193  -52.094 1.00 36.77 ? 355 LYS B CD    1 
ATOM   5405 C CE    . LYS B 1 364 ? 40.396 17.034  -52.095 1.00 41.47 ? 355 LYS B CE    1 
ATOM   5406 N NZ    . LYS B 1 364 ? 39.700 18.338  -51.888 1.00 50.17 ? 355 LYS B NZ    1 
ATOM   5407 N N     . TYR B 1 365 ? 41.634 12.496  -50.039 1.00 36.54 ? 356 TYR B N     1 
ATOM   5408 C CA    . TYR B 1 365 ? 41.310 11.305  -50.811 1.00 38.64 ? 356 TYR B CA    1 
ATOM   5409 C C     . TYR B 1 365 ? 40.224 11.618  -51.834 1.00 35.58 ? 356 TYR B C     1 
ATOM   5410 O O     . TYR B 1 365 ? 39.456 12.572  -51.691 1.00 35.07 ? 356 TYR B O     1 
ATOM   5411 C CB    . TYR B 1 365 ? 40.859 10.159  -49.898 1.00 34.25 ? 356 TYR B CB    1 
ATOM   5412 C CG    . TYR B 1 365 ? 39.955 10.581  -48.760 1.00 36.79 ? 356 TYR B CG    1 
ATOM   5413 C CD1   . TYR B 1 365 ? 38.602 10.819  -48.969 1.00 43.18 ? 356 TYR B CD1   1 
ATOM   5414 C CD2   . TYR B 1 365 ? 40.456 10.743  -47.476 1.00 33.91 ? 356 TYR B CD2   1 
ATOM   5415 C CE1   . TYR B 1 365 ? 37.774 11.204  -47.930 1.00 39.74 ? 356 TYR B CE1   1 
ATOM   5416 C CE2   . TYR B 1 365 ? 39.638 11.128  -46.431 1.00 37.14 ? 356 TYR B CE2   1 
ATOM   5417 C CZ    . TYR B 1 365 ? 38.298 11.356  -46.662 1.00 43.06 ? 356 TYR B CZ    1 
ATOM   5418 O OH    . TYR B 1 365 ? 37.483 11.739  -45.621 1.00 48.27 ? 356 TYR B OH    1 
ATOM   5419 N N     . ASN B 1 366 ? 40.170 10.793  -52.875 1.00 33.32 ? 357 ASN B N     1 
ATOM   5420 C CA    . ASN B 1 366 ? 39.244 10.987  -53.986 1.00 33.87 ? 357 ASN B CA    1 
ATOM   5421 C C     . ASN B 1 366 ? 38.299 9.795   -54.047 1.00 34.10 ? 357 ASN B C     1 
ATOM   5422 O O     . ASN B 1 366 ? 38.689 8.707   -54.486 1.00 32.59 ? 357 ASN B O     1 
ATOM   5423 C CB    . ASN B 1 366 ? 40.008 11.169  -55.295 1.00 32.54 ? 357 ASN B CB    1 
ATOM   5424 C CG    . ASN B 1 366 ? 40.889 12.403  -55.277 1.00 44.52 ? 357 ASN B CG    1 
ATOM   5425 O OD1   . ASN B 1 366 ? 42.111 12.310  -55.390 1.00 49.77 ? 357 ASN B OD1   1 
ATOM   5426 N ND2   . ASN B 1 366 ? 40.271 13.570  -55.124 1.00 45.65 ? 357 ASN B ND2   1 
ATOM   5427 N N     . ARG B 1 367 ? 37.052 10.013  -53.621 1.00 33.42 ? 358 ARG B N     1 
ATOM   5428 C CA    . ARG B 1 367 ? 36.070 8.940   -53.523 1.00 39.79 ? 358 ARG B CA    1 
ATOM   5429 C C     . ARG B 1 367 ? 35.764 8.292   -54.867 1.00 35.61 ? 358 ARG B C     1 
ATOM   5430 O O     . ARG B 1 367 ? 35.297 7.148   -54.898 1.00 35.35 ? 358 ARG B O     1 
ATOM   5431 C CB    . ARG B 1 367 ? 34.781 9.482   -52.902 1.00 37.91 ? 358 ARG B CB    1 
ATOM   5432 C CG    . ARG B 1 367 ? 33.822 8.416   -52.418 1.00 39.52 ? 358 ARG B CG    1 
ATOM   5433 C CD    . ARG B 1 367 ? 32.990 8.921   -51.256 1.00 49.65 ? 358 ARG B CD    1 
ATOM   5434 N NE    . ARG B 1 367 ? 33.243 8.158   -50.041 1.00 50.02 ? 358 ARG B NE    1 
ATOM   5435 C CZ    . ARG B 1 367 ? 32.709 6.974   -49.777 1.00 52.43 ? 358 ARG B CZ    1 
ATOM   5436 N NH1   . ARG B 1 367 ? 31.886 6.381   -50.627 1.00 53.52 ? 358 ARG B NH1   1 
ATOM   5437 N NH2   . ARG B 1 367 ? 33.012 6.366   -48.633 1.00 56.85 ? 358 ARG B NH2   1 
ATOM   5438 N N     . LYS B 1 368 ? 36.017 8.992   -55.975 1.00 35.20 ? 359 LYS B N     1 
ATOM   5439 C CA    . LYS B 1 368 ? 35.670 8.459   -57.288 1.00 28.03 ? 359 LYS B CA    1 
ATOM   5440 C C     . LYS B 1 368 ? 36.485 7.219   -57.637 1.00 28.58 ? 359 LYS B C     1 
ATOM   5441 O O     . LYS B 1 368 ? 36.005 6.354   -58.378 1.00 33.32 ? 359 LYS B O     1 
ATOM   5442 C CB    . LYS B 1 368 ? 35.863 9.537   -58.356 1.00 30.42 ? 359 LYS B CB    1 
ATOM   5443 N N     . THR B 1 369 ? 37.708 7.110   -57.120 1.00 36.56 ? 360 THR B N     1 
ATOM   5444 C CA    . THR B 1 369 ? 38.597 6.006   -57.455 1.00 29.54 ? 360 THR B CA    1 
ATOM   5445 C C     . THR B 1 369 ? 38.713 4.980   -56.329 1.00 35.98 ? 360 THR B C     1 
ATOM   5446 O O     . THR B 1 369 ? 39.623 4.145   -56.349 1.00 28.48 ? 360 THR B O     1 
ATOM   5447 C CB    . THR B 1 369 ? 39.978 6.542   -57.831 1.00 35.14 ? 360 THR B CB    1 
ATOM   5448 O OG1   . THR B 1 369 ? 40.419 7.470   -56.832 1.00 33.31 ? 360 THR B OG1   1 
ATOM   5449 C CG2   . THR B 1 369 ? 39.923 7.251   -59.186 1.00 32.01 ? 360 THR B CG2   1 
ATOM   5450 N N     . PHE B 1 370 ? 37.802 5.022   -55.353 1.00 29.37 ? 361 PHE B N     1 
ATOM   5451 C CA    . PHE B 1 370 ? 37.831 4.053   -54.259 1.00 34.10 ? 361 PHE B CA    1 
ATOM   5452 C C     . PHE B 1 370 ? 37.613 2.633   -54.773 1.00 31.33 ? 361 PHE B C     1 
ATOM   5453 O O     . PHE B 1 370 ? 38.353 1.710   -54.412 1.00 31.49 ? 361 PHE B O     1 
ATOM   5454 C CB    . PHE B 1 370 ? 36.767 4.403   -53.216 1.00 34.16 ? 361 PHE B CB    1 
ATOM   5455 C CG    . PHE B 1 370 ? 37.181 5.478   -52.248 1.00 37.59 ? 361 PHE B CG    1 
ATOM   5456 C CD1   . PHE B 1 370 ? 38.263 6.300   -52.514 1.00 38.54 ? 361 PHE B CD1   1 
ATOM   5457 C CD2   . PHE B 1 370 ? 36.470 5.677   -51.077 1.00 29.77 ? 361 PHE B CD2   1 
ATOM   5458 C CE1   . PHE B 1 370 ? 38.633 7.293   -51.625 1.00 39.79 ? 361 PHE B CE1   1 
ATOM   5459 C CE2   . PHE B 1 370 ? 36.836 6.669   -50.184 1.00 36.81 ? 361 PHE B CE2   1 
ATOM   5460 C CZ    . PHE B 1 370 ? 37.921 7.477   -50.460 1.00 33.63 ? 361 PHE B CZ    1 
ATOM   5461 N N     . TYR B 1 371 ? 36.594 2.440   -55.614 1.00 31.89 ? 362 TYR B N     1 
ATOM   5462 C CA    . TYR B 1 371 ? 36.163 1.116   -56.050 1.00 34.54 ? 362 TYR B CA    1 
ATOM   5463 C C     . TYR B 1 371 ? 36.416 0.867   -57.536 1.00 40.87 ? 362 TYR B C     1 
ATOM   5464 O O     . TYR B 1 371 ? 35.758 0.010   -58.136 1.00 36.74 ? 362 TYR B O     1 
ATOM   5465 C CB    . TYR B 1 371 ? 34.680 0.917   -55.736 1.00 34.24 ? 362 TYR B CB    1 
ATOM   5466 C CG    . TYR B 1 371 ? 34.296 1.188   -54.298 1.00 32.79 ? 362 TYR B CG    1 
ATOM   5467 C CD1   . TYR B 1 371 ? 34.580 0.269   -53.297 1.00 35.13 ? 362 TYR B CD1   1 
ATOM   5468 C CD2   . TYR B 1 371 ? 33.637 2.358   -53.944 1.00 35.88 ? 362 TYR B CD2   1 
ATOM   5469 C CE1   . TYR B 1 371 ? 34.226 0.509   -51.983 1.00 33.24 ? 362 TYR B CE1   1 
ATOM   5470 C CE2   . TYR B 1 371 ? 33.277 2.608   -52.631 1.00 38.59 ? 362 TYR B CE2   1 
ATOM   5471 C CZ    . TYR B 1 371 ? 33.574 1.680   -51.656 1.00 37.07 ? 362 TYR B CZ    1 
ATOM   5472 O OH    . TYR B 1 371 ? 33.220 1.923   -50.349 1.00 39.47 ? 362 TYR B OH    1 
ATOM   5473 N N     . THR B 1 372 ? 37.350 1.589   -58.143 1.00 31.16 ? 363 THR B N     1 
ATOM   5474 C CA    . THR B 1 372 ? 37.638 1.412   -59.558 1.00 36.64 ? 363 THR B CA    1 
ATOM   5475 C C     . THR B 1 372 ? 38.675 0.310   -59.763 1.00 38.48 ? 363 THR B C     1 
ATOM   5476 O O     . THR B 1 372 ? 39.285 -0.195  -58.818 1.00 31.55 ? 363 THR B O     1 
ATOM   5477 C CB    . THR B 1 372 ? 38.119 2.724   -60.175 1.00 29.09 ? 363 THR B CB    1 
ATOM   5478 O OG1   . THR B 1 372 ? 39.043 3.358   -59.284 1.00 35.93 ? 363 THR B OG1   1 
ATOM   5479 C CG2   . THR B 1 372 ? 36.940 3.655   -60.422 1.00 31.95 ? 363 THR B CG2   1 
ATOM   5480 N N     . GLN B 1 373 ? 38.874 -0.062  -61.028 1.00 35.08 ? 364 GLN B N     1 
ATOM   5481 C CA    . GLN B 1 373 ? 39.715 -1.199  -61.375 1.00 33.42 ? 364 GLN B CA    1 
ATOM   5482 C C     . GLN B 1 373 ? 41.118 -0.807  -61.815 1.00 36.89 ? 364 GLN B C     1 
ATOM   5483 O O     . GLN B 1 373 ? 41.953 -1.697  -62.009 1.00 32.36 ? 364 GLN B O     1 
ATOM   5484 C CB    . GLN B 1 373 ? 39.056 -2.028  -62.486 1.00 31.24 ? 364 GLN B CB    1 
ATOM   5485 C CG    . GLN B 1 373 ? 37.979 -2.984  -61.995 1.00 31.82 ? 364 GLN B CG    1 
ATOM   5486 C CD    . GLN B 1 373 ? 36.762 -2.260  -61.453 1.00 38.66 ? 364 GLN B CD    1 
ATOM   5487 O OE1   . GLN B 1 373 ? 35.959 -1.717  -62.213 1.00 30.78 ? 364 GLN B OE1   1 
ATOM   5488 N NE2   . GLN B 1 373 ? 36.621 -2.244  -60.130 1.00 32.65 ? 364 GLN B NE2   1 
ATOM   5489 N N     . ASP B 1 374 ? 41.399 0.481   -61.979 1.00 37.61 ? 365 ASP B N     1 
ATOM   5490 C CA    . ASP B 1 374 ? 42.714 0.890   -62.448 1.00 33.83 ? 365 ASP B CA    1 
ATOM   5491 C C     . ASP B 1 374 ? 43.775 0.504   -61.421 1.00 37.47 ? 365 ASP B C     1 
ATOM   5492 O O     . ASP B 1 374 ? 43.654 0.868   -60.242 1.00 36.45 ? 365 ASP B O     1 
ATOM   5493 C CB    . ASP B 1 374 ? 42.765 2.392   -62.708 1.00 35.67 ? 365 ASP B CB    1 
ATOM   5494 C CG    . ASP B 1 374 ? 44.015 2.807   -63.464 1.00 46.44 ? 365 ASP B CG    1 
ATOM   5495 O OD1   . ASP B 1 374 ? 43.939 2.987   -64.699 1.00 49.86 ? 365 ASP B OD1   1 
ATOM   5496 O OD2   . ASP B 1 374 ? 45.076 2.953   -62.821 1.00 42.87 ? 365 ASP B OD2   1 
ATOM   5497 N N     . PRO B 1 375 ? 44.825 -0.217  -61.822 1.00 40.81 ? 366 PRO B N     1 
ATOM   5498 C CA    . PRO B 1 375 ? 45.848 -0.639  -60.854 1.00 40.00 ? 366 PRO B CA    1 
ATOM   5499 C C     . PRO B 1 375 ? 46.716 0.494   -60.332 1.00 38.18 ? 366 PRO B C     1 
ATOM   5500 O O     . PRO B 1 375 ? 47.500 0.261   -59.403 1.00 35.95 ? 366 PRO B O     1 
ATOM   5501 C CB    . PRO B 1 375 ? 46.684 -1.648  -61.650 1.00 36.20 ? 366 PRO B CB    1 
ATOM   5502 C CG    . PRO B 1 375 ? 46.506 -1.240  -63.075 1.00 38.77 ? 366 PRO B CG    1 
ATOM   5503 C CD    . PRO B 1 375 ? 45.108 -0.702  -63.184 1.00 39.67 ? 366 PRO B CD    1 
ATOM   5504 N N     . VAL B 1 376 ? 46.613 1.700   -60.887 1.00 39.97 ? 367 VAL B N     1 
ATOM   5505 C CA    . VAL B 1 376 ? 47.494 2.793   -60.492 1.00 40.96 ? 367 VAL B CA    1 
ATOM   5506 C C     . VAL B 1 376 ? 46.682 4.012   -60.074 1.00 41.79 ? 367 VAL B C     1 
ATOM   5507 O O     . VAL B 1 376 ? 46.873 4.548   -58.975 1.00 45.09 ? 367 VAL B O     1 
ATOM   5508 C CB    . VAL B 1 376 ? 48.472 3.150   -61.626 1.00 45.90 ? 367 VAL B CB    1 
ATOM   5509 C CG1   . VAL B 1 376 ? 49.305 4.366   -61.249 1.00 40.32 ? 367 VAL B CG1   1 
ATOM   5510 C CG2   . VAL B 1 376 ? 49.370 1.965   -61.942 1.00 41.21 ? 367 VAL B CG2   1 
ATOM   5511 N N     . VAL B 1 377 ? 45.771 4.454   -60.941 1.00 39.74 ? 368 VAL B N     1 
ATOM   5512 C CA    . VAL B 1 377 ? 45.047 5.704   -60.723 1.00 37.50 ? 368 VAL B CA    1 
ATOM   5513 C C     . VAL B 1 377 ? 44.153 5.572   -59.496 1.00 38.50 ? 368 VAL B C     1 
ATOM   5514 O O     . VAL B 1 377 ? 43.271 4.707   -59.440 1.00 39.02 ? 368 VAL B O     1 
ATOM   5515 C CB    . VAL B 1 377 ? 44.231 6.087   -61.962 1.00 41.00 ? 368 VAL B CB    1 
ATOM   5516 C CG1   . VAL B 1 377 ? 43.360 7.299   -61.667 1.00 40.65 ? 368 VAL B CG1   1 
ATOM   5517 C CG2   . VAL B 1 377 ? 45.156 6.359   -63.140 1.00 35.55 ? 368 VAL B CG2   1 
ATOM   5518 N N     . GLY B 1 378 ? 44.365 6.447   -58.514 1.00 34.11 ? 369 GLY B N     1 
ATOM   5519 C CA    . GLY B 1 378 ? 43.602 6.408   -57.282 1.00 37.26 ? 369 GLY B CA    1 
ATOM   5520 C C     . GLY B 1 378 ? 43.922 5.251   -56.365 1.00 34.13 ? 369 GLY B C     1 
ATOM   5521 O O     . GLY B 1 378 ? 43.207 5.046   -55.380 1.00 35.13 ? 369 GLY B O     1 
ATOM   5522 N N     . TYR B 1 379 ? 44.984 4.496   -56.651 1.00 38.32 ? 370 TYR B N     1 
ATOM   5523 C CA    . TYR B 1 379 ? 45.335 3.305   -55.885 1.00 33.80 ? 370 TYR B CA    1 
ATOM   5524 C C     . TYR B 1 379 ? 46.753 3.383   -55.337 1.00 37.30 ? 370 TYR B C     1 
ATOM   5525 O O     . TYR B 1 379 ? 46.942 3.331   -54.117 1.00 41.17 ? 370 TYR B O     1 
ATOM   5526 C CB    . TYR B 1 379 ? 45.165 2.057   -56.762 1.00 29.54 ? 370 TYR B CB    1 
ATOM   5527 C CG    . TYR B 1 379 ? 45.111 0.748   -56.000 1.00 34.27 ? 370 TYR B CG    1 
ATOM   5528 C CD1   . TYR B 1 379 ? 44.310 0.607   -54.875 1.00 32.51 ? 370 TYR B CD1   1 
ATOM   5529 C CD2   . TYR B 1 379 ? 45.857 -0.349  -56.413 1.00 37.40 ? 370 TYR B CD2   1 
ATOM   5530 C CE1   . TYR B 1 379 ? 44.256 -0.592  -54.179 1.00 31.86 ? 370 TYR B CE1   1 
ATOM   5531 C CE2   . TYR B 1 379 ? 45.811 -1.549  -55.724 1.00 35.67 ? 370 TYR B CE2   1 
ATOM   5532 C CZ    . TYR B 1 379 ? 45.007 -1.665  -54.609 1.00 33.11 ? 370 TYR B CZ    1 
ATOM   5533 O OH    . TYR B 1 379 ? 44.959 -2.858  -53.922 1.00 32.77 ? 370 TYR B OH    1 
ATOM   5534 N N     . THR B 1 380 ? 47.758 3.508   -56.203 1.00 32.64 ? 371 THR B N     1 
ATOM   5535 C CA    . THR B 1 380 ? 49.152 3.575   -55.783 1.00 31.02 ? 371 THR B CA    1 
ATOM   5536 C C     . THR B 1 380 ? 49.833 4.870   -56.211 1.00 37.38 ? 371 THR B C     1 
ATOM   5537 O O     . THR B 1 380 ? 51.044 5.014   -56.006 1.00 43.53 ? 371 THR B O     1 
ATOM   5538 C CB    . THR B 1 380 ? 49.933 2.375   -56.329 1.00 39.61 ? 371 THR B CB    1 
ATOM   5539 O OG1   . THR B 1 380 ? 49.896 2.387   -57.761 1.00 42.29 ? 371 THR B OG1   1 
ATOM   5540 C CG2   . THR B 1 380 ? 49.325 1.071   -55.828 1.00 36.82 ? 371 THR B CG2   1 
ATOM   5541 N N     . ASP B 1 381 ? 49.097 5.815   -56.792 1.00 36.21 ? 372 ASP B N     1 
ATOM   5542 C CA    . ASP B 1 381 ? 49.682 7.062   -57.265 1.00 37.64 ? 372 ASP B CA    1 
ATOM   5543 C C     . ASP B 1 381 ? 49.505 8.214   -56.282 1.00 39.07 ? 372 ASP B C     1 
ATOM   5544 O O     . ASP B 1 381 ? 49.759 9.367   -56.645 1.00 37.78 ? 372 ASP B O     1 
ATOM   5545 C CB    . ASP B 1 381 ? 49.099 7.438   -58.631 1.00 41.15 ? 372 ASP B CB    1 
ATOM   5546 C CG    . ASP B 1 381 ? 47.623 7.772   -58.568 1.00 39.75 ? 372 ASP B CG    1 
ATOM   5547 O OD1   . ASP B 1 381 ? 46.951 7.358   -57.600 1.00 44.46 ? 372 ASP B OD1   1 
ATOM   5548 O OD2   . ASP B 1 381 ? 47.132 8.451   -59.493 1.00 50.24 ? 372 ASP B OD2   1 
ATOM   5549 N N     . TYR B 1 382 ? 49.074 7.937   -55.058 1.00 33.02 ? 373 TYR B N     1 
ATOM   5550 C CA    . TYR B 1 382 ? 49.069 8.965   -54.019 1.00 39.31 ? 373 TYR B CA    1 
ATOM   5551 C C     . TYR B 1 382 ? 50.500 9.197   -53.555 1.00 38.32 ? 373 TYR B C     1 
ATOM   5552 O O     . TYR B 1 382 ? 51.143 8.256   -53.070 1.00 44.83 ? 373 TYR B O     1 
ATOM   5553 C CB    . TYR B 1 382 ? 48.191 8.551   -52.843 1.00 31.26 ? 373 TYR B CB    1 
ATOM   5554 C CG    . TYR B 1 382 ? 46.708 8.719   -53.081 1.00 34.86 ? 373 TYR B CG    1 
ATOM   5555 C CD1   . TYR B 1 382 ? 46.119 9.978   -53.095 1.00 35.63 ? 373 TYR B CD1   1 
ATOM   5556 C CD2   . TYR B 1 382 ? 45.894 7.615   -53.287 1.00 33.03 ? 373 TYR B CD2   1 
ATOM   5557 C CE1   . TYR B 1 382 ? 44.756 10.127  -53.305 1.00 34.60 ? 373 TYR B CE1   1 
ATOM   5558 C CE2   . TYR B 1 382 ? 44.540 7.752   -53.500 1.00 31.11 ? 373 TYR B CE2   1 
ATOM   5559 C CZ    . TYR B 1 382 ? 43.974 9.006   -53.508 1.00 33.07 ? 373 TYR B CZ    1 
ATOM   5560 O OH    . TYR B 1 382 ? 42.621 9.128   -53.721 1.00 36.12 ? 373 TYR B OH    1 
ATOM   5561 N N     . PRO B 1 383 ? 51.037 10.407  -53.679 1.00 37.73 ? 374 PRO B N     1 
ATOM   5562 C CA    . PRO B 1 383 ? 52.466 10.615  -53.418 1.00 41.91 ? 374 PRO B CA    1 
ATOM   5563 C C     . PRO B 1 383 ? 52.824 10.446  -51.948 1.00 45.14 ? 374 PRO B C     1 
ATOM   5564 O O     . PRO B 1 383 ? 51.990 10.573  -51.048 1.00 40.78 ? 374 PRO B O     1 
ATOM   5565 C CB    . PRO B 1 383 ? 52.709 12.058  -53.878 1.00 40.89 ? 374 PRO B CB    1 
ATOM   5566 C CG    . PRO B 1 383 ? 51.529 12.406  -54.735 1.00 39.81 ? 374 PRO B CG    1 
ATOM   5567 C CD    . PRO B 1 383 ? 50.383 11.623  -54.186 1.00 42.73 ? 374 PRO B CD    1 
ATOM   5568 N N     . PHE B 1 384 ? 54.103 10.157  -51.721 1.00 44.90 ? 375 PHE B N     1 
ATOM   5569 C CA    . PHE B 1 384 ? 54.661 10.086  -50.381 1.00 39.47 ? 375 PHE B CA    1 
ATOM   5570 C C     . PHE B 1 384 ? 55.034 11.485  -49.893 1.00 43.81 ? 375 PHE B C     1 
ATOM   5571 O O     . PHE B 1 384 ? 54.953 12.474  -50.627 1.00 41.65 ? 375 PHE B O     1 
ATOM   5572 C CB    . PHE B 1 384 ? 55.878 9.164   -50.359 1.00 42.51 ? 375 PHE B CB    1 
ATOM   5573 C CG    . PHE B 1 384 ? 55.535 7.704   -50.361 1.00 46.86 ? 375 PHE B CG    1 
ATOM   5574 C CD1   . PHE B 1 384 ? 55.283 7.039   -51.551 1.00 40.67 ? 375 PHE B CD1   1 
ATOM   5575 C CD2   . PHE B 1 384 ? 55.466 6.994   -49.173 1.00 39.93 ? 375 PHE B CD2   1 
ATOM   5576 C CE1   . PHE B 1 384 ? 54.968 5.694   -51.556 1.00 36.97 ? 375 PHE B CE1   1 
ATOM   5577 C CE2   . PHE B 1 384 ? 55.151 5.647   -49.171 1.00 39.31 ? 375 PHE B CE2   1 
ATOM   5578 C CZ    . PHE B 1 384 ? 54.902 4.997   -50.363 1.00 41.48 ? 375 PHE B CZ    1 
ATOM   5579 N N     . LEU B 1 385 ? 55.458 11.569  -48.637 1.00 44.42 ? 376 LEU B N     1 
ATOM   5580 C CA    . LEU B 1 385 ? 55.916 12.833  -48.074 1.00 49.01 ? 376 LEU B CA    1 
ATOM   5581 C C     . LEU B 1 385 ? 57.238 13.251  -48.705 1.00 51.90 ? 376 LEU B C     1 
ATOM   5582 O O     . LEU B 1 385 ? 57.260 13.953  -49.715 1.00 54.30 ? 376 LEU B O     1 
ATOM   5583 C CB    . LEU B 1 385 ? 56.067 12.729  -46.555 1.00 46.93 ? 376 LEU B CB    1 
ATOM   5584 C CG    . LEU B 1 385 ? 55.938 14.041  -45.780 1.00 51.78 ? 376 LEU B CG    1 
ATOM   5585 C CD1   . LEU B 1 385 ? 54.477 14.398  -45.564 1.00 42.63 ? 376 LEU B CD1   1 
ATOM   5586 C CD2   . LEU B 1 385 ? 56.671 13.946  -44.453 1.00 47.18 ? 376 LEU B CD2   1 
HETATM 5587 N N1    . FMN C 2 .   ? 22.458 -6.892  -0.028  1.00 30.44 ? 401 FMN A N1    1 
HETATM 5588 C C2    . FMN C 2 .   ? 22.286 -5.525  -0.048  1.00 35.35 ? 401 FMN A C2    1 
HETATM 5589 O O2    . FMN C 2 .   ? 21.993 -4.927  0.989   1.00 33.92 ? 401 FMN A O2    1 
HETATM 5590 N N3    . FMN C 2 .   ? 22.439 -4.828  -1.229  1.00 27.68 ? 401 FMN A N3    1 
HETATM 5591 C C4    . FMN C 2 .   ? 22.766 -5.498  -2.391  1.00 30.89 ? 401 FMN A C4    1 
HETATM 5592 O O4    . FMN C 2 .   ? 22.905 -4.871  -3.438  1.00 33.70 ? 401 FMN A O4    1 
HETATM 5593 C C4A   . FMN C 2 .   ? 22.942 -6.877  -2.373  1.00 33.07 ? 401 FMN A C4A   1 
HETATM 5594 N N5    . FMN C 2 .   ? 23.272 -7.563  -3.522  1.00 32.44 ? 401 FMN A N5    1 
HETATM 5595 C C5A   . FMN C 2 .   ? 23.437 -8.932  -3.493  1.00 33.30 ? 401 FMN A C5A   1 
HETATM 5596 C C6    . FMN C 2 .   ? 23.766 -9.614  -4.659  1.00 33.89 ? 401 FMN A C6    1 
HETATM 5597 C C7    . FMN C 2 .   ? 23.937 -10.994 -4.632  1.00 36.45 ? 401 FMN A C7    1 
HETATM 5598 C C7M   . FMN C 2 .   ? 24.286 -11.722 -5.898  1.00 42.64 ? 401 FMN A C7M   1 
HETATM 5599 C C8    . FMN C 2 .   ? 23.787 -11.691 -3.435  1.00 35.07 ? 401 FMN A C8    1 
HETATM 5600 C C8M   . FMN C 2 .   ? 23.973 -13.177 -3.395  1.00 38.82 ? 401 FMN A C8M   1 
HETATM 5601 C C9    . FMN C 2 .   ? 23.449 -11.009 -2.274  1.00 31.94 ? 401 FMN A C9    1 
HETATM 5602 C C9A   . FMN C 2 .   ? 23.278 -9.627  -2.299  1.00 36.12 ? 401 FMN A C9A   1 
HETATM 5603 N N10   . FMN C 2 .   ? 22.954 -8.937  -1.146  1.00 36.67 ? 401 FMN A N10   1 
HETATM 5604 C C10   . FMN C 2 .   ? 22.786 -7.569  -1.182  1.00 29.68 ? 401 FMN A C10   1 
HETATM 5605 C "C1'" . FMN C 2 .   ? 22.767 -9.658  0.154   1.00 29.83 ? 401 FMN A "C1'" 1 
HETATM 5606 C "C2'" . FMN C 2 .   ? 21.305 -10.101 0.218   1.00 32.49 ? 401 FMN A "C2'" 1 
HETATM 5607 O "O2'" . FMN C 2 .   ? 20.442 -8.997  0.038   1.00 30.25 ? 401 FMN A "O2'" 1 
HETATM 5608 C "C3'" . FMN C 2 .   ? 20.968 -10.788 1.534   1.00 33.78 ? 401 FMN A "C3'" 1 
HETATM 5609 O "O3'" . FMN C 2 .   ? 21.655 -10.174 2.604   1.00 38.76 ? 401 FMN A "O3'" 1 
HETATM 5610 C "C4'" . FMN C 2 .   ? 21.337 -12.261 1.489   1.00 35.93 ? 401 FMN A "C4'" 1 
HETATM 5611 O "O4'" . FMN C 2 .   ? 21.541 -12.675 0.154   1.00 40.28 ? 401 FMN A "O4'" 1 
HETATM 5612 C "C5'" . FMN C 2 .   ? 20.203 -13.073 2.089   1.00 34.75 ? 401 FMN A "C5'" 1 
HETATM 5613 O "O5'" . FMN C 2 .   ? 20.609 -14.411 2.201   1.00 33.05 ? 401 FMN A "O5'" 1 
HETATM 5614 P P     . FMN C 2 .   ? 19.914 -15.513 1.263   1.00 34.47 ? 401 FMN A P     1 
HETATM 5615 O O1P   . FMN C 2 .   ? 20.405 -16.874 1.701   1.00 34.69 ? 401 FMN A O1P   1 
HETATM 5616 O O2P   . FMN C 2 .   ? 20.335 -15.267 -0.164  1.00 28.73 ? 401 FMN A O2P   1 
HETATM 5617 O O3P   . FMN C 2 .   ? 18.410 -15.416 1.371   1.00 35.34 ? 401 FMN A O3P   1 
HETATM 5618 C C4    . 5J8 D 3 .   ? 27.893 -19.783 0.737   0.92 71.02 ? 402 5J8 A C4    1 
HETATM 5619 C C5    . 5J8 D 3 .   ? 27.588 -20.209 1.968   0.92 74.03 ? 402 5J8 A C5    1 
HETATM 5620 C C6    . 5J8 D 3 .   ? 26.906 -19.382 2.832   0.92 73.29 ? 402 5J8 A C6    1 
HETATM 5621 C C8    . 5J8 D 3 .   ? 28.646 -21.808 0.965   0.92 74.22 ? 402 5J8 A C8    1 
HETATM 5622 N N1    . 5J8 D 3 .   ? 26.549 -18.166 2.452   0.92 74.77 ? 402 5J8 A N1    1 
HETATM 5623 N N3    . 5J8 D 3 .   ? 27.527 -18.542 0.357   0.92 64.57 ? 402 5J8 A N3    1 
HETATM 5624 N NBU   . 5J8 D 3 .   ? 25.850 -4.738  -2.401  0.92 32.26 ? 402 5J8 A NBU   1 
HETATM 5625 C CBT   . 5J8 D 3 .   ? 25.878 -5.747  -1.366  0.92 32.22 ? 402 5J8 A CBT   1 
HETATM 5626 O OBV   . 5J8 D 3 .   ? 25.499 -5.497  -0.275  0.92 28.51 ? 402 5J8 A OBV   1 
HETATM 5627 C CBR   . 5J8 D 3 .   ? 26.396 -7.139  -1.693  0.92 33.91 ? 402 5J8 A CBR   1 
HETATM 5628 C CBQ   . 5J8 D 3 .   ? 26.050 -8.310  -0.697  0.92 35.70 ? 402 5J8 A CBQ   1 
HETATM 5629 C CBS   . 5J8 D 3 .   ? 26.625 -7.483  -3.008  0.92 32.84 ? 402 5J8 A CBS   1 
HETATM 5630 C CBN   . 5J8 D 3 .   ? 27.468 -8.828  -3.151  0.92 36.36 ? 402 5J8 A CBN   1 
HETATM 5631 C CBO   . 5J8 D 3 .   ? 26.903 -9.868  -2.464  0.92 38.35 ? 402 5J8 A CBO   1 
HETATM 5632 N NBP   . 5J8 D 3 .   ? 26.695 -9.535  -0.886  0.92 41.42 ? 402 5J8 A NBP   1 
HETATM 5633 C CBM   . 5J8 D 3 .   ? 27.112 -10.383 0.191   0.92 43.50 ? 402 5J8 A CBM   1 
HETATM 5634 O OBG   . 5J8 D 3 .   ? 28.728 -10.341 0.326   0.92 46.73 ? 402 5J8 A OBG   1 
HETATM 5635 C CBF   . 5J8 D 3 .   ? 26.760 -11.613 -0.059  0.92 47.89 ? 402 5J8 A CBF   1 
HETATM 5636 O OBI   . 5J8 D 3 .   ? 25.497 -11.945 0.671   0.92 42.30 ? 402 5J8 A OBI   1 
HETATM 5637 C CBE   . 5J8 D 3 .   ? 27.930 -12.466 0.467   0.92 49.39 ? 402 5J8 A CBE   1 
HETATM 5638 O OBJ   . 5J8 D 3 .   ? 27.746 -12.739 1.781   0.92 47.89 ? 402 5J8 A OBJ   1 
HETATM 5639 C CBH   . 5J8 D 3 .   ? 29.171 -11.568 0.274   0.92 49.01 ? 402 5J8 A CBH   1 
HETATM 5640 C CBK   . 5J8 D 3 .   ? 29.841 -11.833 -1.110  0.92 44.84 ? 402 5J8 A CBK   1 
HETATM 5641 O OBL   . 5J8 D 3 .   ? 29.108 -12.836 -1.778  0.92 57.06 ? 402 5J8 A OBL   1 
HETATM 5642 P PAA   . 5J8 D 3 .   ? 29.666 -13.484 -3.199  0.92 55.30 ? 402 5J8 A PAA   1 
HETATM 5643 O OAC   . 5J8 D 3 .   ? 28.694 -13.170 -4.312  0.92 46.48 ? 402 5J8 A OAC   1 
HETATM 5644 O OAB   . 5J8 D 3 .   ? 31.026 -12.914 -3.541  0.92 44.80 ? 402 5J8 A OAB   1 
HETATM 5645 O OAD   . 5J8 D 3 .   ? 29.771 -15.125 -2.968  0.92 61.33 ? 402 5J8 A OAD   1 
HETATM 5646 P PAE   . 5J8 D 3 .   ? 29.452 -15.822 -1.493  0.92 59.49 ? 402 5J8 A PAE   1 
HETATM 5647 O OAG   . 5J8 D 3 .   ? 27.989 -15.657 -1.167  0.92 63.99 ? 402 5J8 A OAG   1 
HETATM 5648 O OAF   . 5J8 D 3 .   ? 30.278 -15.153 -0.424  0.92 59.88 ? 402 5J8 A OAF   1 
HETATM 5649 O "O5'" . 5J8 D 3 .   ? 29.813 -17.437 -1.548  0.92 65.45 ? 402 5J8 A "O5'" 1 
HETATM 5650 C "C5'" . 5J8 D 3 .   ? 30.500 -17.940 -2.668  0.92 67.00 ? 402 5J8 A "C5'" 1 
HETATM 5651 C "C4'" . 5J8 D 3 .   ? 30.469 -19.493 -2.608  0.92 68.66 ? 402 5J8 A "C4'" 1 
HETATM 5652 O "O4'" . 5J8 D 3 .   ? 30.407 -19.884 -1.359  0.92 66.36 ? 402 5J8 A "O4'" 1 
HETATM 5653 C "C3'" . 5J8 D 3 .   ? 29.182 -20.007 -3.289  0.92 66.13 ? 402 5J8 A "C3'" 1 
HETATM 5654 O "O3'" . 5J8 D 3 .   ? 29.448 -21.121 -4.012  0.92 69.53 ? 402 5J8 A "O3'" 1 
HETATM 5655 C "C2'" . 5J8 D 3 .   ? 28.257 -20.341 -2.103  0.92 64.15 ? 402 5J8 A "C2'" 1 
HETATM 5656 O "O2'" . 5J8 D 3 .   ? 27.231 -21.358 -2.479  0.92 61.12 ? 402 5J8 A "O2'" 1 
HETATM 5657 P "P2'" . 5J8 D 3 .   ? 25.818 -20.820 -3.132  0.92 62.39 ? 402 5J8 A "P2'" 1 
HETATM 5658 O OP1   . 5J8 D 3 .   ? 25.311 -19.639 -2.339  0.92 60.06 ? 402 5J8 A OP1   1 
HETATM 5659 O OP3   . 5J8 D 3 .   ? 24.793 -21.928 -3.098  0.92 55.94 ? 402 5J8 A OP3   1 
HETATM 5660 O OP2   . 5J8 D 3 .   ? 26.057 -20.395 -4.563  0.92 50.44 ? 402 5J8 A OP2   1 
HETATM 5661 C "C1'" . 5J8 D 3 .   ? 29.090 -20.818 -1.224  0.92 67.77 ? 402 5J8 A "C1'" 1 
HETATM 5662 N N9    . 5J8 D 3 .   ? 28.551 -20.781 0.116   0.92 70.40 ? 402 5J8 A N9    1 
HETATM 5663 N N7    . 5J8 D 3 .   ? 28.052 -21.458 2.109   0.92 76.62 ? 402 5J8 A N7    1 
HETATM 5664 C C2    . 5J8 D 3 .   ? 26.856 -17.732 1.208   0.92 67.12 ? 402 5J8 A C2    1 
HETATM 5665 N N6    . 5J8 D 3 .   ? 26.456 -19.585 4.198   0.92 66.22 ? 402 5J8 A N6    1 
HETATM 5666 N N1    . FMN E 2 .   ? 35.718 -2.466  -43.679 1.00 27.92 ? 401 FMN B N1    1 
HETATM 5667 C C2    . FMN E 2 .   ? 35.822 -3.840  -43.663 1.00 25.86 ? 401 FMN B C2    1 
HETATM 5668 O O2    . FMN E 2 .   ? 35.698 -4.450  -42.603 1.00 29.74 ? 401 FMN B O2    1 
HETATM 5669 N N3    . FMN E 2 .   ? 36.060 -4.535  -44.830 1.00 29.63 ? 401 FMN B N3    1 
HETATM 5670 C C4    . FMN E 2 .   ? 36.203 -3.854  -46.020 1.00 31.73 ? 401 FMN B C4    1 
HETATM 5671 O O4    . FMN E 2 .   ? 36.415 -4.475  -47.062 1.00 36.11 ? 401 FMN B O4    1 
HETATM 5672 C C4A   . FMN E 2 .   ? 36.095 -2.468  -46.038 1.00 31.40 ? 401 FMN B C4A   1 
HETATM 5673 N N5    . FMN E 2 .   ? 36.225 -1.778  -47.221 1.00 34.09 ? 401 FMN B N5    1 
HETATM 5674 C C5A   . FMN E 2 .   ? 36.130 -0.405  -47.242 1.00 30.52 ? 401 FMN B C5A   1 
HETATM 5675 C C6    . FMN E 2 .   ? 36.272 0.270   -48.446 1.00 27.05 ? 401 FMN B C6    1 
HETATM 5676 C C7    . FMN E 2 .   ? 36.177 1.652   -48.483 1.00 27.38 ? 401 FMN B C7    1 
HETATM 5677 C C7M   . FMN E 2 .   ? 36.334 2.372   -49.790 1.00 34.37 ? 401 FMN B C7M   1 
HETATM 5678 C C8    . FMN E 2 .   ? 35.935 2.361   -47.313 1.00 31.98 ? 401 FMN B C8    1 
HETATM 5679 C C8M   . FMN E 2 .   ? 35.827 3.856   -47.349 1.00 37.49 ? 401 FMN B C8M   1 
HETATM 5680 C C9    . FMN E 2 .   ? 35.792 1.685   -46.108 1.00 30.01 ? 401 FMN B C9    1 
HETATM 5681 C C9A   . FMN E 2 .   ? 35.891 0.296   -46.068 1.00 28.84 ? 401 FMN B C9A   1 
HETATM 5682 N N10   . FMN E 2 .   ? 35.750 -0.396  -44.877 1.00 32.24 ? 401 FMN B N10   1 
HETATM 5683 C C10   . FMN E 2 .   ? 35.852 -1.773  -44.863 1.00 30.07 ? 401 FMN B C10   1 
HETATM 5684 C "C1'" . FMN E 2 .   ? 35.501 0.335   -43.589 1.00 23.47 ? 401 FMN B "C1'" 1 
HETATM 5685 C "C2'" . FMN E 2 .   ? 36.857 0.767   -43.035 1.00 26.82 ? 401 FMN B "C2'" 1 
HETATM 5686 O "O2'" . FMN E 2 .   ? 37.607 -0.365  -42.639 1.00 26.42 ? 401 FMN B "O2'" 1 
HETATM 5687 C "C3'" . FMN E 2 .   ? 36.690 1.733   -41.868 1.00 33.17 ? 401 FMN B "C3'" 1 
HETATM 5688 O "O3'" . FMN E 2 .   ? 35.936 1.112   -40.854 1.00 27.06 ? 401 FMN B "O3'" 1 
HETATM 5689 C "C4'" . FMN E 2 .   ? 35.970 2.988   -42.346 1.00 39.04 ? 401 FMN B "C4'" 1 
HETATM 5690 O "O4'" . FMN E 2 .   ? 36.627 3.497   -43.487 1.00 32.38 ? 401 FMN B "O4'" 1 
HETATM 5691 C "C5'" . FMN E 2 .   ? 35.919 4.070   -41.274 1.00 35.97 ? 401 FMN B "C5'" 1 
HETATM 5692 O "O5'" . FMN E 2 .   ? 37.239 4.442   -40.959 1.00 34.36 ? 401 FMN B "O5'" 1 
HETATM 5693 P P     . FMN E 2 .   ? 37.839 5.858   -41.436 1.00 32.38 ? 401 FMN B P     1 
HETATM 5694 O O1P   . FMN E 2 .   ? 37.020 6.978   -40.849 1.00 36.80 ? 401 FMN B O1P   1 
HETATM 5695 O O2P   . FMN E 2 .   ? 37.798 5.951   -42.942 1.00 32.89 ? 401 FMN B O2P   1 
HETATM 5696 O O3P   . FMN E 2 .   ? 39.270 5.952   -40.959 1.00 33.94 ? 401 FMN B O3P   1 
HETATM 5697 C C4    . 5J8 F 3 .   ? 28.967 11.812  -44.756 0.82 70.82 ? 402 5J8 B C4    1 
HETATM 5698 C C5    . 5J8 F 3 .   ? 29.147 11.408  -43.495 0.82 72.29 ? 402 5J8 B C5    1 
HETATM 5699 C C6    . 5J8 F 3 .   ? 28.342 11.915  -42.499 0.82 74.08 ? 402 5J8 B C6    1 
HETATM 5700 C C8    . 5J8 F 3 .   ? 30.601 10.382  -44.737 0.82 64.52 ? 402 5J8 B C8    1 
HETATM 5701 N N1    . 5J8 F 3 .   ? 27.397 12.796  -42.789 0.82 75.87 ? 402 5J8 B N1    1 
HETATM 5702 N N3    . 5J8 F 3 .   ? 28.007 12.708  -45.049 0.82 68.49 ? 402 5J8 B N3    1 
HETATM 5703 N NBU   . 5J8 F 3 .   ? 33.429 -4.697  -46.989 0.82 31.35 ? 402 5J8 B NBU   1 
HETATM 5704 C CBT   . 5J8 F 3 .   ? 32.995 -3.667  -46.070 0.82 33.91 ? 402 5J8 B CBT   1 
HETATM 5705 O OBV   . 5J8 F 3 .   ? 32.923 -3.886  -44.909 0.82 28.57 ? 402 5J8 B OBV   1 
HETATM 5706 C CBR   . 5J8 F 3 .   ? 32.633 -2.289  -46.597 0.82 30.90 ? 402 5J8 B CBR   1 
HETATM 5707 C CBQ   . 5J8 F 3 .   ? 32.636 -1.098  -45.572 0.82 31.70 ? 402 5J8 B CBQ   1 
HETATM 5708 C CBS   . 5J8 F 3 .   ? 32.864 -1.968  -47.917 0.82 31.97 ? 402 5J8 B CBS   1 
HETATM 5709 C CBN   . 5J8 F 3 .   ? 32.106 -0.639  -48.371 0.82 33.93 ? 402 5J8 B CBN   1 
HETATM 5710 C CBO   . 5J8 F 3 .   ? 32.342 0.422   -47.539 0.82 31.84 ? 402 5J8 B CBO   1 
HETATM 5711 N NBP   . 5J8 F 3 .   ? 32.027 0.089   -45.978 0.82 32.87 ? 402 5J8 B NBP   1 
HETATM 5712 C CBM   . 5J8 F 3 .   ? 31.234 0.896   -45.101 0.82 31.02 ? 402 5J8 B CBM   1 
HETATM 5713 O OBG   . 5J8 F 3 .   ? 29.692 0.884   -45.592 0.82 36.28 ? 402 5J8 B OBG   1 
HETATM 5714 C CBF   . 5J8 F 3 .   ? 31.660 2.127   -45.132 0.82 38.86 ? 402 5J8 B CBF   1 
HETATM 5715 O OBI   . 5J8 F 3 .   ? 32.584 2.379   -43.982 0.82 37.60 ? 402 5J8 B OBI   1 
HETATM 5716 C CBE   . 5J8 F 3 .   ? 30.380 2.971   -44.995 0.82 40.69 ? 402 5J8 B CBE   1 
HETATM 5717 O OBJ   . 5J8 F 3 .   ? 30.088 3.145   -43.683 0.82 44.07 ? 402 5J8 B OBJ   1 
HETATM 5718 C CBH   . 5J8 F 3 .   ? 29.286 2.120   -45.677 0.82 37.57 ? 402 5J8 B CBH   1 
HETATM 5719 C CBK   . 5J8 F 3 .   ? 29.123 2.506   -47.178 0.82 41.86 ? 402 5J8 B CBK   1 
HETATM 5720 O OBL   . 5J8 F 3 .   ? 30.143 3.413   -47.527 0.82 48.06 ? 402 5J8 B OBL   1 
HETATM 5721 P PAA   . 5J8 F 3 .   ? 30.179 4.067   -49.049 0.82 41.11 ? 402 5J8 B PAA   1 
HETATM 5722 O OAC   . 5J8 F 3 .   ? 31.486 3.708   -49.716 0.82 39.02 ? 402 5J8 B OAC   1 
HETATM 5723 O OAB   . 5J8 F 3 .   ? 29.020 3.537   -49.866 0.82 40.20 ? 402 5J8 B OAB   1 
HETATM 5724 O OAD   . 5J8 F 3 .   ? 30.049 5.713   -48.873 0.82 44.31 ? 402 5J8 B OAD   1 
HETATM 5725 P PAE   . 5J8 F 3 .   ? 29.820 6.418   -47.386 0.82 53.21 ? 402 5J8 B PAE   1 
HETATM 5726 O OAG   . 5J8 F 3 .   ? 31.070 6.264   -46.558 0.82 53.49 ? 402 5J8 B OAG   1 
HETATM 5727 O OAF   . 5J8 F 3 .   ? 28.672 5.746   -46.679 0.82 50.54 ? 402 5J8 B OAF   1 
HETATM 5728 O "O5'" . 5J8 F 3 .   ? 29.489 8.029   -47.573 0.82 52.71 ? 402 5J8 B "O5'" 1 
HETATM 5729 C "C5'" . 5J8 F 3 .   ? 29.262 8.521   -48.871 0.82 58.75 ? 402 5J8 B "C5'" 1 
HETATM 5730 C "C4'" . 5J8 F 3 .   ? 29.345 10.073  -48.837 0.82 60.22 ? 402 5J8 B "C4'" 1 
HETATM 5731 O "O4'" . 5J8 F 3 .   ? 28.843 10.519  -47.714 0.82 61.62 ? 402 5J8 B "O4'" 1 
HETATM 5732 C "C3'" . 5J8 F 3 .   ? 30.824 10.508  -48.845 0.82 55.89 ? 402 5J8 B "C3'" 1 
HETATM 5733 O "O3'" . 5J8 F 3 .   ? 30.971 11.636  -49.580 0.82 63.05 ? 402 5J8 B "O3'" 1 
HETATM 5734 C "C2'" . 5J8 F 3 .   ? 31.135 10.792  -47.363 0.82 59.08 ? 402 5J8 B "C2'" 1 
HETATM 5735 O "O2'" . 5J8 F 3 .   ? 32.270 11.758  -47.236 0.82 54.50 ? 402 5J8 B "O2'" 1 
HETATM 5736 P "P2'" . 5J8 F 3 .   ? 33.788 11.255  -47.638 0.82 51.52 ? 402 5J8 B "P2'" 1 
HETATM 5737 O OP1   . 5J8 F 3 .   ? 34.009 9.849   -47.129 0.82 52.69 ? 402 5J8 B OP1   1 
HETATM 5738 O OP3   . 5J8 F 3 .   ? 34.813 12.182  -47.030 0.82 43.68 ? 402 5J8 B OP3   1 
HETATM 5739 O OP2   . 5J8 F 3 .   ? 33.940 11.264  -49.139 0.82 53.46 ? 402 5J8 B OP2   1 
HETATM 5740 C "C1'" . 5J8 F 3 .   ? 30.021 11.322  -46.945 0.82 62.64 ? 402 5J8 B "C1'" 1 
HETATM 5741 N N9    . 5J8 F 3 .   ? 29.866 11.178  -45.520 0.82 67.27 ? 402 5J8 B N9    1 
HETATM 5742 N N7    . 5J8 F 3 .   ? 30.156 10.525  -43.483 0.82 73.76 ? 402 5J8 B N7    1 
HETATM 5743 C C2    . 5J8 F 3 .   ? 27.219 13.203  -44.067 0.82 75.02 ? 402 5J8 B C2    1 
HETATM 5744 N N6    . 5J8 F 3 .   ? 28.306 11.666  -41.068 0.82 72.89 ? 402 5J8 B N6    1 
HETATM 5745 O O     . HOH G 4 .   ? 22.078 17.253  4.236   1.00 53.26 ? 501 HOH A O     1 
HETATM 5746 O O     . HOH G 4 .   ? 37.326 8.562   -5.648  1.00 40.97 ? 502 HOH A O     1 
HETATM 5747 O O     . HOH G 4 .   ? 16.642 -0.203  -21.377 1.00 41.77 ? 503 HOH A O     1 
HETATM 5748 O O     . HOH G 4 .   ? 32.881 -3.084  -4.519  1.00 35.12 ? 504 HOH A O     1 
HETATM 5749 O O     . HOH G 4 .   ? 25.923 -15.200 -1.806  1.00 50.56 ? 505 HOH A O     1 
HETATM 5750 O O     . HOH G 4 .   ? 25.351 -18.749 12.480  1.00 56.20 ? 506 HOH A O     1 
HETATM 5751 O O     . HOH G 4 .   ? 23.729 -10.785 3.191   1.00 41.41 ? 507 HOH A O     1 
HETATM 5752 O O     . HOH G 4 .   ? 5.252  4.902   -16.205 1.00 51.64 ? 508 HOH A O     1 
HETATM 5753 O O     . HOH G 4 .   ? 22.192 -14.251 -24.119 1.00 45.54 ? 509 HOH A O     1 
HETATM 5754 O O     . HOH G 4 .   ? 23.620 -7.064  -21.726 1.00 33.59 ? 510 HOH A O     1 
HETATM 5755 O O     . HOH G 4 .   ? 30.875 -8.836  -16.783 1.00 45.56 ? 511 HOH A O     1 
HETATM 5756 O O     . HOH G 4 .   ? 3.272  -18.973 -9.774  1.00 48.00 ? 512 HOH A O     1 
HETATM 5757 O O     . HOH G 4 .   ? -3.362 1.677   4.810   1.00 52.80 ? 513 HOH A O     1 
HETATM 5758 O O     . HOH G 4 .   ? 31.275 -5.006  -18.284 1.00 39.28 ? 514 HOH A O     1 
HETATM 5759 O O     . HOH G 4 .   ? 17.766 -7.585  -7.494  1.00 30.35 ? 515 HOH A O     1 
HETATM 5760 O O     . HOH G 4 .   ? 34.801 18.817  11.642  1.00 42.13 ? 516 HOH A O     1 
HETATM 5761 O O     . HOH G 4 .   ? 33.959 -13.718 -14.002 1.00 47.44 ? 517 HOH A O     1 
HETATM 5762 O O     . HOH G 4 .   ? 23.772 -13.661 -17.983 1.00 41.14 ? 518 HOH A O     1 
HETATM 5763 O O     . HOH G 4 .   ? 40.320 13.655  1.658   1.00 43.34 ? 519 HOH A O     1 
HETATM 5764 O O     . HOH G 4 .   ? 31.417 10.284  -2.599  1.00 38.85 ? 520 HOH A O     1 
HETATM 5765 O O     . HOH G 4 .   ? 8.551  -26.820 -8.046  1.00 47.44 ? 521 HOH A O     1 
HETATM 5766 O O     . HOH G 4 .   ? 2.354  -4.452  -13.914 1.00 41.35 ? 522 HOH A O     1 
HETATM 5767 O O     . HOH G 4 .   ? 34.191 5.206   -3.064  1.00 33.79 ? 523 HOH A O     1 
HETATM 5768 O O     . HOH G 4 .   ? 24.279 -23.231 -1.001  1.00 49.58 ? 524 HOH A O     1 
HETATM 5769 O O     . HOH G 4 .   ? 36.096 17.223  4.075   1.00 33.62 ? 525 HOH A O     1 
HETATM 5770 O O     . HOH G 4 .   ? 20.255 -4.991  -12.338 1.00 34.36 ? 526 HOH A O     1 
HETATM 5771 O O     . HOH G 4 .   ? 6.994  -13.607 -5.972  1.00 35.95 ? 527 HOH A O     1 
HETATM 5772 O O     . HOH G 4 .   ? 17.031 -18.831 -15.491 1.00 48.65 ? 528 HOH A O     1 
HETATM 5773 O O     . HOH G 4 .   ? 29.989 -7.698  -19.787 1.00 41.23 ? 529 HOH A O     1 
HETATM 5774 O O     . HOH G 4 .   ? 32.603 -5.211  -8.439  1.00 36.33 ? 530 HOH A O     1 
HETATM 5775 O O     . HOH G 4 .   ? 28.195 -13.875 -12.212 1.00 30.80 ? 531 HOH A O     1 
HETATM 5776 O O     . HOH G 4 .   ? 10.269 0.497   12.406  1.00 31.37 ? 532 HOH A O     1 
HETATM 5777 O O     . HOH G 4 .   ? 25.036 3.069   1.524   1.00 26.99 ? 533 HOH A O     1 
HETATM 5778 O O     . HOH G 4 .   ? 6.239  -6.605  16.250  1.00 42.33 ? 534 HOH A O     1 
HETATM 5779 O O     . HOH G 4 .   ? 38.208 15.226  2.332   1.00 37.78 ? 535 HOH A O     1 
HETATM 5780 O O     . HOH G 4 .   ? 24.574 -14.272 -0.133  1.00 41.37 ? 536 HOH A O     1 
HETATM 5781 O O     . HOH G 4 .   ? 39.748 -0.789  -0.572  1.00 34.74 ? 537 HOH A O     1 
HETATM 5782 O O     . HOH G 4 .   ? 15.742 -12.109 15.492  1.00 39.68 ? 538 HOH A O     1 
HETATM 5783 O O     . HOH G 4 .   ? 10.760 -4.127  20.170  1.00 41.94 ? 539 HOH A O     1 
HETATM 5784 O O     . HOH G 4 .   ? 6.424  5.907   -10.524 1.00 55.85 ? 540 HOH A O     1 
HETATM 5785 O O     . HOH G 4 .   ? 26.430 -2.961  9.455   1.00 37.52 ? 541 HOH A O     1 
HETATM 5786 O O     . HOH G 4 .   ? 16.528 -6.668  -5.030  1.00 26.94 ? 542 HOH A O     1 
HETATM 5787 O O     . HOH G 4 .   ? 17.415 -14.883 3.777   1.00 33.18 ? 543 HOH A O     1 
HETATM 5788 O O     . HOH G 4 .   ? 0.662  -5.037  11.713  1.00 44.12 ? 544 HOH A O     1 
HETATM 5789 O O     . HOH G 4 .   ? 21.135 -16.294 -12.008 1.00 29.10 ? 545 HOH A O     1 
HETATM 5790 O O     . HOH G 4 .   ? 31.968 5.358   -8.480  1.00 35.46 ? 546 HOH A O     1 
HETATM 5791 O O     . HOH G 4 .   ? 35.475 -2.876  3.725   1.00 30.04 ? 547 HOH A O     1 
HETATM 5792 O O     . HOH G 4 .   ? 16.988 -16.927 -0.300  1.00 29.52 ? 548 HOH A O     1 
HETATM 5793 O O     . HOH G 4 .   ? 25.111 -12.338 -22.709 1.00 46.53 ? 549 HOH A O     1 
HETATM 5794 O O     . HOH G 4 .   ? 21.925 14.802  9.182   1.00 39.13 ? 550 HOH A O     1 
HETATM 5795 O O     . HOH G 4 .   ? 0.797  -22.112 3.617   1.00 49.10 ? 551 HOH A O     1 
HETATM 5796 O O     . HOH G 4 .   ? 17.732 -6.769  23.744  1.00 30.74 ? 552 HOH A O     1 
HETATM 5797 O O     . HOH G 4 .   ? 18.010 -6.421  -10.087 1.00 33.20 ? 553 HOH A O     1 
HETATM 5798 O O     . HOH G 4 .   ? 23.085 -2.902  -7.593  1.00 28.80 ? 554 HOH A O     1 
HETATM 5799 O O     . HOH G 4 .   ? 6.734  -0.111  10.509  1.00 38.47 ? 555 HOH A O     1 
HETATM 5800 O O     . HOH G 4 .   ? 12.631 -21.141 -11.959 1.00 41.83 ? 556 HOH A O     1 
HETATM 5801 O O     . HOH G 4 .   ? 7.509  -9.557  -1.535  1.00 33.77 ? 557 HOH A O     1 
HETATM 5802 O O     . HOH G 4 .   ? 30.844 7.515   12.435  1.00 35.72 ? 558 HOH A O     1 
HETATM 5803 O O     . HOH G 4 .   ? 29.021 -15.101 -9.987  1.00 38.02 ? 559 HOH A O     1 
HETATM 5804 O O     . HOH G 4 .   ? 14.345 -8.990  -19.727 1.00 52.56 ? 560 HOH A O     1 
HETATM 5805 O O     . HOH G 4 .   ? 28.572 10.389  -2.477  1.00 40.42 ? 561 HOH A O     1 
HETATM 5806 O O     . HOH G 4 .   ? 31.843 -7.979  12.843  1.00 43.64 ? 562 HOH A O     1 
HETATM 5807 O O     . HOH G 4 .   ? 28.415 5.317   11.303  1.00 36.14 ? 563 HOH A O     1 
HETATM 5808 O O     . HOH G 4 .   ? 26.160 -0.688  22.956  1.00 32.16 ? 564 HOH A O     1 
HETATM 5809 O O     . HOH G 4 .   ? 17.131 -13.643 -11.661 1.00 36.85 ? 565 HOH A O     1 
HETATM 5810 O O     . HOH G 4 .   ? 32.551 9.700   22.750  1.00 47.32 ? 566 HOH A O     1 
HETATM 5811 O O     . HOH G 4 .   ? 35.646 -3.251  22.172  1.00 51.28 ? 567 HOH A O     1 
HETATM 5812 O O     . HOH G 4 .   ? 45.149 -3.606  4.018   1.00 46.24 ? 568 HOH A O     1 
HETATM 5813 O O     . HOH G 4 .   ? 24.896 -8.937  11.672  1.00 39.03 ? 569 HOH A O     1 
HETATM 5814 O O     . HOH G 4 .   ? 7.761  3.250   21.080  1.00 46.09 ? 570 HOH A O     1 
HETATM 5815 O O     . HOH G 4 .   ? 39.265 4.690   -14.740 1.00 43.90 ? 571 HOH A O     1 
HETATM 5816 O O     . HOH G 4 .   ? 6.052  -8.584  1.878   1.00 35.52 ? 572 HOH A O     1 
HETATM 5817 O O     . HOH G 4 .   ? 14.404 -16.926 13.853  1.00 42.31 ? 573 HOH A O     1 
HETATM 5818 O O     . HOH G 4 .   ? 44.471 5.003   -4.573  1.00 50.14 ? 574 HOH A O     1 
HETATM 5819 O O     . HOH G 4 .   ? 16.907 16.549  5.151   1.00 50.75 ? 575 HOH A O     1 
HETATM 5820 O O     . HOH G 4 .   ? 34.502 -10.619 -5.803  1.00 46.77 ? 576 HOH A O     1 
HETATM 5821 O O     . HOH G 4 .   ? 29.073 -9.670  19.930  1.00 52.30 ? 577 HOH A O     1 
HETATM 5822 O O     . HOH G 4 .   ? 37.809 -4.977  -16.884 1.00 42.31 ? 578 HOH A O     1 
HETATM 5823 O O     . HOH G 4 .   ? 6.832  8.406   -4.131  1.00 44.40 ? 579 HOH A O     1 
HETATM 5824 O O     . HOH G 4 .   ? 6.414  -9.696  -3.827  1.00 39.26 ? 580 HOH A O     1 
HETATM 5825 O O     . HOH G 4 .   ? 22.405 9.186   -16.162 1.00 38.04 ? 581 HOH A O     1 
HETATM 5826 O O     . HOH G 4 .   ? 7.341  -19.897 -16.633 1.00 47.00 ? 582 HOH A O     1 
HETATM 5827 O O     . HOH G 4 .   ? 30.680 7.445   -12.246 1.00 45.17 ? 583 HOH A O     1 
HETATM 5828 O O     . HOH G 4 .   ? 35.392 -8.947  -2.700  1.00 42.07 ? 584 HOH A O     1 
HETATM 5829 O O     . HOH G 4 .   ? 11.880 -27.943 -8.993  1.00 38.32 ? 585 HOH A O     1 
HETATM 5830 O O     . HOH G 4 .   ? 6.670  3.873   10.498  1.00 47.64 ? 586 HOH A O     1 
HETATM 5831 O O     . HOH G 4 .   ? 11.952 -5.012  16.837  1.00 38.00 ? 587 HOH A O     1 
HETATM 5832 O O     . HOH G 4 .   ? 29.684 1.177   -12.186 1.00 36.33 ? 588 HOH A O     1 
HETATM 5833 O O     . HOH G 4 .   ? 27.453 2.240   2.711   1.00 37.68 ? 589 HOH A O     1 
HETATM 5834 O O     . HOH G 4 .   ? 10.273 -16.207 -17.479 1.00 51.32 ? 590 HOH A O     1 
HETATM 5835 O O     . HOH G 4 .   ? 10.902 4.885   19.149  1.00 42.77 ? 591 HOH A O     1 
HETATM 5836 O O     . HOH G 4 .   ? 28.198 -0.322  -6.495  1.00 33.25 ? 592 HOH A O     1 
HETATM 5837 O O     . HOH G 4 .   ? 22.832 -3.965  -9.833  1.00 33.19 ? 593 HOH A O     1 
HETATM 5838 O O     . HOH G 4 .   ? 32.891 -5.819  -3.943  1.00 36.87 ? 594 HOH A O     1 
HETATM 5839 O O     . HOH G 4 .   ? -2.468 -4.743  8.478   1.00 47.04 ? 595 HOH A O     1 
HETATM 5840 O O     . HOH G 4 .   ? 31.514 3.256   -12.337 1.00 47.82 ? 596 HOH A O     1 
HETATM 5841 O O     . HOH G 4 .   ? 8.089  -4.403  17.138  1.00 42.68 ? 597 HOH A O     1 
HETATM 5842 O O     . HOH G 4 .   ? 13.179 -15.158 -13.803 1.00 40.69 ? 598 HOH A O     1 
HETATM 5843 O O     . HOH G 4 .   ? 29.566 0.367   -15.134 1.00 35.57 ? 599 HOH A O     1 
HETATM 5844 O O     . HOH G 4 .   ? 24.869 17.429  5.523   1.00 44.96 ? 600 HOH A O     1 
HETATM 5845 O O     . HOH G 4 .   ? 16.446 -14.621 16.472  1.00 41.57 ? 601 HOH A O     1 
HETATM 5846 O O     . HOH G 4 .   ? 25.060 -21.927 -8.393  1.00 40.93 ? 602 HOH A O     1 
HETATM 5847 O O     . HOH G 4 .   ? -2.235 -5.802  5.916   1.00 48.74 ? 603 HOH A O     1 
HETATM 5848 O O     . HOH G 4 .   ? 5.686  1.568   -16.881 1.00 46.67 ? 604 HOH A O     1 
HETATM 5849 O O     . HOH G 4 .   ? 10.900 14.387  -3.859  1.00 42.31 ? 605 HOH A O     1 
HETATM 5850 O O     . HOH G 4 .   ? 22.725 -24.087 -7.105  1.00 40.03 ? 606 HOH A O     1 
HETATM 5851 O O     . HOH G 4 .   ? 21.295 -5.575  -19.326 1.00 34.92 ? 607 HOH A O     1 
HETATM 5852 O O     . HOH G 4 .   ? 4.477  -15.266 -6.041  1.00 37.64 ? 608 HOH A O     1 
HETATM 5853 O O     . HOH G 4 .   ? 9.240  -23.994 -12.224 1.00 44.61 ? 609 HOH A O     1 
HETATM 5854 O O     . HOH G 4 .   ? 38.627 -5.032  15.180  1.00 45.16 ? 610 HOH A O     1 
HETATM 5855 O O     . HOH G 4 .   ? -0.653 -8.965  -8.024  1.00 40.19 ? 611 HOH A O     1 
HETATM 5856 O O     . HOH G 4 .   ? 33.202 -7.343  -6.398  1.00 40.91 ? 612 HOH A O     1 
HETATM 5857 O O     . HOH G 4 .   ? 46.457 2.169   -4.330  1.00 49.82 ? 613 HOH A O     1 
HETATM 5858 O O     . HOH G 4 .   ? 46.662 -7.662  2.161   1.00 51.90 ? 614 HOH A O     1 
HETATM 5859 O O     . HOH G 4 .   ? 9.876  -3.840  -18.734 1.00 46.79 ? 615 HOH A O     1 
HETATM 5860 O O     . HOH G 4 .   ? 41.190 -12.407 -12.617 1.00 44.88 ? 616 HOH A O     1 
HETATM 5861 O O     . HOH G 4 .   ? 38.462 15.935  10.832  1.00 40.56 ? 617 HOH A O     1 
HETATM 5862 O O     . HOH G 4 .   ? 27.824 0.016   4.381   1.00 34.89 ? 618 HOH A O     1 
HETATM 5863 O O     . HOH G 4 .   ? 29.116 21.441  5.962   1.00 39.42 ? 619 HOH A O     1 
HETATM 5864 O O     . HOH G 4 .   ? 36.990 4.397   22.392  1.00 47.35 ? 620 HOH A O     1 
HETATM 5865 O O     . HOH G 4 .   ? 42.505 1.575   -8.420  1.00 42.09 ? 621 HOH A O     1 
HETATM 5866 O O     . HOH G 4 .   ? 8.931  -26.031 -10.500 1.00 43.75 ? 622 HOH A O     1 
HETATM 5867 O O     . HOH G 4 .   ? 19.903 11.592  17.676  1.00 45.11 ? 623 HOH A O     1 
HETATM 5868 O O     . HOH G 4 .   ? -1.903 -16.243 8.307   1.00 53.63 ? 624 HOH A O     1 
HETATM 5869 O O     . HOH G 4 .   ? 37.571 18.020  12.875  1.00 44.23 ? 625 HOH A O     1 
HETATM 5870 O O     . HOH G 4 .   ? 29.423 -5.260  26.603  1.00 44.01 ? 626 HOH A O     1 
HETATM 5871 O O     . HOH G 4 .   ? 30.406 -10.390 -15.086 1.00 54.26 ? 627 HOH A O     1 
HETATM 5872 O O     . HOH G 4 .   ? 23.319 0.802   23.627  1.00 41.81 ? 628 HOH A O     1 
HETATM 5873 O O     . HOH G 4 .   ? 28.938 2.553   -16.690 1.00 48.94 ? 629 HOH A O     1 
HETATM 5874 O O     . HOH G 4 .   ? 8.688  6.953   18.497  1.00 48.51 ? 630 HOH A O     1 
HETATM 5875 O O     . HOH G 4 .   ? 7.880  -2.379  19.061  1.00 48.52 ? 631 HOH A O     1 
HETATM 5876 O O     . HOH G 4 .   ? 32.130 -10.942 13.297  1.00 53.03 ? 632 HOH A O     1 
HETATM 5877 O O     . HOH G 4 .   ? 31.940 8.209   24.420  1.00 42.47 ? 633 HOH A O     1 
HETATM 5878 O O     . HOH G 4 .   ? 6.407  1.437   12.232  1.00 48.99 ? 634 HOH A O     1 
HETATM 5879 O O     . HOH G 4 .   ? 36.406 10.964  -5.206  1.00 45.77 ? 635 HOH A O     1 
HETATM 5880 O O     . HOH G 4 .   ? -3.983 -4.763  2.534   1.00 49.02 ? 636 HOH A O     1 
HETATM 5881 O O     . HOH G 4 .   ? 33.615 -10.563 -2.355  1.00 50.79 ? 637 HOH A O     1 
HETATM 5882 O O     . HOH G 4 .   ? 17.597 -3.836  -21.282 1.00 43.88 ? 638 HOH A O     1 
HETATM 5883 O O     . HOH G 4 .   ? 15.739 18.147  4.477   1.00 39.46 ? 639 HOH A O     1 
HETATM 5884 O O     . HOH G 4 .   ? 16.573 -21.580 -16.046 1.00 48.66 ? 640 HOH A O     1 
HETATM 5885 O O     . HOH G 4 .   ? 32.148 -12.024 -8.372  1.00 40.62 ? 641 HOH A O     1 
HETATM 5886 O O     . HOH G 4 .   ? 23.115 -10.669 13.249  1.00 34.23 ? 642 HOH A O     1 
HETATM 5887 O O     . HOH G 4 .   ? 30.417 -12.378 -13.190 1.00 36.92 ? 643 HOH A O     1 
HETATM 5888 O O     . HOH G 4 .   ? 32.045 -9.681  -6.391  1.00 37.48 ? 644 HOH A O     1 
HETATM 5889 O O     . HOH G 4 .   ? 27.701 -23.676 -15.151 1.00 58.08 ? 645 HOH A O     1 
HETATM 5890 O O     . HOH G 4 .   ? -0.138 -23.776 5.049   1.00 55.97 ? 646 HOH A O     1 
HETATM 5891 O O     . HOH G 4 .   ? 31.411 -13.810 -14.803 1.00 47.33 ? 647 HOH A O     1 
HETATM 5892 O O     . HOH G 4 .   ? 41.508 12.470  9.627   1.00 64.47 ? 648 HOH A O     1 
HETATM 5893 O O     . HOH G 4 .   ? 31.409 -13.430 -10.303 1.00 36.08 ? 649 HOH A O     1 
HETATM 5894 O O     . HOH G 4 .   ? 27.381 -24.889 -13.478 1.00 56.16 ? 650 HOH A O     1 
HETATM 5895 O O     . HOH G 4 .   ? 3.653  -14.339 -8.012  1.00 42.22 ? 651 HOH A O     1 
HETATM 5896 O O     . HOH G 4 .   ? 32.132 -0.605  -15.543 1.00 33.20 ? 652 HOH A O     1 
HETATM 5897 O O     . HOH G 4 .   ? 35.704 4.867   24.639  1.00 38.92 ? 653 HOH A O     1 
HETATM 5898 O O     . HOH G 4 .   ? 13.230 -11.597 -24.289 1.00 51.15 ? 654 HOH A O     1 
HETATM 5899 O O     . HOH H 4 .   ? 27.746 -8.925  -28.199 1.00 59.15 ? 501 HOH B O     1 
HETATM 5900 O O     . HOH H 4 .   ? 34.720 12.454  -50.555 1.00 47.97 ? 502 HOH B O     1 
HETATM 5901 O O     . HOH H 4 .   ? 12.876 -8.919  -38.520 1.00 60.20 ? 503 HOH B O     1 
HETATM 5902 O O     . HOH H 4 .   ? 55.209 1.439   -54.864 1.00 41.46 ? 504 HOH B O     1 
HETATM 5903 O O     . HOH H 4 .   ? 43.382 7.855   -24.980 1.00 69.86 ? 505 HOH B O     1 
HETATM 5904 O O     . HOH H 4 .   ? 47.944 16.030  -33.793 1.00 55.05 ? 506 HOH B O     1 
HETATM 5905 O O     . HOH H 4 .   ? 33.102 5.432   -46.532 1.00 47.58 ? 507 HOH B O     1 
HETATM 5906 O O     . HOH H 4 .   ? 16.378 -13.397 -34.094 1.00 50.05 ? 508 HOH B O     1 
HETATM 5907 O O     . HOH H 4 .   ? 11.903 -2.409  -50.715 1.00 54.64 ? 509 HOH B O     1 
HETATM 5908 O O     . HOH H 4 .   ? 26.029 -21.719 -49.421 1.00 44.36 ? 510 HOH B O     1 
HETATM 5909 O O     . HOH H 4 .   ? 32.548 -12.541 -43.031 1.00 25.77 ? 511 HOH B O     1 
HETATM 5910 O O     . HOH H 4 .   ? 45.045 -2.988  -22.988 1.00 41.19 ? 512 HOH B O     1 
HETATM 5911 O O     . HOH H 4 .   ? 16.555 -4.311  -52.584 1.00 40.22 ? 513 HOH B O     1 
HETATM 5912 O O     . HOH H 4 .   ? 59.082 14.841  -50.881 1.00 61.84 ? 514 HOH B O     1 
HETATM 5913 O O     . HOH H 4 .   ? 62.725 -4.732  -46.627 1.00 52.88 ? 515 HOH B O     1 
HETATM 5914 O O     . HOH H 4 .   ? 27.705 -6.133  -51.299 1.00 35.57 ? 516 HOH B O     1 
HETATM 5915 O O     . HOH H 4 .   ? 24.254 -17.792 -53.496 1.00 39.71 ? 517 HOH B O     1 
HETATM 5916 O O     . HOH H 4 .   ? 40.733 7.581   -41.983 1.00 32.65 ? 518 HOH B O     1 
HETATM 5917 O O     . HOH H 4 .   ? 51.010 -19.323 -58.802 1.00 55.88 ? 519 HOH B O     1 
HETATM 5918 O O     . HOH H 4 .   ? 54.250 -15.266 -47.683 1.00 42.94 ? 520 HOH B O     1 
HETATM 5919 O O     . HOH H 4 .   ? 57.957 1.775   -30.923 1.00 53.85 ? 521 HOH B O     1 
HETATM 5920 O O     . HOH H 4 .   ? 40.414 -27.235 -37.039 1.00 48.34 ? 522 HOH B O     1 
HETATM 5921 O O     . HOH H 4 .   ? 35.569 14.204  -48.171 1.00 46.67 ? 523 HOH B O     1 
HETATM 5922 O O     . HOH H 4 .   ? 49.998 -0.416  -39.659 1.00 36.28 ? 524 HOH B O     1 
HETATM 5923 O O     . HOH H 4 .   ? 17.417 -25.522 -35.008 1.00 54.36 ? 525 HOH B O     1 
HETATM 5924 O O     . HOH H 4 .   ? 33.848 -26.497 -39.537 1.00 44.42 ? 526 HOH B O     1 
HETATM 5925 O O     . HOH H 4 .   ? 26.093 1.284   -53.360 1.00 44.55 ? 527 HOH B O     1 
HETATM 5926 O O     . HOH H 4 .   ? 28.633 -6.252  -36.132 1.00 36.20 ? 528 HOH B O     1 
HETATM 5927 O O     . HOH H 4 .   ? 35.730 -2.096  -64.663 1.00 29.41 ? 529 HOH B O     1 
HETATM 5928 O O     . HOH H 4 .   ? 42.017 -4.392  -54.387 1.00 30.25 ? 530 HOH B O     1 
HETATM 5929 O O     . HOH H 4 .   ? 21.413 -26.620 -44.484 1.00 31.86 ? 531 HOH B O     1 
HETATM 5930 O O     . HOH H 4 .   ? 45.269 13.944  -52.659 1.00 35.33 ? 532 HOH B O     1 
HETATM 5931 O O     . HOH H 4 .   ? 11.429 -11.880 -48.840 1.00 36.36 ? 533 HOH B O     1 
HETATM 5932 O O     . HOH H 4 .   ? 34.010 -4.316  -63.803 1.00 42.46 ? 534 HOH B O     1 
HETATM 5933 O O     . HOH H 4 .   ? 37.579 -6.671  -50.852 1.00 34.31 ? 535 HOH B O     1 
HETATM 5934 O O     . HOH H 4 .   ? 44.078 -20.980 -29.778 1.00 45.11 ? 536 HOH B O     1 
HETATM 5935 O O     . HOH H 4 .   ? 39.048 -5.270  -52.716 1.00 30.97 ? 537 HOH B O     1 
HETATM 5936 O O     . HOH H 4 .   ? 15.186 -17.461 -42.029 1.00 41.12 ? 538 HOH B O     1 
HETATM 5937 O O     . HOH H 4 .   ? 28.107 -19.650 -49.094 1.00 38.22 ? 539 HOH B O     1 
HETATM 5938 O O     . HOH H 4 .   ? 39.233 -4.678  -24.160 1.00 35.91 ? 540 HOH B O     1 
HETATM 5939 O O     . HOH H 4 .   ? 33.416 -11.479 -50.433 1.00 33.43 ? 541 HOH B O     1 
HETATM 5940 O O     . HOH H 4 .   ? 46.471 -12.883 -28.477 1.00 40.51 ? 542 HOH B O     1 
HETATM 5941 O O     . HOH H 4 .   ? 52.740 6.766   -55.198 1.00 48.74 ? 543 HOH B O     1 
HETATM 5942 O O     . HOH H 4 .   ? 30.976 9.255   -23.030 1.00 51.27 ? 544 HOH B O     1 
HETATM 5943 O O     . HOH H 4 .   ? 57.396 9.311   -46.112 1.00 46.36 ? 545 HOH B O     1 
HETATM 5944 O O     . HOH H 4 .   ? 28.589 -33.062 -46.116 1.00 45.67 ? 546 HOH B O     1 
HETATM 5945 O O     . HOH H 4 .   ? 20.420 -24.551 -46.633 1.00 38.61 ? 547 HOH B O     1 
HETATM 5946 O O     . HOH H 4 .   ? 42.806 -9.732  -27.461 1.00 36.13 ? 548 HOH B O     1 
HETATM 5947 O O     . HOH H 4 .   ? 33.368 1.447   -41.015 1.00 48.16 ? 549 HOH B O     1 
HETATM 5948 O O     . HOH H 4 .   ? 32.962 -0.899  -65.013 1.00 45.50 ? 550 HOH B O     1 
HETATM 5949 O O     . HOH H 4 .   ? 49.592 11.578  -51.036 1.00 32.97 ? 551 HOH B O     1 
HETATM 5950 O O     . HOH H 4 .   ? 54.549 12.360  -32.783 1.00 49.34 ? 552 HOH B O     1 
HETATM 5951 O O     . HOH H 4 .   ? 19.673 -28.426 -37.141 1.00 40.58 ? 553 HOH B O     1 
HETATM 5952 O O     . HOH H 4 .   ? 44.298 13.607  -38.241 1.00 53.82 ? 554 HOH B O     1 
HETATM 5953 O O     . HOH H 4 .   ? 40.165 -12.259 -67.294 1.00 41.56 ? 555 HOH B O     1 
HETATM 5954 O O     . HOH H 4 .   ? 33.699 4.682   -44.576 1.00 41.15 ? 556 HOH B O     1 
HETATM 5955 O O     . HOH H 4 .   ? 39.058 -14.251 -21.556 1.00 39.68 ? 557 HOH B O     1 
HETATM 5956 O O     . HOH H 4 .   ? 31.717 -2.841  -19.717 1.00 31.88 ? 558 HOH B O     1 
HETATM 5957 O O     . HOH H 4 .   ? 29.830 -14.538 -54.968 1.00 36.49 ? 559 HOH B O     1 
HETATM 5958 O O     . HOH H 4 .   ? 52.194 0.416   -41.633 1.00 38.09 ? 560 HOH B O     1 
HETATM 5959 O O     . HOH H 4 .   ? 16.412 -13.808 -55.528 1.00 48.29 ? 561 HOH B O     1 
HETATM 5960 O O     . HOH H 4 .   ? 41.470 6.842   -54.440 1.00 29.00 ? 562 HOH B O     1 
HETATM 5961 O O     . HOH H 4 .   ? 39.144 9.602   -29.781 1.00 41.83 ? 563 HOH B O     1 
HETATM 5962 O O     . HOH H 4 .   ? 24.254 -0.357  -50.761 1.00 33.65 ? 564 HOH B O     1 
HETATM 5963 O O     . HOH H 4 .   ? 39.301 -5.460  -20.297 1.00 42.44 ? 565 HOH B O     1 
HETATM 5964 O O     . HOH H 4 .   ? 30.152 -11.317 -42.622 1.00 37.87 ? 566 HOH B O     1 
HETATM 5965 O O     . HOH H 4 .   ? 15.008 -11.182 -55.927 1.00 42.74 ? 567 HOH B O     1 
HETATM 5966 O O     . HOH H 4 .   ? 31.675 -26.808 -39.711 1.00 43.69 ? 568 HOH B O     1 
HETATM 5967 O O     . HOH H 4 .   ? 30.745 -19.696 -47.960 1.00 34.41 ? 569 HOH B O     1 
HETATM 5968 O O     . HOH H 4 .   ? 55.748 -13.420 -60.221 1.00 57.52 ? 570 HOH B O     1 
HETATM 5969 O O     . HOH H 4 .   ? 29.445 -4.119  -55.050 1.00 35.58 ? 571 HOH B O     1 
HETATM 5970 O O     . HOH H 4 .   ? 40.957 4.488   -60.785 1.00 37.00 ? 572 HOH B O     1 
HETATM 5971 O O     . HOH H 4 .   ? 49.553 14.950  -39.080 1.00 39.17 ? 573 HOH B O     1 
HETATM 5972 O O     . HOH H 4 .   ? 29.201 -0.632  -33.588 1.00 48.84 ? 574 HOH B O     1 
HETATM 5973 O O     . HOH H 4 .   ? 44.530 5.157   -66.175 1.00 44.64 ? 575 HOH B O     1 
HETATM 5974 O O     . HOH H 4 .   ? 37.560 -23.644 -30.515 1.00 43.16 ? 576 HOH B O     1 
HETATM 5975 O O     . HOH H 4 .   ? 53.658 -15.406 -38.781 1.00 47.51 ? 577 HOH B O     1 
HETATM 5976 O O     . HOH H 4 .   ? 38.184 14.858  -51.012 1.00 42.87 ? 578 HOH B O     1 
HETATM 5977 O O     . HOH H 4 .   ? 50.152 -0.482  -23.662 1.00 45.07 ? 579 HOH B O     1 
HETATM 5978 O O     . HOH H 4 .   ? 35.511 5.388   -25.986 1.00 41.88 ? 580 HOH B O     1 
HETATM 5979 O O     . HOH H 4 .   ? 45.026 4.135   -52.373 1.00 31.62 ? 581 HOH B O     1 
HETATM 5980 O O     . HOH H 4 .   ? 41.445 -18.920 -58.662 1.00 41.91 ? 582 HOH B O     1 
HETATM 5981 O O     . HOH H 4 .   ? 14.720 -19.612 -48.808 1.00 45.58 ? 583 HOH B O     1 
HETATM 5982 O O     . HOH H 4 .   ? 47.359 -0.061  -24.782 1.00 39.34 ? 584 HOH B O     1 
HETATM 5983 O O     . HOH H 4 .   ? 42.919 -1.856  -48.736 1.00 35.46 ? 585 HOH B O     1 
HETATM 5984 O O     . HOH H 4 .   ? 22.001 -1.469  -35.109 1.00 44.85 ? 586 HOH B O     1 
HETATM 5985 O O     . HOH H 4 .   ? 43.189 -2.833  -46.336 1.00 28.13 ? 587 HOH B O     1 
HETATM 5986 O O     . HOH H 4 .   ? 36.850 9.455   -30.666 1.00 49.90 ? 588 HOH B O     1 
HETATM 5987 O O     . HOH H 4 .   ? 18.091 -2.616  -53.466 1.00 41.10 ? 589 HOH B O     1 
HETATM 5988 O O     . HOH H 4 .   ? 34.150 -9.778  -59.746 1.00 36.63 ? 590 HOH B O     1 
HETATM 5989 O O     . HOH H 4 .   ? 29.426 -28.856 -48.249 1.00 45.62 ? 591 HOH B O     1 
HETATM 5990 O O     . HOH H 4 .   ? 50.381 -0.911  -36.164 1.00 37.96 ? 592 HOH B O     1 
HETATM 5991 O O     . HOH H 4 .   ? 22.244 -6.567  -44.844 1.00 29.99 ? 593 HOH B O     1 
HETATM 5992 O O     . HOH H 4 .   ? 25.987 -14.650 -50.541 1.00 35.23 ? 594 HOH B O     1 
HETATM 5993 O O     . HOH H 4 .   ? 41.456 2.921   -65.918 1.00 47.71 ? 595 HOH B O     1 
HETATM 5994 O O     . HOH H 4 .   ? 53.646 -17.792 -54.889 1.00 42.81 ? 596 HOH B O     1 
HETATM 5995 O O     . HOH H 4 .   ? 42.377 -2.421  -64.659 1.00 31.86 ? 597 HOH B O     1 
HETATM 5996 O O     . HOH H 4 .   ? 36.123 -16.407 -59.454 1.00 48.48 ? 598 HOH B O     1 
HETATM 5997 O O     . HOH H 4 .   ? 45.830 10.724  -60.446 1.00 52.34 ? 599 HOH B O     1 
HETATM 5998 O O     . HOH H 4 .   ? 33.723 0.651   -59.936 1.00 41.15 ? 600 HOH B O     1 
HETATM 5999 O O     . HOH H 4 .   ? 34.742 4.203   -56.739 1.00 36.59 ? 601 HOH B O     1 
HETATM 6000 O O     . HOH H 4 .   ? 47.499 -24.207 -43.335 1.00 38.38 ? 602 HOH B O     1 
HETATM 6001 O O     . HOH H 4 .   ? 44.464 -27.111 -37.929 1.00 42.00 ? 603 HOH B O     1 
HETATM 6002 O O     . HOH H 4 .   ? 20.254 -10.364 -58.782 1.00 41.81 ? 604 HOH B O     1 
HETATM 6003 O O     . HOH H 4 .   ? 55.889 6.732   -27.985 1.00 49.92 ? 605 HOH B O     1 
HETATM 6004 O O     . HOH H 4 .   ? 31.504 -12.650 -58.323 1.00 40.25 ? 606 HOH B O     1 
HETATM 6005 O O     . HOH H 4 .   ? 56.413 -9.469  -39.869 1.00 48.11 ? 607 HOH B O     1 
HETATM 6006 O O     . HOH H 4 .   ? 26.272 -14.599 -35.342 1.00 36.79 ? 608 HOH B O     1 
HETATM 6007 O O     . HOH H 4 .   ? 39.163 5.413   -38.186 1.00 28.50 ? 609 HOH B O     1 
HETATM 6008 O O     . HOH H 4 .   ? 18.729 -6.983  -28.685 1.00 55.29 ? 610 HOH B O     1 
HETATM 6009 O O     . HOH H 4 .   ? 23.533 -16.985 -35.196 1.00 36.50 ? 611 HOH B O     1 
HETATM 6010 O O     . HOH H 4 .   ? 54.954 13.603  -27.105 1.00 63.70 ? 612 HOH B O     1 
HETATM 6011 O O     . HOH H 4 .   ? 49.612 5.623   -53.126 1.00 40.14 ? 613 HOH B O     1 
HETATM 6012 O O     . HOH H 4 .   ? 33.189 -10.571 -57.628 1.00 26.69 ? 614 HOH B O     1 
HETATM 6013 O O     . HOH H 4 .   ? 14.632 -21.900 -46.664 1.00 47.19 ? 615 HOH B O     1 
HETATM 6014 O O     . HOH H 4 .   ? 33.950 -25.076 -20.378 1.00 62.51 ? 616 HOH B O     1 
HETATM 6015 O O     . HOH H 4 .   ? 59.441 -4.982  -49.445 1.00 37.65 ? 617 HOH B O     1 
HETATM 6016 O O     . HOH H 4 .   ? 22.270 0.211   -26.993 1.00 47.94 ? 618 HOH B O     1 
HETATM 6017 O O     . HOH H 4 .   ? 43.723 -3.775  -61.101 1.00 35.12 ? 619 HOH B O     1 
HETATM 6018 O O     . HOH H 4 .   ? 50.151 -0.886  -59.501 1.00 48.88 ? 620 HOH B O     1 
HETATM 6019 O O     . HOH H 4 .   ? 55.858 -11.608 -39.020 1.00 52.24 ? 621 HOH B O     1 
HETATM 6020 O O     . HOH H 4 .   ? 36.477 2.714   -26.880 1.00 39.74 ? 622 HOH B O     1 
HETATM 6021 O O     . HOH H 4 .   ? 54.071 -5.789  -56.992 1.00 37.14 ? 623 HOH B O     1 
HETATM 6022 O O     . HOH H 4 .   ? 19.383 -8.468  -49.982 1.00 35.02 ? 624 HOH B O     1 
HETATM 6023 O O     . HOH H 4 .   ? 52.290 4.246   -43.415 1.00 35.08 ? 625 HOH B O     1 
HETATM 6024 O O     . HOH H 4 .   ? 41.596 9.762   -58.243 1.00 45.01 ? 626 HOH B O     1 
HETATM 6025 O O     . HOH H 4 .   ? 51.806 -4.566  -24.728 1.00 42.25 ? 627 HOH B O     1 
HETATM 6026 O O     . HOH H 4 .   ? 40.976 -14.547 -21.259 1.00 37.36 ? 628 HOH B O     1 
HETATM 6027 O O     . HOH H 4 .   ? 56.109 3.014   -46.020 1.00 50.69 ? 629 HOH B O     1 
HETATM 6028 O O     . HOH H 4 .   ? 47.472 -23.829 -38.364 1.00 37.30 ? 630 HOH B O     1 
HETATM 6029 O O     . HOH H 4 .   ? 19.431 -5.089  -60.537 1.00 38.08 ? 631 HOH B O     1 
HETATM 6030 O O     . HOH H 4 .   ? 29.237 -9.363  -41.278 1.00 32.85 ? 632 HOH B O     1 
HETATM 6031 O O     . HOH H 4 .   ? 48.787 18.513  -47.825 1.00 34.88 ? 633 HOH B O     1 
HETATM 6032 O O     . HOH H 4 .   ? 27.117 -30.862 -40.733 1.00 35.54 ? 634 HOH B O     1 
HETATM 6033 O O     . HOH H 4 .   ? 36.053 12.509  -52.320 1.00 42.09 ? 635 HOH B O     1 
HETATM 6034 O O     . HOH H 4 .   ? 57.256 -11.351 -53.472 1.00 42.60 ? 636 HOH B O     1 
HETATM 6035 O O     . HOH H 4 .   ? 50.349 -10.828 -56.323 1.00 45.65 ? 637 HOH B O     1 
HETATM 6036 O O     . HOH H 4 .   ? 55.721 12.336  -25.727 1.00 58.37 ? 638 HOH B O     1 
HETATM 6037 O O     . HOH H 4 .   ? 43.228 -22.726 -58.036 1.00 40.88 ? 639 HOH B O     1 
HETATM 6038 O O     . HOH H 4 .   ? 22.915 3.404   -61.737 1.00 46.54 ? 640 HOH B O     1 
HETATM 6039 O O     . HOH H 4 .   ? 35.355 -12.274 -60.783 1.00 43.80 ? 641 HOH B O     1 
HETATM 6040 O O     . HOH H 4 .   ? 38.539 4.704   -28.410 1.00 46.22 ? 642 HOH B O     1 
HETATM 6041 O O     . HOH H 4 .   ? 42.682 5.145   -18.072 1.00 56.31 ? 643 HOH B O     1 
HETATM 6042 O O     . HOH H 4 .   ? 48.408 -5.552  -61.389 1.00 37.69 ? 644 HOH B O     1 
HETATM 6043 O O     . HOH H 4 .   ? 28.251 -1.856  -53.384 1.00 36.23 ? 645 HOH B O     1 
HETATM 6044 O O     . HOH H 4 .   ? 54.592 5.468   -42.949 1.00 32.90 ? 646 HOH B O     1 
HETATM 6045 O O     . HOH H 4 .   ? 17.473 -1.839  -23.074 1.00 49.17 ? 647 HOH B O     1 
HETATM 6046 O O     . HOH H 4 .   ? 43.105 -4.780  -22.292 1.00 47.78 ? 648 HOH B O     1 
HETATM 6047 O O     . HOH H 4 .   ? 33.460 7.956   -40.119 1.00 43.79 ? 649 HOH B O     1 
HETATM 6048 O O     . HOH H 4 .   ? 24.309 -20.613 -53.062 1.00 36.99 ? 650 HOH B O     1 
HETATM 6049 O O     . HOH H 4 .   ? 32.698 -16.372 -57.950 1.00 48.01 ? 651 HOH B O     1 
HETATM 6050 O O     . HOH H 4 .   ? 44.135 15.780  -35.701 1.00 47.33 ? 652 HOH B O     1 
HETATM 6051 O O     . HOH H 4 .   ? 59.913 15.103  -48.459 1.00 60.62 ? 653 HOH B O     1 
HETATM 6052 O O     . HOH H 4 .   ? 48.569 8.678   -62.323 1.00 40.83 ? 654 HOH B O     1 
HETATM 6053 O O     . HOH H 4 .   ? 19.128 -14.530 -24.789 1.00 48.09 ? 655 HOH B O     1 
HETATM 6054 O O     . HOH H 4 .   ? 60.763 -11.103 -47.000 1.00 46.84 ? 656 HOH B O     1 
HETATM 6055 O O     . HOH H 4 .   ? 18.307 -17.373 -24.443 1.00 48.03 ? 657 HOH B O     1 
HETATM 6056 O O     . HOH H 4 .   ? 32.408 5.326   -54.790 1.00 48.34 ? 658 HOH B O     1 
HETATM 6057 O O     . HOH H 4 .   ? 32.025 -0.350  -18.278 1.00 36.62 ? 659 HOH B O     1 
HETATM 6058 O O     . HOH H 4 .   ? 38.659 7.288   -27.682 1.00 53.63 ? 660 HOH B O     1 
HETATM 6059 O O     . HOH H 4 .   ? 33.163 -8.612  -63.959 1.00 34.00 ? 661 HOH B O     1 
HETATM 6060 O O     . HOH H 4 .   ? 30.736 1.302   -31.476 1.00 38.76 ? 662 HOH B O     1 
HETATM 6061 O O     . HOH H 4 .   ? 57.736 10.336  -26.229 1.00 62.06 ? 663 HOH B O     1 
HETATM 6062 O O     . HOH H 4 .   ? 31.301 1.297   -18.945 1.00 37.59 ? 664 HOH B O     1 
HETATM 6063 O O     . HOH H 4 .   ? 32.465 -20.996 -26.334 1.00 49.12 ? 665 HOH B O     1 
HETATM 6064 O O     . HOH H 4 .   ? 29.827 2.974   -54.514 1.00 45.15 ? 666 HOH B O     1 
HETATM 6065 O O     . HOH H 4 .   ? 28.963 0.338   -53.047 1.00 31.74 ? 667 HOH B O     1 
HETATM 6066 O O     . HOH H 4 .   ? 30.868 4.288   -56.427 1.00 41.57 ? 668 HOH B O     1 
HETATM 6067 O O     . HOH H 4 .   ? 62.104 -3.960  -49.007 1.00 51.52 ? 669 HOH B O     1 
HETATM 6068 O O     . HOH H 4 .   ? 32.770 3.280   -58.920 1.00 45.94 ? 670 HOH B O     1 
HETATM 6069 O O     . HOH H 4 .   ? 46.435 15.312  -38.799 1.00 42.23 ? 671 HOH B O     1 
HETATM 6070 O O     . HOH H 4 .   ? 44.450 -11.279 -66.748 1.00 51.17 ? 672 HOH B O     1 
HETATM 6071 O O     . HOH H 4 .   ? 14.429 -13.763 -26.014 1.00 59.65 ? 673 HOH B O     1 
HETATM 6072 O O     . HOH H 4 .   ? 32.008 -8.735  -61.631 1.00 38.56 ? 674 HOH B O     1 
HETATM 6073 O O     . HOH H 4 .   ? 60.552 -7.058  -51.383 1.00 48.09 ? 675 HOH B O     1 
HETATM 6074 O O     . HOH H 4 .   ? 32.796 -22.204 -28.541 1.00 39.83 ? 676 HOH B O     1 
HETATM 6075 O O     . HOH H 4 .   ? 59.749 8.442   -50.064 1.00 58.36 ? 677 HOH B O     1 
# 
