data_8QO8
# 
_entry.id   8QO8 
# 
_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   8QO8         pdb_00008qo8 10.2210/pdb8qo8/pdb 
WWPDB D_1292133641 ?            ?                   
# 
_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                        8QO8 
_pdbx_database_status.recvd_initial_deposition_date   2023-09-28 
_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 
PDB . 8QNP unspecified 
PDB . 8QNM unspecified 
PDB . 8QNW unspecified 
PDB . 8QNX unspecified 
PDB . 8QNY unspecified 
PDB . 8QO6 unspecified 
PDB . 8QO7 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'                     44373.121 2   ? ? ? ? 
2 non-polymer syn 'FLAVIN MONONUCLEOTIDE'                               456.344   2   ? ? ? ? 
3 non-polymer syn '1,4,5,6-Tetrahydronicotinamide adenine dinucleotide' 667.457   2   ? ? ? ? 
4 water       nat water                                                 18.015    743 ? ? ? ? 
# 
_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       
;HHHHHHMASSAQDGNNPLFSPYKMGKFNLSHRVVLAPMTRCRALNNIPQAALGEYYEQRATAGGFLITEGTMISPTSAGF
PHVPGIFTKEQVREWKKIVDVVHAKGAVIFCQLWHVGRASHEVYQPAGAAPISSTEKPISNRWRILMPDGTHGIYPKPRA
IGTYEISQVVEDYRRSALNAIEAGFDGIEIHGAHGYLIDQFLKDGINDRTDEYGGSLANRCKFITQVVQAVVSAIGADRV
GVRVSPAIDHLDAMDSNPLSLGLAVVERLNKIQLHSGSKLAYLHVTQPEYVAYGQTEAGRLGSEEEEARLMRTLRNAYQG
TFICSGGYTRELGIEAVAQGDADLVSYGRLFISNPDLVMRIKLNAPLNKYNRKTFYTQDPVVGYTDYPFLQGNGSNGPLS
RL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;HHHHHHMASSAQDGNNPLFSPYKMGKFNLSHRVVLAPMTRCRALNNIPQAALGEYYEQRATAGGFLITEGTMISPTSAGF
PHVPGIFTKEQVREWKKIVDVVHAKGAVIFCQLWHVGRASHEVYQPAGAAPISSTEKPISNRWRILMPDGTHGIYPKPRA
IGTYEISQVVEDYRRSALNAIEAGFDGIEIHGAHGYLIDQFLKDGINDRTDEYGGSLANRCKFITQVVQAVVSAIGADRV
GVRVSPAIDHLDAMDSNPLSLGLAVVERLNKIQLHSGSKLAYLHVTQPEYVAYGQTEAGRLGSEEEEARLMRTLRNAYQG
TFICSGGYTRELGIEAVAQGDADLVSYGRLFISNPDLVMRIKLNAPLNKYNRKTFYTQDPVVGYTDYPFLQGNGSNGPLS
RL
;
_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 '1,4,5,6-Tetrahydronicotinamide adenine dinucleotide' WI6 
4 water                                                 HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   HIS n 
1 2   HIS n 
1 3   HIS n 
1 4   HIS n 
1 5   HIS n 
1 6   HIS n 
1 7   MET n 
1 8   ALA n 
1 9   SER n 
1 10  SER n 
1 11  ALA n 
1 12  GLN n 
1 13  ASP n 
1 14  GLY n 
1 15  ASN n 
1 16  ASN n 
1 17  PRO n 
1 18  LEU n 
1 19  PHE n 
1 20  SER n 
1 21  PRO n 
1 22  TYR n 
1 23  LYS n 
1 24  MET n 
1 25  GLY n 
1 26  LYS n 
1 27  PHE n 
1 28  ASN n 
1 29  LEU n 
1 30  SER n 
1 31  HIS n 
1 32  ARG n 
1 33  VAL n 
1 34  VAL n 
1 35  LEU n 
1 36  ALA n 
1 37  PRO n 
1 38  MET n 
1 39  THR n 
1 40  ARG n 
1 41  CYS n 
1 42  ARG n 
1 43  ALA n 
1 44  LEU n 
1 45  ASN n 
1 46  ASN n 
1 47  ILE n 
1 48  PRO n 
1 49  GLN n 
1 50  ALA n 
1 51  ALA n 
1 52  LEU n 
1 53  GLY n 
1 54  GLU n 
1 55  TYR n 
1 56  TYR n 
1 57  GLU n 
1 58  GLN n 
1 59  ARG n 
1 60  ALA n 
1 61  THR n 
1 62  ALA n 
1 63  GLY n 
1 64  GLY n 
1 65  PHE n 
1 66  LEU n 
1 67  ILE n 
1 68  THR n 
1 69  GLU n 
1 70  GLY n 
1 71  THR n 
1 72  MET n 
1 73  ILE n 
1 74  SER n 
1 75  PRO n 
1 76  THR n 
1 77  SER n 
1 78  ALA n 
1 79  GLY n 
1 80  PHE n 
1 81  PRO n 
1 82  HIS n 
1 83  VAL n 
1 84  PRO n 
1 85  GLY n 
1 86  ILE n 
1 87  PHE n 
1 88  THR n 
1 89  LYS n 
1 90  GLU n 
1 91  GLN n 
1 92  VAL n 
1 93  ARG n 
1 94  GLU n 
1 95  TRP n 
1 96  LYS n 
1 97  LYS n 
1 98  ILE n 
1 99  VAL n 
1 100 ASP n 
1 101 VAL n 
1 102 VAL n 
1 103 HIS n 
1 104 ALA n 
1 105 LYS n 
1 106 GLY n 
1 107 ALA n 
1 108 VAL n 
1 109 ILE n 
1 110 PHE n 
1 111 CYS n 
1 112 GLN n 
1 113 LEU n 
1 114 TRP n 
1 115 HIS n 
1 116 VAL n 
1 117 GLY n 
1 118 ARG n 
1 119 ALA n 
1 120 SER n 
1 121 HIS n 
1 122 GLU n 
1 123 VAL n 
1 124 TYR n 
1 125 GLN n 
1 126 PRO n 
1 127 ALA n 
1 128 GLY n 
1 129 ALA n 
1 130 ALA n 
1 131 PRO n 
1 132 ILE n 
1 133 SER n 
1 134 SER n 
1 135 THR n 
1 136 GLU n 
1 137 LYS n 
1 138 PRO n 
1 139 ILE n 
1 140 SER n 
1 141 ASN n 
1 142 ARG n 
1 143 TRP n 
1 144 ARG n 
1 145 ILE n 
1 146 LEU n 
1 147 MET n 
1 148 PRO n 
1 149 ASP n 
1 150 GLY n 
1 151 THR n 
1 152 HIS n 
1 153 GLY n 
1 154 ILE n 
1 155 TYR n 
1 156 PRO n 
1 157 LYS n 
1 158 PRO n 
1 159 ARG n 
1 160 ALA n 
1 161 ILE n 
1 162 GLY n 
1 163 THR n 
1 164 TYR n 
1 165 GLU n 
1 166 ILE n 
1 167 SER n 
1 168 GLN n 
1 169 VAL n 
1 170 VAL n 
1 171 GLU n 
1 172 ASP n 
1 173 TYR n 
1 174 ARG n 
1 175 ARG n 
1 176 SER n 
1 177 ALA n 
1 178 LEU n 
1 179 ASN n 
1 180 ALA n 
1 181 ILE n 
1 182 GLU n 
1 183 ALA n 
1 184 GLY n 
1 185 PHE n 
1 186 ASP n 
1 187 GLY n 
1 188 ILE n 
1 189 GLU n 
1 190 ILE n 
1 191 HIS n 
1 192 GLY n 
1 193 ALA n 
1 194 HIS n 
1 195 GLY n 
1 196 TYR n 
1 197 LEU n 
1 198 ILE n 
1 199 ASP n 
1 200 GLN n 
1 201 PHE n 
1 202 LEU n 
1 203 LYS n 
1 204 ASP n 
1 205 GLY n 
1 206 ILE n 
1 207 ASN n 
1 208 ASP n 
1 209 ARG n 
1 210 THR n 
1 211 ASP n 
1 212 GLU n 
1 213 TYR n 
1 214 GLY n 
1 215 GLY n 
1 216 SER n 
1 217 LEU n 
1 218 ALA n 
1 219 ASN n 
1 220 ARG n 
1 221 CYS n 
1 222 LYS n 
1 223 PHE n 
1 224 ILE n 
1 225 THR n 
1 226 GLN n 
1 227 VAL n 
1 228 VAL n 
1 229 GLN n 
1 230 ALA n 
1 231 VAL n 
1 232 VAL n 
1 233 SER n 
1 234 ALA n 
1 235 ILE n 
1 236 GLY n 
1 237 ALA n 
1 238 ASP n 
1 239 ARG n 
1 240 VAL n 
1 241 GLY n 
1 242 VAL n 
1 243 ARG n 
1 244 VAL n 
1 245 SER n 
1 246 PRO n 
1 247 ALA n 
1 248 ILE n 
1 249 ASP n 
1 250 HIS n 
1 251 LEU n 
1 252 ASP n 
1 253 ALA n 
1 254 MET n 
1 255 ASP n 
1 256 SER n 
1 257 ASN n 
1 258 PRO n 
1 259 LEU n 
1 260 SER n 
1 261 LEU n 
1 262 GLY n 
1 263 LEU n 
1 264 ALA n 
1 265 VAL n 
1 266 VAL n 
1 267 GLU n 
1 268 ARG n 
1 269 LEU n 
1 270 ASN n 
1 271 LYS n 
1 272 ILE n 
1 273 GLN n 
1 274 LEU n 
1 275 HIS n 
1 276 SER n 
1 277 GLY n 
1 278 SER n 
1 279 LYS n 
1 280 LEU n 
1 281 ALA n 
1 282 TYR n 
1 283 LEU n 
1 284 HIS n 
1 285 VAL n 
1 286 THR n 
1 287 GLN n 
1 288 PRO n 
1 289 GLU n 
1 290 TYR n 
1 291 VAL n 
1 292 ALA n 
1 293 TYR n 
1 294 GLY n 
1 295 GLN n 
1 296 THR n 
1 297 GLU n 
1 298 ALA n 
1 299 GLY n 
1 300 ARG n 
1 301 LEU n 
1 302 GLY n 
1 303 SER n 
1 304 GLU n 
1 305 GLU n 
1 306 GLU n 
1 307 GLU n 
1 308 ALA n 
1 309 ARG n 
1 310 LEU n 
1 311 MET n 
1 312 ARG n 
1 313 THR n 
1 314 LEU n 
1 315 ARG n 
1 316 ASN n 
1 317 ALA n 
1 318 TYR n 
1 319 GLN n 
1 320 GLY n 
1 321 THR n 
1 322 PHE n 
1 323 ILE n 
1 324 CYS n 
1 325 SER n 
1 326 GLY n 
1 327 GLY n 
1 328 TYR n 
1 329 THR n 
1 330 ARG n 
1 331 GLU n 
1 332 LEU n 
1 333 GLY n 
1 334 ILE n 
1 335 GLU n 
1 336 ALA n 
1 337 VAL n 
1 338 ALA n 
1 339 GLN n 
1 340 GLY n 
1 341 ASP n 
1 342 ALA n 
1 343 ASP n 
1 344 LEU n 
1 345 VAL n 
1 346 SER n 
1 347 TYR n 
1 348 GLY n 
1 349 ARG n 
1 350 LEU n 
1 351 PHE n 
1 352 ILE n 
1 353 SER n 
1 354 ASN n 
1 355 PRO n 
1 356 ASP n 
1 357 LEU n 
1 358 VAL n 
1 359 MET n 
1 360 ARG n 
1 361 ILE n 
1 362 LYS n 
1 363 LEU n 
1 364 ASN n 
1 365 ALA n 
1 366 PRO n 
1 367 LEU n 
1 368 ASN n 
1 369 LYS n 
1 370 TYR n 
1 371 ASN n 
1 372 ARG n 
1 373 LYS n 
1 374 THR n 
1 375 PHE n 
1 376 TYR n 
1 377 THR n 
1 378 GLN n 
1 379 ASP n 
1 380 PRO n 
1 381 VAL n 
1 382 VAL n 
1 383 GLY n 
1 384 TYR n 
1 385 THR n 
1 386 ASP n 
1 387 TYR n 
1 388 PRO n 
1 389 PHE n 
1 390 LEU n 
1 391 GLN n 
1 392 GLY n 
1 393 ASN n 
1 394 GLY n 
1 395 SER n 
1 396 ASN n 
1 397 GLY n 
1 398 PRO n 
1 399 LEU n 
1 400 SER n 
1 401 ARG n 
1 402 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                   402 
_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 
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 
WI6 non-polymer         . '1,4,5,6-Tetrahydronicotinamide adenine dinucleotide' 
;[[(2R,3S,4R,5R)-5-[(3S)-3-aminocarbonyl-3,6-dihydro-2H-pyridin-1-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] [(2S,3R,4S,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl hydrogen phosphate
;
'C21 H31 N7 O14 P2' 667.457 
# 
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   HIS 1   -5  ?   ?   ?   A . n 
A 1 2   HIS 2   -4  ?   ?   ?   A . n 
A 1 3   HIS 3   -3  ?   ?   ?   A . n 
A 1 4   HIS 4   -2  ?   ?   ?   A . n 
A 1 5   HIS 5   -1  ?   ?   ?   A . n 
A 1 6   HIS 6   0   ?   ?   ?   A . n 
A 1 7   MET 7   1   ?   ?   ?   A . n 
A 1 8   ALA 8   2   ?   ?   ?   A . n 
A 1 9   SER 9   3   ?   ?   ?   A . n 
A 1 10  SER 10  4   ?   ?   ?   A . n 
A 1 11  ALA 11  5   ?   ?   ?   A . n 
A 1 12  GLN 12  6   ?   ?   ?   A . n 
A 1 13  ASP 13  7   ?   ?   ?   A . n 
A 1 14  GLY 14  8   ?   ?   ?   A . n 
A 1 15  ASN 15  9   ?   ?   ?   A . n 
A 1 16  ASN 16  10  10  ASN ASN A . n 
A 1 17  PRO 17  11  11  PRO PRO A . n 
A 1 18  LEU 18  12  12  LEU LEU A . n 
A 1 19  PHE 19  13  13  PHE PHE A . n 
A 1 20  SER 20  14  14  SER SER A . n 
A 1 21  PRO 21  15  15  PRO PRO A . n 
A 1 22  TYR 22  16  16  TYR TYR A . n 
A 1 23  LYS 23  17  17  LYS LYS A . n 
A 1 24  MET 24  18  18  MET MET A . n 
A 1 25  GLY 25  19  19  GLY GLY A . n 
A 1 26  LYS 26  20  20  LYS LYS A . n 
A 1 27  PHE 27  21  21  PHE PHE A . n 
A 1 28  ASN 28  22  22  ASN ASN A . n 
A 1 29  LEU 29  23  23  LEU LEU A . n 
A 1 30  SER 30  24  24  SER SER A . n 
A 1 31  HIS 31  25  25  HIS HIS A . n 
A 1 32  ARG 32  26  26  ARG ARG A . n 
A 1 33  VAL 33  27  27  VAL VAL A . n 
A 1 34  VAL 34  28  28  VAL VAL A . n 
A 1 35  LEU 35  29  29  LEU LEU A . n 
A 1 36  ALA 36  30  30  ALA ALA A . n 
A 1 37  PRO 37  31  31  PRO PRO A . n 
A 1 38  MET 38  32  32  MET MET A . n 
A 1 39  THR 39  33  33  THR THR A . n 
A 1 40  ARG 40  34  34  ARG ARG A . n 
A 1 41  CYS 41  35  35  CYS CYS A . n 
A 1 42  ARG 42  36  36  ARG ARG A . n 
A 1 43  ALA 43  37  37  ALA ALA A . n 
A 1 44  LEU 44  38  38  LEU LEU A . n 
A 1 45  ASN 45  39  39  ASN ASN A . n 
A 1 46  ASN 46  40  40  ASN ASN A . n 
A 1 47  ILE 47  41  41  ILE ILE A . n 
A 1 48  PRO 48  42  42  PRO PRO A . n 
A 1 49  GLN 49  43  43  GLN GLN A . n 
A 1 50  ALA 50  44  44  ALA ALA A . n 
A 1 51  ALA 51  45  45  ALA ALA A . n 
A 1 52  LEU 52  46  46  LEU LEU A . n 
A 1 53  GLY 53  47  47  GLY GLY A . n 
A 1 54  GLU 54  48  48  GLU GLU A . n 
A 1 55  TYR 55  49  49  TYR TYR A . n 
A 1 56  TYR 56  50  50  TYR TYR A . n 
A 1 57  GLU 57  51  51  GLU GLU A . n 
A 1 58  GLN 58  52  52  GLN GLN A . n 
A 1 59  ARG 59  53  53  ARG ARG A . n 
A 1 60  ALA 60  54  54  ALA ALA A . n 
A 1 61  THR 61  55  55  THR THR A . n 
A 1 62  ALA 62  56  56  ALA ALA A . n 
A 1 63  GLY 63  57  57  GLY GLY A . n 
A 1 64  GLY 64  58  58  GLY GLY A . n 
A 1 65  PHE 65  59  59  PHE PHE A . n 
A 1 66  LEU 66  60  60  LEU LEU A . n 
A 1 67  ILE 67  61  61  ILE ILE A . n 
A 1 68  THR 68  62  62  THR THR A . n 
A 1 69  GLU 69  63  63  GLU GLU A . n 
A 1 70  GLY 70  64  64  GLY GLY A . n 
A 1 71  THR 71  65  65  THR THR A . n 
A 1 72  MET 72  66  66  MET MET A . n 
A 1 73  ILE 73  67  67  ILE ILE A . n 
A 1 74  SER 74  68  68  SER SER A . n 
A 1 75  PRO 75  69  69  PRO PRO A . n 
A 1 76  THR 76  70  70  THR THR A . n 
A 1 77  SER 77  71  71  SER SER A . n 
A 1 78  ALA 78  72  72  ALA ALA A . n 
A 1 79  GLY 79  73  73  GLY GLY A . n 
A 1 80  PHE 80  74  74  PHE PHE A . n 
A 1 81  PRO 81  75  75  PRO PRO A . n 
A 1 82  HIS 82  76  76  HIS HIS A . n 
A 1 83  VAL 83  77  77  VAL VAL A . n 
A 1 84  PRO 84  78  78  PRO PRO A . n 
A 1 85  GLY 85  79  79  GLY GLY A . n 
A 1 86  ILE 86  80  80  ILE ILE A . n 
A 1 87  PHE 87  81  81  PHE PHE A . n 
A 1 88  THR 88  82  82  THR THR A . n 
A 1 89  LYS 89  83  83  LYS LYS A . n 
A 1 90  GLU 90  84  84  GLU GLU A . n 
A 1 91  GLN 91  85  85  GLN GLN A . n 
A 1 92  VAL 92  86  86  VAL VAL A . n 
A 1 93  ARG 93  87  87  ARG ARG A . n 
A 1 94  GLU 94  88  88  GLU GLU A . n 
A 1 95  TRP 95  89  89  TRP TRP A . n 
A 1 96  LYS 96  90  90  LYS LYS A . n 
A 1 97  LYS 97  91  91  LYS LYS A . n 
A 1 98  ILE 98  92  92  ILE ILE A . n 
A 1 99  VAL 99  93  93  VAL VAL A . n 
A 1 100 ASP 100 94  94  ASP ASP A . n 
A 1 101 VAL 101 95  95  VAL VAL A . n 
A 1 102 VAL 102 96  96  VAL VAL A . n 
A 1 103 HIS 103 97  97  HIS HIS A . n 
A 1 104 ALA 104 98  98  ALA ALA A . n 
A 1 105 LYS 105 99  99  LYS LYS A . n 
A 1 106 GLY 106 100 100 GLY GLY A . n 
A 1 107 ALA 107 101 101 ALA ALA A . n 
A 1 108 VAL 108 102 102 VAL VAL A . n 
A 1 109 ILE 109 103 103 ILE ILE A . n 
A 1 110 PHE 110 104 104 PHE PHE A . n 
A 1 111 CYS 111 105 105 CYS CYS A . n 
A 1 112 GLN 112 106 106 GLN GLN A . n 
A 1 113 LEU 113 107 107 LEU LEU A . n 
A 1 114 TRP 114 108 108 TRP TRP A . n 
A 1 115 HIS 115 109 109 HIS HIS A . n 
A 1 116 VAL 116 110 110 VAL VAL A . n 
A 1 117 GLY 117 111 111 GLY GLY A . n 
A 1 118 ARG 118 112 112 ARG ARG A . n 
A 1 119 ALA 119 113 113 ALA ALA A . n 
A 1 120 SER 120 114 114 SER SER A . n 
A 1 121 HIS 121 115 115 HIS HIS A . n 
A 1 122 GLU 122 116 116 GLU GLU A . n 
A 1 123 VAL 123 117 117 VAL VAL A . n 
A 1 124 TYR 124 118 118 TYR TYR A . n 
A 1 125 GLN 125 119 119 GLN GLN A . n 
A 1 126 PRO 126 120 120 PRO PRO A . n 
A 1 127 ALA 127 121 121 ALA ALA A . n 
A 1 128 GLY 128 122 122 GLY GLY A . n 
A 1 129 ALA 129 123 123 ALA ALA A . n 
A 1 130 ALA 130 124 124 ALA ALA A . n 
A 1 131 PRO 131 125 125 PRO PRO A . n 
A 1 132 ILE 132 126 126 ILE ILE A . n 
A 1 133 SER 133 127 127 SER SER A . n 
A 1 134 SER 134 128 128 SER SER A . n 
A 1 135 THR 135 129 129 THR THR A . n 
A 1 136 GLU 136 130 130 GLU GLU A . n 
A 1 137 LYS 137 131 131 LYS LYS A . n 
A 1 138 PRO 138 132 132 PRO PRO A . n 
A 1 139 ILE 139 133 133 ILE ILE A . n 
A 1 140 SER 140 134 134 SER SER A . n 
A 1 141 ASN 141 135 135 ASN ASN A . n 
A 1 142 ARG 142 136 136 ARG ARG A . n 
A 1 143 TRP 143 137 137 TRP TRP A . n 
A 1 144 ARG 144 138 138 ARG ARG A . n 
A 1 145 ILE 145 139 139 ILE ILE A . n 
A 1 146 LEU 146 140 140 LEU LEU A . n 
A 1 147 MET 147 141 141 MET MET A . n 
A 1 148 PRO 148 142 142 PRO PRO A . n 
A 1 149 ASP 149 143 143 ASP ASP A . n 
A 1 150 GLY 150 144 144 GLY GLY A . n 
A 1 151 THR 151 145 145 THR THR A . n 
A 1 152 HIS 152 146 146 HIS HIS A . n 
A 1 153 GLY 153 147 147 GLY GLY A . n 
A 1 154 ILE 154 148 148 ILE ILE A . n 
A 1 155 TYR 155 149 149 TYR TYR A . n 
A 1 156 PRO 156 150 150 PRO PRO A . n 
A 1 157 LYS 157 151 151 LYS LYS A . n 
A 1 158 PRO 158 152 152 PRO PRO A . n 
A 1 159 ARG 159 153 153 ARG ARG A . n 
A 1 160 ALA 160 154 154 ALA ALA A . n 
A 1 161 ILE 161 155 155 ILE ILE A . n 
A 1 162 GLY 162 156 156 GLY GLY A . n 
A 1 163 THR 163 157 157 THR THR A . n 
A 1 164 TYR 164 158 158 TYR TYR A . n 
A 1 165 GLU 165 159 159 GLU GLU A . n 
A 1 166 ILE 166 160 160 ILE ILE A . n 
A 1 167 SER 167 161 161 SER SER A . n 
A 1 168 GLN 168 162 162 GLN GLN A . n 
A 1 169 VAL 169 163 163 VAL VAL A . n 
A 1 170 VAL 170 164 164 VAL VAL A . n 
A 1 171 GLU 171 165 165 GLU GLU A . n 
A 1 172 ASP 172 166 166 ASP ASP A . n 
A 1 173 TYR 173 167 167 TYR TYR A . n 
A 1 174 ARG 174 168 168 ARG ARG A . n 
A 1 175 ARG 175 169 169 ARG ARG A . n 
A 1 176 SER 176 170 170 SER SER A . n 
A 1 177 ALA 177 171 171 ALA ALA A . n 
A 1 178 LEU 178 172 172 LEU LEU A . n 
A 1 179 ASN 179 173 173 ASN ASN A . n 
A 1 180 ALA 180 174 174 ALA ALA A . n 
A 1 181 ILE 181 175 175 ILE ILE A . n 
A 1 182 GLU 182 176 176 GLU GLU A . n 
A 1 183 ALA 183 177 177 ALA ALA A . n 
A 1 184 GLY 184 178 178 GLY GLY A . n 
A 1 185 PHE 185 179 179 PHE PHE A . n 
A 1 186 ASP 186 180 180 ASP ASP A . n 
A 1 187 GLY 187 181 181 GLY GLY A . n 
A 1 188 ILE 188 182 182 ILE ILE A . n 
A 1 189 GLU 189 183 183 GLU GLU A . n 
A 1 190 ILE 190 184 184 ILE ILE A . n 
A 1 191 HIS 191 185 185 HIS HIS A . n 
A 1 192 GLY 192 186 186 GLY GLY A . n 
A 1 193 ALA 193 187 187 ALA ALA A . n 
A 1 194 HIS 194 188 188 HIS HIS A . n 
A 1 195 GLY 195 189 189 GLY GLY A . n 
A 1 196 TYR 196 190 190 TYR TYR A . n 
A 1 197 LEU 197 191 191 LEU LEU A . n 
A 1 198 ILE 198 192 192 ILE ILE A . n 
A 1 199 ASP 199 193 193 ASP ASP A . n 
A 1 200 GLN 200 194 194 GLN GLN A . n 
A 1 201 PHE 201 195 195 PHE PHE A . n 
A 1 202 LEU 202 196 196 LEU LEU A . n 
A 1 203 LYS 203 197 197 LYS LYS A . n 
A 1 204 ASP 204 198 198 ASP ASP A . n 
A 1 205 GLY 205 199 199 GLY GLY A . n 
A 1 206 ILE 206 200 200 ILE ILE A . n 
A 1 207 ASN 207 201 201 ASN ASN A . n 
A 1 208 ASP 208 202 202 ASP ASP A . n 
A 1 209 ARG 209 203 203 ARG ARG A . n 
A 1 210 THR 210 204 204 THR THR A . n 
A 1 211 ASP 211 205 205 ASP ASP A . n 
A 1 212 GLU 212 206 206 GLU GLU A . n 
A 1 213 TYR 213 207 207 TYR TYR A . n 
A 1 214 GLY 214 208 208 GLY GLY A . n 
A 1 215 GLY 215 209 209 GLY GLY A . n 
A 1 216 SER 216 210 210 SER SER A . n 
A 1 217 LEU 217 211 211 LEU LEU A . n 
A 1 218 ALA 218 212 212 ALA ALA A . n 
A 1 219 ASN 219 213 213 ASN ASN A . n 
A 1 220 ARG 220 214 214 ARG ARG A . n 
A 1 221 CYS 221 215 215 CYS CYS A . n 
A 1 222 LYS 222 216 216 LYS LYS A . n 
A 1 223 PHE 223 217 217 PHE PHE A . n 
A 1 224 ILE 224 218 218 ILE ILE A . n 
A 1 225 THR 225 219 219 THR THR A . n 
A 1 226 GLN 226 220 220 GLN GLN A . n 
A 1 227 VAL 227 221 221 VAL VAL A . n 
A 1 228 VAL 228 222 222 VAL VAL A . n 
A 1 229 GLN 229 223 223 GLN GLN A . n 
A 1 230 ALA 230 224 224 ALA ALA A . n 
A 1 231 VAL 231 225 225 VAL VAL A . n 
A 1 232 VAL 232 226 226 VAL VAL A . n 
A 1 233 SER 233 227 227 SER SER A . n 
A 1 234 ALA 234 228 228 ALA ALA A . n 
A 1 235 ILE 235 229 229 ILE ILE A . n 
A 1 236 GLY 236 230 230 GLY GLY A . n 
A 1 237 ALA 237 231 231 ALA ALA A . n 
A 1 238 ASP 238 232 232 ASP ASP A . n 
A 1 239 ARG 239 233 233 ARG ARG A . n 
A 1 240 VAL 240 234 234 VAL VAL A . n 
A 1 241 GLY 241 235 235 GLY GLY A . n 
A 1 242 VAL 242 236 236 VAL VAL A . n 
A 1 243 ARG 243 237 237 ARG ARG A . n 
A 1 244 VAL 244 238 238 VAL VAL A . n 
A 1 245 SER 245 239 239 SER SER A . n 
A 1 246 PRO 246 240 240 PRO PRO A . n 
A 1 247 ALA 247 241 241 ALA ALA A . n 
A 1 248 ILE 248 242 242 ILE ILE A . n 
A 1 249 ASP 249 243 243 ASP ASP A . n 
A 1 250 HIS 250 244 244 HIS HIS A . n 
A 1 251 LEU 251 245 245 LEU LEU A . n 
A 1 252 ASP 252 246 246 ASP ASP A . n 
A 1 253 ALA 253 247 247 ALA ALA A . n 
A 1 254 MET 254 248 248 MET MET A . n 
A 1 255 ASP 255 249 249 ASP ASP A . n 
A 1 256 SER 256 250 250 SER SER A . n 
A 1 257 ASN 257 251 251 ASN ASN A . n 
A 1 258 PRO 258 252 252 PRO PRO A . n 
A 1 259 LEU 259 253 253 LEU LEU A . n 
A 1 260 SER 260 254 254 SER SER A . n 
A 1 261 LEU 261 255 255 LEU LEU A . n 
A 1 262 GLY 262 256 256 GLY GLY A . n 
A 1 263 LEU 263 257 257 LEU LEU A . n 
A 1 264 ALA 264 258 258 ALA ALA A . n 
A 1 265 VAL 265 259 259 VAL VAL A . n 
A 1 266 VAL 266 260 260 VAL VAL A . n 
A 1 267 GLU 267 261 261 GLU GLU A . n 
A 1 268 ARG 268 262 262 ARG ARG A . n 
A 1 269 LEU 269 263 263 LEU LEU A . n 
A 1 270 ASN 270 264 264 ASN ASN A . n 
A 1 271 LYS 271 265 265 LYS LYS A . n 
A 1 272 ILE 272 266 266 ILE ILE A . n 
A 1 273 GLN 273 267 267 GLN GLN A . n 
A 1 274 LEU 274 268 268 LEU LEU A . n 
A 1 275 HIS 275 269 269 HIS HIS A . n 
A 1 276 SER 276 270 270 SER SER A . n 
A 1 277 GLY 277 271 271 GLY GLY A . n 
A 1 278 SER 278 272 272 SER SER A . n 
A 1 279 LYS 279 273 273 LYS LYS A . n 
A 1 280 LEU 280 274 274 LEU LEU A . n 
A 1 281 ALA 281 275 275 ALA ALA A . n 
A 1 282 TYR 282 276 276 TYR TYR A . n 
A 1 283 LEU 283 277 277 LEU LEU A . n 
A 1 284 HIS 284 278 278 HIS HIS A . n 
A 1 285 VAL 285 279 279 VAL VAL A . n 
A 1 286 THR 286 280 280 THR THR A . n 
A 1 287 GLN 287 281 281 GLN GLN A . n 
A 1 288 PRO 288 282 282 PRO PRO A . n 
A 1 289 GLU 289 283 283 GLU GLU A . n 
A 1 290 TYR 290 284 ?   ?   ?   A . n 
A 1 291 VAL 291 285 ?   ?   ?   A . n 
A 1 292 ALA 292 286 ?   ?   ?   A . n 
A 1 293 TYR 293 287 ?   ?   ?   A . n 
A 1 294 GLY 294 288 ?   ?   ?   A . n 
A 1 295 GLN 295 289 ?   ?   ?   A . n 
A 1 296 THR 296 290 ?   ?   ?   A . n 
A 1 297 GLU 297 291 ?   ?   ?   A . n 
A 1 298 ALA 298 292 ?   ?   ?   A . n 
A 1 299 GLY 299 293 ?   ?   ?   A . n 
A 1 300 ARG 300 294 ?   ?   ?   A . n 
A 1 301 LEU 301 295 ?   ?   ?   A . n 
A 1 302 GLY 302 296 ?   ?   ?   A . n 
A 1 303 SER 303 297 ?   ?   ?   A . n 
A 1 304 GLU 304 298 ?   ?   ?   A . n 
A 1 305 GLU 305 299 ?   ?   ?   A . n 
A 1 306 GLU 306 300 ?   ?   ?   A . n 
A 1 307 GLU 307 301 ?   ?   ?   A . n 
A 1 308 ALA 308 302 ?   ?   ?   A . n 
A 1 309 ARG 309 303 303 ARG ARG A . n 
A 1 310 LEU 310 304 304 LEU LEU A . n 
A 1 311 MET 311 305 305 MET MET A . n 
A 1 312 ARG 312 306 306 ARG ARG A . n 
A 1 313 THR 313 307 307 THR THR A . n 
A 1 314 LEU 314 308 308 LEU LEU A . n 
A 1 315 ARG 315 309 309 ARG ARG A . n 
A 1 316 ASN 316 310 310 ASN ASN A . n 
A 1 317 ALA 317 311 311 ALA ALA A . n 
A 1 318 TYR 318 312 312 TYR TYR A . n 
A 1 319 GLN 319 313 313 GLN GLN A . n 
A 1 320 GLY 320 314 314 GLY GLY A . n 
A 1 321 THR 321 315 315 THR THR A . n 
A 1 322 PHE 322 316 316 PHE PHE A . n 
A 1 323 ILE 323 317 317 ILE ILE A . n 
A 1 324 CYS 324 318 318 CYS CYS A . n 
A 1 325 SER 325 319 319 SER SER A . n 
A 1 326 GLY 326 320 320 GLY GLY A . n 
A 1 327 GLY 327 321 321 GLY GLY A . n 
A 1 328 TYR 328 322 322 TYR TYR A . n 
A 1 329 THR 329 323 323 THR THR A . n 
A 1 330 ARG 330 324 324 ARG ARG A . n 
A 1 331 GLU 331 325 325 GLU GLU A . n 
A 1 332 LEU 332 326 326 LEU LEU A . n 
A 1 333 GLY 333 327 327 GLY GLY A . n 
A 1 334 ILE 334 328 328 ILE ILE A . n 
A 1 335 GLU 335 329 329 GLU GLU A . n 
A 1 336 ALA 336 330 330 ALA ALA A . n 
A 1 337 VAL 337 331 331 VAL VAL A . n 
A 1 338 ALA 338 332 332 ALA ALA A . n 
A 1 339 GLN 339 333 333 GLN GLN A . n 
A 1 340 GLY 340 334 334 GLY GLY A . n 
A 1 341 ASP 341 335 335 ASP ASP A . n 
A 1 342 ALA 342 336 336 ALA ALA A . n 
A 1 343 ASP 343 337 337 ASP ASP A . n 
A 1 344 LEU 344 338 338 LEU LEU A . n 
A 1 345 VAL 345 339 339 VAL VAL A . n 
A 1 346 SER 346 340 340 SER SER A . n 
A 1 347 TYR 347 341 341 TYR TYR A . n 
A 1 348 GLY 348 342 342 GLY GLY A . n 
A 1 349 ARG 349 343 343 ARG ARG A . n 
A 1 350 LEU 350 344 344 LEU LEU A . n 
A 1 351 PHE 351 345 345 PHE PHE A . n 
A 1 352 ILE 352 346 346 ILE ILE A . n 
A 1 353 SER 353 347 347 SER SER A . n 
A 1 354 ASN 354 348 348 ASN ASN A . n 
A 1 355 PRO 355 349 349 PRO PRO A . n 
A 1 356 ASP 356 350 350 ASP ASP A . n 
A 1 357 LEU 357 351 351 LEU LEU A . n 
A 1 358 VAL 358 352 352 VAL VAL A . n 
A 1 359 MET 359 353 353 MET MET A . n 
A 1 360 ARG 360 354 354 ARG ARG A . n 
A 1 361 ILE 361 355 355 ILE ILE A . n 
A 1 362 LYS 362 356 356 LYS LYS A . n 
A 1 363 LEU 363 357 357 LEU LEU A . n 
A 1 364 ASN 364 358 358 ASN ASN A . n 
A 1 365 ALA 365 359 359 ALA ALA A . n 
A 1 366 PRO 366 360 360 PRO PRO A . n 
A 1 367 LEU 367 361 361 LEU LEU A . n 
A 1 368 ASN 368 362 362 ASN ASN A . n 
A 1 369 LYS 369 363 363 LYS LYS A . n 
A 1 370 TYR 370 364 364 TYR TYR A . n 
A 1 371 ASN 371 365 365 ASN ASN A . n 
A 1 372 ARG 372 366 366 ARG ARG A . n 
A 1 373 LYS 373 367 367 LYS LYS A . n 
A 1 374 THR 374 368 368 THR THR A . n 
A 1 375 PHE 375 369 369 PHE PHE A . n 
A 1 376 TYR 376 370 370 TYR TYR A . n 
A 1 377 THR 377 371 371 THR THR A . n 
A 1 378 GLN 378 372 372 GLN GLN A . n 
A 1 379 ASP 379 373 373 ASP ASP A . n 
A 1 380 PRO 380 374 374 PRO PRO A . n 
A 1 381 VAL 381 375 375 VAL VAL A . n 
A 1 382 VAL 382 376 376 VAL VAL A . n 
A 1 383 GLY 383 377 377 GLY GLY A . n 
A 1 384 TYR 384 378 378 TYR TYR A . n 
A 1 385 THR 385 379 379 THR THR A . n 
A 1 386 ASP 386 380 380 ASP ASP A . n 
A 1 387 TYR 387 381 381 TYR TYR A . n 
A 1 388 PRO 388 382 382 PRO PRO A . n 
A 1 389 PHE 389 383 383 PHE PHE A . n 
A 1 390 LEU 390 384 384 LEU LEU A . n 
A 1 391 GLN 391 385 ?   ?   ?   A . n 
A 1 392 GLY 392 386 ?   ?   ?   A . n 
A 1 393 ASN 393 387 ?   ?   ?   A . n 
A 1 394 GLY 394 388 ?   ?   ?   A . n 
A 1 395 SER 395 389 ?   ?   ?   A . n 
A 1 396 ASN 396 390 ?   ?   ?   A . n 
A 1 397 GLY 397 391 ?   ?   ?   A . n 
A 1 398 PRO 398 392 ?   ?   ?   A . n 
A 1 399 LEU 399 393 ?   ?   ?   A . n 
A 1 400 SER 400 394 ?   ?   ?   A . n 
A 1 401 ARG 401 395 ?   ?   ?   A . n 
A 1 402 LEU 402 396 ?   ?   ?   A . n 
B 1 1   HIS 1   -5  ?   ?   ?   B . n 
B 1 2   HIS 2   -4  ?   ?   ?   B . n 
B 1 3   HIS 3   -3  ?   ?   ?   B . n 
B 1 4   HIS 4   -2  ?   ?   ?   B . n 
B 1 5   HIS 5   -1  ?   ?   ?   B . n 
B 1 6   HIS 6   0   ?   ?   ?   B . n 
B 1 7   MET 7   1   ?   ?   ?   B . n 
B 1 8   ALA 8   2   ?   ?   ?   B . n 
B 1 9   SER 9   3   ?   ?   ?   B . n 
B 1 10  SER 10  4   ?   ?   ?   B . n 
B 1 11  ALA 11  5   ?   ?   ?   B . n 
B 1 12  GLN 12  6   ?   ?   ?   B . n 
B 1 13  ASP 13  7   ?   ?   ?   B . n 
B 1 14  GLY 14  8   ?   ?   ?   B . n 
B 1 15  ASN 15  9   ?   ?   ?   B . n 
B 1 16  ASN 16  10  10  ASN ASN B . n 
B 1 17  PRO 17  11  11  PRO PRO B . n 
B 1 18  LEU 18  12  12  LEU LEU B . n 
B 1 19  PHE 19  13  13  PHE PHE B . n 
B 1 20  SER 20  14  14  SER SER B . n 
B 1 21  PRO 21  15  15  PRO PRO B . n 
B 1 22  TYR 22  16  16  TYR TYR B . n 
B 1 23  LYS 23  17  17  LYS LYS B . n 
B 1 24  MET 24  18  18  MET MET B . n 
B 1 25  GLY 25  19  19  GLY GLY B . n 
B 1 26  LYS 26  20  20  LYS LYS B . n 
B 1 27  PHE 27  21  21  PHE PHE B . n 
B 1 28  ASN 28  22  22  ASN ASN B . n 
B 1 29  LEU 29  23  23  LEU LEU B . n 
B 1 30  SER 30  24  24  SER SER B . n 
B 1 31  HIS 31  25  25  HIS HIS B . n 
B 1 32  ARG 32  26  26  ARG ARG B . n 
B 1 33  VAL 33  27  27  VAL VAL B . n 
B 1 34  VAL 34  28  28  VAL VAL B . n 
B 1 35  LEU 35  29  29  LEU LEU B . n 
B 1 36  ALA 36  30  30  ALA ALA B . n 
B 1 37  PRO 37  31  31  PRO PRO B . n 
B 1 38  MET 38  32  32  MET MET B . n 
B 1 39  THR 39  33  33  THR THR B . n 
B 1 40  ARG 40  34  34  ARG ARG B . n 
B 1 41  CYS 41  35  35  CYS CYS B . n 
B 1 42  ARG 42  36  36  ARG ARG B . n 
B 1 43  ALA 43  37  37  ALA ALA B . n 
B 1 44  LEU 44  38  38  LEU LEU B . n 
B 1 45  ASN 45  39  39  ASN ASN B . n 
B 1 46  ASN 46  40  40  ASN ASN B . n 
B 1 47  ILE 47  41  41  ILE ILE B . n 
B 1 48  PRO 48  42  42  PRO PRO B . n 
B 1 49  GLN 49  43  43  GLN GLN B . n 
B 1 50  ALA 50  44  44  ALA ALA B . n 
B 1 51  ALA 51  45  45  ALA ALA B . n 
B 1 52  LEU 52  46  46  LEU LEU B . n 
B 1 53  GLY 53  47  47  GLY GLY B . n 
B 1 54  GLU 54  48  48  GLU GLU B . n 
B 1 55  TYR 55  49  49  TYR TYR B . n 
B 1 56  TYR 56  50  50  TYR TYR B . n 
B 1 57  GLU 57  51  51  GLU GLU B . n 
B 1 58  GLN 58  52  52  GLN GLN B . n 
B 1 59  ARG 59  53  53  ARG ARG B . n 
B 1 60  ALA 60  54  54  ALA ALA B . n 
B 1 61  THR 61  55  55  THR THR B . n 
B 1 62  ALA 62  56  56  ALA ALA B . n 
B 1 63  GLY 63  57  57  GLY GLY B . n 
B 1 64  GLY 64  58  58  GLY GLY B . n 
B 1 65  PHE 65  59  59  PHE PHE B . n 
B 1 66  LEU 66  60  60  LEU LEU B . n 
B 1 67  ILE 67  61  61  ILE ILE B . n 
B 1 68  THR 68  62  62  THR THR B . n 
B 1 69  GLU 69  63  63  GLU GLU B . n 
B 1 70  GLY 70  64  64  GLY GLY B . n 
B 1 71  THR 71  65  65  THR THR B . n 
B 1 72  MET 72  66  66  MET MET B . n 
B 1 73  ILE 73  67  67  ILE ILE B . n 
B 1 74  SER 74  68  68  SER SER B . n 
B 1 75  PRO 75  69  69  PRO PRO B . n 
B 1 76  THR 76  70  70  THR THR B . n 
B 1 77  SER 77  71  71  SER SER B . n 
B 1 78  ALA 78  72  72  ALA ALA B . n 
B 1 79  GLY 79  73  73  GLY GLY B . n 
B 1 80  PHE 80  74  74  PHE PHE B . n 
B 1 81  PRO 81  75  75  PRO PRO B . n 
B 1 82  HIS 82  76  76  HIS HIS B . n 
B 1 83  VAL 83  77  77  VAL VAL B . n 
B 1 84  PRO 84  78  78  PRO PRO B . n 
B 1 85  GLY 85  79  79  GLY GLY B . n 
B 1 86  ILE 86  80  80  ILE ILE B . n 
B 1 87  PHE 87  81  81  PHE PHE B . n 
B 1 88  THR 88  82  82  THR THR B . n 
B 1 89  LYS 89  83  83  LYS LYS B . n 
B 1 90  GLU 90  84  84  GLU GLU B . n 
B 1 91  GLN 91  85  85  GLN GLN B . n 
B 1 92  VAL 92  86  86  VAL VAL B . n 
B 1 93  ARG 93  87  87  ARG ARG B . n 
B 1 94  GLU 94  88  88  GLU GLU B . n 
B 1 95  TRP 95  89  89  TRP TRP B . n 
B 1 96  LYS 96  90  90  LYS LYS B . n 
B 1 97  LYS 97  91  91  LYS LYS B . n 
B 1 98  ILE 98  92  92  ILE ILE B . n 
B 1 99  VAL 99  93  93  VAL VAL B . n 
B 1 100 ASP 100 94  94  ASP ASP B . n 
B 1 101 VAL 101 95  95  VAL VAL B . n 
B 1 102 VAL 102 96  96  VAL VAL B . n 
B 1 103 HIS 103 97  97  HIS HIS B . n 
B 1 104 ALA 104 98  98  ALA ALA B . n 
B 1 105 LYS 105 99  99  LYS LYS B . n 
B 1 106 GLY 106 100 100 GLY GLY B . n 
B 1 107 ALA 107 101 101 ALA ALA B . n 
B 1 108 VAL 108 102 102 VAL VAL B . n 
B 1 109 ILE 109 103 103 ILE ILE B . n 
B 1 110 PHE 110 104 104 PHE PHE B . n 
B 1 111 CYS 111 105 105 CYS CYS B . n 
B 1 112 GLN 112 106 106 GLN GLN B . n 
B 1 113 LEU 113 107 107 LEU LEU B . n 
B 1 114 TRP 114 108 108 TRP TRP B . n 
B 1 115 HIS 115 109 109 HIS HIS B . n 
B 1 116 VAL 116 110 110 VAL VAL B . n 
B 1 117 GLY 117 111 111 GLY GLY B . n 
B 1 118 ARG 118 112 112 ARG ARG B . n 
B 1 119 ALA 119 113 113 ALA ALA B . n 
B 1 120 SER 120 114 114 SER SER B . n 
B 1 121 HIS 121 115 115 HIS HIS B . n 
B 1 122 GLU 122 116 116 GLU GLU B . n 
B 1 123 VAL 123 117 117 VAL VAL B . n 
B 1 124 TYR 124 118 118 TYR TYR B . n 
B 1 125 GLN 125 119 119 GLN GLN B . n 
B 1 126 PRO 126 120 120 PRO PRO B . n 
B 1 127 ALA 127 121 121 ALA ALA B . n 
B 1 128 GLY 128 122 122 GLY GLY B . n 
B 1 129 ALA 129 123 123 ALA ALA B . n 
B 1 130 ALA 130 124 124 ALA ALA B . n 
B 1 131 PRO 131 125 125 PRO PRO B . n 
B 1 132 ILE 132 126 126 ILE ILE B . n 
B 1 133 SER 133 127 127 SER SER B . n 
B 1 134 SER 134 128 128 SER SER B . n 
B 1 135 THR 135 129 129 THR THR B . n 
B 1 136 GLU 136 130 130 GLU GLU B . n 
B 1 137 LYS 137 131 131 LYS LYS B . n 
B 1 138 PRO 138 132 132 PRO PRO B . n 
B 1 139 ILE 139 133 133 ILE ILE B . n 
B 1 140 SER 140 134 134 SER SER B . n 
B 1 141 ASN 141 135 135 ASN ASN B . n 
B 1 142 ARG 142 136 136 ARG ARG B . n 
B 1 143 TRP 143 137 137 TRP TRP B . n 
B 1 144 ARG 144 138 138 ARG ARG B . n 
B 1 145 ILE 145 139 139 ILE ILE B . n 
B 1 146 LEU 146 140 140 LEU LEU B . n 
B 1 147 MET 147 141 141 MET MET B . n 
B 1 148 PRO 148 142 142 PRO PRO B . n 
B 1 149 ASP 149 143 143 ASP ASP B . n 
B 1 150 GLY 150 144 144 GLY GLY B . n 
B 1 151 THR 151 145 145 THR THR B . n 
B 1 152 HIS 152 146 146 HIS HIS B . n 
B 1 153 GLY 153 147 147 GLY GLY B . n 
B 1 154 ILE 154 148 148 ILE ILE B . n 
B 1 155 TYR 155 149 149 TYR TYR B . n 
B 1 156 PRO 156 150 150 PRO PRO B . n 
B 1 157 LYS 157 151 151 LYS LYS B . n 
B 1 158 PRO 158 152 152 PRO PRO B . n 
B 1 159 ARG 159 153 153 ARG ARG B . n 
B 1 160 ALA 160 154 154 ALA ALA B . n 
B 1 161 ILE 161 155 155 ILE ILE B . n 
B 1 162 GLY 162 156 156 GLY GLY B . n 
B 1 163 THR 163 157 157 THR THR B . n 
B 1 164 TYR 164 158 158 TYR TYR B . n 
B 1 165 GLU 165 159 159 GLU GLU B . n 
B 1 166 ILE 166 160 160 ILE ILE B . n 
B 1 167 SER 167 161 161 SER SER B . n 
B 1 168 GLN 168 162 162 GLN GLN B . n 
B 1 169 VAL 169 163 163 VAL VAL B . n 
B 1 170 VAL 170 164 164 VAL VAL B . n 
B 1 171 GLU 171 165 165 GLU GLU B . n 
B 1 172 ASP 172 166 166 ASP ASP B . n 
B 1 173 TYR 173 167 167 TYR TYR B . n 
B 1 174 ARG 174 168 168 ARG ARG B . n 
B 1 175 ARG 175 169 169 ARG ARG B . n 
B 1 176 SER 176 170 170 SER SER B . n 
B 1 177 ALA 177 171 171 ALA ALA B . n 
B 1 178 LEU 178 172 172 LEU LEU B . n 
B 1 179 ASN 179 173 173 ASN ASN B . n 
B 1 180 ALA 180 174 174 ALA ALA B . n 
B 1 181 ILE 181 175 175 ILE ILE B . n 
B 1 182 GLU 182 176 176 GLU GLU B . n 
B 1 183 ALA 183 177 177 ALA ALA B . n 
B 1 184 GLY 184 178 178 GLY GLY B . n 
B 1 185 PHE 185 179 179 PHE PHE B . n 
B 1 186 ASP 186 180 180 ASP ASP B . n 
B 1 187 GLY 187 181 181 GLY GLY B . n 
B 1 188 ILE 188 182 182 ILE ILE B . n 
B 1 189 GLU 189 183 183 GLU GLU B . n 
B 1 190 ILE 190 184 184 ILE ILE B . n 
B 1 191 HIS 191 185 185 HIS HIS B . n 
B 1 192 GLY 192 186 186 GLY GLY B . n 
B 1 193 ALA 193 187 187 ALA ALA B . n 
B 1 194 HIS 194 188 188 HIS HIS B . n 
B 1 195 GLY 195 189 189 GLY GLY B . n 
B 1 196 TYR 196 190 190 TYR TYR B . n 
B 1 197 LEU 197 191 191 LEU LEU B . n 
B 1 198 ILE 198 192 192 ILE ILE B . n 
B 1 199 ASP 199 193 193 ASP ASP B . n 
B 1 200 GLN 200 194 194 GLN GLN B . n 
B 1 201 PHE 201 195 195 PHE PHE B . n 
B 1 202 LEU 202 196 196 LEU LEU B . n 
B 1 203 LYS 203 197 197 LYS LYS B . n 
B 1 204 ASP 204 198 198 ASP ASP B . n 
B 1 205 GLY 205 199 199 GLY GLY B . n 
B 1 206 ILE 206 200 200 ILE ILE B . n 
B 1 207 ASN 207 201 201 ASN ASN B . n 
B 1 208 ASP 208 202 202 ASP ASP B . n 
B 1 209 ARG 209 203 203 ARG ARG B . n 
B 1 210 THR 210 204 204 THR THR B . n 
B 1 211 ASP 211 205 205 ASP ASP B . n 
B 1 212 GLU 212 206 206 GLU GLU B . n 
B 1 213 TYR 213 207 207 TYR TYR B . n 
B 1 214 GLY 214 208 208 GLY GLY B . n 
B 1 215 GLY 215 209 209 GLY GLY B . n 
B 1 216 SER 216 210 210 SER SER B . n 
B 1 217 LEU 217 211 211 LEU LEU B . n 
B 1 218 ALA 218 212 212 ALA ALA B . n 
B 1 219 ASN 219 213 213 ASN ASN B . n 
B 1 220 ARG 220 214 214 ARG ARG B . n 
B 1 221 CYS 221 215 215 CYS CYS B . n 
B 1 222 LYS 222 216 216 LYS LYS B . n 
B 1 223 PHE 223 217 217 PHE PHE B . n 
B 1 224 ILE 224 218 218 ILE ILE B . n 
B 1 225 THR 225 219 219 THR THR B . n 
B 1 226 GLN 226 220 220 GLN GLN B . n 
B 1 227 VAL 227 221 221 VAL VAL B . n 
B 1 228 VAL 228 222 222 VAL VAL B . n 
B 1 229 GLN 229 223 223 GLN GLN B . n 
B 1 230 ALA 230 224 224 ALA ALA B . n 
B 1 231 VAL 231 225 225 VAL VAL B . n 
B 1 232 VAL 232 226 226 VAL VAL B . n 
B 1 233 SER 233 227 227 SER SER B . n 
B 1 234 ALA 234 228 228 ALA ALA B . n 
B 1 235 ILE 235 229 229 ILE ILE B . n 
B 1 236 GLY 236 230 230 GLY GLY B . n 
B 1 237 ALA 237 231 231 ALA ALA B . n 
B 1 238 ASP 238 232 232 ASP ASP B . n 
B 1 239 ARG 239 233 233 ARG ARG B . n 
B 1 240 VAL 240 234 234 VAL VAL B . n 
B 1 241 GLY 241 235 235 GLY GLY B . n 
B 1 242 VAL 242 236 236 VAL VAL B . n 
B 1 243 ARG 243 237 237 ARG ARG B . n 
B 1 244 VAL 244 238 238 VAL VAL B . n 
B 1 245 SER 245 239 239 SER SER B . n 
B 1 246 PRO 246 240 240 PRO PRO B . n 
B 1 247 ALA 247 241 241 ALA ALA B . n 
B 1 248 ILE 248 242 242 ILE ILE B . n 
B 1 249 ASP 249 243 243 ASP ASP B . n 
B 1 250 HIS 250 244 244 HIS HIS B . n 
B 1 251 LEU 251 245 245 LEU LEU B . n 
B 1 252 ASP 252 246 246 ASP ASP B . n 
B 1 253 ALA 253 247 247 ALA ALA B . n 
B 1 254 MET 254 248 248 MET MET B . n 
B 1 255 ASP 255 249 249 ASP ASP B . n 
B 1 256 SER 256 250 250 SER SER B . n 
B 1 257 ASN 257 251 251 ASN ASN B . n 
B 1 258 PRO 258 252 252 PRO PRO B . n 
B 1 259 LEU 259 253 253 LEU LEU B . n 
B 1 260 SER 260 254 254 SER SER B . n 
B 1 261 LEU 261 255 255 LEU LEU B . n 
B 1 262 GLY 262 256 256 GLY GLY B . n 
B 1 263 LEU 263 257 257 LEU LEU B . n 
B 1 264 ALA 264 258 258 ALA ALA B . n 
B 1 265 VAL 265 259 259 VAL VAL B . n 
B 1 266 VAL 266 260 260 VAL VAL B . n 
B 1 267 GLU 267 261 261 GLU GLU B . n 
B 1 268 ARG 268 262 262 ARG ARG B . n 
B 1 269 LEU 269 263 263 LEU LEU B . n 
B 1 270 ASN 270 264 264 ASN ASN B . n 
B 1 271 LYS 271 265 265 LYS LYS B . n 
B 1 272 ILE 272 266 266 ILE ILE B . n 
B 1 273 GLN 273 267 267 GLN GLN B . n 
B 1 274 LEU 274 268 268 LEU LEU B . n 
B 1 275 HIS 275 269 269 HIS HIS B . n 
B 1 276 SER 276 270 270 SER SER B . n 
B 1 277 GLY 277 271 271 GLY GLY B . n 
B 1 278 SER 278 272 272 SER SER B . n 
B 1 279 LYS 279 273 273 LYS LYS B . n 
B 1 280 LEU 280 274 274 LEU LEU B . n 
B 1 281 ALA 281 275 275 ALA ALA B . n 
B 1 282 TYR 282 276 276 TYR TYR B . n 
B 1 283 LEU 283 277 277 LEU LEU B . n 
B 1 284 HIS 284 278 278 HIS HIS B . n 
B 1 285 VAL 285 279 279 VAL VAL B . n 
B 1 286 THR 286 280 280 THR THR B . n 
B 1 287 GLN 287 281 281 GLN GLN B . n 
B 1 288 PRO 288 282 282 PRO PRO B . n 
B 1 289 GLU 289 283 ?   ?   ?   B . n 
B 1 290 TYR 290 284 ?   ?   ?   B . n 
B 1 291 VAL 291 285 ?   ?   ?   B . n 
B 1 292 ALA 292 286 ?   ?   ?   B . n 
B 1 293 TYR 293 287 ?   ?   ?   B . n 
B 1 294 GLY 294 288 ?   ?   ?   B . n 
B 1 295 GLN 295 289 ?   ?   ?   B . n 
B 1 296 THR 296 290 ?   ?   ?   B . n 
B 1 297 GLU 297 291 ?   ?   ?   B . n 
B 1 298 ALA 298 292 ?   ?   ?   B . n 
B 1 299 GLY 299 293 ?   ?   ?   B . n 
B 1 300 ARG 300 294 ?   ?   ?   B . n 
B 1 301 LEU 301 295 ?   ?   ?   B . n 
B 1 302 GLY 302 296 ?   ?   ?   B . n 
B 1 303 SER 303 297 ?   ?   ?   B . n 
B 1 304 GLU 304 298 ?   ?   ?   B . n 
B 1 305 GLU 305 299 ?   ?   ?   B . n 
B 1 306 GLU 306 300 ?   ?   ?   B . n 
B 1 307 GLU 307 301 ?   ?   ?   B . n 
B 1 308 ALA 308 302 302 ALA ALA B . n 
B 1 309 ARG 309 303 303 ARG ARG B . n 
B 1 310 LEU 310 304 304 LEU LEU B . n 
B 1 311 MET 311 305 305 MET MET B . n 
B 1 312 ARG 312 306 306 ARG ARG B . n 
B 1 313 THR 313 307 307 THR THR B . n 
B 1 314 LEU 314 308 308 LEU LEU B . n 
B 1 315 ARG 315 309 309 ARG ARG B . n 
B 1 316 ASN 316 310 310 ASN ASN B . n 
B 1 317 ALA 317 311 311 ALA ALA B . n 
B 1 318 TYR 318 312 312 TYR TYR B . n 
B 1 319 GLN 319 313 313 GLN GLN B . n 
B 1 320 GLY 320 314 314 GLY GLY B . n 
B 1 321 THR 321 315 315 THR THR B . n 
B 1 322 PHE 322 316 316 PHE PHE B . n 
B 1 323 ILE 323 317 317 ILE ILE B . n 
B 1 324 CYS 324 318 318 CYS CYS B . n 
B 1 325 SER 325 319 319 SER SER B . n 
B 1 326 GLY 326 320 320 GLY GLY B . n 
B 1 327 GLY 327 321 321 GLY GLY B . n 
B 1 328 TYR 328 322 322 TYR TYR B . n 
B 1 329 THR 329 323 323 THR THR B . n 
B 1 330 ARG 330 324 324 ARG ARG B . n 
B 1 331 GLU 331 325 325 GLU GLU B . n 
B 1 332 LEU 332 326 326 LEU LEU B . n 
B 1 333 GLY 333 327 327 GLY GLY B . n 
B 1 334 ILE 334 328 328 ILE ILE B . n 
B 1 335 GLU 335 329 329 GLU GLU B . n 
B 1 336 ALA 336 330 330 ALA ALA B . n 
B 1 337 VAL 337 331 331 VAL VAL B . n 
B 1 338 ALA 338 332 332 ALA ALA B . n 
B 1 339 GLN 339 333 333 GLN GLN B . n 
B 1 340 GLY 340 334 334 GLY GLY B . n 
B 1 341 ASP 341 335 335 ASP ASP B . n 
B 1 342 ALA 342 336 336 ALA ALA B . n 
B 1 343 ASP 343 337 337 ASP ASP B . n 
B 1 344 LEU 344 338 338 LEU LEU B . n 
B 1 345 VAL 345 339 339 VAL VAL B . n 
B 1 346 SER 346 340 340 SER SER B . n 
B 1 347 TYR 347 341 341 TYR TYR B . n 
B 1 348 GLY 348 342 342 GLY GLY B . n 
B 1 349 ARG 349 343 343 ARG ARG B . n 
B 1 350 LEU 350 344 344 LEU LEU B . n 
B 1 351 PHE 351 345 345 PHE PHE B . n 
B 1 352 ILE 352 346 346 ILE ILE B . n 
B 1 353 SER 353 347 347 SER SER B . n 
B 1 354 ASN 354 348 348 ASN ASN B . n 
B 1 355 PRO 355 349 349 PRO PRO B . n 
B 1 356 ASP 356 350 350 ASP ASP B . n 
B 1 357 LEU 357 351 351 LEU LEU B . n 
B 1 358 VAL 358 352 352 VAL VAL B . n 
B 1 359 MET 359 353 353 MET MET B . n 
B 1 360 ARG 360 354 354 ARG ARG B . n 
B 1 361 ILE 361 355 355 ILE ILE B . n 
B 1 362 LYS 362 356 356 LYS LYS B . n 
B 1 363 LEU 363 357 357 LEU LEU B . n 
B 1 364 ASN 364 358 358 ASN ASN B . n 
B 1 365 ALA 365 359 359 ALA ALA B . n 
B 1 366 PRO 366 360 360 PRO PRO B . n 
B 1 367 LEU 367 361 361 LEU LEU B . n 
B 1 368 ASN 368 362 362 ASN ASN B . n 
B 1 369 LYS 369 363 363 LYS LYS B . n 
B 1 370 TYR 370 364 364 TYR TYR B . n 
B 1 371 ASN 371 365 365 ASN ASN B . n 
B 1 372 ARG 372 366 366 ARG ARG B . n 
B 1 373 LYS 373 367 367 LYS LYS B . n 
B 1 374 THR 374 368 368 THR THR B . n 
B 1 375 PHE 375 369 369 PHE PHE B . n 
B 1 376 TYR 376 370 370 TYR TYR B . n 
B 1 377 THR 377 371 371 THR THR B . n 
B 1 378 GLN 378 372 372 GLN GLN B . n 
B 1 379 ASP 379 373 373 ASP ASP B . n 
B 1 380 PRO 380 374 374 PRO PRO B . n 
B 1 381 VAL 381 375 375 VAL VAL B . n 
B 1 382 VAL 382 376 376 VAL VAL B . n 
B 1 383 GLY 383 377 377 GLY GLY B . n 
B 1 384 TYR 384 378 378 TYR TYR B . n 
B 1 385 THR 385 379 379 THR THR B . n 
B 1 386 ASP 386 380 380 ASP ASP B . n 
B 1 387 TYR 387 381 381 TYR TYR B . n 
B 1 388 PRO 388 382 382 PRO PRO B . n 
B 1 389 PHE 389 383 383 PHE PHE B . n 
B 1 390 LEU 390 384 384 LEU LEU B . n 
B 1 391 GLN 391 385 ?   ?   ?   B . n 
B 1 392 GLY 392 386 ?   ?   ?   B . n 
B 1 393 ASN 393 387 ?   ?   ?   B . n 
B 1 394 GLY 394 388 ?   ?   ?   B . n 
B 1 395 SER 395 389 ?   ?   ?   B . n 
B 1 396 ASN 396 390 ?   ?   ?   B . n 
B 1 397 GLY 397 391 ?   ?   ?   B . n 
B 1 398 PRO 398 392 ?   ?   ?   B . n 
B 1 399 LEU 399 393 ?   ?   ?   B . n 
B 1 400 SER 400 394 ?   ?   ?   B . n 
B 1 401 ARG 401 395 ?   ?   ?   B . n 
B 1 402 LEU 402 396 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        WI6 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   WI6 
_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   401 395 FMN FMN A . 
D 3 WI6 1   402 396 WI6 TXD A . 
E 2 FMN 1   401 395 FMN FMN B . 
F 3 WI6 1   402 396 WI6 TXD B . 
G 4 HOH 1   501 511 HOH HOH A . 
G 4 HOH 2   502 725 HOH HOH A . 
G 4 HOH 3   503 102 HOH HOH A . 
G 4 HOH 4   504 564 HOH HOH A . 
G 4 HOH 5   505 423 HOH HOH A . 
G 4 HOH 6   506 748 HOH HOH A . 
G 4 HOH 7   507 684 HOH HOH A . 
G 4 HOH 8   508 501 HOH HOH A . 
G 4 HOH 9   509 436 HOH HOH A . 
G 4 HOH 10  510 64  HOH HOH A . 
G 4 HOH 11  511 144 HOH HOH A . 
G 4 HOH 12  512 722 HOH HOH A . 
G 4 HOH 13  513 403 HOH HOH A . 
G 4 HOH 14  514 523 HOH HOH A . 
G 4 HOH 15  515 505 HOH HOH A . 
G 4 HOH 16  516 284 HOH HOH A . 
G 4 HOH 17  517 662 HOH HOH A . 
G 4 HOH 18  518 247 HOH HOH A . 
G 4 HOH 19  519 323 HOH HOH A . 
G 4 HOH 20  520 462 HOH HOH A . 
G 4 HOH 21  521 252 HOH HOH A . 
G 4 HOH 22  522 199 HOH HOH A . 
G 4 HOH 23  523 534 HOH HOH A . 
G 4 HOH 24  524 443 HOH HOH A . 
G 4 HOH 25  525 238 HOH HOH A . 
G 4 HOH 26  526 107 HOH HOH A . 
G 4 HOH 27  527 486 HOH HOH A . 
G 4 HOH 28  528 567 HOH HOH A . 
G 4 HOH 29  529 672 HOH HOH A . 
G 4 HOH 30  530 695 HOH HOH A . 
G 4 HOH 31  531 380 HOH HOH A . 
G 4 HOH 32  532 352 HOH HOH A . 
G 4 HOH 33  533 108 HOH HOH A . 
G 4 HOH 34  534 178 HOH HOH A . 
G 4 HOH 35  535 425 HOH HOH A . 
G 4 HOH 36  536 154 HOH HOH A . 
G 4 HOH 37  537 87  HOH HOH A . 
G 4 HOH 38  538 123 HOH HOH A . 
G 4 HOH 39  539 244 HOH HOH A . 
G 4 HOH 40  540 265 HOH HOH A . 
G 4 HOH 41  541 426 HOH HOH A . 
G 4 HOH 42  542 16  HOH HOH A . 
G 4 HOH 43  543 619 HOH HOH A . 
G 4 HOH 44  544 11  HOH HOH A . 
G 4 HOH 45  545 38  HOH HOH A . 
G 4 HOH 46  546 616 HOH HOH A . 
G 4 HOH 47  547 475 HOH HOH A . 
G 4 HOH 48  548 122 HOH HOH A . 
G 4 HOH 49  549 213 HOH HOH A . 
G 4 HOH 50  550 183 HOH HOH A . 
G 4 HOH 51  551 89  HOH HOH A . 
G 4 HOH 52  552 485 HOH HOH A . 
G 4 HOH 53  553 201 HOH HOH A . 
G 4 HOH 54  554 393 HOH HOH A . 
G 4 HOH 55  555 506 HOH HOH A . 
G 4 HOH 56  556 413 HOH HOH A . 
G 4 HOH 57  557 22  HOH HOH A . 
G 4 HOH 58  558 596 HOH HOH A . 
G 4 HOH 59  559 470 HOH HOH A . 
G 4 HOH 60  560 347 HOH HOH A . 
G 4 HOH 61  561 666 HOH HOH A . 
G 4 HOH 62  562 163 HOH HOH A . 
G 4 HOH 63  563 14  HOH HOH A . 
G 4 HOH 64  564 592 HOH HOH A . 
G 4 HOH 65  565 330 HOH HOH A . 
G 4 HOH 66  566 385 HOH HOH A . 
G 4 HOH 67  567 343 HOH HOH A . 
G 4 HOH 68  568 206 HOH HOH A . 
G 4 HOH 69  569 391 HOH HOH A . 
G 4 HOH 70  570 131 HOH HOH A . 
G 4 HOH 71  571 350 HOH HOH A . 
G 4 HOH 72  572 55  HOH HOH A . 
G 4 HOH 73  573 307 HOH HOH A . 
G 4 HOH 74  574 315 HOH HOH A . 
G 4 HOH 75  575 3   HOH HOH A . 
G 4 HOH 76  576 603 HOH HOH A . 
G 4 HOH 77  577 554 HOH HOH A . 
G 4 HOH 78  578 146 HOH HOH A . 
G 4 HOH 79  579 309 HOH HOH A . 
G 4 HOH 80  580 165 HOH HOH A . 
G 4 HOH 81  581 328 HOH HOH A . 
G 4 HOH 82  582 447 HOH HOH A . 
G 4 HOH 83  583 304 HOH HOH A . 
G 4 HOH 84  584 68  HOH HOH A . 
G 4 HOH 85  585 468 HOH HOH A . 
G 4 HOH 86  586 321 HOH HOH A . 
G 4 HOH 87  587 34  HOH HOH A . 
G 4 HOH 88  588 384 HOH HOH A . 
G 4 HOH 89  589 76  HOH HOH A . 
G 4 HOH 90  590 620 HOH HOH A . 
G 4 HOH 91  591 401 HOH HOH A . 
G 4 HOH 92  592 103 HOH HOH A . 
G 4 HOH 93  593 688 HOH HOH A . 
G 4 HOH 94  594 381 HOH HOH A . 
G 4 HOH 95  595 224 HOH HOH A . 
G 4 HOH 96  596 106 HOH HOH A . 
G 4 HOH 97  597 217 HOH HOH A . 
G 4 HOH 98  598 218 HOH HOH A . 
G 4 HOH 99  599 440 HOH HOH A . 
G 4 HOH 100 600 53  HOH HOH A . 
G 4 HOH 101 601 97  HOH HOH A . 
G 4 HOH 102 602 79  HOH HOH A . 
G 4 HOH 103 603 732 HOH HOH A . 
G 4 HOH 104 604 268 HOH HOH A . 
G 4 HOH 105 605 349 HOH HOH A . 
G 4 HOH 106 606 520 HOH HOH A . 
G 4 HOH 107 607 56  HOH HOH A . 
G 4 HOH 108 608 188 HOH HOH A . 
G 4 HOH 109 609 487 HOH HOH A . 
G 4 HOH 110 610 320 HOH HOH A . 
G 4 HOH 111 611 50  HOH HOH A . 
G 4 HOH 112 612 72  HOH HOH A . 
G 4 HOH 113 613 353 HOH HOH A . 
G 4 HOH 114 614 37  HOH HOH A . 
G 4 HOH 115 615 376 HOH HOH A . 
G 4 HOH 116 616 198 HOH HOH A . 
G 4 HOH 117 617 318 HOH HOH A . 
G 4 HOH 118 618 129 HOH HOH A . 
G 4 HOH 119 619 300 HOH HOH A . 
G 4 HOH 120 620 171 HOH HOH A . 
G 4 HOH 121 621 142 HOH HOH A . 
G 4 HOH 122 622 214 HOH HOH A . 
G 4 HOH 123 623 49  HOH HOH A . 
G 4 HOH 124 624 67  HOH HOH A . 
G 4 HOH 125 625 85  HOH HOH A . 
G 4 HOH 126 626 101 HOH HOH A . 
G 4 HOH 127 627 340 HOH HOH A . 
G 4 HOH 128 628 255 HOH HOH A . 
G 4 HOH 129 629 126 HOH HOH A . 
G 4 HOH 130 630 5   HOH HOH A . 
G 4 HOH 131 631 241 HOH HOH A . 
G 4 HOH 132 632 153 HOH HOH A . 
G 4 HOH 133 633 148 HOH HOH A . 
G 4 HOH 134 634 237 HOH HOH A . 
G 4 HOH 135 635 585 HOH HOH A . 
G 4 HOH 136 636 615 HOH HOH A . 
G 4 HOH 137 637 111 HOH HOH A . 
G 4 HOH 138 638 235 HOH HOH A . 
G 4 HOH 139 639 92  HOH HOH A . 
G 4 HOH 140 640 240 HOH HOH A . 
G 4 HOH 141 641 220 HOH HOH A . 
G 4 HOH 142 642 19  HOH HOH A . 
G 4 HOH 143 643 13  HOH HOH A . 
G 4 HOH 144 644 441 HOH HOH A . 
G 4 HOH 145 645 25  HOH HOH A . 
G 4 HOH 146 646 508 HOH HOH A . 
G 4 HOH 147 647 140 HOH HOH A . 
G 4 HOH 148 648 293 HOH HOH A . 
G 4 HOH 149 649 30  HOH HOH A . 
G 4 HOH 150 650 430 HOH HOH A . 
G 4 HOH 151 651 319 HOH HOH A . 
G 4 HOH 152 652 389 HOH HOH A . 
G 4 HOH 153 653 109 HOH HOH A . 
G 4 HOH 154 654 18  HOH HOH A . 
G 4 HOH 155 655 175 HOH HOH A . 
G 4 HOH 156 656 221 HOH HOH A . 
G 4 HOH 157 657 250 HOH HOH A . 
G 4 HOH 158 658 162 HOH HOH A . 
G 4 HOH 159 659 9   HOH HOH A . 
G 4 HOH 160 660 43  HOH HOH A . 
G 4 HOH 161 661 273 HOH HOH A . 
G 4 HOH 162 662 23  HOH HOH A . 
G 4 HOH 163 663 402 HOH HOH A . 
G 4 HOH 164 664 606 HOH HOH A . 
G 4 HOH 165 665 35  HOH HOH A . 
G 4 HOH 166 666 74  HOH HOH A . 
G 4 HOH 167 667 248 HOH HOH A . 
G 4 HOH 168 668 448 HOH HOH A . 
G 4 HOH 169 669 279 HOH HOH A . 
G 4 HOH 170 670 305 HOH HOH A . 
G 4 HOH 171 671 429 HOH HOH A . 
G 4 HOH 172 672 453 HOH HOH A . 
G 4 HOH 173 673 83  HOH HOH A . 
G 4 HOH 174 674 739 HOH HOH A . 
G 4 HOH 175 675 155 HOH HOH A . 
G 4 HOH 176 676 382 HOH HOH A . 
G 4 HOH 177 677 661 HOH HOH A . 
G 4 HOH 178 678 82  HOH HOH A . 
G 4 HOH 179 679 158 HOH HOH A . 
G 4 HOH 180 680 4   HOH HOH A . 
G 4 HOH 181 681 127 HOH HOH A . 
G 4 HOH 182 682 359 HOH HOH A . 
G 4 HOH 183 683 105 HOH HOH A . 
G 4 HOH 184 684 62  HOH HOH A . 
G 4 HOH 185 685 295 HOH HOH A . 
G 4 HOH 186 686 132 HOH HOH A . 
G 4 HOH 187 687 233 HOH HOH A . 
G 4 HOH 188 688 204 HOH HOH A . 
G 4 HOH 189 689 659 HOH HOH A . 
G 4 HOH 190 690 639 HOH HOH A . 
G 4 HOH 191 691 285 HOH HOH A . 
G 4 HOH 192 692 648 HOH HOH A . 
G 4 HOH 193 693 489 HOH HOH A . 
G 4 HOH 194 694 277 HOH HOH A . 
G 4 HOH 195 695 98  HOH HOH A . 
G 4 HOH 196 696 749 HOH HOH A . 
G 4 HOH 197 697 21  HOH HOH A . 
G 4 HOH 198 698 405 HOH HOH A . 
G 4 HOH 199 699 180 HOH HOH A . 
G 4 HOH 200 700 215 HOH HOH A . 
G 4 HOH 201 701 276 HOH HOH A . 
G 4 HOH 202 702 125 HOH HOH A . 
G 4 HOH 203 703 181 HOH HOH A . 
G 4 HOH 204 704 270 HOH HOH A . 
G 4 HOH 205 705 73  HOH HOH A . 
G 4 HOH 206 706 151 HOH HOH A . 
G 4 HOH 207 707 583 HOH HOH A . 
G 4 HOH 208 708 686 HOH HOH A . 
G 4 HOH 209 709 289 HOH HOH A . 
G 4 HOH 210 710 552 HOH HOH A . 
G 4 HOH 211 711 622 HOH HOH A . 
G 4 HOH 212 712 724 HOH HOH A . 
G 4 HOH 213 713 71  HOH HOH A . 
G 4 HOH 214 714 170 HOH HOH A . 
G 4 HOH 215 715 42  HOH HOH A . 
G 4 HOH 216 716 1   HOH HOH A . 
G 4 HOH 217 717 207 HOH HOH A . 
G 4 HOH 218 718 705 HOH HOH A . 
G 4 HOH 219 719 332 HOH HOH A . 
G 4 HOH 220 720 472 HOH HOH A . 
G 4 HOH 221 721 369 HOH HOH A . 
G 4 HOH 222 722 545 HOH HOH A . 
G 4 HOH 223 723 412 HOH HOH A . 
G 4 HOH 224 724 322 HOH HOH A . 
G 4 HOH 225 725 525 HOH HOH A . 
G 4 HOH 226 726 239 HOH HOH A . 
G 4 HOH 227 727 172 HOH HOH A . 
G 4 HOH 228 728 211 HOH HOH A . 
G 4 HOH 229 729 110 HOH HOH A . 
G 4 HOH 230 730 301 HOH HOH A . 
G 4 HOH 231 731 278 HOH HOH A . 
G 4 HOH 232 732 735 HOH HOH A . 
G 4 HOH 233 733 228 HOH HOH A . 
G 4 HOH 234 734 99  HOH HOH A . 
G 4 HOH 235 735 40  HOH HOH A . 
G 4 HOH 236 736 437 HOH HOH A . 
G 4 HOH 237 737 326 HOH HOH A . 
G 4 HOH 238 738 294 HOH HOH A . 
G 4 HOH 239 739 720 HOH HOH A . 
G 4 HOH 240 740 374 HOH HOH A . 
G 4 HOH 241 741 528 HOH HOH A . 
G 4 HOH 242 742 535 HOH HOH A . 
G 4 HOH 243 743 339 HOH HOH A . 
G 4 HOH 244 744 80  HOH HOH A . 
G 4 HOH 245 745 478 HOH HOH A . 
G 4 HOH 246 746 518 HOH HOH A . 
G 4 HOH 247 747 173 HOH HOH A . 
G 4 HOH 248 748 225 HOH HOH A . 
G 4 HOH 249 749 536 HOH HOH A . 
G 4 HOH 250 750 500 HOH HOH A . 
G 4 HOH 251 751 538 HOH HOH A . 
G 4 HOH 252 752 375 HOH HOH A . 
G 4 HOH 253 753 497 HOH HOH A . 
G 4 HOH 254 754 396 HOH HOH A . 
G 4 HOH 255 755 499 HOH HOH A . 
G 4 HOH 256 756 656 HOH HOH A . 
G 4 HOH 257 757 58  HOH HOH A . 
G 4 HOH 258 758 356 HOH HOH A . 
G 4 HOH 259 759 257 HOH HOH A . 
G 4 HOH 260 760 177 HOH HOH A . 
G 4 HOH 261 761 298 HOH HOH A . 
G 4 HOH 262 762 704 HOH HOH A . 
G 4 HOH 263 763 580 HOH HOH A . 
G 4 HOH 264 764 623 HOH HOH A . 
G 4 HOH 265 765 611 HOH HOH A . 
G 4 HOH 266 766 483 HOH HOH A . 
G 4 HOH 267 767 658 HOH HOH A . 
G 4 HOH 268 768 539 HOH HOH A . 
G 4 HOH 269 769 626 HOH HOH A . 
G 4 HOH 270 770 591 HOH HOH A . 
G 4 HOH 271 771 582 HOH HOH A . 
G 4 HOH 272 772 222 HOH HOH A . 
G 4 HOH 273 773 668 HOH HOH A . 
G 4 HOH 274 774 653 HOH HOH A . 
G 4 HOH 275 775 549 HOH HOH A . 
G 4 HOH 276 776 706 HOH HOH A . 
G 4 HOH 277 777 736 HOH HOH A . 
G 4 HOH 278 778 190 HOH HOH A . 
G 4 HOH 279 779 370 HOH HOH A . 
G 4 HOH 280 780 645 HOH HOH A . 
G 4 HOH 281 781 716 HOH HOH A . 
G 4 HOH 282 782 746 HOH HOH A . 
G 4 HOH 283 783 586 HOH HOH A . 
G 4 HOH 284 784 681 HOH HOH A . 
G 4 HOH 285 785 121 HOH HOH A . 
G 4 HOH 286 786 685 HOH HOH A . 
G 4 HOH 287 787 565 HOH HOH A . 
G 4 HOH 288 788 673 HOH HOH A . 
G 4 HOH 289 789 262 HOH HOH A . 
G 4 HOH 290 790 574 HOH HOH A . 
G 4 HOH 291 791 387 HOH HOH A . 
G 4 HOH 292 792 543 HOH HOH A . 
G 4 HOH 293 793 584 HOH HOH A . 
G 4 HOH 294 794 296 HOH HOH A . 
G 4 HOH 295 795 422 HOH HOH A . 
G 4 HOH 296 796 394 HOH HOH A . 
G 4 HOH 297 797 570 HOH HOH A . 
G 4 HOH 298 798 136 HOH HOH A . 
G 4 HOH 299 799 728 HOH HOH A . 
G 4 HOH 300 800 740 HOH HOH A . 
G 4 HOH 301 801 531 HOH HOH A . 
G 4 HOH 302 802 689 HOH HOH A . 
G 4 HOH 303 803 696 HOH HOH A . 
G 4 HOH 304 804 342 HOH HOH A . 
G 4 HOH 305 805 600 HOH HOH A . 
G 4 HOH 306 806 613 HOH HOH A . 
G 4 HOH 307 807 612 HOH HOH A . 
G 4 HOH 308 808 594 HOH HOH A . 
G 4 HOH 309 809 627 HOH HOH A . 
G 4 HOH 310 810 533 HOH HOH A . 
G 4 HOH 311 811 750 HOH HOH A . 
G 4 HOH 312 812 245 HOH HOH A . 
G 4 HOH 313 813 657 HOH HOH A . 
G 4 HOH 314 814 714 HOH HOH A . 
G 4 HOH 315 815 671 HOH HOH A . 
G 4 HOH 316 816 587 HOH HOH A . 
G 4 HOH 317 817 383 HOH HOH A . 
G 4 HOH 318 818 456 HOH HOH A . 
G 4 HOH 319 819 329 HOH HOH A . 
G 4 HOH 320 820 712 HOH HOH A . 
G 4 HOH 321 821 451 HOH HOH A . 
G 4 HOH 322 822 636 HOH HOH A . 
G 4 HOH 323 823 96  HOH HOH A . 
G 4 HOH 324 824 631 HOH HOH A . 
G 4 HOH 325 825 715 HOH HOH A . 
G 4 HOH 326 826 461 HOH HOH A . 
G 4 HOH 327 827 601 HOH HOH A . 
G 4 HOH 328 828 559 HOH HOH A . 
G 4 HOH 329 829 81  HOH HOH A . 
G 4 HOH 330 830 701 HOH HOH A . 
G 4 HOH 331 831 744 HOH HOH A . 
G 4 HOH 332 832 576 HOH HOH A . 
G 4 HOH 333 833 395 HOH HOH A . 
G 4 HOH 334 834 625 HOH HOH A . 
G 4 HOH 335 835 682 HOH HOH A . 
G 4 HOH 336 836 409 HOH HOH A . 
G 4 HOH 337 837 509 HOH HOH A . 
G 4 HOH 338 838 597 HOH HOH A . 
G 4 HOH 339 839 442 HOH HOH A . 
G 4 HOH 340 840 541 HOH HOH A . 
G 4 HOH 341 841 195 HOH HOH A . 
G 4 HOH 342 842 299 HOH HOH A . 
G 4 HOH 343 843 449 HOH HOH A . 
G 4 HOH 344 844 280 HOH HOH A . 
G 4 HOH 345 845 588 HOH HOH A . 
G 4 HOH 346 846 515 HOH HOH A . 
G 4 HOH 347 847 598 HOH HOH A . 
G 4 HOH 348 848 467 HOH HOH A . 
G 4 HOH 349 849 479 HOH HOH A . 
G 4 HOH 350 850 491 HOH HOH A . 
G 4 HOH 351 851 254 HOH HOH A . 
G 4 HOH 352 852 510 HOH HOH A . 
G 4 HOH 353 853 589 HOH HOH A . 
G 4 HOH 354 854 360 HOH HOH A . 
G 4 HOH 355 855 692 HOH HOH A . 
G 4 HOH 356 856 492 HOH HOH A . 
G 4 HOH 357 857 408 HOH HOH A . 
G 4 HOH 358 858 480 HOH HOH A . 
G 4 HOH 359 859 494 HOH HOH A . 
G 4 HOH 360 860 133 HOH HOH A . 
G 4 HOH 361 861 484 HOH HOH A . 
G 4 HOH 362 862 219 HOH HOH A . 
G 4 HOH 363 863 599 HOH HOH A . 
G 4 HOH 364 864 513 HOH HOH A . 
G 4 HOH 365 865 579 HOH HOH A . 
G 4 HOH 366 866 711 HOH HOH A . 
G 4 HOH 367 867 457 HOH HOH A . 
G 4 HOH 368 868 495 HOH HOH A . 
G 4 HOH 369 869 312 HOH HOH A . 
G 4 HOH 370 870 709 HOH HOH A . 
G 4 HOH 371 871 205 HOH HOH A . 
G 4 HOH 372 872 185 HOH HOH A . 
G 4 HOH 373 873 287 HOH HOH A . 
G 4 HOH 374 874 604 HOH HOH A . 
G 4 HOH 375 875 581 HOH HOH A . 
G 4 HOH 376 876 493 HOH HOH A . 
G 4 HOH 377 877 699 HOH HOH A . 
G 4 HOH 378 878 697 HOH HOH A . 
G 4 HOH 379 879 733 HOH HOH A . 
G 4 HOH 380 880 745 HOH HOH A . 
G 4 HOH 381 881 719 HOH HOH A . 
G 4 HOH 382 882 507 HOH HOH A . 
G 4 HOH 383 883 544 HOH HOH A . 
G 4 HOH 384 884 529 HOH HOH A . 
G 4 HOH 385 885 694 HOH HOH A . 
G 4 HOH 386 886 324 HOH HOH A . 
H 4 HOH 1   501 169 HOH HOH B . 
H 4 HOH 2   502 438 HOH HOH B . 
H 4 HOH 3   503 551 HOH HOH B . 
H 4 HOH 4   504 406 HOH HOH B . 
H 4 HOH 5   505 355 HOH HOH B . 
H 4 HOH 6   506 542 HOH HOH B . 
H 4 HOH 7   507 710 HOH HOH B . 
H 4 HOH 8   508 488 HOH HOH B . 
H 4 HOH 9   509 723 HOH HOH B . 
H 4 HOH 10  510 693 HOH HOH B . 
H 4 HOH 11  511 690 HOH HOH B . 
H 4 HOH 12  512 112 HOH HOH B . 
H 4 HOH 13  513 281 HOH HOH B . 
H 4 HOH 14  514 742 HOH HOH B . 
H 4 HOH 15  515 90  HOH HOH B . 
H 4 HOH 16  516 39  HOH HOH B . 
H 4 HOH 17  517 463 HOH HOH B . 
H 4 HOH 18  518 341 HOH HOH B . 
H 4 HOH 19  519 476 HOH HOH B . 
H 4 HOH 20  520 595 HOH HOH B . 
H 4 HOH 21  521 404 HOH HOH B . 
H 4 HOH 22  522 708 HOH HOH B . 
H 4 HOH 23  523 236 HOH HOH B . 
H 4 HOH 24  524 550 HOH HOH B . 
H 4 HOH 25  525 115 HOH HOH B . 
H 4 HOH 26  526 683 HOH HOH B . 
H 4 HOH 27  527 274 HOH HOH B . 
H 4 HOH 28  528 548 HOH HOH B . 
H 4 HOH 29  529 336 HOH HOH B . 
H 4 HOH 30  530 168 HOH HOH B . 
H 4 HOH 31  531 572 HOH HOH B . 
H 4 HOH 32  532 66  HOH HOH B . 
H 4 HOH 33  533 200 HOH HOH B . 
H 4 HOH 34  534 421 HOH HOH B . 
H 4 HOH 35  535 607 HOH HOH B . 
H 4 HOH 36  536 54  HOH HOH B . 
H 4 HOH 37  537 232 HOH HOH B . 
H 4 HOH 38  538 29  HOH HOH B . 
H 4 HOH 39  539 114 HOH HOH B . 
H 4 HOH 40  540 20  HOH HOH B . 
H 4 HOH 41  541 311 HOH HOH B . 
H 4 HOH 42  542 526 HOH HOH B . 
H 4 HOH 43  543 197 HOH HOH B . 
H 4 HOH 44  544 187 HOH HOH B . 
H 4 HOH 45  545 670 HOH HOH B . 
H 4 HOH 46  546 184 HOH HOH B . 
H 4 HOH 47  547 454 HOH HOH B . 
H 4 HOH 48  548 60  HOH HOH B . 
H 4 HOH 49  549 473 HOH HOH B . 
H 4 HOH 50  550 546 HOH HOH B . 
H 4 HOH 51  551 119 HOH HOH B . 
H 4 HOH 52  552 614 HOH HOH B . 
H 4 HOH 53  553 179 HOH HOH B . 
H 4 HOH 54  554 24  HOH HOH B . 
H 4 HOH 55  555 665 HOH HOH B . 
H 4 HOH 56  556 524 HOH HOH B . 
H 4 HOH 57  557 482 HOH HOH B . 
H 4 HOH 58  558 411 HOH HOH B . 
H 4 HOH 59  559 446 HOH HOH B . 
H 4 HOH 60  560 159 HOH HOH B . 
H 4 HOH 61  561 113 HOH HOH B . 
H 4 HOH 62  562 47  HOH HOH B . 
H 4 HOH 63  563 675 HOH HOH B . 
H 4 HOH 64  564 118 HOH HOH B . 
H 4 HOH 65  565 721 HOH HOH B . 
H 4 HOH 66  566 203 HOH HOH B . 
H 4 HOH 67  567 167 HOH HOH B . 
H 4 HOH 68  568 192 HOH HOH B . 
H 4 HOH 69  569 261 HOH HOH B . 
H 4 HOH 70  570 128 HOH HOH B . 
H 4 HOH 71  571 282 HOH HOH B . 
H 4 HOH 72  572 415 HOH HOH B . 
H 4 HOH 73  573 32  HOH HOH B . 
H 4 HOH 74  574 139 HOH HOH B . 
H 4 HOH 75  575 308 HOH HOH B . 
H 4 HOH 76  576 537 HOH HOH B . 
H 4 HOH 77  577 290 HOH HOH B . 
H 4 HOH 78  578 260 HOH HOH B . 
H 4 HOH 79  579 7   HOH HOH B . 
H 4 HOH 80  580 628 HOH HOH B . 
H 4 HOH 81  581 266 HOH HOH B . 
H 4 HOH 82  582 310 HOH HOH B . 
H 4 HOH 83  583 8   HOH HOH B . 
H 4 HOH 84  584 390 HOH HOH B . 
H 4 HOH 85  585 12  HOH HOH B . 
H 4 HOH 86  586 45  HOH HOH B . 
H 4 HOH 87  587 344 HOH HOH B . 
H 4 HOH 88  588 325 HOH HOH B . 
H 4 HOH 89  589 117 HOH HOH B . 
H 4 HOH 90  590 223 HOH HOH B . 
H 4 HOH 91  591 15  HOH HOH B . 
H 4 HOH 92  592 297 HOH HOH B . 
H 4 HOH 93  593 230 HOH HOH B . 
H 4 HOH 94  594 189 HOH HOH B . 
H 4 HOH 95  595 314 HOH HOH B . 
H 4 HOH 96  596 378 HOH HOH B . 
H 4 HOH 97  597 288 HOH HOH B . 
H 4 HOH 98  598 420 HOH HOH B . 
H 4 HOH 99  599 157 HOH HOH B . 
H 4 HOH 100 600 416 HOH HOH B . 
H 4 HOH 101 601 392 HOH HOH B . 
H 4 HOH 102 602 439 HOH HOH B . 
H 4 HOH 103 603 654 HOH HOH B . 
H 4 HOH 104 604 156 HOH HOH B . 
H 4 HOH 105 605 28  HOH HOH B . 
H 4 HOH 106 606 458 HOH HOH B . 
H 4 HOH 107 607 134 HOH HOH B . 
H 4 HOH 108 608 161 HOH HOH B . 
H 4 HOH 109 609 27  HOH HOH B . 
H 4 HOH 110 610 33  HOH HOH B . 
H 4 HOH 111 611 196 HOH HOH B . 
H 4 HOH 112 612 519 HOH HOH B . 
H 4 HOH 113 613 407 HOH HOH B . 
H 4 HOH 114 614 561 HOH HOH B . 
H 4 HOH 115 615 258 HOH HOH B . 
H 4 HOH 116 616 231 HOH HOH B . 
H 4 HOH 117 617 100 HOH HOH B . 
H 4 HOH 118 618 226 HOH HOH B . 
H 4 HOH 119 619 555 HOH HOH B . 
H 4 HOH 120 620 371 HOH HOH B . 
H 4 HOH 121 621 362 HOH HOH B . 
H 4 HOH 122 622 120 HOH HOH B . 
H 4 HOH 123 623 303 HOH HOH B . 
H 4 HOH 124 624 91  HOH HOH B . 
H 4 HOH 125 625 36  HOH HOH B . 
H 4 HOH 126 626 70  HOH HOH B . 
H 4 HOH 127 627 242 HOH HOH B . 
H 4 HOH 128 628 753 HOH HOH B . 
H 4 HOH 129 629 61  HOH HOH B . 
H 4 HOH 130 630 48  HOH HOH B . 
H 4 HOH 131 631 150 HOH HOH B . 
H 4 HOH 132 632 145 HOH HOH B . 
H 4 HOH 133 633 17  HOH HOH B . 
H 4 HOH 134 634 69  HOH HOH B . 
H 4 HOH 135 635 130 HOH HOH B . 
H 4 HOH 136 636 6   HOH HOH B . 
H 4 HOH 137 637 86  HOH HOH B . 
H 4 HOH 138 638 94  HOH HOH B . 
H 4 HOH 139 639 44  HOH HOH B . 
H 4 HOH 140 640 667 HOH HOH B . 
H 4 HOH 141 641 335 HOH HOH B . 
H 4 HOH 142 642 316 HOH HOH B . 
H 4 HOH 143 643 334 HOH HOH B . 
H 4 HOH 144 644 253 HOH HOH B . 
H 4 HOH 145 645 51  HOH HOH B . 
H 4 HOH 146 646 640 HOH HOH B . 
H 4 HOH 147 647 400 HOH HOH B . 
H 4 HOH 148 648 65  HOH HOH B . 
H 4 HOH 149 649 455 HOH HOH B . 
H 4 HOH 150 650 95  HOH HOH B . 
H 4 HOH 151 651 450 HOH HOH B . 
H 4 HOH 152 652 431 HOH HOH B . 
H 4 HOH 153 653 427 HOH HOH B . 
H 4 HOH 154 654 313 HOH HOH B . 
H 4 HOH 155 655 755 HOH HOH B . 
H 4 HOH 156 656 152 HOH HOH B . 
H 4 HOH 157 657 669 HOH HOH B . 
H 4 HOH 158 658 46  HOH HOH B . 
H 4 HOH 159 659 104 HOH HOH B . 
H 4 HOH 160 660 333 HOH HOH B . 
H 4 HOH 161 661 345 HOH HOH B . 
H 4 HOH 162 662 569 HOH HOH B . 
H 4 HOH 163 663 434 HOH HOH B . 
H 4 HOH 164 664 264 HOH HOH B . 
H 4 HOH 165 665 78  HOH HOH B . 
H 4 HOH 166 666 271 HOH HOH B . 
H 4 HOH 167 667 59  HOH HOH B . 
H 4 HOH 168 668 703 HOH HOH B . 
H 4 HOH 169 669 655 HOH HOH B . 
H 4 HOH 170 670 718 HOH HOH B . 
H 4 HOH 171 671 363 HOH HOH B . 
H 4 HOH 172 672 246 HOH HOH B . 
H 4 HOH 173 673 691 HOH HOH B . 
H 4 HOH 174 674 10  HOH HOH B . 
H 4 HOH 175 675 77  HOH HOH B . 
H 4 HOH 176 676 31  HOH HOH B . 
H 4 HOH 177 677 202 HOH HOH B . 
H 4 HOH 178 678 164 HOH HOH B . 
H 4 HOH 179 679 737 HOH HOH B . 
H 4 HOH 180 680 414 HOH HOH B . 
H 4 HOH 181 681 700 HOH HOH B . 
H 4 HOH 182 682 52  HOH HOH B . 
H 4 HOH 183 683 365 HOH HOH B . 
H 4 HOH 184 684 176 HOH HOH B . 
H 4 HOH 185 685 141 HOH HOH B . 
H 4 HOH 186 686 26  HOH HOH B . 
H 4 HOH 187 687 346 HOH HOH B . 
H 4 HOH 188 688 560 HOH HOH B . 
H 4 HOH 189 689 521 HOH HOH B . 
H 4 HOH 190 690 317 HOH HOH B . 
H 4 HOH 191 691 516 HOH HOH B . 
H 4 HOH 192 692 348 HOH HOH B . 
H 4 HOH 193 693 379 HOH HOH B . 
H 4 HOH 194 694 563 HOH HOH B . 
H 4 HOH 195 695 386 HOH HOH B . 
H 4 HOH 196 696 678 HOH HOH B . 
H 4 HOH 197 697 212 HOH HOH B . 
H 4 HOH 198 698 410 HOH HOH B . 
H 4 HOH 199 699 149 HOH HOH B . 
H 4 HOH 200 700 291 HOH HOH B . 
H 4 HOH 201 701 193 HOH HOH B . 
H 4 HOH 202 702 624 HOH HOH B . 
H 4 HOH 203 703 63  HOH HOH B . 
H 4 HOH 204 704 729 HOH HOH B . 
H 4 HOH 205 705 216 HOH HOH B . 
H 4 HOH 206 706 2   HOH HOH B . 
H 4 HOH 207 707 503 HOH HOH B . 
H 4 HOH 208 708 234 HOH HOH B . 
H 4 HOH 209 709 527 HOH HOH B . 
H 4 HOH 210 710 354 HOH HOH B . 
H 4 HOH 211 711 747 HOH HOH B . 
H 4 HOH 212 712 337 HOH HOH B . 
H 4 HOH 213 713 292 HOH HOH B . 
H 4 HOH 214 714 286 HOH HOH B . 
H 4 HOH 215 715 577 HOH HOH B . 
H 4 HOH 216 716 143 HOH HOH B . 
H 4 HOH 217 717 124 HOH HOH B . 
H 4 HOH 218 718 677 HOH HOH B . 
H 4 HOH 219 719 752 HOH HOH B . 
H 4 HOH 220 720 75  HOH HOH B . 
H 4 HOH 221 721 84  HOH HOH B . 
H 4 HOH 222 722 227 HOH HOH B . 
H 4 HOH 223 723 444 HOH HOH B . 
H 4 HOH 224 724 727 HOH HOH B . 
H 4 HOH 225 725 275 HOH HOH B . 
H 4 HOH 226 726 464 HOH HOH B . 
H 4 HOH 227 727 642 HOH HOH B . 
H 4 HOH 228 728 372 HOH HOH B . 
H 4 HOH 229 729 116 HOH HOH B . 
H 4 HOH 230 730 465 HOH HOH B . 
H 4 HOH 231 731 208 HOH HOH B . 
H 4 HOH 232 732 498 HOH HOH B . 
H 4 HOH 233 733 490 HOH HOH B . 
H 4 HOH 234 734 194 HOH HOH B . 
H 4 HOH 235 735 57  HOH HOH B . 
H 4 HOH 236 736 698 HOH HOH B . 
H 4 HOH 237 737 283 HOH HOH B . 
H 4 HOH 238 738 269 HOH HOH B . 
H 4 HOH 239 739 93  HOH HOH B . 
H 4 HOH 240 740 166 HOH HOH B . 
H 4 HOH 241 741 367 HOH HOH B . 
H 4 HOH 242 742 605 HOH HOH B . 
H 4 HOH 243 743 182 HOH HOH B . 
H 4 HOH 244 744 209 HOH HOH B . 
H 4 HOH 245 745 256 HOH HOH B . 
H 4 HOH 246 746 138 HOH HOH B . 
H 4 HOH 247 747 547 HOH HOH B . 
H 4 HOH 248 748 571 HOH HOH B . 
H 4 HOH 249 749 399 HOH HOH B . 
H 4 HOH 250 750 618 HOH HOH B . 
H 4 HOH 251 751 388 HOH HOH B . 
H 4 HOH 252 752 424 HOH HOH B . 
H 4 HOH 253 753 302 HOH HOH B . 
H 4 HOH 254 754 652 HOH HOH B . 
H 4 HOH 255 755 731 HOH HOH B . 
H 4 HOH 256 756 88  HOH HOH B . 
H 4 HOH 257 757 373 HOH HOH B . 
H 4 HOH 258 758 364 HOH HOH B . 
H 4 HOH 259 759 644 HOH HOH B . 
H 4 HOH 260 760 147 HOH HOH B . 
H 4 HOH 261 761 263 HOH HOH B . 
H 4 HOH 262 762 514 HOH HOH B . 
H 4 HOH 263 763 660 HOH HOH B . 
H 4 HOH 264 764 249 HOH HOH B . 
H 4 HOH 265 765 713 HOH HOH B . 
H 4 HOH 266 766 502 HOH HOH B . 
H 4 HOH 267 767 174 HOH HOH B . 
H 4 HOH 268 768 751 HOH HOH B . 
H 4 HOH 269 769 368 HOH HOH B . 
H 4 HOH 270 770 562 HOH HOH B . 
H 4 HOH 271 771 643 HOH HOH B . 
H 4 HOH 272 772 633 HOH HOH B . 
H 4 HOH 273 773 496 HOH HOH B . 
H 4 HOH 274 774 186 HOH HOH B . 
H 4 HOH 275 775 610 HOH HOH B . 
H 4 HOH 276 776 398 HOH HOH B . 
H 4 HOH 277 777 741 HOH HOH B . 
H 4 HOH 278 778 418 HOH HOH B . 
H 4 HOH 279 779 243 HOH HOH B . 
H 4 HOH 280 780 674 HOH HOH B . 
H 4 HOH 281 781 272 HOH HOH B . 
H 4 HOH 282 782 210 HOH HOH B . 
H 4 HOH 283 783 730 HOH HOH B . 
H 4 HOH 284 784 532 HOH HOH B . 
H 4 HOH 285 785 608 HOH HOH B . 
H 4 HOH 286 786 522 HOH HOH B . 
H 4 HOH 287 787 638 HOH HOH B . 
H 4 HOH 288 788 452 HOH HOH B . 
H 4 HOH 289 789 397 HOH HOH B . 
H 4 HOH 290 790 358 HOH HOH B . 
H 4 HOH 291 791 637 HOH HOH B . 
H 4 HOH 292 792 578 HOH HOH B . 
H 4 HOH 293 793 512 HOH HOH B . 
H 4 HOH 294 794 556 HOH HOH B . 
H 4 HOH 295 795 474 HOH HOH B . 
H 4 HOH 296 796 417 HOH HOH B . 
H 4 HOH 297 797 428 HOH HOH B . 
H 4 HOH 298 798 557 HOH HOH B . 
H 4 HOH 299 799 137 HOH HOH B . 
H 4 HOH 300 800 717 HOH HOH B . 
H 4 HOH 301 801 573 HOH HOH B . 
H 4 HOH 302 802 433 HOH HOH B . 
H 4 HOH 303 803 558 HOH HOH B . 
H 4 HOH 304 804 754 HOH HOH B . 
H 4 HOH 305 805 634 HOH HOH B . 
H 4 HOH 306 806 679 HOH HOH B . 
H 4 HOH 307 807 466 HOH HOH B . 
H 4 HOH 308 808 41  HOH HOH B . 
H 4 HOH 309 809 641 HOH HOH B . 
H 4 HOH 310 810 632 HOH HOH B . 
H 4 HOH 311 811 445 HOH HOH B . 
H 4 HOH 312 812 664 HOH HOH B . 
H 4 HOH 313 813 338 HOH HOH B . 
H 4 HOH 314 814 477 HOH HOH B . 
H 4 HOH 315 815 471 HOH HOH B . 
H 4 HOH 316 816 734 HOH HOH B . 
H 4 HOH 317 817 635 HOH HOH B . 
H 4 HOH 318 818 435 HOH HOH B . 
H 4 HOH 319 819 432 HOH HOH B . 
H 4 HOH 320 820 251 HOH HOH B . 
H 4 HOH 321 821 327 HOH HOH B . 
H 4 HOH 322 822 351 HOH HOH B . 
H 4 HOH 323 823 469 HOH HOH B . 
H 4 HOH 324 824 366 HOH HOH B . 
H 4 HOH 325 825 361 HOH HOH B . 
H 4 HOH 326 826 649 HOH HOH B . 
H 4 HOH 327 827 602 HOH HOH B . 
H 4 HOH 328 828 517 HOH HOH B . 
H 4 HOH 329 829 566 HOH HOH B . 
H 4 HOH 330 830 160 HOH HOH B . 
H 4 HOH 331 831 460 HOH HOH B . 
H 4 HOH 332 832 259 HOH HOH B . 
H 4 HOH 333 833 687 HOH HOH B . 
H 4 HOH 334 834 331 HOH HOH B . 
H 4 HOH 335 835 630 HOH HOH B . 
H 4 HOH 336 836 481 HOH HOH B . 
H 4 HOH 337 837 647 HOH HOH B . 
H 4 HOH 338 838 609 HOH HOH B . 
H 4 HOH 339 839 726 HOH HOH B . 
H 4 HOH 340 840 135 HOH HOH B . 
H 4 HOH 341 841 191 HOH HOH B . 
H 4 HOH 342 842 575 HOH HOH B . 
H 4 HOH 343 843 306 HOH HOH B . 
H 4 HOH 344 844 646 HOH HOH B . 
H 4 HOH 345 845 377 HOH HOH B . 
H 4 HOH 346 846 267 HOH HOH B . 
H 4 HOH 347 847 459 HOH HOH B . 
H 4 HOH 348 848 568 HOH HOH B . 
H 4 HOH 349 849 419 HOH HOH B . 
H 4 HOH 350 850 540 HOH HOH B . 
H 4 HOH 351 851 707 HOH HOH B . 
H 4 HOH 352 852 743 HOH HOH B . 
H 4 HOH 353 853 530 HOH HOH B . 
H 4 HOH 354 854 504 HOH HOH B . 
H 4 HOH 355 855 629 HOH HOH B . 
H 4 HOH 356 856 593 HOH HOH B . 
H 4 HOH 357 857 680 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 17  ? CG    ? A LYS 23  CG    
2   1 Y 1 A LYS 17  ? CD    ? A LYS 23  CD    
3   1 Y 1 A LYS 17  ? CE    ? A LYS 23  CE    
4   1 Y 1 A LYS 17  ? NZ    ? A LYS 23  NZ    
5   1 Y 1 A LYS 83  ? CG    ? A LYS 89  CG    
6   1 Y 1 A LYS 83  ? CD    ? A LYS 89  CD    
7   1 Y 1 A LYS 83  ? CE    ? A LYS 89  CE    
8   1 Y 1 A LYS 83  ? NZ    ? A LYS 89  NZ    
9   1 Y 1 A GLU 116 ? CG    ? A GLU 122 CG    
10  1 Y 1 A GLU 116 ? CD    ? A GLU 122 CD    
11  1 Y 1 A GLU 116 ? OE1   ? A GLU 122 OE1   
12  1 Y 1 A GLU 116 ? OE2   ? A GLU 122 OE2   
13  1 Y 1 A ARG 136 ? CG    ? A ARG 142 CG    
14  1 Y 1 A ARG 136 ? CD    ? A ARG 142 CD    
15  1 Y 1 A ARG 136 ? NE    ? A ARG 142 NE    
16  1 Y 1 A ARG 136 ? CZ    ? A ARG 142 CZ    
17  1 Y 1 A ARG 136 ? NH1   ? A ARG 142 NH1   
18  1 Y 1 A ARG 136 ? NH2   ? A ARG 142 NH2   
19  1 Y 1 A HIS 244 ? NE2   ? A HIS 250 NE2   
20  1 Y 1 A LYS 265 ? CG    ? A LYS 271 CG    
21  1 Y 1 A LYS 265 ? CD    ? A LYS 271 CD    
22  1 Y 1 A LYS 265 ? CE    ? A LYS 271 CE    
23  1 Y 1 A LYS 265 ? NZ    ? A LYS 271 NZ    
24  1 Y 1 A HIS 269 ? CG    ? A HIS 275 CG    
25  1 Y 1 A HIS 269 ? ND1   ? A HIS 275 ND1   
26  1 Y 1 A HIS 269 ? CD2   ? A HIS 275 CD2   
27  1 Y 1 A HIS 269 ? CE1   ? A HIS 275 CE1   
28  1 Y 1 A HIS 269 ? NE2   ? A HIS 275 NE2   
29  1 Y 1 A ARG 303 ? CG    ? A ARG 309 CG    
30  1 Y 1 A ARG 303 ? CD    ? A ARG 309 CD    
31  1 Y 1 A ARG 303 ? NE    ? A ARG 309 NE    
32  1 Y 1 A ARG 303 ? CZ    ? A ARG 309 CZ    
33  1 Y 1 A ARG 303 ? NH1   ? A ARG 309 NH1   
34  1 Y 1 A ARG 303 ? NH2   ? A ARG 309 NH2   
35  1 Y 1 A GLU 325 ? CG    ? A GLU 331 CG    
36  1 Y 1 A GLU 325 ? CD    ? A GLU 331 CD    
37  1 Y 1 A GLU 325 ? OE1   ? A GLU 331 OE1   
38  1 Y 1 A GLU 325 ? OE2   ? A GLU 331 OE2   
39  1 Y 1 A LYS 367 ? CG    ? A LYS 373 CG    
40  1 Y 1 A LYS 367 ? CD    ? A LYS 373 CD    
41  1 Y 1 A LYS 367 ? CE    ? A LYS 373 CE    
42  1 Y 1 A LYS 367 ? NZ    ? A LYS 373 NZ    
43  1 Y 1 B GLU 48  ? CG    ? B GLU 54  CG    
44  1 Y 1 B GLU 48  ? CD    ? B GLU 54  CD    
45  1 Y 1 B GLU 48  ? OE1   ? B GLU 54  OE1   
46  1 Y 1 B GLU 48  ? OE2   ? B GLU 54  OE2   
47  1 Y 1 B ASN 135 ? CG    ? B ASN 141 CG    
48  1 Y 1 B ASN 135 ? OD1   ? B ASN 141 OD1   
49  1 Y 1 B ASN 135 ? ND2   ? B ASN 141 ND2   
50  1 Y 1 B ARG 136 ? CG    ? B ARG 142 CG    
51  1 Y 1 B ARG 136 ? CD    ? B ARG 142 CD    
52  1 Y 1 B ARG 136 ? NE    ? B ARG 142 NE    
53  1 Y 1 B ARG 136 ? CZ    ? B ARG 142 CZ    
54  1 Y 1 B ARG 136 ? NH1   ? B ARG 142 NH1   
55  1 Y 1 B ARG 136 ? NH2   ? B ARG 142 NH2   
56  1 Y 1 B ARG 169 ? CG    ? B ARG 175 CG    
57  1 Y 1 B ARG 169 ? CD    ? B ARG 175 CD    
58  1 Y 1 B ARG 169 ? NE    ? B ARG 175 NE    
59  1 Y 1 B ARG 169 ? CZ    ? B ARG 175 CZ    
60  1 Y 1 B ARG 169 ? NH1   ? B ARG 175 NH1   
61  1 Y 1 B ARG 169 ? NH2   ? B ARG 175 NH2   
62  1 Y 1 B HIS 269 ? CG    ? B HIS 275 CG    
63  1 Y 1 B HIS 269 ? ND1   ? B HIS 275 ND1   
64  1 Y 1 B HIS 269 ? CD2   ? B HIS 275 CD2   
65  1 Y 1 B HIS 269 ? CE1   ? B HIS 275 CE1   
66  1 Y 1 B HIS 269 ? NE2   ? B HIS 275 NE2   
67  1 Y 1 B LYS 367 ? CG    ? B LYS 373 CG    
68  1 Y 1 B LYS 367 ? CD    ? B LYS 373 CD    
69  1 Y 1 B LYS 367 ? CE    ? B LYS 373 CE    
70  1 Y 1 B LYS 367 ? NZ    ? B LYS 373 NZ    
71  1 N 1 A WI6 402 ? "C5'" ? D WI6 1   "C5'" 
72  1 N 1 A WI6 402 ? "C4'" ? D WI6 1   "C4'" 
73  1 N 1 A WI6 402 ? "O4'" ? D WI6 1   "O4'" 
74  1 N 1 A WI6 402 ? "C1'" ? D WI6 1   "C1'" 
75  1 N 1 A WI6 402 ? "C2'" ? D WI6 1   "C2'" 
76  1 N 1 A WI6 402 ? "C3'" ? D WI6 1   "C3'" 
77  1 N 1 A WI6 402 ? N9A   ? D WI6 1   N9A   
78  1 N 1 A WI6 402 ? C4A   ? D WI6 1   C4A   
79  1 N 1 A WI6 402 ? C5A   ? D WI6 1   C5A   
80  1 N 1 A WI6 402 ? N7A   ? D WI6 1   N7A   
81  1 N 1 A WI6 402 ? C8A   ? D WI6 1   C8A   
82  1 N 1 A WI6 402 ? C6A   ? D WI6 1   C6A   
83  1 N 1 A WI6 402 ? N1A   ? D WI6 1   N1A   
84  1 N 1 A WI6 402 ? C2A   ? D WI6 1   C2A   
85  1 N 1 A WI6 402 ? N3A   ? D WI6 1   N3A   
86  1 N 1 A WI6 402 ? "O2'" ? D WI6 1   "O2'" 
87  1 N 1 A WI6 402 ? "O3'" ? D WI6 1   "O3'" 
88  1 N 1 A WI6 402 ? N6A   ? D WI6 1   N6A   
89  1 N 1 B WI6 402 ? "C5'" ? F WI6 1   "C5'" 
90  1 N 1 B WI6 402 ? "C4'" ? F WI6 1   "C4'" 
91  1 N 1 B WI6 402 ? "O4'" ? F WI6 1   "O4'" 
92  1 N 1 B WI6 402 ? "C1'" ? F WI6 1   "C1'" 
93  1 N 1 B WI6 402 ? "C2'" ? F WI6 1   "C2'" 
94  1 N 1 B WI6 402 ? "C3'" ? F WI6 1   "C3'" 
95  1 N 1 B WI6 402 ? N9A   ? F WI6 1   N9A   
96  1 N 1 B WI6 402 ? C4A   ? F WI6 1   C4A   
97  1 N 1 B WI6 402 ? C5A   ? F WI6 1   C5A   
98  1 N 1 B WI6 402 ? N7A   ? F WI6 1   N7A   
99  1 N 1 B WI6 402 ? C8A   ? F WI6 1   C8A   
100 1 N 1 B WI6 402 ? C6A   ? F WI6 1   C6A   
101 1 N 1 B WI6 402 ? N1A   ? F WI6 1   N1A   
102 1 N 1 B WI6 402 ? C2A   ? F WI6 1   C2A   
103 1 N 1 B WI6 402 ? N3A   ? F WI6 1   N3A   
104 1 N 1 B WI6 402 ? "O2'" ? F WI6 1   "O2'" 
105 1 N 1 B WI6 402 ? "O3'" ? F WI6 1   "O3'" 
106 1 N 1 B WI6 402 ? N6A   ? F WI6 1   N6A   
# 
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'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? .            3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? '(dev_4761)' 4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   97.73 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8QO8 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     49.470 
_cell.length_a_esd                 ? 
_cell.length_b                     93.320 
_cell.length_b_esd                 ? 
_cell.length_c                     89.400 
_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                         8QO8 
_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                   8QO8 
_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          46.62 
_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, 10 mM ammonium sulfate, 14% 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   1.0332 
_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        1.0332 
_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                                       8QO8 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.47 
_reflns.d_resolution_low                               46.66 
_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                                     905053 
_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                           97.17 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.88 
_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                                   0.998 
_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                                    1.47 
_reflns_shell.d_res_low                                     1.51 
_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                             44830 
_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                                  0.62 
_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                                 8QO8 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.47 
_refine.ls_d_res_low                             46.66 
_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                     132568 
_refine.ls_number_reflns_R_free                  1874 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.17 
_refine.ls_percent_reflns_R_free                 1.41 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1870 
_refine.ls_R_factor_R_free                       0.2036 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1868 
_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                 29.12 
_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                            0.20 
_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        5484 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         114 
_refine_hist.number_atoms_solvent             743 
_refine_hist.number_atoms_total               6341 
_refine_hist.d_res_high                       1.47 
_refine_hist.d_res_low                        46.66 
# 
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' ? 0.010  ? 5757 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.093  ? 7851 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 15.879 ? 2078 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.085  ? 868  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.015  ? 1007 ? 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' 1.47 1.51  . . 121 8381  81.00  . . . . 0.4343 . . . . . . . . . . . 0.4987 
'X-RAY DIFFRACTION' 1.51 1.55  . . 140 9803  95.00  . . . . 0.3618 . . . . . . . . . . . 0.3973 
'X-RAY DIFFRACTION' 1.55 1.60  . . 146 10219 99.00  . . . . 0.3051 . . . . . . . . . . . 0.3662 
'X-RAY DIFFRACTION' 1.60 1.66  . . 145 10169 99.00  . . . . 0.2773 . . . . . . . . . . . 0.2898 
'X-RAY DIFFRACTION' 1.66 1.73  . . 147 10185 99.00  . . . . 0.2519 . . . . . . . . . . . 0.2752 
'X-RAY DIFFRACTION' 1.73 1.81  . . 146 10134 98.00  . . . . 0.2186 . . . . . . . . . . . 0.2697 
'X-RAY DIFFRACTION' 1.81 1.90  . . 143 10045 97.00  . . . . 0.1976 . . . . . . . . . . . 0.2135 
'X-RAY DIFFRACTION' 1.90 2.02  . . 147 10252 100.00 . . . . 0.1783 . . . . . . . . . . . 0.1794 
'X-RAY DIFFRACTION' 2.02 2.18  . . 149 10318 100.00 . . . . 0.1780 . . . . . . . . . . . 0.1846 
'X-RAY DIFFRACTION' 2.18 2.40  . . 146 10307 100.00 . . . . 0.1734 . . . . . . . . . . . 0.1945 
'X-RAY DIFFRACTION' 2.40 2.74  . . 146 10140 98.00  . . . . 0.1785 . . . . . . . . . . . 0.2058 
'X-RAY DIFFRACTION' 2.74 3.46  . . 148 10349 100.00 . . . . 0.1740 . . . . . . . . . . . 0.1792 
'X-RAY DIFFRACTION' 3.46 46.66 . . 150 10392 99.00  . . . . 0.1529 . . . . . . . . . . . 0.1668 
# 
_struct.entry_id                     8QO8 
_struct.title                        'OPR3 variant R283E in complex with NADH4' 
_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        8QO8 
_struct_keywords.text            'Old Yellow Enzyme, ene-reductase, flavoenzyme, 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 8QO8 A 7 ? 402 ? Q9FEW9 1 ? 396 ? 1 396 
2 1 8QO8 B 7 ? 402 ? Q9FEW9 1 ? 396 ? 1 396 
# 
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 8QO8 HIS A 1   ? UNP Q9FEW9 ?   ?   'expression tag'      -5  1  
1 8QO8 HIS A 2   ? UNP Q9FEW9 ?   ?   'expression tag'      -4  2  
1 8QO8 HIS A 3   ? UNP Q9FEW9 ?   ?   'expression tag'      -3  3  
1 8QO8 HIS A 4   ? UNP Q9FEW9 ?   ?   'expression tag'      -2  4  
1 8QO8 HIS A 5   ? UNP Q9FEW9 ?   ?   'expression tag'      -1  5  
1 8QO8 HIS A 6   ? UNP Q9FEW9 ?   ?   'expression tag'      0   6  
1 8QO8 GLU A 289 ? UNP Q9FEW9 ARG 283 'engineered mutation' 283 7  
2 8QO8 HIS B 1   ? UNP Q9FEW9 ?   ?   'expression tag'      -5  8  
2 8QO8 HIS B 2   ? UNP Q9FEW9 ?   ?   'expression tag'      -4  9  
2 8QO8 HIS B 3   ? UNP Q9FEW9 ?   ?   'expression tag'      -3  10 
2 8QO8 HIS B 4   ? UNP Q9FEW9 ?   ?   'expression tag'      -2  11 
2 8QO8 HIS B 5   ? UNP Q9FEW9 ?   ?   'expression tag'      -1  12 
2 8QO8 HIS B 6   ? UNP Q9FEW9 ?   ?   'expression tag'      0   13 
2 8QO8 GLU B 289 ? UNP Q9FEW9 ARG 283 'engineered mutation' 283 14 
# 
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 16  ? SER A 20  ? ASN A 10  SER A 14  5 ? 5  
HELX_P HELX_P2  AA2 ALA A 43  ? ILE A 47  ? ALA A 37  ILE A 41  5 ? 5  
HELX_P HELX_P3  AA3 GLN A 49  ? ALA A 60  ? GLN A 43  ALA A 54  1 ? 12 
HELX_P HELX_P4  AA4 THR A 88  ? ALA A 104 ? THR A 82  ALA A 98  1 ? 17 
HELX_P HELX_P5  AA5 HIS A 121 ? ALA A 129 ? HIS A 115 ALA A 123 5 ? 9  
HELX_P HELX_P6  AA6 GLY A 162 ? ALA A 183 ? GLY A 156 ALA A 177 1 ? 22 
HELX_P HELX_P7  AA7 TYR A 196 ? LYS A 203 ? TYR A 190 LYS A 197 1 ? 8  
HELX_P HELX_P8  AA8 SER A 216 ? CYS A 221 ? SER A 210 CYS A 215 1 ? 6  
HELX_P HELX_P9  AA9 CYS A 221 ? GLY A 236 ? CYS A 215 GLY A 230 1 ? 16 
HELX_P HELX_P10 AB1 ASN A 257 ? GLY A 277 ? ASN A 251 GLY A 271 1 ? 21 
HELX_P HELX_P11 AB2 LEU A 310 ? TYR A 318 ? LEU A 304 TYR A 312 1 ? 9  
HELX_P HELX_P12 AB3 THR A 329 ? GLN A 339 ? THR A 323 GLN A 333 1 ? 11 
HELX_P HELX_P13 AB4 GLY A 348 ? ASN A 354 ? GLY A 342 ASN A 348 1 ? 7  
HELX_P HELX_P14 AB5 ASP A 356 ? ASN A 364 ? ASP A 350 ASN A 358 1 ? 9  
HELX_P HELX_P15 AB6 ASN A 371 ? PHE A 375 ? ASN A 365 PHE A 369 5 ? 5  
HELX_P HELX_P16 AB7 ASN B 16  ? SER B 20  ? ASN B 10  SER B 14  5 ? 5  
HELX_P HELX_P17 AB8 ALA B 43  ? ILE B 47  ? ALA B 37  ILE B 41  5 ? 5  
HELX_P HELX_P18 AB9 GLN B 49  ? ALA B 60  ? GLN B 43  ALA B 54  1 ? 12 
HELX_P HELX_P19 AC1 THR B 88  ? ALA B 104 ? THR B 82  ALA B 98  1 ? 17 
HELX_P HELX_P20 AC2 HIS B 121 ? ALA B 129 ? HIS B 115 ALA B 123 5 ? 9  
HELX_P HELX_P21 AC3 GLY B 162 ? ALA B 183 ? GLY B 156 ALA B 177 1 ? 22 
HELX_P HELX_P22 AC4 TYR B 196 ? LYS B 203 ? TYR B 190 LYS B 197 1 ? 8  
HELX_P HELX_P23 AC5 SER B 216 ? CYS B 221 ? SER B 210 CYS B 215 1 ? 6  
HELX_P HELX_P24 AC6 CYS B 221 ? GLY B 236 ? CYS B 215 GLY B 230 1 ? 16 
HELX_P HELX_P25 AC7 ASN B 257 ? GLY B 277 ? ASN B 251 GLY B 271 1 ? 21 
HELX_P HELX_P26 AC8 ARG B 309 ? TYR B 318 ? ARG B 303 TYR B 312 1 ? 10 
HELX_P HELX_P27 AC9 THR B 329 ? GLN B 339 ? THR B 323 GLN B 333 1 ? 11 
HELX_P HELX_P28 AD1 GLY B 348 ? ASN B 354 ? GLY B 342 ASN B 348 1 ? 7  
HELX_P HELX_P29 AD2 ASP B 356 ? ASN B 364 ? ASP B 350 ASN B 358 1 ? 9  
HELX_P HELX_P30 AD3 ASN B 371 ? PHE B 375 ? ASN B 365 PHE B 369 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 ? 10 ? 
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      
AA6 9 10 ? 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 22  ? MET A 24  ? TYR A 16  MET A 18  
AA1 2  PHE A 27  ? LEU A 29  ? PHE A 21  LEU A 23  
AA2 1  VAL A 33  ? LEU A 35  ? VAL A 27  LEU A 29  
AA2 2  PHE A 65  ? MET A 72  ? PHE A 59  MET A 66  
AA2 3  VAL A 108 ? TRP A 114 ? VAL A 102 TRP A 108 
AA2 4  GLY A 187 ? GLY A 192 ? GLY A 181 GLY A 186 
AA2 5  VAL A 240 ? VAL A 244 ? VAL A 234 VAL A 238 
AA2 6  TYR A 282 ? THR A 286 ? TYR A 276 THR A 280 
AA2 7  PHE A 322 ? SER A 325 ? PHE A 316 SER A 319 
AA2 8  LEU A 344 ? TYR A 347 ? LEU A 338 TYR A 341 
AA2 9  VAL A 33  ? LEU A 35  ? VAL A 27  LEU A 29  
AA3 1  ILE A 132 ? SER A 133 ? ILE A 126 SER A 127 
AA3 2  ARG A 159 ? ALA A 160 ? ARG A 153 ALA A 154 
AA4 1  ARG A 144 ? LEU A 146 ? ARG A 138 LEU A 140 
AA4 2  HIS A 152 ? ILE A 154 ? HIS A 146 ILE A 148 
AA5 1  TYR B 22  ? MET B 24  ? TYR B 16  MET B 18  
AA5 2  PHE B 27  ? LEU B 29  ? PHE B 21  LEU B 23  
AA6 1  THR B 71  ? MET B 72  ? THR B 65  MET B 66  
AA6 2  VAL B 108 ? TRP B 114 ? VAL B 102 TRP B 108 
AA6 3  GLY B 187 ? GLY B 192 ? GLY B 181 GLY B 186 
AA6 4  VAL B 240 ? VAL B 244 ? VAL B 234 VAL B 238 
AA6 5  TYR B 282 ? THR B 286 ? TYR B 276 THR B 280 
AA6 6  PHE B 322 ? SER B 325 ? PHE B 316 SER B 319 
AA6 7  LEU B 344 ? TYR B 347 ? LEU B 338 TYR B 341 
AA6 8  VAL B 33  ? LEU B 35  ? VAL B 27  LEU B 29  
AA6 9  PHE B 65  ? ILE B 67  ? PHE B 59  ILE B 61  
AA6 10 VAL B 108 ? TRP B 114 ? VAL B 102 TRP B 108 
AA7 1  ILE B 132 ? SER B 133 ? ILE B 126 SER B 127 
AA7 2  ARG B 159 ? ALA B 160 ? ARG B 153 ALA B 154 
AA8 1  ARG B 144 ? LEU B 146 ? ARG B 138 LEU B 140 
AA8 2  HIS B 152 ? ILE B 154 ? HIS B 146 ILE B 148 
# 
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 22  ? N TYR A 16  O LEU A 29  ? O LEU A 23  
AA2 1 2  N LEU A 35  ? N LEU A 29  O PHE A 65  ? O PHE A 59  
AA2 2 3  N THR A 71  ? N THR A 65  O TRP A 114 ? O TRP A 108 
AA2 3 4  N LEU A 113 ? N LEU A 107 O GLU A 189 ? O GLU A 183 
AA2 4 5  N ILE A 188 ? N ILE A 182 O GLY A 241 ? O GLY A 235 
AA2 5 6  N VAL A 242 ? N VAL A 236 O HIS A 284 ? O HIS A 278 
AA2 6 7  N LEU A 283 ? N LEU A 277 O ILE A 323 ? O ILE A 317 
AA2 7 8  N CYS A 324 ? N CYS A 318 O SER A 346 ? O SER A 340 
AA2 8 9  O VAL A 345 ? O VAL A 339 N VAL A 34  ? N VAL A 28  
AA3 1 2  N SER A 133 ? N SER A 127 O ARG A 159 ? O ARG A 153 
AA4 1 2  N ILE A 145 ? N ILE A 139 O GLY A 153 ? O GLY A 147 
AA5 1 2  N TYR B 22  ? N TYR B 16  O LEU B 29  ? O LEU B 23  
AA6 1 2  N THR B 71  ? N THR B 65  O TRP B 114 ? O TRP B 108 
AA6 2 3  N LEU B 113 ? N LEU B 107 O GLU B 189 ? O GLU B 183 
AA6 3 4  N ILE B 188 ? N ILE B 182 O GLY B 241 ? O GLY B 235 
AA6 4 5  N VAL B 242 ? N VAL B 236 O HIS B 284 ? O HIS B 278 
AA6 5 6  N LEU B 283 ? N LEU B 277 O ILE B 323 ? O ILE B 317 
AA6 6 7  N CYS B 324 ? N CYS B 318 O SER B 346 ? O SER B 340 
AA6 7 8  O VAL B 345 ? O VAL B 339 N VAL B 34  ? N VAL B 28  
AA6 8 9  N LEU B 35  ? N LEU B 29  O PHE B 65  ? O PHE B 59  
AA6 9 10 N LEU B 66  ? N LEU B 60  O VAL B 108 ? O VAL B 102 
AA7 1 2  N SER B 133 ? N SER B 127 O ARG B 159 ? O ARG B 153 
AA8 1 2  N ILE B 145 ? N ILE B 139 O GLY B 153 ? O GLY B 147 
# 
_pdbx_entry_details.entry_id                   8QO8 
_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 798 ? ? O B HOH 851 ? ? 1.88 
2  1 O   A HOH 767 ? ? O A HOH 803 ? ? 1.94 
3  1 O   A HOH 732 ? ? O A HOH 815 ? ? 1.94 
4  1 O   A HOH 756 ? ? O A HOH 834 ? ? 1.95 
5  1 O   A HOH 800 ? ? O A HOH 866 ? ? 2.07 
6  1 O   A HOH 514 ? ? O A HOH 651 ? ? 2.10 
7  1 O   B HOH 742 ? ? O B HOH 762 ? ? 2.11 
8  1 O   B HOH 578 ? ? O B HOH 620 ? ? 2.12 
9  1 O   A HOH 839 ? ? O A HOH 853 ? ? 2.13 
10 1 O   B HOH 800 ? ? O B HOH 804 ? ? 2.15 
11 1 O   B HOH 822 ? ? O B HOH 847 ? ? 2.15 
12 1 OE1 A GLU 130 ? ? O A HOH 501 ? ? 2.16 
13 1 O   A HOH 559 ? ? O A HOH 709 ? ? 2.19 
14 1 O   B HOH 565 ? ? O B HOH 580 ? ? 2.19 
15 1 O   B HOH 807 ? ? O B HOH 814 ? ? 2.19 
# 
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  ? ? -140.73 29.82  
2  1 ALA A 121 ? ? 58.68   18.70  
3  1 SER A 239 ? ? -150.50 71.56  
4  1 ALA A 247 ? ? -116.17 72.07  
5  1 ASP A 350 ? ? -96.24  42.17  
6  1 VAL A 375 ? ? -123.52 -54.74 
7  1 TYR A 378 ? ? -127.97 -61.27 
8  1 SER B 239 ? ? -150.95 70.58  
9  1 ALA B 247 ? ? -104.96 66.34  
10 1 ASP B 350 ? ? -95.78  42.12  
11 1 VAL B 375 ? ? -121.91 -51.44 
12 1 TYR B 378 ? ? -128.52 -64.52 
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    B 
_pdbx_validate_planes.auth_seq_id     303 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.236 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 885 ? 6.30 . 
2 1 O ? A HOH 886 ? 6.60 . 
3 1 O ? B HOH 856 ? 6.62 . 
4 1 O ? B HOH 857 ? 7.39 . 
# 
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 HIS -5  ? A HIS 1   
2  1 Y 1 A HIS -4  ? A HIS 2   
3  1 Y 1 A HIS -3  ? A HIS 3   
4  1 Y 1 A HIS -2  ? A HIS 4   
5  1 Y 1 A HIS -1  ? A HIS 5   
6  1 Y 1 A HIS 0   ? A HIS 6   
7  1 Y 1 A MET 1   ? A MET 7   
8  1 Y 1 A ALA 2   ? A ALA 8   
9  1 Y 1 A SER 3   ? A SER 9   
10 1 Y 1 A SER 4   ? A SER 10  
11 1 Y 1 A ALA 5   ? A ALA 11  
12 1 Y 1 A GLN 6   ? A GLN 12  
13 1 Y 1 A ASP 7   ? A ASP 13  
14 1 Y 1 A GLY 8   ? A GLY 14  
15 1 Y 1 A ASN 9   ? A ASN 15  
16 1 Y 1 A TYR 284 ? A TYR 290 
17 1 Y 1 A VAL 285 ? A VAL 291 
18 1 Y 1 A ALA 286 ? A ALA 292 
19 1 Y 1 A TYR 287 ? A TYR 293 
20 1 Y 1 A GLY 288 ? A GLY 294 
21 1 Y 1 A GLN 289 ? A GLN 295 
22 1 Y 1 A THR 290 ? A THR 296 
23 1 Y 1 A GLU 291 ? A GLU 297 
24 1 Y 1 A ALA 292 ? A ALA 298 
25 1 Y 1 A GLY 293 ? A GLY 299 
26 1 Y 1 A ARG 294 ? A ARG 300 
27 1 Y 1 A LEU 295 ? A LEU 301 
28 1 Y 1 A GLY 296 ? A GLY 302 
29 1 Y 1 A SER 297 ? A SER 303 
30 1 Y 1 A GLU 298 ? A GLU 304 
31 1 Y 1 A GLU 299 ? A GLU 305 
32 1 Y 1 A GLU 300 ? A GLU 306 
33 1 Y 1 A GLU 301 ? A GLU 307 
34 1 Y 1 A ALA 302 ? A ALA 308 
35 1 Y 1 A GLN 385 ? A GLN 391 
36 1 Y 1 A GLY 386 ? A GLY 392 
37 1 Y 1 A ASN 387 ? A ASN 393 
38 1 Y 1 A GLY 388 ? A GLY 394 
39 1 Y 1 A SER 389 ? A SER 395 
40 1 Y 1 A ASN 390 ? A ASN 396 
41 1 Y 1 A GLY 391 ? A GLY 397 
42 1 Y 1 A PRO 392 ? A PRO 398 
43 1 Y 1 A LEU 393 ? A LEU 399 
44 1 Y 1 A SER 394 ? A SER 400 
45 1 Y 1 A ARG 395 ? A ARG 401 
46 1 Y 1 A LEU 396 ? A LEU 402 
47 1 Y 1 B HIS -5  ? B HIS 1   
48 1 Y 1 B HIS -4  ? B HIS 2   
49 1 Y 1 B HIS -3  ? B HIS 3   
50 1 Y 1 B HIS -2  ? B HIS 4   
51 1 Y 1 B HIS -1  ? B HIS 5   
52 1 Y 1 B HIS 0   ? B HIS 6   
53 1 Y 1 B MET 1   ? B MET 7   
54 1 Y 1 B ALA 2   ? B ALA 8   
55 1 Y 1 B SER 3   ? B SER 9   
56 1 Y 1 B SER 4   ? B SER 10  
57 1 Y 1 B ALA 5   ? B ALA 11  
58 1 Y 1 B GLN 6   ? B GLN 12  
59 1 Y 1 B ASP 7   ? B ASP 13  
60 1 Y 1 B GLY 8   ? B GLY 14  
61 1 Y 1 B ASN 9   ? B ASN 15  
62 1 Y 1 B GLU 283 ? B GLU 289 
63 1 Y 1 B TYR 284 ? B TYR 290 
64 1 Y 1 B VAL 285 ? B VAL 291 
65 1 Y 1 B ALA 286 ? B ALA 292 
66 1 Y 1 B TYR 287 ? B TYR 293 
67 1 Y 1 B GLY 288 ? B GLY 294 
68 1 Y 1 B GLN 289 ? B GLN 295 
69 1 Y 1 B THR 290 ? B THR 296 
70 1 Y 1 B GLU 291 ? B GLU 297 
71 1 Y 1 B ALA 292 ? B ALA 298 
72 1 Y 1 B GLY 293 ? B GLY 299 
73 1 Y 1 B ARG 294 ? B ARG 300 
74 1 Y 1 B LEU 295 ? B LEU 301 
75 1 Y 1 B GLY 296 ? B GLY 302 
76 1 Y 1 B SER 297 ? B SER 303 
77 1 Y 1 B GLU 298 ? B GLU 304 
78 1 Y 1 B GLU 299 ? B GLU 305 
79 1 Y 1 B GLU 300 ? B GLU 306 
80 1 Y 1 B GLU 301 ? B GLU 307 
81 1 Y 1 B GLN 385 ? B GLN 391 
82 1 Y 1 B GLY 386 ? B GLY 392 
83 1 Y 1 B ASN 387 ? B ASN 393 
84 1 Y 1 B GLY 388 ? B GLY 394 
85 1 Y 1 B SER 389 ? B SER 395 
86 1 Y 1 B ASN 390 ? B ASN 396 
87 1 Y 1 B GLY 391 ? B GLY 397 
88 1 Y 1 B PRO 392 ? B PRO 398 
89 1 Y 1 B LEU 393 ? B LEU 399 
90 1 Y 1 B SER 394 ? B SER 400 
91 1 Y 1 B ARG 395 ? B ARG 401 
92 1 Y 1 B LEU 396 ? B LEU 402 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N      N N N 1   
ALA CA     C N S 2   
ALA C      C N N 3   
ALA O      O N N 4   
ALA CB     C N N 5   
ALA OXT    O N N 6   
ALA H      H N N 7   
ALA H2     H N N 8   
ALA HA     H N N 9   
ALA HB1    H N N 10  
ALA HB2    H N N 11  
ALA HB3    H N N 12  
ALA HXT    H N N 13  
ARG N      N N N 14  
ARG CA     C N S 15  
ARG C      C N N 16  
ARG O      O N N 17  
ARG CB     C N N 18  
ARG CG     C N N 19  
ARG CD     C N N 20  
ARG NE     N N N 21  
ARG CZ     C N N 22  
ARG NH1    N N N 23  
ARG NH2    N N N 24  
ARG OXT    O N N 25  
ARG H      H N N 26  
ARG H2     H N N 27  
ARG HA     H N N 28  
ARG HB2    H N N 29  
ARG HB3    H N N 30  
ARG HG2    H N N 31  
ARG HG3    H N N 32  
ARG HD2    H N N 33  
ARG HD3    H N N 34  
ARG HE     H N N 35  
ARG HH11   H N N 36  
ARG HH12   H N N 37  
ARG HH21   H N N 38  
ARG HH22   H N N 39  
ARG HXT    H N N 40  
ASN N      N N N 41  
ASN CA     C N S 42  
ASN C      C N N 43  
ASN O      O N N 44  
ASN CB     C N N 45  
ASN CG     C N N 46  
ASN OD1    O N N 47  
ASN ND2    N N N 48  
ASN OXT    O N N 49  
ASN H      H N N 50  
ASN H2     H N N 51  
ASN HA     H N N 52  
ASN HB2    H N N 53  
ASN HB3    H N N 54  
ASN HD21   H N N 55  
ASN HD22   H N N 56  
ASN HXT    H N N 57  
ASP N      N N N 58  
ASP CA     C N S 59  
ASP C      C N N 60  
ASP O      O N N 61  
ASP CB     C N N 62  
ASP CG     C N N 63  
ASP OD1    O N N 64  
ASP OD2    O N N 65  
ASP OXT    O N N 66  
ASP H      H N N 67  
ASP H2     H N N 68  
ASP HA     H N N 69  
ASP HB2    H N N 70  
ASP HB3    H N N 71  
ASP HD2    H N N 72  
ASP HXT    H N N 73  
CYS N      N N N 74  
CYS CA     C N R 75  
CYS C      C N N 76  
CYS O      O N N 77  
CYS CB     C N N 78  
CYS SG     S N N 79  
CYS OXT    O N N 80  
CYS H      H N N 81  
CYS H2     H N N 82  
CYS HA     H N N 83  
CYS HB2    H N N 84  
CYS HB3    H N N 85  
CYS HG     H N N 86  
CYS HXT    H N N 87  
FMN N1     N N N 88  
FMN C2     C N N 89  
FMN O2     O N N 90  
FMN N3     N N N 91  
FMN C4     C N N 92  
FMN O4     O N N 93  
FMN C4A    C N N 94  
FMN N5     N N N 95  
FMN C5A    C Y N 96  
FMN C6     C Y N 97  
FMN C7     C Y N 98  
FMN C7M    C N N 99  
FMN C8     C Y N 100 
FMN C8M    C N N 101 
FMN C9     C Y N 102 
FMN C9A    C Y N 103 
FMN N10    N N N 104 
FMN C10    C N N 105 
FMN "C1'"  C N N 106 
FMN "C2'"  C N S 107 
FMN "O2'"  O N N 108 
FMN "C3'"  C N S 109 
FMN "O3'"  O N N 110 
FMN "C4'"  C N R 111 
FMN "O4'"  O N N 112 
FMN "C5'"  C N N 113 
FMN "O5'"  O N N 114 
FMN P      P N N 115 
FMN O1P    O N N 116 
FMN O2P    O N N 117 
FMN O3P    O N N 118 
FMN HN3    H N N 119 
FMN H6     H N N 120 
FMN HM71   H N N 121 
FMN HM72   H N N 122 
FMN HM73   H N N 123 
FMN HM81   H N N 124 
FMN HM82   H N N 125 
FMN HM83   H N N 126 
FMN H9     H N N 127 
FMN "H1'1" H N N 128 
FMN "H1'2" H N N 129 
FMN "H2'"  H N N 130 
FMN "HO2'" H N N 131 
FMN "H3'"  H N N 132 
FMN "HO3'" H N N 133 
FMN "H4'"  H N N 134 
FMN "HO4'" H N N 135 
FMN "H5'1" H N N 136 
FMN "H5'2" H N N 137 
FMN HOP2   H N N 138 
FMN HOP3   H N N 139 
GLN N      N N N 140 
GLN CA     C N S 141 
GLN C      C N N 142 
GLN O      O N N 143 
GLN CB     C N N 144 
GLN CG     C N N 145 
GLN CD     C N N 146 
GLN OE1    O N N 147 
GLN NE2    N N N 148 
GLN OXT    O N N 149 
GLN H      H N N 150 
GLN H2     H N N 151 
GLN HA     H N N 152 
GLN HB2    H N N 153 
GLN HB3    H N N 154 
GLN HG2    H N N 155 
GLN HG3    H N N 156 
GLN HE21   H N N 157 
GLN HE22   H N N 158 
GLN HXT    H N N 159 
GLU N      N N N 160 
GLU CA     C N S 161 
GLU C      C N N 162 
GLU O      O N N 163 
GLU CB     C N N 164 
GLU CG     C N N 165 
GLU CD     C N N 166 
GLU OE1    O N N 167 
GLU OE2    O N N 168 
GLU OXT    O N N 169 
GLU H      H N N 170 
GLU H2     H N N 171 
GLU HA     H N N 172 
GLU HB2    H N N 173 
GLU HB3    H N N 174 
GLU HG2    H N N 175 
GLU HG3    H N N 176 
GLU HE2    H N N 177 
GLU HXT    H N N 178 
GLY N      N N N 179 
GLY CA     C N N 180 
GLY C      C N N 181 
GLY O      O N N 182 
GLY OXT    O N N 183 
GLY H      H N N 184 
GLY H2     H N N 185 
GLY HA2    H N N 186 
GLY HA3    H N N 187 
GLY HXT    H N N 188 
HIS N      N N N 189 
HIS CA     C N S 190 
HIS C      C N N 191 
HIS O      O N N 192 
HIS CB     C N N 193 
HIS CG     C Y N 194 
HIS ND1    N Y N 195 
HIS CD2    C Y N 196 
HIS CE1    C Y N 197 
HIS NE2    N Y N 198 
HIS OXT    O N N 199 
HIS H      H N N 200 
HIS H2     H N N 201 
HIS HA     H N N 202 
HIS HB2    H N N 203 
HIS HB3    H N N 204 
HIS HD1    H N N 205 
HIS HD2    H N N 206 
HIS HE1    H N N 207 
HIS HE2    H N N 208 
HIS HXT    H N N 209 
HOH O      O N N 210 
HOH H1     H N N 211 
HOH H2     H N N 212 
ILE N      N N N 213 
ILE CA     C N S 214 
ILE C      C N N 215 
ILE O      O N N 216 
ILE CB     C N S 217 
ILE CG1    C N N 218 
ILE CG2    C N N 219 
ILE CD1    C N N 220 
ILE OXT    O N N 221 
ILE H      H N N 222 
ILE H2     H N N 223 
ILE HA     H N N 224 
ILE HB     H N N 225 
ILE HG12   H N N 226 
ILE HG13   H N N 227 
ILE HG21   H N N 228 
ILE HG22   H N N 229 
ILE HG23   H N N 230 
ILE HD11   H N N 231 
ILE HD12   H N N 232 
ILE HD13   H N N 233 
ILE HXT    H N N 234 
LEU N      N N N 235 
LEU CA     C N S 236 
LEU C      C N N 237 
LEU O      O N N 238 
LEU CB     C N N 239 
LEU CG     C N N 240 
LEU CD1    C N N 241 
LEU CD2    C N N 242 
LEU OXT    O N N 243 
LEU H      H N N 244 
LEU H2     H N N 245 
LEU HA     H N N 246 
LEU HB2    H N N 247 
LEU HB3    H N N 248 
LEU HG     H N N 249 
LEU HD11   H N N 250 
LEU HD12   H N N 251 
LEU HD13   H N N 252 
LEU HD21   H N N 253 
LEU HD22   H N N 254 
LEU HD23   H N N 255 
LEU HXT    H N N 256 
LYS N      N N N 257 
LYS CA     C N S 258 
LYS C      C N N 259 
LYS O      O N N 260 
LYS CB     C N N 261 
LYS CG     C N N 262 
LYS CD     C N N 263 
LYS CE     C N N 264 
LYS NZ     N N N 265 
LYS OXT    O N N 266 
LYS H      H N N 267 
LYS H2     H N N 268 
LYS HA     H N N 269 
LYS HB2    H N N 270 
LYS HB3    H N N 271 
LYS HG2    H N N 272 
LYS HG3    H N N 273 
LYS HD2    H N N 274 
LYS HD3    H N N 275 
LYS HE2    H N N 276 
LYS HE3    H N N 277 
LYS HZ1    H N N 278 
LYS HZ2    H N N 279 
LYS HZ3    H N N 280 
LYS HXT    H N N 281 
MET N      N N N 282 
MET CA     C N S 283 
MET C      C N N 284 
MET O      O N N 285 
MET CB     C N N 286 
MET CG     C N N 287 
MET SD     S N N 288 
MET CE     C N N 289 
MET OXT    O N N 290 
MET H      H N N 291 
MET H2     H N N 292 
MET HA     H N N 293 
MET HB2    H N N 294 
MET HB3    H N N 295 
MET HG2    H N N 296 
MET HG3    H N N 297 
MET HE1    H N N 298 
MET HE2    H N N 299 
MET HE3    H N N 300 
MET HXT    H N N 301 
PHE N      N N N 302 
PHE CA     C N S 303 
PHE C      C N N 304 
PHE O      O N N 305 
PHE CB     C N N 306 
PHE CG     C Y N 307 
PHE CD1    C Y N 308 
PHE CD2    C Y N 309 
PHE CE1    C Y N 310 
PHE CE2    C Y N 311 
PHE CZ     C Y N 312 
PHE OXT    O N N 313 
PHE H      H N N 314 
PHE H2     H N N 315 
PHE HA     H N N 316 
PHE HB2    H N N 317 
PHE HB3    H N N 318 
PHE HD1    H N N 319 
PHE HD2    H N N 320 
PHE HE1    H N N 321 
PHE HE2    H N N 322 
PHE HZ     H N N 323 
PHE HXT    H N N 324 
PRO N      N N N 325 
PRO CA     C N S 326 
PRO C      C N N 327 
PRO O      O N N 328 
PRO CB     C N N 329 
PRO CG     C N N 330 
PRO CD     C N N 331 
PRO OXT    O N N 332 
PRO H      H N N 333 
PRO HA     H N N 334 
PRO HB2    H N N 335 
PRO HB3    H N N 336 
PRO HG2    H N N 337 
PRO HG3    H N N 338 
PRO HD2    H N N 339 
PRO HD3    H N N 340 
PRO HXT    H N N 341 
SER N      N N N 342 
SER CA     C N S 343 
SER C      C N N 344 
SER O      O N N 345 
SER CB     C N N 346 
SER OG     O N N 347 
SER OXT    O N N 348 
SER H      H N N 349 
SER H2     H N N 350 
SER HA     H N N 351 
SER HB2    H N N 352 
SER HB3    H N N 353 
SER HG     H N N 354 
SER HXT    H N N 355 
THR N      N N N 356 
THR CA     C N S 357 
THR C      C N N 358 
THR O      O N N 359 
THR CB     C N R 360 
THR OG1    O N N 361 
THR CG2    C N N 362 
THR OXT    O N N 363 
THR H      H N N 364 
THR H2     H N N 365 
THR HA     H N N 366 
THR HB     H N N 367 
THR HG1    H N N 368 
THR HG21   H N N 369 
THR HG22   H N N 370 
THR HG23   H N N 371 
THR HXT    H N N 372 
TRP N      N N N 373 
TRP CA     C N S 374 
TRP C      C N N 375 
TRP O      O N N 376 
TRP CB     C N N 377 
TRP CG     C Y N 378 
TRP CD1    C Y N 379 
TRP CD2    C Y N 380 
TRP NE1    N Y N 381 
TRP CE2    C Y N 382 
TRP CE3    C Y N 383 
TRP CZ2    C Y N 384 
TRP CZ3    C Y N 385 
TRP CH2    C Y N 386 
TRP OXT    O N N 387 
TRP H      H N N 388 
TRP H2     H N N 389 
TRP HA     H N N 390 
TRP HB2    H N N 391 
TRP HB3    H N N 392 
TRP HD1    H N N 393 
TRP HE1    H N N 394 
TRP HE3    H N N 395 
TRP HZ2    H N N 396 
TRP HZ3    H N N 397 
TRP HH2    H N N 398 
TRP HXT    H N N 399 
TYR N      N N N 400 
TYR CA     C N S 401 
TYR C      C N N 402 
TYR O      O N N 403 
TYR CB     C N N 404 
TYR CG     C Y N 405 
TYR CD1    C Y N 406 
TYR CD2    C Y N 407 
TYR CE1    C Y N 408 
TYR CE2    C Y N 409 
TYR CZ     C Y N 410 
TYR OH     O N N 411 
TYR OXT    O N N 412 
TYR H      H N N 413 
TYR H2     H N N 414 
TYR HA     H N N 415 
TYR HB2    H N N 416 
TYR HB3    H N N 417 
TYR HD1    H N N 418 
TYR HD2    H N N 419 
TYR HE1    H N N 420 
TYR HE2    H N N 421 
TYR HH     H N N 422 
TYR HXT    H N N 423 
VAL N      N N N 424 
VAL CA     C N S 425 
VAL C      C N N 426 
VAL O      O N N 427 
VAL CB     C N N 428 
VAL CG1    C N N 429 
VAL CG2    C N N 430 
VAL OXT    O N N 431 
VAL H      H N N 432 
VAL H2     H N N 433 
VAL HA     H N N 434 
VAL HB     H N N 435 
VAL HG11   H N N 436 
VAL HG12   H N N 437 
VAL HG13   H N N 438 
VAL HG21   H N N 439 
VAL HG22   H N N 440 
VAL HG23   H N N 441 
VAL HXT    H N N 442 
WI6 O7N    O N N 443 
WI6 C7N    C N N 444 
WI6 N7N    N N N 445 
WI6 C3N    C N S 446 
WI6 C2N    C N N 447 
WI6 C4N    C N N 448 
WI6 C5N    C N N 449 
WI6 C6N    C N N 450 
WI6 N1N    N N N 451 
WI6 "C1'A" C N R 452 
WI6 "O4'A" O N N 453 
WI6 "C2'A" C N R 454 
WI6 "O2'A" O N N 455 
WI6 "C3'A" C N S 456 
WI6 "O3'A" O N N 457 
WI6 "C4'A" C N R 458 
WI6 "C5'A" C N N 459 
WI6 "O5'A" O N N 460 
WI6 PN     P N N 461 
WI6 O1N    O N N 462 
WI6 O2N    O N N 463 
WI6 O3     O N N 464 
WI6 PA     P N N 465 
WI6 O2P    O N N 466 
WI6 O1     O N N 467 
WI6 "O5'"  O N N 468 
WI6 H7N1   H N N 469 
WI6 H7N2   H N N 470 
WI6 H3N    H N N 471 
WI6 H2N1   H N N 472 
WI6 H2N2   H N N 473 
WI6 H4N    H N N 474 
WI6 H5N    H N N 475 
WI6 H6N1   H N N 476 
WI6 H6N2   H N N 477 
WI6 "H1'A" H N N 478 
WI6 "H2'A" H N N 479 
WI6 HO2A   H N N 480 
WI6 "H3'A" H N N 481 
WI6 HO3A   H N N 482 
WI6 "H4'A" H N N 483 
WI6 "H5'1" H N N 484 
WI6 "H5'2" H N N 485 
WI6 HO2N   H N N 486 
WI6 HO2P   H N N 487 
WI6 "C5'"  C N N 488 
WI6 "C4'"  C N N 489 
WI6 "O4'"  O N N 490 
WI6 "C1'"  C N N 491 
WI6 "C2'"  C N N 492 
WI6 "C3'"  C N N 493 
WI6 N9A    N Y N 494 
WI6 C4A    C Y N 495 
WI6 C5A    C Y N 496 
WI6 N7A    N Y N 497 
WI6 C8A    C Y N 498 
WI6 C6A    C Y N 499 
WI6 N1A    N Y N 500 
WI6 C2A    C Y N 501 
WI6 N3A    N Y N 502 
WI6 "O2'"  O N N 503 
WI6 "O3'"  O N N 504 
WI6 "H5'A" H N N 505 
WI6 "H5'B" H N N 506 
WI6 "H4'"  H N N 507 
WI6 "H1'"  H N N 508 
WI6 "H2'"  H N N 509 
WI6 "H3'"  H N N 510 
WI6 H8A    H N N 511 
WI6 H2A    H N N 512 
WI6 "HO2'" H N N 513 
WI6 "HO3'" H N N 514 
WI6 N6A    N N N 515 
WI6 H6A1   H N N 516 
WI6 H6A2   H N N 517 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N      CA     sing N N 1   
ALA N      H      sing N N 2   
ALA N      H2     sing N N 3   
ALA CA     C      sing N N 4   
ALA CA     CB     sing N N 5   
ALA CA     HA     sing N N 6   
ALA C      O      doub N N 7   
ALA C      OXT    sing N N 8   
ALA CB     HB1    sing N N 9   
ALA CB     HB2    sing N N 10  
ALA CB     HB3    sing N N 11  
ALA OXT    HXT    sing N N 12  
ARG N      CA     sing N N 13  
ARG N      H      sing N N 14  
ARG N      H2     sing N N 15  
ARG CA     C      sing N N 16  
ARG CA     CB     sing N N 17  
ARG CA     HA     sing N N 18  
ARG C      O      doub N N 19  
ARG C      OXT    sing N N 20  
ARG CB     CG     sing N N 21  
ARG CB     HB2    sing N N 22  
ARG CB     HB3    sing N N 23  
ARG CG     CD     sing N N 24  
ARG CG     HG2    sing N N 25  
ARG CG     HG3    sing N N 26  
ARG CD     NE     sing N N 27  
ARG CD     HD2    sing N N 28  
ARG CD     HD3    sing N N 29  
ARG NE     CZ     sing N N 30  
ARG NE     HE     sing N N 31  
ARG CZ     NH1    sing N N 32  
ARG CZ     NH2    doub N N 33  
ARG NH1    HH11   sing N N 34  
ARG NH1    HH12   sing N N 35  
ARG NH2    HH21   sing N N 36  
ARG NH2    HH22   sing N N 37  
ARG OXT    HXT    sing N N 38  
ASN N      CA     sing N N 39  
ASN N      H      sing N N 40  
ASN N      H2     sing N N 41  
ASN CA     C      sing N N 42  
ASN CA     CB     sing N N 43  
ASN CA     HA     sing N N 44  
ASN C      O      doub N N 45  
ASN C      OXT    sing N N 46  
ASN CB     CG     sing N N 47  
ASN CB     HB2    sing N N 48  
ASN CB     HB3    sing N N 49  
ASN CG     OD1    doub N N 50  
ASN CG     ND2    sing N N 51  
ASN ND2    HD21   sing N N 52  
ASN ND2    HD22   sing N N 53  
ASN OXT    HXT    sing N N 54  
ASP N      CA     sing N N 55  
ASP N      H      sing N N 56  
ASP N      H2     sing N N 57  
ASP CA     C      sing N N 58  
ASP CA     CB     sing N N 59  
ASP CA     HA     sing N N 60  
ASP C      O      doub N N 61  
ASP C      OXT    sing N N 62  
ASP CB     CG     sing N N 63  
ASP CB     HB2    sing N N 64  
ASP CB     HB3    sing N N 65  
ASP CG     OD1    doub N N 66  
ASP CG     OD2    sing N N 67  
ASP OD2    HD2    sing N N 68  
ASP OXT    HXT    sing N N 69  
CYS N      CA     sing N N 70  
CYS N      H      sing N N 71  
CYS N      H2     sing N N 72  
CYS CA     C      sing N N 73  
CYS CA     CB     sing N N 74  
CYS CA     HA     sing N N 75  
CYS C      O      doub N N 76  
CYS C      OXT    sing N N 77  
CYS CB     SG     sing N N 78  
CYS CB     HB2    sing N N 79  
CYS CB     HB3    sing N N 80  
CYS SG     HG     sing N N 81  
CYS OXT    HXT    sing N N 82  
FMN N1     C2     sing N N 83  
FMN N1     C10    doub N N 84  
FMN C2     O2     doub N N 85  
FMN C2     N3     sing N N 86  
FMN N3     C4     sing N N 87  
FMN N3     HN3    sing N N 88  
FMN C4     O4     doub N N 89  
FMN C4     C4A    sing N N 90  
FMN C4A    N5     doub N N 91  
FMN C4A    C10    sing N N 92  
FMN N5     C5A    sing N N 93  
FMN C5A    C6     doub Y N 94  
FMN C5A    C9A    sing Y N 95  
FMN C6     C7     sing Y N 96  
FMN C6     H6     sing N N 97  
FMN C7     C7M    sing N N 98  
FMN C7     C8     doub Y N 99  
FMN C7M    HM71   sing N N 100 
FMN C7M    HM72   sing N N 101 
FMN C7M    HM73   sing N N 102 
FMN C8     C8M    sing N N 103 
FMN C8     C9     sing Y N 104 
FMN C8M    HM81   sing N N 105 
FMN C8M    HM82   sing N N 106 
FMN C8M    HM83   sing N N 107 
FMN C9     C9A    doub Y N 108 
FMN C9     H9     sing N N 109 
FMN C9A    N10    sing N N 110 
FMN N10    C10    sing N N 111 
FMN N10    "C1'"  sing N N 112 
FMN "C1'"  "C2'"  sing N N 113 
FMN "C1'"  "H1'1" sing N N 114 
FMN "C1'"  "H1'2" sing N N 115 
FMN "C2'"  "O2'"  sing N N 116 
FMN "C2'"  "C3'"  sing N N 117 
FMN "C2'"  "H2'"  sing N N 118 
FMN "O2'"  "HO2'" sing N N 119 
FMN "C3'"  "O3'"  sing N N 120 
FMN "C3'"  "C4'"  sing N N 121 
FMN "C3'"  "H3'"  sing N N 122 
FMN "O3'"  "HO3'" sing N N 123 
FMN "C4'"  "O4'"  sing N N 124 
FMN "C4'"  "C5'"  sing N N 125 
FMN "C4'"  "H4'"  sing N N 126 
FMN "O4'"  "HO4'" sing N N 127 
FMN "C5'"  "O5'"  sing N N 128 
FMN "C5'"  "H5'1" sing N N 129 
FMN "C5'"  "H5'2" sing N N 130 
FMN "O5'"  P      sing N N 131 
FMN P      O1P    doub N N 132 
FMN P      O2P    sing N N 133 
FMN P      O3P    sing N N 134 
FMN O2P    HOP2   sing N N 135 
FMN O3P    HOP3   sing N N 136 
GLN N      CA     sing N N 137 
GLN N      H      sing N N 138 
GLN N      H2     sing N N 139 
GLN CA     C      sing N N 140 
GLN CA     CB     sing N N 141 
GLN CA     HA     sing N N 142 
GLN C      O      doub N N 143 
GLN C      OXT    sing N N 144 
GLN CB     CG     sing N N 145 
GLN CB     HB2    sing N N 146 
GLN CB     HB3    sing N N 147 
GLN CG     CD     sing N N 148 
GLN CG     HG2    sing N N 149 
GLN CG     HG3    sing N N 150 
GLN CD     OE1    doub N N 151 
GLN CD     NE2    sing N N 152 
GLN NE2    HE21   sing N N 153 
GLN NE2    HE22   sing N N 154 
GLN OXT    HXT    sing N N 155 
GLU N      CA     sing N N 156 
GLU N      H      sing N N 157 
GLU N      H2     sing N N 158 
GLU CA     C      sing N N 159 
GLU CA     CB     sing N N 160 
GLU CA     HA     sing N N 161 
GLU C      O      doub N N 162 
GLU C      OXT    sing N N 163 
GLU CB     CG     sing N N 164 
GLU CB     HB2    sing N N 165 
GLU CB     HB3    sing N N 166 
GLU CG     CD     sing N N 167 
GLU CG     HG2    sing N N 168 
GLU CG     HG3    sing N N 169 
GLU CD     OE1    doub N N 170 
GLU CD     OE2    sing N N 171 
GLU OE2    HE2    sing N N 172 
GLU OXT    HXT    sing N N 173 
GLY N      CA     sing N N 174 
GLY N      H      sing N N 175 
GLY N      H2     sing N N 176 
GLY CA     C      sing N N 177 
GLY CA     HA2    sing N N 178 
GLY CA     HA3    sing N N 179 
GLY C      O      doub N N 180 
GLY C      OXT    sing N N 181 
GLY OXT    HXT    sing N N 182 
HIS N      CA     sing N N 183 
HIS N      H      sing N N 184 
HIS N      H2     sing N N 185 
HIS CA     C      sing N N 186 
HIS CA     CB     sing N N 187 
HIS CA     HA     sing N N 188 
HIS C      O      doub N N 189 
HIS C      OXT    sing N N 190 
HIS CB     CG     sing N N 191 
HIS CB     HB2    sing N N 192 
HIS CB     HB3    sing N N 193 
HIS CG     ND1    sing Y N 194 
HIS CG     CD2    doub Y N 195 
HIS ND1    CE1    doub Y N 196 
HIS ND1    HD1    sing N N 197 
HIS CD2    NE2    sing Y N 198 
HIS CD2    HD2    sing N N 199 
HIS CE1    NE2    sing Y N 200 
HIS CE1    HE1    sing N N 201 
HIS NE2    HE2    sing N N 202 
HIS OXT    HXT    sing N N 203 
HOH O      H1     sing N N 204 
HOH O      H2     sing N N 205 
ILE N      CA     sing N N 206 
ILE N      H      sing N N 207 
ILE N      H2     sing N N 208 
ILE CA     C      sing N N 209 
ILE CA     CB     sing N N 210 
ILE CA     HA     sing N N 211 
ILE C      O      doub N N 212 
ILE C      OXT    sing N N 213 
ILE CB     CG1    sing N N 214 
ILE CB     CG2    sing N N 215 
ILE CB     HB     sing N N 216 
ILE CG1    CD1    sing N N 217 
ILE CG1    HG12   sing N N 218 
ILE CG1    HG13   sing N N 219 
ILE CG2    HG21   sing N N 220 
ILE CG2    HG22   sing N N 221 
ILE CG2    HG23   sing N N 222 
ILE CD1    HD11   sing N N 223 
ILE CD1    HD12   sing N N 224 
ILE CD1    HD13   sing N N 225 
ILE OXT    HXT    sing N N 226 
LEU N      CA     sing N N 227 
LEU N      H      sing N N 228 
LEU N      H2     sing N N 229 
LEU CA     C      sing N N 230 
LEU CA     CB     sing N N 231 
LEU CA     HA     sing N N 232 
LEU C      O      doub N N 233 
LEU C      OXT    sing N N 234 
LEU CB     CG     sing N N 235 
LEU CB     HB2    sing N N 236 
LEU CB     HB3    sing N N 237 
LEU CG     CD1    sing N N 238 
LEU CG     CD2    sing N N 239 
LEU CG     HG     sing N N 240 
LEU CD1    HD11   sing N N 241 
LEU CD1    HD12   sing N N 242 
LEU CD1    HD13   sing N N 243 
LEU CD2    HD21   sing N N 244 
LEU CD2    HD22   sing N N 245 
LEU CD2    HD23   sing N N 246 
LEU OXT    HXT    sing N N 247 
LYS N      CA     sing N N 248 
LYS N      H      sing N N 249 
LYS N      H2     sing N N 250 
LYS CA     C      sing N N 251 
LYS CA     CB     sing N N 252 
LYS CA     HA     sing N N 253 
LYS C      O      doub N N 254 
LYS C      OXT    sing N N 255 
LYS CB     CG     sing N N 256 
LYS CB     HB2    sing N N 257 
LYS CB     HB3    sing N N 258 
LYS CG     CD     sing N N 259 
LYS CG     HG2    sing N N 260 
LYS CG     HG3    sing N N 261 
LYS CD     CE     sing N N 262 
LYS CD     HD2    sing N N 263 
LYS CD     HD3    sing N N 264 
LYS CE     NZ     sing N N 265 
LYS CE     HE2    sing N N 266 
LYS CE     HE3    sing N N 267 
LYS NZ     HZ1    sing N N 268 
LYS NZ     HZ2    sing N N 269 
LYS NZ     HZ3    sing N N 270 
LYS OXT    HXT    sing N N 271 
MET N      CA     sing N N 272 
MET N      H      sing N N 273 
MET N      H2     sing N N 274 
MET CA     C      sing N N 275 
MET CA     CB     sing N N 276 
MET CA     HA     sing N N 277 
MET C      O      doub N N 278 
MET C      OXT    sing N N 279 
MET CB     CG     sing N N 280 
MET CB     HB2    sing N N 281 
MET CB     HB3    sing N N 282 
MET CG     SD     sing N N 283 
MET CG     HG2    sing N N 284 
MET CG     HG3    sing N N 285 
MET SD     CE     sing N N 286 
MET CE     HE1    sing N N 287 
MET CE     HE2    sing N N 288 
MET CE     HE3    sing N N 289 
MET OXT    HXT    sing N N 290 
PHE N      CA     sing N N 291 
PHE N      H      sing N N 292 
PHE N      H2     sing N N 293 
PHE CA     C      sing N N 294 
PHE CA     CB     sing N N 295 
PHE CA     HA     sing N N 296 
PHE C      O      doub N N 297 
PHE C      OXT    sing N N 298 
PHE CB     CG     sing N N 299 
PHE CB     HB2    sing N N 300 
PHE CB     HB3    sing N N 301 
PHE CG     CD1    doub Y N 302 
PHE CG     CD2    sing Y N 303 
PHE CD1    CE1    sing Y N 304 
PHE CD1    HD1    sing N N 305 
PHE CD2    CE2    doub Y N 306 
PHE CD2    HD2    sing N N 307 
PHE CE1    CZ     doub Y N 308 
PHE CE1    HE1    sing N N 309 
PHE CE2    CZ     sing Y N 310 
PHE CE2    HE2    sing N N 311 
PHE CZ     HZ     sing N N 312 
PHE OXT    HXT    sing N N 313 
PRO N      CA     sing N N 314 
PRO N      CD     sing N N 315 
PRO N      H      sing N N 316 
PRO CA     C      sing N N 317 
PRO CA     CB     sing N N 318 
PRO CA     HA     sing N N 319 
PRO C      O      doub N N 320 
PRO C      OXT    sing N N 321 
PRO CB     CG     sing N N 322 
PRO CB     HB2    sing N N 323 
PRO CB     HB3    sing N N 324 
PRO CG     CD     sing N N 325 
PRO CG     HG2    sing N N 326 
PRO CG     HG3    sing N N 327 
PRO CD     HD2    sing N N 328 
PRO CD     HD3    sing N N 329 
PRO OXT    HXT    sing N N 330 
SER N      CA     sing N N 331 
SER N      H      sing N N 332 
SER N      H2     sing N N 333 
SER CA     C      sing N N 334 
SER CA     CB     sing N N 335 
SER CA     HA     sing N N 336 
SER C      O      doub N N 337 
SER C      OXT    sing N N 338 
SER CB     OG     sing N N 339 
SER CB     HB2    sing N N 340 
SER CB     HB3    sing N N 341 
SER OG     HG     sing N N 342 
SER OXT    HXT    sing N N 343 
THR N      CA     sing N N 344 
THR N      H      sing N N 345 
THR N      H2     sing N N 346 
THR CA     C      sing N N 347 
THR CA     CB     sing N N 348 
THR CA     HA     sing N N 349 
THR C      O      doub N N 350 
THR C      OXT    sing N N 351 
THR CB     OG1    sing N N 352 
THR CB     CG2    sing N N 353 
THR CB     HB     sing N N 354 
THR OG1    HG1    sing N N 355 
THR CG2    HG21   sing N N 356 
THR CG2    HG22   sing N N 357 
THR CG2    HG23   sing N N 358 
THR OXT    HXT    sing N N 359 
TRP N      CA     sing N N 360 
TRP N      H      sing N N 361 
TRP N      H2     sing N N 362 
TRP CA     C      sing N N 363 
TRP CA     CB     sing N N 364 
TRP CA     HA     sing N N 365 
TRP C      O      doub N N 366 
TRP C      OXT    sing N N 367 
TRP CB     CG     sing N N 368 
TRP CB     HB2    sing N N 369 
TRP CB     HB3    sing N N 370 
TRP CG     CD1    doub Y N 371 
TRP CG     CD2    sing Y N 372 
TRP CD1    NE1    sing Y N 373 
TRP CD1    HD1    sing N N 374 
TRP CD2    CE2    doub Y N 375 
TRP CD2    CE3    sing Y N 376 
TRP NE1    CE2    sing Y N 377 
TRP NE1    HE1    sing N N 378 
TRP CE2    CZ2    sing Y N 379 
TRP CE3    CZ3    doub Y N 380 
TRP CE3    HE3    sing N N 381 
TRP CZ2    CH2    doub Y N 382 
TRP CZ2    HZ2    sing N N 383 
TRP CZ3    CH2    sing Y N 384 
TRP CZ3    HZ3    sing N N 385 
TRP CH2    HH2    sing N N 386 
TRP OXT    HXT    sing N N 387 
TYR N      CA     sing N N 388 
TYR N      H      sing N N 389 
TYR N      H2     sing N N 390 
TYR CA     C      sing N N 391 
TYR CA     CB     sing N N 392 
TYR CA     HA     sing N N 393 
TYR C      O      doub N N 394 
TYR C      OXT    sing N N 395 
TYR CB     CG     sing N N 396 
TYR CB     HB2    sing N N 397 
TYR CB     HB3    sing N N 398 
TYR CG     CD1    doub Y N 399 
TYR CG     CD2    sing Y N 400 
TYR CD1    CE1    sing Y N 401 
TYR CD1    HD1    sing N N 402 
TYR CD2    CE2    doub Y N 403 
TYR CD2    HD2    sing N N 404 
TYR CE1    CZ     doub Y N 405 
TYR CE1    HE1    sing N N 406 
TYR CE2    CZ     sing Y N 407 
TYR CE2    HE2    sing N N 408 
TYR CZ     OH     sing N N 409 
TYR OH     HH     sing N N 410 
TYR OXT    HXT    sing N N 411 
VAL N      CA     sing N N 412 
VAL N      H      sing N N 413 
VAL N      H2     sing N N 414 
VAL CA     C      sing N N 415 
VAL CA     CB     sing N N 416 
VAL CA     HA     sing N N 417 
VAL C      O      doub N N 418 
VAL C      OXT    sing N N 419 
VAL CB     CG1    sing N N 420 
VAL CB     CG2    sing N N 421 
VAL CB     HB     sing N N 422 
VAL CG1    HG11   sing N N 423 
VAL CG1    HG12   sing N N 424 
VAL CG1    HG13   sing N N 425 
VAL CG2    HG21   sing N N 426 
VAL CG2    HG22   sing N N 427 
VAL CG2    HG23   sing N N 428 
VAL OXT    HXT    sing N N 429 
WI6 "O3'A" "C3'A" sing N N 430 
WI6 "O2'A" "C2'A" sing N N 431 
WI6 "C3'A" "C4'A" sing N N 432 
WI6 "C3'A" "C2'A" sing N N 433 
WI6 "C4'A" "C5'A" sing N N 434 
WI6 "C4'A" "O4'A" sing N N 435 
WI6 "C2'A" "C1'A" sing N N 436 
WI6 "C1'A" "O4'A" sing N N 437 
WI6 "C1'A" N1N    sing N N 438 
WI6 "C5'A" "O5'A" sing N N 439 
WI6 O7N    C7N    doub N N 440 
WI6 C2N    N1N    sing N N 441 
WI6 C2N    C3N    sing N N 442 
WI6 N1N    C6N    sing N N 443 
WI6 O1N    PN     doub N N 444 
WI6 "O5'A" PN     sing N N 445 
WI6 C7N    C3N    sing N N 446 
WI6 C7N    N7N    sing N N 447 
WI6 PN     O2N    sing N N 448 
WI6 PN     O3     sing N N 449 
WI6 C3N    C4N    sing N N 450 
WI6 C6N    C5N    sing N N 451 
WI6 O2P    PA     doub N N 452 
WI6 C4N    C5N    doub N N 453 
WI6 O3     PA     sing N N 454 
WI6 "O5'"  PA     sing N N 455 
WI6 PA     O1     sing N N 456 
WI6 N7N    H7N1   sing N N 457 
WI6 N7N    H7N2   sing N N 458 
WI6 C3N    H3N    sing N N 459 
WI6 C2N    H2N1   sing N N 460 
WI6 C2N    H2N2   sing N N 461 
WI6 C4N    H4N    sing N N 462 
WI6 C5N    H5N    sing N N 463 
WI6 C6N    H6N1   sing N N 464 
WI6 C6N    H6N2   sing N N 465 
WI6 "C1'A" "H1'A" sing N N 466 
WI6 "C2'A" "H2'A" sing N N 467 
WI6 "O2'A" HO2A   sing N N 468 
WI6 "C3'A" "H3'A" sing N N 469 
WI6 "O3'A" HO3A   sing N N 470 
WI6 "C4'A" "H4'A" sing N N 471 
WI6 "C5'A" "H5'1" sing N N 472 
WI6 "C5'A" "H5'2" sing N N 473 
WI6 O2N    HO2N   sing N N 474 
WI6 O1     HO2P   sing N N 475 
WI6 "O5'"  "C5'"  sing N N 476 
WI6 "C5'"  "C4'"  sing N N 477 
WI6 "C4'"  "O4'"  sing N N 478 
WI6 "O4'"  "C1'"  sing N N 479 
WI6 "C1'"  "C2'"  sing N N 480 
WI6 "C2'"  "C3'"  sing N N 481 
WI6 "C3'"  "C4'"  sing N N 482 
WI6 "C1'"  N9A    sing N N 483 
WI6 N9A    C4A    sing Y N 484 
WI6 C4A    C5A    doub Y N 485 
WI6 C5A    N7A    sing Y N 486 
WI6 N7A    C8A    doub Y N 487 
WI6 C8A    N9A    sing Y N 488 
WI6 C5A    C6A    sing Y N 489 
WI6 C6A    N1A    doub Y N 490 
WI6 N1A    C2A    sing Y N 491 
WI6 C2A    N3A    doub Y N 492 
WI6 N3A    C4A    sing Y N 493 
WI6 "C2'"  "O2'"  sing N N 494 
WI6 "C3'"  "O3'"  sing N N 495 
WI6 "C5'"  "H5'A" sing N N 496 
WI6 "C5'"  "H5'B" sing N N 497 
WI6 "C4'"  "H4'"  sing N N 498 
WI6 "C1'"  "H1'"  sing N N 499 
WI6 "C2'"  "H2'"  sing N N 500 
WI6 "C3'"  "H3'"  sing N N 501 
WI6 C8A    H8A    sing N N 502 
WI6 C2A    H2A    sing N N 503 
WI6 "O2'"  "HO2'" sing N N 504 
WI6 "O3'"  "HO3'" sing N N 505 
WI6 C6A    N6A    sing N N 506 
WI6 N6A    H6A1   sing N N 507 
WI6 N6A    H6A2   sing N N 508 
# 
_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                    8QO8 
_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]   0.020214 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002744 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.010716 
_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]   0.011288 
_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 16  ? 0.111  -20.489 10.228  1.00 40.82 ? 10  ASN A N      1 
ATOM   2    C CA     . ASN A 1 16  ? 1.451  -20.027 9.890   1.00 33.97 ? 10  ASN A CA     1 
ATOM   3    C C      . ASN A 1 16  ? 1.554  -18.538 10.189  1.00 33.00 ? 10  ASN A C      1 
ATOM   4    O O      . ASN A 1 16  ? 0.893  -17.726 9.539   1.00 32.06 ? 10  ASN A O      1 
ATOM   5    C CB     . ASN A 1 16  ? 1.737  -20.273 8.405   1.00 38.57 ? 10  ASN A CB     1 
ATOM   6    C CG     . ASN A 1 16  ? 3.195  -19.997 8.021   1.00 35.61 ? 10  ASN A CG     1 
ATOM   7    O OD1    . ASN A 1 16  ? 3.896  -19.213 8.670   1.00 32.67 ? 10  ASN A OD1    1 
ATOM   8    N ND2    . ASN A 1 16  ? 3.644  -20.627 6.935   1.00 36.14 ? 10  ASN A ND2    1 
ATOM   9    N N      . PRO A 1 17  ? 2.405  -18.175 11.152  1.00 30.47 ? 11  PRO A N      1 
ATOM   10   C CA     . PRO A 1 17  ? 2.525  -16.754 11.522  1.00 33.21 ? 11  PRO A CA     1 
ATOM   11   C C      . PRO A 1 17  ? 3.109  -15.870 10.424  1.00 24.42 ? 11  PRO A C      1 
ATOM   12   O O      . PRO A 1 17  ? 2.873  -14.655 10.447  1.00 28.08 ? 11  PRO A O      1 
ATOM   13   C CB     . PRO A 1 17  ? 3.412  -16.781 12.778  1.00 28.78 ? 11  PRO A CB     1 
ATOM   14   C CG     . PRO A 1 17  ? 4.164  -18.055 12.689  1.00 37.52 ? 11  PRO A CG     1 
ATOM   15   C CD     . PRO A 1 17  ? 3.325  -19.037 11.913  1.00 39.02 ? 11  PRO A CD     1 
ATOM   16   N N      . LEU A 1 18  ? 3.840  -16.428 9.454   1.00 27.73 ? 12  LEU A N      1 
ATOM   17   C CA     . LEU A 1 18  ? 4.312  -15.611 8.341   1.00 25.20 ? 12  LEU A CA     1 
ATOM   18   C C      . LEU A 1 18  ? 3.173  -15.090 7.477   1.00 25.65 ? 12  LEU A C      1 
ATOM   19   O O      . LEU A 1 18  ? 3.402  -14.208 6.636   1.00 26.07 ? 12  LEU A O      1 
ATOM   20   C CB     . LEU A 1 18  ? 5.283  -16.416 7.470   1.00 26.55 ? 12  LEU A CB     1 
ATOM   21   C CG     . LEU A 1 18  ? 6.669  -16.682 8.061   1.00 28.24 ? 12  LEU A CG     1 
ATOM   22   C CD1    . LEU A 1 18  ? 7.465  -17.561 7.111   1.00 25.43 ? 12  LEU A CD1    1 
ATOM   23   C CD2    . LEU A 1 18  ? 7.389  -15.368 8.297   1.00 27.21 ? 12  LEU A CD2    1 
ATOM   24   N N      . PHE A 1 19  ? 1.955  -15.611 7.652   1.00 25.51 ? 13  PHE A N      1 
ATOM   25   C CA     . PHE A 1 19  ? 0.822  -15.212 6.825   1.00 27.29 ? 13  PHE A CA     1 
ATOM   26   C C      . PHE A 1 19  ? -0.245 -14.473 7.618   1.00 27.69 ? 13  PHE A C      1 
ATOM   27   O O      . PHE A 1 19  ? -1.389 -14.351 7.165   1.00 29.97 ? 13  PHE A O      1 
ATOM   28   C CB     . PHE A 1 19  ? 0.278  -16.395 6.027   1.00 27.62 ? 13  PHE A CB     1 
ATOM   29   C CG     . PHE A 1 19  ? 1.242  -16.850 4.999   1.00 30.59 ? 13  PHE A CG     1 
ATOM   30   C CD1    . PHE A 1 19  ? 2.192  -17.807 5.304   1.00 31.26 ? 13  PHE A CD1    1 
ATOM   31   C CD2    . PHE A 1 19  ? 1.292  -16.220 3.773   1.00 28.30 ? 13  PHE A CD2    1 
ATOM   32   C CE1    . PHE A 1 19  ? 3.134  -18.183 4.371   1.00 32.63 ? 13  PHE A CE1    1 
ATOM   33   C CE2    . PHE A 1 19  ? 2.234  -16.590 2.836   1.00 30.68 ? 13  PHE A CE2    1 
ATOM   34   C CZ     . PHE A 1 19  ? 3.158  -17.569 3.142   1.00 28.44 ? 13  PHE A CZ     1 
ATOM   35   N N      . SER A 1 20  ? 0.111  -13.979 8.787   1.00 28.76 ? 14  SER A N      1 
ATOM   36   C CA     . SER A 1 20  ? -0.760 -13.006 9.415   1.00 32.08 ? 14  SER A CA     1 
ATOM   37   C C      . SER A 1 20  ? -0.413 -11.618 8.883   1.00 32.79 ? 14  SER A C      1 
ATOM   38   O O      . SER A 1 20  ? 0.759  -11.330 8.616   1.00 28.81 ? 14  SER A O      1 
ATOM   39   C CB     . SER A 1 20  ? -0.594 -13.037 10.931  1.00 32.79 ? 14  SER A CB     1 
ATOM   40   O OG     . SER A 1 20  ? 0.760  -13.136 11.296  1.00 35.89 ? 14  SER A OG     1 
ATOM   41   N N      . PRO A 1 21  ? -1.404 -10.756 8.684   1.00 27.71 ? 15  PRO A N      1 
ATOM   42   C CA     . PRO A 1 21  ? -1.120 -9.431  8.133   1.00 27.14 ? 15  PRO A CA     1 
ATOM   43   C C      . PRO A 1 21  ? -0.307 -8.594  9.104   1.00 26.46 ? 15  PRO A C      1 
ATOM   44   O O      . PRO A 1 21  ? -0.226 -8.873  10.302  1.00 27.15 ? 15  PRO A O      1 
ATOM   45   C CB     . PRO A 1 21  ? -2.512 -8.833  7.901   1.00 33.21 ? 15  PRO A CB     1 
ATOM   46   C CG     . PRO A 1 21  ? -3.373 -9.521  8.911   1.00 37.96 ? 15  PRO A CG     1 
ATOM   47   C CD     . PRO A 1 21  ? -2.832 -10.930 9.005   1.00 33.00 ? 15  PRO A CD     1 
ATOM   48   N N      . TYR A 1 22  ? 0.333  -7.567  8.556   1.00 27.03 ? 16  TYR A N      1 
ATOM   49   C CA     . TYR A 1 22  ? 1.163  -6.678  9.349   1.00 24.93 ? 16  TYR A CA     1 
ATOM   50   C C      . TYR A 1 22  ? 1.091  -5.270  8.790   1.00 26.43 ? 16  TYR A C      1 
ATOM   51   O O      . TYR A 1 22  ? 1.231  -5.065  7.580   1.00 29.05 ? 16  TYR A O      1 
ATOM   52   C CB     . TYR A 1 22  ? 2.635  -7.125  9.386   1.00 26.38 ? 16  TYR A CB     1 
ATOM   53   C CG     . TYR A 1 22  ? 3.444  -6.274  10.335  1.00 25.53 ? 16  TYR A CG     1 
ATOM   54   C CD1    . TYR A 1 22  ? 3.329  -6.441  11.720  1.00 23.51 ? 16  TYR A CD1    1 
ATOM   55   C CD2    . TYR A 1 22  ? 4.257  -5.249  9.863   1.00 25.88 ? 16  TYR A CD2    1 
ATOM   56   C CE1    . TYR A 1 22  ? 4.046  -5.648  12.604  1.00 28.23 ? 16  TYR A CE1    1 
ATOM   57   C CE2    . TYR A 1 22  ? 4.976  -4.446  10.746  1.00 21.93 ? 16  TYR A CE2    1 
ATOM   58   C CZ     . TYR A 1 22  ? 4.862  -4.652  12.105  1.00 26.14 ? 16  TYR A CZ     1 
ATOM   59   O OH     . TYR A 1 22  ? 5.568  -3.859  12.975  1.00 26.26 ? 16  TYR A OH     1 
ATOM   60   N N      . LYS A 1 23  ? 0.911  -4.299  9.678   1.00 23.20 ? 17  LYS A N      1 
ATOM   61   C CA     . LYS A 1 23  ? 0.854  -2.895  9.292   1.00 26.43 ? 17  LYS A CA     1 
ATOM   62   C C      . LYS A 1 23  ? 2.252  -2.305  9.410   1.00 27.86 ? 17  LYS A C      1 
ATOM   63   O O      . LYS A 1 23  ? 2.718  -1.985  10.509  1.00 28.59 ? 17  LYS A O      1 
ATOM   64   C CB     . LYS A 1 23  ? -0.148 -2.135  10.153  1.00 30.49 ? 17  LYS A CB     1 
ATOM   65   N N      . MET A 1 24  ? 2.927  -2.173  8.270   1.00 30.13 ? 18  MET A N      1 
ATOM   66   C CA     . MET A 1 24  ? 4.170  -1.411  8.183   1.00 29.28 ? 18  MET A CA     1 
ATOM   67   C C      . MET A 1 24  ? 3.838  0.069   8.005   1.00 30.20 ? 18  MET A C      1 
ATOM   68   O O      . MET A 1 24  ? 3.944  0.652   6.923   1.00 36.24 ? 18  MET A O      1 
ATOM   69   C CB     . MET A 1 24  ? 5.059  -1.967  7.084   1.00 28.79 ? 18  MET A CB     1 
ATOM   70   C CG     . MET A 1 24  ? 6.460  -1.440  7.118   1.00 29.59 ? 18  MET A CG     1 
ATOM   71   S SD     . MET A 1 24  ? 7.439  -2.196  5.817   1.00 30.60 ? 18  MET A SD     1 
ATOM   72   C CE     . MET A 1 24  ? 6.724  -1.507  4.304   1.00 24.91 ? 18  MET A CE     1 
ATOM   73   N N      . GLY A 1 25  ? 3.393  0.666   9.110   1.00 38.71 ? 19  GLY A N      1 
ATOM   74   C CA     . GLY A 1 25  ? 2.853  2.012   9.045   1.00 34.07 ? 19  GLY A CA     1 
ATOM   75   C C      . GLY A 1 25  ? 1.651  2.030   8.127   1.00 32.42 ? 19  GLY A C      1 
ATOM   76   O O      . GLY A 1 25  ? 0.728  1.218   8.258   1.00 34.26 ? 19  GLY A O      1 
ATOM   77   N N      . LYS A 1 26  ? 1.662  2.944   7.162   1.00 42.11 ? 20  LYS A N      1 
ATOM   78   C CA     . LYS A 1 26  ? 0.503  3.091   6.291   1.00 44.92 ? 20  LYS A CA     1 
ATOM   79   C C      . LYS A 1 26  ? 0.400  2.016   5.217   1.00 36.67 ? 20  LYS A C      1 
ATOM   80   O O      . LYS A 1 26  ? -0.526 2.075   4.401   1.00 35.65 ? 20  LYS A O      1 
ATOM   81   C CB     . LYS A 1 26  ? 0.418  4.509   5.711   1.00 38.04 ? 20  LYS A CB     1 
ATOM   82   C CG     . LYS A 1 26  ? 1.502  4.890   4.732   1.00 43.38 ? 20  LYS A CG     1 
ATOM   83   C CD     . LYS A 1 26  ? 1.557  6.409   4.612   1.00 54.50 ? 20  LYS A CD     1 
ATOM   84   C CE     . LYS A 1 26  ? 2.615  6.862   3.617   1.00 44.00 ? 20  LYS A CE     1 
ATOM   85   N NZ     . LYS A 1 26  ? 2.937  5.793   2.635   1.00 39.74 ? 20  LYS A NZ     1 
ATOM   86   N N      . PHE A 1 27  ? 1.290  1.024   5.206   1.00 31.76 ? 21  PHE A N      1 
ATOM   87   C CA     . PHE A 1 27  ? 1.220  -0.071  4.240   1.00 33.14 ? 21  PHE A CA     1 
ATOM   88   C C      . PHE A 1 27  ? 0.754  -1.318  4.978   1.00 33.65 ? 21  PHE A C      1 
ATOM   89   O O      . PHE A 1 27  ? 1.460  -1.825  5.858   1.00 34.62 ? 21  PHE A O      1 
ATOM   90   C CB     . PHE A 1 27  ? 2.571  -0.329  3.567   1.00 34.84 ? 21  PHE A CB     1 
ATOM   91   C CG     . PHE A 1 27  ? 3.255  0.911   3.070   1.00 34.83 ? 21  PHE A CG     1 
ATOM   92   C CD1    . PHE A 1 27  ? 2.861  1.509   1.887   1.00 32.38 ? 21  PHE A CD1    1 
ATOM   93   C CD2    . PHE A 1 27  ? 4.280  1.492   3.801   1.00 43.06 ? 21  PHE A CD2    1 
ATOM   94   C CE1    . PHE A 1 27  ? 3.481  2.659   1.432   1.00 34.06 ? 21  PHE A CE1    1 
ATOM   95   C CE2    . PHE A 1 27  ? 4.914  2.641   3.350   1.00 35.78 ? 21  PHE A CE2    1 
ATOM   96   C CZ     . PHE A 1 27  ? 4.512  3.224   2.160   1.00 32.66 ? 21  PHE A CZ     1 
ATOM   97   N N      . ASN A 1 28  ? -0.314 -1.859  4.731   1.00 31.37 ? 22  ASN A N      1 
ATOM   98   C CA     . ASN A 1 28  ? -0.830 -3.104  5.290   1.00 34.50 ? 22  ASN A CA     1 
ATOM   99   C C      . ASN A 1 28  ? -0.366 -4.242  4.394   1.00 33.18 ? 22  ASN A C      1 
ATOM   100  O O      . ASN A 1 28  ? -0.834 -4.376  3.258   1.00 35.83 ? 22  ASN A O      1 
ATOM   101  C CB     . ASN A 1 28  ? -2.354 -3.078  5.415   1.00 40.63 ? 22  ASN A CB     1 
ATOM   102  C CG     . ASN A 1 28  ? -2.890 -4.223  6.251   1.00 47.29 ? 22  ASN A CG     1 
ATOM   103  O OD1    . ASN A 1 28  ? -2.229 -4.696  7.174   1.00 49.52 ? 22  ASN A OD1    1 
ATOM   104  N ND2    . ASN A 1 28  ? -4.097 -4.677  5.930   1.00 61.84 ? 22  ASN A ND2    1 
ATOM   105  N N      . LEU A 1 29  ? 0.455  -4.983  4.953   1.00 28.73 ? 23  LEU A N      1 
ATOM   106  C CA     . LEU A 1 29  ? 1.010  -6.143  4.272   1.00 25.15 ? 23  LEU A CA     1 
ATOM   107  C C      . LEU A 1 29  ? 0.156  -7.363  4.578   1.00 24.47 ? 23  LEU A C      1 
ATOM   108  O O      . LEU A 1 29  ? -0.360 -7.512  5.692   1.00 25.68 ? 23  LEU A O      1 
ATOM   109  C CB     . LEU A 1 29  ? 2.454  -6.395  4.728   1.00 24.48 ? 23  LEU A CB     1 
ATOM   110  C CG     . LEU A 1 29  ? 3.424  -5.227  4.544   1.00 22.61 ? 23  LEU A CG     1 
ATOM   111  C CD1    . LEU A 1 29  ? 4.834  -5.597  5.040   1.00 25.66 ? 23  LEU A CD1    1 
ATOM   112  C CD2    . LEU A 1 29  ? 3.462  -4.755  3.083   1.00 22.85 ? 23  LEU A CD2    1 
ATOM   113  N N      . SER A 1 30  ? -0.041 -8.184  3.557   1.00 24.88 ? 24  SER A N      1 
ATOM   114  C CA     A SER A 1 30  ? -0.794 -9.436  3.726   0.47 26.33 ? 24  SER A CA     1 
ATOM   115  C CA     B SER A 1 30  ? -0.770 -9.473  3.734   0.53 26.32 ? 24  SER A CA     1 
ATOM   116  C C      . SER A 1 30  ? 0.009  -10.687 4.338   1.00 25.72 ? 24  SER A C      1 
ATOM   117  O O      . SER A 1 30  ? -0.458 -11.784 4.870   1.00 28.82 ? 24  SER A O      1 
ATOM   118  C CB     A SER A 1 30  ? -1.413 -9.832  2.375   0.47 26.48 ? 24  SER A CB     1 
ATOM   119  C CB     B SER A 1 30  ? -1.369 -9.874  2.406   0.53 26.47 ? 24  SER A CB     1 
ATOM   120  O OG     A SER A 1 30  ? -0.395 -10.191 1.458   0.47 32.58 ? 24  SER A OG     1 
ATOM   121  O OG     B SER A 1 30  ? -2.171 -8.831  1.879   0.53 28.63 ? 24  SER A OG     1 
ATOM   122  N N      . HIS A 1 31  ? 1.340  -10.491 4.304   1.00 23.87 ? 25  HIS A N      1 
ATOM   123  C CA     . HIS A 1 31  ? 2.183  -11.547 4.837   1.00 23.85 ? 25  HIS A CA     1 
ATOM   124  C C      . HIS A 1 31  ? 3.551  -10.950 5.122   1.00 20.43 ? 25  HIS A C      1 
ATOM   125  O O      . HIS A 1 31  ? 3.835  -9.805  4.765   1.00 24.62 ? 25  HIS A O      1 
ATOM   126  C CB     . HIS A 1 31  ? 2.256  -12.729 3.879   1.00 24.16 ? 25  HIS A CB     1 
ATOM   127  C CG     . HIS A 1 31  ? 2.929  -12.403 2.588   1.00 21.12 ? 25  HIS A CG     1 
ATOM   128  N ND1    . HIS A 1 31  ? 4.257  -12.041 2.500   1.00 20.04 ? 25  HIS A ND1    1 
ATOM   129  C CD2    . HIS A 1 31  ? 2.426  -12.301 1.335   1.00 23.23 ? 25  HIS A CD2    1 
ATOM   130  C CE1    . HIS A 1 31  ? 4.560  -11.802 1.236   1.00 22.67 ? 25  HIS A CE1    1 
ATOM   131  N NE2    . HIS A 1 31  ? 3.463  -11.935 0.512   1.00 23.73 ? 25  HIS A NE2    1 
ATOM   132  N N      . ARG A 1 32  ? 4.397  -11.746 5.768   1.00 19.32 ? 26  ARG A N      1 
ATOM   133  C CA     . ARG A 1 32  ? 5.619  -11.234 6.368   1.00 20.42 ? 26  ARG A CA     1 
ATOM   134  C C      . ARG A 1 32  ? 6.885  -11.671 5.641   1.00 20.28 ? 26  ARG A C      1 
ATOM   135  O O      . ARG A 1 32  ? 7.988  -11.452 6.157   1.00 21.07 ? 26  ARG A O      1 
ATOM   136  C CB     . ARG A 1 32  ? 5.676  -11.600 7.848   1.00 19.94 ? 26  ARG A CB     1 
ATOM   137  C CG     . ARG A 1 32  ? 4.455  -11.054 8.585   1.00 23.51 ? 26  ARG A CG     1 
ATOM   138  C CD     . ARG A 1 32  ? 4.281  -11.692 9.910   1.00 30.78 ? 26  ARG A CD     1 
ATOM   139  N NE     . ARG A 1 32  ? 3.124  -11.130 10.589  1.00 28.24 ? 26  ARG A NE     1 
ATOM   140  C CZ     . ARG A 1 32  ? 3.199  -10.329 11.640  1.00 26.35 ? 26  ARG A CZ     1 
ATOM   141  N NH1    . ARG A 1 32  ? 4.362  -9.883  12.082  1.00 25.20 ? 26  ARG A NH1    1 
ATOM   142  N NH2    . ARG A 1 32  ? 2.079  -9.980  12.274  1.00 25.07 ? 26  ARG A NH2    1 
ATOM   143  N N      . VAL A 1 33  ? 6.755  -12.257 4.452   1.00 21.68 ? 27  VAL A N      1 
ATOM   144  C CA     . VAL A 1 33  ? 7.903  -12.697 3.663   1.00 22.05 ? 27  VAL A CA     1 
ATOM   145  C C      . VAL A 1 33  ? 8.316  -11.536 2.768   1.00 22.13 ? 27  VAL A C      1 
ATOM   146  O O      . VAL A 1 33  ? 7.516  -11.054 1.961   1.00 24.48 ? 27  VAL A O      1 
ATOM   147  C CB     . VAL A 1 33  ? 7.559  -13.947 2.835   1.00 22.06 ? 27  VAL A CB     1 
ATOM   148  C CG1    . VAL A 1 33  ? 8.758  -14.383 1.993   1.00 21.53 ? 27  VAL A CG1    1 
ATOM   149  C CG2    . VAL A 1 33  ? 7.104  -15.093 3.751   1.00 23.43 ? 27  VAL A CG2    1 
ATOM   150  N N      . VAL A 1 34  ? 9.558  -11.087 2.911   1.00 18.66 ? 28  VAL A N      1 
ATOM   151  C CA     . VAL A 1 34  ? 10.062 -9.895  2.237   1.00 22.00 ? 28  VAL A CA     1 
ATOM   152  C C      . VAL A 1 34  ? 11.172 -10.277 1.258   1.00 22.05 ? 28  VAL A C      1 
ATOM   153  O O      . VAL A 1 34  ? 12.032 -11.111 1.569   1.00 20.29 ? 28  VAL A O      1 
ATOM   154  C CB     . VAL A 1 34  ? 10.573 -8.888  3.289   1.00 19.35 ? 28  VAL A CB     1 
ATOM   155  C CG1    . VAL A 1 34  ? 11.157 -7.645  2.645   1.00 19.79 ? 28  VAL A CG1    1 
ATOM   156  C CG2    . VAL A 1 34  ? 9.439  -8.508  4.238   1.00 21.41 ? 28  VAL A CG2    1 
ATOM   157  N N      . LEU A 1 35  ? 11.172 -9.648  0.088   1.00 20.17 ? 29  LEU A N      1 
ATOM   158  C CA     . LEU A 1 35  ? 12.289 -9.813  -0.847  1.00 18.23 ? 29  LEU A CA     1 
ATOM   159  C C      . LEU A 1 35  ? 13.438 -8.943  -0.368  1.00 17.68 ? 29  LEU A C      1 
ATOM   160  O O      . LEU A 1 35  ? 13.335 -7.711  -0.373  1.00 19.91 ? 29  LEU A O      1 
ATOM   161  C CB     . LEU A 1 35  ? 11.887 -9.414  -2.265  1.00 19.97 ? 29  LEU A CB     1 
ATOM   162  C CG     . LEU A 1 35  ? 13.042 -9.358  -3.287  1.00 18.79 ? 29  LEU A CG     1 
ATOM   163  C CD1    . LEU A 1 35  ? 13.655 -10.728 -3.513  1.00 21.63 ? 29  LEU A CD1    1 
ATOM   164  C CD2    . LEU A 1 35  ? 12.553 -8.792  -4.609  1.00 20.66 ? 29  LEU A CD2    1 
ATOM   165  N N      . ALA A 1 36  ? 14.545 -9.574  0.034   1.00 21.21 ? 30  ALA A N      1 
ATOM   166  C CA     . ALA A 1 36  ? 15.714 -8.824  0.450   1.00 19.92 ? 30  ALA A CA     1 
ATOM   167  C C      . ALA A 1 36  ? 16.361 -8.137  -0.755  1.00 18.11 ? 30  ALA A C      1 
ATOM   168  O O      . ALA A 1 36  ? 16.248 -8.617  -1.890  1.00 19.95 ? 30  ALA A O      1 
ATOM   169  C CB     . ALA A 1 36  ? 16.729 -9.760  1.115   1.00 20.12 ? 30  ALA A CB     1 
ATOM   170  N N      . PRO A 1 37  ? 17.016 -6.991  -0.535  1.00 18.92 ? 31  PRO A N      1 
ATOM   171  C CA     . PRO A 1 37  ? 17.704 -6.296  -1.641  1.00 20.71 ? 31  PRO A CA     1 
ATOM   172  C C      . PRO A 1 37  ? 18.848 -7.136  -2.186  1.00 19.31 ? 31  PRO A C      1 
ATOM   173  O O      . PRO A 1 37  ? 19.697 -7.605  -1.428  1.00 19.50 ? 31  PRO A O      1 
ATOM   174  C CB     . PRO A 1 37  ? 18.241 -5.021  -0.979  1.00 23.48 ? 31  PRO A CB     1 
ATOM   175  C CG     . PRO A 1 37  ? 18.305 -5.348  0.538   1.00 20.82 ? 31  PRO A CG     1 
ATOM   176  C CD     . PRO A 1 37  ? 17.232 -6.364  0.795   1.00 19.16 ? 31  PRO A CD     1 
ATOM   177  N N      . MET A 1 38  ? 18.886 -7.304  -3.503  1.00 19.31 ? 32  MET A N      1 
ATOM   178  C CA     . MET A 1 38  ? 19.930 -8.114  -4.129  1.00 18.62 ? 32  MET A CA     1 
ATOM   179  C C      . MET A 1 38  ? 20.430 -7.499  -5.432  1.00 19.95 ? 32  MET A C      1 
ATOM   180  O O      . MET A 1 38  ? 19.699 -7.428  -6.427  1.00 19.53 ? 32  MET A O      1 
ATOM   181  C CB     . MET A 1 38  ? 19.479 -9.556  -4.322  1.00 20.29 ? 32  MET A CB     1 
ATOM   182  C CG     . MET A 1 38  ? 19.501 -10.344 -3.022  1.00 25.82 ? 32  MET A CG     1 
ATOM   183  S SD     . MET A 1 38  ? 18.960 -12.005 -3.345  1.00 25.13 ? 32  MET A SD     1 
ATOM   184  C CE     . MET A 1 38  ? 17.301 -11.699 -3.953  1.00 24.02 ? 32  MET A CE     1 
ATOM   185  N N      . THR A 1 39  ? 21.694 -7.081  -5.424  1.00 18.93 ? 33  THR A N      1 
ATOM   186  C CA     . THR A 1 39  ? 22.410 -6.678  -6.630  1.00 17.69 ? 33  THR A CA     1 
ATOM   187  C C      . THR A 1 39  ? 22.479 -7.851  -7.601  1.00 21.25 ? 33  THR A C      1 
ATOM   188  O O      . THR A 1 39  ? 22.952 -8.937  -7.246  1.00 20.76 ? 33  THR A O      1 
ATOM   189  C CB     . THR A 1 39  ? 23.822 -6.257  -6.212  1.00 18.27 ? 33  THR A CB     1 
ATOM   190  O OG1    . THR A 1 39  ? 23.760 -5.067  -5.403  1.00 21.31 ? 33  THR A OG1    1 
ATOM   191  C CG2    . THR A 1 39  ? 24.724 -6.022  -7.405  1.00 17.38 ? 33  THR A CG2    1 
ATOM   192  N N      . ARG A 1 40  ? 21.993 -7.632  -8.827  1.00 18.08 ? 34  ARG A N      1 
ATOM   193  C CA     . ARG A 1 40  ? 22.025 -8.646  -9.871  1.00 19.55 ? 34  ARG A CA     1 
ATOM   194  C C      . ARG A 1 40  ? 22.694 -8.184  -11.158 1.00 21.81 ? 34  ARG A C      1 
ATOM   195  O O      . ARG A 1 40  ? 22.932 -9.022  -12.032 1.00 22.24 ? 34  ARG A O      1 
ATOM   196  C CB     . ARG A 1 40  ? 20.608 -9.153  -10.193 1.00 20.61 ? 34  ARG A CB     1 
ATOM   197  C CG     . ARG A 1 40  ? 19.820 -9.609  -8.946  1.00 19.82 ? 34  ARG A CG     1 
ATOM   198  C CD     . ARG A 1 40  ? 20.478 -10.807 -8.218  1.00 20.60 ? 34  ARG A CD     1 
ATOM   199  N NE     . ARG A 1 40  ? 20.824 -11.891 -9.139  1.00 19.70 ? 34  ARG A NE     1 
ATOM   200  C CZ     . ARG A 1 40  ? 19.940 -12.726 -9.673  1.00 22.36 ? 34  ARG A CZ     1 
ATOM   201  N NH1    . ARG A 1 40  ? 18.654 -12.657 -9.368  1.00 21.63 ? 34  ARG A NH1    1 
ATOM   202  N NH2    . ARG A 1 40  ? 20.352 -13.639 -10.556 1.00 22.25 ? 34  ARG A NH2    1 
ATOM   203  N N      . CYS A 1 41  ? 22.974 -6.888  -11.316 1.00 18.99 ? 35  CYS A N      1 
ATOM   204  C CA     . CYS A 1 41  ? 23.787 -6.384  -12.427 1.00 18.69 ? 35  CYS A CA     1 
ATOM   205  C C      . CYS A 1 41  ? 23.142 -6.569  -13.799 1.00 21.12 ? 35  CYS A C      1 
ATOM   206  O O      . CYS A 1 41  ? 23.851 -6.744  -14.787 1.00 20.97 ? 35  CYS A O      1 
ATOM   207  C CB     . CYS A 1 41  ? 25.223 -6.937  -12.411 1.00 19.30 ? 35  CYS A CB     1 
ATOM   208  S SG     . CYS A 1 41  ? 26.043 -6.886  -10.800 1.00 21.24 ? 35  CYS A SG     1 
ATOM   209  N N      . ARG A 1 42  ? 21.812 -6.522  -13.890 1.00 20.18 ? 36  ARG A N      1 
ATOM   210  C CA     . ARG A 1 42  ? 21.136 -6.537  -15.184 1.00 21.39 ? 36  ARG A CA     1 
ATOM   211  C C      . ARG A 1 42  ? 20.753 -5.144  -15.665 1.00 25.10 ? 36  ARG A C      1 
ATOM   212  O O      . ARG A 1 42  ? 20.208 -5.016  -16.768 1.00 24.00 ? 36  ARG A O      1 
ATOM   213  C CB     . ARG A 1 42  ? 19.888 -7.433  -15.151 1.00 21.09 ? 36  ARG A CB     1 
ATOM   214  C CG     . ARG A 1 42  ? 20.122 -8.896  -15.521 1.00 19.83 ? 36  ARG A CG     1 
ATOM   215  C CD     . ARG A 1 42  ? 20.972 -9.630  -14.509 1.00 23.65 ? 36  ARG A CD     1 
ATOM   216  N NE     . ARG A 1 42  ? 21.069 -11.053 -14.817 1.00 21.30 ? 36  ARG A NE     1 
ATOM   217  C CZ     . ARG A 1 42  ? 21.652 -11.945 -14.027 1.00 21.97 ? 36  ARG A CZ     1 
ATOM   218  N NH1    . ARG A 1 42  ? 22.197 -11.592 -12.873 1.00 19.37 ? 36  ARG A NH1    1 
ATOM   219  N NH2    . ARG A 1 42  ? 21.672 -13.226 -14.394 1.00 20.39 ? 36  ARG A NH2    1 
ATOM   220  N N      . ALA A 1 43  ? 21.022 -4.103  -14.875 1.00 19.66 ? 37  ALA A N      1 
ATOM   221  C CA     . ALA A 1 43  ? 20.620 -2.733  -15.208 1.00 21.02 ? 37  ALA A CA     1 
ATOM   222  C C      . ALA A 1 43  ? 21.723 -2.099  -16.052 1.00 21.56 ? 37  ALA A C      1 
ATOM   223  O O      . ALA A 1 43  ? 22.510 -1.272  -15.592 1.00 22.65 ? 37  ALA A O      1 
ATOM   224  C CB     . ALA A 1 43  ? 20.317 -1.938  -13.938 1.00 20.48 ? 37  ALA A CB     1 
ATOM   225  N N      . LEU A 1 44  ? 21.762 -2.494  -17.330 1.00 21.76 ? 38  LEU A N      1 
ATOM   226  C CA     . LEU A 1 44  ? 22.895 -2.166  -18.185 1.00 21.91 ? 38  LEU A CA     1 
ATOM   227  C C      . LEU A 1 44  ? 23.131 -0.658  -18.269 1.00 20.13 ? 38  LEU A C      1 
ATOM   228  O O      . LEU A 1 44  ? 22.197 0.124   -18.493 1.00 22.92 ? 38  LEU A O      1 
ATOM   229  C CB     . LEU A 1 44  ? 22.656 -2.738  -19.591 1.00 19.89 ? 38  LEU A CB     1 
ATOM   230  C CG     . LEU A 1 44  ? 22.310 -4.231  -19.655 1.00 22.01 ? 38  LEU A CG     1 
ATOM   231  C CD1    . LEU A 1 44  ? 22.209 -4.707  -21.107 1.00 20.26 ? 38  LEU A CD1    1 
ATOM   232  C CD2    . LEU A 1 44  ? 23.332 -5.062  -18.897 1.00 21.72 ? 38  LEU A CD2    1 
ATOM   233  N N      . ASN A 1 45  ? 24.392 -0.258  -18.072 1.00 21.55 ? 39  ASN A N      1 
ATOM   234  C CA     . ASN A 1 45  ? 24.806 1.148   -18.125 1.00 23.96 ? 39  ASN A CA     1 
ATOM   235  C C      . ASN A 1 45  ? 24.057 1.993   -17.106 1.00 24.95 ? 39  ASN A C      1 
ATOM   236  O O      . ASN A 1 45  ? 23.815 3.182   -17.326 1.00 25.96 ? 39  ASN A O      1 
ATOM   237  C CB     . ASN A 1 45  ? 24.701 1.741   -19.538 1.00 23.20 ? 39  ASN A CB     1 
ATOM   238  C CG     . ASN A 1 45  ? 25.910 1.424   -20.383 1.00 42.85 ? 39  ASN A CG     1 
ATOM   239  O OD1    . ASN A 1 45  ? 26.703 0.547   -20.036 1.00 40.64 ? 39  ASN A OD1    1 
ATOM   240  N ND2    . ASN A 1 45  ? 26.057 2.124   -21.505 1.00 42.62 ? 39  ASN A ND2    1 
ATOM   241  N N      . ASN A 1 46  ? 23.677 1.363   -15.992 1.00 20.96 ? 40  ASN A N      1 
ATOM   242  C CA     . ASN A 1 46  ? 22.975 1.976   -14.865 1.00 21.68 ? 40  ASN A CA     1 
ATOM   243  C C      . ASN A 1 46  ? 21.530 2.348   -15.174 1.00 22.42 ? 40  ASN A C      1 
ATOM   244  O O      . ASN A 1 46  ? 20.884 3.016   -14.357 1.00 23.49 ? 40  ASN A O      1 
ATOM   245  C CB     . ASN A 1 46  ? 23.745 3.141   -14.232 1.00 23.74 ? 40  ASN A CB     1 
ATOM   246  C CG     . ASN A 1 46  ? 25.221 2.817   -14.029 1.00 22.02 ? 40  ASN A CG     1 
ATOM   247  O OD1    . ASN A 1 46  ? 26.098 3.519   -14.534 1.00 31.49 ? 40  ASN A OD1    1 
ATOM   248  N ND2    . ASN A 1 46  ? 25.498 1.724   -13.310 1.00 21.79 ? 40  ASN A ND2    1 
ATOM   249  N N      . ILE A 1 47  ? 21.001 1.925   -16.322 1.00 21.37 ? 41  ILE A N      1 
ATOM   250  C CA     . ILE A 1 47  ? 19.602 2.179   -16.638 1.00 25.80 ? 41  ILE A CA     1 
ATOM   251  C C      . ILE A 1 47  ? 18.782 0.973   -16.206 1.00 22.63 ? 41  ILE A C      1 
ATOM   252  O O      . ILE A 1 47  ? 19.106 -0.163  -16.591 1.00 24.69 ? 41  ILE A O      1 
ATOM   253  C CB     . ILE A 1 47  ? 19.403 2.428   -18.140 1.00 26.54 ? 41  ILE A CB     1 
ATOM   254  C CG1    . ILE A 1 47  ? 20.357 3.514   -18.656 1.00 35.52 ? 41  ILE A CG1    1 
ATOM   255  C CG2    . ILE A 1 47  ? 17.919 2.732   -18.423 1.00 25.27 ? 41  ILE A CG2    1 
ATOM   256  C CD1    . ILE A 1 47  ? 20.375 4.787   -17.843 1.00 41.92 ? 41  ILE A CD1    1 
ATOM   257  N N      . PRO A 1 48  ? 17.729 1.159   -15.410 1.00 21.89 ? 42  PRO A N      1 
ATOM   258  C CA     . PRO A 1 48  ? 16.798 0.055   -15.161 1.00 21.75 ? 42  PRO A CA     1 
ATOM   259  C C      . PRO A 1 48  ? 16.207 -0.448  -16.473 1.00 25.66 ? 42  PRO A C      1 
ATOM   260  O O      . PRO A 1 48  ? 15.678 0.324   -17.277 1.00 36.40 ? 42  PRO A O      1 
ATOM   261  C CB     . PRO A 1 48  ? 15.730 0.686   -14.256 1.00 24.56 ? 42  PRO A CB     1 
ATOM   262  C CG     . PRO A 1 48  ? 16.355 1.946   -13.733 1.00 26.28 ? 42  PRO A CG     1 
ATOM   263  C CD     . PRO A 1 48  ? 17.268 2.421   -14.813 1.00 23.26 ? 42  PRO A CD     1 
ATOM   264  N N      . GLN A 1 49  ? 16.338 -1.749  -16.697 1.00 24.57 ? 43  GLN A N      1 
ATOM   265  C CA     . GLN A 1 49  ? 15.966 -2.405  -17.941 1.00 29.66 ? 43  GLN A CA     1 
ATOM   266  C C      . GLN A 1 49  ? 14.615 -3.093  -17.760 1.00 26.77 ? 43  GLN A C      1 
ATOM   267  O O      . GLN A 1 49  ? 14.176 -3.363  -16.639 1.00 25.66 ? 43  GLN A O      1 
ATOM   268  C CB     . GLN A 1 49  ? 17.022 -3.466  -18.278 1.00 25.41 ? 43  GLN A CB     1 
ATOM   269  C CG     . GLN A 1 49  ? 18.433 -2.973  -18.672 1.00 32.71 ? 43  GLN A CG     1 
ATOM   270  C CD     . GLN A 1 49  ? 18.470 -1.986  -19.831 1.00 29.34 ? 43  GLN A CD     1 
ATOM   271  O OE1    . GLN A 1 49  ? 17.853 -2.216  -20.868 1.00 36.22 ? 43  GLN A OE1    1 
ATOM   272  N NE2    . GLN A 1 49  ? 19.207 -0.894  -19.666 1.00 37.68 ? 43  GLN A NE2    1 
ATOM   273  N N      . ALA A 1 50  ? 13.953 -3.382  -18.889 1.00 26.16 ? 44  ALA A N      1 
ATOM   274  C CA     . ALA A 1 50  ? 12.689 -4.114  -18.840 1.00 26.59 ? 44  ALA A CA     1 
ATOM   275  C C      . ALA A 1 50  ? 12.833 -5.447  -18.111 1.00 27.69 ? 44  ALA A C      1 
ATOM   276  O O      . ALA A 1 50  ? 11.879 -5.907  -17.465 1.00 26.32 ? 44  ALA A O      1 
ATOM   277  C CB     . ALA A 1 50  ? 12.156 -4.336  -20.259 1.00 30.95 ? 44  ALA A CB     1 
ATOM   278  N N      . ALA A 1 51  ? 14.018 -6.066  -18.183 1.00 24.53 ? 45  ALA A N      1 
ATOM   279  C CA     . ALA A 1 51  ? 14.255 -7.326  -17.485 1.00 22.00 ? 45  ALA A CA     1 
ATOM   280  C C      . ALA A 1 51  ? 14.003 -7.183  -15.991 1.00 22.78 ? 45  ALA A C      1 
ATOM   281  O O      . ALA A 1 51  ? 13.518 -8.123  -15.350 1.00 23.30 ? 45  ALA A O      1 
ATOM   282  C CB     . ALA A 1 51  ? 15.694 -7.787  -17.705 1.00 22.54 ? 45  ALA A CB     1 
ATOM   283  N N      . LEU A 1 52  ? 14.368 -6.030  -15.417 1.00 22.18 ? 46  LEU A N      1 
ATOM   284  C CA     . LEU A 1 52  ? 14.118 -5.800  -13.996 1.00 23.03 ? 46  LEU A CA     1 
ATOM   285  C C      . LEU A 1 52  ? 12.632 -5.839  -13.710 1.00 24.20 ? 46  LEU A C      1 
ATOM   286  O O      . LEU A 1 52  ? 12.204 -6.398  -12.692 1.00 23.47 ? 46  LEU A O      1 
ATOM   287  C CB     . LEU A 1 52  ? 14.704 -4.460  -13.539 1.00 23.11 ? 46  LEU A CB     1 
ATOM   288  C CG     . LEU A 1 52  ? 16.175 -4.441  -13.097 1.00 20.99 ? 46  LEU A CG     1 
ATOM   289  C CD1    . LEU A 1 52  ? 17.145 -4.817  -14.238 1.00 21.47 ? 46  LEU A CD1    1 
ATOM   290  C CD2    . LEU A 1 52  ? 16.527 -3.080  -12.504 1.00 23.50 ? 46  LEU A CD2    1 
ATOM   291  N N      . GLY A 1 53  ? 11.826 -5.260  -14.604 1.00 24.99 ? 47  GLY A N      1 
ATOM   292  C CA     . GLY A 1 53  ? 10.385 -5.321  -14.414 1.00 26.63 ? 47  GLY A CA     1 
ATOM   293  C C      . GLY A 1 53  ? 9.875  -6.747  -14.380 1.00 23.60 ? 47  GLY A C      1 
ATOM   294  O O      . GLY A 1 53  ? 9.071  -7.110  -13.520 1.00 25.55 ? 47  GLY A O      1 
ATOM   295  N N      . GLU A 1 54  ? 10.340 -7.576  -15.322 1.00 23.86 ? 48  GLU A N      1 
ATOM   296  C CA     . GLU A 1 54  ? 9.942  -8.981  -15.334 1.00 23.37 ? 48  GLU A CA     1 
ATOM   297  C C      . GLU A 1 54  ? 10.374 -9.700  -14.059 1.00 26.14 ? 48  GLU A C      1 
ATOM   298  O O      . GLU A 1 54  ? 9.610  -10.487 -13.493 1.00 21.68 ? 48  GLU A O      1 
ATOM   299  C CB     . GLU A 1 54  ? 10.506 -9.681  -16.573 1.00 29.32 ? 48  GLU A CB     1 
ATOM   300  C CG     . GLU A 1 54  ? 10.260 -11.182 -16.578 1.00 33.22 ? 48  GLU A CG     1 
ATOM   301  C CD     . GLU A 1 54  ? 9.661  -11.685 -17.875 1.00 53.31 ? 48  GLU A CD     1 
ATOM   302  O OE1    . GLU A 1 54  ? 9.041  -10.877 -18.600 1.00 66.24 ? 48  GLU A OE1    1 
ATOM   303  O OE2    . GLU A 1 54  ? 9.812  -12.893 -18.165 1.00 52.83 ? 48  GLU A OE2    1 
ATOM   304  N N      . TYR A 1 55  ? 11.600 -9.438  -13.598 1.00 21.57 ? 49  TYR A N      1 
ATOM   305  C CA     . TYR A 1 55  ? 12.138 -10.103 -12.411 1.00 20.45 ? 49  TYR A CA     1 
ATOM   306  C C      . TYR A 1 55  ? 11.336 -9.757  -11.162 1.00 22.55 ? 49  TYR A C      1 
ATOM   307  O O      . TYR A 1 55  ? 10.922 -10.648 -10.413 1.00 20.37 ? 49  TYR A O      1 
ATOM   308  C CB     . TYR A 1 55  ? 13.580 -9.649  -12.267 1.00 20.64 ? 49  TYR A CB     1 
ATOM   309  C CG     . TYR A 1 55  ? 14.308 -10.018 -10.997 1.00 21.73 ? 49  TYR A CG     1 
ATOM   310  C CD1    . TYR A 1 55  ? 14.870 -11.279 -10.829 1.00 21.97 ? 49  TYR A CD1    1 
ATOM   311  C CD2    . TYR A 1 55  ? 14.476 -9.081  -9.986  1.00 22.52 ? 49  TYR A CD2    1 
ATOM   312  C CE1    . TYR A 1 55  ? 15.566 -11.599 -9.661  1.00 21.77 ? 49  TYR A CE1    1 
ATOM   313  C CE2    . TYR A 1 55  ? 15.169 -9.396  -8.826  1.00 23.99 ? 49  TYR A CE2    1 
ATOM   314  C CZ     . TYR A 1 55  ? 15.717 -10.652 -8.682  1.00 23.38 ? 49  TYR A CZ     1 
ATOM   315  O OH     . TYR A 1 55  ? 16.423 -10.956 -7.539  1.00 26.23 ? 49  TYR A OH     1 
ATOM   316  N N      . TYR A 1 56  ? 11.106 -8.465  -10.927 1.00 19.73 ? 50  TYR A N      1 
ATOM   317  C CA     . TYR A 1 56  ? 10.349 -8.058  -9.747  1.00 20.17 ? 50  TYR A CA     1 
ATOM   318  C C      . TYR A 1 56  ? 8.887  -8.469  -9.859  1.00 22.51 ? 50  TYR A C      1 
ATOM   319  O O      . TYR A 1 56  ? 8.271  -8.852  -8.858  1.00 22.25 ? 50  TYR A O      1 
ATOM   320  C CB     . TYR A 1 56  ? 10.480 -6.552  -9.518  1.00 21.00 ? 50  TYR A CB     1 
ATOM   321  C CG     . TYR A 1 56  ? 11.844 -6.163  -9.014  1.00 19.73 ? 50  TYR A CG     1 
ATOM   322  C CD1    . TYR A 1 56  ? 12.278 -6.557  -7.751  1.00 22.80 ? 50  TYR A CD1    1 
ATOM   323  C CD2    . TYR A 1 56  ? 12.706 -5.417  -9.806  1.00 22.86 ? 50  TYR A CD2    1 
ATOM   324  C CE1    . TYR A 1 56  ? 13.544 -6.215  -7.295  1.00 22.22 ? 50  TYR A CE1    1 
ATOM   325  C CE2    . TYR A 1 56  ? 13.970 -5.070  -9.359  1.00 21.24 ? 50  TYR A CE2    1 
ATOM   326  C CZ     . TYR A 1 56  ? 14.385 -5.471  -8.109  1.00 24.18 ? 50  TYR A CZ     1 
ATOM   327  O OH     . TYR A 1 56  ? 15.653 -5.117  -7.684  1.00 21.76 ? 50  TYR A OH     1 
ATOM   328  N N      . GLU A 1 57  ? 8.321  -8.412  -11.072 1.00 21.85 ? 51  GLU A N      1 
ATOM   329  C CA     . GLU A 1 57  ? 6.943  -8.854  -11.261 1.00 23.32 ? 51  GLU A CA     1 
ATOM   330  C C      . GLU A 1 57  ? 6.771  -10.319 -10.887 1.00 23.29 ? 51  GLU A C      1 
ATOM   331  O O      . GLU A 1 57  ? 5.785  -10.686 -10.240 1.00 25.27 ? 51  GLU A O      1 
ATOM   332  C CB     . GLU A 1 57  ? 6.513  -8.629  -12.711 1.00 23.04 ? 51  GLU A CB     1 
ATOM   333  C CG     . GLU A 1 57  ? 5.010  -8.750  -12.930 1.00 26.42 ? 51  GLU A CG     1 
ATOM   334  C CD     . GLU A 1 57  ? 4.634  -8.745  -14.394 1.00 36.98 ? 51  GLU A CD     1 
ATOM   335  O OE1    . GLU A 1 57  ? 5.490  -9.112  -15.230 1.00 42.37 ? 51  GLU A OE1    1 
ATOM   336  O OE2    . GLU A 1 57  ? 3.484  -8.382  -14.713 1.00 42.36 ? 51  GLU A OE2    1 
ATOM   337  N N      . GLN A 1 58  ? 7.721  -11.170 -11.276 1.00 22.02 ? 52  GLN A N      1 
ATOM   338  C CA     . GLN A 1 58  ? 7.607  -12.590 -10.962 1.00 22.62 ? 52  GLN A CA     1 
ATOM   339  C C      . GLN A 1 58  ? 7.550  -12.817 -9.465  1.00 21.62 ? 52  GLN A C      1 
ATOM   340  O O      . GLN A 1 58  ? 6.922  -13.775 -9.012  1.00 22.36 ? 52  GLN A O      1 
ATOM   341  C CB     . GLN A 1 58  ? 8.838  -13.337 -11.470 1.00 23.18 ? 52  GLN A CB     1 
ATOM   342  C CG     . GLN A 1 58  ? 8.900  -13.529 -12.980 1.00 21.18 ? 52  GLN A CG     1 
ATOM   343  C CD     . GLN A 1 58  ? 10.100 -14.355 -13.399 1.00 23.25 ? 52  GLN A CD     1 
ATOM   344  O OE1    . GLN A 1 58  ? 11.120 -14.402 -12.702 1.00 22.92 ? 52  GLN A OE1    1 
ATOM   345  N NE2    . GLN A 1 58  ? 9.987  -15.011 -14.550 1.00 26.17 ? 52  GLN A NE2    1 
ATOM   346  N N      . ARG A 1 59  ? 8.236  -11.976 -8.696  1.00 23.11 ? 53  ARG A N      1 
ATOM   347  C CA     . ARG A 1 59  ? 8.386  -12.159 -7.261  1.00 21.02 ? 53  ARG A CA     1 
ATOM   348  C C      . ARG A 1 59  ? 7.336  -11.403 -6.453  1.00 22.86 ? 53  ARG A C      1 
ATOM   349  O O      . ARG A 1 59  ? 7.127  -11.721 -5.273  1.00 24.07 ? 53  ARG A O      1 
ATOM   350  C CB     . ARG A 1 59  ? 9.812  -11.771 -6.856  1.00 21.39 ? 53  ARG A CB     1 
ATOM   351  C CG     . ARG A 1 59  ? 10.812 -12.859 -7.270  1.00 22.71 ? 53  ARG A CG     1 
ATOM   352  C CD     . ARG A 1 59  ? 12.234 -12.384 -7.578  1.00 22.23 ? 53  ARG A CD     1 
ATOM   353  N NE     . ARG A 1 59  ? 12.974 -13.536 -8.079  1.00 23.68 ? 53  ARG A NE     1 
ATOM   354  C CZ     . ARG A 1 59  ? 12.850 -14.001 -9.318  1.00 22.97 ? 53  ARG A CZ     1 
ATOM   355  N NH1    . ARG A 1 59  ? 12.144 -13.352 -10.232 1.00 23.31 ? 53  ARG A NH1    1 
ATOM   356  N NH2    . ARG A 1 59  ? 13.440 -15.148 -9.646  1.00 24.55 ? 53  ARG A NH2    1 
ATOM   357  N N      . ALA A 1 60  ? 6.644  -10.455 -7.079  1.00 22.86 ? 54  ALA A N      1 
ATOM   358  C CA     . ALA A 1 60  ? 5.639  -9.646  -6.403  1.00 22.25 ? 54  ALA A CA     1 
ATOM   359  C C      . ALA A 1 60  ? 4.396  -10.470 -6.072  1.00 23.93 ? 54  ALA A C      1 
ATOM   360  O O      . ALA A 1 60  ? 3.995  -11.358 -6.829  1.00 25.19 ? 54  ALA A O      1 
ATOM   361  C CB     . ALA A 1 60  ? 5.252  -8.472  -7.304  1.00 26.19 ? 54  ALA A CB     1 
ATOM   362  N N      . THR A 1 61  ? 3.797  -10.180 -4.912  1.00 23.67 ? 55  THR A N      1 
ATOM   363  C CA     . THR A 1 61  ? 2.532  -10.768 -4.494  1.00 25.72 ? 55  THR A CA     1 
ATOM   364  C C      . THR A 1 61  ? 1.639  -9.661  -3.947  1.00 28.07 ? 55  THR A C      1 
ATOM   365  O O      . THR A 1 61  ? 2.109  -8.599  -3.532  1.00 22.93 ? 55  THR A O      1 
ATOM   366  C CB     . THR A 1 61  ? 2.713  -11.826 -3.389  1.00 24.17 ? 55  THR A CB     1 
ATOM   367  O OG1    . THR A 1 61  ? 3.519  -11.297 -2.324  1.00 23.34 ? 55  THR A OG1    1 
ATOM   368  C CG2    . THR A 1 61  ? 3.367  -13.080 -3.941  1.00 26.07 ? 55  THR A CG2    1 
ATOM   369  N N      . ALA A 1 62  ? 0.332  -9.915  -3.939  1.00 26.00 ? 56  ALA A N      1 
ATOM   370  C CA     . ALA A 1 62  ? -0.595 -8.921  -3.414  1.00 24.22 ? 56  ALA A CA     1 
ATOM   371  C C      . ALA A 1 62  ? -0.388 -8.770  -1.913  1.00 25.66 ? 56  ALA A C      1 
ATOM   372  O O      . ALA A 1 62  ? -0.494 -9.745  -1.166  1.00 24.58 ? 56  ALA A O      1 
ATOM   373  C CB     . ALA A 1 62  ? -2.028 -9.348  -3.707  1.00 26.39 ? 56  ALA A CB     1 
ATOM   374  N N      . GLY A 1 63  ? -0.073 -7.552  -1.480  1.00 22.52 ? 57  GLY A N      1 
ATOM   375  C CA     . GLY A 1 63  ? 0.249  -7.283  -0.102  1.00 22.03 ? 57  GLY A CA     1 
ATOM   376  C C      . GLY A 1 63  ? 1.631  -7.715  0.332   1.00 26.09 ? 57  GLY A C      1 
ATOM   377  O O      . GLY A 1 63  ? 1.904  -7.727  1.537   1.00 25.36 ? 57  GLY A O      1 
ATOM   378  N N      . GLY A 1 64  ? 2.507  -8.085  -0.595  1.00 23.08 ? 58  GLY A N      1 
ATOM   379  C CA     . GLY A 1 64  ? 3.871  -8.453  -0.262  1.00 25.54 ? 58  GLY A CA     1 
ATOM   380  C C      . GLY A 1 64  ? 4.833  -7.290  -0.429  1.00 26.01 ? 58  GLY A C      1 
ATOM   381  O O      . GLY A 1 64  ? 4.658  -6.436  -1.293  1.00 25.59 ? 58  GLY A O      1 
ATOM   382  N N      . PHE A 1 65  ? 5.882  -7.281  0.387   1.00 22.91 ? 59  PHE A N      1 
ATOM   383  C CA     . PHE A 1 65  ? 6.855  -6.197  0.386   1.00 19.31 ? 59  PHE A CA     1 
ATOM   384  C C      . PHE A 1 65  ? 8.117  -6.628  -0.359  1.00 22.74 ? 59  PHE A C      1 
ATOM   385  O O      . PHE A 1 65  ? 8.658  -7.713  -0.105  1.00 23.70 ? 59  PHE A O      1 
ATOM   386  C CB     . PHE A 1 65  ? 7.193  -5.816  1.836   1.00 21.11 ? 59  PHE A CB     1 
ATOM   387  C CG     . PHE A 1 65  ? 8.192  -4.692  1.976   1.00 20.53 ? 59  PHE A CG     1 
ATOM   388  C CD1    . PHE A 1 65  ? 8.209  -3.619  1.094   1.00 21.53 ? 59  PHE A CD1    1 
ATOM   389  C CD2    . PHE A 1 65  ? 9.099  -4.695  3.034   1.00 22.36 ? 59  PHE A CD2    1 
ATOM   390  C CE1    . PHE A 1 65  ? 9.136  -2.584  1.249   1.00 20.47 ? 59  PHE A CE1    1 
ATOM   391  C CE2    . PHE A 1 65  ? 10.018 -3.665  3.199   1.00 21.95 ? 59  PHE A CE2    1 
ATOM   392  C CZ     . PHE A 1 65  ? 10.041 -2.611  2.312   1.00 22.06 ? 59  PHE A CZ     1 
ATOM   393  N N      . LEU A 1 66  ? 8.580  -5.772  -1.263  1.00 20.30 ? 60  LEU A N      1 
ATOM   394  C CA     . LEU A 1 66  ? 9.795  -5.985  -2.044  1.00 18.89 ? 60  LEU A CA     1 
ATOM   395  C C      . LEU A 1 66  ? 10.766 -4.843  -1.788  1.00 21.28 ? 60  LEU A C      1 
ATOM   396  O O      . LEU A 1 66  ? 10.369 -3.674  -1.748  1.00 21.07 ? 60  LEU A O      1 
ATOM   397  C CB     . LEU A 1 66  ? 9.482  -5.983  -3.548  1.00 20.37 ? 60  LEU A CB     1 
ATOM   398  C CG     . LEU A 1 66  ? 8.445  -6.950  -4.123  1.00 26.52 ? 60  LEU A CG     1 
ATOM   399  C CD1    . LEU A 1 66  ? 8.391  -6.785  -5.640  1.00 23.91 ? 60  LEU A CD1    1 
ATOM   400  C CD2    . LEU A 1 66  ? 8.728  -8.400  -3.757  1.00 24.30 ? 60  LEU A CD2    1 
ATOM   401  N N      . ILE A 1 67  ? 12.051 -5.175  -1.660  1.00 19.35 ? 61  ILE A N      1 
ATOM   402  C CA     . ILE A 1 67  ? 13.121 -4.189  -1.578  1.00 20.15 ? 61  ILE A CA     1 
ATOM   403  C C      . ILE A 1 67  ? 14.016 -4.396  -2.789  1.00 20.12 ? 61  ILE A C      1 
ATOM   404  O O      . ILE A 1 67  ? 14.450 -5.526  -3.048  1.00 20.93 ? 61  ILE A O      1 
ATOM   405  C CB     . ILE A 1 67  ? 13.931 -4.344  -0.278  1.00 19.79 ? 61  ILE A CB     1 
ATOM   406  C CG1    . ILE A 1 67  ? 13.015 -4.340  0.943   1.00 21.22 ? 61  ILE A CG1    1 
ATOM   407  C CG2    . ILE A 1 67  ? 14.950 -3.221  -0.188  1.00 21.32 ? 61  ILE A CG2    1 
ATOM   408  C CD1    . ILE A 1 67  ? 13.735 -4.788  2.229   1.00 20.14 ? 61  ILE A CD1    1 
ATOM   409  N N      . THR A 1 68  ? 14.259 -3.325  -3.547  1.00 18.47 ? 62  THR A N      1 
ATOM   410  C CA     . THR A 1 68  ? 15.070 -3.475  -4.754  1.00 18.64 ? 62  THR A CA     1 
ATOM   411  C C      . THR A 1 68  ? 16.537 -3.674  -4.401  1.00 21.20 ? 62  THR A C      1 
ATOM   412  O O      . THR A 1 68  ? 16.999 -3.398  -3.288  1.00 21.26 ? 62  THR A O      1 
ATOM   413  C CB     . THR A 1 68  ? 15.035 -2.235  -5.646  1.00 17.68 ? 62  THR A CB     1 
ATOM   414  O OG1    . THR A 1 68  ? 15.775 -1.164  -5.049  1.00 20.06 ? 62  THR A OG1    1 
ATOM   415  C CG2    . THR A 1 68  ? 13.625 -1.798  -5.974  1.00 21.56 ? 62  THR A CG2    1 
ATOM   416  N N      . GLU A 1 69  ? 17.272 -4.115  -5.415  1.00 21.23 ? 63  GLU A N      1 
ATOM   417  C CA     . GLU A 1 69  ? 18.722 -4.107  -5.393  1.00 21.48 ? 63  GLU A CA     1 
ATOM   418  C C      . GLU A 1 69  ? 19.233 -2.721  -5.027  1.00 19.31 ? 63  GLU A C      1 
ATOM   419  O O      . GLU A 1 69  ? 18.574 -1.704  -5.270  1.00 20.60 ? 63  GLU A O      1 
ATOM   420  C CB     . GLU A 1 69  ? 19.206 -4.424  -6.807  1.00 21.58 ? 63  GLU A CB     1 
ATOM   421  C CG     . GLU A 1 69  ? 18.645 -3.483  -7.861  1.00 22.05 ? 63  GLU A CG     1 
ATOM   422  C CD     . GLU A 1 69  ? 18.460 -4.169  -9.201  1.00 26.07 ? 63  GLU A CD     1 
ATOM   423  O OE1    . GLU A 1 69  ? 19.399 -4.137  -10.026 1.00 24.66 ? 63  GLU A OE1    1 
ATOM   424  O OE2    . GLU A 1 69  ? 17.364 -4.723  -9.441  1.00 25.72 ? 63  GLU A OE2    1 
ATOM   425  N N      . GLY A 1 70  ? 20.431 -2.678  -4.454  1.00 18.23 ? 64  GLY A N      1 
ATOM   426  C CA     . GLY A 1 70  ? 21.085 -1.406  -4.221  1.00 20.11 ? 64  GLY A CA     1 
ATOM   427  C C      . GLY A 1 70  ? 21.102 -0.534  -5.460  1.00 20.18 ? 64  GLY A C      1 
ATOM   428  O O      . GLY A 1 70  ? 21.388 -1.013  -6.565  1.00 20.30 ? 64  GLY A O      1 
ATOM   429  N N      . THR A 1 71  ? 20.789 0.749   -5.290  1.00 18.43 ? 65  THR A N      1 
ATOM   430  C CA     . THR A 1 71  ? 20.632 1.676   -6.406  1.00 19.62 ? 65  THR A CA     1 
ATOM   431  C C      . THR A 1 71  ? 21.512 2.896   -6.155  1.00 21.27 ? 65  THR A C      1 
ATOM   432  O O      . THR A 1 71  ? 21.546 3.419   -5.029  1.00 22.24 ? 65  THR A O      1 
ATOM   433  C CB     . THR A 1 71  ? 19.142 2.039   -6.511  1.00 20.67 ? 65  THR A CB     1 
ATOM   434  O OG1    . THR A 1 71  ? 18.400 0.846   -6.820  1.00 22.11 ? 65  THR A OG1    1 
ATOM   435  C CG2    . THR A 1 71  ? 18.878 3.080   -7.600  1.00 20.98 ? 65  THR A CG2    1 
ATOM   436  N N      . MET A 1 72  ? 22.257 3.320   -7.184  1.00 21.38 ? 66  MET A N      1 
ATOM   437  C CA     . MET A 1 72  ? 23.200 4.423   -7.017  1.00 19.42 ? 66  MET A CA     1 
ATOM   438  C C      . MET A 1 72  ? 22.522 5.758   -6.767  1.00 21.33 ? 66  MET A C      1 
ATOM   439  O O      . MET A 1 72  ? 21.480 6.075   -7.355  1.00 22.38 ? 66  MET A O      1 
ATOM   440  C CB     . MET A 1 72  ? 24.184 4.581   -8.199  1.00 26.78 ? 66  MET A CB     1 
ATOM   441  C CG     . MET A 1 72  ? 24.679 3.341   -8.891  1.00 19.93 ? 66  MET A CG     1 
ATOM   442  S SD     . MET A 1 72  ? 25.373 3.635   -10.542 1.00 22.67 ? 66  MET A SD     1 
ATOM   443  C CE     . MET A 1 72  ? 26.370 5.089   -10.318 1.00 22.39 ? 66  MET A CE     1 
ATOM   444  N N      . ILE A 1 73  ? 23.157 6.559   -5.908  1.00 20.73 ? 67  ILE A N      1 
ATOM   445  C CA     . ILE A 1 73  ? 22.686 7.894   -5.564  1.00 21.24 ? 67  ILE A CA     1 
ATOM   446  C C      . ILE A 1 73  ? 23.454 8.996   -6.269  1.00 24.92 ? 67  ILE A C      1 
ATOM   447  O O      . ILE A 1 73  ? 23.121 10.175  -6.088  1.00 23.45 ? 67  ILE A O      1 
ATOM   448  C CB     . ILE A 1 73  ? 22.735 8.135   -4.040  1.00 21.08 ? 67  ILE A CB     1 
ATOM   449  C CG1    . ILE A 1 73  ? 24.194 8.174   -3.551  1.00 20.77 ? 67  ILE A CG1    1 
ATOM   450  C CG2    . ILE A 1 73  ? 21.880 7.114   -3.310  1.00 21.89 ? 67  ILE A CG2    1 
ATOM   451  C CD1    . ILE A 1 73  ? 24.342 8.475   -2.052  1.00 22.26 ? 67  ILE A CD1    1 
ATOM   452  N N      . SER A 1 74  ? 24.485 8.662   -7.039  1.00 21.79 ? 68  SER A N      1 
ATOM   453  C CA     . SER A 1 74  ? 25.367 9.655   -7.639  1.00 24.20 ? 68  SER A CA     1 
ATOM   454  C C      . SER A 1 74  ? 26.328 8.936   -8.576  1.00 25.65 ? 68  SER A C      1 
ATOM   455  O O      . SER A 1 74  ? 26.486 7.716   -8.482  1.00 24.35 ? 68  SER A O      1 
ATOM   456  C CB     . SER A 1 74  ? 26.161 10.414  -6.564  1.00 26.67 ? 68  SER A CB     1 
ATOM   457  O OG     . SER A 1 74  ? 27.256 9.635   -6.104  1.00 25.44 ? 68  SER A OG     1 
ATOM   458  N N      . PRO A 1 75  ? 26.975 9.673   -9.486  1.00 26.43 ? 69  PRO A N      1 
ATOM   459  C CA     . PRO A 1 75  ? 27.931 9.036   -10.409 1.00 27.82 ? 69  PRO A CA     1 
ATOM   460  C C      . PRO A 1 75  ? 29.107 8.351   -9.735  1.00 27.91 ? 69  PRO A C      1 
ATOM   461  O O      . PRO A 1 75  ? 29.762 7.520   -10.381 1.00 26.62 ? 69  PRO A O      1 
ATOM   462  C CB     . PRO A 1 75  ? 28.411 10.207  -11.277 1.00 25.33 ? 69  PRO A CB     1 
ATOM   463  C CG     . PRO A 1 75  ? 27.275 11.165  -11.267 1.00 26.54 ? 69  PRO A CG     1 
ATOM   464  C CD     . PRO A 1 75  ? 26.726 11.080  -9.849  1.00 26.17 ? 69  PRO A CD     1 
ATOM   465  N N      . THR A 1 76  ? 29.411 8.686   -8.482  1.00 24.39 ? 70  THR A N      1 
ATOM   466  C CA     . THR A 1 76  ? 30.571 8.163   -7.776  1.00 27.53 ? 70  THR A CA     1 
ATOM   467  C C      . THR A 1 76  ? 30.222 7.039   -6.804  1.00 24.61 ? 70  THR A C      1 
ATOM   468  O O      . THR A 1 76  ? 31.110 6.549   -6.101  1.00 24.24 ? 70  THR A O      1 
ATOM   469  C CB     . THR A 1 76  ? 31.287 9.298   -7.035  1.00 28.65 ? 70  THR A CB     1 
ATOM   470  O OG1    . THR A 1 76  ? 30.330 10.061  -6.282  1.00 31.37 ? 70  THR A OG1    1 
ATOM   471  C CG2    . THR A 1 76  ? 31.997 10.211  -8.029  1.00 34.90 ? 70  THR A CG2    1 
ATOM   472  N N      . SER A 1 77  ? 28.965 6.595   -6.774  1.00 21.38 ? 71  SER A N      1 
ATOM   473  C CA     . SER A 1 77  ? 28.472 5.709   -5.727  1.00 22.66 ? 71  SER A CA     1 
ATOM   474  C C      . SER A 1 77  ? 28.546 4.219   -6.065  1.00 24.90 ? 71  SER A C      1 
ATOM   475  O O      . SER A 1 77  ? 28.170 3.400   -5.224  1.00 22.15 ? 71  SER A O      1 
ATOM   476  C CB     . SER A 1 77  ? 27.039 6.102   -5.334  1.00 23.21 ? 71  SER A CB     1 
ATOM   477  O OG     . SER A 1 77  ? 26.174 5.868   -6.418  1.00 28.72 ? 71  SER A OG     1 
ATOM   478  N N      . ALA A 1 78  ? 29.040 3.834   -7.242  1.00 20.96 ? 72  ALA A N      1 
ATOM   479  C CA     . ALA A 1 78  ? 28.962 2.444   -7.683  1.00 20.49 ? 72  ALA A CA     1 
ATOM   480  C C      . ALA A 1 78  ? 30.286 1.704   -7.528  1.00 20.39 ? 72  ALA A C      1 
ATOM   481  O O      . ALA A 1 78  ? 31.367 2.274   -7.685  1.00 21.05 ? 72  ALA A O      1 
ATOM   482  C CB     . ALA A 1 78  ? 28.537 2.353   -9.154  1.00 20.99 ? 72  ALA A CB     1 
ATOM   483  N N      . GLY A 1 79  ? 30.178 0.403   -7.270  1.00 21.54 ? 73  GLY A N      1 
ATOM   484  C CA     . GLY A 1 79  ? 31.329 -0.480  -7.231  1.00 20.78 ? 73  GLY A CA     1 
ATOM   485  C C      . GLY A 1 79  ? 30.980 -1.857  -7.757  1.00 20.98 ? 73  GLY A C      1 
ATOM   486  O O      . GLY A 1 79  ? 31.657 -2.835  -7.432  1.00 22.41 ? 73  GLY A O      1 
ATOM   487  N N      . PHE A 1 80  ? 29.914 -1.945  -8.550  1.00 19.16 ? 74  PHE A N      1 
ATOM   488  C CA     . PHE A 1 80  ? 29.519 -3.147  -9.266  1.00 19.84 ? 74  PHE A CA     1 
ATOM   489  C C      . PHE A 1 80  ? 29.133 -2.717  -10.675 1.00 19.46 ? 74  PHE A C      1 
ATOM   490  O O      . PHE A 1 80  ? 28.743 -1.566  -10.889 1.00 21.22 ? 74  PHE A O      1 
ATOM   491  C CB     . PHE A 1 80  ? 28.296 -3.813  -8.621  1.00 21.77 ? 74  PHE A CB     1 
ATOM   492  C CG     . PHE A 1 80  ? 28.626 -4.832  -7.554  1.00 21.24 ? 74  PHE A CG     1 
ATOM   493  C CD1    . PHE A 1 80  ? 29.032 -4.428  -6.295  1.00 20.61 ? 74  PHE A CD1    1 
ATOM   494  C CD2    . PHE A 1 80  ? 28.515 -6.193  -7.820  1.00 20.71 ? 74  PHE A CD2    1 
ATOM   495  C CE1    . PHE A 1 80  ? 29.319 -5.374  -5.294  1.00 23.01 ? 74  PHE A CE1    1 
ATOM   496  C CE2    . PHE A 1 80  ? 28.825 -7.142  -6.846  1.00 21.59 ? 74  PHE A CE2    1 
ATOM   497  C CZ     . PHE A 1 80  ? 29.218 -6.730  -5.574  1.00 20.92 ? 74  PHE A CZ     1 
ATOM   498  N N      . PRO A 1 81  ? 29.208 -3.621  -11.645 1.00 21.13 ? 75  PRO A N      1 
ATOM   499  C CA     . PRO A 1 81  ? 28.816 -3.248  -13.012 1.00 20.27 ? 75  PRO A CA     1 
ATOM   500  C C      . PRO A 1 81  ? 27.304 -3.325  -13.179 1.00 21.37 ? 75  PRO A C      1 
ATOM   501  O O      . PRO A 1 81  ? 26.642 -4.202  -12.618 1.00 21.74 ? 75  PRO A O      1 
ATOM   502  C CB     . PRO A 1 81  ? 29.519 -4.307  -13.868 1.00 23.48 ? 75  PRO A CB     1 
ATOM   503  C CG     . PRO A 1 81  ? 29.520 -5.533  -12.999 1.00 22.73 ? 75  PRO A CG     1 
ATOM   504  C CD     . PRO A 1 81  ? 29.615 -5.036  -11.545 1.00 21.77 ? 75  PRO A CD     1 
ATOM   505  N N      . HIS A 1 82  ? 26.754 -2.374  -13.942 1.00 19.55 ? 76  HIS A N      1 
ATOM   506  C CA     . HIS A 1 82  ? 25.362 -2.459  -14.408 1.00 21.50 ? 76  HIS A CA     1 
ATOM   507  C C      . HIS A 1 82  ? 24.364 -2.527  -13.253 1.00 21.79 ? 76  HIS A C      1 
ATOM   508  O O      . HIS A 1 82  ? 23.388 -3.285  -13.285 1.00 22.13 ? 76  HIS A O      1 
ATOM   509  C CB     . HIS A 1 82  ? 25.191 -3.606  -15.397 1.00 22.62 ? 76  HIS A CB     1 
ATOM   510  C CG     . HIS A 1 82  ? 26.185 -3.543  -16.509 1.00 23.46 ? 76  HIS A CG     1 
ATOM   511  N ND1    . HIS A 1 82  ? 26.228 -2.478  -17.378 1.00 21.81 ? 76  HIS A ND1    1 
ATOM   512  C CD2    . HIS A 1 82  ? 27.245 -4.328  -16.817 1.00 24.67 ? 76  HIS A CD2    1 
ATOM   513  C CE1    . HIS A 1 82  ? 27.228 -2.648  -18.228 1.00 23.51 ? 76  HIS A CE1    1 
ATOM   514  N NE2    . HIS A 1 82  ? 27.867 -3.757  -17.899 1.00 23.23 ? 76  HIS A NE2    1 
ATOM   515  N N      . VAL A 1 83  ? 24.624 -1.734  -12.222 1.00 20.65 ? 77  VAL A N      1 
ATOM   516  C CA     . VAL A 1 83  ? 23.673 -1.555  -11.127 1.00 20.02 ? 77  VAL A CA     1 
ATOM   517  C C      . VAL A 1 83  ? 22.835 -0.329  -11.467 1.00 20.11 ? 77  VAL A C      1 
ATOM   518  O O      . VAL A 1 83  ? 23.357 0.632   -12.060 1.00 21.83 ? 77  VAL A O      1 
ATOM   519  C CB     . VAL A 1 83  ? 24.400 -1.433  -9.781  1.00 22.40 ? 77  VAL A CB     1 
ATOM   520  C CG1    . VAL A 1 83  ? 25.122 -2.721  -9.491  1.00 24.45 ? 77  VAL A CG1    1 
ATOM   521  C CG2    . VAL A 1 83  ? 25.382 -0.274  -9.807  1.00 22.31 ? 77  VAL A CG2    1 
ATOM   522  N N      . PRO A 1 84  ? 21.546 -0.327  -11.160 1.00 18.73 ? 78  PRO A N      1 
ATOM   523  C CA     . PRO A 1 84  ? 20.709 0.814   -11.536 1.00 25.89 ? 78  PRO A CA     1 
ATOM   524  C C      . PRO A 1 84  ? 21.026 2.036   -10.694 1.00 24.86 ? 78  PRO A C      1 
ATOM   525  O O      . PRO A 1 84  ? 21.462 1.935   -9.543  1.00 21.47 ? 78  PRO A O      1 
ATOM   526  C CB     . PRO A 1 84  ? 19.286 0.311   -11.262 1.00 21.15 ? 78  PRO A CB     1 
ATOM   527  C CG     . PRO A 1 84  ? 19.441 -0.660  -10.114 1.00 21.68 ? 78  PRO A CG     1 
ATOM   528  C CD     . PRO A 1 84  ? 20.819 -1.307  -10.327 1.00 21.71 ? 78  PRO A CD     1 
ATOM   529  N N      . GLY A 1 85  ? 20.797 3.206   -11.289 1.00 21.45 ? 79  GLY A N      1 
ATOM   530  C CA     . GLY A 1 85  ? 20.854 4.465   -10.586 1.00 23.05 ? 79  GLY A CA     1 
ATOM   531  C C      . GLY A 1 85  ? 19.459 5.052   -10.417 1.00 22.15 ? 79  GLY A C      1 
ATOM   532  O O      . GLY A 1 85  ? 18.487 4.608   -11.027 1.00 22.09 ? 79  GLY A O      1 
ATOM   533  N N      . ILE A 1 86  ? 19.376 6.062   -9.555  1.00 22.98 ? 80  ILE A N      1 
ATOM   534  C CA     . ILE A 1 86  ? 18.144 6.834   -9.437  1.00 23.25 ? 80  ILE A CA     1 
ATOM   535  C C      . ILE A 1 86  ? 18.477 8.310   -9.254  1.00 26.66 ? 80  ILE A C      1 
ATOM   536  O O      . ILE A 1 86  ? 17.718 9.070   -8.639  1.00 27.14 ? 80  ILE A O      1 
ATOM   537  C CB     . ILE A 1 86  ? 17.196 6.258   -8.361  1.00 26.65 ? 80  ILE A CB     1 
ATOM   538  C CG1    . ILE A 1 86  ? 15.751 6.723   -8.615  1.00 29.86 ? 80  ILE A CG1    1 
ATOM   539  C CG2    . ILE A 1 86  ? 17.692 6.549   -6.936  1.00 26.44 ? 80  ILE A CG2    1 
ATOM   540  C CD1    . ILE A 1 86  ? 14.720 5.803   -8.051  1.00 27.02 ? 80  ILE A CD1    1 
ATOM   541  N N      . PHE A 1 87  ? 19.607 8.735   -9.816  1.00 24.57 ? 81  PHE A N      1 
ATOM   542  C CA     . PHE A 1 87  ? 20.027 10.121  -9.701  1.00 25.20 ? 81  PHE A CA     1 
ATOM   543  C C      . PHE A 1 87  ? 19.779 10.949  -10.957 1.00 28.45 ? 81  PHE A C      1 
ATOM   544  O O      . PHE A 1 87  ? 20.012 12.160  -10.921 1.00 32.54 ? 81  PHE A O      1 
ATOM   545  C CB     . PHE A 1 87  ? 21.501 10.223  -9.267  1.00 27.03 ? 81  PHE A CB     1 
ATOM   546  C CG     . PHE A 1 87  ? 22.459 9.500   -10.174 1.00 28.43 ? 81  PHE A CG     1 
ATOM   547  C CD1    . PHE A 1 87  ? 22.696 8.137   -10.026 1.00 22.01 ? 81  PHE A CD1    1 
ATOM   548  C CD2    . PHE A 1 87  ? 23.130 10.190  -11.173 1.00 29.05 ? 81  PHE A CD2    1 
ATOM   549  C CE1    . PHE A 1 87  ? 23.588 7.476   -10.865 1.00 23.85 ? 81  PHE A CE1    1 
ATOM   550  C CE2    . PHE A 1 87  ? 24.012 9.540   -12.013 1.00 25.61 ? 81  PHE A CE2    1 
ATOM   551  C CZ     . PHE A 1 87  ? 24.240 8.180   -11.862 1.00 28.78 ? 81  PHE A CZ     1 
ATOM   552  N N      . THR A 1 88  ? 19.324 10.342  -12.057 1.00 27.20 ? 82  THR A N      1 
ATOM   553  C CA     . THR A 1 88  ? 19.004 11.078  -13.275 1.00 33.60 ? 82  THR A CA     1 
ATOM   554  C C      . THR A 1 88  ? 17.523 10.937  -13.610 1.00 32.44 ? 82  THR A C      1 
ATOM   555  O O      . THR A 1 88  ? 16.856 9.984   -13.200 1.00 25.50 ? 82  THR A O      1 
ATOM   556  C CB     . THR A 1 88  ? 19.855 10.627  -14.478 1.00 27.31 ? 82  THR A CB     1 
ATOM   557  O OG1    . THR A 1 88  ? 19.382 9.361   -14.964 1.00 28.31 ? 82  THR A OG1    1 
ATOM   558  C CG2    . THR A 1 88  ? 21.319 10.532  -14.110 1.00 29.69 ? 82  THR A CG2    1 
ATOM   559  N N      . LYS A 1 89  ? 17.009 11.902  -14.374 1.00 35.98 ? 83  LYS A N      1 
ATOM   560  C CA     . LYS A 1 89  ? 15.601 11.840  -14.751 1.00 35.15 ? 83  LYS A CA     1 
ATOM   561  C C      . LYS A 1 89  ? 15.333 10.675  -15.697 1.00 29.99 ? 83  LYS A C      1 
ATOM   562  O O      . LYS A 1 89  ? 14.245 10.093  -15.668 1.00 29.58 ? 83  LYS A O      1 
ATOM   563  C CB     . LYS A 1 89  ? 15.158 13.174  -15.353 1.00 47.26 ? 83  LYS A CB     1 
ATOM   564  N N      . GLU A 1 90  ? 16.316 10.350  -16.518 1.00 33.07 ? 84  GLU A N      1 
ATOM   565  C CA     A GLU A 1 90  ? 16.174 9.100   -17.360 0.50 33.25 ? 84  GLU A CA     1 
ATOM   566  C CA     B GLU A 1 90  ? 16.170 9.101   -17.332 0.50 33.23 ? 84  GLU A CA     1 
ATOM   567  C C      . GLU A 1 90  ? 15.971 7.780   -16.516 1.00 27.47 ? 84  GLU A C      1 
ATOM   568  O O      . GLU A 1 90  ? 15.100 6.817   -16.699 1.00 28.38 ? 84  GLU A O      1 
ATOM   569  C CB     A GLU A 1 90  ? 17.416 8.888   -18.222 0.50 34.71 ? 84  GLU A CB     1 
ATOM   570  C CB     B GLU A 1 90  ? 17.371 8.926   -18.263 0.50 34.70 ? 84  GLU A CB     1 
ATOM   571  C CG     A GLU A 1 90  ? 17.873 10.132  -18.946 0.50 40.55 ? 84  GLU A CG     1 
ATOM   572  C CG     B GLU A 1 90  ? 17.042 8.110   -19.497 0.50 37.14 ? 84  GLU A CG     1 
ATOM   573  C CD     A GLU A 1 90  ? 18.871 11.048  -18.258 0.50 33.95 ? 84  GLU A CD     1 
ATOM   574  C CD     B GLU A 1 90  ? 18.108 7.126   -19.945 0.50 44.15 ? 84  GLU A CD     1 
ATOM   575  O OE1    A GLU A 1 90  ? 20.081 10.755  -18.327 0.50 40.80 ? 84  GLU A OE1    1 
ATOM   576  O OE1    B GLU A 1 90  ? 19.301 7.483   -19.897 0.50 43.03 ? 84  GLU A OE1    1 
ATOM   577  O OE2    A GLU A 1 90  ? 18.437 12.063  -17.686 0.50 32.11 ? 84  GLU A OE2    1 
ATOM   578  O OE2    B GLU A 1 90  ? 17.740 6.008   -20.355 0.50 48.57 ? 84  GLU A OE2    1 
ATOM   579  N N      . GLN A 1 91  ? 16.781 7.733   -15.440 1.00 25.00 ? 85  GLN A N      1 
ATOM   580  C CA     . GLN A 1 91  ? 16.627 6.580   -14.557 1.00 25.26 ? 85  GLN A CA     1 
ATOM   581  C C      . GLN A 1 91  ? 15.271 6.590   -13.860 1.00 25.84 ? 85  GLN A C      1 
ATOM   582  O O      . GLN A 1 91  ? 14.654 5.534   -13.677 1.00 26.06 ? 85  GLN A O      1 
ATOM   583  C CB     . GLN A 1 91  ? 17.773 6.543   -13.540 1.00 22.22 ? 85  GLN A CB     1 
ATOM   584  C CG     . GLN A 1 91  ? 19.133 6.282   -14.178 1.00 23.26 ? 85  GLN A CG     1 
ATOM   585  C CD     . GLN A 1 91  ? 20.285 6.757   -13.316 1.00 26.08 ? 85  GLN A CD     1 
ATOM   586  O OE1    . GLN A 1 91  ? 20.082 7.421   -12.296 1.00 24.78 ? 85  GLN A OE1    1 
ATOM   587  N NE2    . GLN A 1 91  ? 21.508 6.412   -13.717 1.00 26.49 ? 85  GLN A NE2    1 
ATOM   588  N N      . VAL A 1 92  ? 14.797 7.772   -13.454 1.00 23.98 ? 86  VAL A N      1 
ATOM   589  C CA     . VAL A 1 92  ? 13.461 7.892   -12.867 1.00 25.22 ? 86  VAL A CA     1 
ATOM   590  C C      . VAL A 1 92  ? 12.394 7.383   -13.831 1.00 28.08 ? 86  VAL A C      1 
ATOM   591  O O      . VAL A 1 92  ? 11.519 6.597   -13.451 1.00 25.72 ? 86  VAL A O      1 
ATOM   592  C CB     . VAL A 1 92  ? 13.193 9.337   -12.407 1.00 26.01 ? 86  VAL A CB     1 
ATOM   593  C CG1    . VAL A 1 92  ? 11.719 9.537   -12.064 1.00 26.74 ? 86  VAL A CG1    1 
ATOM   594  C CG2    . VAL A 1 92  ? 14.065 9.675   -11.202 1.00 28.65 ? 86  VAL A CG2    1 
ATOM   595  N N      . ARG A 1 93  ? 12.459 7.806   -15.103 1.00 28.25 ? 87  ARG A N      1 
ATOM   596  C CA     . ARG A 1 93  ? 11.447 7.369   -16.065 1.00 28.37 ? 87  ARG A CA     1 
ATOM   597  C C      . ARG A 1 93  ? 11.421 5.852   -16.205 1.00 23.93 ? 87  ARG A C      1 
ATOM   598  O O      . ARG A 1 93  ? 10.348 5.248   -16.328 1.00 25.81 ? 87  ARG A O      1 
ATOM   599  C CB     . ARG A 1 93  ? 11.682 7.993   -17.443 1.00 29.16 ? 87  ARG A CB     1 
ATOM   600  C CG     . ARG A 1 93  ? 10.854 9.233   -17.737 1.00 47.07 ? 87  ARG A CG     1 
ATOM   601  C CD     . ARG A 1 93  ? 11.337 9.919   -19.009 1.00 50.92 ? 87  ARG A CD     1 
ATOM   602  N NE     . ARG A 1 93  ? 12.530 10.738  -18.823 1.00 47.25 ? 87  ARG A NE     1 
ATOM   603  C CZ     . ARG A 1 93  ? 13.607 10.669  -19.592 1.00 49.84 ? 87  ARG A CZ     1 
ATOM   604  N NH1    . ARG A 1 93  ? 13.719 9.756   -20.543 1.00 54.61 ? 87  ARG A NH1    1 
ATOM   605  N NH2    . ARG A 1 93  ? 14.599 11.532  -19.397 1.00 49.60 ? 87  ARG A NH2    1 
ATOM   606  N N      . GLU A 1 94  ? 12.592 5.221   -16.221 1.00 23.32 ? 88  GLU A N      1 
ATOM   607  C CA     . GLU A 1 94  ? 12.636 3.780   -16.434 1.00 25.45 ? 88  GLU A CA     1 
ATOM   608  C C      . GLU A 1 94  ? 12.217 3.013   -15.183 1.00 24.80 ? 88  GLU A C      1 
ATOM   609  O O      . GLU A 1 94  ? 11.554 1.972   -15.282 1.00 24.19 ? 88  GLU A O      1 
ATOM   610  C CB     . GLU A 1 94  ? 14.031 3.353   -16.900 1.00 23.31 ? 88  GLU A CB     1 
ATOM   611  C CG     . GLU A 1 94  ? 14.405 3.856   -18.304 1.00 26.86 ? 88  GLU A CG     1 
ATOM   612  C CD     . GLU A 1 94  ? 13.289 3.653   -19.327 1.00 36.87 ? 88  GLU A CD     1 
ATOM   613  O OE1    . GLU A 1 94  ? 12.812 2.505   -19.501 1.00 33.73 ? 88  GLU A OE1    1 
ATOM   614  O OE2    . GLU A 1 94  ? 12.881 4.657   -19.948 1.00 43.78 ? 88  GLU A OE2    1 
ATOM   615  N N      . TRP A 1 95  ? 12.597 3.501   -13.998 1.00 23.85 ? 89  TRP A N      1 
ATOM   616  C CA     . TRP A 1 95  ? 12.110 2.878   -12.774 1.00 24.48 ? 89  TRP A CA     1 
ATOM   617  C C      . TRP A 1 95  ? 10.592 2.942   -12.700 1.00 23.63 ? 89  TRP A C      1 
ATOM   618  O O      . TRP A 1 95  ? 9.948  2.015   -12.193 1.00 23.90 ? 89  TRP A O      1 
ATOM   619  C CB     . TRP A 1 95  ? 12.701 3.579   -11.557 1.00 20.83 ? 89  TRP A CB     1 
ATOM   620  C CG     . TRP A 1 95  ? 13.998 3.026   -11.036 1.00 21.77 ? 89  TRP A CG     1 
ATOM   621  C CD1    . TRP A 1 95  ? 15.161 3.713   -10.877 1.00 24.84 ? 89  TRP A CD1    1 
ATOM   622  C CD2    . TRP A 1 95  ? 14.239 1.702   -10.544 1.00 20.08 ? 89  TRP A CD2    1 
ATOM   623  N NE1    . TRP A 1 95  ? 16.123 2.899   -10.319 1.00 22.65 ? 89  TRP A NE1    1 
ATOM   624  C CE2    . TRP A 1 95  ? 15.587 1.658   -10.112 1.00 23.03 ? 89  TRP A CE2    1 
ATOM   625  C CE3    . TRP A 1 95  ? 13.458 0.547   -10.437 1.00 21.21 ? 89  TRP A CE3    1 
ATOM   626  C CZ2    . TRP A 1 95  ? 16.166 0.508   -9.565  1.00 20.43 ? 89  TRP A CZ2    1 
ATOM   627  C CZ3    . TRP A 1 95  ? 14.042 -0.602  -9.891  1.00 21.61 ? 89  TRP A CZ3    1 
ATOM   628  C CH2    . TRP A 1 95  ? 15.387 -0.607  -9.466  1.00 18.91 ? 89  TRP A CH2    1 
ATOM   629  N N      . LYS A 1 96  ? 10.004 4.037   -13.195 1.00 24.07 ? 90  LYS A N      1 
ATOM   630  C CA     . LYS A 1 96  ? 8.556  4.216   -13.091 1.00 22.99 ? 90  LYS A CA     1 
ATOM   631  C C      . LYS A 1 96  ? 7.814  3.066   -13.764 1.00 28.56 ? 90  LYS A C      1 
ATOM   632  O O      . LYS A 1 96  ? 6.803  2.579   -13.245 1.00 24.73 ? 90  LYS A O      1 
ATOM   633  C CB     . LYS A 1 96  ? 8.174  5.561   -13.712 1.00 27.62 ? 90  LYS A CB     1 
ATOM   634  C CG     . LYS A 1 96  ? 6.703  5.738   -14.074 1.00 38.28 ? 90  LYS A CG     1 
ATOM   635  C CD     . LYS A 1 96  ? 5.901  6.242   -12.913 1.00 49.30 ? 90  LYS A CD     1 
ATOM   636  C CE     . LYS A 1 96  ? 4.474  6.603   -13.327 1.00 51.80 ? 90  LYS A CE     1 
ATOM   637  N NZ     . LYS A 1 96  ? 4.042  5.896   -14.570 1.00 52.61 ? 90  LYS A NZ     1 
ATOM   638  N N      . LYS A 1 97  ? 8.317  2.607   -14.917 1.00 26.58 ? 91  LYS A N      1 
ATOM   639  C CA     . LYS A 1 97  ? 7.705  1.475   -15.606 1.00 29.37 ? 91  LYS A CA     1 
ATOM   640  C C      . LYS A 1 97  ? 7.796  0.201   -14.775 1.00 30.20 ? 91  LYS A C      1 
ATOM   641  O O      . LYS A 1 97  ? 6.892  -0.643  -14.818 1.00 29.73 ? 91  LYS A O      1 
ATOM   642  C CB     . LYS A 1 97  ? 8.390  1.266   -16.955 1.00 29.65 ? 91  LYS A CB     1 
ATOM   643  C CG     . LYS A 1 97  ? 8.471  2.516   -17.808 1.00 30.35 ? 91  LYS A CG     1 
ATOM   644  C CD     . LYS A 1 97  ? 9.037  2.182   -19.175 1.00 30.90 ? 91  LYS A CD     1 
ATOM   645  C CE     . LYS A 1 97  ? 9.482  3.430   -19.899 1.00 38.76 ? 91  LYS A CE     1 
ATOM   646  N NZ     . LYS A 1 97  ? 10.255 3.071   -21.124 1.00 38.48 ? 91  LYS A NZ     1 
ATOM   647  N N      . ILE A 1 98  ? 8.897  0.026   -14.036 1.00 24.04 ? 92  ILE A N      1 
ATOM   648  C CA     . ILE A 1 98  ? 9.050  -1.159  -13.196 1.00 24.64 ? 92  ILE A CA     1 
ATOM   649  C C      . ILE A 1 98  ? 8.121  -1.083  -11.990 1.00 24.32 ? 92  ILE A C      1 
ATOM   650  O O      . ILE A 1 98  ? 7.429  -2.052  -11.652 1.00 24.95 ? 92  ILE A O      1 
ATOM   651  C CB     . ILE A 1 98  ? 10.527 -1.330  -12.795 1.00 24.17 ? 92  ILE A CB     1 
ATOM   652  C CG1    . ILE A 1 98  ? 11.359 -1.620  -14.045 1.00 24.28 ? 92  ILE A CG1    1 
ATOM   653  C CG2    . ILE A 1 98  ? 10.701 -2.437  -11.756 1.00 24.58 ? 92  ILE A CG2    1 
ATOM   654  C CD1    . ILE A 1 98  ? 12.778 -1.139  -13.947 1.00 26.66 ? 92  ILE A CD1    1 
ATOM   655  N N      . VAL A 1 99  ? 8.082  0.076   -11.334 1.00 22.83 ? 93  VAL A N      1 
ATOM   656  C CA     . VAL A 1 99  ? 7.213  0.254   -10.176 1.00 23.99 ? 93  VAL A CA     1 
ATOM   657  C C      . VAL A 1 99  ? 5.755  0.035   -10.563 1.00 25.62 ? 93  VAL A C      1 
ATOM   658  O O      . VAL A 1 99  ? 4.990  -0.584  -9.818  1.00 24.23 ? 93  VAL A O      1 
ATOM   659  C CB     . VAL A 1 99  ? 7.456  1.637   -9.548  1.00 26.43 ? 93  VAL A CB     1 
ATOM   660  C CG1    . VAL A 1 99  ? 6.436  1.924   -8.477  1.00 26.71 ? 93  VAL A CG1    1 
ATOM   661  C CG2    . VAL A 1 99  ? 8.870  1.713   -8.973  1.00 24.00 ? 93  VAL A CG2    1 
ATOM   662  N N      . ASP A 1 100 ? 5.361  0.496   -11.753 1.00 25.89 ? 94  ASP A N      1 
ATOM   663  C CA     . ASP A 1 100 ? 3.966  0.362   -12.167 1.00 26.56 ? 94  ASP A CA     1 
ATOM   664  C C      . ASP A 1 100 ? 3.575  -1.105  -12.305 1.00 24.93 ? 94  ASP A C      1 
ATOM   665  O O      . ASP A 1 100 ? 2.467  -1.505  -11.921 1.00 27.06 ? 94  ASP A O      1 
ATOM   666  C CB     . ASP A 1 100 ? 3.783  1.069   -13.511 1.00 30.79 ? 94  ASP A CB     1 
ATOM   667  C CG     . ASP A 1 100 ? 3.575  2.566   -13.364 1.00 31.90 ? 94  ASP A CG     1 
ATOM   668  O OD1    . ASP A 1 100 ? 3.538  3.059   -12.215 1.00 32.12 ? 94  ASP A OD1    1 
ATOM   669  O OD2    . ASP A 1 100 ? 3.456  3.252   -14.403 1.00 39.33 ? 94  ASP A OD2    1 
ATOM   670  N N      . VAL A 1 101 ? 4.471  -1.916  -12.869 1.00 25.40 ? 95  VAL A N      1 
ATOM   671  C CA     . VAL A 1 101 ? 4.218  -3.341  -13.055 1.00 24.77 ? 95  VAL A CA     1 
ATOM   672  C C      . VAL A 1 101 ? 4.073  -4.052  -11.705 1.00 28.60 ? 95  VAL A C      1 
ATOM   673  O O      . VAL A 1 101 ? 3.204  -4.914  -11.529 1.00 28.38 ? 95  VAL A O      1 
ATOM   674  C CB     . VAL A 1 101 ? 5.353  -3.921  -13.921 1.00 32.62 ? 95  VAL A CB     1 
ATOM   675  C CG1    . VAL A 1 101 ? 5.537  -5.391  -13.683 1.00 39.12 ? 95  VAL A CG1    1 
ATOM   676  C CG2    . VAL A 1 101 ? 5.111  -3.627  -15.399 1.00 31.69 ? 95  VAL A CG2    1 
ATOM   677  N N      . VAL A 1 102 ? 4.918  -3.701  -10.732 1.00 23.94 ? 96  VAL A N      1 
ATOM   678  C CA     . VAL A 1 102 ? 4.853  -4.326  -9.414  1.00 26.43 ? 96  VAL A CA     1 
ATOM   679  C C      . VAL A 1 102 ? 3.592  -3.891  -8.672  1.00 27.04 ? 96  VAL A C      1 
ATOM   680  O O      . VAL A 1 102 ? 2.924  -4.701  -8.011  1.00 25.24 ? 96  VAL A O      1 
ATOM   681  C CB     . VAL A 1 102 ? 6.138  -3.984  -8.633  1.00 25.60 ? 96  VAL A CB     1 
ATOM   682  C CG1    . VAL A 1 102 ? 6.020  -4.373  -7.178  1.00 30.81 ? 96  VAL A CG1    1 
ATOM   683  C CG2    . VAL A 1 102 ? 7.343  -4.668  -9.277  1.00 28.06 ? 96  VAL A CG2    1 
ATOM   684  N N      . HIS A 1 103 ? 3.250  -2.606  -8.767  1.00 23.54 ? 97  HIS A N      1 
ATOM   685  C CA     . HIS A 1 103 ? 2.042  -2.099  -8.123  1.00 22.41 ? 97  HIS A CA     1 
ATOM   686  C C      . HIS A 1 103 ? 0.783  -2.727  -8.705  1.00 25.95 ? 97  HIS A C      1 
ATOM   687  O O      . HIS A 1 103 ? -0.216 -2.879  -7.990  1.00 27.07 ? 97  HIS A O      1 
ATOM   688  C CB     . HIS A 1 103 ? 2.000  -0.579  -8.252  1.00 23.96 ? 97  HIS A CB     1 
ATOM   689  C CG     . HIS A 1 103 ? 2.798  0.129   -7.203  1.00 22.97 ? 97  HIS A CG     1 
ATOM   690  N ND1    . HIS A 1 103 ? 3.140  1.461   -7.295  1.00 25.91 ? 97  HIS A ND1    1 
ATOM   691  C CD2    . HIS A 1 103 ? 3.325  -0.316  -6.035  1.00 26.78 ? 97  HIS A CD2    1 
ATOM   692  C CE1    . HIS A 1 103 ? 3.840  1.807   -6.228  1.00 28.96 ? 97  HIS A CE1    1 
ATOM   693  N NE2    . HIS A 1 103 ? 3.957  0.750   -5.442  1.00 27.38 ? 97  HIS A NE2    1 
ATOM   694  N N      . ALA A 1 104 ? 0.807  -3.103  -9.989  1.00 27.91 ? 98  ALA A N      1 
ATOM   695  C CA     . ALA A 1 104 ? -0.351 -3.759  -10.587 1.00 28.48 ? 98  ALA A CA     1 
ATOM   696  C C      . ALA A 1 104 ? -0.572 -5.164  -10.043 1.00 31.59 ? 98  ALA A C      1 
ATOM   697  O O      . ALA A 1 104 ? -1.678 -5.702  -10.172 1.00 33.71 ? 98  ALA A O      1 
ATOM   698  C CB     . ALA A 1 104 ? -0.227 -3.779  -12.111 1.00 22.94 ? 98  ALA A CB     1 
ATOM   699  N N      . LYS A 1 105 ? 0.431  -5.710  -9.373  1.00 27.99 ? 99  LYS A N      1 
ATOM   700  C CA     . LYS A 1 105 ? 0.261  -7.024  -8.706  1.00 28.69 ? 99  LYS A CA     1 
ATOM   701  C C      . LYS A 1 105 ? -0.079 -6.807  -7.222  1.00 23.48 ? 99  LYS A C      1 
ATOM   702  O O      . LYS A 1 105 ? -0.261 -7.790  -6.529  1.00 28.68 ? 99  LYS A O      1 
ATOM   703  C CB     . LYS A 1 105 ? 1.523  -7.869  -8.892  1.00 32.14 ? 99  LYS A CB     1 
ATOM   704  C CG     . LYS A 1 105 ? 1.576  -8.629  -10.209 1.00 38.44 ? 99  LYS A CG     1 
ATOM   705  C CD     . LYS A 1 105 ? 2.694  -9.631  -10.277 1.00 42.69 ? 99  LYS A CD     1 
ATOM   706  C CE     . LYS A 1 105 ? 2.361  -10.952 -9.620  1.00 47.20 ? 99  LYS A CE     1 
ATOM   707  N NZ     . LYS A 1 105 ? 3.459  -11.933 -9.786  1.00 40.09 ? 99  LYS A NZ     1 
ATOM   708  N N      . GLY A 1 106 ? -0.149 -5.561  -6.779  1.00 23.45 ? 100 GLY A N      1 
ATOM   709  C CA     . GLY A 1 106 ? -0.549 -5.269  -5.396  1.00 26.26 ? 100 GLY A CA     1 
ATOM   710  C C      . GLY A 1 106 ? 0.598  -5.290  -4.399  1.00 27.17 ? 100 GLY A C      1 
ATOM   711  O O      . GLY A 1 106 ? 0.330  -5.336  -3.203  1.00 25.83 ? 100 GLY A O      1 
ATOM   712  N N      . ALA A 1 107 ? 1.831  -5.250  -4.890  1.00 25.22 ? 101 ALA A N      1 
ATOM   713  C CA     . ALA A 1 107 ? 2.947  -5.289  -3.959  1.00 24.45 ? 101 ALA A CA     1 
ATOM   714  C C      . ALA A 1 107 ? 3.337  -3.886  -3.508  1.00 24.60 ? 101 ALA A C      1 
ATOM   715  O O      . ALA A 1 107 ? 3.007  -2.881  -4.142  1.00 25.97 ? 101 ALA A O      1 
ATOM   716  C CB     . ALA A 1 107 ? 4.145  -5.990  -4.595  1.00 25.17 ? 101 ALA A CB     1 
ATOM   717  N N      . VAL A 1 108 ? 4.033  -3.833  -2.367  1.00 21.79 ? 102 VAL A N      1 
ATOM   718  C CA     . VAL A 1 108 ? 4.694  -2.629  -1.885  1.00 18.81 ? 102 VAL A CA     1 
ATOM   719  C C      . VAL A 1 108 ? 6.171  -2.783  -2.214  1.00 21.49 ? 102 VAL A C      1 
ATOM   720  O O      . VAL A 1 108 ? 6.740  -3.870  -2.040  1.00 22.03 ? 102 VAL A O      1 
ATOM   721  C CB     . VAL A 1 108 ? 4.486  -2.483  -0.361  1.00 19.76 ? 102 VAL A CB     1 
ATOM   722  C CG1    . VAL A 1 108 ? 5.137  -1.213  0.146   1.00 23.25 ? 102 VAL A CG1    1 
ATOM   723  C CG2    . VAL A 1 108 ? 2.979  -2.508  -0.012  1.00 22.95 ? 102 VAL A CG2    1 
ATOM   724  N N      . ILE A 1 109 ? 6.789  -1.718  -2.717  1.00 21.38 ? 103 ILE A N      1 
ATOM   725  C CA     . ILE A 1 109 ? 8.187  -1.778  -3.152  1.00 20.54 ? 103 ILE A CA     1 
ATOM   726  C C      . ILE A 1 109 ? 8.945  -0.550  -2.665  1.00 21.74 ? 103 ILE A C      1 
ATOM   727  O O      . ILE A 1 109 ? 8.513  0.587   -2.879  1.00 20.55 ? 103 ILE A O      1 
ATOM   728  C CB     . ILE A 1 109 ? 8.328  -1.975  -4.680  1.00 21.56 ? 103 ILE A CB     1 
ATOM   729  C CG1    . ILE A 1 109 ? 9.803  -2.127  -5.083  1.00 22.33 ? 103 ILE A CG1    1 
ATOM   730  C CG2    . ILE A 1 109 ? 7.663  -0.843  -5.471  1.00 23.10 ? 103 ILE A CG2    1 
ATOM   731  C CD1    . ILE A 1 109 ? 10.001 -2.673  -6.511  1.00 22.73 ? 103 ILE A CD1    1 
ATOM   732  N N      . PHE A 1 110 ? 10.099 -0.782  -2.031  1.00 19.42 ? 104 PHE A N      1 
ATOM   733  C CA     . PHE A 1 110 ? 11.015 0.266   -1.604  1.00 18.24 ? 104 PHE A CA     1 
ATOM   734  C C      . PHE A 1 110 ? 12.299 0.148   -2.422  1.00 20.67 ? 104 PHE A C      1 
ATOM   735  O O      . PHE A 1 110 ? 12.732 -0.958  -2.756  1.00 21.45 ? 104 PHE A O      1 
ATOM   736  C CB     . PHE A 1 110 ? 11.399 0.036   -0.139  1.00 19.26 ? 104 PHE A CB     1 
ATOM   737  C CG     . PHE A 1 110 ? 10.477 0.690   0.882   1.00 20.05 ? 104 PHE A CG     1 
ATOM   738  C CD1    . PHE A 1 110 ? 9.108  0.806   0.651   1.00 23.24 ? 104 PHE A CD1    1 
ATOM   739  C CD2    . PHE A 1 110 ? 10.995 1.125   2.096   1.00 19.05 ? 104 PHE A CD2    1 
ATOM   740  C CE1    . PHE A 1 110 ? 8.274  1.390   1.602   1.00 21.48 ? 104 PHE A CE1    1 
ATOM   741  C CE2    . PHE A 1 110 ? 10.171 1.701   3.068   1.00 19.90 ? 104 PHE A CE2    1 
ATOM   742  C CZ     . PHE A 1 110 ? 8.809  1.831   2.820   1.00 20.51 ? 104 PHE A CZ     1 
ATOM   743  N N      . CYS A 1 111 ? 12.922 1.284   -2.716  1.00 19.64 ? 105 CYS A N      1 
ATOM   744  C CA     . CYS A 1 111 ? 14.176 1.320   -3.461  1.00 21.43 ? 105 CYS A CA     1 
ATOM   745  C C      . CYS A 1 111 ? 15.323 1.487   -2.473  1.00 20.71 ? 105 CYS A C      1 
ATOM   746  O O      . CYS A 1 111 ? 15.325 2.434   -1.677  1.00 20.37 ? 105 CYS A O      1 
ATOM   747  C CB     . CYS A 1 111 ? 14.166 2.501   -4.432  1.00 21.14 ? 105 CYS A CB     1 
ATOM   748  S SG     . CYS A 1 111 ? 15.732 2.761   -5.321  1.00 22.32 ? 105 CYS A SG     1 
ATOM   749  N N      . GLN A 1 112 ? 16.297 0.584   -2.524  1.00 17.89 ? 106 GLN A N      1 
ATOM   750  C CA     . GLN A 1 112 ? 17.436 0.675   -1.612  1.00 21.22 ? 106 GLN A CA     1 
ATOM   751  C C      . GLN A 1 112 ? 18.484 1.616   -2.198  1.00 21.14 ? 106 GLN A C      1 
ATOM   752  O O      . GLN A 1 112 ? 18.938 1.420   -3.334  1.00 19.17 ? 106 GLN A O      1 
ATOM   753  C CB     . GLN A 1 112 ? 18.041 -0.694  -1.308  1.00 20.98 ? 106 GLN A CB     1 
ATOM   754  C CG     . GLN A 1 112 ? 19.190 -0.569  -0.307  1.00 20.43 ? 106 GLN A CG     1 
ATOM   755  C CD     . GLN A 1 112 ? 20.036 -1.814  -0.174  1.00 22.19 ? 106 GLN A CD     1 
ATOM   756  O OE1    . GLN A 1 112 ? 20.740 -2.205  -1.109  1.00 20.09 ? 106 GLN A OE1    1 
ATOM   757  N NE2    . GLN A 1 112 ? 20.018 -2.420  1.020   1.00 18.50 ? 106 GLN A NE2    1 
ATOM   758  N N      . LEU A 1 113 ? 18.845 2.649   -1.439  1.00 19.39 ? 107 LEU A N      1 
ATOM   759  C CA     . LEU A 1 113 ? 19.827 3.634   -1.877  1.00 19.24 ? 107 LEU A CA     1 
ATOM   760  C C      . LEU A 1 113 ? 21.209 3.236   -1.375  1.00 18.21 ? 107 LEU A C      1 
ATOM   761  O O      . LEU A 1 113 ? 21.403 3.048   -0.166  1.00 20.75 ? 107 LEU A O      1 
ATOM   762  C CB     . LEU A 1 113 ? 19.446 5.013   -1.339  1.00 20.50 ? 107 LEU A CB     1 
ATOM   763  C CG     . LEU A 1 113 ? 18.012 5.461   -1.661  1.00 20.58 ? 107 LEU A CG     1 
ATOM   764  C CD1    . LEU A 1 113 ? 17.779 6.858   -1.108  1.00 22.19 ? 107 LEU A CD1    1 
ATOM   765  C CD2    . LEU A 1 113 ? 17.760 5.427   -3.168  1.00 22.18 ? 107 LEU A CD2    1 
ATOM   766  N N      . TRP A 1 114 ? 22.175 3.142   -2.295  1.00 19.73 ? 108 TRP A N      1 
ATOM   767  C CA     . TRP A 1 114 ? 23.428 2.436   -2.020  1.00 20.60 ? 108 TRP A CA     1 
ATOM   768  C C      . TRP A 1 114 ? 24.610 3.267   -2.505  1.00 21.17 ? 108 TRP A C      1 
ATOM   769  O O      . TRP A 1 114 ? 24.706 3.582   -3.702  1.00 19.97 ? 108 TRP A O      1 
ATOM   770  C CB     . TRP A 1 114 ? 23.391 1.101   -2.764  1.00 18.65 ? 108 TRP A CB     1 
ATOM   771  C CG     . TRP A 1 114 ? 24.584 0.185   -2.606  1.00 19.76 ? 108 TRP A CG     1 
ATOM   772  C CD1    . TRP A 1 114 ? 25.441 0.116   -1.545  1.00 22.22 ? 108 TRP A CD1    1 
ATOM   773  C CD2    . TRP A 1 114 ? 25.019 -0.806  -3.543  1.00 19.61 ? 108 TRP A CD2    1 
ATOM   774  N NE1    . TRP A 1 114 ? 26.384 -0.862  -1.763  1.00 20.04 ? 108 TRP A NE1    1 
ATOM   775  C CE2    . TRP A 1 114 ? 26.147 -1.442  -2.983  1.00 19.35 ? 108 TRP A CE2    1 
ATOM   776  C CE3    . TRP A 1 114 ? 24.570 -1.211  -4.808  1.00 20.88 ? 108 TRP A CE3    1 
ATOM   777  C CZ2    . TRP A 1 114 ? 26.821 -2.469  -3.634  1.00 20.06 ? 108 TRP A CZ2    1 
ATOM   778  C CZ3    . TRP A 1 114 ? 25.227 -2.226  -5.445  1.00 20.27 ? 108 TRP A CZ3    1 
ATOM   779  C CH2    . TRP A 1 114 ? 26.354 -2.837  -4.875  1.00 19.95 ? 108 TRP A CH2    1 
ATOM   780  N N      . HIS A 1 115 ? 25.524 3.597   -1.590  1.00 20.70 ? 109 HIS A N      1 
ATOM   781  C CA     . HIS A 1 115 ? 26.836 4.150   -1.934  1.00 20.71 ? 109 HIS A CA     1 
ATOM   782  C C      . HIS A 1 115 ? 27.900 3.192   -1.415  1.00 20.14 ? 109 HIS A C      1 
ATOM   783  O O      . HIS A 1 115 ? 27.915 2.870   -0.223  1.00 19.87 ? 109 HIS A O      1 
ATOM   784  C CB     . HIS A 1 115 ? 27.016 5.542   -1.325  1.00 20.59 ? 109 HIS A CB     1 
ATOM   785  C CG     . HIS A 1 115 ? 28.140 6.335   -1.924  1.00 21.76 ? 109 HIS A CG     1 
ATOM   786  N ND1    . HIS A 1 115 ? 29.438 5.868   -1.989  1.00 21.31 ? 109 HIS A ND1    1 
ATOM   787  C CD2    . HIS A 1 115 ? 28.166 7.580   -2.459  1.00 22.93 ? 109 HIS A CD2    1 
ATOM   788  C CE1    . HIS A 1 115 ? 30.210 6.785   -2.543  1.00 22.00 ? 109 HIS A CE1    1 
ATOM   789  N NE2    . HIS A 1 115 ? 29.462 7.832   -2.843  1.00 24.65 ? 109 HIS A NE2    1 
ATOM   790  N N      . VAL A 1 116 ? 28.785 2.729   -2.305  1.00 18.95 ? 110 VAL A N      1 
ATOM   791  C CA     . VAL A 1 116 ? 29.790 1.733   -1.923  1.00 19.07 ? 110 VAL A CA     1 
ATOM   792  C C      . VAL A 1 116 ? 31.005 2.307   -1.212  1.00 19.64 ? 110 VAL A C      1 
ATOM   793  O O      . VAL A 1 116 ? 31.811 1.537   -0.668  1.00 20.95 ? 110 VAL A O      1 
ATOM   794  C CB     . VAL A 1 116 ? 30.308 0.959   -3.149  1.00 19.66 ? 110 VAL A CB     1 
ATOM   795  C CG1    . VAL A 1 116 ? 29.159 0.284   -3.852  1.00 20.80 ? 110 VAL A CG1    1 
ATOM   796  C CG2    . VAL A 1 116 ? 31.059 1.908   -4.104  1.00 19.34 ? 110 VAL A CG2    1 
ATOM   797  N N      . GLY A 1 117 ? 31.186 3.620   -1.221  1.00 18.48 ? 111 GLY A N      1 
ATOM   798  C CA     . GLY A 1 117 ? 32.378 4.175   -0.601  1.00 19.91 ? 111 GLY A CA     1 
ATOM   799  C C      . GLY A 1 117 ? 33.642 3.612   -1.233  1.00 20.28 ? 111 GLY A C      1 
ATOM   800  O O      . GLY A 1 117 ? 33.797 3.585   -2.463  1.00 20.16 ? 111 GLY A O      1 
ATOM   801  N N      . ARG A 1 118 ? 34.559 3.148   -0.374  1.00 19.46 ? 112 ARG A N      1 
ATOM   802  C CA     . ARG A 1 118 ? 35.859 2.672   -0.835  1.00 22.88 ? 112 ARG A CA     1 
ATOM   803  C C      . ARG A 1 118 ? 35.782 1.336   -1.554  1.00 20.95 ? 112 ARG A C      1 
ATOM   804  O O      . ARG A 1 118 ? 36.785 0.911   -2.142  1.00 22.09 ? 112 ARG A O      1 
ATOM   805  C CB     . ARG A 1 118 ? 36.812 2.560   0.355   1.00 22.29 ? 112 ARG A CB     1 
ATOM   806  C CG     . ARG A 1 118 ? 36.564 1.344   1.231   1.00 21.14 ? 112 ARG A CG     1 
ATOM   807  C CD     . ARG A 1 118 ? 37.493 1.332   2.461   1.00 18.99 ? 112 ARG A CD     1 
ATOM   808  N NE     . ARG A 1 118 ? 37.186 0.225   3.362   1.00 19.75 ? 112 ARG A NE     1 
ATOM   809  C CZ     . ARG A 1 118 ? 38.027 -0.239  4.279   1.00 19.67 ? 112 ARG A CZ     1 
ATOM   810  N NH1    . ARG A 1 118 ? 39.197 0.337   4.496   1.00 22.96 ? 112 ARG A NH1    1 
ATOM   811  N NH2    . ARG A 1 118 ? 37.687 -1.309  4.987   1.00 24.53 ? 112 ARG A NH2    1 
ATOM   812  N N      . ALA A 1 119 ? 34.624 0.672   -1.540  1.00 20.36 ? 113 ALA A N      1 
ATOM   813  C CA     . ALA A 1 119 ? 34.446 -0.608  -2.224  1.00 18.64 ? 113 ALA A CA     1 
ATOM   814  C C      . ALA A 1 119 ? 34.137 -0.379  -3.708  1.00 22.48 ? 113 ALA A C      1 
ATOM   815  O O      . ALA A 1 119 ? 33.062 -0.704  -4.216  1.00 21.82 ? 113 ALA A O      1 
ATOM   816  C CB     . ALA A 1 119 ? 33.367 -1.439  -1.540  1.00 20.86 ? 113 ALA A CB     1 
ATOM   817  N N      . SER A 1 120 ? 35.119 0.188   -4.404  1.00 19.91 ? 114 SER A N      1 
ATOM   818  C CA     . SER A 1 120 ? 34.963 0.545   -5.808  1.00 19.60 ? 114 SER A CA     1 
ATOM   819  C C      . SER A 1 120 ? 36.314 0.366   -6.488  1.00 20.72 ? 114 SER A C      1 
ATOM   820  O O      . SER A 1 120 ? 37.236 -0.218  -5.912  1.00 21.01 ? 114 SER A O      1 
ATOM   821  C CB     . SER A 1 120 ? 34.422 1.973   -5.940  1.00 23.67 ? 114 SER A CB     1 
ATOM   822  O OG     . SER A 1 120 ? 33.995 2.231   -7.264  1.00 21.19 ? 114 SER A OG     1 
ATOM   823  N N      . HIS A 1 121 ? 36.425 0.877   -7.717  1.00 21.66 ? 115 HIS A N      1 
ATOM   824  C CA     . HIS A 1 121 ? 37.628 0.732   -8.532  1.00 21.08 ? 115 HIS A CA     1 
ATOM   825  C C      . HIS A 1 121 ? 37.595 1.848   -9.568  1.00 20.77 ? 115 HIS A C      1 
ATOM   826  O O      . HIS A 1 121 ? 36.526 2.381   -9.890  1.00 23.07 ? 115 HIS A O      1 
ATOM   827  C CB     . HIS A 1 121 ? 37.642 -0.664  -9.182  1.00 19.67 ? 115 HIS A CB     1 
ATOM   828  C CG     . HIS A 1 121 ? 38.882 -0.985  -9.970  1.00 21.47 ? 115 HIS A CG     1 
ATOM   829  N ND1    . HIS A 1 121 ? 39.152 -0.442  -11.207 1.00 25.33 ? 115 HIS A ND1    1 
ATOM   830  C CD2    . HIS A 1 121 ? 39.914 -1.819  -9.692  1.00 24.79 ? 115 HIS A CD2    1 
ATOM   831  C CE1    . HIS A 1 121 ? 40.302 -0.917  -11.652 1.00 26.02 ? 115 HIS A CE1    1 
ATOM   832  N NE2    . HIS A 1 121 ? 40.781 -1.761  -10.757 1.00 24.67 ? 115 HIS A NE2    1 
ATOM   833  N N      . GLU A 1 122 ? 38.779 2.199   -10.091 1.00 24.26 ? 116 GLU A N      1 
ATOM   834  C CA     . GLU A 1 122 ? 38.861 3.234   -11.123 1.00 25.29 ? 116 GLU A CA     1 
ATOM   835  C C      . GLU A 1 122 ? 37.882 2.980   -12.268 1.00 22.06 ? 116 GLU A C      1 
ATOM   836  O O      . GLU A 1 122 ? 37.309 3.922   -12.824 1.00 24.27 ? 116 GLU A O      1 
ATOM   837  C CB     . GLU A 1 122 ? 40.291 3.343   -11.657 1.00 28.90 ? 116 GLU A CB     1 
ATOM   838  N N      . VAL A 1 123 ? 37.665 1.712   -12.624 1.00 22.86 ? 117 VAL A N      1 
ATOM   839  C CA     . VAL A 1 123 ? 36.791 1.393   -13.748 1.00 25.28 ? 117 VAL A CA     1 
ATOM   840  C C      . VAL A 1 123 ? 35.347 1.819   -13.496 1.00 24.03 ? 117 VAL A C      1 
ATOM   841  O O      . VAL A 1 123 ? 34.587 2.020   -14.450 1.00 24.91 ? 117 VAL A O      1 
ATOM   842  C CB     . VAL A 1 123 ? 36.886 -0.108  -14.098 1.00 22.73 ? 117 VAL A CB     1 
ATOM   843  C CG1    . VAL A 1 123 ? 36.124 -0.947  -13.080 1.00 24.59 ? 117 VAL A CG1    1 
ATOM   844  C CG2    . VAL A 1 123 ? 36.369 -0.358  -15.506 1.00 23.58 ? 117 VAL A CG2    1 
ATOM   845  N N      . TYR A 1 124 ? 34.953 1.972   -12.231 1.00 22.75 ? 118 TYR A N      1 
ATOM   846  C CA     . TYR A 1 124 ? 33.583 2.310   -11.866 1.00 22.25 ? 118 TYR A CA     1 
ATOM   847  C C      . TYR A 1 124 ? 33.411 3.784   -11.534 1.00 22.70 ? 118 TYR A C      1 
ATOM   848  O O      . TYR A 1 124 ? 32.287 4.219   -11.259 1.00 25.86 ? 118 TYR A O      1 
ATOM   849  C CB     . TYR A 1 124 ? 33.121 1.461   -10.667 1.00 20.83 ? 118 TYR A CB     1 
ATOM   850  C CG     . TYR A 1 124 ? 33.015 -0.018  -10.979 1.00 19.75 ? 118 TYR A CG     1 
ATOM   851  C CD1    . TYR A 1 124 ? 32.188 -0.472  -12.009 1.00 21.37 ? 118 TYR A CD1    1 
ATOM   852  C CD2    . TYR A 1 124 ? 33.739 -0.961  -10.241 1.00 19.98 ? 118 TYR A CD2    1 
ATOM   853  C CE1    . TYR A 1 124 ? 32.092 -1.813  -12.299 1.00 22.85 ? 118 TYR A CE1    1 
ATOM   854  C CE2    . TYR A 1 124 ? 33.647 -2.318  -10.535 1.00 22.50 ? 118 TYR A CE2    1 
ATOM   855  C CZ     . TYR A 1 124 ? 32.824 -2.733  -11.573 1.00 21.46 ? 118 TYR A CZ     1 
ATOM   856  O OH     . TYR A 1 124 ? 32.709 -4.070  -11.894 1.00 20.97 ? 118 TYR A OH     1 
ATOM   857  N N      . GLN A 1 125 ? 34.492 4.559   -11.561 1.00 23.72 ? 119 GLN A N      1 
ATOM   858  C CA     . GLN A 1 125 ? 34.477 5.944   -11.145 1.00 25.66 ? 119 GLN A CA     1 
ATOM   859  C C      . GLN A 1 125 ? 34.602 6.870   -12.348 1.00 29.05 ? 119 GLN A C      1 
ATOM   860  O O      . GLN A 1 125 ? 35.342 6.568   -13.294 1.00 30.33 ? 119 GLN A O      1 
ATOM   861  C CB     . GLN A 1 125 ? 35.649 6.200   -10.199 1.00 27.12 ? 119 GLN A CB     1 
ATOM   862  C CG     . GLN A 1 125 ? 35.467 5.593   -8.818  1.00 21.90 ? 119 GLN A CG     1 
ATOM   863  C CD     . GLN A 1 125 ? 34.215 6.087   -8.113  1.00 27.15 ? 119 GLN A CD     1 
ATOM   864  O OE1    . GLN A 1 125 ? 33.940 7.286   -8.085  1.00 27.67 ? 119 GLN A OE1    1 
ATOM   865  N NE2    . GLN A 1 125 ? 33.460 5.165   -7.528  1.00 23.39 ? 119 GLN A NE2    1 
ATOM   866  N N      . PRO A 1 126 ? 33.893 7.997   -12.338 1.00 29.64 ? 120 PRO A N      1 
ATOM   867  C CA     . PRO A 1 126 ? 34.052 8.977   -13.420 1.00 34.23 ? 120 PRO A CA     1 
ATOM   868  C C      . PRO A 1 126 ? 35.499 9.431   -13.518 1.00 38.94 ? 120 PRO A C      1 
ATOM   869  O O      . PRO A 1 126 ? 36.144 9.730   -12.511 1.00 34.44 ? 120 PRO A O      1 
ATOM   870  C CB     . PRO A 1 126 ? 33.131 10.129  -12.999 1.00 37.47 ? 120 PRO A CB     1 
ATOM   871  C CG     . PRO A 1 126 ? 32.223 9.555   -11.949 1.00 36.58 ? 120 PRO A CG     1 
ATOM   872  C CD     . PRO A 1 126 ? 33.005 8.480   -11.269 1.00 32.79 ? 120 PRO A CD     1 
ATOM   873  N N      . ALA A 1 127 ? 36.013 9.461   -14.747 1.00 33.47 ? 121 ALA A N      1 
ATOM   874  C CA     . ALA A 1 127 ? 37.393 9.846   -15.029 1.00 39.05 ? 121 ALA A CA     1 
ATOM   875  C C      . ALA A 1 127 ? 38.419 8.965   -14.315 1.00 36.76 ? 121 ALA A C      1 
ATOM   876  O O      . ALA A 1 127 ? 39.586 9.350   -14.183 1.00 41.01 ? 121 ALA A O      1 
ATOM   877  C CB     . ALA A 1 127 ? 37.648 11.334  -14.754 1.00 43.07 ? 121 ALA A CB     1 
ATOM   878  N N      . GLY A 1 128 ? 38.016 7.779   -13.864 1.00 31.09 ? 122 GLY A N      1 
ATOM   879  C CA     . GLY A 1 128 ? 38.932 6.906   -13.149 1.00 32.42 ? 122 GLY A CA     1 
ATOM   880  C C      . GLY A 1 128 ? 39.406 7.461   -11.825 1.00 35.34 ? 122 GLY A C      1 
ATOM   881  O O      . GLY A 1 128 ? 40.500 7.108   -11.366 1.00 35.00 ? 122 GLY A O      1 
ATOM   882  N N      . ALA A 1 129 ? 38.609 8.324   -11.196 1.00 35.32 ? 123 ALA A N      1 
ATOM   883  C CA     . ALA A 1 129 ? 38.987 8.936   -9.930  1.00 36.04 ? 123 ALA A CA     1 
ATOM   884  C C      . ALA A 1 129 ? 39.006 7.898   -8.811  1.00 31.49 ? 123 ALA A C      1 
ATOM   885  O O      . ALA A 1 129 ? 38.452 6.803   -8.927  1.00 31.00 ? 123 ALA A O      1 
ATOM   886  C CB     . ALA A 1 129 ? 38.006 10.051  -9.568  1.00 38.85 ? 123 ALA A CB     1 
ATOM   887  N N      . ALA A 1 130 ? 39.671 8.251   -7.719  1.00 31.42 ? 124 ALA A N      1 
ATOM   888  C CA     . ALA A 1 130 ? 39.677 7.380   -6.558  1.00 28.37 ? 124 ALA A CA     1 
ATOM   889  C C      . ALA A 1 130 ? 38.296 7.384   -5.902  1.00 28.48 ? 124 ALA A C      1 
ATOM   890  O O      . ALA A 1 130 ? 37.633 8.427   -5.852  1.00 28.29 ? 124 ALA A O      1 
ATOM   891  C CB     . ALA A 1 130 ? 40.717 7.863   -5.546  1.00 28.76 ? 124 ALA A CB     1 
ATOM   892  N N      . PRO A 1 131 ? 37.837 6.244   -5.394  1.00 26.41 ? 125 PRO A N      1 
ATOM   893  C CA     . PRO A 1 131 ? 36.596 6.237   -4.609  1.00 21.56 ? 125 PRO A CA     1 
ATOM   894  C C      . PRO A 1 131 ? 36.756 7.034   -3.325  1.00 25.23 ? 125 PRO A C      1 
ATOM   895  O O      . PRO A 1 131 ? 37.864 7.360   -2.893  1.00 27.68 ? 125 PRO A O      1 
ATOM   896  C CB     . PRO A 1 131 ? 36.379 4.753   -4.306  1.00 25.54 ? 125 PRO A CB     1 
ATOM   897  C CG     . PRO A 1 131 ? 37.727 4.159   -4.376  1.00 36.23 ? 125 PRO A CG     1 
ATOM   898  C CD     . PRO A 1 131 ? 38.455 4.910   -5.452  1.00 26.72 ? 125 PRO A CD     1 
ATOM   899  N N      . ILE A 1 132 ? 35.620 7.346   -2.701  1.00 22.31 ? 126 ILE A N      1 
ATOM   900  C CA     . ILE A 1 132 ? 35.606 8.159   -1.487  1.00 21.59 ? 126 ILE A CA     1 
ATOM   901  C C      . ILE A 1 132 ? 35.294 7.284   -0.283  1.00 24.77 ? 126 ILE A C      1 
ATOM   902  O O      . ILE A 1 132 ? 34.621 6.254   -0.390  1.00 23.00 ? 126 ILE A O      1 
ATOM   903  C CB     . ILE A 1 132 ? 34.616 9.340   -1.560  1.00 23.08 ? 126 ILE A CB     1 
ATOM   904  C CG1    . ILE A 1 132 ? 33.185 8.831   -1.732  1.00 23.32 ? 126 ILE A CG1    1 
ATOM   905  C CG2    . ILE A 1 132 ? 34.988 10.277  -2.691  1.00 25.96 ? 126 ILE A CG2    1 
ATOM   906  C CD1    . ILE A 1 132 ? 32.171 9.644   -1.000  1.00 24.85 ? 126 ILE A CD1    1 
ATOM   907  N N      . SER A 1 133 ? 35.762 7.718   0.883   1.00 21.83 ? 127 SER A N      1 
ATOM   908  C CA     . SER A 1 133 ? 35.498 6.976   2.109   1.00 20.85 ? 127 SER A CA     1 
ATOM   909  C C      . SER A 1 133 ? 35.654 7.910   3.305   1.00 22.31 ? 127 SER A C      1 
ATOM   910  O O      . SER A 1 133 ? 35.942 9.101   3.164   1.00 23.80 ? 127 SER A O      1 
ATOM   911  C CB     . SER A 1 133 ? 36.413 5.749   2.214   1.00 22.62 ? 127 SER A CB     1 
ATOM   912  O OG     . SER A 1 133 ? 36.051 4.916   3.313   1.00 24.49 ? 127 SER A OG     1 
ATOM   913  N N      . SER A 1 134 ? 35.433 7.354   4.498   1.00 22.81 ? 128 SER A N      1 
ATOM   914  C CA     . SER A 1 134 ? 35.797 8.030   5.736   1.00 22.54 ? 128 SER A CA     1 
ATOM   915  C C      . SER A 1 134 ? 37.305 8.065   5.935   1.00 24.18 ? 128 SER A C      1 
ATOM   916  O O      . SER A 1 134 ? 37.806 8.879   6.722   1.00 24.58 ? 128 SER A O      1 
ATOM   917  C CB     . SER A 1 134 ? 35.189 7.245   6.890   1.00 24.81 ? 128 SER A CB     1 
ATOM   918  O OG     . SER A 1 134 ? 35.660 5.904   6.837   1.00 25.08 ? 128 SER A OG     1 
ATOM   919  N N      . THR A 1 135 ? 38.027 7.192   5.241   1.00 23.75 ? 129 THR A N      1 
ATOM   920  C CA     . THR A 1 135 ? 39.422 6.888   5.528   1.00 24.61 ? 129 THR A CA     1 
ATOM   921  C C      . THR A 1 135 ? 40.177 6.830   4.207   1.00 25.11 ? 129 THR A C      1 
ATOM   922  O O      . THR A 1 135 ? 39.580 6.773   3.129   1.00 25.17 ? 129 THR A O      1 
ATOM   923  C CB     . THR A 1 135 ? 39.522 5.524   6.233   1.00 28.00 ? 129 THR A CB     1 
ATOM   924  O OG1    . THR A 1 135 ? 40.890 5.222   6.536   1.00 29.38 ? 129 THR A OG1    1 
ATOM   925  C CG2    . THR A 1 135 ? 38.948 4.417   5.338   1.00 28.82 ? 129 THR A CG2    1 
ATOM   926  N N      . GLU A 1 136 ? 41.508 6.848   4.291   1.00 26.26 ? 130 GLU A N      1 
ATOM   927  C CA     . GLU A 1 136 ? 42.348 6.533   3.140   1.00 26.88 ? 130 GLU A CA     1 
ATOM   928  C C      . GLU A 1 136 ? 42.815 5.084   3.133   1.00 28.49 ? 130 GLU A C      1 
ATOM   929  O O      . GLU A 1 136 ? 43.546 4.690   2.221   1.00 29.44 ? 130 GLU A O      1 
ATOM   930  C CB     . GLU A 1 136 ? 43.569 7.456   3.062   1.00 31.86 ? 130 GLU A CB     1 
ATOM   931  C CG     . GLU A 1 136 ? 43.283 8.924   3.268   1.00 40.94 ? 130 GLU A CG     1 
ATOM   932  C CD     . GLU A 1 136 ? 44.552 9.755   3.274   1.00 54.19 ? 130 GLU A CD     1 
ATOM   933  O OE1    . GLU A 1 136 ? 45.621 9.216   3.640   1.00 54.21 ? 130 GLU A OE1    1 
ATOM   934  O OE2    . GLU A 1 136 ? 44.483 10.946  2.901   1.00 53.71 ? 130 GLU A OE2    1 
ATOM   935  N N      . LYS A 1 137 ? 42.415 4.291   4.114   1.00 24.84 ? 131 LYS A N      1 
ATOM   936  C CA     . LYS A 1 137 ? 42.805 2.889   4.147   1.00 25.28 ? 131 LYS A CA     1 
ATOM   937  C C      . LYS A 1 137 ? 42.035 2.116   3.086   1.00 29.86 ? 131 LYS A C      1 
ATOM   938  O O      . LYS A 1 137 ? 40.797 2.166   3.064   1.00 26.17 ? 131 LYS A O      1 
ATOM   939  C CB     . LYS A 1 137 ? 42.483 2.291   5.510   1.00 31.25 ? 131 LYS A CB     1 
ATOM   940  C CG     . LYS A 1 137 ? 43.314 2.836   6.643   1.00 32.84 ? 131 LYS A CG     1 
ATOM   941  C CD     . LYS A 1 137 ? 43.070 2.027   7.909   1.00 37.06 ? 131 LYS A CD     1 
ATOM   942  C CE     . LYS A 1 137 ? 41.662 2.267   8.451   1.00 30.53 ? 131 LYS A CE     1 
ATOM   943  N NZ     . LYS A 1 137 ? 41.587 2.001   9.925   1.00 32.67 ? 131 LYS A NZ     1 
ATOM   944  N N      . PRO A 1 138 ? 42.710 1.381   2.211   1.00 27.41 ? 132 PRO A N      1 
ATOM   945  C CA     . PRO A 1 138 ? 41.997 0.516   1.273   1.00 26.29 ? 132 PRO A CA     1 
ATOM   946  C C      . PRO A 1 138 ? 41.523 -0.753  1.960   1.00 24.54 ? 132 PRO A C      1 
ATOM   947  O O      . PRO A 1 138 ? 42.044 -1.174  2.995   1.00 26.85 ? 132 PRO A O      1 
ATOM   948  C CB     . PRO A 1 138 ? 43.072 0.189   0.230   1.00 26.77 ? 132 PRO A CB     1 
ATOM   949  C CG     . PRO A 1 138 ? 44.327 0.167   1.022   1.00 31.18 ? 132 PRO A CG     1 
ATOM   950  C CD     . PRO A 1 138 ? 44.174 1.269   2.052   1.00 27.60 ? 132 PRO A CD     1 
ATOM   951  N N      . ILE A 1 139 ? 40.483 -1.348  1.373   1.00 22.52 ? 133 ILE A N      1 
ATOM   952  C CA     . ILE A 1 139 ? 40.134 -2.717  1.723   1.00 21.74 ? 133 ILE A CA     1 
ATOM   953  C C      . ILE A 1 139 ? 41.373 -3.578  1.498   1.00 27.73 ? 133 ILE A C      1 
ATOM   954  O O      . ILE A 1 139 ? 42.091 -3.413  0.500   1.00 29.84 ? 133 ILE A O      1 
ATOM   955  C CB     . ILE A 1 139 ? 38.958 -3.180  0.845   1.00 22.64 ? 133 ILE A CB     1 
ATOM   956  C CG1    . ILE A 1 139 ? 37.674 -2.415  1.202   1.00 21.49 ? 133 ILE A CG1    1 
ATOM   957  C CG2    . ILE A 1 139 ? 38.713 -4.681  0.984   1.00 25.11 ? 133 ILE A CG2    1 
ATOM   958  C CD1    . ILE A 1 139 ? 36.644 -2.448  0.075   1.00 21.55 ? 133 ILE A CD1    1 
ATOM   959  N N      . SER A 1 140 ? 41.638 -4.498  2.427   1.00 27.25 ? 134 SER A N      1 
ATOM   960  C CA     . SER A 1 140 ? 42.878 -5.264  2.337   1.00 30.32 ? 134 SER A CA     1 
ATOM   961  C C      . SER A 1 140 ? 42.849 -6.192  1.125   1.00 30.85 ? 134 SER A C      1 
ATOM   962  O O      . SER A 1 140 ? 41.814 -6.404  0.490   1.00 30.51 ? 134 SER A O      1 
ATOM   963  C CB     . SER A 1 140 ? 43.104 -6.100  3.590   1.00 32.34 ? 134 SER A CB     1 
ATOM   964  O OG     . SER A 1 140 ? 42.227 -7.208  3.615   1.00 33.62 ? 134 SER A OG     1 
ATOM   965  N N      . ASN A 1 141 ? 44.010 -6.768  0.819   1.00 30.96 ? 135 ASN A N      1 
ATOM   966  C CA     . ASN A 1 141 ? 44.140 -7.578  -0.387  1.00 28.41 ? 135 ASN A CA     1 
ATOM   967  C C      . ASN A 1 141 ? 43.426 -8.921  -0.284  1.00 30.75 ? 135 ASN A C      1 
ATOM   968  O O      . ASN A 1 141 ? 43.334 -9.631  -1.293  1.00 38.62 ? 135 ASN A O      1 
ATOM   969  C CB     . ASN A 1 141 ? 45.614 -7.743  -0.763  1.00 29.70 ? 135 ASN A CB     1 
ATOM   970  C CG     . ASN A 1 141 ? 46.202 -6.476  -1.349  1.00 30.04 ? 135 ASN A CG     1 
ATOM   971  O OD1    . ASN A 1 141 ? 46.067 -6.205  -2.548  1.00 37.35 ? 135 ASN A OD1    1 
ATOM   972  N ND2    . ASN A 1 141 ? 46.864 -5.688  -0.509  1.00 34.11 ? 135 ASN A ND2    1 
ATOM   973  N N      . ARG A 1 142 ? 42.898 -9.266  0.894   1.00 33.50 ? 136 ARG A N      1 
ATOM   974  C CA     . ARG A 1 142 ? 42.122 -10.490 1.067   1.00 33.93 ? 136 ARG A CA     1 
ATOM   975  C C      . ARG A 1 142 ? 40.801 -10.462 0.303   1.00 39.88 ? 136 ARG A C      1 
ATOM   976  O O      . ARG A 1 142 ? 40.245 -11.528 0.015   1.00 42.47 ? 136 ARG A O      1 
ATOM   977  C CB     . ARG A 1 142 ? 41.856 -10.731 2.553   1.00 36.18 ? 136 ARG A CB     1 
ATOM   978  N N      . TRP A 1 143 ? 40.284 -9.279  -0.014  1.00 30.68 ? 137 TRP A N      1 
ATOM   979  C CA     . TRP A 1 143 ? 39.072 -9.127  -0.812  1.00 26.78 ? 137 TRP A CA     1 
ATOM   980  C C      . TRP A 1 143 ? 39.413 -8.588  -2.190  1.00 22.03 ? 137 TRP A C      1 
ATOM   981  O O      . TRP A 1 143 ? 40.283 -7.725  -2.328  1.00 29.28 ? 137 TRP A O      1 
ATOM   982  C CB     . TRP A 1 143 ? 38.085 -8.168  -0.146  1.00 30.41 ? 137 TRP A CB     1 
ATOM   983  C CG     . TRP A 1 143 ? 37.909 -8.435  1.292   1.00 32.08 ? 137 TRP A CG     1 
ATOM   984  C CD1    . TRP A 1 143 ? 38.686 -7.980  2.321   1.00 32.95 ? 137 TRP A CD1    1 
ATOM   985  C CD2    . TRP A 1 143 ? 36.910 -9.268  1.877   1.00 36.32 ? 137 TRP A CD2    1 
ATOM   986  N NE1    . TRP A 1 143 ? 38.205 -8.458  3.517   1.00 33.49 ? 137 TRP A NE1    1 
ATOM   987  C CE2    . TRP A 1 143 ? 37.124 -9.260  3.269   1.00 30.52 ? 137 TRP A CE2    1 
ATOM   988  C CE3    . TRP A 1 143 ? 35.848 -10.016 1.360   1.00 36.75 ? 137 TRP A CE3    1 
ATOM   989  C CZ2    . TRP A 1 143 ? 36.313 -9.966  4.152   1.00 39.86 ? 137 TRP A CZ2    1 
ATOM   990  C CZ3    . TRP A 1 143 ? 35.044 -10.718 2.242   1.00 41.71 ? 137 TRP A CZ3    1 
ATOM   991  C CH2    . TRP A 1 143 ? 35.283 -10.689 3.619   1.00 37.81 ? 137 TRP A CH2    1 
ATOM   992  N N      . ARG A 1 144 ? 38.689 -9.076  -3.203  1.00 25.50 ? 138 ARG A N      1 
ATOM   993  C CA     . ARG A 1 144 ? 38.833 -8.640  -4.589  1.00 24.04 ? 138 ARG A CA     1 
ATOM   994  C C      . ARG A 1 144 ? 37.493 -8.152  -5.133  1.00 22.48 ? 138 ARG A C      1 
ATOM   995  O O      . ARG A 1 144 ? 36.428 -8.619  -4.720  1.00 28.31 ? 138 ARG A O      1 
ATOM   996  C CB     . ARG A 1 144 ? 39.342 -9.765  -5.508  1.00 26.48 ? 138 ARG A CB     1 
ATOM   997  C CG     . ARG A 1 144 ? 40.552 -10.540 -5.020  1.00 41.53 ? 138 ARG A CG     1 
ATOM   998  C CD     . ARG A 1 144 ? 41.688 -9.588  -4.726  1.00 42.66 ? 138 ARG A CD     1 
ATOM   999  N NE     . ARG A 1 144 ? 42.829 -10.237 -4.096  1.00 56.23 ? 138 ARG A NE     1 
ATOM   1000 C CZ     . ARG A 1 144 ? 43.931 -10.593 -4.745  1.00 61.40 ? 138 ARG A CZ     1 
ATOM   1001 N NH1    . ARG A 1 144 ? 44.077 -10.359 -6.040  1.00 48.69 ? 138 ARG A NH1    1 
ATOM   1002 N NH2    . ARG A 1 144 ? 44.905 -11.209 -4.080  1.00 56.57 ? 138 ARG A NH2    1 
ATOM   1003 N N      . ILE A 1 145 ? 37.556 -7.211  -6.084  1.00 22.24 ? 139 ILE A N      1 
ATOM   1004 C CA     . ILE A 1 145 ? 36.360 -6.585  -6.643  1.00 21.36 ? 139 ILE A CA     1 
ATOM   1005 C C      . ILE A 1 145 ? 36.032 -7.225  -7.985  1.00 22.54 ? 139 ILE A C      1 
ATOM   1006 O O      . ILE A 1 145 ? 36.920 -7.466  -8.810  1.00 24.28 ? 139 ILE A O      1 
ATOM   1007 C CB     . ILE A 1 145 ? 36.527 -5.054  -6.760  1.00 20.15 ? 139 ILE A CB     1 
ATOM   1008 C CG1    . ILE A 1 145 ? 35.183 -4.385  -7.075  1.00 21.60 ? 139 ILE A CG1    1 
ATOM   1009 C CG2    . ILE A 1 145 ? 37.570 -4.661  -7.809  1.00 25.16 ? 139 ILE A CG2    1 
ATOM   1010 C CD1    . ILE A 1 145 ? 35.269 -2.875  -7.102  1.00 24.70 ? 139 ILE A CD1    1 
ATOM   1011 N N      . LEU A 1 146 ? 34.754 -7.524  -8.202  1.00 20.01 ? 140 LEU A N      1 
ATOM   1012 C CA     . LEU A 1 146 ? 34.321 -7.987  -9.519  1.00 19.13 ? 140 LEU A CA     1 
ATOM   1013 C C      . LEU A 1 146 ? 34.449 -6.852  -10.528 1.00 20.70 ? 140 LEU A C      1 
ATOM   1014 O O      . LEU A 1 146 ? 33.972 -5.741  -10.301 1.00 20.75 ? 140 LEU A O      1 
ATOM   1015 C CB     . LEU A 1 146 ? 32.867 -8.468  -9.438  1.00 23.48 ? 140 LEU A CB     1 
ATOM   1016 C CG     . LEU A 1 146 ? 32.179 -8.900  -10.740 1.00 22.84 ? 140 LEU A CG     1 
ATOM   1017 C CD1    . LEU A 1 146 ? 32.880 -10.112 -11.349 1.00 24.28 ? 140 LEU A CD1    1 
ATOM   1018 C CD2    . LEU A 1 146 ? 30.697 -9.194  -10.507 1.00 23.37 ? 140 LEU A CD2    1 
ATOM   1019 N N      . MET A 1 147 ? 35.114 -7.132  -11.645 1.00 20.54 ? 141 MET A N      1 
ATOM   1020 C CA     . MET A 1 147 ? 35.380 -6.257  -12.774 1.00 21.31 ? 141 MET A CA     1 
ATOM   1021 C C      . MET A 1 147 ? 34.305 -6.418  -13.838 1.00 22.67 ? 141 MET A C      1 
ATOM   1022 O O      . MET A 1 147 ? 33.633 -7.447  -13.898 1.00 22.48 ? 141 MET A O      1 
ATOM   1023 C CB     . MET A 1 147 ? 36.725 -6.653  -13.368 1.00 23.94 ? 141 MET A CB     1 
ATOM   1024 C CG     . MET A 1 147 ? 38.005 -6.149  -12.676 1.00 30.58 ? 141 MET A CG     1 
ATOM   1025 S SD     . MET A 1 147 ? 38.003 -4.608  -11.771 1.00 26.55 ? 141 MET A SD     1 
ATOM   1026 C CE     . MET A 1 147 ? 38.514 -3.561  -13.141 1.00 31.53 ? 141 MET A CE     1 
ATOM   1027 N N      . PRO A 1 148 ? 34.126 -5.412  -14.698 1.00 19.80 ? 142 PRO A N      1 
ATOM   1028 C CA     . PRO A 1 148 ? 33.116 -5.536  -15.763 1.00 24.22 ? 142 PRO A CA     1 
ATOM   1029 C C      . PRO A 1 148 ? 33.339 -6.714  -16.702 1.00 24.77 ? 142 PRO A C      1 
ATOM   1030 O O      . PRO A 1 148 ? 32.366 -7.222  -17.272 1.00 27.29 ? 142 PRO A O      1 
ATOM   1031 C CB     . PRO A 1 148 ? 33.217 -4.189  -16.492 1.00 26.41 ? 142 PRO A CB     1 
ATOM   1032 C CG     . PRO A 1 148 ? 33.669 -3.235  -15.436 1.00 26.30 ? 142 PRO A CG     1 
ATOM   1033 C CD     . PRO A 1 148 ? 34.639 -4.034  -14.582 1.00 21.92 ? 142 PRO A CD     1 
ATOM   1034 N N      . ASP A 1 149 ? 34.574 -7.186  -16.859 1.00 21.83 ? 143 ASP A N      1 
ATOM   1035 C CA     . ASP A 1 149 ? 34.834 -8.334  -17.722 1.00 24.94 ? 143 ASP A CA     1 
ATOM   1036 C C      . ASP A 1 149 ? 34.723 -9.672  -17.000 1.00 31.43 ? 143 ASP A C      1 
ATOM   1037 O O      . ASP A 1 149 ? 35.052 -10.707 -17.588 1.00 28.50 ? 143 ASP A O      1 
ATOM   1038 C CB     . ASP A 1 149 ? 36.191 -8.220  -18.433 1.00 25.18 ? 143 ASP A CB     1 
ATOM   1039 C CG     . ASP A 1 149 ? 37.384 -8.256  -17.482 1.00 29.72 ? 143 ASP A CG     1 
ATOM   1040 O OD1    . ASP A 1 149 ? 37.207 -8.439  -16.250 1.00 27.96 ? 143 ASP A OD1    1 
ATOM   1041 O OD2    . ASP A 1 149 ? 38.520 -8.079  -17.984 1.00 30.05 ? 143 ASP A OD2    1 
ATOM   1042 N N      . GLY A 1 150 ? 34.278 -9.687  -15.746 1.00 25.86 ? 144 GLY A N      1 
ATOM   1043 C CA     . GLY A 1 150 ? 34.093 -10.933 -15.043 1.00 25.99 ? 144 GLY A CA     1 
ATOM   1044 C C      . GLY A 1 150 ? 35.301 -11.422 -14.273 1.00 26.36 ? 144 GLY A C      1 
ATOM   1045 O O      . GLY A 1 150 ? 35.191 -12.419 -13.546 1.00 31.65 ? 144 GLY A O      1 
ATOM   1046 N N      . THR A 1 151 ? 36.445 -10.764 -14.412 1.00 26.43 ? 145 THR A N      1 
ATOM   1047 C CA     . THR A 1 151 ? 37.594 -11.080 -13.583 1.00 28.11 ? 145 THR A CA     1 
ATOM   1048 C C      . THR A 1 151 ? 37.471 -10.338 -12.259 1.00 26.72 ? 145 THR A C      1 
ATOM   1049 O O      . THR A 1 151 ? 36.507 -9.608  -12.012 1.00 24.25 ? 145 THR A O      1 
ATOM   1050 C CB     . THR A 1 151 ? 38.885 -10.666 -14.276 1.00 26.73 ? 145 THR A CB     1 
ATOM   1051 O OG1    . THR A 1 151 ? 38.872 -9.252  -14.520 1.00 29.20 ? 145 THR A OG1    1 
ATOM   1052 C CG2    . THR A 1 151 ? 39.057 -11.407 -15.592 1.00 31.05 ? 145 THR A CG2    1 
ATOM   1053 N N      . HIS A 1 152 ? 38.470 -10.503 -11.402 1.00 25.67 ? 146 HIS A N      1 
ATOM   1054 C CA     . HIS A 1 152 ? 38.481 -9.846  -10.106 1.00 26.67 ? 146 HIS A CA     1 
ATOM   1055 C C      . HIS A 1 152 ? 39.723 -8.975  -9.999  1.00 30.99 ? 146 HIS A C      1 
ATOM   1056 O O      . HIS A 1 152 ? 40.813 -9.372  -10.426 1.00 39.55 ? 146 HIS A O      1 
ATOM   1057 C CB     . HIS A 1 152 ? 38.401 -10.887 -8.994  1.00 30.49 ? 146 HIS A CB     1 
ATOM   1058 C CG     . HIS A 1 152 ? 37.042 -11.502 -8.869  1.00 29.47 ? 146 HIS A CG     1 
ATOM   1059 N ND1    . HIS A 1 152 ? 36.058 -10.993 -8.046  1.00 30.77 ? 146 HIS A ND1    1 
ATOM   1060 C CD2    . HIS A 1 152 ? 36.484 -12.552 -9.519  1.00 34.71 ? 146 HIS A CD2    1 
ATOM   1061 C CE1    . HIS A 1 152 ? 34.966 -11.727 -8.167  1.00 33.84 ? 146 HIS A CE1    1 
ATOM   1062 N NE2    . HIS A 1 152 ? 35.197 -12.678 -9.055  1.00 42.91 ? 146 HIS A NE2    1 
ATOM   1063 N N      . GLY A 1 153 ? 39.537 -7.764  -9.485  1.00 24.28 ? 147 GLY A N      1 
ATOM   1064 C CA     . GLY A 1 153 ? 40.593 -6.773  -9.406  1.00 21.52 ? 147 GLY A CA     1 
ATOM   1065 C C      . GLY A 1 153 ? 40.901 -6.366  -7.979  1.00 22.78 ? 147 GLY A C      1 
ATOM   1066 O O      . GLY A 1 153 ? 40.341 -6.925  -7.029  1.00 25.55 ? 147 GLY A O      1 
ATOM   1067 N N      . ILE A 1 154 ? 41.783 -5.381  -7.819  1.00 23.67 ? 148 ILE A N      1 
ATOM   1068 C CA     . ILE A 1 154 ? 42.279 -4.976  -6.505  1.00 21.94 ? 148 ILE A CA     1 
ATOM   1069 C C      . ILE A 1 154 ? 41.604 -3.674  -6.088  1.00 24.93 ? 148 ILE A C      1 
ATOM   1070 O O      . ILE A 1 154 ? 41.539 -2.719  -6.871  1.00 25.05 ? 148 ILE A O      1 
ATOM   1071 C CB     . ILE A 1 154 ? 43.811 -4.833  -6.525  1.00 31.15 ? 148 ILE A CB     1 
ATOM   1072 C CG1    . ILE A 1 154 ? 44.463 -6.199  -6.723  1.00 32.14 ? 148 ILE A CG1    1 
ATOM   1073 C CG2    . ILE A 1 154 ? 44.310 -4.242  -5.220  1.00 28.84 ? 148 ILE A CG2    1 
ATOM   1074 C CD1    . ILE A 1 154 ? 45.797 -6.130  -7.447  1.00 37.42 ? 148 ILE A CD1    1 
ATOM   1075 N N      . TYR A 1 155 ? 41.107 -3.627  -4.845  1.00 22.16 ? 149 TYR A N      1 
ATOM   1076 C CA     . TYR A 1 155 ? 40.505 -2.397  -4.334  1.00 26.22 ? 149 TYR A CA     1 
ATOM   1077 C C      . TYR A 1 155 ? 41.572 -1.322  -4.161  1.00 25.75 ? 149 TYR A C      1 
ATOM   1078 O O      . TYR A 1 155 ? 42.596 -1.569  -3.502  1.00 24.64 ? 149 TYR A O      1 
ATOM   1079 C CB     . TYR A 1 155 ? 39.819 -2.640  -2.989  1.00 21.49 ? 149 TYR A CB     1 
ATOM   1080 C CG     . TYR A 1 155 ? 38.545 -3.431  -3.077  1.00 21.36 ? 149 TYR A CG     1 
ATOM   1081 C CD1    . TYR A 1 155 ? 37.364 -2.828  -3.504  1.00 21.46 ? 149 TYR A CD1    1 
ATOM   1082 C CD2    . TYR A 1 155 ? 38.498 -4.767  -2.691  1.00 22.49 ? 149 TYR A CD2    1 
ATOM   1083 C CE1    . TYR A 1 155 ? 36.181 -3.536  -3.561  1.00 22.07 ? 149 TYR A CE1    1 
ATOM   1084 C CE2    . TYR A 1 155 ? 37.315 -5.485  -2.748  1.00 21.83 ? 149 TYR A CE2    1 
ATOM   1085 C CZ     . TYR A 1 155 ? 36.159 -4.859  -3.179  1.00 19.67 ? 149 TYR A CZ     1 
ATOM   1086 O OH     . TYR A 1 155 ? 34.983 -5.558  -3.265  1.00 24.03 ? 149 TYR A OH     1 
ATOM   1087 N N      . PRO A 1 156 ? 41.371 -0.129  -4.710  1.00 24.53 ? 150 PRO A N      1 
ATOM   1088 C CA     . PRO A 1 156 ? 42.373 0.932   -4.604  1.00 25.43 ? 150 PRO A CA     1 
ATOM   1089 C C      . PRO A 1 156 ? 42.246 1.701   -3.296  1.00 28.01 ? 150 PRO A C      1 
ATOM   1090 O O      . PRO A 1 156 ? 41.290 1.559   -2.532  1.00 25.71 ? 150 PRO A O      1 
ATOM   1091 C CB     . PRO A 1 156 ? 42.021 1.845   -5.783  1.00 28.31 ? 150 PRO A CB     1 
ATOM   1092 C CG     . PRO A 1 156 ? 40.548 1.712   -5.892  1.00 28.12 ? 150 PRO A CG     1 
ATOM   1093 C CD     . PRO A 1 156 ? 40.271 0.253   -5.614  1.00 27.44 ? 150 PRO A CD     1 
ATOM   1094 N N      . LYS A 1 157 ? 43.241 2.535   -3.066  1.00 27.49 ? 151 LYS A N      1 
ATOM   1095 C CA     . LYS A 1 157 ? 43.232 3.431   -1.921  1.00 28.51 ? 151 LYS A CA     1 
ATOM   1096 C C      . LYS A 1 157 ? 42.158 4.491   -2.134  1.00 28.61 ? 151 LYS A C      1 
ATOM   1097 O O      . LYS A 1 157 ? 42.123 5.129   -3.197  1.00 29.55 ? 151 LYS A O      1 
ATOM   1098 C CB     . LYS A 1 157 ? 44.601 4.102   -1.852  1.00 37.58 ? 151 LYS A CB     1 
ATOM   1099 C CG     . LYS A 1 157 ? 45.063 4.434   -0.468  1.00 40.70 ? 151 LYS A CG     1 
ATOM   1100 C CD     . LYS A 1 157 ? 46.448 5.055   -0.478  1.00 39.91 ? 151 LYS A CD     1 
ATOM   1101 C CE     . LYS A 1 157 ? 46.675 5.871   0.790   1.00 41.55 ? 151 LYS A CE     1 
ATOM   1102 N NZ     . LYS A 1 157 ? 46.342 5.114   2.043   1.00 37.22 ? 151 LYS A NZ     1 
ATOM   1103 N N      . PRO A 1 158 ? 41.253 4.688   -1.182  1.00 25.95 ? 152 PRO A N      1 
ATOM   1104 C CA     . PRO A 1 158 ? 40.227 5.719   -1.333  1.00 23.63 ? 152 PRO A CA     1 
ATOM   1105 C C      . PRO A 1 158 ? 40.742 7.082   -0.883  1.00 28.84 ? 152 PRO A C      1 
ATOM   1106 O O      . PRO A 1 158 ? 41.827 7.222   -0.309  1.00 29.24 ? 152 PRO A O      1 
ATOM   1107 C CB     . PRO A 1 158 ? 39.124 5.238   -0.380  1.00 24.94 ? 152 PRO A CB     1 
ATOM   1108 C CG     . PRO A 1 158 ? 39.889 4.559   0.728   1.00 24.33 ? 152 PRO A CG     1 
ATOM   1109 C CD     . PRO A 1 158 ? 41.011 3.832   -0.008  1.00 23.92 ? 152 PRO A CD     1 
ATOM   1110 N N      . ARG A 1 159 ? 39.922 8.087   -1.152  1.00 27.07 ? 153 ARG A N      1 
ATOM   1111 C CA     . ARG A 1 159 ? 40.143 9.459   -0.728  1.00 28.22 ? 153 ARG A CA     1 
ATOM   1112 C C      . ARG A 1 159 ? 39.257 9.737   0.487   1.00 30.28 ? 153 ARG A C      1 
ATOM   1113 O O      . ARG A 1 159 ? 38.044 9.498   0.444   1.00 27.85 ? 153 ARG A O      1 
ATOM   1114 C CB     . ARG A 1 159 ? 39.766 10.383  -1.885  1.00 27.63 ? 153 ARG A CB     1 
ATOM   1115 C CG     . ARG A 1 159 ? 39.905 11.858  -1.630  1.00 36.16 ? 153 ARG A CG     1 
ATOM   1116 C CD     . ARG A 1 159 ? 39.761 12.635  -2.936  1.00 32.08 ? 153 ARG A CD     1 
ATOM   1117 N NE     . ARG A 1 159 ? 38.448 12.527  -3.572  1.00 30.63 ? 153 ARG A NE     1 
ATOM   1118 C CZ     . ARG A 1 159 ? 37.363 13.175  -3.170  1.00 34.81 ? 153 ARG A CZ     1 
ATOM   1119 N NH1    . ARG A 1 159 ? 37.372 13.927  -2.081  1.00 31.13 ? 153 ARG A NH1    1 
ATOM   1120 N NH2    . ARG A 1 159 ? 36.241 13.066  -3.879  1.00 28.90 ? 153 ARG A NH2    1 
ATOM   1121 N N      . ALA A 1 160 ? 39.860 10.220  1.571   1.00 27.00 ? 154 ALA A N      1 
ATOM   1122 C CA     . ALA A 1 160 ? 39.105 10.544  2.778   1.00 28.54 ? 154 ALA A CA     1 
ATOM   1123 C C      . ALA A 1 160 ? 38.464 11.917  2.611   1.00 30.14 ? 154 ALA A C      1 
ATOM   1124 O O      . ALA A 1 160 ? 39.157 12.903  2.340   1.00 34.76 ? 154 ALA A O      1 
ATOM   1125 C CB     . ALA A 1 160 ? 40.020 10.522  4.001   1.00 28.10 ? 154 ALA A CB     1 
ATOM   1126 N N      . ILE A 1 161 ? 37.149 11.985  2.763   1.00 25.20 ? 155 ILE A N      1 
ATOM   1127 C CA     . ILE A 1 161 ? 36.408 13.207  2.474   1.00 24.62 ? 155 ILE A CA     1 
ATOM   1128 C C      . ILE A 1 161 ? 36.320 14.086  3.714   1.00 27.01 ? 155 ILE A C      1 
ATOM   1129 O O      . ILE A 1 161 ? 36.277 13.601  4.850   1.00 25.65 ? 155 ILE A O      1 
ATOM   1130 C CB     . ILE A 1 161 ? 35.015 12.890  1.892   1.00 21.12 ? 155 ILE A CB     1 
ATOM   1131 C CG1    . ILE A 1 161 ? 34.185 12.048  2.870   1.00 24.79 ? 155 ILE A CG1    1 
ATOM   1132 C CG2    . ILE A 1 161 ? 35.167 12.205  0.522   1.00 23.80 ? 155 ILE A CG2    1 
ATOM   1133 C CD1    . ILE A 1 161 ? 32.767 11.794  2.391   1.00 26.12 ? 155 ILE A CD1    1 
ATOM   1134 N N      . GLY A 1 162 ? 36.294 15.401  3.485   1.00 25.64 ? 156 GLY A N      1 
ATOM   1135 C CA     . GLY A 1 162 ? 36.057 16.365  4.537   1.00 27.55 ? 156 GLY A CA     1 
ATOM   1136 C C      . GLY A 1 162 ? 34.578 16.532  4.821   1.00 23.78 ? 156 GLY A C      1 
ATOM   1137 O O      . GLY A 1 162 ? 33.715 15.895  4.216   1.00 24.85 ? 156 GLY A O      1 
ATOM   1138 N N      . THR A 1 163 ? 34.274 17.410  5.776   1.00 24.92 ? 157 THR A N      1 
ATOM   1139 C CA     . THR A 1 163 ? 32.888 17.488  6.223   1.00 22.28 ? 157 THR A CA     1 
ATOM   1140 C C      . THR A 1 163 ? 31.985 18.211  5.230   1.00 25.07 ? 157 THR A C      1 
ATOM   1141 O O      . THR A 1 163 ? 30.776 17.958  5.213   1.00 25.72 ? 157 THR A O      1 
ATOM   1142 C CB     . THR A 1 163 ? 32.790 18.107  7.620   1.00 24.29 ? 157 THR A CB     1 
ATOM   1143 O OG1    . THR A 1 163 ? 33.282 19.450  7.590   1.00 25.63 ? 157 THR A OG1    1 
ATOM   1144 C CG2    . THR A 1 163 ? 33.591 17.286  8.625   1.00 26.66 ? 157 THR A CG2    1 
ATOM   1145 N N      . TYR A 1 164 ? 32.534 19.105  4.401   1.00 25.95 ? 158 TYR A N      1 
ATOM   1146 C CA     . TYR A 1 164 ? 31.722 19.698  3.341   1.00 26.14 ? 158 TYR A CA     1 
ATOM   1147 C C      . TYR A 1 164 ? 31.258 18.628  2.363   1.00 23.53 ? 158 TYR A C      1 
ATOM   1148 O O      . TYR A 1 164 ? 30.078 18.562  2.003   1.00 24.22 ? 158 TYR A O      1 
ATOM   1149 C CB     . TYR A 1 164 ? 32.507 20.785  2.608   1.00 25.69 ? 158 TYR A CB     1 
ATOM   1150 C CG     . TYR A 1 164 ? 31.741 21.416  1.467   1.00 26.67 ? 158 TYR A CG     1 
ATOM   1151 C CD1    . TYR A 1 164 ? 30.641 22.230  1.714   1.00 29.60 ? 158 TYR A CD1    1 
ATOM   1152 C CD2    . TYR A 1 164 ? 32.115 21.204  0.146   1.00 29.09 ? 158 TYR A CD2    1 
ATOM   1153 C CE1    . TYR A 1 164 ? 29.932 22.812  0.686   1.00 30.98 ? 158 TYR A CE1    1 
ATOM   1154 C CE2    . TYR A 1 164 ? 31.407 21.785  -0.892  1.00 31.01 ? 158 TYR A CE2    1 
ATOM   1155 C CZ     . TYR A 1 164 ? 30.319 22.591  -0.613  1.00 32.66 ? 158 TYR A CZ     1 
ATOM   1156 O OH     . TYR A 1 164 ? 29.611 23.175  -1.641  1.00 34.62 ? 158 TYR A OH     1 
ATOM   1157 N N      . GLU A 1 165 ? 32.178 17.755  1.948   1.00 25.52 ? 159 GLU A N      1 
ATOM   1158 C CA     . GLU A 1 165 ? 31.812 16.695  1.018   1.00 23.30 ? 159 GLU A CA     1 
ATOM   1159 C C      . GLU A 1 165 ? 30.859 15.693  1.663   1.00 22.69 ? 159 GLU A C      1 
ATOM   1160 O O      . GLU A 1 165 ? 29.983 15.150  0.984   1.00 24.25 ? 159 GLU A O      1 
ATOM   1161 C CB     . GLU A 1 165 ? 33.079 16.011  0.493   1.00 26.99 ? 159 GLU A CB     1 
ATOM   1162 C CG     . GLU A 1 165 ? 32.833 14.834  -0.440  1.00 32.34 ? 159 GLU A CG     1 
ATOM   1163 C CD     . GLU A 1 165 ? 33.916 14.703  -1.501  1.00 35.55 ? 159 GLU A CD     1 
ATOM   1164 O OE1    . GLU A 1 165 ? 34.993 15.326  -1.341  1.00 33.80 ? 159 GLU A OE1    1 
ATOM   1165 O OE2    . GLU A 1 165 ? 33.703 13.955  -2.482  1.00 31.30 ? 159 GLU A OE2    1 
ATOM   1166 N N      . ILE A 1 166 ? 30.993 15.449  2.972   1.00 22.61 ? 160 ILE A N      1 
ATOM   1167 C CA     . ILE A 1 166 ? 30.014 14.611  3.670   1.00 21.72 ? 160 ILE A CA     1 
ATOM   1168 C C      . ILE A 1 166 ? 28.613 15.187  3.508   1.00 22.91 ? 160 ILE A C      1 
ATOM   1169 O O      . ILE A 1 166 ? 27.652 14.463  3.211   1.00 22.63 ? 160 ILE A O      1 
ATOM   1170 C CB     . ILE A 1 166 ? 30.385 14.457  5.158   1.00 22.86 ? 160 ILE A CB     1 
ATOM   1171 C CG1    . ILE A 1 166 ? 31.560 13.500  5.319   1.00 22.96 ? 160 ILE A CG1    1 
ATOM   1172 C CG2    . ILE A 1 166 ? 29.181 13.953  5.963   1.00 24.63 ? 160 ILE A CG2    1 
ATOM   1173 C CD1    . ILE A 1 166 ? 32.141 13.508  6.718   1.00 26.85 ? 160 ILE A CD1    1 
ATOM   1174 N N      . SER A 1 167 ? 28.475 16.502  3.708   1.00 25.19 ? 161 SER A N      1 
ATOM   1175 C CA     . SER A 1 167 ? 27.173 17.140  3.532   1.00 27.37 ? 161 SER A CA     1 
ATOM   1176 C C      . SER A 1 167 ? 26.674 17.028  2.096   1.00 23.43 ? 161 SER A C      1 
ATOM   1177 O O      . SER A 1 167 ? 25.463 16.921  1.873   1.00 24.24 ? 161 SER A O      1 
ATOM   1178 C CB     . SER A 1 167 ? 27.216 18.595  4.008   1.00 28.47 ? 161 SER A CB     1 
ATOM   1179 O OG     . SER A 1 167 ? 27.769 19.470  3.040   1.00 35.91 ? 161 SER A OG     1 
ATOM   1180 N N      . GLN A 1 168 ? 27.584 17.020  1.116   1.00 25.38 ? 162 GLN A N      1 
ATOM   1181 C CA     . GLN A 1 168 ? 27.157 16.844  -0.270  1.00 25.28 ? 162 GLN A CA     1 
ATOM   1182 C C      . GLN A 1 168 ? 26.649 15.430  -0.526  1.00 24.82 ? 162 GLN A C      1 
ATOM   1183 O O      . GLN A 1 168 ? 25.702 15.237  -1.299  1.00 26.15 ? 162 GLN A O      1 
ATOM   1184 C CB     . GLN A 1 168 ? 28.294 17.193  -1.237  1.00 26.54 ? 162 GLN A CB     1 
ATOM   1185 C CG     . GLN A 1 168 ? 28.646 18.668  -1.266  1.00 30.04 ? 162 GLN A CG     1 
ATOM   1186 C CD     . GLN A 1 168 ? 29.812 18.973  -2.185  1.00 33.88 ? 162 GLN A CD     1 
ATOM   1187 O OE1    . GLN A 1 168 ? 30.872 18.344  -2.101  1.00 32.51 ? 162 GLN A OE1    1 
ATOM   1188 N NE2    . GLN A 1 168 ? 29.619 19.935  -3.079  1.00 37.95 ? 162 GLN A NE2    1 
ATOM   1189 N N      . VAL A 1 169 ? 27.279 14.427  0.091   1.00 23.86 ? 163 VAL A N      1 
ATOM   1190 C CA     . VAL A 1 169 ? 26.817 13.051  -0.074  1.00 22.07 ? 163 VAL A CA     1 
ATOM   1191 C C      . VAL A 1 169 ? 25.446 12.873  0.564   1.00 23.38 ? 163 VAL A C      1 
ATOM   1192 O O      . VAL A 1 169 ? 24.572 12.192  0.013   1.00 23.56 ? 163 VAL A O      1 
ATOM   1193 C CB     . VAL A 1 169 ? 27.857 12.057  0.483   1.00 24.96 ? 163 VAL A CB     1 
ATOM   1194 C CG1    . VAL A 1 169 ? 27.329 10.640  0.403   1.00 26.14 ? 163 VAL A CG1    1 
ATOM   1195 C CG2    . VAL A 1 169 ? 29.185 12.181  -0.259  1.00 24.08 ? 163 VAL A CG2    1 
ATOM   1196 N N      . VAL A 1 170 ? 25.239 13.472  1.744   1.00 22.81 ? 164 VAL A N      1 
ATOM   1197 C CA     . VAL A 1 170 ? 23.915 13.475  2.364   1.00 23.01 ? 164 VAL A CA     1 
ATOM   1198 C C      . VAL A 1 170 ? 22.878 14.055  1.409   1.00 22.99 ? 164 VAL A C      1 
ATOM   1199 O O      . VAL A 1 170 ? 21.776 13.512  1.259   1.00 22.47 ? 164 VAL A O      1 
ATOM   1200 C CB     . VAL A 1 170 ? 23.962 14.239  3.696   1.00 22.41 ? 164 VAL A CB     1 
ATOM   1201 C CG1    . VAL A 1 170 ? 22.557 14.405  4.262   1.00 26.25 ? 164 VAL A CG1    1 
ATOM   1202 C CG2    . VAL A 1 170 ? 24.857 13.516  4.693   1.00 24.64 ? 164 VAL A CG2    1 
ATOM   1203 N N      . GLU A 1 171 ? 23.221 15.154  0.734   1.00 23.11 ? 165 GLU A N      1 
ATOM   1204 C CA     . GLU A 1 171 ? 22.303 15.736  -0.239  1.00 24.69 ? 165 GLU A CA     1 
ATOM   1205 C C      . GLU A 1 171 ? 22.018 14.776  -1.393  1.00 23.85 ? 165 GLU A C      1 
ATOM   1206 O O      . GLU A 1 171 ? 20.896 14.753  -1.909  1.00 24.57 ? 165 GLU A O      1 
ATOM   1207 C CB     . GLU A 1 171 ? 22.848 17.080  -0.738  1.00 29.98 ? 165 GLU A CB     1 
ATOM   1208 C CG     . GLU A 1 171 ? 21.988 17.767  -1.794  1.00 30.15 ? 165 GLU A CG     1 
ATOM   1209 C CD     . GLU A 1 171 ? 20.587 18.125  -1.310  1.00 41.78 ? 165 GLU A CD     1 
ATOM   1210 O OE1    . GLU A 1 171 ? 20.371 18.256  -0.079  1.00 38.14 ? 165 GLU A OE1    1 
ATOM   1211 O OE2    . GLU A 1 171 ? 19.694 18.276  -2.175  1.00 43.44 ? 165 GLU A OE2    1 
ATOM   1212 N N      . ASP A 1 172 ? 23.005 13.965  -1.797  1.00 25.74 ? 166 ASP A N      1 
ATOM   1213 C CA     . ASP A 1 172 ? 22.767 12.967  -2.844  1.00 26.90 ? 166 ASP A CA     1 
ATOM   1214 C C      . ASP A 1 172 ? 21.734 11.933  -2.398  1.00 25.90 ? 166 ASP A C      1 
ATOM   1215 O O      . ASP A 1 172 ? 20.863 11.536  -3.181  1.00 22.62 ? 166 ASP A O      1 
ATOM   1216 C CB     . ASP A 1 172 ? 24.080 12.278  -3.243  1.00 23.36 ? 166 ASP A CB     1 
ATOM   1217 C CG     . ASP A 1 172 ? 25.005 13.178  -4.050  1.00 29.00 ? 166 ASP A CG     1 
ATOM   1218 O OD1    . ASP A 1 172 ? 24.508 14.101  -4.734  1.00 34.10 ? 166 ASP A OD1    1 
ATOM   1219 O OD2    . ASP A 1 172 ? 26.239 12.949  -4.008  1.00 27.05 ? 166 ASP A OD2    1 
ATOM   1220 N N      . TYR A 1 173 ? 21.807 11.487  -1.138  1.00 22.84 ? 167 TYR A N      1 
ATOM   1221 C CA     . TYR A 1 173 ? 20.763 10.614  -0.608  1.00 22.19 ? 167 TYR A CA     1 
ATOM   1222 C C      . TYR A 1 173 ? 19.405 11.310  -0.629  1.00 22.29 ? 167 TYR A C      1 
ATOM   1223 O O      . TYR A 1 173 ? 18.396 10.710  -1.019  1.00 22.73 ? 167 TYR A O      1 
ATOM   1224 C CB     . TYR A 1 173 ? 21.101 10.207  0.827   1.00 20.71 ? 167 TYR A CB     1 
ATOM   1225 C CG     . TYR A 1 173 ? 22.108 9.093   0.976   1.00 19.87 ? 167 TYR A CG     1 
ATOM   1226 C CD1    . TYR A 1 173 ? 21.739 7.763   0.798   1.00 21.71 ? 167 TYR A CD1    1 
ATOM   1227 C CD2    . TYR A 1 173 ? 23.419 9.371   1.335   1.00 21.29 ? 167 TYR A CD2    1 
ATOM   1228 C CE1    . TYR A 1 173 ? 22.661 6.733   0.968   1.00 19.95 ? 167 TYR A CE1    1 
ATOM   1229 C CE2    . TYR A 1 173 ? 24.352 8.351   1.498   1.00 22.96 ? 167 TYR A CE2    1 
ATOM   1230 C CZ     . TYR A 1 173 ? 23.959 7.035   1.317   1.00 21.18 ? 167 TYR A CZ     1 
ATOM   1231 O OH     . TYR A 1 173 ? 24.871 6.017   1.492   1.00 22.40 ? 167 TYR A OH     1 
ATOM   1232 N N      . ARG A 1 174 ? 19.367 12.585  -0.234  1.00 22.30 ? 168 ARG A N      1 
ATOM   1233 C CA     . ARG A 1 174 ? 18.100 13.317  -0.192  1.00 23.13 ? 168 ARG A CA     1 
ATOM   1234 C C      . ARG A 1 174 ? 17.470 13.429  -1.578  1.00 24.86 ? 168 ARG A C      1 
ATOM   1235 O O      . ARG A 1 174 ? 16.282 13.134  -1.756  1.00 25.46 ? 168 ARG A O      1 
ATOM   1236 C CB     . ARG A 1 174 ? 18.319 14.703  0.419   1.00 26.85 ? 168 ARG A CB     1 
ATOM   1237 C CG     . ARG A 1 174 ? 17.023 15.435  0.775   1.00 29.99 ? 168 ARG A CG     1 
ATOM   1238 C CD     . ARG A 1 174 ? 17.302 16.854  1.241   1.00 36.46 ? 168 ARG A CD     1 
ATOM   1239 N NE     . ARG A 1 174 ? 17.602 17.734  0.119   1.00 42.30 ? 168 ARG A NE     1 
ATOM   1240 C CZ     . ARG A 1 174 ? 16.698 18.224  -0.720  1.00 48.69 ? 168 ARG A CZ     1 
ATOM   1241 N NH1    . ARG A 1 174 ? 15.404 17.987  -0.560  1.00 50.68 ? 168 ARG A NH1    1 
ATOM   1242 N NH2    . ARG A 1 174 ? 17.100 18.977  -1.740  1.00 50.17 ? 168 ARG A NH2    1 
ATOM   1243 N N      . ARG A 1 175 ? 18.256 13.845  -2.578  1.00 24.64 ? 169 ARG A N      1 
ATOM   1244 C CA     . ARG A 1 175 ? 17.725 13.957  -3.939  1.00 24.40 ? 169 ARG A CA     1 
ATOM   1245 C C      . ARG A 1 175 ? 17.300 12.601  -4.490  1.00 22.11 ? 169 ARG A C      1 
ATOM   1246 O O      . ARG A 1 175 ? 16.279 12.494  -5.181  1.00 22.82 ? 169 ARG A O      1 
ATOM   1247 C CB     . ARG A 1 175 ? 18.757 14.600  -4.864  1.00 32.77 ? 169 ARG A CB     1 
ATOM   1248 C CG     . ARG A 1 175 ? 19.257 15.946  -4.403  1.00 39.22 ? 169 ARG A CG     1 
ATOM   1249 C CD     . ARG A 1 175 ? 20.460 16.391  -5.228  1.00 45.55 ? 169 ARG A CD     1 
ATOM   1250 N NE     . ARG A 1 175 ? 20.847 17.760  -4.911  1.00 59.02 ? 169 ARG A NE     1 
ATOM   1251 C CZ     . ARG A 1 175 ? 20.520 18.822  -5.635  1.00 72.76 ? 169 ARG A CZ     1 
ATOM   1252 N NH1    . ARG A 1 175 ? 19.817 18.708  -6.753  1.00 71.87 ? 169 ARG A NH1    1 
ATOM   1253 N NH2    . ARG A 1 175 ? 20.909 20.028  -5.229  1.00 73.19 ? 169 ARG A NH2    1 
ATOM   1254 N N      . SER A 1 176 ? 18.084 11.556  -4.219  1.00 24.26 ? 170 SER A N      1 
ATOM   1255 C CA     . SER A 1 176 ? 17.718 10.227  -4.693  1.00 27.03 ? 170 SER A CA     1 
ATOM   1256 C C      . SER A 1 176 ? 16.424 9.750   -4.048  1.00 24.55 ? 170 SER A C      1 
ATOM   1257 O O      . SER A 1 176 ? 15.607 9.091   -4.698  1.00 24.06 ? 170 SER A O      1 
ATOM   1258 C CB     . SER A 1 176 ? 18.856 9.243   -4.428  1.00 23.73 ? 170 SER A CB     1 
ATOM   1259 O OG     . SER A 1 176 ? 19.949 9.538   -5.282  1.00 26.41 ? 170 SER A OG     1 
ATOM   1260 N N      . ALA A 1 177 ? 16.223 10.065  -2.761  1.00 22.04 ? 171 ALA A N      1 
ATOM   1261 C CA     . ALA A 1 177 ? 14.976 9.702   -2.100  1.00 22.36 ? 171 ALA A CA     1 
ATOM   1262 C C      . ALA A 1 177 ? 13.788 10.395  -2.756  1.00 22.12 ? 171 ALA A C      1 
ATOM   1263 O O      . ALA A 1 177 ? 12.750 9.768   -2.993  1.00 23.10 ? 171 ALA A O      1 
ATOM   1264 C CB     . ALA A 1 177 ? 15.052 10.029  -0.601  1.00 23.66 ? 171 ALA A CB     1 
ATOM   1265 N N      . LEU A 1 178 ? 13.935 11.682  -3.083  1.00 25.32 ? 172 LEU A N      1 
ATOM   1266 C CA     . LEU A 1 178 ? 12.874 12.391  -3.799  1.00 27.50 ? 172 LEU A CA     1 
ATOM   1267 C C      . LEU A 1 178 ? 12.649 11.809  -5.190  1.00 26.59 ? 172 LEU A C      1 
ATOM   1268 O O      . LEU A 1 178 ? 11.504 11.712  -5.652  1.00 25.82 ? 172 LEU A O      1 
ATOM   1269 C CB     . LEU A 1 178 ? 13.211 13.879  -3.891  1.00 24.20 ? 172 LEU A CB     1 
ATOM   1270 C CG     . LEU A 1 178 ? 13.113 14.638  -2.564  1.00 31.17 ? 172 LEU A CG     1 
ATOM   1271 C CD1    . LEU A 1 178 ? 13.769 16.009  -2.667  1.00 31.58 ? 172 LEU A CD1    1 
ATOM   1272 C CD2    . LEU A 1 178 ? 11.653 14.774  -2.155  1.00 28.73 ? 172 LEU A CD2    1 
ATOM   1273 N N      . ASN A 1 179 ? 13.730 11.429  -5.881  1.00 24.00 ? 173 ASN A N      1 
ATOM   1274 C CA     . ASN A 1 179 ? 13.585 10.807  -7.197  1.00 24.05 ? 173 ASN A CA     1 
ATOM   1275 C C      . ASN A 1 179 ? 12.851 9.477   -7.093  1.00 23.44 ? 173 ASN A C      1 
ATOM   1276 O O      . ASN A 1 179 ? 12.032 9.140   -7.954  1.00 22.90 ? 173 ASN A O      1 
ATOM   1277 C CB     . ASN A 1 179 ? 14.957 10.603  -7.841  1.00 23.42 ? 173 ASN A CB     1 
ATOM   1278 C CG     . ASN A 1 179 ? 15.550 11.888  -8.368  1.00 32.77 ? 173 ASN A CG     1 
ATOM   1279 O OD1    . ASN A 1 179 ? 14.885 12.921  -8.407  1.00 30.06 ? 173 ASN A OD1    1 
ATOM   1280 N ND2    . ASN A 1 179 ? 16.818 11.834  -8.776  1.00 33.45 ? 173 ASN A ND2    1 
ATOM   1281 N N      . ALA A 1 180 ? 13.119 8.707   -6.034  1.00 23.64 ? 174 ALA A N      1 
ATOM   1282 C CA     . ALA A 1 180 ? 12.412 7.443   -5.860  1.00 22.02 ? 174 ALA A CA     1 
ATOM   1283 C C      . ALA A 1 180 ? 10.915 7.666   -5.693  1.00 23.76 ? 174 ALA A C      1 
ATOM   1284 O O      . ALA A 1 180 ? 10.103 6.940   -6.279  1.00 23.10 ? 174 ALA A O      1 
ATOM   1285 C CB     . ALA A 1 180 ? 12.982 6.676   -4.666  1.00 23.94 ? 174 ALA A CB     1 
ATOM   1286 N N      . ILE A 1 181 ? 10.530 8.675   -4.913  1.00 24.89 ? 175 ILE A N      1 
ATOM   1287 C CA     . ILE A 1 181 ? 9.110  8.975   -4.756  1.00 24.23 ? 175 ILE A CA     1 
ATOM   1288 C C      . ILE A 1 181 ? 8.504  9.393   -6.091  1.00 26.31 ? 175 ILE A C      1 
ATOM   1289 O O      . ILE A 1 181 ? 7.380  9.001   -6.429  1.00 27.79 ? 175 ILE A O      1 
ATOM   1290 C CB     . ILE A 1 181 ? 8.894  10.034  -3.663  1.00 23.62 ? 175 ILE A CB     1 
ATOM   1291 C CG1    . ILE A 1 181 ? 9.326  9.485   -2.302  1.00 26.88 ? 175 ILE A CG1    1 
ATOM   1292 C CG2    . ILE A 1 181 ? 7.414  10.432  -3.613  1.00 25.47 ? 175 ILE A CG2    1 
ATOM   1293 C CD1    . ILE A 1 181 ? 8.686  8.162   -1.966  1.00 29.25 ? 175 ILE A CD1    1 
ATOM   1294 N N      . GLU A 1 182 ? 9.240  10.194  -6.865  1.00 25.09 ? 176 GLU A N      1 
ATOM   1295 C CA     . GLU A 1 182 ? 8.761  10.622  -8.178  1.00 23.77 ? 176 GLU A CA     1 
ATOM   1296 C C      . GLU A 1 182 ? 8.534  9.430   -9.106  1.00 29.04 ? 176 GLU A C      1 
ATOM   1297 O O      . GLU A 1 182 ? 7.585  9.422   -9.902  1.00 27.49 ? 176 GLU A O      1 
ATOM   1298 C CB     . GLU A 1 182 ? 9.749  11.621  -8.781  1.00 25.68 ? 176 GLU A CB     1 
ATOM   1299 C CG     . GLU A 1 182 ? 9.436  11.977  -10.227 1.00 35.04 ? 176 GLU A CG     1 
ATOM   1300 C CD     . GLU A 1 182 ? 10.350 13.045  -10.802 1.00 42.56 ? 176 GLU A CD     1 
ATOM   1301 O OE1    . GLU A 1 182 ? 11.330 13.429  -10.130 1.00 47.12 ? 176 GLU A OE1    1 
ATOM   1302 O OE2    . GLU A 1 182 ? 10.101 13.482  -11.948 1.00 50.50 ? 176 GLU A OE2    1 
ATOM   1303 N N      . ALA A 1 183 ? 9.386  8.405   -9.011  1.00 25.98 ? 177 ALA A N      1 
ATOM   1304 C CA     . ALA A 1 183 ? 9.203  7.186   -9.792  1.00 25.34 ? 177 ALA A CA     1 
ATOM   1305 C C      . ALA A 1 183 ? 8.033  6.339   -9.310  1.00 24.69 ? 177 ALA A C      1 
ATOM   1306 O O      . ALA A 1 183 ? 7.669  5.373   -9.990  1.00 27.49 ? 177 ALA A O      1 
ATOM   1307 C CB     . ALA A 1 183 ? 10.479 6.343   -9.752  1.00 23.97 ? 177 ALA A CB     1 
ATOM   1308 N N      . GLY A 1 184 ? 7.444  6.662   -8.159  1.00 22.44 ? 178 GLY A N      1 
ATOM   1309 C CA     . GLY A 1 184 ? 6.321  5.912   -7.644  1.00 24.35 ? 178 GLY A CA     1 
ATOM   1310 C C      . GLY A 1 184 ? 6.649  4.933   -6.541  1.00 23.26 ? 178 GLY A C      1 
ATOM   1311 O O      . GLY A 1 184 ? 5.737  4.263   -6.041  1.00 23.15 ? 178 GLY A O      1 
ATOM   1312 N N      . PHE A 1 185 ? 7.919  4.807   -6.159  1.00 22.64 ? 179 PHE A N      1 
ATOM   1313 C CA     . PHE A 1 185 ? 8.264  3.910   -5.066  1.00 22.35 ? 179 PHE A CA     1 
ATOM   1314 C C      . PHE A 1 185 ? 7.482  4.266   -3.806  1.00 22.15 ? 179 PHE A C      1 
ATOM   1315 O O      . PHE A 1 185 ? 7.223  5.436   -3.514  1.00 23.69 ? 179 PHE A O      1 
ATOM   1316 C CB     . PHE A 1 185 ? 9.755  3.992   -4.762  1.00 21.28 ? 179 PHE A CB     1 
ATOM   1317 C CG     . PHE A 1 185 ? 10.621 3.193   -5.697  1.00 24.15 ? 179 PHE A CG     1 
ATOM   1318 C CD1    . PHE A 1 185 ? 10.682 1.809   -5.593  1.00 20.76 ? 179 PHE A CD1    1 
ATOM   1319 C CD2    . PHE A 1 185 ? 11.376 3.827   -6.676  1.00 21.31 ? 179 PHE A CD2    1 
ATOM   1320 C CE1    . PHE A 1 185 ? 11.494 1.070   -6.445  1.00 19.30 ? 179 PHE A CE1    1 
ATOM   1321 C CE2    . PHE A 1 185 ? 12.195 3.096   -7.535  1.00 22.05 ? 179 PHE A CE2    1 
ATOM   1322 C CZ     . PHE A 1 185 ? 12.246 1.717   -7.422  1.00 22.57 ? 179 PHE A CZ     1 
ATOM   1323 N N      . ASP A 1 186 ? 7.120  3.239   -3.049  1.00 18.92 ? 180 ASP A N      1 
ATOM   1324 C CA     . ASP A 1 186 ? 6.428  3.439   -1.784  1.00 20.37 ? 180 ASP A CA     1 
ATOM   1325 C C      . ASP A 1 186 ? 7.353  4.003   -0.718  1.00 22.79 ? 180 ASP A C      1 
ATOM   1326 O O      . ASP A 1 186 ? 6.881  4.660   0.216   1.00 25.09 ? 180 ASP A O      1 
ATOM   1327 C CB     . ASP A 1 186 ? 5.837  2.104   -1.367  1.00 22.58 ? 180 ASP A CB     1 
ATOM   1328 C CG     . ASP A 1 186 ? 4.816  1.606   -2.372  1.00 26.89 ? 180 ASP A CG     1 
ATOM   1329 O OD1    . ASP A 1 186 ? 3.791  2.304   -2.543  1.00 29.01 ? 180 ASP A OD1    1 
ATOM   1330 O OD2    . ASP A 1 186 ? 5.020  0.525   -2.964  1.00 25.64 ? 180 ASP A OD2    1 
ATOM   1331 N N      . GLY A 1 187 ? 8.654  3.780   -0.854  1.00 22.33 ? 181 GLY A N      1 
ATOM   1332 C CA     . GLY A 1 187 ? 9.611  4.299   0.099   1.00 20.86 ? 181 GLY A CA     1 
ATOM   1333 C C      . GLY A 1 187 ? 11.010 3.942   -0.351  1.00 19.47 ? 181 GLY A C      1 
ATOM   1334 O O      . GLY A 1 187 ? 11.219 3.447   -1.465  1.00 21.53 ? 181 GLY A O      1 
ATOM   1335 N N      . ILE A 1 188 ? 11.971 4.214   0.528   1.00 20.22 ? 182 ILE A N      1 
ATOM   1336 C CA     . ILE A 1 188 ? 13.369 3.891   0.274   1.00 19.20 ? 182 ILE A CA     1 
ATOM   1337 C C      . ILE A 1 188 ? 13.937 3.162   1.481   1.00 18.65 ? 182 ILE A C      1 
ATOM   1338 O O      . ILE A 1 188 ? 13.449 3.286   2.609   1.00 19.83 ? 182 ILE A O      1 
ATOM   1339 C CB     . ILE A 1 188 ? 14.228 5.129   -0.063  1.00 17.35 ? 182 ILE A CB     1 
ATOM   1340 C CG1    . ILE A 1 188 ? 14.309 6.127   1.089   1.00 25.62 ? 182 ILE A CG1    1 
ATOM   1341 C CG2    . ILE A 1 188 ? 13.689 5.829   -1.333  1.00 22.29 ? 182 ILE A CG2    1 
ATOM   1342 C CD1    . ILE A 1 188 ? 15.533 5.942   2.017   1.00 24.67 ? 182 ILE A CD1    1 
ATOM   1343 N N      . GLU A 1 189 ? 15.025 2.436   1.240   1.00 18.63 ? 183 GLU A N      1 
ATOM   1344 C CA     . GLU A 1 189 ? 15.812 1.847   2.315   1.00 18.01 ? 183 GLU A CA     1 
ATOM   1345 C C      . GLU A 1 189 ? 17.227 2.390   2.227   1.00 19.48 ? 183 GLU A C      1 
ATOM   1346 O O      . GLU A 1 189 ? 17.814 2.429   1.137   1.00 20.40 ? 183 GLU A O      1 
ATOM   1347 C CB     . GLU A 1 189 ? 15.836 0.320   2.224   1.00 19.18 ? 183 GLU A CB     1 
ATOM   1348 C CG     . GLU A 1 189 ? 16.693 -0.319  3.332   1.00 18.99 ? 183 GLU A CG     1 
ATOM   1349 C CD     . GLU A 1 189 ? 16.689 -1.823  3.260   1.00 21.18 ? 183 GLU A CD     1 
ATOM   1350 O OE1    . GLU A 1 189 ? 15.745 -2.440  3.760   1.00 22.51 ? 183 GLU A OE1    1 
ATOM   1351 O OE2    . GLU A 1 189 ? 17.617 -2.407  2.667   1.00 21.34 ? 183 GLU A OE2    1 
ATOM   1352 N N      . ILE A 1 190 ? 17.774 2.801   3.364   1.00 19.11 ? 184 ILE A N      1 
ATOM   1353 C CA     . ILE A 1 190 ? 19.154 3.266   3.443   1.00 23.85 ? 184 ILE A CA     1 
ATOM   1354 C C      . ILE A 1 190 ? 20.067 2.054   3.628   1.00 19.80 ? 184 ILE A C      1 
ATOM   1355 O O      . ILE A 1 190 ? 19.967 1.331   4.627   1.00 22.11 ? 184 ILE A O      1 
ATOM   1356 C CB     . ILE A 1 190 ? 19.324 4.271   4.594   1.00 20.34 ? 184 ILE A CB     1 
ATOM   1357 C CG1    . ILE A 1 190 ? 18.548 5.563   4.299   1.00 21.21 ? 184 ILE A CG1    1 
ATOM   1358 C CG2    . ILE A 1 190 ? 20.802 4.569   4.807   1.00 22.49 ? 184 ILE A CG2    1 
ATOM   1359 C CD1    . ILE A 1 190 ? 18.926 6.228   2.969   1.00 24.42 ? 184 ILE A CD1    1 
ATOM   1360 N N      . HIS A 1 191 ? 20.960 1.823   2.668   1.00 19.55 ? 185 HIS A N      1 
ATOM   1361 C CA     . HIS A 1 191 ? 21.930 0.734   2.778   1.00 21.27 ? 185 HIS A CA     1 
ATOM   1362 C C      . HIS A 1 191 ? 23.061 1.190   3.688   1.00 20.93 ? 185 HIS A C      1 
ATOM   1363 O O      . HIS A 1 191 ? 23.980 1.890   3.257   1.00 19.93 ? 185 HIS A O      1 
ATOM   1364 C CB     . HIS A 1 191 ? 22.452 0.342   1.398   1.00 19.03 ? 185 HIS A CB     1 
ATOM   1365 C CG     . HIS A 1 191 ? 23.226 -0.942  1.391   1.00 18.18 ? 185 HIS A CG     1 
ATOM   1366 N ND1    . HIS A 1 191 ? 23.776 -1.485  2.536   1.00 22.32 ? 185 HIS A ND1    1 
ATOM   1367 C CD2    . HIS A 1 191 ? 23.528 -1.797  0.385   1.00 20.19 ? 185 HIS A CD2    1 
ATOM   1368 C CE1    . HIS A 1 191 ? 24.390 -2.615  2.231   1.00 23.09 ? 185 HIS A CE1    1 
ATOM   1369 N NE2    . HIS A 1 191 ? 24.253 -2.829  0.933   1.00 21.06 ? 185 HIS A NE2    1 
ATOM   1370 N N      . GLY A 1 192 ? 22.983 0.809   4.965   1.00 19.10 ? 186 GLY A N      1 
ATOM   1371 C CA     . GLY A 1 192 ? 24.035 1.118   5.921   1.00 22.71 ? 186 GLY A CA     1 
ATOM   1372 C C      . GLY A 1 192 ? 24.793 -0.109  6.390   1.00 21.80 ? 186 GLY A C      1 
ATOM   1373 O O      . GLY A 1 192 ? 25.311 -0.136  7.517   1.00 22.92 ? 186 GLY A O      1 
ATOM   1374 N N      . ALA A 1 193 ? 24.892 -1.115  5.524   1.00 21.32 ? 187 ALA A N      1 
ATOM   1375 C CA     . ALA A 1 193 ? 25.387 -2.436  5.880   1.00 21.09 ? 187 ALA A CA     1 
ATOM   1376 C C      . ALA A 1 193 ? 26.581 -2.846  5.007   1.00 23.43 ? 187 ALA A C      1 
ATOM   1377 O O      . ALA A 1 193 ? 27.023 -2.114  4.106   1.00 19.94 ? 187 ALA A O      1 
ATOM   1378 C CB     . ALA A 1 193 ? 24.266 -3.468  5.738   1.00 22.23 ? 187 ALA A CB     1 
ATOM   1379 N N      . HIS A 1 194 ? 27.110 -4.035  5.330   1.00 21.14 ? 188 HIS A N      1 
ATOM   1380 C CA     . HIS A 1 194 ? 28.001 -4.812  4.452   1.00 22.00 ? 188 HIS A CA     1 
ATOM   1381 C C      . HIS A 1 194 ? 29.322 -4.123  4.105   1.00 21.33 ? 188 HIS A C      1 
ATOM   1382 O O      . HIS A 1 194 ? 29.925 -4.428  3.067   1.00 21.63 ? 188 HIS A O      1 
ATOM   1383 C CB     . HIS A 1 194 ? 27.259 -5.276  3.193   1.00 21.36 ? 188 HIS A CB     1 
ATOM   1384 C CG     . HIS A 1 194 ? 26.046 -6.095  3.498   1.00 22.74 ? 188 HIS A CG     1 
ATOM   1385 N ND1    . HIS A 1 194 ? 24.910 -6.073  2.720   1.00 24.59 ? 188 HIS A ND1    1 
ATOM   1386 C CD2    . HIS A 1 194 ? 25.790 -6.957  4.510   1.00 36.38 ? 188 HIS A CD2    1 
ATOM   1387 C CE1    . HIS A 1 194 ? 24.010 -6.892  3.229   1.00 29.85 ? 188 HIS A CE1    1 
ATOM   1388 N NE2    . HIS A 1 194 ? 24.519 -7.443  4.316   1.00 36.71 ? 188 HIS A NE2    1 
ATOM   1389 N N      . GLY A 1 195 ? 29.786 -3.192  4.932   1.00 22.84 ? 189 GLY A N      1 
ATOM   1390 C CA     . GLY A 1 195 ? 31.063 -2.544  4.683   1.00 20.97 ? 189 GLY A CA     1 
ATOM   1391 C C      . GLY A 1 195 ? 31.067 -1.460  3.628   1.00 21.19 ? 189 GLY A C      1 
ATOM   1392 O O      . GLY A 1 195 ? 32.143 -1.066  3.167   1.00 21.24 ? 189 GLY A O      1 
ATOM   1393 N N      . TYR A 1 196 ? 29.903 -0.957  3.227   1.00 19.33 ? 190 TYR A N      1 
ATOM   1394 C CA     . TYR A 1 196 ? 29.841 0.092   2.215   1.00 18.60 ? 190 TYR A CA     1 
ATOM   1395 C C      . TYR A 1 196 ? 30.005 1.454   2.897   1.00 19.40 ? 190 TYR A C      1 
ATOM   1396 O O      . TYR A 1 196 ? 30.492 1.518   4.027   1.00 19.29 ? 190 TYR A O      1 
ATOM   1397 C CB     . TYR A 1 196 ? 28.624 -0.135  1.301   1.00 19.05 ? 190 TYR A CB     1 
ATOM   1398 C CG     . TYR A 1 196 ? 28.759 -1.420  0.510   1.00 19.09 ? 190 TYR A CG     1 
ATOM   1399 C CD1    . TYR A 1 196 ? 29.743 -1.553  -0.477  1.00 23.01 ? 190 TYR A CD1    1 
ATOM   1400 C CD2    . TYR A 1 196 ? 27.930 -2.504  0.752   1.00 20.89 ? 190 TYR A CD2    1 
ATOM   1401 C CE1    . TYR A 1 196 ? 29.879 -2.730  -1.203  1.00 21.81 ? 190 TYR A CE1    1 
ATOM   1402 C CE2    . TYR A 1 196 ? 28.066 -3.682  0.043   1.00 20.74 ? 190 TYR A CE2    1 
ATOM   1403 C CZ     . TYR A 1 196 ? 29.040 -3.789  -0.936  1.00 22.29 ? 190 TYR A CZ     1 
ATOM   1404 O OH     . TYR A 1 196 ? 29.177 -4.955  -1.650  1.00 26.99 ? 190 TYR A OH     1 
ATOM   1405 N N      . LEU A 1 197 ? 29.613 2.550   2.245   1.00 21.26 ? 191 LEU A N      1 
ATOM   1406 C CA     . LEU A 1 197 ? 30.060 3.871   2.703   1.00 19.03 ? 191 LEU A CA     1 
ATOM   1407 C C      . LEU A 1 197 ? 29.611 4.169   4.134   1.00 17.95 ? 191 LEU A C      1 
ATOM   1408 O O      . LEU A 1 197 ? 30.416 4.606   4.967   1.00 20.15 ? 191 LEU A O      1 
ATOM   1409 C CB     . LEU A 1 197 ? 29.574 4.968   1.757   1.00 21.98 ? 191 LEU A CB     1 
ATOM   1410 C CG     . LEU A 1 197 ? 29.983 6.375   2.213   1.00 21.97 ? 191 LEU A CG     1 
ATOM   1411 C CD1    . LEU A 1 197 ? 31.510 6.559   2.190   1.00 22.78 ? 191 LEU A CD1    1 
ATOM   1412 C CD2    . LEU A 1 197 ? 29.300 7.453   1.373   1.00 23.00 ? 191 LEU A CD2    1 
ATOM   1413 N N      . ILE A 1 198 ? 28.321 3.973   4.429   1.00 17.75 ? 192 ILE A N      1 
ATOM   1414 C CA     . ILE A 1 198 ? 27.829 4.244   5.785   1.00 16.29 ? 192 ILE A CA     1 
ATOM   1415 C C      . ILE A 1 198 ? 28.549 3.372   6.806   1.00 18.42 ? 192 ILE A C      1 
ATOM   1416 O O      . ILE A 1 198 ? 28.922 3.835   7.897   1.00 20.90 ? 192 ILE A O      1 
ATOM   1417 C CB     . ILE A 1 198 ? 26.304 4.078   5.854   1.00 18.49 ? 192 ILE A CB     1 
ATOM   1418 C CG1    . ILE A 1 198 ? 25.640 5.233   5.116   1.00 20.57 ? 192 ILE A CG1    1 
ATOM   1419 C CG2    . ILE A 1 198 ? 25.823 4.020   7.329   1.00 21.13 ? 192 ILE A CG2    1 
ATOM   1420 C CD1    . ILE A 1 198 ? 24.193 4.985   4.804   1.00 18.75 ? 192 ILE A CD1    1 
ATOM   1421 N N      . ASP A 1 199 ? 28.771 2.104   6.465   1.00 22.77 ? 193 ASP A N      1 
ATOM   1422 C CA     . ASP A 1 199 ? 29.446 1.193   7.383   1.00 20.91 ? 193 ASP A CA     1 
ATOM   1423 C C      . ASP A 1 199 ? 30.917 1.585   7.568   1.00 20.58 ? 193 ASP A C      1 
ATOM   1424 O O      . ASP A 1 199 ? 31.506 1.301   8.622   1.00 22.76 ? 193 ASP A O      1 
ATOM   1425 C CB     . ASP A 1 199 ? 29.284 -0.237  6.852   1.00 25.28 ? 193 ASP A CB     1 
ATOM   1426 C CG     . ASP A 1 199 ? 29.271 -1.283  7.948   1.00 24.94 ? 193 ASP A CG     1 
ATOM   1427 O OD1    . ASP A 1 199 ? 28.791 -0.971  9.057   1.00 25.39 ? 193 ASP A OD1    1 
ATOM   1428 O OD2    . ASP A 1 199 ? 29.706 -2.432  7.711   1.00 27.36 ? 193 ASP A OD2    1 
ATOM   1429 N N      . GLN A 1 200 ? 31.517 2.267   6.577   1.00 19.32 ? 194 GLN A N      1 
ATOM   1430 C CA     . GLN A 1 200 ? 32.887 2.764   6.714   1.00 18.92 ? 194 GLN A CA     1 
ATOM   1431 C C      . GLN A 1 200 ? 32.995 3.905   7.716   1.00 21.09 ? 194 GLN A C      1 
ATOM   1432 O O      . GLN A 1 200 ? 34.088 4.158   8.242   1.00 22.21 ? 194 GLN A O      1 
ATOM   1433 C CB     . GLN A 1 200 ? 33.421 3.199   5.342   1.00 20.43 ? 194 GLN A CB     1 
ATOM   1434 C CG     . GLN A 1 200 ? 33.573 2.023   4.381   1.00 21.15 ? 194 GLN A CG     1 
ATOM   1435 C CD     . GLN A 1 200 ? 33.522 2.390   2.891   1.00 18.64 ? 194 GLN A CD     1 
ATOM   1436 O OE1    . GLN A 1 200 ? 33.902 3.487   2.466   1.00 21.43 ? 194 GLN A OE1    1 
ATOM   1437 N NE2    . GLN A 1 200 ? 33.035 1.453   2.092   1.00 20.61 ? 194 GLN A NE2    1 
ATOM   1438 N N      . PHE A 1 201 ? 31.891 4.593   7.994   1.00 20.23 ? 195 PHE A N      1 
ATOM   1439 C CA     . PHE A 1 201 ? 31.830 5.525   9.112   1.00 21.50 ? 195 PHE A CA     1 
ATOM   1440 C C      . PHE A 1 201 ? 31.474 4.828   10.426  1.00 20.25 ? 195 PHE A C      1 
ATOM   1441 O O      . PHE A 1 201 ? 32.024 5.182   11.475  1.00 23.80 ? 195 PHE A O      1 
ATOM   1442 C CB     . PHE A 1 201 ? 30.838 6.648   8.796   1.00 19.60 ? 195 PHE A CB     1 
ATOM   1443 C CG     . PHE A 1 201 ? 31.407 7.707   7.897   1.00 21.95 ? 195 PHE A CG     1 
ATOM   1444 C CD1    . PHE A 1 201 ? 31.339 7.555   6.513   1.00 22.48 ? 195 PHE A CD1    1 
ATOM   1445 C CD2    . PHE A 1 201 ? 32.043 8.827   8.415   1.00 23.31 ? 195 PHE A CD2    1 
ATOM   1446 C CE1    . PHE A 1 201 ? 31.865 8.504   5.669   1.00 24.91 ? 195 PHE A CE1    1 
ATOM   1447 C CE2    . PHE A 1 201 ? 32.589 9.789   7.559   1.00 21.48 ? 195 PHE A CE2    1 
ATOM   1448 C CZ     . PHE A 1 201 ? 32.497 9.618   6.182   1.00 20.69 ? 195 PHE A CZ     1 
ATOM   1449 N N      . LEU A 1 202 ? 30.584 3.827   10.396  1.00 19.25 ? 196 LEU A N      1 
ATOM   1450 C CA     . LEU A 1 202 ? 30.115 3.214   11.647  1.00 20.39 ? 196 LEU A CA     1 
ATOM   1451 C C      . LEU A 1 202 ? 31.199 2.392   12.336  1.00 21.46 ? 196 LEU A C      1 
ATOM   1452 O O      . LEU A 1 202 ? 31.309 2.419   13.575  1.00 22.63 ? 196 LEU A O      1 
ATOM   1453 C CB     . LEU A 1 202 ? 28.902 2.319   11.387  1.00 20.30 ? 196 LEU A CB     1 
ATOM   1454 C CG     . LEU A 1 202 ? 27.598 3.006   11.033  1.00 20.99 ? 196 LEU A CG     1 
ATOM   1455 C CD1    . LEU A 1 202 ? 26.600 1.959   10.628  1.00 22.55 ? 196 LEU A CD1    1 
ATOM   1456 C CD2    . LEU A 1 202 ? 27.102 3.804   12.238  1.00 24.20 ? 196 LEU A CD2    1 
ATOM   1457 N N      . LYS A 1 203 ? 31.994 1.642   11.568  1.00 22.83 ? 197 LYS A N      1 
ATOM   1458 C CA     . LYS A 1 203 ? 32.846 0.585   12.112  1.00 20.87 ? 197 LYS A CA     1 
ATOM   1459 C C      . LYS A 1 203 ? 34.204 1.145   12.526  1.00 24.31 ? 197 LYS A C      1 
ATOM   1460 O O      . LYS A 1 203 ? 34.901 1.760   11.711  1.00 26.31 ? 197 LYS A O      1 
ATOM   1461 C CB     . LYS A 1 203 ? 33.018 -0.518  11.065  1.00 24.40 ? 197 LYS A CB     1 
ATOM   1462 C CG     . LYS A 1 203 ? 31.741 -1.272  10.682  1.00 27.46 ? 197 LYS A CG     1 
ATOM   1463 C CD     . LYS A 1 203 ? 31.275 -2.212  11.766  1.00 28.74 ? 197 LYS A CD     1 
ATOM   1464 C CE     . LYS A 1 203 ? 29.966 -2.928  11.400  1.00 27.27 ? 197 LYS A CE     1 
ATOM   1465 N NZ     . LYS A 1 203 ? 30.057 -3.864  10.244  1.00 28.72 ? 197 LYS A NZ     1 
ATOM   1466 N N      . ASP A 1 204 ? 34.589 0.914   13.794  1.00 22.84 ? 198 ASP A N      1 
ATOM   1467 C CA     . ASP A 1 204 ? 35.876 1.424   14.267  1.00 24.66 ? 198 ASP A CA     1 
ATOM   1468 C C      . ASP A 1 204 ? 37.076 0.714   13.652  1.00 26.29 ? 198 ASP A C      1 
ATOM   1469 O O      . ASP A 1 204 ? 38.193 1.234   13.752  1.00 27.65 ? 198 ASP A O      1 
ATOM   1470 C CB     . ASP A 1 204 ? 35.977 1.513   15.804  1.00 22.97 ? 198 ASP A CB     1 
ATOM   1471 C CG     . ASP A 1 204 ? 35.881 0.160   16.506  1.00 27.09 ? 198 ASP A CG     1 
ATOM   1472 O OD1    . ASP A 1 204 ? 35.878 -0.903  15.868  1.00 29.76 ? 198 ASP A OD1    1 
ATOM   1473 O OD2    . ASP A 1 204 ? 35.808 0.162   17.751  1.00 30.14 ? 198 ASP A OD2    1 
ATOM   1474 N N      . GLY A 1 205 ? 36.881 -0.437  13.002  1.00 23.72 ? 199 GLY A N      1 
ATOM   1475 C CA     . GLY A 1 205 ? 37.967 -1.037  12.245  1.00 27.03 ? 199 GLY A CA     1 
ATOM   1476 C C      . GLY A 1 205 ? 38.283 -0.312  10.953  1.00 30.54 ? 199 GLY A C      1 
ATOM   1477 O O      . GLY A 1 205 ? 39.347 -0.543  10.365  1.00 30.21 ? 199 GLY A O      1 
ATOM   1478 N N      . ILE A 1 206 ? 37.382 0.552   10.494  1.00 25.90 ? 200 ILE A N      1 
ATOM   1479 C CA     . ILE A 1 206 ? 37.572 1.333   9.277   1.00 22.31 ? 200 ILE A CA     1 
ATOM   1480 C C      . ILE A 1 206 ? 37.785 2.805   9.593   1.00 24.55 ? 200 ILE A C      1 
ATOM   1481 O O      . ILE A 1 206 ? 38.698 3.443   9.064   1.00 26.80 ? 200 ILE A O      1 
ATOM   1482 C CB     . ILE A 1 206 ? 36.384 1.157   8.305   1.00 23.88 ? 200 ILE A CB     1 
ATOM   1483 C CG1    . ILE A 1 206 ? 36.126 -0.313  7.980   1.00 24.06 ? 200 ILE A CG1    1 
ATOM   1484 C CG2    . ILE A 1 206 ? 36.637 1.969   7.032   1.00 22.03 ? 200 ILE A CG2    1 
ATOM   1485 C CD1    . ILE A 1 206 ? 34.940 -0.517  7.026   1.00 22.21 ? 200 ILE A CD1    1 
ATOM   1486 N N      . ASN A 1 207 ? 36.929 3.366   10.438  1.00 22.30 ? 201 ASN A N      1 
ATOM   1487 C CA     . ASN A 1 207 ? 36.886 4.806   10.669  1.00 22.97 ? 201 ASN A CA     1 
ATOM   1488 C C      . ASN A 1 207 ? 38.038 5.166   11.596  1.00 26.59 ? 201 ASN A C      1 
ATOM   1489 O O      . ASN A 1 207 ? 37.978 4.926   12.807  1.00 29.74 ? 201 ASN A O      1 
ATOM   1490 C CB     . ASN A 1 207 ? 35.533 5.183   11.262  1.00 22.32 ? 201 ASN A CB     1 
ATOM   1491 C CG     . ASN A 1 207 ? 35.355 6.681   11.439  1.00 25.98 ? 201 ASN A CG     1 
ATOM   1492 O OD1    . ASN A 1 207 ? 36.323 7.427   11.548  1.00 24.62 ? 201 ASN A OD1    1 
ATOM   1493 N ND2    . ASN A 1 207 ? 34.100 7.124   11.503  1.00 22.53 ? 201 ASN A ND2    1 
ATOM   1494 N N      . ASP A 1 208 ? 39.094 5.745   11.022  1.00 30.27 ? 202 ASP A N      1 
ATOM   1495 C CA     . ASP A 1 208 ? 40.233 6.251   11.776  1.00 32.89 ? 202 ASP A CA     1 
ATOM   1496 C C      . ASP A 1 208 ? 40.256 7.778   11.822  1.00 32.25 ? 202 ASP A C      1 
ATOM   1497 O O      . ASP A 1 208 ? 41.321 8.383   11.971  1.00 35.35 ? 202 ASP A O      1 
ATOM   1498 C CB     . ASP A 1 208 ? 41.560 5.711   11.237  1.00 28.13 ? 202 ASP A CB     1 
ATOM   1499 C CG     . ASP A 1 208 ? 41.725 5.917   9.730   1.00 36.97 ? 202 ASP A CG     1 
ATOM   1500 O OD1    . ASP A 1 208 ? 40.843 6.537   9.094   1.00 33.08 ? 202 ASP A OD1    1 
ATOM   1501 O OD2    . ASP A 1 208 ? 42.786 5.518   9.187   1.00 37.12 ? 202 ASP A OD2    1 
ATOM   1502 N N      . ARG A 1 209 ? 39.094 8.414   11.702  1.00 27.64 ? 203 ARG A N      1 
ATOM   1503 C CA     . ARG A 1 209 ? 39.037 9.869   11.694  1.00 26.02 ? 203 ARG A CA     1 
ATOM   1504 C C      . ARG A 1 209 ? 39.245 10.432  13.094  1.00 30.20 ? 203 ARG A C      1 
ATOM   1505 O O      . ARG A 1 209 ? 38.872 9.823   14.099  1.00 29.96 ? 203 ARG A O      1 
ATOM   1506 C CB     . ARG A 1 209 ? 37.679 10.339  11.180  1.00 23.76 ? 203 ARG A CB     1 
ATOM   1507 C CG     . ARG A 1 209 ? 37.397 9.925   9.746   1.00 21.23 ? 203 ARG A CG     1 
ATOM   1508 C CD     . ARG A 1 209 ? 35.990 10.335  9.360   1.00 22.71 ? 203 ARG A CD     1 
ATOM   1509 N NE     . ARG A 1 209 ? 35.886 11.764  9.112   1.00 22.86 ? 203 ARG A NE     1 
ATOM   1510 C CZ     . ARG A 1 209 ? 35.977 12.304  7.903   1.00 23.63 ? 203 ARG A CZ     1 
ATOM   1511 N NH1    . ARG A 1 209 ? 36.256 11.566  6.835   1.00 24.57 ? 203 ARG A NH1    1 
ATOM   1512 N NH2    . ARG A 1 209 ? 35.787 13.612  7.758   1.00 24.67 ? 203 ARG A NH2    1 
ATOM   1513 N N      . THR A 1 210 ? 39.829 11.628  13.143  1.00 34.25 ? 204 THR A N      1 
ATOM   1514 C CA     . THR A 1 210 ? 39.988 12.373  14.385  1.00 33.74 ? 204 THR A CA     1 
ATOM   1515 C C      . THR A 1 210 ? 39.150 13.646  14.412  1.00 36.04 ? 204 THR A C      1 
ATOM   1516 O O      . THR A 1 210 ? 39.326 14.472  15.312  1.00 37.51 ? 204 THR A O      1 
ATOM   1517 C CB     . THR A 1 210 ? 41.466 12.691  14.634  1.00 38.21 ? 204 THR A CB     1 
ATOM   1518 O OG1    . THR A 1 210 ? 42.027 13.314  13.471  1.00 42.32 ? 204 THR A OG1    1 
ATOM   1519 C CG2    . THR A 1 210 ? 42.237 11.412  14.947  1.00 39.00 ? 204 THR A CG2    1 
ATOM   1520 N N      . ASP A 1 211 ? 38.247 13.827  13.451  1.00 28.32 ? 205 ASP A N      1 
ATOM   1521 C CA     . ASP A 1 211 ? 37.332 14.959  13.467  1.00 28.49 ? 205 ASP A CA     1 
ATOM   1522 C C      . ASP A 1 211 ? 36.014 14.537  14.120  1.00 28.93 ? 205 ASP A C      1 
ATOM   1523 O O      . ASP A 1 211 ? 35.926 13.485  14.760  1.00 30.01 ? 205 ASP A O      1 
ATOM   1524 C CB     . ASP A 1 211 ? 37.184 15.556  12.058  1.00 27.34 ? 205 ASP A CB     1 
ATOM   1525 C CG     . ASP A 1 211 ? 36.357 14.683  11.118  1.00 33.14 ? 205 ASP A CG     1 
ATOM   1526 O OD1    . ASP A 1 211 ? 36.039 13.522  11.460  1.00 23.97 ? 205 ASP A OD1    1 
ATOM   1527 O OD2    . ASP A 1 211 ? 36.029 15.169  10.013  1.00 28.72 ? 205 ASP A OD2    1 
ATOM   1528 N N      . GLU A 1 212 ? 34.964 15.335  13.939  1.00 24.83 ? 206 GLU A N      1 
ATOM   1529 C CA     . GLU A 1 212 ? 33.703 15.078  14.617  1.00 30.10 ? 206 GLU A CA     1 
ATOM   1530 C C      . GLU A 1 212 ? 32.929 13.897  14.033  1.00 28.46 ? 206 GLU A C      1 
ATOM   1531 O O      . GLU A 1 212 ? 31.852 13.583  14.541  1.00 26.49 ? 206 GLU A O      1 
ATOM   1532 C CB     . GLU A 1 212 ? 32.870 16.361  14.624  1.00 28.16 ? 206 GLU A CB     1 
ATOM   1533 C CG     . GLU A 1 212 ? 32.279 16.715  13.273  1.00 31.54 ? 206 GLU A CG     1 
ATOM   1534 C CD     . GLU A 1 212 ? 33.089 17.780  12.546  1.00 38.20 ? 206 GLU A CD     1 
ATOM   1535 O OE1    . GLU A 1 212 ? 34.328 17.811  12.730  1.00 37.85 ? 206 GLU A OE1    1 
ATOM   1536 O OE2    . GLU A 1 212 ? 32.491 18.589  11.801  1.00 36.60 ? 206 GLU A OE2    1 
ATOM   1537 N N      . TYR A 1 213 ? 33.440 13.232  12.992  1.00 25.94 ? 207 TYR A N      1 
ATOM   1538 C CA     . TYR A 1 213 ? 32.822 12.025  12.457  1.00 23.25 ? 207 TYR A CA     1 
ATOM   1539 C C      . TYR A 1 213 ? 33.565 10.757  12.852  1.00 24.43 ? 207 TYR A C      1 
ATOM   1540 O O      . TYR A 1 213 ? 33.256 9.681   12.325  1.00 25.31 ? 207 TYR A O      1 
ATOM   1541 C CB     . TYR A 1 213 ? 32.709 12.102  10.924  1.00 21.40 ? 207 TYR A CB     1 
ATOM   1542 C CG     . TYR A 1 213 ? 31.636 13.050  10.469  1.00 22.33 ? 207 TYR A CG     1 
ATOM   1543 C CD1    . TYR A 1 213 ? 31.887 14.413  10.377  1.00 23.50 ? 207 TYR A CD1    1 
ATOM   1544 C CD2    . TYR A 1 213 ? 30.357 12.592  10.174  1.00 21.78 ? 207 TYR A CD2    1 
ATOM   1545 C CE1    . TYR A 1 213 ? 30.895 15.291  9.981   1.00 24.94 ? 207 TYR A CE1    1 
ATOM   1546 C CE2    . TYR A 1 213 ? 29.369 13.457  9.776   1.00 24.24 ? 207 TYR A CE2    1 
ATOM   1547 C CZ     . TYR A 1 213 ? 29.637 14.807  9.687   1.00 27.35 ? 207 TYR A CZ     1 
ATOM   1548 O OH     . TYR A 1 213 ? 28.643 15.673  9.283   1.00 30.30 ? 207 TYR A OH     1 
ATOM   1549 N N      . GLY A 1 214 ? 34.553 10.852  13.751  1.00 27.59 ? 208 GLY A N      1 
ATOM   1550 C CA     . GLY A 1 214 ? 35.321 9.691   14.144  1.00 26.69 ? 208 GLY A CA     1 
ATOM   1551 C C      . GLY A 1 214 ? 35.545 9.655   15.643  1.00 28.08 ? 208 GLY A C      1 
ATOM   1552 O O      . GLY A 1 214 ? 35.349 10.645  16.345  1.00 26.66 ? 208 GLY A O      1 
ATOM   1553 N N      . GLY A 1 215 ? 35.977 8.489   16.115  1.00 24.82 ? 209 GLY A N      1 
ATOM   1554 C CA     . GLY A 1 215 ? 36.271 8.293   17.520  1.00 22.88 ? 209 GLY A CA     1 
ATOM   1555 C C      . GLY A 1 215 ? 35.116 7.659   18.265  1.00 25.21 ? 209 GLY A C      1 
ATOM   1556 O O      . GLY A 1 215 ? 34.885 6.446   18.162  1.00 26.63 ? 209 GLY A O      1 
ATOM   1557 N N      . SER A 1 216 ? 34.368 8.481   18.994  1.00 23.94 ? 210 SER A N      1 
ATOM   1558 C CA     . SER A 1 216 ? 33.311 7.988   19.867  1.00 26.37 ? 210 SER A CA     1 
ATOM   1559 C C      . SER A 1 216 ? 32.171 7.384   19.051  1.00 24.68 ? 210 SER A C      1 
ATOM   1560 O O      . SER A 1 216 ? 32.029 7.639   17.850  1.00 22.53 ? 210 SER A O      1 
ATOM   1561 C CB     . SER A 1 216 ? 32.745 9.138   20.704  1.00 24.97 ? 210 SER A CB     1 
ATOM   1562 O OG     . SER A 1 216 ? 32.104 10.095  19.861  1.00 27.37 ? 210 SER A OG     1 
ATOM   1563 N N      . LEU A 1 217 ? 31.354 6.569   19.727  1.00 25.16 ? 211 LEU A N      1 
ATOM   1564 C CA     . LEU A 1 217 ? 30.146 6.019   19.120  1.00 22.85 ? 211 LEU A CA     1 
ATOM   1565 C C      . LEU A 1 217 ? 29.270 7.124   18.545  1.00 27.93 ? 211 LEU A C      1 
ATOM   1566 O O      . LEU A 1 217 ? 28.756 7.003   17.424  1.00 25.11 ? 211 LEU A O      1 
ATOM   1567 C CB     . LEU A 1 217 ? 29.366 5.203   20.165  1.00 24.32 ? 211 LEU A CB     1 
ATOM   1568 C CG     . LEU A 1 217 ? 29.874 3.797   20.513  1.00 23.78 ? 211 LEU A CG     1 
ATOM   1569 C CD1    . LEU A 1 217 ? 29.204 3.308   21.800  1.00 22.62 ? 211 LEU A CD1    1 
ATOM   1570 C CD2    . LEU A 1 217 ? 29.621 2.811   19.388  1.00 26.69 ? 211 LEU A CD2    1 
ATOM   1571 N N      . ALA A 1 218 ? 29.116 8.227   19.282  1.00 22.50 ? 212 ALA A N      1 
ATOM   1572 C CA     . ALA A 1 218 ? 28.270 9.320   18.811  1.00 23.05 ? 212 ALA A CA     1 
ATOM   1573 C C      . ALA A 1 218 ? 28.810 9.905   17.517  1.00 23.94 ? 212 ALA A C      1 
ATOM   1574 O O      . ALA A 1 218 ? 28.048 10.159  16.575  1.00 24.85 ? 212 ALA A O      1 
ATOM   1575 C CB     . ALA A 1 218 ? 28.157 10.410  19.877  1.00 28.33 ? 212 ALA A CB     1 
ATOM   1576 N N      . ASN A 1 219 ? 30.125 10.126  17.457  1.00 24.02 ? 213 ASN A N      1 
ATOM   1577 C CA     . ASN A 1 219 ? 30.730 10.658  16.239  1.00 21.66 ? 213 ASN A CA     1 
ATOM   1578 C C      . ASN A 1 219 ? 30.616 9.670   15.087  1.00 24.93 ? 213 ASN A C      1 
ATOM   1579 O O      . ASN A 1 219 ? 30.351 10.072  13.950  1.00 23.62 ? 213 ASN A O      1 
ATOM   1580 C CB     . ASN A 1 219 ? 32.193 11.019  16.485  1.00 24.03 ? 213 ASN A CB     1 
ATOM   1581 C CG     . ASN A 1 219 ? 32.352 12.275  17.323  1.00 27.86 ? 213 ASN A CG     1 
ATOM   1582 O OD1    . ASN A 1 219 ? 31.368 12.864  17.766  1.00 27.06 ? 213 ASN A OD1    1 
ATOM   1583 N ND2    . ASN A 1 219 ? 33.594 12.698  17.525  1.00 28.85 ? 213 ASN A ND2    1 
ATOM   1584 N N      . ARG A 1 220 ? 30.809 8.373   15.356  1.00 20.65 ? 214 ARG A N      1 
ATOM   1585 C CA     . ARG A 1 220 ? 30.750 7.388   14.277  1.00 23.24 ? 214 ARG A CA     1 
ATOM   1586 C C      . ARG A 1 220 ? 29.334 7.198   13.741  1.00 23.00 ? 214 ARG A C      1 
ATOM   1587 O O      . ARG A 1 220 ? 29.163 6.844   12.563  1.00 21.87 ? 214 ARG A O      1 
ATOM   1588 C CB     . ARG A 1 220 ? 31.384 6.068   14.717  1.00 22.72 ? 214 ARG A CB     1 
ATOM   1589 C CG     . ARG A 1 220 ? 32.870 6.237   15.010  1.00 22.41 ? 214 ARG A CG     1 
ATOM   1590 C CD     . ARG A 1 220 ? 33.656 4.946   15.001  1.00 29.05 ? 214 ARG A CD     1 
ATOM   1591 N NE     . ARG A 1 220 ? 32.870 3.759   15.306  1.00 31.73 ? 214 ARG A NE     1 
ATOM   1592 C CZ     . ARG A 1 220 ? 32.793 3.201   16.505  1.00 25.12 ? 214 ARG A CZ     1 
ATOM   1593 N NH1    . ARG A 1 220 ? 33.340 3.765   17.567  1.00 40.09 ? 214 ARG A NH1    1 
ATOM   1594 N NH2    . ARG A 1 220 ? 32.147 2.049   16.641  1.00 33.90 ? 214 ARG A NH2    1 
ATOM   1595 N N      . CYS A 1 221 ? 28.321 7.442   14.569  1.00 23.89 ? 215 CYS A N      1 
ATOM   1596 C CA     . CYS A 1 221 ? 26.919 7.400   14.165  1.00 23.14 ? 215 CYS A CA     1 
ATOM   1597 C C      . CYS A 1 221 ? 26.428 8.687   13.527  1.00 22.47 ? 215 CYS A C      1 
ATOM   1598 O O      . CYS A 1 221 ? 25.278 8.725   13.079  1.00 23.15 ? 215 CYS A O      1 
ATOM   1599 C CB     . CYS A 1 221 ? 26.020 7.058   15.361  1.00 22.36 ? 215 CYS A CB     1 
ATOM   1600 S SG     . CYS A 1 221 ? 26.234 5.392   15.992  1.00 25.97 ? 215 CYS A SG     1 
ATOM   1601 N N      . LYS A 1 222 ? 27.253 9.734   13.473  1.00 22.16 ? 216 LYS A N      1 
ATOM   1602 C CA     . LYS A 1 222 ? 26.798 11.014  12.936  1.00 24.67 ? 216 LYS A CA     1 
ATOM   1603 C C      . LYS A 1 222 ? 26.384 10.902  11.472  1.00 22.34 ? 216 LYS A C      1 
ATOM   1604 O O      . LYS A 1 222 ? 25.350 11.449  11.072  1.00 22.60 ? 216 LYS A O      1 
ATOM   1605 C CB     . LYS A 1 222 ? 27.905 12.051  13.092  1.00 26.29 ? 216 LYS A CB     1 
ATOM   1606 C CG     . LYS A 1 222 ? 27.470 13.491  12.886  1.00 33.39 ? 216 LYS A CG     1 
ATOM   1607 C CD     . LYS A 1 222 ? 28.471 14.444  13.541  1.00 40.98 ? 216 LYS A CD     1 
ATOM   1608 C CE     . LYS A 1 222 ? 28.563 14.171  15.040  1.00 39.43 ? 216 LYS A CE     1 
ATOM   1609 N NZ     . LYS A 1 222 ? 29.610 14.954  15.773  1.00 37.80 ? 216 LYS A NZ     1 
ATOM   1610 N N      . PHE A 1 223 ? 27.179 10.213  10.653  1.00 23.05 ? 217 PHE A N      1 
ATOM   1611 C CA     . PHE A 1 223 ? 26.867 10.148  9.230   1.00 21.16 ? 217 PHE A CA     1 
ATOM   1612 C C      . PHE A 1 223 ? 25.539 9.442   8.982   1.00 19.58 ? 217 PHE A C      1 
ATOM   1613 O O      . PHE A 1 223 ? 24.675 9.962   8.261   1.00 24.05 ? 217 PHE A O      1 
ATOM   1614 C CB     . PHE A 1 223 ? 28.015 9.486   8.463   1.00 18.21 ? 217 PHE A CB     1 
ATOM   1615 C CG     . PHE A 1 223 ? 27.818 9.483   6.964   1.00 20.59 ? 217 PHE A CG     1 
ATOM   1616 C CD1    . PHE A 1 223 ? 27.630 10.671  6.279   1.00 25.56 ? 217 PHE A CD1    1 
ATOM   1617 C CD2    . PHE A 1 223 ? 27.806 8.291   6.256   1.00 23.96 ? 217 PHE A CD2    1 
ATOM   1618 C CE1    . PHE A 1 223 ? 27.446 10.672  4.889   1.00 27.32 ? 217 PHE A CE1    1 
ATOM   1619 C CE2    . PHE A 1 223 ? 27.630 8.278   4.871   1.00 22.60 ? 217 PHE A CE2    1 
ATOM   1620 C CZ     . PHE A 1 223 ? 27.445 9.472   4.189   1.00 24.57 ? 217 PHE A CZ     1 
ATOM   1621 N N      . ILE A 1 224 ? 25.353 8.244   9.548   1.00 20.74 ? 218 ILE A N      1 
ATOM   1622 C CA     . ILE A 1 224 ? 24.083 7.550   9.324   1.00 19.98 ? 218 ILE A CA     1 
ATOM   1623 C C      . ILE A 1 224 ? 22.914 8.369   9.853   1.00 23.74 ? 218 ILE A C      1 
ATOM   1624 O O      . ILE A 1 224 ? 21.842 8.402   9.239   1.00 20.21 ? 218 ILE A O      1 
ATOM   1625 C CB     . ILE A 1 224 ? 24.078 6.096   9.837   1.00 16.61 ? 218 ILE A CB     1 
ATOM   1626 C CG1    . ILE A 1 224 ? 22.854 5.357   9.260   1.00 21.55 ? 218 ILE A CG1    1 
ATOM   1627 C CG2    . ILE A 1 224 ? 24.116 6.038   11.379  1.00 20.47 ? 218 ILE A CG2    1 
ATOM   1628 C CD1    . ILE A 1 224 ? 22.784 3.847   9.541   1.00 21.40 ? 218 ILE A CD1    1 
ATOM   1629 N N      . THR A 1 225 ? 23.107 9.064   10.979  1.00 22.74 ? 219 THR A N      1 
ATOM   1630 C CA     . THR A 1 225 ? 22.032 9.893   11.525  1.00 21.13 ? 219 THR A CA     1 
ATOM   1631 C C      . THR A 1 225 ? 21.665 11.012  10.559  1.00 23.74 ? 219 THR A C      1 
ATOM   1632 O O      . THR A 1 225 ? 20.479 11.258  10.289  1.00 24.30 ? 219 THR A O      1 
ATOM   1633 C CB     . THR A 1 225 ? 22.456 10.458  12.880  1.00 22.97 ? 219 THR A CB     1 
ATOM   1634 O OG1    . THR A 1 225 ? 22.693 9.370   13.777  1.00 25.84 ? 219 THR A OG1    1 
ATOM   1635 C CG2    . THR A 1 225 ? 21.348 11.340  13.460  1.00 26.38 ? 219 THR A CG2    1 
ATOM   1636 N N      . GLN A 1 226 ? 22.677 11.690  10.013  1.00 23.46 ? 220 GLN A N      1 
ATOM   1637 C CA     . GLN A 1 226 ? 22.429 12.784  9.079   1.00 25.65 ? 220 GLN A CA     1 
ATOM   1638 C C      . GLN A 1 226 ? 21.786 12.286  7.788   1.00 24.99 ? 220 GLN A C      1 
ATOM   1639 O O      . GLN A 1 226 ? 20.911 12.958  7.229   1.00 22.83 ? 220 GLN A O      1 
ATOM   1640 C CB     . GLN A 1 226 ? 23.723 13.555  8.813   1.00 24.81 ? 220 GLN A CB     1 
ATOM   1641 C CG     . GLN A 1 226 ? 24.154 14.415  10.010  1.00 26.93 ? 220 GLN A CG     1 
ATOM   1642 C CD     . GLN A 1 226 ? 25.572 14.944  9.880   1.00 35.17 ? 220 GLN A CD     1 
ATOM   1643 O OE1    . GLN A 1 226 ? 26.261 14.677  8.899   1.00 30.98 ? 220 GLN A OE1    1 
ATOM   1644 N NE2    . GLN A 1 226 ? 26.018 15.688  10.888  1.00 43.03 ? 220 GLN A NE2    1 
ATOM   1645 N N      . VAL A 1 227 ? 22.188 11.104  7.308   1.00 22.09 ? 221 VAL A N      1 
ATOM   1646 C CA     . VAL A 1 227 ? 21.561 10.541  6.110   1.00 22.96 ? 221 VAL A CA     1 
ATOM   1647 C C      . VAL A 1 227 ? 20.087 10.251  6.368   1.00 22.35 ? 221 VAL A C      1 
ATOM   1648 O O      . VAL A 1 227 ? 19.207 10.646  5.593   1.00 22.11 ? 221 VAL A O      1 
ATOM   1649 C CB     . VAL A 1 227 ? 22.317 9.283   5.638   1.00 20.75 ? 221 VAL A CB     1 
ATOM   1650 C CG1    . VAL A 1 227 ? 21.500 8.535   4.573   1.00 23.88 ? 221 VAL A CG1    1 
ATOM   1651 C CG2    . VAL A 1 227 ? 23.688 9.650   5.110   1.00 21.00 ? 221 VAL A CG2    1 
ATOM   1652 N N      . VAL A 1 228 ? 19.795 9.551   7.461   1.00 23.72 ? 222 VAL A N      1 
ATOM   1653 C CA     . VAL A 1 228 ? 18.413 9.195   7.766   1.00 21.57 ? 222 VAL A CA     1 
ATOM   1654 C C      . VAL A 1 228 ? 17.561 10.444  7.983   1.00 24.58 ? 222 VAL A C      1 
ATOM   1655 O O      . VAL A 1 228 ? 16.443 10.543  7.461   1.00 24.47 ? 222 VAL A O      1 
ATOM   1656 C CB     . VAL A 1 228 ? 18.357 8.223   8.960   1.00 23.27 ? 222 VAL A CB     1 
ATOM   1657 C CG1    . VAL A 1 228 ? 16.912 7.970   9.368   1.00 23.30 ? 222 VAL A CG1    1 
ATOM   1658 C CG2    . VAL A 1 228 ? 19.037 6.909   8.583   1.00 23.58 ? 222 VAL A CG2    1 
ATOM   1659 N N      . GLN A 1 229 ? 18.080 11.423  8.738   1.00 24.90 ? 223 GLN A N      1 
ATOM   1660 C CA     . GLN A 1 229 ? 17.336 12.664  8.957   1.00 28.32 ? 223 GLN A CA     1 
ATOM   1661 C C      . GLN A 1 229 ? 17.037 13.375  7.640   1.00 27.33 ? 223 GLN A C      1 
ATOM   1662 O O      . GLN A 1 229 ? 15.930 13.889  7.444   1.00 26.79 ? 223 GLN A O      1 
ATOM   1663 C CB     . GLN A 1 229 ? 18.124 13.602  9.867   1.00 30.21 ? 223 GLN A CB     1 
ATOM   1664 C CG     . GLN A 1 229 ? 17.309 14.724  10.527  1.00 38.52 ? 223 GLN A CG     1 
ATOM   1665 C CD     . GLN A 1 229 ? 15.845 14.368  10.794  1.00 44.31 ? 223 GLN A CD     1 
ATOM   1666 O OE1    . GLN A 1 229 ? 14.961 14.592  9.960   1.00 39.28 ? 223 GLN A OE1    1 
ATOM   1667 N NE2    . GLN A 1 229 ? 15.587 13.815  11.978  1.00 38.72 ? 223 GLN A NE2    1 
ATOM   1668 N N      . ALA A 1 230 ? 18.018 13.433  6.733   1.00 25.39 ? 224 ALA A N      1 
ATOM   1669 C CA     . ALA A 1 230 ? 17.806 14.114  5.457   1.00 25.91 ? 224 ALA A CA     1 
ATOM   1670 C C      . ALA A 1 230 ? 16.674 13.467  4.671   1.00 30.19 ? 224 ALA A C      1 
ATOM   1671 O O      . ALA A 1 230 ? 15.781 14.157  4.166   1.00 27.33 ? 224 ALA A O      1 
ATOM   1672 C CB     . ALA A 1 230 ? 19.104 14.126  4.644   1.00 23.40 ? 224 ALA A CB     1 
ATOM   1673 N N      . VAL A 1 231 ? 16.680 12.135  4.574   1.00 24.07 ? 225 VAL A N      1 
ATOM   1674 C CA     . VAL A 1 231 ? 15.631 11.477  3.803   1.00 23.62 ? 225 VAL A CA     1 
ATOM   1675 C C      . VAL A 1 231 ? 14.292 11.518  4.539   1.00 26.71 ? 225 VAL A C      1 
ATOM   1676 O O      . VAL A 1 231 ? 13.236 11.639  3.908   1.00 26.21 ? 225 VAL A O      1 
ATOM   1677 C CB     . VAL A 1 231 ? 16.051 10.067  3.339   1.00 24.01 ? 225 VAL A CB     1 
ATOM   1678 C CG1    . VAL A 1 231 ? 17.335 10.154  2.507   1.00 23.42 ? 225 VAL A CG1    1 
ATOM   1679 C CG2    . VAL A 1 231 ? 16.255 9.130   4.513   1.00 24.15 ? 225 VAL A CG2    1 
ATOM   1680 N N      . VAL A 1 232 ? 14.308 11.441  5.873   1.00 24.62 ? 226 VAL A N      1 
ATOM   1681 C CA     . VAL A 1 232 ? 13.073 11.568  6.649   1.00 25.66 ? 226 VAL A CA     1 
ATOM   1682 C C      . VAL A 1 232 ? 12.430 12.932  6.425   1.00 27.98 ? 226 VAL A C      1 
ATOM   1683 O O      . VAL A 1 232 ? 11.211 13.038  6.237   1.00 27.43 ? 226 VAL A O      1 
ATOM   1684 C CB     . VAL A 1 232 ? 13.347 11.300  8.141   1.00 25.97 ? 226 VAL A CB     1 
ATOM   1685 C CG1    . VAL A 1 232 ? 12.228 11.904  9.002   1.00 26.86 ? 226 VAL A CG1    1 
ATOM   1686 C CG2    . VAL A 1 232 ? 13.471 9.798   8.397   1.00 25.25 ? 226 VAL A CG2    1 
ATOM   1687 N N      . SER A 1 233 ? 13.232 13.996  6.448   1.00 25.57 ? 227 SER A N      1 
ATOM   1688 C CA     . SER A 1 233 ? 12.683 15.325  6.209   1.00 29.26 ? 227 SER A CA     1 
ATOM   1689 C C      . SER A 1 233 ? 12.131 15.457  4.797   1.00 30.06 ? 227 SER A C      1 
ATOM   1690 O O      . SER A 1 233 ? 11.173 16.206  4.572   1.00 32.34 ? 227 SER A O      1 
ATOM   1691 C CB     . SER A 1 233 ? 13.756 16.381  6.457   1.00 31.54 ? 227 SER A CB     1 
ATOM   1692 O OG     . SER A 1 233 ? 14.041 16.487  7.840   1.00 39.14 ? 227 SER A OG     1 
ATOM   1693 N N      . ALA A 1 234 ? 12.703 14.724  3.840   1.00 28.71 ? 228 ALA A N      1 
ATOM   1694 C CA     . ALA A 1 234 ? 12.329 14.900  2.442   1.00 25.03 ? 228 ALA A CA     1 
ATOM   1695 C C      . ALA A 1 234 ? 11.072 14.120  2.068   1.00 30.03 ? 228 ALA A C      1 
ATOM   1696 O O      . ALA A 1 234 ? 10.251 14.613  1.283   1.00 28.53 ? 228 ALA A O      1 
ATOM   1697 C CB     . ALA A 1 234 ? 13.497 14.498  1.544   1.00 26.80 ? 228 ALA A CB     1 
ATOM   1698 N N      . ILE A 1 235 ? 10.903 12.900  2.585   1.00 24.40 ? 229 ILE A N      1 
ATOM   1699 C CA     . ILE A 1 235 ? 9.818  12.036  2.118   1.00 28.09 ? 229 ILE A CA     1 
ATOM   1700 C C      . ILE A 1 235 ? 8.930  11.518  3.244   1.00 28.21 ? 229 ILE A C      1 
ATOM   1701 O O      . ILE A 1 235 ? 7.906  10.874  2.988   1.00 26.54 ? 229 ILE A O      1 
ATOM   1702 C CB     . ILE A 1 235 ? 10.326 10.884  1.222   1.00 27.26 ? 229 ILE A CB     1 
ATOM   1703 C CG1    . ILE A 1 235 ? 11.182 9.880   2.007   1.00 25.76 ? 229 ILE A CG1    1 
ATOM   1704 C CG2    . ILE A 1 235 ? 11.123 11.427  0.029   1.00 26.81 ? 229 ILE A CG2    1 
ATOM   1705 C CD1    . ILE A 1 235 ? 11.424 8.575   1.238   1.00 24.01 ? 229 ILE A CD1    1 
ATOM   1706 N N      . GLY A 1 236 ? 9.302  11.787  4.491   1.00 27.28 ? 230 GLY A N      1 
ATOM   1707 C CA     . GLY A 1 236 ? 8.509  11.313  5.613   1.00 29.14 ? 230 GLY A CA     1 
ATOM   1708 C C      . GLY A 1 236 ? 9.069  10.044  6.221   1.00 28.17 ? 230 GLY A C      1 
ATOM   1709 O O      . GLY A 1 236 ? 9.471  9.132   5.492   1.00 25.81 ? 230 GLY A O      1 
ATOM   1710 N N      . ALA A 1 237 ? 9.087  9.963   7.556   1.00 25.60 ? 231 ALA A N      1 
ATOM   1711 C CA     . ALA A 1 237 ? 9.728  8.829   8.214   1.00 24.24 ? 231 ALA A CA     1 
ATOM   1712 C C      . ALA A 1 237 ? 9.079  7.505   7.831   1.00 22.38 ? 231 ALA A C      1 
ATOM   1713 O O      . ALA A 1 237 ? 9.767  6.483   7.728   1.00 22.65 ? 231 ALA A O      1 
ATOM   1714 C CB     . ALA A 1 237 ? 9.721  9.016   9.732   1.00 24.24 ? 231 ALA A CB     1 
ATOM   1715 N N      . ASP A 1 238 ? 7.762  7.494   7.606   1.00 22.33 ? 232 ASP A N      1 
ATOM   1716 C CA     . ASP A 1 238 ? 7.119  6.206   7.356   1.00 24.42 ? 232 ASP A CA     1 
ATOM   1717 C C      . ASP A 1 238 ? 7.439  5.639   5.985   1.00 21.78 ? 232 ASP A C      1 
ATOM   1718 O O      . ASP A 1 238 ? 7.030  4.514   5.682   1.00 25.94 ? 232 ASP A O      1 
ATOM   1719 C CB     . ASP A 1 238 ? 5.603  6.250   7.578   1.00 31.37 ? 232 ASP A CB     1 
ATOM   1720 C CG     . ASP A 1 238 ? 4.927  7.406   6.864   1.00 39.17 ? 232 ASP A CG     1 
ATOM   1721 O OD1    . ASP A 1 238 ? 5.550  8.053   6.003   1.00 39.73 ? 232 ASP A OD1    1 
ATOM   1722 O OD2    . ASP A 1 238 ? 3.735  7.649   7.155   1.00 55.50 ? 232 ASP A OD2    1 
ATOM   1723 N N      . ARG A 1 239 ? 8.163  6.387   5.160   1.00 23.89 ? 233 ARG A N      1 
ATOM   1724 C CA     . ARG A 1 239 ? 8.626  5.899   3.874   1.00 21.20 ? 233 ARG A CA     1 
ATOM   1725 C C      . ARG A 1 239 ? 10.124 5.605   3.877   1.00 20.59 ? 233 ARG A C      1 
ATOM   1726 O O      . ARG A 1 239 ? 10.726 5.478   2.804   1.00 22.24 ? 233 ARG A O      1 
ATOM   1727 C CB     . ARG A 1 239 ? 8.269  6.906   2.785   1.00 23.70 ? 233 ARG A CB     1 
ATOM   1728 C CG     . ARG A 1 239 ? 6.786  7.226   2.748   1.00 25.67 ? 233 ARG A CG     1 
ATOM   1729 C CD     . ARG A 1 239 ? 6.396  7.774   1.399   1.00 31.85 ? 233 ARG A CD     1 
ATOM   1730 N NE     . ARG A 1 239 ? 6.747  9.181   1.270   1.00 37.65 ? 233 ARG A NE     1 
ATOM   1731 C CZ     . ARG A 1 239 ? 6.235  10.003  0.362   1.00 40.35 ? 233 ARG A CZ     1 
ATOM   1732 N NH1    . ARG A 1 239 ? 5.362  9.581   -0.540  1.00 48.85 ? 233 ARG A NH1    1 
ATOM   1733 N NH2    . ARG A 1 239 ? 6.620  11.278  0.350   1.00 36.16 ? 233 ARG A NH2    1 
ATOM   1734 N N      . VAL A 1 240 ? 10.733 5.475   5.059   1.00 23.26 ? 234 VAL A N      1 
ATOM   1735 C CA     . VAL A 1 240 ? 12.182 5.299   5.181   1.00 21.51 ? 234 VAL A CA     1 
ATOM   1736 C C      . VAL A 1 240 ? 12.474 4.053   6.012   1.00 20.73 ? 234 VAL A C      1 
ATOM   1737 O O      . VAL A 1 240 ? 12.114 3.990   7.196   1.00 20.87 ? 234 VAL A O      1 
ATOM   1738 C CB     . VAL A 1 240 ? 12.876 6.528   5.794   1.00 17.73 ? 234 VAL A CB     1 
ATOM   1739 C CG1    . VAL A 1 240 ? 14.369 6.240   6.038   1.00 19.51 ? 234 VAL A CG1    1 
ATOM   1740 C CG2    . VAL A 1 240 ? 12.703 7.739   4.904   1.00 23.32 ? 234 VAL A CG2    1 
ATOM   1741 N N      . GLY A 1 241 ? 13.154 3.077   5.404   1.00 23.16 ? 235 GLY A N      1 
ATOM   1742 C CA     . GLY A 1 241 ? 13.708 1.957   6.144   1.00 19.89 ? 235 GLY A CA     1 
ATOM   1743 C C      . GLY A 1 241 ? 15.219 2.094   6.246   1.00 18.67 ? 235 GLY A C      1 
ATOM   1744 O O      . GLY A 1 241 ? 15.831 2.818   5.450   1.00 19.06 ? 235 GLY A O      1 
ATOM   1745 N N      . VAL A 1 242 ? 15.833 1.442   7.238   1.00 19.24 ? 236 VAL A N      1 
ATOM   1746 C CA     . VAL A 1 242 ? 17.279 1.523   7.465   1.00 22.23 ? 236 VAL A CA     1 
ATOM   1747 C C      . VAL A 1 242 ? 17.831 0.107   7.629   1.00 18.90 ? 236 VAL A C      1 
ATOM   1748 O O      . VAL A 1 242 ? 17.311 -0.673  8.432   1.00 20.21 ? 236 VAL A O      1 
ATOM   1749 C CB     . VAL A 1 242 ? 17.619 2.370   8.713   1.00 22.81 ? 236 VAL A CB     1 
ATOM   1750 C CG1    . VAL A 1 242 ? 19.140 2.508   8.875   1.00 24.03 ? 236 VAL A CG1    1 
ATOM   1751 C CG2    . VAL A 1 242 ? 16.981 3.751   8.631   1.00 24.14 ? 236 VAL A CG2    1 
ATOM   1752 N N      . ARG A 1 243 ? 18.903 -0.220  6.899   1.00 20.30 ? 237 ARG A N      1 
ATOM   1753 C CA     . ARG A 1 243 ? 19.513 -1.543  6.985   1.00 17.35 ? 237 ARG A CA     1 
ATOM   1754 C C      . ARG A 1 243 ? 20.934 -1.425  7.516   1.00 19.82 ? 237 ARG A C      1 
ATOM   1755 O O      . ARG A 1 243 ? 21.719 -0.621  7.011   1.00 18.88 ? 237 ARG A O      1 
ATOM   1756 C CB     . ARG A 1 243 ? 19.538 -2.257  5.621   1.00 17.34 ? 237 ARG A CB     1 
ATOM   1757 C CG     . ARG A 1 243 ? 19.883 -3.748  5.741   1.00 20.48 ? 237 ARG A CG     1 
ATOM   1758 C CD     . ARG A 1 243 ? 19.814 -4.496  4.409   1.00 23.14 ? 237 ARG A CD     1 
ATOM   1759 N NE     . ARG A 1 243 ? 19.334 -5.864  4.599   1.00 23.69 ? 237 ARG A NE     1 
ATOM   1760 C CZ     . ARG A 1 243 ? 19.661 -6.884  3.816   1.00 22.86 ? 237 ARG A CZ     1 
ATOM   1761 N NH1    . ARG A 1 243 ? 20.534 -6.743  2.832   1.00 22.98 ? 237 ARG A NH1    1 
ATOM   1762 N NH2    . ARG A 1 243 ? 19.083 -8.066  4.009   1.00 21.50 ? 237 ARG A NH2    1 
ATOM   1763 N N      . VAL A 1 244 ? 21.268 -2.235  8.527   1.00 19.80 ? 238 VAL A N      1 
ATOM   1764 C CA     . VAL A 1 244 ? 22.612 -2.271  9.099   1.00 19.59 ? 238 VAL A CA     1 
ATOM   1765 C C      . VAL A 1 244 ? 23.021 -3.718  9.351   1.00 19.51 ? 238 VAL A C      1 
ATOM   1766 O O      . VAL A 1 244 ? 22.203 -4.636  9.339   1.00 20.59 ? 238 VAL A O      1 
ATOM   1767 C CB     . VAL A 1 244 ? 22.743 -1.457  10.407  1.00 22.03 ? 238 VAL A CB     1 
ATOM   1768 C CG1    . VAL A 1 244 ? 22.585 0.036   10.142  1.00 24.73 ? 238 VAL A CG1    1 
ATOM   1769 C CG2    . VAL A 1 244 ? 21.745 -1.959  11.465  1.00 19.74 ? 238 VAL A CG2    1 
ATOM   1770 N N      . SER A 1 245 ? 24.321 -3.914  9.594   1.00 20.27 ? 239 SER A N      1 
ATOM   1771 C CA     . SER A 1 245 ? 24.881 -5.250  9.804   1.00 20.68 ? 239 SER A CA     1 
ATOM   1772 C C      . SER A 1 245 ? 26.087 -5.143  10.727  1.00 22.04 ? 239 SER A C      1 
ATOM   1773 O O      . SER A 1 245 ? 27.237 -5.314  10.308  1.00 22.32 ? 239 SER A O      1 
ATOM   1774 C CB     . SER A 1 245 ? 25.256 -5.900  8.471   1.00 24.04 ? 239 SER A CB     1 
ATOM   1775 O OG     . SER A 1 245 ? 26.292 -5.190  7.801   1.00 20.79 ? 239 SER A OG     1 
ATOM   1776 N N      . PRO A 1 246 ? 25.852 -4.870  12.009  1.00 21.70 ? 240 PRO A N      1 
ATOM   1777 C CA     . PRO A 1 246 ? 26.987 -4.635  12.918  1.00 22.91 ? 240 PRO A CA     1 
ATOM   1778 C C      . PRO A 1 246 ? 27.956 -5.801  13.017  1.00 20.30 ? 240 PRO A C      1 
ATOM   1779 O O      . PRO A 1 246 ? 29.136 -5.573  13.296  1.00 26.12 ? 240 PRO A O      1 
ATOM   1780 C CB     . PRO A 1 246 ? 26.324 -4.340  14.274  1.00 25.60 ? 240 PRO A CB     1 
ATOM   1781 C CG     . PRO A 1 246 ? 24.860 -4.623  14.104  1.00 24.66 ? 240 PRO A CG     1 
ATOM   1782 C CD     . PRO A 1 246 ? 24.544 -4.637  12.642  1.00 22.22 ? 240 PRO A CD     1 
ATOM   1783 N N      . ALA A 1 247 ? 27.497 -7.038  12.840  1.00 21.31 ? 241 ALA A N      1 
ATOM   1784 C CA     . ALA A 1 247 ? 28.319 -8.218  13.076  1.00 28.70 ? 241 ALA A CA     1 
ATOM   1785 C C      . ALA A 1 247 ? 28.862 -8.847  11.797  1.00 28.27 ? 241 ALA A C      1 
ATOM   1786 O O      . ALA A 1 247 ? 29.587 -9.843  11.873  1.00 32.60 ? 241 ALA A O      1 
ATOM   1787 C CB     . ALA A 1 247 ? 27.532 -9.262  13.869  1.00 29.52 ? 241 ALA A CB     1 
ATOM   1788 N N      . ILE A 1 248 ? 28.537 -8.305  10.631  1.00 23.59 ? 242 ILE A N      1 
ATOM   1789 C CA     . ILE A 1 248 ? 29.106 -8.801  9.382   1.00 23.67 ? 242 ILE A CA     1 
ATOM   1790 C C      . ILE A 1 248 ? 30.394 -8.042  9.110   1.00 25.16 ? 242 ILE A C      1 
ATOM   1791 O O      . ILE A 1 248 ? 30.399 -6.805  9.101   1.00 24.94 ? 242 ILE A O      1 
ATOM   1792 C CB     . ILE A 1 248 ? 28.114 -8.638  8.221   1.00 23.33 ? 242 ILE A CB     1 
ATOM   1793 C CG1    . ILE A 1 248 ? 26.955 -9.620  8.387   1.00 25.27 ? 242 ILE A CG1    1 
ATOM   1794 C CG2    . ILE A 1 248 ? 28.819 -8.870  6.871   1.00 23.39 ? 242 ILE A CG2    1 
ATOM   1795 C CD1    . ILE A 1 248 ? 25.874 -9.463  7.339   1.00 27.09 ? 242 ILE A CD1    1 
ATOM   1796 N N      . ASP A 1 249 ? 31.486 -8.784  8.993   1.00 27.67 ? 243 ASP A N      1 
ATOM   1797 C CA     A ASP A 1 249 ? 32.828 -8.229  8.723   0.48 27.61 ? 243 ASP A CA     1 
ATOM   1798 C CA     B ASP A 1 249 ? 32.804 -8.143  8.692   0.52 27.61 ? 243 ASP A CA     1 
ATOM   1799 C C      . ASP A 1 249 ? 33.323 -8.136  7.217   1.00 30.66 ? 243 ASP A C      1 
ATOM   1800 O O      . ASP A 1 249 ? 34.554 -7.973  6.784   1.00 31.23 ? 243 ASP A O      1 
ATOM   1801 C CB     A ASP A 1 249 ? 33.852 -9.039  9.522   0.48 34.51 ? 243 ASP A CB     1 
ATOM   1802 C CB     B ASP A 1 249 ? 33.890 -8.680  9.629   0.52 34.51 ? 243 ASP A CB     1 
ATOM   1803 C CG     A ASP A 1 249 ? 33.548 -9.068  10.999  0.48 48.44 ? 243 ASP A CG     1 
ATOM   1804 C CG     B ASP A 1 249 ? 33.855 -10.185 9.812   0.52 48.44 ? 243 ASP A CG     1 
ATOM   1805 O OD1    A ASP A 1 249 ? 32.898 -8.119  11.488  0.48 57.82 ? 243 ASP A OD1    1 
ATOM   1806 O OD1    B ASP A 1 249 ? 33.739 -10.895 8.796   0.52 57.82 ? 243 ASP A OD1    1 
ATOM   1807 O OD2    A ASP A 1 249 ? 33.955 -10.042 11.674  0.48 59.26 ? 243 ASP A OD2    1 
ATOM   1808 O OD2    B ASP A 1 249 ? 33.949 -10.631 10.972  0.52 59.26 ? 243 ASP A OD2    1 
ATOM   1809 N N      . HIS A 1 250 ? 32.329 -8.276  6.336   1.00 28.59 ? 244 HIS A N      1 
ATOM   1810 C CA     . HIS A 1 250 ? 32.613 -8.221  4.903   1.00 26.16 ? 244 HIS A CA     1 
ATOM   1811 C C      . HIS A 1 250 ? 33.398 -6.961  4.549   1.00 23.87 ? 244 HIS A C      1 
ATOM   1812 O O      . HIS A 1 250 ? 33.116 -5.874  5.050   1.00 25.37 ? 244 HIS A O      1 
ATOM   1813 C CB     . HIS A 1 250 ? 31.254 -8.211  4.191   1.00 28.91 ? 244 HIS A CB     1 
ATOM   1814 C CG     . HIS A 1 250 ? 31.326 -8.216  2.695   1.00 33.57 ? 244 HIS A CG     1 
ATOM   1815 N ND1    . HIS A 1 250 ? 30.627 -7.306  1.922   1.00 33.87 ? 244 HIS A ND1    1 
ATOM   1816 C CD2    . HIS A 1 250 ? 31.971 -9.043  1.836   1.00 35.19 ? 244 HIS A CD2    1 
ATOM   1817 C CE1    . HIS A 1 250 ? 30.829 -7.527  0.630   1.00 33.81 ? 244 HIS A CE1    1 
ATOM   1818 N N      . LEU A 1 251 ? 34.384 -7.107  3.648   1.00 26.04 ? 245 LEU A N      1 
ATOM   1819 C CA     . LEU A 1 251 ? 35.172 -5.970  3.153   1.00 24.82 ? 245 LEU A CA     1 
ATOM   1820 C C      . LEU A 1 251 ? 35.916 -5.245  4.271   1.00 28.28 ? 245 LEU A C      1 
ATOM   1821 O O      . LEU A 1 251 ? 36.017 -4.015  4.276   1.00 26.59 ? 245 LEU A O      1 
ATOM   1822 C CB     . LEU A 1 251 ? 34.326 -4.990  2.335   1.00 24.22 ? 245 LEU A CB     1 
ATOM   1823 C CG     . LEU A 1 251 ? 33.516 -5.560  1.171   1.00 26.04 ? 245 LEU A CG     1 
ATOM   1824 C CD1    . LEU A 1 251 ? 32.640 -4.466  0.582   1.00 27.36 ? 245 LEU A CD1    1 
ATOM   1825 C CD2    . LEU A 1 251 ? 34.416 -6.183  0.099   1.00 25.52 ? 245 LEU A CD2    1 
ATOM   1826 N N      . ASP A 1 252 ? 36.436 -6.010  5.234   1.00 23.66 ? 246 ASP A N      1 
ATOM   1827 C CA     . ASP A 1 252 ? 37.263 -5.448  6.308   1.00 32.43 ? 246 ASP A CA     1 
ATOM   1828 C C      . ASP A 1 252 ? 36.474 -4.471  7.164   1.00 31.31 ? 246 ASP A C      1 
ATOM   1829 O O      . ASP A 1 252 ? 36.971 -3.406  7.531   1.00 41.73 ? 246 ASP A O      1 
ATOM   1830 C CB     . ASP A 1 252 ? 38.495 -4.739  5.757   1.00 38.40 ? 246 ASP A CB     1 
ATOM   1831 C CG     . ASP A 1 252 ? 39.598 -5.676  5.418   1.00 37.47 ? 246 ASP A CG     1 
ATOM   1832 O OD1    . ASP A 1 252 ? 39.389 -6.902  5.509   1.00 47.69 ? 246 ASP A OD1    1 
ATOM   1833 O OD2    . ASP A 1 252 ? 40.670 -5.169  5.050   1.00 40.60 ? 246 ASP A OD2    1 
ATOM   1834 N N      . ALA A 1 253 ? 35.235 -4.821  7.478   1.00 26.91 ? 247 ALA A N      1 
ATOM   1835 C CA     . ALA A 1 253 ? 34.332 -3.920  8.183   1.00 24.28 ? 247 ALA A CA     1 
ATOM   1836 C C      . ALA A 1 253 ? 33.980 -4.512  9.543   1.00 24.14 ? 247 ALA A C      1 
ATOM   1837 O O      . ALA A 1 253 ? 32.874 -4.983  9.785   1.00 29.58 ? 247 ALA A O      1 
ATOM   1838 C CB     . ALA A 1 253 ? 33.098 -3.663  7.336   1.00 27.89 ? 247 ALA A CB     1 
ATOM   1839 N N      . MET A 1 254 ? 34.956 -4.490  10.436  1.00 22.40 ? 248 MET A N      1 
ATOM   1840 C CA     . MET A 1 254 ? 34.798 -5.034  11.775  1.00 23.49 ? 248 MET A CA     1 
ATOM   1841 C C      . MET A 1 254 ? 34.673 -3.901  12.780  1.00 23.12 ? 248 MET A C      1 
ATOM   1842 O O      . MET A 1 254 ? 35.265 -2.833  12.618  1.00 25.19 ? 248 MET A O      1 
ATOM   1843 C CB     . MET A 1 254 ? 36.017 -5.899  12.118  1.00 30.92 ? 248 MET A CB     1 
ATOM   1844 C CG     . MET A 1 254 ? 35.881 -6.729  13.381  1.00 42.28 ? 248 MET A CG     1 
ATOM   1845 S SD     . MET A 1 254 ? 37.391 -7.667  13.683  1.00 78.86 ? 248 MET A SD     1 
ATOM   1846 C CE     . MET A 1 254 ? 37.937 -7.981  12.001  1.00 50.96 ? 248 MET A CE     1 
ATOM   1847 N N      . ASP A 1 255 ? 33.881 -4.139  13.817  1.00 28.61 ? 249 ASP A N      1 
ATOM   1848 C CA     . ASP A 1 255 ? 33.852 -3.277  14.987  1.00 25.15 ? 249 ASP A CA     1 
ATOM   1849 C C      . ASP A 1 255 ? 34.293 -4.078  16.196  1.00 24.31 ? 249 ASP A C      1 
ATOM   1850 O O      . ASP A 1 255 ? 33.977 -5.267  16.314  1.00 26.81 ? 249 ASP A O      1 
ATOM   1851 C CB     . ASP A 1 255 ? 32.462 -2.700  15.255  1.00 26.49 ? 249 ASP A CB     1 
ATOM   1852 C CG     . ASP A 1 255 ? 32.504 -1.504  16.193  1.00 27.69 ? 249 ASP A CG     1 
ATOM   1853 O OD1    . ASP A 1 255 ? 32.698 -0.373  15.707  1.00 24.97 ? 249 ASP A OD1    1 
ATOM   1854 O OD2    . ASP A 1 255 ? 32.359 -1.691  17.426  1.00 29.36 ? 249 ASP A OD2    1 
ATOM   1855 N N      . SER A 1 256 ? 35.028 -3.409  17.085  1.00 29.26 ? 250 SER A N      1 
ATOM   1856 C CA     . SER A 1 256 ? 35.516 -4.039  18.304  1.00 26.96 ? 250 SER A CA     1 
ATOM   1857 C C      . SER A 1 256 ? 34.377 -4.468  19.216  1.00 31.06 ? 250 SER A C      1 
ATOM   1858 O O      . SER A 1 256 ? 34.560 -5.366  20.046  1.00 27.46 ? 250 SER A O      1 
ATOM   1859 C CB     . SER A 1 256 ? 36.415 -3.052  19.041  1.00 28.51 ? 250 SER A CB     1 
ATOM   1860 O OG     . SER A 1 256 ? 35.702 -1.864  19.352  1.00 30.15 ? 250 SER A OG     1 
ATOM   1861 N N      . ASN A 1 257 ? 33.205 -3.858  19.075  1.00 24.31 ? 251 ASN A N      1 
ATOM   1862 C CA     . ASN A 1 257 ? 32.051 -4.185  19.915  1.00 26.62 ? 251 ASN A CA     1 
ATOM   1863 C C      . ASN A 1 257 ? 30.787 -4.071  19.080  1.00 26.86 ? 251 ASN A C      1 
ATOM   1864 O O      . ASN A 1 257 ? 30.061 -3.071  19.147  1.00 22.98 ? 251 ASN A O      1 
ATOM   1865 C CB     . ASN A 1 257 ? 32.020 -3.304  21.164  1.00 24.60 ? 251 ASN A CB     1 
ATOM   1866 C CG     . ASN A 1 257 ? 31.048 -3.804  22.224  1.00 29.91 ? 251 ASN A CG     1 
ATOM   1867 O OD1    . ASN A 1 257 ? 30.165 -4.631  21.957  1.00 25.78 ? 251 ASN A OD1    1 
ATOM   1868 N ND2    . ASN A 1 257 ? 31.264 -3.362  23.460  1.00 30.94 ? 251 ASN A ND2    1 
ATOM   1869 N N      . PRO A 1 258 ? 30.484 -5.102  18.278  1.00 22.10 ? 252 PRO A N      1 
ATOM   1870 C CA     . PRO A 1 258 ? 29.305 -5.021  17.388  1.00 25.45 ? 252 PRO A CA     1 
ATOM   1871 C C      . PRO A 1 258 ? 27.995 -4.766  18.103  1.00 23.68 ? 252 PRO A C      1 
ATOM   1872 O O      . PRO A 1 258 ? 27.146 -4.024  17.585  1.00 22.46 ? 252 PRO A O      1 
ATOM   1873 C CB     . PRO A 1 258 ? 29.301 -6.386  16.680  1.00 27.83 ? 252 PRO A CB     1 
ATOM   1874 C CG     . PRO A 1 258 ? 30.719 -6.823  16.694  1.00 26.88 ? 252 PRO A CG     1 
ATOM   1875 C CD     . PRO A 1 258 ? 31.293 -6.306  18.010  1.00 21.37 ? 252 PRO A CD     1 
ATOM   1876 N N      . LEU A 1 259 ? 27.782 -5.391  19.263  1.00 23.80 ? 253 LEU A N      1 
ATOM   1877 C CA     . LEU A 1 259 ? 26.525 -5.185  19.973  1.00 24.52 ? 253 LEU A CA     1 
ATOM   1878 C C      . LEU A 1 259 ? 26.378 -3.734  20.424  1.00 22.65 ? 253 LEU A C      1 
ATOM   1879 O O      . LEU A 1 259 ? 25.308 -3.133  20.252  1.00 22.53 ? 253 LEU A O      1 
ATOM   1880 C CB     . LEU A 1 259 ? 26.414 -6.153  21.154  1.00 26.62 ? 253 LEU A CB     1 
ATOM   1881 C CG     . LEU A 1 259 ? 25.079 -6.076  21.895  1.00 30.10 ? 253 LEU A CG     1 
ATOM   1882 C CD1    . LEU A 1 259 ? 23.938 -6.167  20.889  1.00 33.92 ? 253 LEU A CD1    1 
ATOM   1883 C CD2    . LEU A 1 259 ? 24.985 -7.186  22.924  1.00 31.30 ? 253 LEU A CD2    1 
ATOM   1884 N N      . SER A 1 260 ? 27.446 -3.157  20.991  1.00 20.45 ? 254 SER A N      1 
ATOM   1885 C CA     . SER A 1 260 ? 27.437 -1.747  21.370  1.00 24.77 ? 254 SER A CA     1 
ATOM   1886 C C      . SER A 1 260 ? 27.138 -0.853  20.184  1.00 22.00 ? 254 SER A C      1 
ATOM   1887 O O      . SER A 1 260 ? 26.344 0.096   20.284  1.00 22.15 ? 254 SER A O      1 
ATOM   1888 C CB     . SER A 1 260 ? 28.789 -1.358  21.961  1.00 27.15 ? 254 SER A CB     1 
ATOM   1889 O OG     . SER A 1 260 ? 28.699 -0.098  22.576  1.00 25.28 ? 254 SER A OG     1 
ATOM   1890 N N      . LEU A 1 261 ? 27.795 -1.128  19.057  1.00 18.40 ? 255 LEU A N      1 
ATOM   1891 C CA     . LEU A 1 261 ? 27.580 -0.316  17.869  1.00 22.52 ? 255 LEU A CA     1 
ATOM   1892 C C      . LEU A 1 261 ? 26.130 -0.402  17.419  1.00 21.76 ? 255 LEU A C      1 
ATOM   1893 O O      . LEU A 1 261 ? 25.492 0.624   17.142  1.00 19.77 ? 255 LEU A O      1 
ATOM   1894 C CB     . LEU A 1 261 ? 28.521 -0.781  16.762  1.00 21.00 ? 255 LEU A CB     1 
ATOM   1895 C CG     . LEU A 1 261 ? 28.308 -0.076  15.425  1.00 19.53 ? 255 LEU A CG     1 
ATOM   1896 C CD1    . LEU A 1 261 ? 28.487 1.429   15.585  1.00 22.37 ? 255 LEU A CD1    1 
ATOM   1897 C CD2    . LEU A 1 261 ? 29.285 -0.654  14.398  1.00 21.54 ? 255 LEU A CD2    1 
ATOM   1898 N N      . GLY A 1 262 ? 25.587 -1.625  17.369  1.00 17.85 ? 256 GLY A N      1 
ATOM   1899 C CA     . GLY A 1 262 ? 24.203 -1.802  16.971  1.00 18.11 ? 256 GLY A CA     1 
ATOM   1900 C C      . GLY A 1 262 ? 23.241 -1.059  17.874  1.00 21.76 ? 256 GLY A C      1 
ATOM   1901 O O      . GLY A 1 262 ? 22.302 -0.409  17.409  1.00 20.67 ? 256 GLY A O      1 
ATOM   1902 N N      . LEU A 1 263 ? 23.477 -1.127  19.180  1.00 19.77 ? 257 LEU A N      1 
ATOM   1903 C CA     . LEU A 1 263 ? 22.605 -0.417  20.105  1.00 19.30 ? 257 LEU A CA     1 
ATOM   1904 C C      . LEU A 1 263 ? 22.746 1.096   19.954  1.00 21.05 ? 257 LEU A C      1 
ATOM   1905 O O      . LEU A 1 263 ? 21.761 1.832   20.119  1.00 21.29 ? 257 LEU A O      1 
ATOM   1906 C CB     . LEU A 1 263 ? 22.911 -0.867  21.534  1.00 22.62 ? 257 LEU A CB     1 
ATOM   1907 C CG     . LEU A 1 263 ? 22.430 -2.285  21.873  1.00 20.59 ? 257 LEU A CG     1 
ATOM   1908 C CD1    . LEU A 1 263 ? 22.966 -2.770  23.235  1.00 22.91 ? 257 LEU A CD1    1 
ATOM   1909 C CD2    . LEU A 1 263 ? 20.902 -2.368  21.859  1.00 26.40 ? 257 LEU A CD2    1 
ATOM   1910 N N      . ALA A 1 264 ? 23.954 1.575   19.644  1.00 21.78 ? 258 ALA A N      1 
ATOM   1911 C CA     . ALA A 1 264 ? 24.161 3.006   19.441  1.00 20.64 ? 258 ALA A CA     1 
ATOM   1912 C C      . ALA A 1 264 ? 23.389 3.505   18.227  1.00 22.41 ? 258 ALA A C      1 
ATOM   1913 O O      . ALA A 1 264 ? 22.797 4.591   18.259  1.00 22.30 ? 258 ALA A O      1 
ATOM   1914 C CB     . ALA A 1 264 ? 25.656 3.309   19.308  1.00 22.00 ? 258 ALA A CB     1 
ATOM   1915 N N      . VAL A 1 265 ? 23.383 2.728   17.143  1.00 21.36 ? 259 VAL A N      1 
ATOM   1916 C CA     . VAL A 1 265 ? 22.593 3.107   15.976  1.00 21.50 ? 259 VAL A CA     1 
ATOM   1917 C C      . VAL A 1 265 ? 21.112 3.129   16.321  1.00 20.95 ? 259 VAL A C      1 
ATOM   1918 O O      . VAL A 1 265 ? 20.389 4.069   15.966  1.00 21.86 ? 259 VAL A O      1 
ATOM   1919 C CB     . VAL A 1 265 ? 22.902 2.175   14.788  1.00 19.62 ? 259 VAL A CB     1 
ATOM   1920 C CG1    . VAL A 1 265 ? 21.953 2.469   13.624  1.00 22.26 ? 259 VAL A CG1    1 
ATOM   1921 C CG2    . VAL A 1 265 ? 24.375 2.311   14.357  1.00 23.08 ? 259 VAL A CG2    1 
ATOM   1922 N N      . VAL A 1 266 ? 20.639 2.105   17.037  1.00 20.56 ? 260 VAL A N      1 
ATOM   1923 C CA     . VAL A 1 266 ? 19.222 2.041   17.393  1.00 20.56 ? 260 VAL A CA     1 
ATOM   1924 C C      . VAL A 1 266 ? 18.826 3.265   18.216  1.00 21.98 ? 260 VAL A C      1 
ATOM   1925 O O      . VAL A 1 266 ? 17.763 3.863   17.996  1.00 21.87 ? 260 VAL A O      1 
ATOM   1926 C CB     . VAL A 1 266 ? 18.912 0.717   18.119  1.00 18.63 ? 260 VAL A CB     1 
ATOM   1927 C CG1    . VAL A 1 266 ? 17.569 0.801   18.862  1.00 23.89 ? 260 VAL A CG1    1 
ATOM   1928 C CG2    . VAL A 1 266 ? 18.934 -0.463  17.144  1.00 22.22 ? 260 VAL A CG2    1 
ATOM   1929 N N      . GLU A 1 267 ? 19.680 3.651   19.173  1.00 23.64 ? 261 GLU A N      1 
ATOM   1930 C CA     . GLU A 1 267 ? 19.488 4.873   19.958  1.00 26.60 ? 261 GLU A CA     1 
ATOM   1931 C C      . GLU A 1 267 ? 19.206 6.081   19.077  1.00 27.69 ? 261 GLU A C      1 
ATOM   1932 O O      . GLU A 1 267 ? 18.257 6.833   19.325  1.00 24.41 ? 261 GLU A O      1 
ATOM   1933 C CB     . GLU A 1 267 ? 20.741 5.140   20.795  1.00 28.16 ? 261 GLU A CB     1 
ATOM   1934 C CG     . GLU A 1 267 ? 20.609 6.241   21.829  1.00 30.41 ? 261 GLU A CG     1 
ATOM   1935 C CD     . GLU A 1 267 ? 21.934 6.512   22.525  1.00 36.31 ? 261 GLU A CD     1 
ATOM   1936 O OE1    . GLU A 1 267 ? 22.543 5.549   23.032  1.00 32.64 ? 261 GLU A OE1    1 
ATOM   1937 O OE2    . GLU A 1 267 ? 22.367 7.689   22.562  1.00 31.54 ? 261 GLU A OE2    1 
ATOM   1938 N N      . ARG A 1 268 ? 20.038 6.299   18.052  1.00 24.25 ? 262 ARG A N      1 
ATOM   1939 C CA     . ARG A 1 268 ? 19.851 7.471   17.203  1.00 24.30 ? 262 ARG A CA     1 
ATOM   1940 C C      . ARG A 1 268 ? 18.577 7.369   16.379  1.00 24.94 ? 262 ARG A C      1 
ATOM   1941 O O      . ARG A 1 268 ? 17.914 8.386   16.146  1.00 24.86 ? 262 ARG A O      1 
ATOM   1942 C CB     . ARG A 1 268 ? 21.067 7.691   16.296  1.00 24.22 ? 262 ARG A CB     1 
ATOM   1943 C CG     . ARG A 1 268 ? 22.163 8.531   16.952  1.00 31.80 ? 262 ARG A CG     1 
ATOM   1944 C CD     . ARG A 1 268 ? 23.060 7.646   17.777  1.00 33.25 ? 262 ARG A CD     1 
ATOM   1945 N NE     . ARG A 1 268 ? 24.030 8.378   18.580  1.00 33.11 ? 262 ARG A NE     1 
ATOM   1946 C CZ     . ARG A 1 268 ? 24.668 7.848   19.614  1.00 31.33 ? 262 ARG A CZ     1 
ATOM   1947 N NH1    . ARG A 1 268 ? 24.498 6.580   19.951  1.00 27.34 ? 262 ARG A NH1    1 
ATOM   1948 N NH2    . ARG A 1 268 ? 25.494 8.608   20.326  1.00 29.15 ? 262 ARG A NH2    1 
ATOM   1949 N N      . LEU A 1 269 ? 18.210 6.157   15.946  1.00 22.76 ? 263 LEU A N      1 
ATOM   1950 C CA     . LEU A 1 269 ? 16.972 5.989   15.195  1.00 21.98 ? 263 LEU A CA     1 
ATOM   1951 C C      . LEU A 1 269 ? 15.758 6.257   16.073  1.00 22.04 ? 263 LEU A C      1 
ATOM   1952 O O      . LEU A 1 269 ? 14.792 6.894   15.631  1.00 23.50 ? 263 LEU A O      1 
ATOM   1953 C CB     . LEU A 1 269 ? 16.899 4.585   14.596  1.00 21.72 ? 263 LEU A CB     1 
ATOM   1954 C CG     . LEU A 1 269 ? 17.997 4.240   13.581  1.00 20.28 ? 263 LEU A CG     1 
ATOM   1955 C CD1    . LEU A 1 269 ? 17.822 2.833   13.066  1.00 24.00 ? 263 LEU A CD1    1 
ATOM   1956 C CD2    . LEU A 1 269 ? 18.054 5.244   12.430  1.00 23.06 ? 263 LEU A CD2    1 
ATOM   1957 N N      . ASN A 1 270 ? 15.782 5.764   17.311  1.00 21.46 ? 264 ASN A N      1 
ATOM   1958 C CA     . ASN A 1 270 ? 14.692 6.052   18.239  1.00 26.16 ? 264 ASN A CA     1 
ATOM   1959 C C      . ASN A 1 270 ? 14.554 7.557   18.455  1.00 21.71 ? 264 ASN A C      1 
ATOM   1960 O O      . ASN A 1 270 ? 13.435 8.082   18.505  1.00 24.19 ? 264 ASN A O      1 
ATOM   1961 C CB     . ASN A 1 270 ? 14.943 5.336   19.567  1.00 24.39 ? 264 ASN A CB     1 
ATOM   1962 C CG     . ASN A 1 270 ? 14.581 3.843   19.534  1.00 22.82 ? 264 ASN A CG     1 
ATOM   1963 O OD1    . ASN A 1 270 ? 13.957 3.344   18.594  1.00 23.98 ? 264 ASN A OD1    1 
ATOM   1964 N ND2    . ASN A 1 270 ? 14.957 3.130   20.599  1.00 25.50 ? 264 ASN A ND2    1 
ATOM   1965 N N      . LYS A 1 271 ? 15.683 8.271   18.530  1.00 23.76 ? 265 LYS A N      1 
ATOM   1966 C CA     . LYS A 1 271 ? 15.659 9.720   18.729  1.00 25.28 ? 265 LYS A CA     1 
ATOM   1967 C C      . LYS A 1 271 ? 15.144 10.451  17.492  1.00 30.36 ? 265 LYS A C      1 
ATOM   1968 O O      . LYS A 1 271 ? 14.401 11.433  17.611  1.00 26.36 ? 265 LYS A O      1 
ATOM   1969 C CB     . LYS A 1 271 ? 17.051 10.230  19.108  1.00 25.47 ? 265 LYS A CB     1 
ATOM   1970 N N      . ILE A 1 272 ? 15.543 10.006  16.297  1.00 24.29 ? 266 ILE A N      1 
ATOM   1971 C CA     . ILE A 1 272 ? 14.989 10.602  15.085  1.00 26.19 ? 266 ILE A CA     1 
ATOM   1972 C C      . ILE A 1 272 ? 13.474 10.479  15.081  1.00 24.22 ? 266 ILE A C      1 
ATOM   1973 O O      . ILE A 1 272 ? 12.761 11.417  14.705  1.00 28.60 ? 266 ILE A O      1 
ATOM   1974 C CB     . ILE A 1 272 ? 15.618 9.979   13.828  1.00 23.68 ? 266 ILE A CB     1 
ATOM   1975 C CG1    . ILE A 1 272 ? 17.076 10.421  13.719  1.00 25.51 ? 266 ILE A CG1    1 
ATOM   1976 C CG2    . ILE A 1 272 ? 14.817 10.378  12.583  1.00 26.05 ? 266 ILE A CG2    1 
ATOM   1977 C CD1    . ILE A 1 272 ? 17.869 9.725   12.612  1.00 23.72 ? 266 ILE A CD1    1 
ATOM   1978 N N      . GLN A 1 273 ? 12.960 9.324   15.512  1.00 24.00 ? 267 GLN A N      1 
ATOM   1979 C CA     . GLN A 1 273 ? 11.517 9.111   15.522  1.00 24.99 ? 267 GLN A CA     1 
ATOM   1980 C C      . GLN A 1 273 ? 10.820 10.049  16.501  1.00 32.20 ? 267 GLN A C      1 
ATOM   1981 O O      . GLN A 1 273 ? 9.763  10.606  16.182  1.00 32.09 ? 267 GLN A O      1 
ATOM   1982 C CB     . GLN A 1 273 ? 11.202 7.646   15.825  1.00 27.75 ? 267 GLN A CB     1 
ATOM   1983 C CG     . GLN A 1 273 ? 11.603 6.729   14.680  1.00 25.98 ? 267 GLN A CG     1 
ATOM   1984 C CD     . GLN A 1 273 ? 11.321 5.259   14.929  1.00 26.75 ? 267 GLN A CD     1 
ATOM   1985 O OE1    . GLN A 1 273 ? 11.269 4.463   13.985  1.00 27.05 ? 267 GLN A OE1    1 
ATOM   1986 N NE2    . GLN A 1 273 ? 11.183 4.878   16.197  1.00 24.33 ? 267 GLN A NE2    1 
ATOM   1987 N N      . LEU A 1 274 ? 11.401 10.247  17.686  1.00 28.62 ? 268 LEU A N      1 
ATOM   1988 C CA     . LEU A 1 274 ? 10.799 11.154  18.662  1.00 33.31 ? 268 LEU A CA     1 
ATOM   1989 C C      . LEU A 1 274 ? 10.770 12.585  18.141  1.00 38.73 ? 268 LEU A C      1 
ATOM   1990 O O      . LEU A 1 274 ? 9.753  13.281  18.253  1.00 39.67 ? 268 LEU A O      1 
ATOM   1991 C CB     . LEU A 1 274 ? 11.572 11.089  19.977  1.00 33.34 ? 268 LEU A CB     1 
ATOM   1992 C CG     . LEU A 1 274 ? 11.554 9.789   20.777  1.00 41.74 ? 268 LEU A CG     1 
ATOM   1993 C CD1    . LEU A 1 274 ? 12.008 10.077  22.193  1.00 48.88 ? 268 LEU A CD1    1 
ATOM   1994 C CD2    . LEU A 1 274 ? 10.160 9.184   20.786  1.00 44.62 ? 268 LEU A CD2    1 
ATOM   1995 N N      . HIS A 1 275 ? 11.883 13.044  17.570  1.00 35.68 ? 269 HIS A N      1 
ATOM   1996 C CA     . HIS A 1 275 ? 11.976 14.431  17.123  1.00 40.10 ? 269 HIS A CA     1 
ATOM   1997 C C      . HIS A 1 275 ? 11.093 14.702  15.909  1.00 42.61 ? 269 HIS A C      1 
ATOM   1998 O O      . HIS A 1 275 ? 10.618 15.828  15.730  1.00 42.53 ? 269 HIS A O      1 
ATOM   1999 C CB     . HIS A 1 275 ? 13.433 14.789  16.821  1.00 39.05 ? 269 HIS A CB     1 
ATOM   2000 N N      . SER A 1 276 ? 10.873 13.701  15.063  1.00 38.91 ? 270 SER A N      1 
ATOM   2001 C CA     . SER A 1 276 ? 10.016 13.864  13.898  1.00 38.98 ? 270 SER A CA     1 
ATOM   2002 C C      . SER A 1 276 ? 8.547  13.597  14.200  1.00 43.38 ? 270 SER A C      1 
ATOM   2003 O O      . SER A 1 276 ? 7.688  13.946  13.382  1.00 42.79 ? 270 SER A O      1 
ATOM   2004 C CB     . SER A 1 276 ? 10.477 12.929  12.782  1.00 42.37 ? 270 SER A CB     1 
ATOM   2005 O OG     . SER A 1 276 ? 9.993  11.620  13.020  1.00 43.94 ? 270 SER A OG     1 
ATOM   2006 N N      . GLY A 1 277 ? 8.238  12.991  15.345  1.00 38.05 ? 271 GLY A N      1 
ATOM   2007 C CA     . GLY A 1 277 ? 6.868  12.631  15.648  1.00 41.49 ? 271 GLY A CA     1 
ATOM   2008 C C      . GLY A 1 277 ? 6.302  11.526  14.787  1.00 45.87 ? 271 GLY A C      1 
ATOM   2009 O O      . GLY A 1 277 ? 5.082  11.430  14.639  1.00 37.37 ? 271 GLY A O      1 
ATOM   2010 N N      . SER A 1 278 ? 7.154  10.690  14.198  1.00 36.95 ? 272 SER A N      1 
ATOM   2011 C CA     . SER A 1 278 ? 6.676  9.593   13.373  1.00 34.23 ? 272 SER A CA     1 
ATOM   2012 C C      . SER A 1 278 ? 7.689  8.459   13.426  1.00 34.82 ? 272 SER A C      1 
ATOM   2013 O O      . SER A 1 278 ? 8.870  8.668   13.710  1.00 37.15 ? 272 SER A O      1 
ATOM   2014 C CB     . SER A 1 278 ? 6.464  10.031  11.920  1.00 43.07 ? 272 SER A CB     1 
ATOM   2015 O OG     . SER A 1 278 ? 6.154  8.914   11.101  1.00 46.68 ? 272 SER A OG     1 
ATOM   2016 N N      . LYS A 1 279 ? 7.213  7.252   13.145  1.00 30.74 ? 273 LYS A N      1 
ATOM   2017 C CA     . LYS A 1 279 ? 8.083  6.090   13.111  1.00 26.99 ? 273 LYS A CA     1 
ATOM   2018 C C      . LYS A 1 279 ? 8.610  5.858   11.701  1.00 22.58 ? 273 LYS A C      1 
ATOM   2019 O O      . LYS A 1 279 ? 7.926  6.109   10.697  1.00 25.42 ? 273 LYS A O      1 
ATOM   2020 C CB     . LYS A 1 279 ? 7.364  4.834   13.615  1.00 30.57 ? 273 LYS A CB     1 
ATOM   2021 C CG     . LYS A 1 279 ? 7.341  4.701   15.163  1.00 36.41 ? 273 LYS A CG     1 
ATOM   2022 C CD     . LYS A 1 279 ? 7.010  3.270   15.580  1.00 40.68 ? 273 LYS A CD     1 
ATOM   2023 C CE     . LYS A 1 279 ? 6.804  3.110   17.088  1.00 43.95 ? 273 LYS A CE     1 
ATOM   2024 N NZ     . LYS A 1 279 ? 7.470  4.155   17.916  1.00 39.09 ? 273 LYS A NZ     1 
ATOM   2025 N N      . LEU A 1 280 ? 9.850  5.387   11.638  1.00 25.57 ? 274 LEU A N      1 
ATOM   2026 C CA     . LEU A 1 280 ? 10.397 4.902   10.386  1.00 20.73 ? 274 LEU A CA     1 
ATOM   2027 C C      . LEU A 1 280 ? 9.563  3.723   9.889   1.00 21.70 ? 274 LEU A C      1 
ATOM   2028 O O      . LEU A 1 280 ? 8.773  3.122   10.623  1.00 22.82 ? 274 LEU A O      1 
ATOM   2029 C CB     . LEU A 1 280 ? 11.840 4.451   10.600  1.00 21.47 ? 274 LEU A CB     1 
ATOM   2030 C CG     . LEU A 1 280 ? 12.812 5.554   11.017  1.00 21.87 ? 274 LEU A CG     1 
ATOM   2031 C CD1    . LEU A 1 280 ? 14.087 4.979   11.657  1.00 24.76 ? 274 LEU A CD1    1 
ATOM   2032 C CD2    . LEU A 1 280 ? 13.168 6.390   9.796   1.00 25.56 ? 274 LEU A CD2    1 
ATOM   2033 N N      . ALA A 1 281 ? 9.754  3.380   8.616   1.00 20.32 ? 275 ALA A N      1 
ATOM   2034 C CA     . ALA A 1 281 ? 9.090  2.191   8.097   1.00 21.66 ? 275 ALA A CA     1 
ATOM   2035 C C      . ALA A 1 281 ? 9.561  0.947   8.833   1.00 19.08 ? 275 ALA A C      1 
ATOM   2036 O O      . ALA A 1 281 ? 8.749  0.079   9.178   1.00 22.56 ? 275 ALA A O      1 
ATOM   2037 C CB     . ALA A 1 281 ? 9.338  2.046   6.594   1.00 19.70 ? 275 ALA A CB     1 
ATOM   2038 N N      . TYR A 1 282 ? 10.866 0.850   9.102   1.00 21.29 ? 276 TYR A N      1 
ATOM   2039 C CA     . TYR A 1 282 ? 11.428 -0.318  9.774   1.00 22.08 ? 276 TYR A CA     1 
ATOM   2040 C C      . TYR A 1 282 ? 12.925 -0.143  9.966   1.00 20.00 ? 276 TYR A C      1 
ATOM   2041 O O      . TYR A 1 282 ? 13.572 0.682   9.307   1.00 21.84 ? 276 TYR A O      1 
ATOM   2042 C CB     . TYR A 1 282 ? 11.212 -1.600  8.959   1.00 21.67 ? 276 TYR A CB     1 
ATOM   2043 C CG     . TYR A 1 282 ? 11.784 -1.529  7.563   1.00 19.49 ? 276 TYR A CG     1 
ATOM   2044 C CD1    . TYR A 1 282 ? 13.130 -1.805  7.317   1.00 20.71 ? 276 TYR A CD1    1 
ATOM   2045 C CD2    . TYR A 1 282 ? 10.980 -1.165  6.492   1.00 20.55 ? 276 TYR A CD2    1 
ATOM   2046 C CE1    . TYR A 1 282 ? 13.656 -1.728  6.015   1.00 18.67 ? 276 TYR A CE1    1 
ATOM   2047 C CE2    . TYR A 1 282 ? 11.490 -1.088  5.198   1.00 21.81 ? 276 TYR A CE2    1 
ATOM   2048 C CZ     . TYR A 1 282 ? 12.826 -1.377  4.974   1.00 17.99 ? 276 TYR A CZ     1 
ATOM   2049 O OH     . TYR A 1 282 ? 13.341 -1.306  3.703   1.00 17.91 ? 276 TYR A OH     1 
ATOM   2050 N N      . LEU A 1 283 ? 13.464 -0.962  10.869  1.00 20.63 ? 277 LEU A N      1 
ATOM   2051 C CA     . LEU A 1 283 ? 14.884 -1.281  10.943  1.00 18.00 ? 277 LEU A CA     1 
ATOM   2052 C C      . LEU A 1 283 ? 15.079 -2.708  10.435  1.00 18.65 ? 277 LEU A C      1 
ATOM   2053 O O      . LEU A 1 283 ? 14.330 -3.618  10.809  1.00 19.94 ? 277 LEU A O      1 
ATOM   2054 C CB     . LEU A 1 283 ? 15.395 -1.140  12.383  1.00 19.49 ? 277 LEU A CB     1 
ATOM   2055 C CG     . LEU A 1 283 ? 16.786 -1.709  12.685  1.00 16.66 ? 277 LEU A CG     1 
ATOM   2056 C CD1    . LEU A 1 283 ? 17.839 -0.799  12.111  1.00 21.58 ? 277 LEU A CD1    1 
ATOM   2057 C CD2    . LEU A 1 283 ? 16.989 -1.820  14.197  1.00 20.32 ? 277 LEU A CD2    1 
ATOM   2058 N N      . HIS A 1 284 ? 16.078 -2.890  9.573   1.00 19.07 ? 278 HIS A N      1 
ATOM   2059 C CA     . HIS A 1 284 ? 16.358 -4.143  8.881   1.00 18.95 ? 278 HIS A CA     1 
ATOM   2060 C C      . HIS A 1 284 ? 17.787 -4.524  9.247   1.00 19.44 ? 278 HIS A C      1 
ATOM   2061 O O      . HIS A 1 284 ? 18.719 -3.770  8.961   1.00 19.94 ? 278 HIS A O      1 
ATOM   2062 C CB     . HIS A 1 284 ? 16.228 -3.868  7.378   1.00 21.17 ? 278 HIS A CB     1 
ATOM   2063 C CG     . HIS A 1 284 ? 16.272 -5.075  6.488   1.00 19.18 ? 278 HIS A CG     1 
ATOM   2064 N ND1    . HIS A 1 284 ? 16.132 -4.966  5.120   1.00 22.60 ? 278 HIS A ND1    1 
ATOM   2065 C CD2    . HIS A 1 284 ? 16.422 -6.396  6.747   1.00 18.86 ? 278 HIS A CD2    1 
ATOM   2066 C CE1    . HIS A 1 284 ? 16.181 -6.168  4.575   1.00 21.90 ? 278 HIS A CE1    1 
ATOM   2067 N NE2    . HIS A 1 284 ? 16.376 -7.052  5.536   1.00 20.63 ? 278 HIS A NE2    1 
ATOM   2068 N N      . VAL A 1 285 ? 17.954 -5.646  9.944   1.00 19.84 ? 279 VAL A N      1 
ATOM   2069 C CA     . VAL A 1 285 ? 19.268 -6.076  10.412  1.00 20.78 ? 279 VAL A CA     1 
ATOM   2070 C C      . VAL A 1 285 ? 19.606 -7.399  9.753   1.00 17.54 ? 279 VAL A C      1 
ATOM   2071 O O      . VAL A 1 285 ? 18.788 -8.325  9.741   1.00 20.58 ? 279 VAL A O      1 
ATOM   2072 C CB     . VAL A 1 285 ? 19.328 -6.211  11.942  1.00 21.70 ? 279 VAL A CB     1 
ATOM   2073 C CG1    . VAL A 1 285 ? 20.702 -6.752  12.361  1.00 25.19 ? 279 VAL A CG1    1 
ATOM   2074 C CG2    . VAL A 1 285 ? 19.084 -4.869  12.574  1.00 22.47 ? 279 VAL A CG2    1 
ATOM   2075 N N      . THR A 1 286 ? 20.809 -7.491  9.209   1.00 20.80 ? 280 THR A N      1 
ATOM   2076 C CA     . THR A 1 286 ? 21.257 -8.723  8.599   1.00 19.47 ? 280 THR A CA     1 
ATOM   2077 C C      . THR A 1 286 ? 22.464 -9.239  9.371   1.00 28.79 ? 280 THR A C      1 
ATOM   2078 O O      . THR A 1 286 ? 23.284 -8.456  9.864   1.00 27.37 ? 280 THR A O      1 
ATOM   2079 C CB     . THR A 1 286 ? 21.518 -8.500  7.105   1.00 29.99 ? 280 THR A CB     1 
ATOM   2080 O OG1    . THR A 1 286 ? 21.476 -9.753  6.405   1.00 31.32 ? 280 THR A OG1    1 
ATOM   2081 C CG2    . THR A 1 286 ? 22.823 -7.794  6.896   1.00 28.12 ? 280 THR A CG2    1 
ATOM   2082 N N      . GLN A 1 287 ? 22.526 -10.551 9.527   1.00 25.19 ? 281 GLN A N      1 
ATOM   2083 C CA     . GLN A 1 287 ? 23.535 -11.223 10.328  1.00 29.05 ? 281 GLN A CA     1 
ATOM   2084 C C      . GLN A 1 287 ? 24.368 -12.138 9.436   1.00 29.27 ? 281 GLN A C      1 
ATOM   2085 O O      . GLN A 1 287 ? 23.942 -12.490 8.329   1.00 29.62 ? 281 GLN A O      1 
ATOM   2086 C CB     . GLN A 1 287 ? 22.822 -12.055 11.402  1.00 26.38 ? 281 GLN A CB     1 
ATOM   2087 C CG     . GLN A 1 287 ? 21.904 -13.115 10.829  1.00 28.24 ? 281 GLN A CG     1 
ATOM   2088 C CD     . GLN A 1 287 ? 21.127 -13.865 11.898  1.00 28.56 ? 281 GLN A CD     1 
ATOM   2089 O OE1    . GLN A 1 287 ? 21.267 -13.603 13.106  1.00 30.42 ? 281 GLN A OE1    1 
ATOM   2090 N NE2    . GLN A 1 287 ? 20.300 -14.804 11.464  1.00 30.13 ? 281 GLN A NE2    1 
ATOM   2091 N N      . PRO A 1 288 ? 25.563 -12.538 9.877   1.00 32.16 ? 282 PRO A N      1 
ATOM   2092 C CA     . PRO A 1 288 ? 26.397 -13.413 9.042   1.00 36.49 ? 282 PRO A CA     1 
ATOM   2093 C C      . PRO A 1 288 ? 25.869 -14.839 9.026   1.00 43.95 ? 282 PRO A C      1 
ATOM   2094 O O      . PRO A 1 288 ? 25.142 -15.276 9.920   1.00 42.99 ? 282 PRO A O      1 
ATOM   2095 C CB     . PRO A 1 288 ? 27.779 -13.360 9.713   1.00 37.16 ? 282 PRO A CB     1 
ATOM   2096 C CG     . PRO A 1 288 ? 27.656 -12.415 10.859  1.00 30.82 ? 282 PRO A CG     1 
ATOM   2097 C CD     . PRO A 1 288 ? 26.202 -12.253 11.173  1.00 31.90 ? 282 PRO A CD     1 
ATOM   2098 N N      . GLU A 1 289 ? 26.263 -15.573 7.988   1.00 50.27 ? 283 GLU A N      1 
ATOM   2099 C CA     . GLU A 1 289 ? 25.870 -16.973 7.843   1.00 56.98 ? 283 GLU A CA     1 
ATOM   2100 C C      . GLU A 1 289 ? 26.514 -17.835 8.927   1.00 56.21 ? 283 GLU A C      1 
ATOM   2101 O O      . GLU A 1 289 ? 25.826 -18.562 9.644   1.00 59.02 ? 283 GLU A O      1 
ATOM   2102 C CB     . GLU A 1 289 ? 26.260 -17.501 6.460   1.00 48.76 ? 283 GLU A CB     1 
ATOM   2103 C CG     . GLU A 1 289 ? 25.732 -18.897 6.144   1.00 60.15 ? 283 GLU A CG     1 
ATOM   2104 C CD     . GLU A 1 289 ? 24.309 -18.874 5.606   1.00 62.17 ? 283 GLU A CD     1 
ATOM   2105 O OE1    . GLU A 1 289 ? 23.636 -17.832 5.753   1.00 54.46 ? 283 GLU A OE1    1 
ATOM   2106 O OE2    . GLU A 1 289 ? 23.865 -19.893 5.030   1.00 60.84 ? 283 GLU A OE2    1 
ATOM   2107 N N      . ARG A 1 309 ? 22.254 -13.953 19.914  1.00 50.46 ? 303 ARG A N      1 
ATOM   2108 C CA     . ARG A 1 309 ? 21.276 -13.183 20.674  1.00 46.38 ? 303 ARG A CA     1 
ATOM   2109 C C      . ARG A 1 309 ? 21.271 -11.730 20.209  1.00 43.24 ? 303 ARG A C      1 
ATOM   2110 O O      . ARG A 1 309 ? 20.476 -10.922 20.692  1.00 45.18 ? 303 ARG A O      1 
ATOM   2111 C CB     . ARG A 1 309 ? 21.583 -13.251 22.173  1.00 40.10 ? 303 ARG A CB     1 
ATOM   2112 N N      . LEU A 1 310 ? 22.159 -11.414 19.263  1.00 37.64 ? 304 LEU A N      1 
ATOM   2113 C CA     . LEU A 1 310 ? 22.339 -10.026 18.846  1.00 35.00 ? 304 LEU A CA     1 
ATOM   2114 C C      . LEU A 1 310 ? 21.102 -9.498  18.127  1.00 31.94 ? 304 LEU A C      1 
ATOM   2115 O O      . LEU A 1 310 ? 20.683 -8.357  18.359  1.00 26.94 ? 304 LEU A O      1 
ATOM   2116 C CB     . LEU A 1 310 ? 23.604 -9.908  17.987  1.00 34.70 ? 304 LEU A CB     1 
ATOM   2117 C CG     . LEU A 1 310 ? 24.257 -8.573  17.595  1.00 40.80 ? 304 LEU A CG     1 
ATOM   2118 C CD1    . LEU A 1 310 ? 25.540 -8.851  16.823  1.00 47.20 ? 304 LEU A CD1    1 
ATOM   2119 C CD2    . LEU A 1 310 ? 23.387 -7.691  16.747  1.00 46.32 ? 304 LEU A CD2    1 
ATOM   2120 N N      . MET A 1 311 ? 20.498 -10.317 17.265  1.00 31.47 ? 305 MET A N      1 
ATOM   2121 C CA     . MET A 1 311 ? 19.325 -9.883  16.512  1.00 27.38 ? 305 MET A CA     1 
ATOM   2122 C C      . MET A 1 311 ? 18.180 -9.500  17.447  1.00 31.42 ? 305 MET A C      1 
ATOM   2123 O O      . MET A 1 311 ? 17.558 -8.441  17.287  1.00 26.41 ? 305 MET A O      1 
ATOM   2124 C CB     . MET A 1 311 ? 18.901 -10.991 15.542  1.00 27.24 ? 305 MET A CB     1 
ATOM   2125 C CG     . MET A 1 311 ? 17.790 -10.612 14.584  1.00 24.58 ? 305 MET A CG     1 
ATOM   2126 S SD     . MET A 1 311 ? 18.385 -9.677  13.148  1.00 33.41 ? 305 MET A SD     1 
ATOM   2127 C CE     . MET A 1 311 ? 19.163 -10.951 12.158  1.00 27.40 ? 305 MET A CE     1 
ATOM   2128 N N      . ARG A 1 312 ? 17.885 -10.357 18.428  1.00 30.75 ? 306 ARG A N      1 
ATOM   2129 C CA     . ARG A 1 312 ? 16.810 -10.065 19.372  1.00 28.19 ? 306 ARG A CA     1 
ATOM   2130 C C      . ARG A 1 312 ? 17.127 -8.836  20.218  1.00 25.18 ? 306 ARG A C      1 
ATOM   2131 O O      . ARG A 1 312 ? 16.235 -8.030  20.505  1.00 23.28 ? 306 ARG A O      1 
ATOM   2132 C CB     . ARG A 1 312 ? 16.534 -11.284 20.258  1.00 30.68 ? 306 ARG A CB     1 
ATOM   2133 C CG     . ARG A 1 312 ? 15.392 -11.090 21.233  1.00 35.12 ? 306 ARG A CG     1 
ATOM   2134 C CD     . ARG A 1 312 ? 14.102 -10.783 20.490  1.00 38.42 ? 306 ARG A CD     1 
ATOM   2135 N NE     . ARG A 1 312 ? 13.004 -10.507 21.404  1.00 32.53 ? 306 ARG A NE     1 
ATOM   2136 C CZ     . ARG A 1 312 ? 11.979 -11.322 21.614  1.00 38.56 ? 306 ARG A CZ     1 
ATOM   2137 N NH1    . ARG A 1 312 ? 11.877 -12.481 20.985  1.00 37.80 ? 306 ARG A NH1    1 
ATOM   2138 N NH2    . ARG A 1 312 ? 11.037 -10.969 22.485  1.00 44.57 ? 306 ARG A NH2    1 
ATOM   2139 N N      . THR A 1 313 ? 18.393 -8.663  20.613  1.00 25.98 ? 307 THR A N      1 
ATOM   2140 C CA     . THR A 1 313 ? 18.763 -7.505  21.423  1.00 25.38 ? 307 THR A CA     1 
ATOM   2141 C C      . THR A 1 313 ? 18.516 -6.194  20.683  1.00 27.35 ? 307 THR A C      1 
ATOM   2142 O O      . THR A 1 313 ? 18.000 -5.233  21.261  1.00 23.96 ? 307 THR A O      1 
ATOM   2143 C CB     . THR A 1 313 ? 20.226 -7.605  21.853  1.00 30.19 ? 307 THR A CB     1 
ATOM   2144 O OG1    . THR A 1 313 ? 20.429 -8.807  22.609  1.00 38.81 ? 307 THR A OG1    1 
ATOM   2145 C CG2    . THR A 1 313 ? 20.605 -6.398  22.699  1.00 31.78 ? 307 THR A CG2    1 
ATOM   2146 N N      . LEU A 1 314 ? 18.880 -6.121  19.401  1.00 20.59 ? 308 LEU A N      1 
ATOM   2147 C CA     . LEU A 1 314 ? 18.589 -4.887  18.674  1.00 20.65 ? 308 LEU A CA     1 
ATOM   2148 C C      . LEU A 1 314 ? 17.088 -4.691  18.486  1.00 19.82 ? 308 LEU A C      1 
ATOM   2149 O O      . LEU A 1 314 ? 16.582 -3.570  18.614  1.00 23.45 ? 308 LEU A O      1 
ATOM   2150 C CB     . LEU A 1 314 ? 19.321 -4.851  17.334  1.00 22.30 ? 308 LEU A CB     1 
ATOM   2151 C CG     . LEU A 1 314 ? 20.831 -5.076  17.401  1.00 22.73 ? 308 LEU A CG     1 
ATOM   2152 C CD1    . LEU A 1 314 ? 21.338 -5.090  15.963  1.00 22.61 ? 308 LEU A CD1    1 
ATOM   2153 C CD2    . LEU A 1 314 ? 21.556 -4.031  18.230  1.00 24.70 ? 308 LEU A CD2    1 
ATOM   2154 N N      . ARG A 1 315 ? 16.361 -5.771  18.205  1.00 19.19 ? 309 ARG A N      1 
ATOM   2155 C CA     . ARG A 1 315 ? 14.910 -5.679  18.074  1.00 21.28 ? 309 ARG A CA     1 
ATOM   2156 C C      . ARG A 1 315 ? 14.290 -5.140  19.356  1.00 20.99 ? 309 ARG A C      1 
ATOM   2157 O O      . ARG A 1 315 ? 13.433 -4.249  19.323  1.00 22.83 ? 309 ARG A O      1 
ATOM   2158 C CB     . ARG A 1 315 ? 14.338 -7.060  17.749  1.00 22.03 ? 309 ARG A CB     1 
ATOM   2159 C CG     . ARG A 1 315 ? 12.880 -7.055  17.299  1.00 21.91 ? 309 ARG A CG     1 
ATOM   2160 C CD     . ARG A 1 315 ? 11.877 -7.025  18.463  1.00 20.33 ? 309 ARG A CD     1 
ATOM   2161 N NE     . ARG A 1 315 ? 10.644 -7.712  18.100  1.00 23.89 ? 309 ARG A NE     1 
ATOM   2162 C CZ     . ARG A 1 315 ? 9.774  -7.281  17.195  1.00 25.45 ? 309 ARG A CZ     1 
ATOM   2163 N NH1    . ARG A 1 315 ? 9.880  -6.082  16.644  1.00 21.65 ? 309 ARG A NH1    1 
ATOM   2164 N NH2    . ARG A 1 315 ? 8.772  -8.076  16.835  1.00 24.51 ? 309 ARG A NH2    1 
ATOM   2165 N N      . ASN A 1 316 ? 14.721 -5.665  20.499  1.00 20.85 ? 310 ASN A N      1 
ATOM   2166 C CA     . ASN A 1 316 ? 14.132 -5.229  21.761  1.00 21.33 ? 310 ASN A CA     1 
ATOM   2167 C C      . ASN A 1 316 ? 14.405 -3.755  22.020  1.00 24.29 ? 310 ASN A C      1 
ATOM   2168 O O      . ASN A 1 316 ? 13.609 -3.080  22.685  1.00 24.45 ? 310 ASN A O      1 
ATOM   2169 C CB     . ASN A 1 316 ? 14.707 -6.066  22.902  1.00 23.64 ? 310 ASN A CB     1 
ATOM   2170 C CG     . ASN A 1 316 ? 14.043 -7.429  23.029  1.00 22.74 ? 310 ASN A CG     1 
ATOM   2171 O OD1    . ASN A 1 316 ? 13.006 -7.699  22.422  1.00 26.39 ? 310 ASN A OD1    1 
ATOM   2172 N ND2    . ASN A 1 316 ? 14.660 -8.310  23.823  1.00 26.00 ? 310 ASN A ND2    1 
ATOM   2173 N N      . ALA A 1 317 ? 15.525 -3.242  21.519  1.00 20.08 ? 311 ALA A N      1 
ATOM   2174 C CA     . ALA A 1 317 ? 15.897 -1.858  21.771  1.00 20.11 ? 311 ALA A CA     1 
ATOM   2175 C C      . ALA A 1 317 ? 15.227 -0.888  20.819  1.00 24.40 ? 311 ALA A C      1 
ATOM   2176 O O      . ALA A 1 317 ? 15.159 0.306   21.119  1.00 22.73 ? 311 ALA A O      1 
ATOM   2177 C CB     . ALA A 1 317 ? 17.412 -1.695  21.663  1.00 22.69 ? 311 ALA A CB     1 
ATOM   2178 N N      . TYR A 1 318 ? 14.772 -1.358  19.660  1.00 22.98 ? 312 TYR A N      1 
ATOM   2179 C CA     . TYR A 1 318 ? 14.248 -0.474  18.641  1.00 20.09 ? 312 TYR A CA     1 
ATOM   2180 C C      . TYR A 1 318 ? 12.739 -0.321  18.787  1.00 18.80 ? 312 TYR A C      1 
ATOM   2181 O O      . TYR A 1 318 ? 12.009 -1.314  18.909  1.00 21.83 ? 312 TYR A O      1 
ATOM   2182 C CB     . TYR A 1 318 ? 14.618 -1.000  17.249  1.00 19.20 ? 312 TYR A CB     1 
ATOM   2183 C CG     . TYR A 1 318 ? 13.950 -0.203  16.169  1.00 20.86 ? 312 TYR A CG     1 
ATOM   2184 C CD1    . TYR A 1 318 ? 14.187 1.167   16.050  1.00 20.93 ? 312 TYR A CD1    1 
ATOM   2185 C CD2    . TYR A 1 318 ? 13.024 -0.789  15.324  1.00 20.02 ? 312 TYR A CD2    1 
ATOM   2186 C CE1    . TYR A 1 318 ? 13.542 1.924   15.097  1.00 22.92 ? 312 TYR A CE1    1 
ATOM   2187 C CE2    . TYR A 1 318 ? 12.376 -0.036  14.356  1.00 21.22 ? 312 TYR A CE2    1 
ATOM   2188 C CZ     . TYR A 1 318 ? 12.640 1.316   14.253  1.00 23.21 ? 312 TYR A CZ     1 
ATOM   2189 O OH     . TYR A 1 318 ? 11.979 2.064   13.312  1.00 25.01 ? 312 TYR A OH     1 
ATOM   2190 N N      . GLN A 1 319 ? 12.280 0.935   18.766  1.00 21.21 ? 313 GLN A N      1 
ATOM   2191 C CA     . GLN A 1 319 ? 10.859 1.287   18.874  1.00 22.95 ? 313 GLN A CA     1 
ATOM   2192 C C      . GLN A 1 319 ? 10.238 1.331   17.477  1.00 22.43 ? 313 GLN A C      1 
ATOM   2193 O O      . GLN A 1 319 ? 10.048 2.394   16.885  1.00 28.94 ? 313 GLN A O      1 
ATOM   2194 C CB     . GLN A 1 319 ? 10.738 2.643   19.553  1.00 23.13 ? 313 GLN A CB     1 
ATOM   2195 C CG     . GLN A 1 319 ? 11.407 2.661   20.929  1.00 23.85 ? 313 GLN A CG     1 
ATOM   2196 C CD     . GLN A 1 319 ? 11.283 3.981   21.646  1.00 32.18 ? 313 GLN A CD     1 
ATOM   2197 O OE1    . GLN A 1 319 ? 10.654 4.912   21.159  1.00 30.88 ? 313 GLN A OE1    1 
ATOM   2198 N NE2    . GLN A 1 319 ? 11.894 4.069   22.825  1.00 31.83 ? 313 GLN A NE2    1 
ATOM   2199 N N      . GLY A 1 320 ? 9.896  0.159   16.950  1.00 23.74 ? 314 GLY A N      1 
ATOM   2200 C CA     . GLY A 1 320 ? 9.278  0.112   15.632  1.00 20.57 ? 314 GLY A CA     1 
ATOM   2201 C C      . GLY A 1 320 ? 9.369  -1.276  15.011  1.00 24.34 ? 314 GLY A C      1 
ATOM   2202 O O      . GLY A 1 320 ? 9.691  -2.257  15.680  1.00 24.76 ? 314 GLY A O      1 
ATOM   2203 N N      . THR A 1 321 ? 9.083  -1.315  13.709  1.00 21.84 ? 315 THR A N      1 
ATOM   2204 C CA     . THR A 1 321 ? 9.034  -2.557  12.952  1.00 21.78 ? 315 THR A CA     1 
ATOM   2205 C C      . THR A 1 321 ? 10.445 -3.063  12.672  1.00 21.26 ? 315 THR A C      1 
ATOM   2206 O O      . THR A 1 321 ? 11.342 -2.288  12.338  1.00 20.84 ? 315 THR A O      1 
ATOM   2207 C CB     . THR A 1 321 ? 8.330  -2.287  11.622  1.00 23.67 ? 315 THR A CB     1 
ATOM   2208 O OG1    . THR A 1 321 ? 6.963  -1.939  11.892  1.00 23.63 ? 315 THR A OG1    1 
ATOM   2209 C CG2    . THR A 1 321 ? 8.372  -3.515  10.715  1.00 24.48 ? 315 THR A CG2    1 
ATOM   2210 N N      . PHE A 1 322 ? 10.636 -4.372  12.815  1.00 21.60 ? 316 PHE A N      1 
ATOM   2211 C CA     . PHE A 1 322 ? 11.957 -4.977  12.692  1.00 19.87 ? 316 PHE A CA     1 
ATOM   2212 C C      . PHE A 1 322 ? 11.922 -6.082  11.643  1.00 20.35 ? 316 PHE A C      1 
ATOM   2213 O O      . PHE A 1 322 ? 11.097 -6.997  11.735  1.00 20.49 ? 316 PHE A O      1 
ATOM   2214 C CB     . PHE A 1 322 ? 12.352 -5.572  14.044  1.00 18.50 ? 316 PHE A CB     1 
ATOM   2215 C CG     . PHE A 1 322 ? 13.785 -5.981  14.135  1.00 19.56 ? 316 PHE A CG     1 
ATOM   2216 C CD1    . PHE A 1 322 ? 14.763 -5.059  14.471  1.00 19.53 ? 316 PHE A CD1    1 
ATOM   2217 C CD2    . PHE A 1 322 ? 14.151 -7.294  13.880  1.00 21.59 ? 316 PHE A CD2    1 
ATOM   2218 C CE1    . PHE A 1 322 ? 16.097 -5.444  14.553  1.00 20.54 ? 316 PHE A CE1    1 
ATOM   2219 C CE2    . PHE A 1 322 ? 15.479 -7.682  13.972  1.00 23.37 ? 316 PHE A CE2    1 
ATOM   2220 C CZ     . PHE A 1 322 ? 16.445 -6.755  14.312  1.00 21.27 ? 316 PHE A CZ     1 
ATOM   2221 N N      . ILE A 1 323 ? 12.834 -6.008  10.665  1.00 20.36 ? 317 ILE A N      1 
ATOM   2222 C CA     . ILE A 1 323 ? 13.014 -7.038  9.645   1.00 20.67 ? 317 ILE A CA     1 
ATOM   2223 C C      . ILE A 1 323 ? 14.330 -7.755  9.924   1.00 20.34 ? 317 ILE A C      1 
ATOM   2224 O O      . ILE A 1 323 ? 15.396 -7.123  9.965   1.00 20.99 ? 317 ILE A O      1 
ATOM   2225 C CB     . ILE A 1 323 ? 13.058 -6.445  8.230   1.00 21.47 ? 317 ILE A CB     1 
ATOM   2226 C CG1    . ILE A 1 323 ? 11.856 -5.528  7.973   1.00 20.22 ? 317 ILE A CG1    1 
ATOM   2227 C CG2    . ILE A 1 323 ? 13.097 -7.582  7.201   1.00 18.49 ? 317 ILE A CG2    1 
ATOM   2228 C CD1    . ILE A 1 323 ? 11.771 -5.053  6.512   1.00 19.71 ? 317 ILE A CD1    1 
ATOM   2229 N N      . CYS A 1 324 ? 14.261 -9.068  10.098  1.00 20.74 ? 318 CYS A N      1 
ATOM   2230 C CA     . CYS A 1 324 ? 15.447 -9.897  10.273  1.00 21.65 ? 318 CYS A CA     1 
ATOM   2231 C C      . CYS A 1 324 ? 15.860 -10.558 8.963   1.00 22.79 ? 318 CYS A C      1 
ATOM   2232 O O      . CYS A 1 324 ? 15.032 -10.807 8.081   1.00 20.68 ? 318 CYS A O      1 
ATOM   2233 C CB     . CYS A 1 324 ? 15.210 -10.927 11.380  1.00 22.13 ? 318 CYS A CB     1 
ATOM   2234 S SG     . CYS A 1 324 ? 14.004 -12.219 10.986  1.00 26.51 ? 318 CYS A SG     1 
ATOM   2235 N N      . SER A 1 325 ? 17.164 -10.812 8.834   1.00 20.95 ? 319 SER A N      1 
ATOM   2236 C CA     . SER A 1 325 ? 17.716 -11.239 7.560   1.00 21.53 ? 319 SER A CA     1 
ATOM   2237 C C      . SER A 1 325 ? 19.020 -11.993 7.797   1.00 22.85 ? 319 SER A C      1 
ATOM   2238 O O      . SER A 1 325 ? 19.785 -11.667 8.707   1.00 22.86 ? 319 SER A O      1 
ATOM   2239 C CB     . SER A 1 325 ? 17.997 -10.004 6.703   1.00 23.23 ? 319 SER A CB     1 
ATOM   2240 O OG     . SER A 1 325 ? 18.741 -10.339 5.544   1.00 30.12 ? 319 SER A OG     1 
ATOM   2241 N N      . GLY A 1 326 ? 19.270 -12.986 6.945   1.00 22.54 ? 320 GLY A N      1 
ATOM   2242 C CA     . GLY A 1 326 ? 20.529 -13.709 6.957   1.00 23.31 ? 320 GLY A CA     1 
ATOM   2243 C C      . GLY A 1 326 ? 20.373 -15.163 7.348   1.00 24.70 ? 320 GLY A C      1 
ATOM   2244 O O      . GLY A 1 326 ? 20.269 -15.485 8.537   1.00 25.22 ? 320 GLY A O      1 
ATOM   2245 N N      . GLY A 1 327 ? 20.343 -16.055 6.365   1.00 26.75 ? 321 GLY A N      1 
ATOM   2246 C CA     . GLY A 1 327 ? 20.271 -17.472 6.656   1.00 28.57 ? 321 GLY A CA     1 
ATOM   2247 C C      . GLY A 1 327 ? 18.914 -17.985 7.071   1.00 32.50 ? 321 GLY A C      1 
ATOM   2248 O O      . GLY A 1 327 ? 18.821 -19.124 7.544   1.00 34.55 ? 321 GLY A O      1 
ATOM   2249 N N      . TYR A 1 328 ? 17.858 -17.194 6.917   1.00 27.98 ? 322 TYR A N      1 
ATOM   2250 C CA     . TYR A 1 328 ? 16.543 -17.670 7.306   1.00 27.41 ? 322 TYR A CA     1 
ATOM   2251 C C      . TYR A 1 328 ? 16.020 -18.706 6.322   1.00 26.84 ? 322 TYR A C      1 
ATOM   2252 O O      . TYR A 1 328 ? 16.241 -18.617 5.108   1.00 29.16 ? 322 TYR A O      1 
ATOM   2253 C CB     . TYR A 1 328 ? 15.574 -16.502 7.507   1.00 28.03 ? 322 TYR A CB     1 
ATOM   2254 C CG     . TYR A 1 328 ? 15.900 -15.787 8.793   1.00 25.54 ? 322 TYR A CG     1 
ATOM   2255 C CD1    . TYR A 1 328 ? 16.848 -14.775 8.815   1.00 25.77 ? 322 TYR A CD1    1 
ATOM   2256 C CD2    . TYR A 1 328 ? 15.307 -16.162 10.004  1.00 31.16 ? 322 TYR A CD2    1 
ATOM   2257 C CE1    . TYR A 1 328 ? 17.188 -14.132 9.985   1.00 24.83 ? 322 TYR A CE1    1 
ATOM   2258 C CE2    . TYR A 1 328 ? 15.637 -15.519 11.188  1.00 25.53 ? 322 TYR A CE2    1 
ATOM   2259 C CZ     . TYR A 1 328 ? 16.578 -14.507 11.173  1.00 28.47 ? 322 TYR A CZ     1 
ATOM   2260 O OH     . TYR A 1 328 ? 16.927 -13.857 12.331  1.00 30.75 ? 322 TYR A OH     1 
ATOM   2261 N N      . THR A 1 329 ? 15.388 -19.729 6.874   1.00 28.28 ? 323 THR A N      1 
ATOM   2262 C CA     . THR A 1 329 ? 14.661 -20.765 6.166   1.00 28.42 ? 323 THR A CA     1 
ATOM   2263 C C      . THR A 1 329 ? 13.175 -20.567 6.440   1.00 32.27 ? 323 THR A C      1 
ATOM   2264 O O      . THR A 1 329 ? 12.779 -19.665 7.182   1.00 27.08 ? 323 THR A O      1 
ATOM   2265 C CB     . THR A 1 329 ? 15.116 -22.137 6.664   1.00 28.91 ? 323 THR A CB     1 
ATOM   2266 O OG1    . THR A 1 329 ? 14.748 -22.292 8.047   1.00 29.31 ? 323 THR A OG1    1 
ATOM   2267 C CG2    . THR A 1 329 ? 16.635 -22.289 6.521   1.00 32.25 ? 323 THR A CG2    1 
ATOM   2268 N N      . ARG A 1 330 ? 12.346 -21.422 5.837   1.00 28.80 ? 324 ARG A N      1 
ATOM   2269 C CA     . ARG A 1 330 ? 10.926 -21.425 6.181   1.00 29.09 ? 324 ARG A CA     1 
ATOM   2270 C C      . ARG A 1 330 ? 10.725 -21.616 7.680   1.00 27.51 ? 324 ARG A C      1 
ATOM   2271 O O      . ARG A 1 330 ? 10.000 -20.850 8.325   1.00 27.27 ? 324 ARG A O      1 
ATOM   2272 C CB     . ARG A 1 330 ? 10.203 -22.528 5.418   1.00 28.77 ? 324 ARG A CB     1 
ATOM   2273 C CG     . ARG A 1 330 ? 8.727  -22.553 5.703   1.00 30.23 ? 324 ARG A CG     1 
ATOM   2274 C CD     . ARG A 1 330 ? 8.052  -23.670 4.968   1.00 30.17 ? 324 ARG A CD     1 
ATOM   2275 N NE     . ARG A 1 330 ? 6.615  -23.633 5.188   1.00 33.54 ? 324 ARG A NE     1 
ATOM   2276 C CZ     . ARG A 1 330 ? 5.993  -24.313 6.140   1.00 35.41 ? 324 ARG A CZ     1 
ATOM   2277 N NH1    . ARG A 1 330 ? 6.656  -25.115 6.955   1.00 34.61 ? 324 ARG A NH1    1 
ATOM   2278 N NH2    . ARG A 1 330 ? 4.676  -24.186 6.273   1.00 35.97 ? 324 ARG A NH2    1 
ATOM   2279 N N      . GLU A 1 331 ? 11.376 -22.632 8.252   1.00 27.47 ? 325 GLU A N      1 
ATOM   2280 C CA     . GLU A 1 331 ? 11.189 -22.938 9.670   1.00 28.57 ? 325 GLU A CA     1 
ATOM   2281 C C      . GLU A 1 331 ? 11.746 -21.835 10.564  1.00 28.01 ? 325 GLU A C      1 
ATOM   2282 O O      . GLU A 1 331 ? 11.109 -21.455 11.555  1.00 29.15 ? 325 GLU A O      1 
ATOM   2283 C CB     . GLU A 1 331 ? 11.821 -24.290 10.000  1.00 35.54 ? 325 GLU A CB     1 
ATOM   2284 N N      . LEU A 1 332 ? 12.928 -21.305 10.238  1.00 28.69 ? 326 LEU A N      1 
ATOM   2285 C CA     . LEU A 1 332 ? 13.508 -20.249 11.064  1.00 31.53 ? 326 LEU A CA     1 
ATOM   2286 C C      . LEU A 1 332 ? 12.735 -18.942 10.948  1.00 27.91 ? 326 LEU A C      1 
ATOM   2287 O O      . LEU A 1 332 ? 12.634 -18.201 11.933  1.00 26.86 ? 326 LEU A O      1 
ATOM   2288 C CB     . LEU A 1 332 ? 14.987 -20.046 10.727  1.00 28.35 ? 326 LEU A CB     1 
ATOM   2289 C CG     . LEU A 1 332 ? 15.913 -21.188 11.144  1.00 27.87 ? 326 LEU A CG     1 
ATOM   2290 C CD1    . LEU A 1 332 ? 17.312 -20.983 10.608  1.00 32.34 ? 326 LEU A CD1    1 
ATOM   2291 C CD2    . LEU A 1 332 ? 15.923 -21.321 12.665  1.00 33.01 ? 326 LEU A CD2    1 
ATOM   2292 N N      . GLY A 1 333 ? 12.181 -18.641 9.768   1.00 26.88 ? 327 GLY A N      1 
ATOM   2293 C CA     . GLY A 1 333 ? 11.323 -17.473 9.639   1.00 27.48 ? 327 GLY A CA     1 
ATOM   2294 C C      . GLY A 1 333 ? 10.033 -17.596 10.434  1.00 29.00 ? 327 GLY A C      1 
ATOM   2295 O O      . GLY A 1 333 ? 9.605  -16.639 11.090  1.00 27.18 ? 327 GLY A O      1 
ATOM   2296 N N      . ILE A 1 334 ? 9.390  -18.769 10.378  1.00 24.71 ? 328 ILE A N      1 
ATOM   2297 C CA     . ILE A 1 334 ? 8.189  -19.003 11.177  1.00 27.66 ? 328 ILE A CA     1 
ATOM   2298 C C      . ILE A 1 334 ? 8.498  -18.792 12.651  1.00 28.40 ? 328 ILE A C      1 
ATOM   2299 O O      . ILE A 1 334 ? 7.769  -18.095 13.367  1.00 27.59 ? 328 ILE A O      1 
ATOM   2300 C CB     . ILE A 1 334 ? 7.626  -20.414 10.921  1.00 28.74 ? 328 ILE A CB     1 
ATOM   2301 C CG1    . ILE A 1 334 ? 6.971  -20.505 9.538   1.00 32.80 ? 328 ILE A CG1    1 
ATOM   2302 C CG2    . ILE A 1 334 ? 6.612  -20.788 11.996  1.00 31.35 ? 328 ILE A CG2    1 
ATOM   2303 C CD1    . ILE A 1 334 ? 6.708  -21.934 9.078   1.00 30.68 ? 328 ILE A CD1    1 
ATOM   2304 N N      . GLU A 1 335 ? 9.602  -19.381 13.114  1.00 28.42 ? 329 GLU A N      1 
ATOM   2305 C CA     . GLU A 1 335 ? 9.998  -19.279 14.516  1.00 30.06 ? 329 GLU A CA     1 
ATOM   2306 C C      . GLU A 1 335 ? 10.277 -17.832 14.915  1.00 28.30 ? 329 GLU A C      1 
ATOM   2307 O O      . GLU A 1 335 ? 9.881  -17.396 16.004  1.00 31.24 ? 329 GLU A O      1 
ATOM   2308 C CB     . GLU A 1 335 ? 11.227 -20.162 14.732  1.00 31.11 ? 329 GLU A CB     1 
ATOM   2309 C CG     . GLU A 1 335 ? 11.743 -20.272 16.145  1.00 45.69 ? 329 GLU A CG     1 
ATOM   2310 C CD     . GLU A 1 335 ? 13.097 -20.965 16.192  1.00 56.94 ? 329 GLU A CD     1 
ATOM   2311 O OE1    . GLU A 1 335 ? 14.126 -20.289 15.961  1.00 52.44 ? 329 GLU A OE1    1 
ATOM   2312 O OE2    . GLU A 1 335 ? 13.130 -22.187 16.454  1.00 64.88 ? 329 GLU A OE2    1 
ATOM   2313 N N      . ALA A 1 336 ? 10.949 -17.069 14.046  1.00 27.27 ? 330 ALA A N      1 
ATOM   2314 C CA     . ALA A 1 336 ? 11.292 -15.690 14.383  1.00 25.24 ? 330 ALA A CA     1 
ATOM   2315 C C      . ALA A 1 336 ? 10.045 -14.851 14.630  1.00 27.82 ? 330 ALA A C      1 
ATOM   2316 O O      . ALA A 1 336 ? 9.993  -14.062 15.579  1.00 30.78 ? 330 ALA A O      1 
ATOM   2317 C CB     . ALA A 1 336 ? 12.145 -15.068 13.275  1.00 27.45 ? 330 ALA A CB     1 
ATOM   2318 N N      . VAL A 1 337 ? 9.029  -14.998 13.779  1.00 27.56 ? 331 VAL A N      1 
ATOM   2319 C CA     . VAL A 1 337 ? 7.806  -14.228 13.973  1.00 25.10 ? 331 VAL A CA     1 
ATOM   2320 C C      . VAL A 1 337 ? 7.021  -14.754 15.171  1.00 29.09 ? 331 VAL A C      1 
ATOM   2321 O O      . VAL A 1 337 ? 6.486  -13.974 15.970  1.00 26.60 ? 331 VAL A O      1 
ATOM   2322 C CB     . VAL A 1 337 ? 6.978  -14.207 12.679  1.00 26.69 ? 331 VAL A CB     1 
ATOM   2323 C CG1    . VAL A 1 337 ? 5.641  -13.512 12.916  1.00 26.22 ? 331 VAL A CG1    1 
ATOM   2324 C CG2    . VAL A 1 337 ? 7.791  -13.523 11.558  1.00 24.38 ? 331 VAL A CG2    1 
ATOM   2325 N N      . ALA A 1 338 ? 6.962  -16.081 15.331  1.00 25.54 ? 332 ALA A N      1 
ATOM   2326 C CA     . ALA A 1 338 ? 6.189  -16.660 16.432  1.00 28.03 ? 332 ALA A CA     1 
ATOM   2327 C C      . ALA A 1 338 ? 6.775  -16.300 17.791  1.00 32.02 ? 332 ALA A C      1 
ATOM   2328 O O      . ALA A 1 338 ? 6.029  -16.107 18.758  1.00 33.29 ? 332 ALA A O      1 
ATOM   2329 C CB     . ALA A 1 338 ? 6.082  -18.177 16.271  1.00 30.46 ? 332 ALA A CB     1 
ATOM   2330 N N      . GLN A 1 339 ? 8.096  -16.207 17.896  1.00 30.15 ? 333 GLN A N      1 
ATOM   2331 C CA     . GLN A 1 339 ? 8.733  -15.880 19.170  1.00 31.07 ? 333 GLN A CA     1 
ATOM   2332 C C      . GLN A 1 339 ? 8.890  -14.383 19.409  1.00 33.58 ? 333 GLN A C      1 
ATOM   2333 O O      . GLN A 1 339 ? 9.410  -13.989 20.463  1.00 32.44 ? 333 GLN A O      1 
ATOM   2334 C CB     . GLN A 1 339 ? 10.078 -16.598 19.306  1.00 32.85 ? 333 GLN A CB     1 
ATOM   2335 C CG     . GLN A 1 339 ? 10.007 -18.072 18.972  1.00 35.77 ? 333 GLN A CG     1 
ATOM   2336 C CD     . GLN A 1 339 ? 11.326 -18.788 19.172  1.00 53.67 ? 333 GLN A CD     1 
ATOM   2337 O OE1    . GLN A 1 339 ? 12.396 -18.232 18.919  1.00 52.22 ? 333 GLN A OE1    1 
ATOM   2338 N NE2    . GLN A 1 339 ? 11.255 -20.038 19.617  1.00 60.23 ? 333 GLN A NE2    1 
ATOM   2339 N N      . GLY A 1 340 ? 8.426  -13.546 18.481  1.00 31.26 ? 334 GLY A N      1 
ATOM   2340 C CA     . GLY A 1 340 ? 8.561  -12.112 18.616  1.00 28.88 ? 334 GLY A CA     1 
ATOM   2341 C C      . GLY A 1 340 ? 9.937  -11.568 18.325  1.00 33.95 ? 334 GLY A C      1 
ATOM   2342 O O      . GLY A 1 340 ? 10.237 -10.436 18.723  1.00 30.86 ? 334 GLY A O      1 
ATOM   2343 N N      . ASP A 1 341 ? 10.790 -12.340 17.635  1.00 27.64 ? 335 ASP A N      1 
ATOM   2344 C CA     . ASP A 1 341 ? 12.133 -11.893 17.298  1.00 27.42 ? 335 ASP A CA     1 
ATOM   2345 C C      . ASP A 1 341 ? 12.134 -10.907 16.134  1.00 28.86 ? 335 ASP A C      1 
ATOM   2346 O O      . ASP A 1 341 ? 13.127 -10.195 15.934  1.00 27.62 ? 335 ASP A O      1 
ATOM   2347 C CB     . ASP A 1 341 ? 12.985 -13.090 16.871  1.00 34.46 ? 335 ASP A CB     1 
ATOM   2348 C CG     . ASP A 1 341 ? 13.309 -14.023 18.016  1.00 45.08 ? 335 ASP A CG     1 
ATOM   2349 O OD1    . ASP A 1 341 ? 13.510 -13.543 19.151  1.00 48.64 ? 335 ASP A OD1    1 
ATOM   2350 O OD2    . ASP A 1 341 ? 13.336 -15.251 17.782  1.00 44.52 ? 335 ASP A OD2    1 
ATOM   2351 N N      . ALA A 1 342 ? 11.062 -10.871 15.347  1.00 22.17 ? 336 ALA A N      1 
ATOM   2352 C CA     . ALA A 1 342 ? 10.969 -9.943  14.235  1.00 21.52 ? 336 ALA A CA     1 
ATOM   2353 C C      . ALA A 1 342 ? 9.523  -9.835  13.798  1.00 21.27 ? 336 ALA A C      1 
ATOM   2354 O O      . ALA A 1 342 ? 8.711  -10.731 14.041  1.00 25.76 ? 336 ALA A O      1 
ATOM   2355 C CB     . ALA A 1 342 ? 11.811 -10.399 13.040  1.00 24.52 ? 336 ALA A CB     1 
ATOM   2356 N N      . ASP A 1 343 ? 9.226  -8.739  13.106  1.00 20.44 ? 337 ASP A N      1 
ATOM   2357 C CA     . ASP A 1 343 ? 7.910  -8.568  12.511  1.00 20.30 ? 337 ASP A CA     1 
ATOM   2358 C C      . ASP A 1 343 ? 7.863  -9.062  11.076  1.00 21.54 ? 337 ASP A C      1 
ATOM   2359 O O      . ASP A 1 343 ? 6.816  -9.541  10.622  1.00 21.42 ? 337 ASP A O      1 
ATOM   2360 C CB     . ASP A 1 343 ? 7.519  -7.092  12.547  1.00 21.97 ? 337 ASP A CB     1 
ATOM   2361 C CG     . ASP A 1 343 ? 7.610  -6.516  13.938  1.00 20.82 ? 337 ASP A CG     1 
ATOM   2362 O OD1    . ASP A 1 343 ? 6.803  -6.947  14.783  1.00 23.92 ? 337 ASP A OD1    1 
ATOM   2363 O OD2    . ASP A 1 343 ? 8.473  -5.645  14.189  1.00 21.27 ? 337 ASP A OD2    1 
ATOM   2364 N N      . LEU A 1 344 ? 8.975  -8.951  10.354  1.00 19.61 ? 338 LEU A N      1 
ATOM   2365 C CA     . LEU A 1 344 ? 9.054  -9.373  8.961   1.00 19.36 ? 338 LEU A CA     1 
ATOM   2366 C C      . LEU A 1 344 ? 10.375 -10.107 8.792   1.00 19.39 ? 338 LEU A C      1 
ATOM   2367 O O      . LEU A 1 344 ? 11.320 -9.869  9.540   1.00 20.00 ? 338 LEU A O      1 
ATOM   2368 C CB     . LEU A 1 344 ? 9.006  -8.163  8.013   1.00 22.60 ? 338 LEU A CB     1 
ATOM   2369 C CG     . LEU A 1 344 ? 7.801  -7.218  8.169   1.00 23.14 ? 338 LEU A CG     1 
ATOM   2370 C CD1    . LEU A 1 344 ? 8.057  -5.903  7.456   1.00 22.88 ? 338 LEU A CD1    1 
ATOM   2371 C CD2    . LEU A 1 344 ? 6.514  -7.858  7.671   1.00 23.28 ? 338 LEU A CD2    1 
ATOM   2372 N N      . VAL A 1 345 ? 10.439 -10.992 7.795   1.00 20.40 ? 339 VAL A N      1 
ATOM   2373 C CA     . VAL A 1 345 ? 11.617 -11.821 7.546   1.00 19.32 ? 339 VAL A CA     1 
ATOM   2374 C C      . VAL A 1 345 ? 11.949 -11.653 6.072   1.00 18.43 ? 339 VAL A C      1 
ATOM   2375 O O      . VAL A 1 345 ? 11.087 -11.891 5.217   1.00 19.92 ? 339 VAL A O      1 
ATOM   2376 C CB     . VAL A 1 345 ? 11.331 -13.305 7.846   1.00 19.53 ? 339 VAL A CB     1 
ATOM   2377 C CG1    . VAL A 1 345 ? 12.573 -14.167 7.634   1.00 24.12 ? 339 VAL A CG1    1 
ATOM   2378 C CG2    . VAL A 1 345 ? 10.754 -13.492 9.276   1.00 19.81 ? 339 VAL A CG2    1 
ATOM   2379 N N      . SER A 1 346 ? 13.174 -11.244 5.766   1.00 18.19 ? 340 SER A N      1 
ATOM   2380 C CA     . SER A 1 346 ? 13.575 -11.067 4.375   1.00 15.40 ? 340 SER A CA     1 
ATOM   2381 C C      . SER A 1 346 ? 14.427 -12.246 3.924   1.00 20.69 ? 340 SER A C      1 
ATOM   2382 O O      . SER A 1 346 ? 15.221 -12.788 4.700   1.00 22.64 ? 340 SER A O      1 
ATOM   2383 C CB     . SER A 1 346 ? 14.284 -9.731  4.165   1.00 20.79 ? 340 SER A CB     1 
ATOM   2384 O OG     . SER A 1 346 ? 15.584 -9.730  4.739   1.00 22.25 ? 340 SER A OG     1 
ATOM   2385 N N      . TYR A 1 347 ? 14.218 -12.666 2.677   1.00 20.26 ? 341 TYR A N      1 
ATOM   2386 C CA     . TYR A 1 347 ? 14.922 -13.787 2.063   1.00 20.26 ? 341 TYR A CA     1 
ATOM   2387 C C      . TYR A 1 347 ? 15.668 -13.276 0.841   1.00 21.87 ? 341 TYR A C      1 
ATOM   2388 O O      . TYR A 1 347 ? 15.110 -12.524 0.037   1.00 21.99 ? 341 TYR A O      1 
ATOM   2389 C CB     . TYR A 1 347 ? 13.946 -14.905 1.658   1.00 20.95 ? 341 TYR A CB     1 
ATOM   2390 C CG     . TYR A 1 347 ? 13.278 -15.565 2.851   1.00 21.39 ? 341 TYR A CG     1 
ATOM   2391 C CD1    . TYR A 1 347 ? 12.147 -15.007 3.442   1.00 21.83 ? 341 TYR A CD1    1 
ATOM   2392 C CD2    . TYR A 1 347 ? 13.788 -16.741 3.388   1.00 22.63 ? 341 TYR A CD2    1 
ATOM   2393 C CE1    . TYR A 1 347 ? 11.554 -15.605 4.546   1.00 24.18 ? 341 TYR A CE1    1 
ATOM   2394 C CE2    . TYR A 1 347 ? 13.202 -17.343 4.491   1.00 22.47 ? 341 TYR A CE2    1 
ATOM   2395 C CZ     . TYR A 1 347 ? 12.078 -16.776 5.061   1.00 24.34 ? 341 TYR A CZ     1 
ATOM   2396 O OH     . TYR A 1 347 ? 11.487 -17.368 6.166   1.00 24.65 ? 341 TYR A OH     1 
ATOM   2397 N N      . GLY A 1 348 ? 16.929 -13.668 0.720   1.00 19.79 ? 342 GLY A N      1 
ATOM   2398 C CA     . GLY A 1 348 ? 17.731 -13.299 -0.426  1.00 23.29 ? 342 GLY A CA     1 
ATOM   2399 C C      . GLY A 1 348 ? 17.931 -14.423 -1.423  1.00 20.75 ? 342 GLY A C      1 
ATOM   2400 O O      . GLY A 1 348 ? 17.203 -14.521 -2.414  1.00 22.38 ? 342 GLY A O      1 
ATOM   2401 N N      . ARG A 1 349 ? 18.925 -15.278 -1.164  1.00 22.53 ? 343 ARG A N      1 
ATOM   2402 C CA     . ARG A 1 349 ? 19.330 -16.277 -2.153  1.00 23.93 ? 343 ARG A CA     1 
ATOM   2403 C C      . ARG A 1 349 ? 18.168 -17.168 -2.584  1.00 22.20 ? 343 ARG A C      1 
ATOM   2404 O O      . ARG A 1 349 ? 18.033 -17.481 -3.773  1.00 20.96 ? 343 ARG A O      1 
ATOM   2405 C CB     . ARG A 1 349 ? 20.505 -17.101 -1.614  1.00 22.83 ? 343 ARG A CB     1 
ATOM   2406 C CG     . ARG A 1 349 ? 21.816 -16.330 -1.632  1.00 27.30 ? 343 ARG A CG     1 
ATOM   2407 C CD     . ARG A 1 349 ? 22.881 -16.948 -0.732  1.00 28.06 ? 343 ARG A CD     1 
ATOM   2408 N NE     . ARG A 1 349 ? 22.504 -16.962 0.675   1.00 25.62 ? 343 ARG A NE     1 
ATOM   2409 C CZ     . ARG A 1 349 ? 23.158 -17.642 1.607   1.00 27.52 ? 343 ARG A CZ     1 
ATOM   2410 N NH1    . ARG A 1 349 ? 24.240 -18.347 1.312   1.00 34.66 ? 343 ARG A NH1    1 
ATOM   2411 N NH2    . ARG A 1 349 ? 22.727 -17.600 2.865   1.00 31.71 ? 343 ARG A NH2    1 
ATOM   2412 N N      . LEU A 1 350 ? 17.299 -17.572 -1.649  1.00 24.68 ? 344 LEU A N      1 
ATOM   2413 C CA     . LEU A 1 350 ? 16.190 -18.443 -2.043  1.00 22.41 ? 344 LEU A CA     1 
ATOM   2414 C C      . LEU A 1 350 ? 15.183 -17.721 -2.930  1.00 20.50 ? 344 LEU A C      1 
ATOM   2415 O O      . LEU A 1 350 ? 14.497 -18.367 -3.734  1.00 21.96 ? 344 LEU A O      1 
ATOM   2416 C CB     . LEU A 1 350 ? 15.506 -19.063 -0.825  1.00 22.88 ? 344 LEU A CB     1 
ATOM   2417 C CG     . LEU A 1 350 ? 16.303 -20.158 -0.106  1.00 31.01 ? 344 LEU A CG     1 
ATOM   2418 C CD1    . LEU A 1 350 ? 15.633 -20.502 1.217   1.00 28.81 ? 344 LEU A CD1    1 
ATOM   2419 C CD2    . LEU A 1 350 ? 16.462 -21.396 -0.964  1.00 31.31 ? 344 LEU A CD2    1 
ATOM   2420 N N      . PHE A 1 351 ? 15.091 -16.393 -2.809  1.00 20.71 ? 345 PHE A N      1 
ATOM   2421 C CA     . PHE A 1 351 ? 14.243 -15.606 -3.699  1.00 20.90 ? 345 PHE A CA     1 
ATOM   2422 C C      . PHE A 1 351 ? 14.845 -15.467 -5.097  1.00 22.73 ? 345 PHE A C      1 
ATOM   2423 O O      . PHE A 1 351 ? 14.105 -15.227 -6.057  1.00 23.53 ? 345 PHE A O      1 
ATOM   2424 C CB     . PHE A 1 351 ? 13.973 -14.231 -3.072  1.00 24.40 ? 345 PHE A CB     1 
ATOM   2425 C CG     . PHE A 1 351 ? 12.507 -13.922 -2.861  1.00 23.71 ? 345 PHE A CG     1 
ATOM   2426 C CD1    . PHE A 1 351 ? 11.586 -14.124 -3.872  1.00 22.94 ? 345 PHE A CD1    1 
ATOM   2427 C CD2    . PHE A 1 351 ? 12.062 -13.408 -1.649  1.00 23.17 ? 345 PHE A CD2    1 
ATOM   2428 C CE1    . PHE A 1 351 ? 10.228 -13.829 -3.675  1.00 23.28 ? 345 PHE A CE1    1 
ATOM   2429 C CE2    . PHE A 1 351 ? 10.714 -13.110 -1.443  1.00 22.56 ? 345 PHE A CE2    1 
ATOM   2430 C CZ     . PHE A 1 351 ? 9.799  -13.314 -2.459  1.00 24.17 ? 345 PHE A CZ     1 
ATOM   2431 N N      . ILE A 1 352 ? 16.167 -15.614 -5.237  1.00 20.81 ? 346 ILE A N      1 
ATOM   2432 C CA     . ILE A 1 352 ? 16.763 -15.635 -6.573  1.00 19.60 ? 346 ILE A CA     1 
ATOM   2433 C C      . ILE A 1 352 ? 16.181 -16.781 -7.391  1.00 23.36 ? 346 ILE A C      1 
ATOM   2434 O O      . ILE A 1 352 ? 15.789 -16.610 -8.554  1.00 23.70 ? 346 ILE A O      1 
ATOM   2435 C CB     . ILE A 1 352 ? 18.299 -15.724 -6.479  1.00 20.21 ? 346 ILE A CB     1 
ATOM   2436 C CG1    . ILE A 1 352 ? 18.876 -14.416 -5.942  1.00 21.95 ? 346 ILE A CG1    1 
ATOM   2437 C CG2    . ILE A 1 352 ? 18.902 -16.018 -7.852  1.00 23.17 ? 346 ILE A CG2    1 
ATOM   2438 C CD1    . ILE A 1 352 ? 20.368 -14.471 -5.651  1.00 24.85 ? 346 ILE A CD1    1 
ATOM   2439 N N      . SER A 1 353 ? 16.100 -17.967 -6.793  1.00 20.73 ? 347 SER A N      1 
ATOM   2440 C CA     . SER A 1 353 ? 15.776 -19.172 -7.547  1.00 22.29 ? 347 SER A CA     1 
ATOM   2441 C C      . SER A 1 353 ? 14.329 -19.618 -7.409  1.00 26.68 ? 347 SER A C      1 
ATOM   2442 O O      . SER A 1 353 ? 13.915 -20.546 -8.113  1.00 23.38 ? 347 SER A O      1 
ATOM   2443 C CB     . SER A 1 353 ? 16.702 -20.323 -7.139  1.00 22.61 ? 347 SER A CB     1 
ATOM   2444 O OG     . SER A 1 353 ? 16.693 -20.533 -5.741  1.00 23.48 ? 347 SER A OG     1 
ATOM   2445 N N      . ASN A 1 354 ? 13.553 -18.993 -6.527  1.00 24.53 ? 348 ASN A N      1 
ATOM   2446 C CA     . ASN A 1 354 ? 12.148 -19.345 -6.327  1.00 24.10 ? 348 ASN A CA     1 
ATOM   2447 C C      . ASN A 1 354 ? 11.340 -18.071 -6.504  1.00 26.83 ? 348 ASN A C      1 
ATOM   2448 O O      . ASN A 1 354 ? 11.147 -17.314 -5.541  1.00 22.49 ? 348 ASN A O      1 
ATOM   2449 C CB     . ASN A 1 354 ? 11.936 -19.955 -4.942  1.00 21.68 ? 348 ASN A CB     1 
ATOM   2450 C CG     . ASN A 1 354 ? 12.703 -21.241 -4.770  1.00 21.13 ? 348 ASN A CG     1 
ATOM   2451 O OD1    . ASN A 1 354 ? 12.210 -22.315 -5.110  1.00 24.35 ? 348 ASN A OD1    1 
ATOM   2452 N ND2    . ASN A 1 354 ? 13.942 -21.138 -4.277  1.00 20.78 ? 348 ASN A ND2    1 
ATOM   2453 N N      . PRO A 1 355 ? 10.879 -17.781 -7.726  1.00 23.95 ? 349 PRO A N      1 
ATOM   2454 C CA     . PRO A 1 355 ? 10.138 -16.527 -7.926  1.00 19.71 ? 349 PRO A CA     1 
ATOM   2455 C C      . PRO A 1 355 ? 8.877  -16.496 -7.090  1.00 23.11 ? 349 PRO A C      1 
ATOM   2456 O O      . PRO A 1 355 ? 8.494  -15.442 -6.569  1.00 23.84 ? 349 PRO A O      1 
ATOM   2457 C CB     . PRO A 1 355 ? 9.849  -16.510 -9.442  1.00 22.59 ? 349 PRO A CB     1 
ATOM   2458 C CG     . PRO A 1 355 ? 10.039 -17.924 -9.897  1.00 22.65 ? 349 PRO A CG     1 
ATOM   2459 C CD     . PRO A 1 355 ? 11.106 -18.494 -8.999  1.00 22.82 ? 349 PRO A CD     1 
ATOM   2460 N N      . ASP A 1 356 ? 8.259  -17.659 -6.903  1.00 23.71 ? 350 ASP A N      1 
ATOM   2461 C CA     . ASP A 1 356 ? 7.089  -17.829 -6.047  1.00 23.26 ? 350 ASP A CA     1 
ATOM   2462 C C      . ASP A 1 356 ? 7.474  -18.315 -4.656  1.00 26.30 ? 350 ASP A C      1 
ATOM   2463 O O      . ASP A 1 356 ? 6.815  -19.184 -4.082  1.00 24.51 ? 350 ASP A O      1 
ATOM   2464 C CB     . ASP A 1 356 ? 6.067  -18.752 -6.719  1.00 24.51 ? 350 ASP A CB     1 
ATOM   2465 C CG     . ASP A 1 356 ? 6.670  -20.078 -7.208  1.00 26.90 ? 350 ASP A CG     1 
ATOM   2466 O OD1    . ASP A 1 356 ? 7.913  -20.270 -7.134  1.00 25.14 ? 350 ASP A OD1    1 
ATOM   2467 O OD2    . ASP A 1 356 ? 5.883  -20.927 -7.693  1.00 28.20 ? 350 ASP A OD2    1 
ATOM   2468 N N      . LEU A 1 357 ? 8.549  -17.749 -4.096  1.00 24.85 ? 351 LEU A N      1 
ATOM   2469 C CA     . LEU A 1 357 ? 8.991  -18.131 -2.757  1.00 21.29 ? 351 LEU A CA     1 
ATOM   2470 C C      . LEU A 1 357 ? 7.869  -18.010 -1.733  1.00 24.32 ? 351 LEU A C      1 
ATOM   2471 O O      . LEU A 1 357 ? 7.719  -18.884 -0.874  1.00 25.37 ? 351 LEU A O      1 
ATOM   2472 C CB     . LEU A 1 357 ? 10.200 -17.298 -2.321  1.00 20.52 ? 351 LEU A CB     1 
ATOM   2473 C CG     . LEU A 1 357 ? 10.754 -17.731 -0.955  1.00 20.82 ? 351 LEU A CG     1 
ATOM   2474 C CD1    . LEU A 1 357 ? 11.135 -19.206 -0.927  1.00 24.64 ? 351 LEU A CD1    1 
ATOM   2475 C CD2    . LEU A 1 357 ? 11.920 -16.859 -0.536  1.00 22.85 ? 351 LEU A CD2    1 
ATOM   2476 N N      . VAL A 1 358 ? 7.076  -16.931 -1.804  1.00 23.59 ? 352 VAL A N      1 
ATOM   2477 C CA     . VAL A 1 358 ? 6.004  -16.727 -0.823  1.00 23.54 ? 352 VAL A CA     1 
ATOM   2478 C C      . VAL A 1 358 ? 5.041  -17.904 -0.845  1.00 22.11 ? 352 VAL A C      1 
ATOM   2479 O O      . VAL A 1 358 ? 4.719  -18.488 0.196   1.00 24.03 ? 352 VAL A O      1 
ATOM   2480 C CB     . VAL A 1 358 ? 5.264  -15.401 -1.090  1.00 24.15 ? 352 VAL A CB     1 
ATOM   2481 C CG1    . VAL A 1 358 ? 4.113  -15.220 -0.088  1.00 25.30 ? 352 VAL A CG1    1 
ATOM   2482 C CG2    . VAL A 1 358 ? 6.222  -14.212 -1.054  1.00 23.91 ? 352 VAL A CG2    1 
ATOM   2483 N N      . MET A 1 359 ? 4.580  -18.277 -2.039  1.00 24.21 ? 353 MET A N      1 
ATOM   2484 C CA     . MET A 1 359 ? 3.659  -19.399 -2.146  1.00 25.32 ? 353 MET A CA     1 
ATOM   2485 C C      . MET A 1 359 ? 4.309  -20.713 -1.722  1.00 28.92 ? 353 MET A C      1 
ATOM   2486 O O      . MET A 1 359 ? 3.658  -21.559 -1.101  1.00 27.88 ? 353 MET A O      1 
ATOM   2487 C CB     . MET A 1 359 ? 3.056  -19.461 -3.549  1.00 29.83 ? 353 MET A CB     1 
ATOM   2488 C CG     . MET A 1 359 ? 2.224  -20.698 -3.761  1.00 32.67 ? 353 MET A CG     1 
ATOM   2489 S SD     . MET A 1 359 ? 0.520  -20.426 -3.204  1.00 51.99 ? 353 MET A SD     1 
ATOM   2490 C CE     . MET A 1 359 ? 0.386  -18.635 -3.210  1.00 40.90 ? 353 MET A CE     1 
ATOM   2491 N N      . ARG A 1 360 ? 5.593  -20.902 -2.026  1.00 25.69 ? 354 ARG A N      1 
ATOM   2492 C CA     . ARG A 1 360 ? 6.254  -22.131 -1.600  1.00 24.72 ? 354 ARG A CA     1 
ATOM   2493 C C      . ARG A 1 360 ? 6.362  -22.207 -0.083  1.00 27.26 ? 354 ARG A C      1 
ATOM   2494 O O      . ARG A 1 360 ? 6.244  -23.288 0.503   1.00 27.73 ? 354 ARG A O      1 
ATOM   2495 C CB     . ARG A 1 360 ? 7.636  -22.223 -2.244  1.00 24.61 ? 354 ARG A CB     1 
ATOM   2496 C CG     . ARG A 1 360 ? 7.560  -22.432 -3.728  1.00 26.92 ? 354 ARG A CG     1 
ATOM   2497 C CD     . ARG A 1 360 ? 8.907  -22.787 -4.284  1.00 25.22 ? 354 ARG A CD     1 
ATOM   2498 N NE     . ARG A 1 360 ? 8.903  -22.576 -5.721  1.00 22.40 ? 354 ARG A NE     1 
ATOM   2499 C CZ     . ARG A 1 360 ? 9.411  -23.421 -6.605  1.00 25.65 ? 354 ARG A CZ     1 
ATOM   2500 N NH1    . ARG A 1 360 ? 9.991  -24.548 -6.229  1.00 26.10 ? 354 ARG A NH1    1 
ATOM   2501 N NH2    . ARG A 1 360 ? 9.328  -23.130 -7.898  1.00 29.14 ? 354 ARG A NH2    1 
ATOM   2502 N N      . ILE A 1 361 ? 6.605  -21.070 0.568   1.00 24.25 ? 355 ILE A N      1 
ATOM   2503 C CA     . ILE A 1 361 ? 6.622  -21.043 2.023   1.00 27.35 ? 355 ILE A CA     1 
ATOM   2504 C C      . ILE A 1 361 ? 5.227  -21.331 2.568   1.00 26.14 ? 355 ILE A C      1 
ATOM   2505 O O      . ILE A 1 361 ? 5.070  -22.065 3.553   1.00 29.22 ? 355 ILE A O      1 
ATOM   2506 C CB     . ILE A 1 361 ? 7.207  -19.705 2.518   1.00 23.94 ? 355 ILE A CB     1 
ATOM   2507 C CG1    . ILE A 1 361 ? 8.728  -19.687 2.318   1.00 23.88 ? 355 ILE A CG1    1 
ATOM   2508 C CG2    . ILE A 1 361 ? 6.864  -19.451 3.991   1.00 25.05 ? 355 ILE A CG2    1 
ATOM   2509 C CD1    . ILE A 1 361 ? 9.361  -18.325 2.542   1.00 23.87 ? 355 ILE A CD1    1 
ATOM   2510 N N      . LYS A 1 362 ? 4.192  -20.801 1.908   1.00 24.05 ? 356 LYS A N      1 
ATOM   2511 C CA     . LYS A 1 362 ? 2.819  -21.041 2.355   1.00 26.58 ? 356 LYS A CA     1 
ATOM   2512 C C      . LYS A 1 362 ? 2.466  -22.521 2.292   1.00 33.75 ? 356 LYS A C      1 
ATOM   2513 O O      . LYS A 1 362 ? 1.878  -23.069 3.233   1.00 31.67 ? 356 LYS A O      1 
ATOM   2514 C CB     . LYS A 1 362 ? 1.838  -20.229 1.508   1.00 26.61 ? 356 LYS A CB     1 
ATOM   2515 C CG     . LYS A 1 362 ? 0.465  -20.038 2.149   1.00 39.17 ? 356 LYS A CG     1 
ATOM   2516 C CD     . LYS A 1 362 ? -0.569 -19.622 1.120   1.00 41.00 ? 356 LYS A CD     1 
ATOM   2517 C CE     . LYS A 1 362 ? -1.919 -19.333 1.765   1.00 49.53 ? 356 LYS A CE     1 
ATOM   2518 N NZ     . LYS A 1 362 ? -1.949 -19.685 3.215   1.00 50.36 ? 356 LYS A NZ     1 
ATOM   2519 N N      . LEU A 1 363 ? 2.823  -23.181 1.192   1.00 29.28 ? 357 LEU A N      1 
ATOM   2520 C CA     . LEU A 1 363 ? 2.478  -24.573 0.951   1.00 30.42 ? 357 LEU A CA     1 
ATOM   2521 C C      . LEU A 1 363 ? 3.496  -25.547 1.521   1.00 30.33 ? 357 LEU A C      1 
ATOM   2522 O O      . LEU A 1 363 ? 3.250  -26.759 1.491   1.00 31.05 ? 357 LEU A O      1 
ATOM   2523 C CB     . LEU A 1 363 ? 2.377  -24.823 -0.557  1.00 29.12 ? 357 LEU A CB     1 
ATOM   2524 C CG     . LEU A 1 363 ? 1.351  -24.011 -1.347  1.00 29.96 ? 357 LEU A CG     1 
ATOM   2525 C CD1    . LEU A 1 363 ? 1.550  -24.261 -2.828  1.00 34.25 ? 357 LEU A CD1    1 
ATOM   2526 C CD2    . LEU A 1 363 ? -0.064 -24.372 -0.946  1.00 38.04 ? 357 LEU A CD2    1 
ATOM   2527 N N      . ASN A 1 364 ? 4.626  -25.053 2.030   1.00 27.12 ? 358 ASN A N      1 
ATOM   2528 C CA     . ASN A 1 364 ? 5.763  -25.904 2.385   1.00 29.68 ? 358 ASN A CA     1 
ATOM   2529 C C      . ASN A 1 364 ? 6.175  -26.781 1.205   1.00 30.31 ? 358 ASN A C      1 
ATOM   2530 O O      . ASN A 1 364 ? 6.437  -27.978 1.351   1.00 29.65 ? 358 ASN A O      1 
ATOM   2531 C CB     . ASN A 1 364 ? 5.513  -26.736 3.645   1.00 30.69 ? 358 ASN A CB     1 
ATOM   2532 C CG     . ASN A 1 364 ? 6.796  -27.291 4.229   1.00 35.57 ? 358 ASN A CG     1 
ATOM   2533 O OD1    . ASN A 1 364 ? 7.891  -26.832 3.894   1.00 33.77 ? 358 ASN A OD1    1 
ATOM   2534 N ND2    . ASN A 1 364 ? 6.672  -28.294 5.091   1.00 37.84 ? 358 ASN A ND2    1 
ATOM   2535 N N      . ALA A 1 365 ? 6.220  -26.168 0.009   1.00 29.34 ? 359 ALA A N      1 
ATOM   2536 C CA     . ALA A 1 365 ? 6.624  -26.832 -1.215  1.00 30.34 ? 359 ALA A CA     1 
ATOM   2537 C C      . ALA A 1 365 ? 8.144  -26.805 -1.343  1.00 28.67 ? 359 ALA A C      1 
ATOM   2538 O O      . ALA A 1 365 ? 8.798  -25.895 -0.830  1.00 28.30 ? 359 ALA A O      1 
ATOM   2539 C CB     . ALA A 1 365 ? 6.011  -26.119 -2.421  1.00 26.87 ? 359 ALA A CB     1 
ATOM   2540 N N      . PRO A 1 366 ? 8.728  -27.791 -2.029  1.00 29.46 ? 360 PRO A N      1 
ATOM   2541 C CA     . PRO A 1 366 ? 10.190 -27.826 -2.173  1.00 29.41 ? 360 PRO A CA     1 
ATOM   2542 C C      . PRO A 1 366 ? 10.716 -26.627 -2.953  1.00 28.31 ? 360 PRO A C      1 
ATOM   2543 O O      . PRO A 1 366 ? 10.069 -26.121 -3.872  1.00 29.11 ? 360 PRO A O      1 
ATOM   2544 C CB     . PRO A 1 366 ? 10.439 -29.131 -2.939  1.00 32.18 ? 360 PRO A CB     1 
ATOM   2545 C CG     . PRO A 1 366 ? 9.220  -29.956 -2.716  1.00 38.75 ? 360 PRO A CG     1 
ATOM   2546 C CD     . PRO A 1 366 ? 8.083  -28.992 -2.590  1.00 33.59 ? 360 PRO A CD     1 
ATOM   2547 N N      . LEU A 1 367 ? 11.918 -26.190 -2.583  1.00 25.88 ? 361 LEU A N      1 
ATOM   2548 C CA     . LEU A 1 367 ? 12.539 -24.997 -3.142  1.00 25.53 ? 361 LEU A CA     1 
ATOM   2549 C C      . LEU A 1 367 ? 13.575 -25.363 -4.198  1.00 24.15 ? 361 LEU A C      1 
ATOM   2550 O O      . LEU A 1 367 ? 14.209 -26.421 -4.132  1.00 24.98 ? 361 LEU A O      1 
ATOM   2551 C CB     . LEU A 1 367 ? 13.225 -24.185 -2.041  1.00 26.19 ? 361 LEU A CB     1 
ATOM   2552 C CG     . LEU A 1 367 ? 12.365 -23.848 -0.820  1.00 25.09 ? 361 LEU A CG     1 
ATOM   2553 C CD1    . LEU A 1 367 ? 13.141 -22.968 0.139   1.00 28.11 ? 361 LEU A CD1    1 
ATOM   2554 C CD2    . LEU A 1 367 ? 11.089 -23.162 -1.272  1.00 28.07 ? 361 LEU A CD2    1 
ATOM   2555 N N      . ASN A 1 368 ? 13.753 -24.457 -5.163  1.00 23.39 ? 362 ASN A N      1 
ATOM   2556 C CA     . ASN A 1 368 ? 14.727 -24.627 -6.236  1.00 23.84 ? 362 ASN A CA     1 
ATOM   2557 C C      . ASN A 1 368 ? 16.109 -24.174 -5.785  1.00 26.38 ? 362 ASN A C      1 
ATOM   2558 O O      . ASN A 1 368 ? 16.254 -23.189 -5.054  1.00 24.18 ? 362 ASN A O      1 
ATOM   2559 C CB     . ASN A 1 368 ? 14.366 -23.731 -7.415  1.00 24.62 ? 362 ASN A CB     1 
ATOM   2560 C CG     . ASN A 1 368 ? 13.084 -24.130 -8.104  1.00 25.62 ? 362 ASN A CG     1 
ATOM   2561 O OD1    . ASN A 1 368 ? 12.616 -25.267 -8.003  1.00 29.27 ? 362 ASN A OD1    1 
ATOM   2562 N ND2    . ASN A 1 368 ? 12.517 -23.187 -8.849  1.00 29.27 ? 362 ASN A ND2    1 
ATOM   2563 N N      . LYS A 1 369 ? 17.137 -24.864 -6.283  1.00 24.96 ? 363 LYS A N      1 
ATOM   2564 C CA     . LYS A 1 369 ? 18.504 -24.430 -6.031  1.00 24.10 ? 363 LYS A CA     1 
ATOM   2565 C C      . LYS A 1 369 ? 18.800 -23.159 -6.817  1.00 25.36 ? 363 LYS A C      1 
ATOM   2566 O O      . LYS A 1 369 ? 18.207 -22.900 -7.868  1.00 27.26 ? 363 LYS A O      1 
ATOM   2567 C CB     . LYS A 1 369 ? 19.502 -25.519 -6.431  1.00 25.18 ? 363 LYS A CB     1 
ATOM   2568 C CG     . LYS A 1 369 ? 19.469 -25.889 -7.910  1.00 31.04 ? 363 LYS A CG     1 
ATOM   2569 C CD     . LYS A 1 369 ? 20.765 -26.543 -8.372  1.00 39.85 ? 363 LYS A CD     1 
ATOM   2570 C CE     . LYS A 1 369 ? 21.355 -27.456 -7.321  1.00 49.62 ? 363 LYS A CE     1 
ATOM   2571 N NZ     . LYS A 1 369 ? 20.734 -28.822 -7.331  1.00 41.01 ? 363 LYS A NZ     1 
ATOM   2572 N N      . TYR A 1 370 ? 19.727 -22.361 -6.299  1.00 25.26 ? 364 TYR A N      1 
ATOM   2573 C CA     . TYR A 1 370 ? 20.200 -21.175 -6.993  1.00 27.30 ? 364 TYR A CA     1 
ATOM   2574 C C      . TYR A 1 370 ? 21.594 -21.430 -7.552  1.00 29.17 ? 364 TYR A C      1 
ATOM   2575 O O      . TYR A 1 370 ? 22.337 -22.286 -7.063  1.00 30.25 ? 364 TYR A O      1 
ATOM   2576 C CB     . TYR A 1 370 ? 20.200 -19.945 -6.074  1.00 24.30 ? 364 TYR A CB     1 
ATOM   2577 C CG     . TYR A 1 370 ? 20.841 -20.156 -4.725  1.00 28.75 ? 364 TYR A CG     1 
ATOM   2578 C CD1    . TYR A 1 370 ? 22.221 -20.069 -4.568  1.00 32.84 ? 364 TYR A CD1    1 
ATOM   2579 C CD2    . TYR A 1 370 ? 20.065 -20.429 -3.597  1.00 29.55 ? 364 TYR A CD2    1 
ATOM   2580 C CE1    . TYR A 1 370 ? 22.813 -20.254 -3.327  1.00 32.76 ? 364 TYR A CE1    1 
ATOM   2581 C CE2    . TYR A 1 370 ? 20.651 -20.616 -2.351  1.00 29.03 ? 364 TYR A CE2    1 
ATOM   2582 C CZ     . TYR A 1 370 ? 22.027 -20.533 -2.230  1.00 28.57 ? 364 TYR A CZ     1 
ATOM   2583 O OH     . TYR A 1 370 ? 22.611 -20.715 -0.991  1.00 37.91 ? 364 TYR A OH     1 
ATOM   2584 N N      . ASN A 1 371 ? 21.856 -20.743 -8.653  1.00 26.11 ? 365 ASN A N      1 
ATOM   2585 C CA     A ASN A 1 371 ? 23.213 -20.836 -9.290  0.61 25.68 ? 365 ASN A CA     1 
ATOM   2586 C CA     B ASN A 1 371 ? 23.202 -20.796 -9.299  0.39 25.68 ? 365 ASN A CA     1 
ATOM   2587 C C      . ASN A 1 371 ? 24.101 -19.527 -9.108  1.00 24.61 ? 365 ASN A C      1 
ATOM   2588 O O      . ASN A 1 371 ? 23.982 -18.357 -9.690  1.00 24.39 ? 365 ASN A O      1 
ATOM   2589 C CB     A ASN A 1 371 ? 22.954 -21.087 -10.773 0.61 29.81 ? 365 ASN A CB     1 
ATOM   2590 C CB     B ASN A 1 371 ? 23.003 -21.069 -10.794 0.39 29.81 ? 365 ASN A CB     1 
ATOM   2591 C CG     A ASN A 1 371 ? 22.027 -22.271 -11.000 0.61 43.76 ? 365 ASN A CG     1 
ATOM   2592 C CG     B ASN A 1 371 ? 24.271 -21.045 -11.619 0.39 43.76 ? 365 ASN A CG     1 
ATOM   2593 O OD1    A ASN A 1 371 ? 21.049 -22.180 -11.747 0.61 46.83 ? 365 ASN A OD1    1 
ATOM   2594 O OD1    B ASN A 1 371 ? 25.278 -21.631 -11.239 0.39 46.83 ? 365 ASN A OD1    1 
ATOM   2595 N ND2    A ASN A 1 371 ? 22.328 -23.390 -10.344 0.61 44.60 ? 365 ASN A ND2    1 
ATOM   2596 N ND2    B ASN A 1 371 ? 24.224 -20.400 -12.771 0.39 44.60 ? 365 ASN A ND2    1 
ATOM   2597 N N      . ARG A 1 372 ? 25.055 -19.696 -8.192  1.00 24.22 ? 366 ARG A N      1 
ATOM   2598 C CA     . ARG A 1 372 ? 25.925 -18.566 -7.878  1.00 24.02 ? 366 ARG A CA     1 
ATOM   2599 C C      . ARG A 1 372 ? 26.576 -17.983 -9.127  1.00 23.70 ? 366 ARG A C      1 
ATOM   2600 O O      . ARG A 1 372 ? 26.804 -16.769 -9.198  1.00 23.68 ? 366 ARG A O      1 
ATOM   2601 C CB     . ARG A 1 372 ? 27.001 -19.007 -6.889  1.00 27.94 ? 366 ARG A CB     1 
ATOM   2602 C CG     . ARG A 1 372 ? 28.018 -17.927 -6.541  1.00 31.49 ? 366 ARG A CG     1 
ATOM   2603 C CD     . ARG A 1 372 ? 28.695 -18.207 -5.194  1.00 37.01 ? 366 ARG A CD     1 
ATOM   2604 N NE     . ARG A 1 372 ? 27.753 -18.178 -4.078  1.00 48.00 ? 366 ARG A NE     1 
ATOM   2605 C CZ     . ARG A 1 372 ? 27.530 -17.115 -3.315  1.00 37.99 ? 366 ARG A CZ     1 
ATOM   2606 N NH1    . ARG A 1 372 ? 28.160 -15.970 -3.524  1.00 46.20 ? 366 ARG A NH1    1 
ATOM   2607 N NH2    . ARG A 1 372 ? 26.648 -17.202 -2.321  1.00 37.52 ? 366 ARG A NH2    1 
ATOM   2608 N N      . LYS A 1 373 ? 26.871 -18.823 -10.125 1.00 25.04 ? 367 LYS A N      1 
ATOM   2609 C CA     . LYS A 1 373 ? 27.577 -18.342 -11.308 1.00 26.66 ? 367 LYS A CA     1 
ATOM   2610 C C      . LYS A 1 373 ? 26.815 -17.230 -12.022 1.00 24.76 ? 367 LYS A C      1 
ATOM   2611 O O      . LYS A 1 373 ? 27.431 -16.394 -12.695 1.00 27.71 ? 367 LYS A O      1 
ATOM   2612 C CB     . LYS A 1 373 ? 27.862 -19.505 -12.262 1.00 27.82 ? 367 LYS A CB     1 
ATOM   2613 N N      . THR A 1 374 ? 25.489 -17.188 -11.884 1.00 22.48 ? 368 THR A N      1 
ATOM   2614 C CA     . THR A 1 374 ? 24.683 -16.192 -12.588 1.00 21.61 ? 368 THR A CA     1 
ATOM   2615 C C      . THR A 1 374 ? 24.089 -15.136 -11.658 1.00 21.91 ? 368 THR A C      1 
ATOM   2616 O O      . THR A 1 374 ? 23.132 -14.448 -12.032 1.00 21.20 ? 368 THR A O      1 
ATOM   2617 C CB     . THR A 1 374 ? 23.621 -16.845 -13.476 1.00 24.37 ? 368 THR A CB     1 
ATOM   2618 O OG1    . THR A 1 374 ? 22.868 -17.796 -12.716 1.00 28.26 ? 368 THR A OG1    1 
ATOM   2619 C CG2    . THR A 1 374 ? 24.289 -17.547 -14.660 1.00 24.81 ? 368 THR A CG2    1 
ATOM   2620 N N      . PHE A 1 375 ? 24.663 -14.971 -10.464 1.00 22.97 ? 369 PHE A N      1 
ATOM   2621 C CA     . PHE A 1 375 ? 24.214 -13.908 -9.569  1.00 21.96 ? 369 PHE A CA     1 
ATOM   2622 C C      . PHE A 1 375 ? 24.428 -12.532 -10.187 1.00 21.96 ? 369 PHE A C      1 
ATOM   2623 O O      . PHE A 1 375 ? 23.542 -11.672 -10.120 1.00 21.05 ? 369 PHE A O      1 
ATOM   2624 C CB     . PHE A 1 375 ? 24.977 -13.977 -8.249  1.00 21.09 ? 369 PHE A CB     1 
ATOM   2625 C CG     . PHE A 1 375 ? 24.433 -14.978 -7.254  1.00 23.55 ? 369 PHE A CG     1 
ATOM   2626 C CD1    . PHE A 1 375 ? 23.385 -15.830 -7.577  1.00 24.38 ? 369 PHE A CD1    1 
ATOM   2627 C CD2    . PHE A 1 375 ? 24.995 -15.066 -5.990  1.00 23.68 ? 369 PHE A CD2    1 
ATOM   2628 C CE1    . PHE A 1 375 ? 22.905 -16.746 -6.646  1.00 29.87 ? 369 PHE A CE1    1 
ATOM   2629 C CE2    . PHE A 1 375 ? 24.515 -15.978 -5.059  1.00 23.55 ? 369 PHE A CE2    1 
ATOM   2630 C CZ     . PHE A 1 375 ? 23.474 -16.814 -5.386  1.00 25.48 ? 369 PHE A CZ     1 
ATOM   2631 N N      . TYR A 1 376 ? 25.583 -12.316 -10.839 1.00 20.53 ? 370 TYR A N      1 
ATOM   2632 C CA     . TYR A 1 376 ? 26.021 -10.976 -11.230 1.00 19.02 ? 370 TYR A CA     1 
ATOM   2633 C C      . TYR A 1 376 ? 26.303 -10.863 -12.721 1.00 21.43 ? 370 TYR A C      1 
ATOM   2634 O O      . TYR A 1 376 ? 26.966 -9.911  -13.149 1.00 21.28 ? 370 TYR A O      1 
ATOM   2635 C CB     . TYR A 1 376 ? 27.263 -10.532 -10.459 1.00 19.55 ? 370 TYR A CB     1 
ATOM   2636 C CG     . TYR A 1 376 ? 27.142 -10.662 -8.958  1.00 18.48 ? 370 TYR A CG     1 
ATOM   2637 C CD1    . TYR A 1 376 ? 26.254 -9.866  -8.253  1.00 21.05 ? 370 TYR A CD1    1 
ATOM   2638 C CD2    . TYR A 1 376 ? 27.963 -11.534 -8.248  1.00 22.00 ? 370 TYR A CD2    1 
ATOM   2639 C CE1    . TYR A 1 376 ? 26.141 -9.971  -6.882  1.00 22.76 ? 370 TYR A CE1    1 
ATOM   2640 C CE2    . TYR A 1 376 ? 27.863 -11.647 -6.859  1.00 21.90 ? 370 TYR A CE2    1 
ATOM   2641 C CZ     . TYR A 1 376 ? 26.950 -10.854 -6.193  1.00 21.36 ? 370 TYR A CZ     1 
ATOM   2642 O OH     . TYR A 1 376 ? 26.836 -10.946 -4.820  1.00 23.73 ? 370 TYR A OH     1 
ATOM   2643 N N      . THR A 1 377 ? 25.806 -11.804 -13.509 1.00 18.77 ? 371 THR A N      1 
ATOM   2644 C CA     . THR A 1 377 ? 25.991 -11.752 -14.952 1.00 22.29 ? 371 THR A CA     1 
ATOM   2645 C C      . THR A 1 377 ? 24.948 -10.819 -15.573 1.00 21.35 ? 371 THR A C      1 
ATOM   2646 O O      . THR A 1 377 ? 24.036 -10.336 -14.891 1.00 23.36 ? 371 THR A O      1 
ATOM   2647 C CB     . THR A 1 377 ? 25.918 -13.161 -15.524 1.00 23.31 ? 371 THR A CB     1 
ATOM   2648 O OG1    . THR A 1 377 ? 24.847 -13.872 -14.898 1.00 23.53 ? 371 THR A OG1    1 
ATOM   2649 C CG2    . THR A 1 377 ? 27.219 -13.901 -15.261 1.00 26.11 ? 371 THR A CG2    1 
ATOM   2650 N N      . GLN A 1 378 ? 25.096 -10.532 -16.879 1.00 19.94 ? 372 GLN A N      1 
ATOM   2651 C CA     . GLN A 1 378 ? 24.280 -9.482  -17.487 1.00 21.44 ? 372 GLN A CA     1 
ATOM   2652 C C      . GLN A 1 378 ? 23.099 -9.981  -18.310 1.00 22.27 ? 372 GLN A C      1 
ATOM   2653 O O      . GLN A 1 378 ? 22.347 -9.147  -18.827 1.00 25.65 ? 372 GLN A O      1 
ATOM   2654 C CB     . GLN A 1 378 ? 25.109 -8.534  -18.366 1.00 23.53 ? 372 GLN A CB     1 
ATOM   2655 C CG     . GLN A 1 378 ? 25.917 -7.499  -17.619 1.00 21.64 ? 372 GLN A CG     1 
ATOM   2656 C CD     . GLN A 1 378 ? 26.821 -8.114  -16.588 1.00 22.04 ? 372 GLN A CD     1 
ATOM   2657 O OE1    . GLN A 1 378 ? 27.880 -8.658  -16.910 1.00 23.87 ? 372 GLN A OE1    1 
ATOM   2658 N NE2    . GLN A 1 378 ? 26.419 -8.028  -15.334 1.00 20.33 ? 372 GLN A NE2    1 
ATOM   2659 N N      . ASP A 1 379 ? 22.925 -11.287 -18.479 1.00 23.41 ? 373 ASP A N      1 
ATOM   2660 C CA     . ASP A 1 379 ? 21.835 -11.773 -19.323 1.00 25.25 ? 373 ASP A CA     1 
ATOM   2661 C C      . ASP A 1 379 ? 20.481 -11.361 -18.759 1.00 23.45 ? 373 ASP A C      1 
ATOM   2662 O O      . ASP A 1 379 ? 20.248 -11.503 -17.548 1.00 23.89 ? 373 ASP A O      1 
ATOM   2663 C CB     . ASP A 1 379 ? 21.874 -13.290 -19.504 1.00 28.41 ? 373 ASP A CB     1 
ATOM   2664 C CG     . ASP A 1 379 ? 21.167 -13.737 -20.771 1.00 24.94 ? 373 ASP A CG     1 
ATOM   2665 O OD1    . ASP A 1 379 ? 19.931 -13.951 -20.715 1.00 24.01 ? 373 ASP A OD1    1 
ATOM   2666 O OD2    . ASP A 1 379 ? 21.825 -13.856 -21.831 1.00 28.52 ? 373 ASP A OD2    1 
ATOM   2667 N N      . PRO A 1 380 ? 19.556 -10.868 -19.590 1.00 21.06 ? 374 PRO A N      1 
ATOM   2668 C CA     . PRO A 1 380 ? 18.249 -10.461 -19.055 1.00 23.34 ? 374 PRO A CA     1 
ATOM   2669 C C      . PRO A 1 380 ? 17.357 -11.624 -18.665 1.00 23.37 ? 374 PRO A C      1 
ATOM   2670 O O      . PRO A 1 380 ? 16.326 -11.390 -18.025 1.00 26.00 ? 374 PRO A O      1 
ATOM   2671 C CB     . PRO A 1 380 ? 17.631 -9.652  -20.204 1.00 24.36 ? 374 PRO A CB     1 
ATOM   2672 C CG     . PRO A 1 380 ? 18.298 -10.207 -21.452 1.00 25.71 ? 374 PRO A CG     1 
ATOM   2673 C CD     . PRO A 1 380 ? 19.712 -10.529 -21.019 1.00 21.80 ? 374 PRO A CD     1 
ATOM   2674 N N      . VAL A 1 381 ? 17.704 -12.857 -19.040 1.00 21.60 ? 375 VAL A N      1 
ATOM   2675 C CA     . VAL A 1 381 ? 16.880 -14.034 -18.787 1.00 21.96 ? 375 VAL A CA     1 
ATOM   2676 C C      . VAL A 1 381 ? 17.644 -15.099 -18.007 1.00 26.51 ? 375 VAL A C      1 
ATOM   2677 O O      . VAL A 1 381 ? 17.208 -15.532 -16.931 1.00 25.44 ? 375 VAL A O      1 
ATOM   2678 C CB     . VAL A 1 381 ? 16.307 -14.614 -20.098 1.00 25.68 ? 375 VAL A CB     1 
ATOM   2679 C CG1    . VAL A 1 381 ? 15.573 -15.915 -19.831 1.00 25.32 ? 375 VAL A CG1    1 
ATOM   2680 C CG2    . VAL A 1 381 ? 15.381 -13.603 -20.749 1.00 27.34 ? 375 VAL A CG2    1 
ATOM   2681 N N      . VAL A 1 382 ? 18.806 -15.510 -18.519 1.00 22.03 ? 376 VAL A N      1 
ATOM   2682 C CA     . VAL A 1 382 ? 19.512 -16.673 -17.985 1.00 22.90 ? 376 VAL A CA     1 
ATOM   2683 C C      . VAL A 1 382 ? 19.953 -16.411 -16.550 1.00 24.69 ? 376 VAL A C      1 
ATOM   2684 O O      . VAL A 1 382 ? 20.700 -15.464 -16.276 1.00 23.64 ? 376 VAL A O      1 
ATOM   2685 C CB     . VAL A 1 382 ? 20.711 -17.021 -18.874 1.00 21.83 ? 376 VAL A CB     1 
ATOM   2686 C CG1    . VAL A 1 382 ? 21.584 -18.058 -18.202 1.00 25.63 ? 376 VAL A CG1    1 
ATOM   2687 C CG2    . VAL A 1 382 ? 20.241 -17.513 -20.251 1.00 26.40 ? 376 VAL A CG2    1 
ATOM   2688 N N      . GLY A 1 383 ? 19.512 -17.268 -15.631 1.00 22.26 ? 377 GLY A N      1 
ATOM   2689 C CA     . GLY A 1 383 ? 19.819 -17.078 -14.224 1.00 20.91 ? 377 GLY A CA     1 
ATOM   2690 C C      . GLY A 1 383 ? 19.142 -15.889 -13.590 1.00 21.81 ? 377 GLY A C      1 
ATOM   2691 O O      . GLY A 1 383 ? 19.510 -15.511 -12.470 1.00 24.20 ? 377 GLY A O      1 
ATOM   2692 N N      . TYR A 1 384 ? 18.140 -15.310 -14.246 1.00 23.17 ? 378 TYR A N      1 
ATOM   2693 C CA     . TYR A 1 384 ? 17.495 -14.101 -13.757 1.00 21.57 ? 378 TYR A CA     1 
ATOM   2694 C C      . TYR A 1 384 ? 15.987 -14.296 -13.701 1.00 25.58 ? 378 TYR A C      1 
ATOM   2695 O O      . TYR A 1 384 ? 15.379 -14.246 -12.624 1.00 23.67 ? 378 TYR A O      1 
ATOM   2696 C CB     . TYR A 1 384 ? 17.902 -12.912 -14.638 1.00 23.96 ? 378 TYR A CB     1 
ATOM   2697 C CG     . TYR A 1 384 ? 17.593 -11.558 -14.041 1.00 23.92 ? 378 TYR A CG     1 
ATOM   2698 C CD1    . TYR A 1 384 ? 17.981 -11.237 -12.735 1.00 24.67 ? 378 TYR A CD1    1 
ATOM   2699 C CD2    . TYR A 1 384 ? 16.886 -10.609 -14.768 1.00 23.27 ? 378 TYR A CD2    1 
ATOM   2700 C CE1    . TYR A 1 384 ? 17.689 -9.985  -12.188 1.00 23.27 ? 378 TYR A CE1    1 
ATOM   2701 C CE2    . TYR A 1 384 ? 16.597 -9.367  -14.236 1.00 22.85 ? 378 TYR A CE2    1 
ATOM   2702 C CZ     . TYR A 1 384 ? 16.986 -9.063  -12.946 1.00 25.04 ? 378 TYR A CZ     1 
ATOM   2703 O OH     . TYR A 1 384 ? 16.689 -7.820  -12.438 1.00 25.14 ? 378 TYR A OH     1 
ATOM   2704 N N      . THR A 1 385 ? 15.368 -14.554 -14.851 1.00 21.23 ? 379 THR A N      1 
ATOM   2705 C CA     . THR A 1 385 ? 13.929 -14.777 -14.911 1.00 24.93 ? 379 THR A CA     1 
ATOM   2706 C C      . THR A 1 385 ? 13.550 -16.188 -15.338 1.00 20.87 ? 379 THR A C      1 
ATOM   2707 O O      . THR A 1 385 ? 12.355 -16.484 -15.456 1.00 25.31 ? 379 THR A O      1 
ATOM   2708 C CB     . THR A 1 385 ? 13.265 -13.772 -15.861 1.00 28.88 ? 379 THR A CB     1 
ATOM   2709 O OG1    . THR A 1 385 ? 13.852 -13.899 -17.151 1.00 24.20 ? 379 THR A OG1    1 
ATOM   2710 C CG2    . THR A 1 385 ? 13.450 -12.350 -15.375 1.00 28.06 ? 379 THR A CG2    1 
ATOM   2711 N N      . ASP A 1 386 ? 14.518 -17.069 -15.565 1.00 21.52 ? 380 ASP A N      1 
ATOM   2712 C CA     . ASP A 1 386 ? 14.228 -18.412 -16.041 1.00 24.07 ? 380 ASP A CA     1 
ATOM   2713 C C      . ASP A 1 386 ? 14.215 -19.461 -14.933 1.00 28.42 ? 380 ASP A C      1 
ATOM   2714 O O      . ASP A 1 386 ? 14.139 -20.661 -15.222 1.00 24.38 ? 380 ASP A O      1 
ATOM   2715 C CB     . ASP A 1 386 ? 15.160 -18.782 -17.205 1.00 22.62 ? 380 ASP A CB     1 
ATOM   2716 C CG     . ASP A 1 386 ? 16.619 -18.849 -16.797 1.00 26.90 ? 380 ASP A CG     1 
ATOM   2717 O OD1    . ASP A 1 386 ? 16.960 -18.487 -15.651 1.00 30.86 ? 380 ASP A OD1    1 
ATOM   2718 O OD2    . ASP A 1 386 ? 17.443 -19.258 -17.650 1.00 31.87 ? 380 ASP A OD2    1 
ATOM   2719 N N      . TYR A 1 387 ? 14.257 -19.046 -13.674 1.00 23.72 ? 381 TYR A N      1 
ATOM   2720 C CA     . TYR A 1 387 ? 14.019 -19.994 -12.601 1.00 23.83 ? 381 TYR A CA     1 
ATOM   2721 C C      . TYR A 1 387 ? 12.525 -20.296 -12.563 1.00 24.45 ? 381 TYR A C      1 
ATOM   2722 O O      . TYR A 1 387 ? 11.707 -19.365 -12.614 1.00 26.13 ? 381 TYR A O      1 
ATOM   2723 C CB     . TYR A 1 387 ? 14.449 -19.385 -11.283 1.00 21.98 ? 381 TYR A CB     1 
ATOM   2724 C CG     . TYR A 1 387 ? 15.941 -19.352 -11.030 1.00 23.22 ? 381 TYR A CG     1 
ATOM   2725 C CD1    . TYR A 1 387 ? 16.627 -20.495 -10.631 1.00 22.06 ? 381 TYR A CD1    1 
ATOM   2726 C CD2    . TYR A 1 387 ? 16.647 -18.165 -11.135 1.00 22.85 ? 381 TYR A CD2    1 
ATOM   2727 C CE1    . TYR A 1 387 ? 17.984 -20.456 -10.360 1.00 25.29 ? 381 TYR A CE1    1 
ATOM   2728 C CE2    . TYR A 1 387 ? 18.009 -18.114 -10.859 1.00 21.58 ? 381 TYR A CE2    1 
ATOM   2729 C CZ     . TYR A 1 387 ? 18.670 -19.264 -10.473 1.00 23.31 ? 381 TYR A CZ     1 
ATOM   2730 O OH     . TYR A 1 387 ? 20.020 -19.218 -10.190 1.00 26.14 ? 381 TYR A OH     1 
ATOM   2731 N N      . PRO A 1 388 ? 12.127 -21.562 -12.501 1.00 26.06 ? 382 PRO A N      1 
ATOM   2732 C CA     . PRO A 1 388 ? 10.725 -21.913 -12.749 1.00 29.35 ? 382 PRO A CA     1 
ATOM   2733 C C      . PRO A 1 388 ? 9.845  -21.745 -11.520 1.00 24.81 ? 382 PRO A C      1 
ATOM   2734 O O      . PRO A 1 388 ? 10.294 -21.788 -10.373 1.00 26.29 ? 382 PRO A O      1 
ATOM   2735 C CB     . PRO A 1 388 ? 10.797 -23.390 -13.152 1.00 28.74 ? 382 PRO A CB     1 
ATOM   2736 C CG     . PRO A 1 388 ? 12.030 -23.904 -12.480 1.00 34.08 ? 382 PRO A CG     1 
ATOM   2737 C CD     . PRO A 1 388 ? 12.985 -22.748 -12.336 1.00 30.02 ? 382 PRO A CD     1 
ATOM   2738 N N      . PHE A 1 389 ? 8.561  -21.540 -11.796 1.00 28.04 ? 383 PHE A N      1 
ATOM   2739 C CA     . PHE A 1 389 ? 7.525  -21.582 -10.779 1.00 25.32 ? 383 PHE A CA     1 
ATOM   2740 C C      . PHE A 1 389 ? 7.171  -23.033 -10.455 1.00 30.00 ? 383 PHE A C      1 
ATOM   2741 O O      . PHE A 1 389 ? 7.566  -23.970 -11.153 1.00 33.09 ? 383 PHE A O      1 
ATOM   2742 C CB     . PHE A 1 389 ? 6.279  -20.842 -11.264 1.00 26.71 ? 383 PHE A CB     1 
ATOM   2743 C CG     . PHE A 1 389 ? 6.467  -19.358 -11.411 1.00 24.85 ? 383 PHE A CG     1 
ATOM   2744 C CD1    . PHE A 1 389 ? 7.142  -18.828 -12.511 1.00 32.22 ? 383 PHE A CD1    1 
ATOM   2745 C CD2    . PHE A 1 389 ? 5.959  -18.491 -10.454 1.00 29.05 ? 383 PHE A CD2    1 
ATOM   2746 C CE1    . PHE A 1 389 ? 7.313  -17.459 -12.642 1.00 29.28 ? 383 PHE A CE1    1 
ATOM   2747 C CE2    . PHE A 1 389 ? 6.123  -17.126 -10.575 1.00 30.41 ? 383 PHE A CE2    1 
ATOM   2748 C CZ     . PHE A 1 389 ? 6.801  -16.606 -11.668 1.00 34.08 ? 383 PHE A CZ     1 
ATOM   2749 N N      . LEU A 1 390 ? 6.417  -23.211 -9.373  1.00 28.35 ? 384 LEU A N      1 
ATOM   2750 C CA     . LEU A 1 390 ? 5.999  -24.539 -8.914  1.00 31.94 ? 384 LEU A CA     1 
ATOM   2751 C C      . LEU A 1 390 ? 5.422  -25.421 -10.019 1.00 33.05 ? 384 LEU A C      1 
ATOM   2752 O O      . LEU A 1 390 ? 4.432  -25.064 -10.647 1.00 35.24 ? 384 LEU A O      1 
ATOM   2753 C CB     . LEU A 1 390 ? 4.969  -24.405 -7.790  1.00 36.23 ? 384 LEU A CB     1 
ATOM   2754 C CG     . LEU A 1 390 ? 5.542  -24.404 -6.382  1.00 34.62 ? 384 LEU A CG     1 
ATOM   2755 C CD1    . LEU A 1 390 ? 4.421  -24.359 -5.341  1.00 31.54 ? 384 LEU A CD1    1 
ATOM   2756 C CD2    . LEU A 1 390 ? 6.441  -25.620 -6.163  1.00 31.26 ? 384 LEU A CD2    1 
ATOM   2757 N N      . ASN B 1 16  ? 39.776 12.360  60.666  1.00 39.34 ? 10  ASN B N      1 
ATOM   2758 C CA     . ASN B 1 16  ? 38.596 11.847  59.980  1.00 38.15 ? 10  ASN B CA     1 
ATOM   2759 C C      . ASN B 1 16  ? 38.424 10.358  60.261  1.00 33.60 ? 10  ASN B C      1 
ATOM   2760 O O      . ASN B 1 16  ? 39.233 9.543   59.816  1.00 34.33 ? 10  ASN B O      1 
ATOM   2761 C CB     . ASN B 1 16  ? 38.702 12.098  58.471  1.00 37.44 ? 10  ASN B CB     1 
ATOM   2762 C CG     . ASN B 1 16  ? 37.387 11.850  57.733  1.00 38.06 ? 10  ASN B CG     1 
ATOM   2763 O OD1    . ASN B 1 16  ? 36.515 11.122  58.207  1.00 35.58 ? 10  ASN B OD1    1 
ATOM   2764 N ND2    . ASN B 1 16  ? 37.252 12.453  56.555  1.00 39.50 ? 10  ASN B ND2    1 
ATOM   2765 N N      . PRO B 1 17  ? 37.356 10.003  60.984  1.00 30.75 ? 11  PRO B N      1 
ATOM   2766 C CA     . PRO B 1 17  ? 37.125 8.586   61.303  1.00 38.02 ? 11  PRO B CA     1 
ATOM   2767 C C      . PRO B 1 17  ? 36.852 7.716   60.085  1.00 30.22 ? 11  PRO B C      1 
ATOM   2768 O O      . PRO B 1 17  ? 37.060 6.498   60.162  1.00 29.79 ? 11  PRO B O      1 
ATOM   2769 C CB     . PRO B 1 17  ? 35.914 8.618   62.253  1.00 32.40 ? 11  PRO B CB     1 
ATOM   2770 C CG     . PRO B 1 17  ? 35.676 10.078  62.562  1.00 40.14 ? 11  PRO B CG     1 
ATOM   2771 C CD     . PRO B 1 17  ? 36.238 10.850  61.421  1.00 38.51 ? 11  PRO B CD     1 
ATOM   2772 N N      . LEU B 1 18  ? 36.413 8.290   58.962  1.00 29.04 ? 12  LEU B N      1 
ATOM   2773 C CA     . LEU B 1 18  ? 36.236 7.485   57.759  1.00 30.15 ? 12  LEU B CA     1 
ATOM   2774 C C      . LEU B 1 18  ? 37.556 6.960   57.217  1.00 30.46 ? 12  LEU B C      1 
ATOM   2775 O O      . LEU B 1 18  ? 37.549 6.087   56.339  1.00 28.86 ? 12  LEU B O      1 
ATOM   2776 C CB     . LEU B 1 18  ? 35.515 8.284   56.666  1.00 27.45 ? 12  LEU B CB     1 
ATOM   2777 C CG     . LEU B 1 18  ? 34.015 8.514   56.901  1.00 35.04 ? 12  LEU B CG     1 
ATOM   2778 C CD1    . LEU B 1 18  ? 33.432 9.437   55.834  1.00 28.53 ? 12  LEU B CD1    1 
ATOM   2779 C CD2    . LEU B 1 18  ? 33.267 7.192   56.941  1.00 29.49 ? 12  LEU B CD2    1 
ATOM   2780 N N      . PHE B 1 19  ? 38.687 7.465   57.712  1.00 27.36 ? 13  PHE B N      1 
ATOM   2781 C CA     . PHE B 1 19  ? 39.994 7.042   57.222  1.00 27.82 ? 13  PHE B CA     1 
ATOM   2782 C C      . PHE B 1 19  ? 40.797 6.312   58.286  1.00 29.37 ? 13  PHE B C      1 
ATOM   2783 O O      . PHE B 1 19  ? 42.022 6.195   58.180  1.00 30.75 ? 13  PHE B O      1 
ATOM   2784 C CB     . PHE B 1 19  ? 40.733 8.209   56.576  1.00 30.44 ? 13  PHE B CB     1 
ATOM   2785 C CG     . PHE B 1 19  ? 40.060 8.652   55.327  1.00 27.65 ? 13  PHE B CG     1 
ATOM   2786 C CD1    . PHE B 1 19  ? 40.310 8.000   54.134  1.00 32.18 ? 13  PHE B CD1    1 
ATOM   2787 C CD2    . PHE B 1 19  ? 39.078 9.625   55.370  1.00 30.96 ? 13  PHE B CD2    1 
ATOM   2788 C CE1    . PHE B 1 19  ? 39.641 8.360   52.983  1.00 32.73 ? 13  PHE B CE1    1 
ATOM   2789 C CE2    . PHE B 1 19  ? 38.404 9.990   54.219  1.00 34.59 ? 13  PHE B CE2    1 
ATOM   2790 C CZ     . PHE B 1 19  ? 38.684 9.352   53.031  1.00 30.50 ? 13  PHE B CZ     1 
ATOM   2791 N N      . SER B 1 20  ? 40.110 5.819   59.296  1.00 32.70 ? 14  SER B N      1 
ATOM   2792 C CA     . SER B 1 20  ? 40.648 4.829   60.206  1.00 33.03 ? 14  SER B CA     1 
ATOM   2793 C C      . SER B 1 20  ? 40.561 3.459   59.542  1.00 37.52 ? 14  SER B C      1 
ATOM   2794 O O      . SER B 1 20  ? 39.517 3.119   58.974  1.00 31.99 ? 14  SER B O      1 
ATOM   2795 C CB     . SER B 1 20  ? 39.796 4.831   61.470  1.00 33.49 ? 14  SER B CB     1 
ATOM   2796 O OG     . SER B 1 20  ? 39.855 3.581   62.132  1.00 48.61 ? 14  SER B OG     1 
ATOM   2797 N N      . PRO B 1 21  ? 41.625 2.655   59.571  1.00 29.93 ? 15  PRO B N      1 
ATOM   2798 C CA     . PRO B 1 21  ? 41.535 1.310   58.997  1.00 29.08 ? 15  PRO B CA     1 
ATOM   2799 C C      . PRO B 1 21  ? 40.490 0.471   59.718  1.00 28.94 ? 15  PRO B C      1 
ATOM   2800 O O      . PRO B 1 21  ? 40.101 0.750   60.852  1.00 26.73 ? 15  PRO B O      1 
ATOM   2801 C CB     . PRO B 1 21  ? 42.949 0.745   59.191  1.00 34.26 ? 15  PRO B CB     1 
ATOM   2802 C CG     . PRO B 1 21  ? 43.502 1.529   60.338  1.00 40.86 ? 15  PRO B CG     1 
ATOM   2803 C CD     . PRO B 1 21  ? 42.964 2.920   60.123  1.00 37.09 ? 15  PRO B CD     1 
ATOM   2804 N N      . TYR B 1 22  ? 40.015 -0.558  59.026  1.00 28.83 ? 16  TYR B N      1 
ATOM   2805 C CA     . TYR B 1 22  ? 39.020 -1.464  59.575  1.00 28.70 ? 16  TYR B CA     1 
ATOM   2806 C C      . TYR B 1 22  ? 39.285 -2.861  59.047  1.00 28.51 ? 16  TYR B C      1 
ATOM   2807 O O      . TYR B 1 22  ? 39.582 -3.043  57.862  1.00 30.44 ? 16  TYR B O      1 
ATOM   2808 C CB     . TYR B 1 22  ? 37.585 -1.067  59.195  1.00 25.87 ? 16  TYR B CB     1 
ATOM   2809 C CG     . TYR B 1 22  ? 36.548 -1.924  59.897  1.00 24.91 ? 16  TYR B CG     1 
ATOM   2810 C CD1    . TYR B 1 22  ? 36.238 -1.711  61.236  1.00 22.78 ? 16  TYR B CD1    1 
ATOM   2811 C CD2    . TYR B 1 22  ? 35.913 -2.980  59.239  1.00 27.02 ? 16  TYR B CD2    1 
ATOM   2812 C CE1    . TYR B 1 22  ? 35.311 -2.493  61.894  1.00 31.13 ? 16  TYR B CE1    1 
ATOM   2813 C CE2    . TYR B 1 22  ? 34.971 -3.775  59.902  1.00 21.94 ? 16  TYR B CE2    1 
ATOM   2814 C CZ     . TYR B 1 22  ? 34.682 -3.521  61.225  1.00 27.92 ? 16  TYR B CZ     1 
ATOM   2815 O OH     . TYR B 1 22  ? 33.761 -4.289  61.901  1.00 28.05 ? 16  TYR B OH     1 
ATOM   2816 N N      . LYS B 1 23  ? 39.141 -3.843  59.922  1.00 27.48 ? 17  LYS B N      1 
ATOM   2817 C CA     . LYS B 1 23  ? 39.346 -5.247  59.588  1.00 26.68 ? 17  LYS B CA     1 
ATOM   2818 C C      . LYS B 1 23  ? 37.978 -5.881  59.331  1.00 28.76 ? 17  LYS B C      1 
ATOM   2819 O O      . LYS B 1 23  ? 37.241 -6.198  60.271  1.00 31.56 ? 17  LYS B O      1 
ATOM   2820 C CB     . LYS B 1 23  ? 40.079 -5.926  60.740  1.00 40.87 ? 17  LYS B CB     1 
ATOM   2821 C CG     . LYS B 1 23  ? 40.433 -7.374  60.509  1.00 50.27 ? 17  LYS B CG     1 
ATOM   2822 C CD     . LYS B 1 23  ? 41.784 -7.734  61.116  1.00 60.78 ? 17  LYS B CD     1 
ATOM   2823 C CE     . LYS B 1 23  ? 42.120 -9.197  60.863  1.00 62.01 ? 17  LYS B CE     1 
ATOM   2824 N NZ     . LYS B 1 23  ? 40.899 -10.057 60.952  1.00 58.57 ? 17  LYS B NZ     1 
ATOM   2825 N N      . MET B 1 24  ? 37.627 -6.043  58.052  1.00 34.52 ? 18  MET B N      1 
ATOM   2826 C CA     . MET B 1 24  ? 36.419 -6.777  57.659  1.00 33.04 ? 18  MET B CA     1 
ATOM   2827 C C      . MET B 1 24  ? 36.740 -8.266  57.595  1.00 34.66 ? 18  MET B C      1 
ATOM   2828 O O      . MET B 1 24  ? 36.892 -8.863  56.526  1.00 41.23 ? 18  MET B O      1 
ATOM   2829 C CB     . MET B 1 24  ? 35.882 -6.267  56.331  1.00 35.22 ? 18  MET B CB     1 
ATOM   2830 C CG     . MET B 1 24  ? 34.430 -6.623  56.077  1.00 32.60 ? 18  MET B CG     1 
ATOM   2831 S SD     . MET B 1 24  ? 33.854 -5.847  54.564  1.00 33.13 ? 18  MET B SD     1 
ATOM   2832 C CE     . MET B 1 24  ? 34.601 -6.929  53.344  1.00 35.00 ? 18  MET B CE     1 
ATOM   2833 N N      . GLY B 1 25  ? 36.838 -8.877  58.774  1.00 42.26 ? 19  GLY B N      1 
ATOM   2834 C CA     . GLY B 1 25  ? 37.303 -10.247 58.844  1.00 42.42 ? 19  GLY B CA     1 
ATOM   2835 C C      . GLY B 1 25  ? 38.727 -10.353 58.341  1.00 37.47 ? 19  GLY B C      1 
ATOM   2836 O O      . GLY B 1 25  ? 39.621 -9.707  58.885  1.00 45.64 ? 19  GLY B O      1 
ATOM   2837 N N      . LYS B 1 26  ? 38.965 -11.141 57.299  1.00 45.50 ? 20  LYS B N      1 
ATOM   2838 C CA     . LYS B 1 26  ? 40.323 -11.286 56.790  1.00 44.76 ? 20  LYS B CA     1 
ATOM   2839 C C      . LYS B 1 26  ? 40.719 -10.195 55.805  1.00 41.64 ? 20  LYS B C      1 
ATOM   2840 O O      . LYS B 1 26  ? 41.846 -10.217 55.300  1.00 40.85 ? 20  LYS B O      1 
ATOM   2841 C CB     . LYS B 1 26  ? 40.524 -12.664 56.160  1.00 43.89 ? 20  LYS B CB     1 
ATOM   2842 C CG     . LYS B 1 26  ? 39.828 -12.847 54.839  1.00 47.46 ? 20  LYS B CG     1 
ATOM   2843 C CD     . LYS B 1 26  ? 39.488 -14.303 54.661  1.00 55.37 ? 20  LYS B CD     1 
ATOM   2844 C CE     . LYS B 1 26  ? 38.965 -14.591 53.279  1.00 54.30 ? 20  LYS B CE     1 
ATOM   2845 N NZ     . LYS B 1 26  ? 38.584 -16.030 53.209  1.00 58.68 ? 20  LYS B NZ     1 
ATOM   2846 N N      . PHE B 1 27  ? 39.837 -9.243  55.520  1.00 34.32 ? 21  PHE B N      1 
ATOM   2847 C CA     . PHE B 1 27  ? 40.149 -8.145  54.613  1.00 33.96 ? 21  PHE B CA     1 
ATOM   2848 C C      . PHE B 1 27  ? 40.474 -6.906  55.436  1.00 32.60 ? 21  PHE B C      1 
ATOM   2849 O O      . PHE B 1 27  ? 39.637 -6.434  56.212  1.00 35.98 ? 21  PHE B O      1 
ATOM   2850 C CB     . PHE B 1 27  ? 38.983 -7.880  53.656  1.00 39.12 ? 21  PHE B CB     1 
ATOM   2851 C CG     . PHE B 1 27  ? 38.479 -9.117  52.967  1.00 36.94 ? 21  PHE B CG     1 
ATOM   2852 C CD1    . PHE B 1 27  ? 39.225 -9.716  51.961  1.00 32.81 ? 21  PHE B CD1    1 
ATOM   2853 C CD2    . PHE B 1 27  ? 37.273 -9.693  53.336  1.00 39.13 ? 21  PHE B CD2    1 
ATOM   2854 C CE1    . PHE B 1 27  ? 38.778 -10.863 51.327  1.00 32.89 ? 21  PHE B CE1    1 
ATOM   2855 C CE2    . PHE B 1 27  ? 36.813 -10.839 52.705  1.00 37.91 ? 21  PHE B CE2    1 
ATOM   2856 C CZ     . PHE B 1 27  ? 37.568 -11.424 51.699  1.00 33.33 ? 21  PHE B CZ     1 
ATOM   2857 N N      . ASN B 1 28  ? 41.688 -6.391  55.279  1.00 32.29 ? 22  ASN B N      1 
ATOM   2858 C CA     . ASN B 1 28  ? 42.118 -5.181  55.971  1.00 31.47 ? 22  ASN B CA     1 
ATOM   2859 C C      . ASN B 1 28  ? 41.835 -3.984  55.073  1.00 32.70 ? 22  ASN B C      1 
ATOM   2860 O O      . ASN B 1 28  ? 42.532 -3.765  54.075  1.00 35.91 ? 22  ASN B O      1 
ATOM   2861 C CB     . ASN B 1 28  ? 43.602 -5.261  56.310  1.00 36.34 ? 22  ASN B CB     1 
ATOM   2862 C CG     . ASN B 1 28  ? 43.957 -6.533  57.046  1.00 42.23 ? 22  ASN B CG     1 
ATOM   2863 O OD1    . ASN B 1 28  ? 43.474 -6.779  58.153  1.00 37.46 ? 22  ASN B OD1    1 
ATOM   2864 N ND2    . ASN B 1 28  ? 44.786 -7.364  56.423  1.00 48.77 ? 22  ASN B ND2    1 
ATOM   2865 N N      . LEU B 1 29  ? 40.809 -3.218  55.417  1.00 27.29 ? 23  LEU B N      1 
ATOM   2866 C CA     . LEU B 1 29  ? 40.464 -2.030  54.654  1.00 28.91 ? 23  LEU B CA     1 
ATOM   2867 C C      . LEU B 1 29  ? 41.228 -0.834  55.201  1.00 27.68 ? 23  LEU B C      1 
ATOM   2868 O O      . LEU B 1 29  ? 41.446 -0.718  56.410  1.00 29.56 ? 23  LEU B O      1 
ATOM   2869 C CB     . LEU B 1 29  ? 38.956 -1.776  54.730  1.00 25.01 ? 23  LEU B CB     1 
ATOM   2870 C CG     . LEU B 1 29  ? 38.097 -2.973  54.317  1.00 24.04 ? 23  LEU B CG     1 
ATOM   2871 C CD1    . LEU B 1 29  ? 36.604 -2.639  54.487  1.00 27.09 ? 23  LEU B CD1    1 
ATOM   2872 C CD2    . LEU B 1 29  ? 38.399 -3.402  52.883  1.00 26.52 ? 23  LEU B CD2    1 
ATOM   2873 N N      . SER B 1 30  ? 41.641 0.053   54.302  1.00 24.94 ? 24  SER B N      1 
ATOM   2874 C CA     . SER B 1 30  ? 42.352 1.260   54.696  1.00 27.10 ? 24  SER B CA     1 
ATOM   2875 C C      . SER B 1 30  ? 41.420 2.418   55.008  1.00 26.62 ? 24  SER B C      1 
ATOM   2876 O O      . SER B 1 30  ? 41.860 3.410   55.591  1.00 27.49 ? 24  SER B O      1 
ATOM   2877 C CB     . SER B 1 30  ? 43.357 1.671   53.610  1.00 27.50 ? 24  SER B CB     1 
ATOM   2878 O OG     . SER B 1 30  ? 42.681 2.078   52.434  1.00 38.66 ? 24  SER B OG     1 
ATOM   2879 N N      . HIS B 1 31  ? 40.149 2.324   54.628  1.00 25.82 ? 25  HIS B N      1 
ATOM   2880 C CA     . HIS B 1 31  ? 39.189 3.377   54.918  1.00 28.22 ? 25  HIS B CA     1 
ATOM   2881 C C      . HIS B 1 31  ? 37.796 2.769   54.841  1.00 23.99 ? 25  HIS B C      1 
ATOM   2882 O O      . HIS B 1 31  ? 37.622 1.617   54.437  1.00 24.01 ? 25  HIS B O      1 
ATOM   2883 C CB     . HIS B 1 31  ? 39.364 4.563   53.972  1.00 24.44 ? 25  HIS B CB     1 
ATOM   2884 C CG     . HIS B 1 31  ? 39.081 4.225   52.547  1.00 21.31 ? 25  HIS B CG     1 
ATOM   2885 N ND1    . HIS B 1 31  ? 37.808 3.976   52.080  1.00 23.65 ? 25  HIS B ND1    1 
ATOM   2886 C CD2    . HIS B 1 31  ? 39.913 4.055   51.493  1.00 24.43 ? 25  HIS B CD2    1 
ATOM   2887 C CE1    . HIS B 1 31  ? 37.866 3.694   50.792  1.00 25.20 ? 25  HIS B CE1    1 
ATOM   2888 N NE2    . HIS B 1 31  ? 39.134 3.731   50.411  1.00 25.06 ? 25  HIS B NE2    1 
ATOM   2889 N N      . ARG B 1 32  ? 36.804 3.557   55.242  1.00 22.80 ? 26  ARG B N      1 
ATOM   2890 C CA     . ARG B 1 32  ? 35.467 3.042   55.487  1.00 20.44 ? 26  ARG B CA     1 
ATOM   2891 C C      . ARG B 1 32  ? 34.448 3.503   54.454  1.00 23.60 ? 26  ARG B C      1 
ATOM   2892 O O      . ARG B 1 32  ? 33.240 3.315   54.664  1.00 21.73 ? 26  ARG B O      1 
ATOM   2893 C CB     . ARG B 1 32  ? 35.033 3.426   56.895  1.00 21.47 ? 26  ARG B CB     1 
ATOM   2894 C CG     . ARG B 1 32  ? 36.073 2.984   57.909  1.00 25.35 ? 26  ARG B CG     1 
ATOM   2895 C CD     . ARG B 1 32  ? 35.765 3.485   59.267  1.00 30.47 ? 26  ARG B CD     1 
ATOM   2896 N NE     . ARG B 1 32  ? 36.751 2.980   60.209  1.00 28.23 ? 26  ARG B NE     1 
ATOM   2897 C CZ     . ARG B 1 32  ? 36.459 2.189   61.230  1.00 29.58 ? 26  ARG B CZ     1 
ATOM   2898 N NH1    . ARG B 1 32  ? 35.231 1.734   61.418  1.00 26.21 ? 26  ARG B NH1    1 
ATOM   2899 N NH2    . ARG B 1 32  ? 37.421 1.853   62.085  1.00 27.49 ? 26  ARG B NH2    1 
ATOM   2900 N N      . VAL B 1 33  ? 34.903 4.090   53.348  1.00 22.55 ? 27  VAL B N      1 
ATOM   2901 C CA     . VAL B 1 33  ? 34.017 4.524   52.271  1.00 21.92 ? 27  VAL B CA     1 
ATOM   2902 C C      . VAL B 1 33  ? 33.859 3.359   51.305  1.00 22.51 ? 27  VAL B C      1 
ATOM   2903 O O      . VAL B 1 33  ? 34.843 2.890   50.719  1.00 23.55 ? 27  VAL B O      1 
ATOM   2904 C CB     . VAL B 1 33  ? 34.575 5.770   51.563  1.00 23.09 ? 27  VAL B CB     1 
ATOM   2905 C CG1    . VAL B 1 33  ? 33.653 6.207   50.428  1.00 21.87 ? 27  VAL B CG1    1 
ATOM   2906 C CG2    . VAL B 1 33  ? 34.765 6.912   52.567  1.00 23.71 ? 27  VAL B CG2    1 
ATOM   2907 N N      . VAL B 1 34  ? 32.622 2.899   51.132  1.00 19.27 ? 28  VAL B N      1 
ATOM   2908 C CA     . VAL B 1 34  ? 32.308 1.714   50.338  1.00 20.86 ? 28  VAL B CA     1 
ATOM   2909 C C      . VAL B 1 34  ? 31.486 2.116   49.112  1.00 20.63 ? 28  VAL B C      1 
ATOM   2910 O O      . VAL B 1 34  ? 30.572 2.946   49.212  1.00 21.39 ? 28  VAL B O      1 
ATOM   2911 C CB     . VAL B 1 34  ? 31.525 0.701   51.205  1.00 20.05 ? 28  VAL B CB     1 
ATOM   2912 C CG1    . VAL B 1 34  ? 31.128 -0.525  50.382  1.00 22.33 ? 28  VAL B CG1    1 
ATOM   2913 C CG2    . VAL B 1 34  ? 32.346 0.291   52.425  1.00 22.09 ? 28  VAL B CG2    1 
ATOM   2914 N N      . LEU B 1 35  ? 31.787 1.504   47.963  1.00 21.48 ? 29  LEU B N      1 
ATOM   2915 C CA     . LEU B 1 35  ? 30.950 1.656   46.771  1.00 20.41 ? 29  LEU B CA     1 
ATOM   2916 C C      . LEU B 1 35  ? 29.719 0.779   46.939  1.00 18.19 ? 29  LEU B C      1 
ATOM   2917 O O      . LEU B 1 35  ? 29.821 -0.452  46.965  1.00 20.66 ? 29  LEU B O      1 
ATOM   2918 C CB     . LEU B 1 35  ? 31.723 1.269   45.508  1.00 19.21 ? 29  LEU B CB     1 
ATOM   2919 C CG     . LEU B 1 35  ? 30.886 1.195   44.223  1.00 19.97 ? 29  LEU B CG     1 
ATOM   2920 C CD1    . LEU B 1 35  ? 30.379 2.571   43.834  1.00 22.26 ? 29  LEU B CD1    1 
ATOM   2921 C CD2    . LEU B 1 35  ? 31.675 0.568   43.092  1.00 20.70 ? 29  LEU B CD2    1 
ATOM   2922 N N      . ALA B 1 36  ? 28.556 1.409   47.021  1.00 21.72 ? 30  ALA B N      1 
ATOM   2923 C CA     . ALA B 1 36  ? 27.298 0.654   47.139  1.00 20.58 ? 30  ALA B CA     1 
ATOM   2924 C C      . ALA B 1 36  ? 27.008 -0.047  45.809  1.00 18.16 ? 30  ALA B C      1 
ATOM   2925 O O      . ALA B 1 36  ? 27.427 0.443   44.762  1.00 20.10 ? 30  ALA B O      1 
ATOM   2926 C CB     . ALA B 1 36  ? 26.189 1.610   47.507  1.00 21.12 ? 30  ALA B CB     1 
ATOM   2927 N N      . PRO B 1 37  ? 26.287 -1.180  45.837  1.00 19.49 ? 31  PRO B N      1 
ATOM   2928 C CA     . PRO B 1 37  ? 25.910 -1.862  44.608  1.00 18.18 ? 31  PRO B CA     1 
ATOM   2929 C C      . PRO B 1 37  ? 24.949 -1.007  43.771  1.00 16.95 ? 31  PRO B C      1 
ATOM   2930 O O      . PRO B 1 37  ? 23.982 -0.565  44.281  1.00 20.51 ? 31  PRO B O      1 
ATOM   2931 C CB     . PRO B 1 37  ? 25.207 -3.123  45.101  1.00 21.20 ? 31  PRO B CB     1 
ATOM   2932 C CG     . PRO B 1 37  ? 24.739 -2.781  46.499  1.00 20.01 ? 31  PRO B CG     1 
ATOM   2933 C CD     . PRO B 1 37  ? 25.788 -1.840  47.042  1.00 20.98 ? 31  PRO B CD     1 
ATOM   2934 N N      . MET B 1 38  ? 25.185 -0.831  42.529  1.00 20.02 ? 32  MET B N      1 
ATOM   2935 C CA     . MET B 1 38  ? 24.335 -0.050  41.609  1.00 19.50 ? 32  MET B CA     1 
ATOM   2936 C C      . MET B 1 38  ? 24.280 -0.673  40.215  1.00 20.43 ? 32  MET B C      1 
ATOM   2937 O O      . MET B 1 38  ? 25.316 -0.753  39.557  1.00 22.32 ? 32  MET B O      1 
ATOM   2938 C CB     . MET B 1 38  ? 24.837 1.391   41.517  1.00 18.94 ? 32  MET B CB     1 
ATOM   2939 C CG     . MET B 1 38  ? 24.684 2.188   42.802  1.00 25.87 ? 32  MET B CG     1 
ATOM   2940 S SD     . MET B 1 38  ? 25.207 3.903   42.625  1.00 26.42 ? 32  MET B SD     1 
ATOM   2941 C CE     . MET B 1 38  ? 26.989 3.717   42.643  1.00 25.61 ? 32  MET B CE     1 
ATOM   2942 N N      . THR B 1 39  ? 23.099 -0.960  39.883  1.00 17.81 ? 33  THR B N      1 
ATOM   2943 C CA     . THR B 1 39  ? 22.780 -1.455  38.530  1.00 19.27 ? 33  THR B CA     1 
ATOM   2944 C C      . THR B 1 39  ? 22.965 -0.306  37.532  1.00 22.00 ? 33  THR B C      1 
ATOM   2945 O O      . THR B 1 39  ? 22.388 0.756   37.755  1.00 20.02 ? 33  THR B O      1 
ATOM   2946 C CB     . THR B 1 39  ? 21.329 -1.933  38.561  1.00 20.85 ? 33  THR B CB     1 
ATOM   2947 O OG1    . THR B 1 39  ? 21.251 -3.104  39.374  1.00 21.65 ? 33  THR B OG1    1 
ATOM   2948 C CG2    . THR B 1 39  ? 20.760 -2.207  37.186  1.00 20.51 ? 33  THR B CG2    1 
ATOM   2949 N N      . ARG B 1 40  ? 23.751 -0.521  36.477  1.00 18.61 ? 34  ARG B N      1 
ATOM   2950 C CA     . ARG B 1 40  ? 24.019 0.534   35.468  1.00 22.31 ? 34  ARG B CA     1 
ATOM   2951 C C      . ARG B 1 40  ? 23.664 0.048   34.052  1.00 21.03 ? 34  ARG B C      1 
ATOM   2952 O O      . ARG B 1 40  ? 23.660 0.888   33.160  1.00 20.64 ? 34  ARG B O      1 
ATOM   2953 C CB     . ARG B 1 40  ? 25.464 1.016   35.602  1.00 22.75 ? 34  ARG B CB     1 
ATOM   2954 C CG     . ARG B 1 40  ? 25.839 1.470   37.004  1.00 21.71 ? 34  ARG B CG     1 
ATOM   2955 C CD     . ARG B 1 40  ? 25.030 2.654   37.494  1.00 19.39 ? 34  ARG B CD     1 
ATOM   2956 N NE     . ARG B 1 40  ? 24.932 3.731   36.524  1.00 19.96 ? 34  ARG B NE     1 
ATOM   2957 C CZ     . ARG B 1 40  ? 25.915 4.572   36.241  1.00 21.77 ? 34  ARG B CZ     1 
ATOM   2958 N NH1    . ARG B 1 40  ? 27.057 4.497   36.899  1.00 20.61 ? 34  ARG B NH1    1 
ATOM   2959 N NH2    . ARG B 1 40  ? 25.753 5.489   35.306  1.00 20.86 ? 34  ARG B NH2    1 
ATOM   2960 N N      . CYS B 1 41  ? 23.437 -1.250  33.859  1.00 20.37 ? 35  CYS B N      1 
ATOM   2961 C CA     . CYS B 1 41  ? 22.940 -1.757  32.578  1.00 16.65 ? 35  CYS B CA     1 
ATOM   2962 C C      . CYS B 1 41  ? 23.934 -1.585  31.430  1.00 19.37 ? 35  CYS B C      1 
ATOM   2963 O O      . CYS B 1 41  ? 23.516 -1.427  30.286  1.00 20.92 ? 35  CYS B O      1 
ATOM   2964 C CB     . CYS B 1 41  ? 21.574 -1.162  32.212  1.00 18.92 ? 35  CYS B CB     1 
ATOM   2965 S SG     . CYS B 1 41  ? 20.354 -1.261  33.546  1.00 20.92 ? 35  CYS B SG     1 
ATOM   2966 N N      . ARG B 1 42  ? 25.243 -1.613  31.708  1.00 18.51 ? 36  ARG B N      1 
ATOM   2967 C CA     . ARG B 1 42  ? 26.251 -1.601  30.646  1.00 19.57 ? 36  ARG B CA     1 
ATOM   2968 C C      . ARG B 1 42  ? 26.744 -2.994  30.281  1.00 21.88 ? 36  ARG B C      1 
ATOM   2969 O O      . ARG B 1 42  ? 27.553 -3.127  29.352  1.00 22.73 ? 36  ARG B O      1 
ATOM   2970 C CB     . ARG B 1 42  ? 27.438 -0.706  31.008  1.00 19.35 ? 36  ARG B CB     1 
ATOM   2971 C CG     . ARG B 1 42  ? 27.316 0.741   30.541  1.00 19.35 ? 36  ARG B CG     1 
ATOM   2972 C CD     . ARG B 1 42  ? 26.216 1.486   31.277  1.00 21.82 ? 36  ARG B CD     1 
ATOM   2973 N NE     . ARG B 1 42  ? 26.225 2.914   30.975  1.00 21.09 ? 36  ARG B NE     1 
ATOM   2974 C CZ     . ARG B 1 42  ? 25.472 3.807   31.603  1.00 21.92 ? 36  ARG B CZ     1 
ATOM   2975 N NH1    . ARG B 1 42  ? 24.649 3.450   32.579  1.00 20.87 ? 36  ARG B NH1    1 
ATOM   2976 N NH2    . ARG B 1 42  ? 25.560 5.090   31.258  1.00 21.19 ? 36  ARG B NH2    1 
ATOM   2977 N N      . ALA B 1 43  ? 26.262 -4.033  30.961  1.00 19.37 ? 37  ALA B N      1 
ATOM   2978 C CA     . ALA B 1 43  ? 26.732 -5.403  30.747  1.00 20.33 ? 37  ALA B CA     1 
ATOM   2979 C C      . ALA B 1 43  ? 25.905 -6.030  29.627  1.00 19.63 ? 37  ALA B C      1 
ATOM   2980 O O      . ALA B 1 43  ? 25.016 -6.854  29.845  1.00 21.37 ? 37  ALA B O      1 
ATOM   2981 C CB     . ALA B 1 43  ? 26.647 -6.193  32.054  1.00 20.26 ? 37  ALA B CB     1 
ATOM   2982 N N      . LEU B 1 44  ? 26.224 -5.632  28.392  1.00 19.73 ? 38  LEU B N      1 
ATOM   2983 C CA     . LEU B 1 44  ? 25.375 -5.958  27.252  1.00 22.88 ? 38  LEU B CA     1 
ATOM   2984 C C      . LEU B 1 44  ? 25.158 -7.465  27.112  1.00 23.16 ? 38  LEU B C      1 
ATOM   2985 O O      . LEU B 1 44  ? 26.112 -8.252  27.149  1.00 23.13 ? 38  LEU B O      1 
ATOM   2986 C CB     . LEU B 1 44  ? 26.002 -5.395  25.973  1.00 20.61 ? 38  LEU B CB     1 
ATOM   2987 C CG     . LEU B 1 44  ? 26.306 -3.888  25.998  1.00 21.81 ? 38  LEU B CG     1 
ATOM   2988 C CD1    . LEU B 1 44  ? 26.802 -3.378  24.627  1.00 19.57 ? 38  LEU B CD1    1 
ATOM   2989 C CD2    . LEU B 1 44  ? 25.093 -3.082  26.473  1.00 21.56 ? 38  LEU B CD2    1 
ATOM   2990 N N      . ASN B 1 45  ? 23.889 -7.859  26.940  1.00 20.42 ? 39  ASN B N      1 
ATOM   2991 C CA     . ASN B 1 45  ? 23.492 -9.265  26.795  1.00 21.24 ? 39  ASN B CA     1 
ATOM   2992 C C      . ASN B 1 45  ? 23.912 -10.116 27.984  1.00 25.20 ? 39  ASN B C      1 
ATOM   2993 O O      . ASN B 1 45  ? 24.164 -11.317 27.840  1.00 24.14 ? 39  ASN B O      1 
ATOM   2994 C CB     . ASN B 1 45  ? 23.974 -9.883  25.476  1.00 23.63 ? 39  ASN B CB     1 
ATOM   2995 C CG     . ASN B 1 45  ? 23.045 -9.589  24.336  1.00 40.62 ? 39  ASN B CG     1 
ATOM   2996 O OD1    . ASN B 1 45  ? 22.136 -8.770  24.465  1.00 42.84 ? 39  ASN B OD1    1 
ATOM   2997 N ND2    . ASN B 1 45  ? 23.268 -10.246 23.200  1.00 44.58 ? 39  ASN B ND2    1 
ATOM   2998 N N      . ASN B 1 46  ? 23.990 -9.489  29.160  1.00 21.52 ? 40  ASN B N      1 
ATOM   2999 C CA     . ASN B 1 46  ? 24.365 -10.110 30.432  1.00 23.50 ? 40  ASN B CA     1 
ATOM   3000 C C      . ASN B 1 46  ? 25.843 -10.481 30.529  1.00 22.84 ? 40  ASN B C      1 
ATOM   3001 O O      . ASN B 1 46  ? 26.241 -11.165 31.482  1.00 24.34 ? 40  ASN B O      1 
ATOM   3002 C CB     . ASN B 1 46  ? 23.464 -11.291 30.816  1.00 24.33 ? 40  ASN B CB     1 
ATOM   3003 C CG     . ASN B 1 46  ? 21.981 -10.982 30.624  1.00 24.04 ? 40  ASN B CG     1 
ATOM   3004 O OD1    . ASN B 1 46  ? 21.260 -11.728 29.958  1.00 28.95 ? 40  ASN B OD1    1 
ATOM   3005 N ND2    . ASN B 1 46  ? 21.522 -9.869  31.204  1.00 23.66 ? 40  ASN B ND2    1 
ATOM   3006 N N      . ILE B 1 47  ? 26.673 -10.049 29.591  1.00 21.20 ? 41  ILE B N      1 
ATOM   3007 C CA     . ILE B 1 47  ? 28.108 -10.317 29.632  1.00 23.79 ? 41  ILE B CA     1 
ATOM   3008 C C      . ILE B 1 47  ? 28.802 -9.118  30.265  1.00 22.88 ? 41  ILE B C      1 
ATOM   3009 O O      . ILE B 1 47  ? 28.595 -7.988  29.802  1.00 25.14 ? 41  ILE B O      1 
ATOM   3010 C CB     . ILE B 1 47  ? 28.673 -10.575 28.225  1.00 26.49 ? 41  ILE B CB     1 
ATOM   3011 C CG1    . ILE B 1 47  ? 27.844 -11.653 27.530  1.00 32.38 ? 41  ILE B CG1    1 
ATOM   3012 C CG2    . ILE B 1 47  ? 30.172 -10.912 28.324  1.00 26.36 ? 41  ILE B CG2    1 
ATOM   3013 C CD1    . ILE B 1 47  ? 27.817 -12.975 28.253  1.00 34.32 ? 41  ILE B CD1    1 
ATOM   3014 N N      . PRO B 1 48  ? 29.614 -9.312  31.303  1.00 22.32 ? 42  PRO B N      1 
ATOM   3015 C CA     . PRO B 1 48  ? 30.423 -8.198  31.804  1.00 22.95 ? 42  PRO B CA     1 
ATOM   3016 C C      . PRO B 1 48  ? 31.346 -7.695  30.705  1.00 25.84 ? 42  PRO B C      1 
ATOM   3017 O O      . PRO B 1 48  ? 32.052 -8.470  30.055  1.00 35.93 ? 42  PRO B O      1 
ATOM   3018 C CB     . PRO B 1 48  ? 31.201 -8.812  32.977  1.00 23.47 ? 42  PRO B CB     1 
ATOM   3019 C CG     . PRO B 1 48  ? 30.496 -10.091 33.304  1.00 24.53 ? 42  PRO B CG     1 
ATOM   3020 C CD     . PRO B 1 48  ? 29.857 -10.566 32.032  1.00 24.02 ? 42  PRO B CD     1 
ATOM   3021 N N      . GLN B 1 49  ? 31.293 -6.392  30.468  1.00 24.99 ? 43  GLN B N      1 
ATOM   3022 C CA     . GLN B 1 49  ? 31.990 -5.746  29.368  1.00 29.61 ? 43  GLN B CA     1 
ATOM   3023 C C      . GLN B 1 49  ? 33.243 -5.054  29.890  1.00 30.36 ? 43  GLN B C      1 
ATOM   3024 O O      . GLN B 1 49  ? 33.367 -4.765  31.081  1.00 25.15 ? 43  GLN B O      1 
ATOM   3025 C CB     . GLN B 1 49  ? 31.075 -4.709  28.713  1.00 25.21 ? 43  GLN B CB     1 
ATOM   3026 C CG     . GLN B 1 49  ? 29.779 -5.256  28.132  1.00 32.13 ? 43  GLN B CG     1 
ATOM   3027 C CD     . GLN B 1 49  ? 30.006 -6.086  26.884  1.00 31.22 ? 43  GLN B CD     1 
ATOM   3028 O OE1    . GLN B 1 49  ? 30.676 -5.645  25.956  1.00 33.35 ? 43  GLN B OE1    1 
ATOM   3029 N NE2    . GLN B 1 49  ? 29.432 -7.281  26.847  1.00 32.58 ? 43  GLN B NE2    1 
ATOM   3030 N N      . ALA B 1 50  ? 34.175 -4.778  28.971  1.00 28.26 ? 44  ALA B N      1 
ATOM   3031 C CA     . ALA B 1 50  ? 35.376 -4.031  29.342  1.00 25.84 ? 44  ALA B CA     1 
ATOM   3032 C C      . ALA B 1 50  ? 35.031 -2.704  30.007  1.00 25.86 ? 44  ALA B C      1 
ATOM   3033 O O      . ALA B 1 50  ? 35.766 -2.246  30.894  1.00 26.54 ? 44  ALA B O      1 
ATOM   3034 C CB     . ALA B 1 50  ? 36.250 -3.792  28.108  1.00 26.62 ? 44  ALA B CB     1 
ATOM   3035 N N      . ALA B 1 51  ? 33.911 -2.089  29.611  1.00 23.03 ? 45  ALA B N      1 
ATOM   3036 C CA     . ALA B 1 51  ? 33.487 -0.835  30.223  1.00 22.43 ? 45  ALA B CA     1 
ATOM   3037 C C      . ALA B 1 51  ? 33.352 -0.977  31.736  1.00 23.48 ? 45  ALA B C      1 
ATOM   3038 O O      . ALA B 1 51  ? 33.699 -0.055  32.480  1.00 24.04 ? 45  ALA B O      1 
ATOM   3039 C CB     . ALA B 1 51  ? 32.153 -0.390  29.631  1.00 24.93 ? 45  ALA B CB     1 
ATOM   3040 N N      . LEU B 1 52  ? 32.827 -2.114  32.205  1.00 21.89 ? 46  LEU B N      1 
ATOM   3041 C CA     . LEU B 1 52  ? 32.694 -2.316  33.648  1.00 22.85 ? 46  LEU B CA     1 
ATOM   3042 C C      . LEU B 1 52  ? 34.057 -2.308  34.311  1.00 21.09 ? 46  LEU B C      1 
ATOM   3043 O O      . LEU B 1 52  ? 34.205 -1.822  35.438  1.00 24.07 ? 46  LEU B O      1 
ATOM   3044 C CB     . LEU B 1 52  ? 31.968 -3.626  33.963  1.00 23.28 ? 46  LEU B CB     1 
ATOM   3045 C CG     . LEU B 1 52  ? 30.436 -3.683  33.964  1.00 21.89 ? 46  LEU B CG     1 
ATOM   3046 C CD1    . LEU B 1 52  ? 29.836 -3.333  32.598  1.00 22.74 ? 46  LEU B CD1    1 
ATOM   3047 C CD2    . LEU B 1 52  ? 30.005 -5.070  34.386  1.00 22.91 ? 46  LEU B CD2    1 
ATOM   3048 N N      . GLY B 1 53  ? 35.070 -2.840  33.621  1.00 24.99 ? 47  GLY B N      1 
ATOM   3049 C CA     . GLY B 1 53  ? 36.413 -2.801  34.174  1.00 26.63 ? 47  GLY B CA     1 
ATOM   3050 C C      . GLY B 1 53  ? 36.904 -1.384  34.374  1.00 23.51 ? 47  GLY B C      1 
ATOM   3051 O O      . GLY B 1 53  ? 37.453 -1.048  35.429  1.00 24.68 ? 47  GLY B O      1 
ATOM   3052 N N      . GLU B 1 54  ? 36.711 -0.529  33.360  1.00 23.08 ? 48  GLU B N      1 
ATOM   3053 C CA     . GLU B 1 54  ? 37.121 0.864   33.493  1.00 24.55 ? 48  GLU B CA     1 
ATOM   3054 C C      . GLU B 1 54  ? 36.339 1.572   34.596  1.00 25.19 ? 48  GLU B C      1 
ATOM   3055 O O      . GLU B 1 54  ? 36.904 2.359   35.355  1.00 23.18 ? 48  GLU B O      1 
ATOM   3056 C CB     . GLU B 1 54  ? 36.968 1.613   32.172  1.00 29.51 ? 48  GLU B CB     1 
ATOM   3057 N N      . TYR B 1 55  ? 35.034 1.310   34.682  1.00 22.94 ? 49  TYR B N      1 
ATOM   3058 C CA     . TYR B 1 55  ? 34.189 1.955   35.682  1.00 20.69 ? 49  TYR B CA     1 
ATOM   3059 C C      . TYR B 1 55  ? 34.633 1.600   37.094  1.00 23.07 ? 49  TYR B C      1 
ATOM   3060 O O      . TYR B 1 55  ? 34.804 2.479   37.949  1.00 19.94 ? 49  TYR B O      1 
ATOM   3061 C CB     . TYR B 1 55  ? 32.773 1.458   35.455  1.00 22.32 ? 49  TYR B CB     1 
ATOM   3062 C CG     . TYR B 1 55  ? 31.722 1.863   36.466  1.00 23.98 ? 49  TYR B CG     1 
ATOM   3063 C CD1    . TYR B 1 55  ? 31.187 3.150   36.492  1.00 21.36 ? 49  TYR B CD1    1 
ATOM   3064 C CD2    . TYR B 1 55  ? 31.260 0.936   37.392  1.00 21.63 ? 49  TYR B CD2    1 
ATOM   3065 C CE1    . TYR B 1 55  ? 30.188 3.486   37.424  1.00 23.86 ? 49  TYR B CE1    1 
ATOM   3066 C CE2    . TYR B 1 55  ? 30.282 1.261   38.311  1.00 21.15 ? 49  TYR B CE2    1 
ATOM   3067 C CZ     . TYR B 1 55  ? 29.751 2.531   38.313  1.00 23.62 ? 49  TYR B CZ     1 
ATOM   3068 O OH     . TYR B 1 55  ? 28.763 2.833   39.217  1.00 24.46 ? 49  TYR B OH     1 
ATOM   3069 N N      . TYR B 1 56  ? 34.797 0.307   37.367  1.00 21.18 ? 50  TYR B N      1 
ATOM   3070 C CA     . TYR B 1 56  ? 35.197 -0.092  38.709  1.00 21.25 ? 50  TYR B CA     1 
ATOM   3071 C C      . TYR B 1 56  ? 36.637 0.303   38.998  1.00 21.76 ? 50  TYR B C      1 
ATOM   3072 O O      . TYR B 1 56  ? 36.955 0.663   40.135  1.00 21.53 ? 50  TYR B O      1 
ATOM   3073 C CB     . TYR B 1 56  ? 34.970 -1.591  38.920  1.00 19.17 ? 50  TYR B CB     1 
ATOM   3074 C CG     . TYR B 1 56  ? 33.507 -1.957  39.034  1.00 18.67 ? 50  TYR B CG     1 
ATOM   3075 C CD1    . TYR B 1 56  ? 32.749 -1.575  40.143  1.00 22.28 ? 50  TYR B CD1    1 
ATOM   3076 C CD2    . TYR B 1 56  ? 32.890 -2.697  38.046  1.00 22.18 ? 50  TYR B CD2    1 
ATOM   3077 C CE1    . TYR B 1 56  ? 31.402 -1.910  40.240  1.00 21.69 ? 50  TYR B CE1    1 
ATOM   3078 C CE2    . TYR B 1 56  ? 31.553 -3.039  38.133  1.00 22.59 ? 50  TYR B CE2    1 
ATOM   3079 C CZ     . TYR B 1 56  ? 30.814 -2.647  39.228  1.00 21.59 ? 50  TYR B CZ     1 
ATOM   3080 O OH     . TYR B 1 56  ? 29.481 -2.998  39.281  1.00 21.73 ? 50  TYR B OH     1 
ATOM   3081 N N      . GLU B 1 57  ? 37.512 0.282   37.981  1.00 21.97 ? 51  GLU B N      1 
ATOM   3082 C CA     . GLU B 1 57  ? 38.896 0.680   38.206  1.00 23.82 ? 51  GLU B CA     1 
ATOM   3083 C C      . GLU B 1 57  ? 38.991 2.152   38.580  1.00 23.35 ? 51  GLU B C      1 
ATOM   3084 O O      . GLU B 1 57  ? 39.822 2.534   39.416  1.00 24.15 ? 51  GLU B O      1 
ATOM   3085 C CB     . GLU B 1 57  ? 39.745 0.378   36.965  1.00 22.26 ? 51  GLU B CB     1 
ATOM   3086 C CG     . GLU B 1 57  ? 41.210 0.741   37.146  1.00 29.11 ? 51  GLU B CG     1 
ATOM   3087 C CD     . GLU B 1 57  ? 42.010 0.615   35.866  1.00 44.24 ? 51  GLU B CD     1 
ATOM   3088 O OE1    . GLU B 1 57  ? 41.418 0.788   34.779  1.00 47.42 ? 51  GLU B OE1    1 
ATOM   3089 O OE2    . GLU B 1 57  ? 43.228 0.339   35.944  1.00 44.85 ? 51  GLU B OE2    1 
ATOM   3090 N N      . GLN B 1 58  ? 38.131 2.987   37.990  1.00 21.97 ? 52  GLN B N      1 
ATOM   3091 C CA     . GLN B 1 58  ? 38.142 4.410   38.306  1.00 23.45 ? 52  GLN B CA     1 
ATOM   3092 C C      . GLN B 1 58  ? 37.809 4.654   39.766  1.00 20.39 ? 52  GLN B C      1 
ATOM   3093 O O      . GLN B 1 58  ? 38.332 5.592   40.372  1.00 24.09 ? 52  GLN B O      1 
ATOM   3094 C CB     . GLN B 1 58  ? 37.093 5.139   37.469  1.00 22.56 ? 52  GLN B CB     1 
ATOM   3095 C CG     . GLN B 1 58  ? 37.493 5.400   36.032  1.00 21.97 ? 52  GLN B CG     1 
ATOM   3096 C CD     . GLN B 1 58  ? 36.442 6.180   35.281  1.00 23.28 ? 52  GLN B CD     1 
ATOM   3097 O OE1    . GLN B 1 58  ? 35.263 6.193   35.654  1.00 23.42 ? 52  GLN B OE1    1 
ATOM   3098 N NE2    . GLN B 1 58  ? 36.858 6.837   34.206  1.00 29.19 ? 52  GLN B NE2    1 
ATOM   3099 N N      . ARG B 1 59  ? 36.930 3.832   40.326  1.00 21.83 ? 53  ARG B N      1 
ATOM   3100 C CA     . ARG B 1 59  ? 36.429 4.003   41.678  1.00 20.18 ? 53  ARG B CA     1 
ATOM   3101 C C      . ARG B 1 59  ? 37.237 3.229   42.714  1.00 21.51 ? 53  ARG B C      1 
ATOM   3102 O O      . ARG B 1 59  ? 37.153 3.537   43.911  1.00 23.14 ? 53  ARG B O      1 
ATOM   3103 C CB     . ARG B 1 59  ? 34.950 3.608   41.689  1.00 21.20 ? 53  ARG B CB     1 
ATOM   3104 C CG     . ARG B 1 59  ? 34.093 4.681   41.023  1.00 21.28 ? 53  ARG B CG     1 
ATOM   3105 C CD     . ARG B 1 59  ? 32.840 4.191   40.306  1.00 20.16 ? 53  ARG B CD     1 
ATOM   3106 N NE     . ARG B 1 59  ? 32.250 5.338   39.627  1.00 23.52 ? 53  ARG B NE     1 
ATOM   3107 C CZ     . ARG B 1 59  ? 32.692 5.822   38.471  1.00 23.67 ? 53  ARG B CZ     1 
ATOM   3108 N NH1    . ARG B 1 59  ? 33.630 5.196   37.769  1.00 22.50 ? 53  ARG B NH1    1 
ATOM   3109 N NH2    . ARG B 1 59  ? 32.194 6.968   38.014  1.00 23.45 ? 53  ARG B NH2    1 
ATOM   3110 N N      . ALA B 1 60  ? 38.046 2.269   42.279  1.00 23.54 ? 54  ALA B N      1 
ATOM   3111 C CA     . ALA B 1 60  ? 38.858 1.463   43.181  1.00 23.26 ? 54  ALA B CA     1 
ATOM   3112 C C      . ALA B 1 60  ? 39.950 2.302   43.846  1.00 24.42 ? 54  ALA B C      1 
ATOM   3113 O O      . ALA B 1 60  ? 40.509 3.225   43.248  1.00 26.26 ? 54  ALA B O      1 
ATOM   3114 C CB     . ALA B 1 60  ? 39.516 0.332   42.388  1.00 22.66 ? 54  ALA B CB     1 
ATOM   3115 N N      . THR B 1 61  ? 40.247 1.974   45.105  1.00 22.25 ? 55  THR B N      1 
ATOM   3116 C CA     . THR B 1 61  ? 41.340 2.600   45.843  1.00 24.15 ? 55  THR B CA     1 
ATOM   3117 C C      . THR B 1 61  ? 42.076 1.526   46.637  1.00 27.04 ? 55  THR B C      1 
ATOM   3118 O O      . THR B 1 61  ? 41.521 0.475   46.966  1.00 24.92 ? 55  THR B O      1 
ATOM   3119 C CB     . THR B 1 61  ? 40.840 3.663   46.838  1.00 25.96 ? 55  THR B CB     1 
ATOM   3120 O OG1    . THR B 1 61  ? 39.823 3.100   47.680  1.00 23.79 ? 55  THR B OG1    1 
ATOM   3121 C CG2    . THR B 1 61  ? 40.280 4.877   46.118  1.00 27.15 ? 55  THR B CG2    1 
ATOM   3122 N N      . ALA B 1 62  ? 43.334 1.808   46.969  1.00 26.54 ? 56  ALA B N      1 
ATOM   3123 C CA     . ALA B 1 62  ? 44.108 0.852   47.748  1.00 27.22 ? 56  ALA B CA     1 
ATOM   3124 C C      . ALA B 1 62  ? 43.476 0.675   49.121  1.00 26.02 ? 56  ALA B C      1 
ATOM   3125 O O      . ALA B 1 62  ? 43.327 1.641   49.874  1.00 28.41 ? 56  ALA B O      1 
ATOM   3126 C CB     . ALA B 1 62  ? 45.552 1.335   47.882  1.00 28.38 ? 56  ALA B CB     1 
ATOM   3127 N N      . GLY B 1 63  ? 43.074 -0.556  49.427  1.00 24.20 ? 57  GLY B N      1 
ATOM   3128 C CA     . GLY B 1 63  ? 42.392 -0.851  50.664  1.00 24.81 ? 57  GLY B CA     1 
ATOM   3129 C C      . GLY B 1 63  ? 40.942 -0.427  50.719  1.00 24.55 ? 57  GLY B C      1 
ATOM   3130 O O      . GLY B 1 63  ? 40.352 -0.436  51.807  1.00 25.78 ? 57  GLY B O      1 
ATOM   3131 N N      . GLY B 1 64  ? 40.351 -0.038  49.593  1.00 24.04 ? 58  GLY B N      1 
ATOM   3132 C CA     . GLY B 1 64  ? 38.937 0.315   49.566  1.00 24.92 ? 58  GLY B CA     1 
ATOM   3133 C C      . GLY B 1 64  ? 38.057 -0.864  49.180  1.00 27.07 ? 58  GLY B C      1 
ATOM   3134 O O      . GLY B 1 64  ? 38.467 -1.752  48.444  1.00 25.15 ? 58  GLY B O      1 
ATOM   3135 N N      . PHE B 1 65  ? 36.819 -0.853  49.673  1.00 24.75 ? 59  PHE B N      1 
ATOM   3136 C CA     . PHE B 1 65  ? 35.864 -1.931  49.431  1.00 22.57 ? 59  PHE B CA     1 
ATOM   3137 C C      . PHE B 1 65  ? 34.837 -1.515  48.377  1.00 22.20 ? 59  PHE B C      1 
ATOM   3138 O O      . PHE B 1 65  ? 34.234 -0.437  48.472  1.00 22.68 ? 59  PHE B O      1 
ATOM   3139 C CB     . PHE B 1 65  ? 35.157 -2.304  50.745  1.00 21.75 ? 59  PHE B CB     1 
ATOM   3140 C CG     . PHE B 1 65  ? 34.162 -3.439  50.620  1.00 21.31 ? 59  PHE B CG     1 
ATOM   3141 C CD1    . PHE B 1 65  ? 34.386 -4.504  49.748  1.00 23.97 ? 59  PHE B CD1    1 
ATOM   3142 C CD2    . PHE B 1 65  ? 33.001 -3.443  51.393  1.00 22.25 ? 59  PHE B CD2    1 
ATOM   3143 C CE1    . PHE B 1 65  ? 33.469 -5.548  49.643  1.00 20.36 ? 59  PHE B CE1    1 
ATOM   3144 C CE2    . PHE B 1 65  ? 32.078 -4.488  51.297  1.00 23.07 ? 59  PHE B CE2    1 
ATOM   3145 C CZ     . PHE B 1 65  ? 32.309 -5.540  50.422  1.00 21.52 ? 59  PHE B CZ     1 
ATOM   3146 N N      . LEU B 1 66  ? 34.626 -2.384  47.394  1.00 20.16 ? 60  LEU B N      1 
ATOM   3147 C CA     . LEU B 1 66  ? 33.678 -2.165  46.306  1.00 18.63 ? 60  LEU B CA     1 
ATOM   3148 C C      . LEU B 1 66  ? 32.676 -3.307  46.286  1.00 21.58 ? 60  LEU B C      1 
ATOM   3149 O O      . LEU B 1 66  ? 33.048 -4.478  46.417  1.00 20.74 ? 60  LEU B O      1 
ATOM   3150 C CB     . LEU B 1 66  ? 34.395 -2.139  44.942  1.00 21.76 ? 60  LEU B CB     1 
ATOM   3151 C CG     . LEU B 1 66  ? 35.551 -1.166  44.692  1.00 24.38 ? 60  LEU B CG     1 
ATOM   3152 C CD1    . LEU B 1 66  ? 36.090 -1.362  43.271  1.00 24.81 ? 60  LEU B CD1    1 
ATOM   3153 C CD2    . LEU B 1 66  ? 35.131 0.276   44.894  1.00 25.19 ? 60  LEU B CD2    1 
ATOM   3154 N N      . ILE B 1 67  ? 31.402 -2.975  46.077  1.00 20.30 ? 61  ILE B N      1 
ATOM   3155 C CA     . ILE B 1 67  ? 30.363 -3.968  45.835  1.00 18.87 ? 61  ILE B CA     1 
ATOM   3156 C C      . ILE B 1 67  ? 29.828 -3.751  44.423  1.00 18.73 ? 61  ILE B C      1 
ATOM   3157 O O      . ILE B 1 67  ? 29.493 -2.619  44.056  1.00 22.68 ? 61  ILE B O      1 
ATOM   3158 C CB     . ILE B 1 67  ? 29.235 -3.863  46.876  1.00 21.29 ? 61  ILE B CB     1 
ATOM   3159 C CG1    . ILE B 1 67  ? 29.802 -3.922  48.300  1.00 21.63 ? 61  ILE B CG1    1 
ATOM   3160 C CG2    . ILE B 1 67  ? 28.227 -4.979  46.646  1.00 21.65 ? 61  ILE B CG2    1 
ATOM   3161 C CD1    . ILE B 1 67  ? 28.786 -3.537  49.389  1.00 21.66 ? 61  ILE B CD1    1 
ATOM   3162 N N      . THR B 1 68  ? 29.771 -4.825  43.631  1.00 20.08 ? 62  THR B N      1 
ATOM   3163 C CA     . THR B 1 68  ? 29.304 -4.697  42.251  1.00 18.41 ? 62  THR B CA     1 
ATOM   3164 C C      . THR B 1 68  ? 27.795 -4.482  42.195  1.00 21.55 ? 62  THR B C      1 
ATOM   3165 O O      . THR B 1 68  ? 27.046 -4.763  43.142  1.00 21.78 ? 62  THR B O      1 
ATOM   3166 C CB     . THR B 1 68  ? 29.589 -5.953  41.417  1.00 20.93 ? 62  THR B CB     1 
ATOM   3167 O OG1    . THR B 1 68  ? 28.679 -7.000  41.775  1.00 21.80 ? 62  THR B OG1    1 
ATOM   3168 C CG2    . THR B 1 68  ? 31.017 -6.430  41.567  1.00 22.61 ? 62  THR B CG2    1 
ATOM   3169 N N      . GLU B 1 69  ? 27.355 -4.025  41.024  1.00 20.61 ? 63  GLU B N      1 
ATOM   3170 C CA     . GLU B 1 69  ? 25.942 -4.035  40.678  1.00 21.63 ? 63  GLU B CA     1 
ATOM   3171 C C      . GLU B 1 69  ? 25.357 -5.421  40.917  1.00 20.53 ? 63  GLU B C      1 
ATOM   3172 O O      . GLU B 1 69  ? 26.061 -6.435  40.861  1.00 20.95 ? 63  GLU B O      1 
ATOM   3173 C CB     . GLU B 1 69  ? 25.794 -3.775  39.180  1.00 22.75 ? 63  GLU B CB     1 
ATOM   3174 C CG     . GLU B 1 69  ? 26.626 -4.706  38.300  1.00 22.27 ? 63  GLU B CG     1 
ATOM   3175 C CD     . GLU B 1 69  ? 27.206 -4.025  37.075  1.00 24.64 ? 63  GLU B CD     1 
ATOM   3176 O OE1    . GLU B 1 69  ? 28.326 -3.468  37.133  1.00 26.55 ? 63  GLU B OE1    1 
ATOM   3177 O OE2    . GLU B 1 69  ? 26.520 -4.036  36.029  1.00 25.42 ? 63  GLU B OE2    1 
ATOM   3178 N N      . GLY B 1 70  ? 24.041 -5.474  41.137  1.00 17.63 ? 64  GLY B N      1 
ATOM   3179 C CA     . GLY B 1 70  ? 23.385 -6.767  41.205  1.00 19.42 ? 64  GLY B CA     1 
ATOM   3180 C C      . GLY B 1 70  ? 23.676 -7.635  39.995  1.00 20.27 ? 64  GLY B C      1 
ATOM   3181 O O      . GLY B 1 70  ? 23.633 -7.153  38.863  1.00 20.45 ? 64  GLY B O      1 
ATOM   3182 N N      . THR B 1 71  ? 23.950 -8.917  40.220  1.00 18.58 ? 65  THR B N      1 
ATOM   3183 C CA     . THR B 1 71  ? 24.377 -9.847  39.182  1.00 18.03 ? 65  THR B CA     1 
ATOM   3184 C C      . THR B 1 71  ? 23.449 -11.057 39.183  1.00 20.57 ? 65  THR B C      1 
ATOM   3185 O O      . THR B 1 71  ? 23.083 -11.564 40.257  1.00 20.70 ? 65  THR B O      1 
ATOM   3186 C CB     . THR B 1 71  ? 25.838 -10.241 39.468  1.00 20.41 ? 65  THR B CB     1 
ATOM   3187 O OG1    . THR B 1 71  ? 26.661 -9.058  39.399  1.00 22.73 ? 65  THR B OG1    1 
ATOM   3188 C CG2    . THR B 1 71  ? 26.359 -11.271 38.468  1.00 23.43 ? 65  THR B CG2    1 
ATOM   3189 N N      . MET B 1 72  ? 23.026 -11.490 37.991  1.00 21.74 ? 66  MET B N      1 
ATOM   3190 C CA     . MET B 1 72  ? 22.077 -12.590 37.919  1.00 21.25 ? 66  MET B CA     1 
ATOM   3191 C C      . MET B 1 72  ? 22.667 -13.914 38.371  1.00 20.07 ? 66  MET B C      1 
ATOM   3192 O O      . MET B 1 72  ? 23.833 -14.221 38.117  1.00 21.48 ? 66  MET B O      1 
ATOM   3193 C CB     . MET B 1 72  ? 21.443 -12.827 36.524  1.00 24.82 ? 66  MET B CB     1 
ATOM   3194 C CG     . MET B 1 72  ? 20.784 -11.677 35.772  1.00 22.39 ? 66  MET B CG     1 
ATOM   3195 S SD     . MET B 1 72  ? 20.917 -11.768 33.969  1.00 22.28 ? 66  MET B SD     1 
ATOM   3196 C CE     . MET B 1 72  ? 19.853 -13.193 33.746  1.00 24.92 ? 66  MET B CE     1 
ATOM   3197 N N      . ILE B 1 73  ? 21.811 -14.725 39.000  1.00 23.18 ? 67  ILE B N      1 
ATOM   3198 C CA     . ILE B 1 73  ? 22.167 -16.059 39.461  1.00 19.83 ? 67  ILE B CA     1 
ATOM   3199 C C      . ILE B 1 73  ? 21.598 -17.159 38.583  1.00 23.17 ? 67  ILE B C      1 
ATOM   3200 O O      . ILE B 1 73  ? 21.865 -18.342 38.841  1.00 23.67 ? 67  ILE B O      1 
ATOM   3201 C CB     . ILE B 1 73  ? 21.721 -16.283 40.925  1.00 18.54 ? 67  ILE B CB     1 
ATOM   3202 C CG1    . ILE B 1 73  ? 20.188 -16.217 41.045  1.00 20.39 ? 67  ILE B CG1    1 
ATOM   3203 C CG2    . ILE B 1 73  ? 22.406 -15.303 41.864  1.00 22.08 ? 67  ILE B CG2    1 
ATOM   3204 C CD1    . ILE B 1 73  ? 19.646 -16.658 42.437  1.00 21.28 ? 67  ILE B CD1    1 
ATOM   3205 N N      . SER B 1 74  ? 20.802 -16.816 37.576  1.00 23.50 ? 68  SER B N      1 
ATOM   3206 C CA     . SER B 1 74  ? 20.126 -17.802 36.743  1.00 24.60 ? 68  SER B CA     1 
ATOM   3207 C C      . SER B 1 74  ? 19.461 -17.068 35.586  1.00 25.70 ? 68  SER B C      1 
ATOM   3208 O O      . SER B 1 74  ? 19.299 -15.846 35.639  1.00 23.32 ? 68  SER B O      1 
ATOM   3209 C CB     . SER B 1 74  ? 19.056 -18.558 37.544  1.00 24.32 ? 68  SER B CB     1 
ATOM   3210 O OG     . SER B 1 74  ? 17.917 -17.734 37.742  1.00 25.03 ? 68  SER B OG     1 
ATOM   3211 N N      . PRO B 1 75  ? 19.064 -17.797 34.537  1.00 26.87 ? 69  PRO B N      1 
ATOM   3212 C CA     . PRO B 1 75  ? 18.391 -17.143 33.401  1.00 27.55 ? 69  PRO B CA     1 
ATOM   3213 C C      . PRO B 1 75  ? 17.082 -16.465 33.754  1.00 26.05 ? 69  PRO B C      1 
ATOM   3214 O O      . PRO B 1 75  ? 16.619 -15.611 32.984  1.00 25.35 ? 69  PRO B O      1 
ATOM   3215 C CB     . PRO B 1 75  ? 18.158 -18.299 32.417  1.00 25.98 ? 69  PRO B CB     1 
ATOM   3216 C CG     . PRO B 1 75  ? 19.224 -19.278 32.727  1.00 24.40 ? 69  PRO B CG     1 
ATOM   3217 C CD     . PRO B 1 75  ? 19.408 -19.200 34.233  1.00 26.56 ? 69  PRO B CD     1 
ATOM   3218 N N      . THR B 1 76  ? 16.458 -16.824 34.875  1.00 23.54 ? 70  THR B N      1 
ATOM   3219 C CA     . THR B 1 76  ? 15.150 -16.302 35.235  1.00 26.74 ? 70  THR B CA     1 
ATOM   3220 C C      . THR B 1 76  ? 15.224 -15.185 36.272  1.00 25.08 ? 70  THR B C      1 
ATOM   3221 O O      . THR B 1 76  ? 14.179 -14.703 36.720  1.00 23.42 ? 70  THR B O      1 
ATOM   3222 C CB     . THR B 1 76  ? 14.249 -17.439 35.731  1.00 31.60 ? 70  THR B CB     1 
ATOM   3223 O OG1    . THR B 1 76  ? 14.942 -18.199 36.733  1.00 31.16 ? 70  THR B OG1    1 
ATOM   3224 C CG2    . THR B 1 76  ? 13.884 -18.362 34.569  1.00 31.20 ? 70  THR B CG2    1 
ATOM   3225 N N      . SER B 1 77  ? 16.428 -14.731 36.630  1.00 21.31 ? 71  SER B N      1 
ATOM   3226 C CA     . SER B 1 77  ? 16.618 -13.843 37.771  1.00 21.89 ? 71  SER B CA     1 
ATOM   3227 C C      . SER B 1 77  ? 16.643 -12.354 37.419  1.00 24.42 ? 71  SER B C      1 
ATOM   3228 O O      . SER B 1 77  ? 16.797 -11.530 38.321  1.00 22.44 ? 71  SER B O      1 
ATOM   3229 C CB     . SER B 1 77  ? 17.896 -14.239 38.524  1.00 23.73 ? 71  SER B CB     1 
ATOM   3230 O OG     . SER B 1 77  ? 19.024 -14.001 37.710  1.00 27.06 ? 71  SER B OG     1 
ATOM   3231 N N      . ALA B 1 78  ? 16.488 -11.975 36.149  1.00 21.19 ? 72  ALA B N      1 
ATOM   3232 C CA     . ALA B 1 78  ? 16.684 -10.586 35.752  1.00 19.81 ? 72  ALA B CA     1 
ATOM   3233 C C      . ALA B 1 78  ? 15.370 -9.836  35.549  1.00 20.71 ? 72  ALA B C      1 
ATOM   3234 O O      . ALA B 1 78  ? 14.359 -10.406 35.127  1.00 21.35 ? 72  ALA B O      1 
ATOM   3235 C CB     . ALA B 1 78  ? 17.509 -10.494 34.460  1.00 22.95 ? 72  ALA B CB     1 
ATOM   3236 N N      . GLY B 1 79  ? 15.421 -8.531  35.813  1.00 20.71 ? 73  GLY B N      1 
ATOM   3237 C CA     . GLY B 1 79  ? 14.295 -7.639  35.621  1.00 19.86 ? 73  GLY B CA     1 
ATOM   3238 C C      . GLY B 1 79  ? 14.751 -6.268  35.170  1.00 20.92 ? 73  GLY B C      1 
ATOM   3239 O O      . GLY B 1 79  ? 14.011 -5.288  35.283  1.00 23.75 ? 73  GLY B O      1 
ATOM   3240 N N      . PHE B 1 80  ? 15.973 -6.192  34.653  1.00 20.11 ? 74  PHE B N      1 
ATOM   3241 C CA     . PHE B 1 80  ? 16.540 -4.980  34.090  1.00 19.20 ? 74  PHE B CA     1 
ATOM   3242 C C      . PHE B 1 80  ? 17.309 -5.396  32.841  1.00 20.94 ? 74  PHE B C      1 
ATOM   3243 O O      . PHE B 1 80  ? 17.731 -6.552  32.727  1.00 21.26 ? 74  PHE B O      1 
ATOM   3244 C CB     . PHE B 1 80  ? 17.543 -4.345  35.065  1.00 22.33 ? 74  PHE B CB     1 
ATOM   3245 C CG     . PHE B 1 80  ? 16.950 -3.314  35.998  1.00 21.21 ? 74  PHE B CG     1 
ATOM   3246 C CD1    . PHE B 1 80  ? 16.200 -3.697  37.098  1.00 20.85 ? 74  PHE B CD1    1 
ATOM   3247 C CD2    . PHE B 1 80  ? 17.151 -1.956  35.765  1.00 23.26 ? 74  PHE B CD2    1 
ATOM   3248 C CE1    . PHE B 1 80  ? 15.666 -2.743  37.972  1.00 22.56 ? 74  PHE B CE1    1 
ATOM   3249 C CE2    . PHE B 1 80  ? 16.607 -0.997  36.619  1.00 20.77 ? 74  PHE B CE2    1 
ATOM   3250 C CZ     . PHE B 1 80  ? 15.874 -1.394  37.731  1.00 22.67 ? 74  PHE B CZ     1 
ATOM   3251 N N      . PRO B 1 81  ? 17.518 -4.479  31.905  1.00 19.55 ? 75  PRO B N      1 
ATOM   3252 C CA     . PRO B 1 81  ? 18.260 -4.845  30.692  1.00 20.28 ? 75  PRO B CA     1 
ATOM   3253 C C      . PRO B 1 81  ? 19.761 -4.794  30.928  1.00 20.28 ? 75  PRO B C      1 
ATOM   3254 O O      . PRO B 1 81  ? 20.271 -3.930  31.647  1.00 20.50 ? 75  PRO B O      1 
ATOM   3255 C CB     . PRO B 1 81  ? 17.822 -3.773  29.687  1.00 22.99 ? 75  PRO B CB     1 
ATOM   3256 C CG     . PRO B 1 81  ? 17.612 -2.556  30.526  1.00 22.80 ? 75  PRO B CG     1 
ATOM   3257 C CD     . PRO B 1 81  ? 17.118 -3.058  31.897  1.00 20.71 ? 75  PRO B CD     1 
ATOM   3258 N N      . HIS B 1 82  ? 20.466 -5.759  30.331  1.00 20.40 ? 76  HIS B N      1 
ATOM   3259 C CA     . HIS B 1 82  ? 21.929 -5.723  30.242  1.00 20.16 ? 76  HIS B CA     1 
ATOM   3260 C C      . HIS B 1 82  ? 22.579 -5.651  31.621  1.00 21.18 ? 76  HIS B C      1 
ATOM   3261 O O      . HIS B 1 82  ? 23.523 -4.893  31.850  1.00 22.02 ? 76  HIS B O      1 
ATOM   3262 C CB     . HIS B 1 82  ? 22.384 -4.598  29.323  1.00 20.15 ? 76  HIS B CB     1 
ATOM   3263 C CG     . HIS B 1 82  ? 21.699 -4.637  27.995  1.00 20.85 ? 76  HIS B CG     1 
ATOM   3264 N ND1    . HIS B 1 82  ? 21.891 -5.671  27.107  1.00 21.86 ? 76  HIS B ND1    1 
ATOM   3265 C CD2    . HIS B 1 82  ? 20.766 -3.828  27.441  1.00 23.54 ? 76  HIS B CD2    1 
ATOM   3266 C CE1    . HIS B 1 82  ? 21.137 -5.474  26.037  1.00 22.90 ? 76  HIS B CE1    1 
ATOM   3267 N NE2    . HIS B 1 82  ? 20.443 -4.364  26.218  1.00 22.31 ? 76  HIS B NE2    1 
ATOM   3268 N N      . VAL B 1 83  ? 22.063 -6.453  32.540  1.00 20.44 ? 77  VAL B N      1 
ATOM   3269 C CA     . VAL B 1 83  ? 22.696 -6.630  33.844  1.00 21.46 ? 77  VAL B CA     1 
ATOM   3270 C C      . VAL B 1 83  ? 23.591 -7.860  33.756  1.00 19.57 ? 77  VAL B C      1 
ATOM   3271 O O      . VAL B 1 83  ? 23.240 -8.832  33.066  1.00 22.83 ? 77  VAL B O      1 
ATOM   3272 C CB     . VAL B 1 83  ? 21.655 -6.723  34.969  1.00 24.80 ? 77  VAL B CB     1 
ATOM   3273 C CG1    . VAL B 1 83  ? 20.870 -5.433  35.056  1.00 24.77 ? 77  VAL B CG1    1 
ATOM   3274 C CG2    . VAL B 1 83  ? 20.728 -7.906  34.763  1.00 21.83 ? 77  VAL B CG2    1 
ATOM   3275 N N      . PRO B 1 84  ? 24.754 -7.857  34.396  1.00 19.78 ? 78  PRO B N      1 
ATOM   3276 C CA     . PRO B 1 84  ? 25.668 -8.993  34.255  1.00 22.67 ? 78  PRO B CA     1 
ATOM   3277 C C      . PRO B 1 84  ? 25.123 -10.216 34.966  1.00 26.07 ? 78  PRO B C      1 
ATOM   3278 O O      . PRO B 1 84  ? 24.379 -10.112 35.942  1.00 22.33 ? 78  PRO B O      1 
ATOM   3279 C CB     . PRO B 1 84  ? 26.954 -8.499  34.931  1.00 21.13 ? 78  PRO B CB     1 
ATOM   3280 C CG     . PRO B 1 84  ? 26.497 -7.478  35.930  1.00 24.16 ? 78  PRO B CG     1 
ATOM   3281 C CD     . PRO B 1 84  ? 25.271 -6.825  35.310  1.00 20.80 ? 78  PRO B CD     1 
ATOM   3282 N N      . GLY B 1 85  ? 25.493 -11.390 34.453  1.00 20.97 ? 79  GLY B N      1 
ATOM   3283 C CA     . GLY B 1 85  ? 25.259 -12.640 35.135  1.00 22.47 ? 79  GLY B CA     1 
ATOM   3284 C C      . GLY B 1 85  ? 26.562 -13.213 35.675  1.00 20.70 ? 79  GLY B C      1 
ATOM   3285 O O      . GLY B 1 85  ? 27.660 -12.793 35.304  1.00 21.74 ? 79  GLY B O      1 
ATOM   3286 N N      . ILE B 1 86  ? 26.421 -14.184 36.582  1.00 20.26 ? 80  ILE B N      1 
ATOM   3287 C CA     . ILE B 1 86  ? 27.581 -14.967 37.003  1.00 23.83 ? 80  ILE B CA     1 
ATOM   3288 C C      . ILE B 1 86  ? 27.232 -16.454 37.035  1.00 28.90 ? 80  ILE B C      1 
ATOM   3289 O O      . ILE B 1 86  ? 27.830 -17.235 37.785  1.00 28.07 ? 80  ILE B O      1 
ATOM   3290 C CB     . ILE B 1 86  ? 28.192 -14.437 38.321  1.00 29.67 ? 80  ILE B CB     1 
ATOM   3291 C CG1    . ILE B 1 86  ? 29.660 -14.885 38.470  1.00 30.13 ? 80  ILE B CG1    1 
ATOM   3292 C CG2    . ILE B 1 86  ? 27.340 -14.803 39.524  1.00 24.05 ? 80  ILE B CG2    1 
ATOM   3293 C CD1    . ILE B 1 86  ? 30.521 -13.902 39.225  1.00 28.95 ? 80  ILE B CD1    1 
ATOM   3294 N N      . PHE B 1 87  ? 26.279 -16.865 36.193  1.00 24.76 ? 81  PHE B N      1 
ATOM   3295 C CA     . PHE B 1 87  ? 25.828 -18.251 36.174  1.00 28.43 ? 81  PHE B CA     1 
ATOM   3296 C C      . PHE B 1 87  ? 26.401 -19.083 35.033  1.00 30.84 ? 81  PHE B C      1 
ATOM   3297 O O      . PHE B 1 87  ? 26.158 -20.294 35.006  1.00 33.13 ? 81  PHE B O      1 
ATOM   3298 C CB     . PHE B 1 87  ? 24.289 -18.356 36.189  1.00 29.35 ? 81  PHE B CB     1 
ATOM   3299 C CG     . PHE B 1 87  ? 23.604 -17.620 35.068  1.00 30.33 ? 81  PHE B CG     1 
ATOM   3300 C CD1    . PHE B 1 87  ? 23.329 -16.262 35.172  1.00 24.07 ? 81  PHE B CD1    1 
ATOM   3301 C CD2    . PHE B 1 87  ? 23.223 -18.288 33.918  1.00 28.49 ? 81  PHE B CD2    1 
ATOM   3302 C CE1    . PHE B 1 87  ? 22.688 -15.583 34.149  1.00 24.62 ? 81  PHE B CE1    1 
ATOM   3303 C CE2    . PHE B 1 87  ? 22.593 -17.615 32.878  1.00 25.03 ? 81  PHE B CE2    1 
ATOM   3304 C CZ     . PHE B 1 87  ? 22.326 -16.261 32.991  1.00 30.63 ? 81  PHE B CZ     1 
ATOM   3305 N N      . THR B 1 88  ? 27.151 -18.482 34.103  1.00 27.45 ? 82  THR B N      1 
ATOM   3306 C CA     . THR B 1 88  ? 27.769 -19.216 33.005  1.00 32.41 ? 82  THR B CA     1 
ATOM   3307 C C      . THR B 1 88  ? 29.284 -19.078 33.051  1.00 30.77 ? 82  THR B C      1 
ATOM   3308 O O      . THR B 1 88  ? 29.832 -18.126 33.610  1.00 27.50 ? 82  THR B O      1 
ATOM   3309 C CB     . THR B 1 88  ? 27.266 -18.755 31.628  1.00 27.99 ? 82  THR B CB     1 
ATOM   3310 O OG1    . THR B 1 88  ? 27.902 -17.522 31.262  1.00 28.67 ? 82  THR B OG1    1 
ATOM   3311 C CG2    . THR B 1 88  ? 25.765 -18.579 31.619  1.00 27.01 ? 82  THR B CG2    1 
ATOM   3312 N N      . LYS B 1 89  ? 29.965 -20.049 32.442  1.00 35.28 ? 83  LYS B N      1 
ATOM   3313 C CA     . LYS B 1 89  ? 31.423 -19.993 32.428  1.00 37.70 ? 83  LYS B CA     1 
ATOM   3314 C C      . LYS B 1 89  ? 31.929 -18.825 31.590  1.00 28.49 ? 83  LYS B C      1 
ATOM   3315 O O      . LYS B 1 89  ? 32.974 -18.247 31.907  1.00 29.94 ? 83  LYS B O      1 
ATOM   3316 C CB     . LYS B 1 89  ? 32.005 -21.334 31.980  1.00 45.89 ? 83  LYS B CB     1 
ATOM   3317 C CG     . LYS B 1 89  ? 31.837 -22.429 33.036  1.00 45.45 ? 83  LYS B CG     1 
ATOM   3318 C CD     . LYS B 1 89  ? 32.110 -21.897 34.444  1.00 52.67 ? 83  LYS B CD     1 
ATOM   3319 C CE     . LYS B 1 89  ? 32.406 -23.020 35.421  1.00 49.40 ? 83  LYS B CE     1 
ATOM   3320 N NZ     . LYS B 1 89  ? 31.573 -22.936 36.652  1.00 50.31 ? 83  LYS B NZ     1 
ATOM   3321 N N      . GLU B 1 90  ? 31.189 -18.440 30.550  1.00 32.26 ? 84  GLU B N      1 
ATOM   3322 C CA     . GLU B 1 90  ? 31.553 -17.247 29.789  1.00 30.59 ? 84  GLU B CA     1 
ATOM   3323 C C      . GLU B 1 90  ? 31.514 -15.999 30.665  1.00 29.02 ? 84  GLU B C      1 
ATOM   3324 O O      . GLU B 1 90  ? 32.415 -15.151 30.599  1.00 28.84 ? 84  GLU B O      1 
ATOM   3325 C CB     . GLU B 1 90  ? 30.632 -17.086 28.581  1.00 32.20 ? 84  GLU B CB     1 
ATOM   3326 C CG     . GLU B 1 90  ? 30.974 -15.873 27.720  1.00 38.35 ? 84  GLU B CG     1 
ATOM   3327 C CD     . GLU B 1 90  ? 29.998 -15.639 26.572  1.00 59.51 ? 84  GLU B CD     1 
ATOM   3328 O OE1    . GLU B 1 90  ? 28.861 -16.156 26.626  1.00 56.65 ? 84  GLU B OE1    1 
ATOM   3329 O OE2    . GLU B 1 90  ? 30.377 -14.934 25.609  1.00 58.33 ? 84  GLU B OE2    1 
ATOM   3330 N N      . GLN B 1 91  ? 30.475 -15.867 31.493  1.00 25.45 ? 85  GLN B N      1 
ATOM   3331 C CA     . GLN B 1 91  ? 30.398 -14.725 32.396  1.00 24.93 ? 85  GLN B CA     1 
ATOM   3332 C C      . GLN B 1 91  ? 31.537 -14.741 33.406  1.00 23.37 ? 85  GLN B C      1 
ATOM   3333 O O      . GLN B 1 91  ? 32.124 -13.694 33.699  1.00 25.38 ? 85  GLN B O      1 
ATOM   3334 C CB     . GLN B 1 91  ? 29.037 -14.703 33.098  1.00 21.12 ? 85  GLN B CB     1 
ATOM   3335 C CG     . GLN B 1 91  ? 27.890 -14.397 32.149  1.00 22.79 ? 85  GLN B CG     1 
ATOM   3336 C CD     . GLN B 1 91  ? 26.551 -14.883 32.664  1.00 22.88 ? 85  GLN B CD     1 
ATOM   3337 O OE1    . GLN B 1 91  ? 26.468 -15.577 33.684  1.00 24.52 ? 85  GLN B OE1    1 
ATOM   3338 N NE2    . GLN B 1 91  ? 25.486 -14.523 31.955  1.00 25.50 ? 85  GLN B NE2    1 
ATOM   3339 N N      . VAL B 1 92  ? 31.858 -15.916 33.953  1.00 24.51 ? 86  VAL B N      1 
ATOM   3340 C CA     . VAL B 1 92  ? 32.987 -16.026 34.877  1.00 25.88 ? 86  VAL B CA     1 
ATOM   3341 C C      . VAL B 1 92  ? 34.270 -15.531 34.222  1.00 26.98 ? 86  VAL B C      1 
ATOM   3342 O O      . VAL B 1 92  ? 35.028 -14.750 34.808  1.00 25.57 ? 86  VAL B O      1 
ATOM   3343 C CB     . VAL B 1 92  ? 33.126 -17.466 35.408  1.00 25.32 ? 86  VAL B CB     1 
ATOM   3344 C CG1    . VAL B 1 92  ? 34.434 -17.625 36.173  1.00 28.44 ? 86  VAL B CG1    1 
ATOM   3345 C CG2    . VAL B 1 92  ? 31.940 -17.827 36.300  1.00 27.21 ? 86  VAL B CG2    1 
ATOM   3346 N N      . ARG B 1 93  ? 34.523 -15.960 32.982  1.00 27.39 ? 87  ARG B N      1 
ATOM   3347 C CA     . ARG B 1 93  ? 35.763 -15.569 32.320  1.00 27.99 ? 87  ARG B CA     1 
ATOM   3348 C C      . ARG B 1 93  ? 35.849 -14.056 32.150  1.00 24.18 ? 87  ARG B C      1 
ATOM   3349 O O      . ARG B 1 93  ? 36.917 -13.464 32.334  1.00 26.72 ? 87  ARG B O      1 
ATOM   3350 C CB     . ARG B 1 93  ? 35.884 -16.286 30.973  1.00 32.14 ? 87  ARG B CB     1 
ATOM   3351 C CG     . ARG B 1 93  ? 36.342 -17.737 31.107  1.00 41.95 ? 87  ARG B CG     1 
ATOM   3352 C CD     . ARG B 1 93  ? 36.774 -18.321 29.769  1.00 49.02 ? 87  ARG B CD     1 
ATOM   3353 N NE     . ARG B 1 93  ? 35.639 -18.521 28.875  1.00 45.12 ? 87  ARG B NE     1 
ATOM   3354 C CZ     . ARG B 1 93  ? 34.829 -19.572 28.905  1.00 42.57 ? 87  ARG B CZ     1 
ATOM   3355 N NH1    . ARG B 1 93  ? 35.011 -20.562 29.766  1.00 48.15 ? 87  ARG B NH1    1 
ATOM   3356 N NH2    . ARG B 1 93  ? 33.813 -19.633 28.047  1.00 44.68 ? 87  ARG B NH2    1 
ATOM   3357 N N      . GLU B 1 94  ? 34.730 -13.408 31.815  1.00 24.14 ? 88  GLU B N      1 
ATOM   3358 C CA     . GLU B 1 94  ? 34.761 -11.961 31.616  1.00 25.26 ? 88  GLU B CA     1 
ATOM   3359 C C      . GLU B 1 94  ? 34.845 -11.203 32.940  1.00 24.64 ? 88  GLU B C      1 
ATOM   3360 O O      . GLU B 1 94  ? 35.522 -10.170 33.024  1.00 25.23 ? 88  GLU B O      1 
ATOM   3361 C CB     . GLU B 1 94  ? 33.556 -11.513 30.782  1.00 24.67 ? 88  GLU B CB     1 
ATOM   3362 C CG     . GLU B 1 94  ? 33.567 -12.071 29.366  1.00 26.38 ? 88  GLU B CG     1 
ATOM   3363 C CD     . GLU B 1 94  ? 34.918 -11.908 28.683  1.00 36.70 ? 88  GLU B CD     1 
ATOM   3364 O OE1    . GLU B 1 94  ? 35.417 -10.766 28.587  1.00 35.41 ? 88  GLU B OE1    1 
ATOM   3365 O OE2    . GLU B 1 94  ? 35.482 -12.930 28.245  1.00 41.72 ? 88  GLU B OE2    1 
ATOM   3366 N N      . TRP B 1 95  ? 34.179 -11.698 33.986  1.00 23.44 ? 89  TRP B N      1 
ATOM   3367 C CA     . TRP B 1 95  ? 34.302 -11.057 35.289  1.00 21.93 ? 89  TRP B CA     1 
ATOM   3368 C C      . TRP B 1 95  ? 35.739 -11.106 35.783  1.00 25.13 ? 89  TRP B C      1 
ATOM   3369 O O      . TRP B 1 95  ? 36.206 -10.170 36.440  1.00 23.04 ? 89  TRP B O      1 
ATOM   3370 C CB     . TRP B 1 95  ? 33.407 -11.756 36.307  1.00 22.83 ? 89  TRP B CB     1 
ATOM   3371 C CG     . TRP B 1 95  ? 32.025 -11.192 36.480  1.00 21.46 ? 89  TRP B CG     1 
ATOM   3372 C CD1    . TRP B 1 95  ? 30.851 -11.865 36.311  1.00 24.41 ? 89  TRP B CD1    1 
ATOM   3373 C CD2    . TRP B 1 95  ? 31.671 -9.863  36.895  1.00 22.36 ? 89  TRP B CD2    1 
ATOM   3374 N NE1    . TRP B 1 95  ? 29.787 -11.041 36.584  1.00 23.90 ? 89  TRP B NE1    1 
ATOM   3375 C CE2    . TRP B 1 95  ? 30.259 -9.805  36.941  1.00 22.04 ? 89  TRP B CE2    1 
ATOM   3376 C CE3    . TRP B 1 95  ? 32.405 -8.714  37.211  1.00 25.88 ? 89  TRP B CE3    1 
ATOM   3377 C CZ2    . TRP B 1 95  ? 29.562 -8.649  37.330  1.00 20.36 ? 89  TRP B CZ2    1 
ATOM   3378 C CZ3    . TRP B 1 95  ? 31.709 -7.558  37.588  1.00 24.50 ? 89  TRP B CZ3    1 
ATOM   3379 C CH2    . TRP B 1 95  ? 30.300 -7.539  37.637  1.00 20.65 ? 89  TRP B CH2    1 
ATOM   3380 N N      . LYS B 1 96  ? 36.456 -12.192 35.471  1.00 25.36 ? 90  LYS B N      1 
ATOM   3381 C CA     . LYS B 1 96  ? 37.822 -12.345 35.972  1.00 26.83 ? 90  LYS B CA     1 
ATOM   3382 C C      . LYS B 1 96  ? 38.713 -11.197 35.508  1.00 28.39 ? 90  LYS B C      1 
ATOM   3383 O O      . LYS B 1 96  ? 39.563 -10.711 36.264  1.00 27.63 ? 90  LYS B O      1 
ATOM   3384 C CB     . LYS B 1 96  ? 38.386 -13.694 35.526  1.00 31.52 ? 90  LYS B CB     1 
ATOM   3385 C CG     . LYS B 1 96  ? 39.715 -14.064 36.163  1.00 39.80 ? 90  LYS B CG     1 
ATOM   3386 C CD     . LYS B 1 96  ? 39.917 -15.574 36.166  1.00 51.06 ? 90  LYS B CD     1 
ATOM   3387 C CE     . LYS B 1 96  ? 41.147 -15.988 36.968  1.00 56.35 ? 90  LYS B CE     1 
ATOM   3388 N NZ     . LYS B 1 96  ? 41.990 -14.830 37.390  1.00 55.04 ? 90  LYS B NZ     1 
ATOM   3389 N N      . LYS B 1 97  ? 38.513 -10.736 34.272  1.00 26.12 ? 91  LYS B N      1 
ATOM   3390 C CA     . LYS B 1 97  ? 39.286 -9.615  33.750  1.00 29.99 ? 91  LYS B CA     1 
ATOM   3391 C C      . LYS B 1 97  ? 38.997 -8.325  34.508  1.00 30.03 ? 91  LYS B C      1 
ATOM   3392 O O      . LYS B 1 97  ? 39.896 -7.493  34.681  1.00 28.69 ? 91  LYS B O      1 
ATOM   3393 C CB     . LYS B 1 97  ? 38.989 -9.452  32.258  1.00 27.70 ? 91  LYS B CB     1 
ATOM   3394 C CG     . LYS B 1 97  ? 39.536 -10.608 31.421  1.00 33.86 ? 91  LYS B CG     1 
ATOM   3395 C CD     . LYS B 1 97  ? 38.524 -11.118 30.418  1.00 41.44 ? 91  LYS B CD     1 
ATOM   3396 C CE     . LYS B 1 97  ? 38.572 -10.298 29.155  1.00 45.63 ? 91  LYS B CE     1 
ATOM   3397 N NZ     . LYS B 1 97  ? 38.171 -11.073 27.937  1.00 42.39 ? 91  LYS B NZ     1 
ATOM   3398 N N      . ILE B 1 98  ? 37.754 -8.142  34.960  1.00 26.10 ? 92  ILE B N      1 
ATOM   3399 C CA     . ILE B 1 98  ? 37.383 -6.971  35.749  1.00 27.93 ? 92  ILE B CA     1 
ATOM   3400 C C      . ILE B 1 98  ? 37.941 -7.053  37.167  1.00 23.26 ? 92  ILE B C      1 
ATOM   3401 O O      . ILE B 1 98  ? 38.472 -6.070  37.694  1.00 26.89 ? 92  ILE B O      1 
ATOM   3402 C CB     . ILE B 1 98  ? 35.852 -6.813  35.720  1.00 25.04 ? 92  ILE B CB     1 
ATOM   3403 C CG1    . ILE B 1 98  ? 35.397 -6.492  34.294  1.00 25.80 ? 92  ILE B CG1    1 
ATOM   3404 C CG2    . ILE B 1 98  ? 35.371 -5.771  36.733  1.00 25.15 ? 92  ILE B CG2    1 
ATOM   3405 C CD1    . ILE B 1 98  ? 33.930 -6.777  34.071  1.00 28.21 ? 92  ILE B CD1    1 
ATOM   3406 N N      . VAL B 1 99  ? 37.816 -8.217  37.810  1.00 24.68 ? 93  VAL B N      1 
ATOM   3407 C CA     . VAL B 1 99  ? 38.330 -8.392  39.164  1.00 23.79 ? 93  VAL B CA     1 
ATOM   3408 C C      . VAL B 1 99  ? 39.838 -8.178  39.177  1.00 24.77 ? 93  VAL B C      1 
ATOM   3409 O O      . VAL B 1 99  ? 40.388 -7.599  40.118  1.00 24.23 ? 93  VAL B O      1 
ATOM   3410 C CB     . VAL B 1 99  ? 37.924 -9.787  39.679  1.00 25.71 ? 93  VAL B CB     1 
ATOM   3411 C CG1    . VAL B 1 99  ? 38.624 -10.123 40.983  1.00 26.27 ? 93  VAL B CG1    1 
ATOM   3412 C CG2    . VAL B 1 99  ? 36.400 -9.884  39.825  1.00 24.24 ? 93  VAL B CG2    1 
ATOM   3413 N N      . ASP B 1 100 ? 40.518 -8.573  38.102  1.00 25.50 ? 94  ASP B N      1 
ATOM   3414 C CA     . ASP B 1 100 ? 41.968 -8.441  38.073  1.00 27.48 ? 94  ASP B CA     1 
ATOM   3415 C C      . ASP B 1 100 ? 42.395 -6.977  38.046  1.00 26.91 ? 94  ASP B C      1 
ATOM   3416 O O      . ASP B 1 100 ? 43.347 -6.597  38.740  1.00 29.21 ? 94  ASP B O      1 
ATOM   3417 C CB     . ASP B 1 100 ? 42.512 -9.172  36.849  1.00 31.82 ? 94  ASP B CB     1 
ATOM   3418 C CG     . ASP B 1 100 ? 42.672 -10.661 37.086  1.00 34.19 ? 94  ASP B CG     1 
ATOM   3419 O OD1    . ASP B 1 100 ? 42.367 -11.124 38.202  1.00 34.63 ? 94  ASP B OD1    1 
ATOM   3420 O OD2    . ASP B 1 100 ? 43.074 -11.374 36.142  1.00 40.84 ? 94  ASP B OD2    1 
ATOM   3421 N N      . VAL B 1 101 ? 41.731 -6.144  37.230  1.00 24.43 ? 95  VAL B N      1 
ATOM   3422 C CA     . VAL B 1 101 ? 42.106 -4.729  37.203  1.00 25.03 ? 95  VAL B CA     1 
ATOM   3423 C C      . VAL B 1 101 ? 41.806 -4.053  38.535  1.00 28.26 ? 95  VAL B C      1 
ATOM   3424 O O      . VAL B 1 101 ? 42.555 -3.173  38.974  1.00 26.68 ? 95  VAL B O      1 
ATOM   3425 C CB     . VAL B 1 101 ? 41.507 -3.957  36.007  1.00 31.55 ? 95  VAL B CB     1 
ATOM   3426 C CG1    . VAL B 1 101 ? 42.053 -4.489  34.692  1.00 34.54 ? 95  VAL B CG1    1 
ATOM   3427 C CG2    . VAL B 1 101 ? 40.000 -4.008  36.016  1.00 36.32 ? 95  VAL B CG2    1 
ATOM   3428 N N      . VAL B 1 102 ? 40.713 -4.437  39.197  1.00 24.90 ? 96  VAL B N      1 
ATOM   3429 C CA     . VAL B 1 102 ? 40.387 -3.834  40.482  1.00 24.43 ? 96  VAL B CA     1 
ATOM   3430 C C      . VAL B 1 102 ? 41.394 -4.265  41.542  1.00 24.92 ? 96  VAL B C      1 
ATOM   3431 O O      . VAL B 1 102 ? 41.854 -3.451  42.355  1.00 27.03 ? 96  VAL B O      1 
ATOM   3432 C CB     . VAL B 1 102 ? 38.935 -4.187  40.866  1.00 25.50 ? 96  VAL B CB     1 
ATOM   3433 C CG1    . VAL B 1 102 ? 38.690 -3.938  42.325  1.00 29.93 ? 96  VAL B CG1    1 
ATOM   3434 C CG2    . VAL B 1 102 ? 37.967 -3.388  40.002  1.00 28.50 ? 96  VAL B CG2    1 
ATOM   3435 N N      . HIS B 1 103 ? 41.764 -5.547  41.540  1.00 25.70 ? 97  HIS B N      1 
ATOM   3436 C CA     . HIS B 1 103 ? 42.760 -6.039  42.489  1.00 23.65 ? 97  HIS B CA     1 
ATOM   3437 C C      . HIS B 1 103 ? 44.125 -5.402  42.271  1.00 27.62 ? 97  HIS B C      1 
ATOM   3438 O O      . HIS B 1 103 ? 44.877 -5.211  43.237  1.00 27.74 ? 97  HIS B O      1 
ATOM   3439 C CB     . HIS B 1 103 ? 42.853 -7.556  42.389  1.00 25.23 ? 97  HIS B CB     1 
ATOM   3440 C CG     . HIS B 1 103 ? 41.794 -8.273  43.161  1.00 24.86 ? 97  HIS B CG     1 
ATOM   3441 N ND1    . HIS B 1 103 ? 41.484 -9.597  42.944  1.00 27.85 ? 97  HIS B ND1    1 
ATOM   3442 C CD2    . HIS B 1 103 ? 40.985 -7.854  44.166  1.00 28.17 ? 97  HIS B CD2    1 
ATOM   3443 C CE1    . HIS B 1 103 ? 40.527 -9.964  43.779  1.00 26.05 ? 97  HIS B CE1    1 
ATOM   3444 N NE2    . HIS B 1 103 ? 40.216 -8.929  44.540  1.00 29.33 ? 97  HIS B NE2    1 
ATOM   3445 N N      . ALA B 1 104 ? 44.468 -5.068  41.024  1.00 27.53 ? 98  ALA B N      1 
ATOM   3446 C CA     . ALA B 1 104 ? 45.732 -4.389  40.757  1.00 28.13 ? 98  ALA B CA     1 
ATOM   3447 C C      . ALA B 1 104 ? 45.757 -2.962  41.288  1.00 31.74 ? 98  ALA B C      1 
ATOM   3448 O O      . ALA B 1 104 ? 46.831 -2.359  41.354  1.00 31.41 ? 98  ALA B O      1 
ATOM   3449 C CB     . ALA B 1 104 ? 46.044 -4.408  39.257  1.00 27.30 ? 98  ALA B CB     1 
ATOM   3450 N N      . LYS B 1 105 ? 44.618 -2.440  41.726  1.00 29.71 ? 99  LYS B N      1 
ATOM   3451 C CA     . LYS B 1 105 ? 44.612 -1.101  42.372  1.00 29.17 ? 99  LYS B CA     1 
ATOM   3452 C C      . LYS B 1 105 ? 44.589 -1.277  43.899  1.00 29.01 ? 99  LYS B C      1 
ATOM   3453 O O      . LYS B 1 105 ? 44.619 -0.270  44.595  1.00 33.44 ? 99  LYS B O      1 
ATOM   3454 C CB     . LYS B 1 105 ? 43.457 -0.263  41.818  1.00 31.75 ? 99  LYS B CB     1 
ATOM   3455 C CG     . LYS B 1 105 ? 43.746 0.374   40.470  1.00 39.86 ? 99  LYS B CG     1 
ATOM   3456 C CD     . LYS B 1 105 ? 42.838 1.525   40.144  1.00 46.98 ? 99  LYS B CD     1 
ATOM   3457 C CE     . LYS B 1 105 ? 42.996 2.718   41.059  1.00 42.81 ? 99  LYS B CE     1 
ATOM   3458 N NZ     . LYS B 1 105 ? 42.104 3.825   40.643  1.00 45.59 ? 99  LYS B NZ     1 
ATOM   3459 N N      . GLY B 1 106 ? 44.532 -2.521  44.377  1.00 29.79 ? 100 GLY B N      1 
ATOM   3460 C CA     . GLY B 1 106 ? 44.557 -2.800  45.825  1.00 26.81 ? 100 GLY B CA     1 
ATOM   3461 C C      . GLY B 1 106 ? 43.190 -2.857  46.484  1.00 25.95 ? 100 GLY B C      1 
ATOM   3462 O O      . GLY B 1 106 ? 43.129 -2.883  47.709  1.00 27.78 ? 100 GLY B O      1 
ATOM   3463 N N      . ALA B 1 107 ? 42.130 -2.876  45.690  1.00 25.98 ? 101 ALA B N      1 
ATOM   3464 C CA     . ALA B 1 107 ? 40.800 -2.860  46.282  1.00 24.93 ? 101 ALA B CA     1 
ATOM   3465 C C      . ALA B 1 107 ? 40.310 -4.271  46.591  1.00 23.73 ? 101 ALA B C      1 
ATOM   3466 O O      . ALA B 1 107 ? 40.803 -5.265  46.063  1.00 26.63 ? 101 ALA B O      1 
ATOM   3467 C CB     . ALA B 1 107 ? 39.806 -2.156  45.360  1.00 27.19 ? 101 ALA B CB     1 
ATOM   3468 N N      . VAL B 1 108 ? 39.333 -4.344  47.494  1.00 24.46 ? 102 VAL B N      1 
ATOM   3469 C CA     . VAL B 1 108 ? 38.577 -5.558  47.772  1.00 21.45 ? 102 VAL B CA     1 
ATOM   3470 C C      . VAL B 1 108 ? 37.239 -5.401  47.063  1.00 22.75 ? 102 VAL B C      1 
ATOM   3471 O O      . VAL B 1 108 ? 36.652 -4.312  47.087  1.00 22.47 ? 102 VAL B O      1 
ATOM   3472 C CB     . VAL B 1 108 ? 38.371 -5.702  49.298  1.00 21.53 ? 102 VAL B CB     1 
ATOM   3473 C CG1    . VAL B 1 108 ? 37.520 -6.915  49.630  1.00 26.01 ? 102 VAL B CG1    1 
ATOM   3474 C CG2    . VAL B 1 108 ? 39.729 -5.752  50.039  1.00 25.45 ? 102 VAL B CG2    1 
ATOM   3475 N N      . ILE B 1 109 ? 36.758 -6.466  46.424  1.00 22.49 ? 103 ILE B N      1 
ATOM   3476 C CA     . ILE B 1 109 ? 35.519 -6.392  45.642  1.00 20.46 ? 103 ILE B CA     1 
ATOM   3477 C C      . ILE B 1 109 ? 34.645 -7.613  45.912  1.00 22.67 ? 103 ILE B C      1 
ATOM   3478 O O      . ILE B 1 109 ? 35.113 -8.753  45.834  1.00 21.68 ? 103 ILE B O      1 
ATOM   3479 C CB     . ILE B 1 109 ? 35.778 -6.190  44.128  1.00 22.45 ? 103 ILE B CB     1 
ATOM   3480 C CG1    . ILE B 1 109 ? 34.460 -6.009  43.362  1.00 22.53 ? 103 ILE B CG1    1 
ATOM   3481 C CG2    . ILE B 1 109 ? 36.613 -7.329  43.533  1.00 23.56 ? 103 ILE B CG2    1 
ATOM   3482 C CD1    . ILE B 1 109 ? 34.657 -5.391  41.973  1.00 26.16 ? 103 ILE B CD1    1 
ATOM   3483 N N      . PHE B 1 110 ? 33.364 -7.372  46.220  1.00 21.33 ? 104 PHE B N      1 
ATOM   3484 C CA     . PHE B 1 110 ? 32.363 -8.418  46.371  1.00 20.50 ? 104 PHE B CA     1 
ATOM   3485 C C      . PHE B 1 110 ? 31.343 -8.297  45.242  1.00 21.98 ? 104 PHE B C      1 
ATOM   3486 O O      . PHE B 1 110 ? 31.020 -7.195  44.797  1.00 20.55 ? 104 PHE B O      1 
ATOM   3487 C CB     . PHE B 1 110 ? 31.577 -8.239  47.677  1.00 19.18 ? 104 PHE B CB     1 
ATOM   3488 C CG     . PHE B 1 110 ? 32.219 -8.858  48.901  1.00 22.54 ? 104 PHE B CG     1 
ATOM   3489 C CD1    . PHE B 1 110 ? 33.594 -9.042  48.986  1.00 24.11 ? 104 PHE B CD1    1 
ATOM   3490 C CD2    . PHE B 1 110 ? 31.424 -9.238  49.978  1.00 20.32 ? 104 PHE B CD2    1 
ATOM   3491 C CE1    . PHE B 1 110 ? 34.164 -9.606  50.123  1.00 21.46 ? 104 PHE B CE1    1 
ATOM   3492 C CE2    . PHE B 1 110 ? 31.988 -9.795  51.125  1.00 20.65 ? 104 PHE B CE2    1 
ATOM   3493 C CZ     . PHE B 1 110 ? 33.361 -9.980  51.197  1.00 21.26 ? 104 PHE B CZ     1 
ATOM   3494 N N      . CYS B 1 111 ? 30.807 -9.433  44.808  1.00 20.66 ? 105 CYS B N      1 
ATOM   3495 C CA     . CYS B 1 111 ? 29.792 -9.481  43.757  1.00 20.84 ? 105 CYS B CA     1 
ATOM   3496 C C      . CYS B 1 111 ? 28.419 -9.630  44.416  1.00 20.89 ? 105 CYS B C      1 
ATOM   3497 O O      . CYS B 1 111 ? 28.189 -10.589 45.156  1.00 20.00 ? 105 CYS B O      1 
ATOM   3498 C CB     . CYS B 1 111 ? 30.057 -10.675 42.839  1.00 20.51 ? 105 CYS B CB     1 
ATOM   3499 S SG     . CYS B 1 111 ? 28.782 -10.936 41.541  1.00 22.24 ? 105 CYS B SG     1 
ATOM   3500 N N      . GLN B 1 112 ? 27.497 -8.717  44.108  1.00 18.86 ? 106 GLN B N      1 
ATOM   3501 C CA     . GLN B 1 112 ? 26.140 -8.807  44.644  1.00 20.87 ? 106 GLN B CA     1 
ATOM   3502 C C      . GLN B 1 112 ? 25.312 -9.784  43.817  1.00 21.39 ? 106 GLN B C      1 
ATOM   3503 O O      . GLN B 1 112 ? 25.173 -9.615  42.600  1.00 20.10 ? 106 GLN B O      1 
ATOM   3504 C CB     . GLN B 1 112 ? 25.458 -7.442  44.664  1.00 22.39 ? 106 GLN B CB     1 
ATOM   3505 C CG     . GLN B 1 112 ? 24.217 -7.475  45.520  1.00 20.06 ? 106 GLN B CG     1 
ATOM   3506 C CD     . GLN B 1 112 ? 23.283 -6.285  45.377  1.00 22.27 ? 106 GLN B CD     1 
ATOM   3507 O OE1    . GLN B 1 112 ? 22.879 -5.903  44.276  1.00 20.61 ? 106 GLN B OE1    1 
ATOM   3508 N NE2    . GLN B 1 112 ? 22.955 -5.670  46.516  1.00 19.58 ? 106 GLN B NE2    1 
ATOM   3509 N N      . LEU B 1 113 ? 24.757 -10.798 44.470  1.00 19.91 ? 107 LEU B N      1 
ATOM   3510 C CA     . LEU B 1 113 ? 23.942 -11.800 43.795  1.00 20.68 ? 107 LEU B CA     1 
ATOM   3511 C C      . LEU B 1 113 ? 22.475 -11.408 43.914  1.00 19.18 ? 107 LEU B C      1 
ATOM   3512 O O      . LEU B 1 113 ? 21.977 -11.207 45.029  1.00 20.42 ? 107 LEU B O      1 
ATOM   3513 C CB     . LEU B 1 113 ? 24.170 -13.167 44.441  1.00 21.80 ? 107 LEU B CB     1 
ATOM   3514 C CG     . LEU B 1 113 ? 25.626 -13.649 44.470  1.00 20.44 ? 107 LEU B CG     1 
ATOM   3515 C CD1    . LEU B 1 113 ? 25.686 -15.035 45.091  1.00 22.60 ? 107 LEU B CD1    1 
ATOM   3516 C CD2    . LEU B 1 113 ? 26.238 -13.649 43.067  1.00 22.02 ? 107 LEU B CD2    1 
ATOM   3517 N N      . TRP B 1 114 ? 21.785 -11.319 42.771  1.00 21.15 ? 108 TRP B N      1 
ATOM   3518 C CA     . TRP B 1 114 ? 20.509 -10.607 42.697  1.00 22.12 ? 108 TRP B CA     1 
ATOM   3519 C C      . TRP B 1 114 ? 19.482 -11.410 41.906  1.00 20.87 ? 108 TRP B C      1 
ATOM   3520 O O      . TRP B 1 114 ? 19.694 -11.711 40.725  1.00 19.70 ? 108 TRP B O      1 
ATOM   3521 C CB     . TRP B 1 114 ? 20.748 -9.249  42.026  1.00 19.12 ? 108 TRP B CB     1 
ATOM   3522 C CG     . TRP B 1 114 ? 19.555 -8.343  41.843  1.00 19.81 ? 108 TRP B CG     1 
ATOM   3523 C CD1    . TRP B 1 114 ? 18.449 -8.240  42.654  1.00 24.50 ? 108 TRP B CD1    1 
ATOM   3524 C CD2    . TRP B 1 114 ? 19.406 -7.344  40.835  1.00 20.58 ? 108 TRP B CD2    1 
ATOM   3525 N NE1    . TRP B 1 114 ? 17.603 -7.265  42.178  1.00 21.21 ? 108 TRP B NE1    1 
ATOM   3526 C CE2    . TRP B 1 114 ? 18.168 -6.698  41.061  1.00 20.42 ? 108 TRP B CE2    1 
ATOM   3527 C CE3    . TRP B 1 114 ? 20.185 -6.952  39.736  1.00 17.98 ? 108 TRP B CE3    1 
ATOM   3528 C CZ2    . TRP B 1 114 ? 17.709 -5.666  40.251  1.00 19.28 ? 108 TRP B CZ2    1 
ATOM   3529 C CZ3    . TRP B 1 114 ? 19.728 -5.934  38.927  1.00 22.79 ? 108 TRP B CZ3    1 
ATOM   3530 C CH2    . TRP B 1 114 ? 18.497 -5.307  39.174  1.00 19.04 ? 108 TRP B CH2    1 
ATOM   3531 N N      . HIS B 1 115 ? 18.356 -11.727 42.544  1.00 20.95 ? 109 HIS B N      1 
ATOM   3532 C CA     . HIS B 1 115 ? 17.188 -12.278 41.859  1.00 18.53 ? 109 HIS B CA     1 
ATOM   3533 C C      . HIS B 1 115 ? 16.028 -11.321 42.085  1.00 20.24 ? 109 HIS B C      1 
ATOM   3534 O O      . HIS B 1 115 ? 15.704 -10.994 43.234  1.00 19.55 ? 109 HIS B O      1 
ATOM   3535 C CB     . HIS B 1 115 ? 16.859 -13.672 42.396  1.00 21.47 ? 109 HIS B CB     1 
ATOM   3536 C CG     . HIS B 1 115 ? 15.919 -14.459 41.531  1.00 20.13 ? 109 HIS B CG     1 
ATOM   3537 N ND1    . HIS B 1 115 ? 14.687 -13.980 41.136  1.00 22.03 ? 109 HIS B ND1    1 
ATOM   3538 C CD2    . HIS B 1 115 ? 16.025 -15.702 41.003  1.00 26.28 ? 109 HIS B CD2    1 
ATOM   3539 C CE1    . HIS B 1 115 ? 14.079 -14.890 40.397  1.00 23.25 ? 109 HIS B CE1    1 
ATOM   3540 N NE2    . HIS B 1 115 ? 14.871 -15.943 40.296  1.00 25.28 ? 109 HIS B NE2    1 
ATOM   3541 N N      . VAL B 1 116 ? 15.404 -10.864 40.993  1.00 20.25 ? 110 VAL B N      1 
ATOM   3542 C CA     . VAL B 1 116 ? 14.347 -9.858  41.106  1.00 19.87 ? 110 VAL B CA     1 
ATOM   3543 C C      . VAL B 1 116 ? 12.991 -10.427 41.467  1.00 20.41 ? 110 VAL B C      1 
ATOM   3544 O O      . VAL B 1 116 ? 12.085 -9.655  41.812  1.00 20.38 ? 110 VAL B O      1 
ATOM   3545 C CB     . VAL B 1 116 ? 14.189 -9.089  39.782  1.00 18.63 ? 110 VAL B CB     1 
ATOM   3546 C CG1    . VAL B 1 116 ? 15.488 -8.409  39.425  1.00 20.17 ? 110 VAL B CG1    1 
ATOM   3547 C CG2    . VAL B 1 116 ? 13.726 -10.037 38.660  1.00 20.30 ? 110 VAL B CG2    1 
ATOM   3548 N N      . GLY B 1 117 ? 12.816 -11.739 41.395  1.00 18.23 ? 111 GLY B N      1 
ATOM   3549 C CA     . GLY B 1 117 ? 11.504 -12.305 41.671  1.00 22.01 ? 111 GLY B CA     1 
ATOM   3550 C C      . GLY B 1 117 ? 10.434 -11.752 40.742  1.00 20.02 ? 111 GLY B C      1 
ATOM   3551 O O      . GLY B 1 117 ? 10.570 -11.766 39.509  1.00 21.18 ? 111 GLY B O      1 
ATOM   3552 N N      . ARG B 1 118 ? 9.346  -11.255 41.343  1.00 20.36 ? 112 ARG B N      1 
ATOM   3553 C CA     . ARG B 1 118 ? 8.208  -10.795 40.556  1.00 23.81 ? 112 ARG B CA     1 
ATOM   3554 C C      . ARG B 1 118 ? 8.454  -9.457  39.876  1.00 20.95 ? 112 ARG B C      1 
ATOM   3555 O O      . ARG B 1 118 ? 7.622  -9.033  39.065  1.00 22.27 ? 112 ARG B O      1 
ATOM   3556 C CB     . ARG B 1 118 ? 6.967  -10.702 41.438  1.00 22.99 ? 112 ARG B CB     1 
ATOM   3557 C CG     . ARG B 1 118 ? 6.958  -9.495  42.337  1.00 20.70 ? 112 ARG B CG     1 
ATOM   3558 C CD     . ARG B 1 118 ? 5.746  -9.530  43.281  1.00 20.30 ? 112 ARG B CD     1 
ATOM   3559 N NE     . ARG B 1 118 ? 5.753  -8.393  44.190  1.00 22.60 ? 112 ARG B NE     1 
ATOM   3560 C CZ     . ARG B 1 118 ? 4.682  -7.952  44.835  1.00 21.59 ? 112 ARG B CZ     1 
ATOM   3561 N NH1    . ARG B 1 118 ? 3.506  -8.549  44.706  1.00 24.62 ? 112 ARG B NH1    1 
ATOM   3562 N NH2    . ARG B 1 118 ? 4.790  -6.876  45.608  1.00 25.93 ? 112 ARG B NH2    1 
ATOM   3563 N N      . ALA B 1 119 ? 9.576  -8.796  40.169  1.00 19.52 ? 113 ALA B N      1 
ATOM   3564 C CA     . ALA B 1 119 ? 9.926  -7.513  39.564  1.00 19.96 ? 113 ALA B CA     1 
ATOM   3565 C C      . ALA B 1 119 ? 10.624 -7.735  38.217  1.00 21.79 ? 113 ALA B C      1 
ATOM   3566 O O      . ALA B 1 119 ? 11.796 -7.410  38.010  1.00 22.41 ? 113 ALA B O      1 
ATOM   3567 C CB     . ALA B 1 119 ? 10.779 -6.687  40.522  1.00 20.13 ? 113 ALA B CB     1 
ATOM   3568 N N      . SER B 1 120 ? 9.869  -8.311  37.286  1.00 20.65 ? 114 SER B N      1 
ATOM   3569 C CA     . SER B 1 120 ? 10.392 -8.653  35.972  1.00 18.74 ? 114 SER B CA     1 
ATOM   3570 C C      . SER B 1 120 ? 9.260  -8.479  34.967  1.00 20.12 ? 114 SER B C      1 
ATOM   3571 O O      . SER B 1 120 ? 8.218  -7.896  35.281  1.00 22.78 ? 114 SER B O      1 
ATOM   3572 C CB     . SER B 1 120 ? 10.988 -10.066 35.997  1.00 22.82 ? 114 SER B CB     1 
ATOM   3573 O OG     . SER B 1 120 ? 11.683 -10.375 34.800  1.00 21.50 ? 114 SER B OG     1 
ATOM   3574 N N      . HIS B 1 121 ? 9.477  -8.987  33.756  1.00 21.64 ? 115 HIS B N      1 
ATOM   3575 C CA     . HIS B 1 121 ? 8.547  -8.832  32.642  1.00 19.74 ? 115 HIS B CA     1 
ATOM   3576 C C      . HIS B 1 121 ? 8.862  -9.945  31.655  1.00 22.76 ? 115 HIS B C      1 
ATOM   3577 O O      . HIS B 1 121 ? 9.981  -10.471 31.627  1.00 23.95 ? 115 HIS B O      1 
ATOM   3578 C CB     . HIS B 1 121 ? 8.724  -7.451  31.997  1.00 21.25 ? 115 HIS B CB     1 
ATOM   3579 C CG     . HIS B 1 121 ? 7.734  -7.133  30.912  1.00 25.16 ? 115 HIS B CG     1 
ATOM   3580 N ND1    . HIS B 1 121 ? 7.839  -7.639  29.636  1.00 26.80 ? 115 HIS B ND1    1 
ATOM   3581 C CD2    . HIS B 1 121 ? 6.648  -6.322  30.906  1.00 24.69 ? 115 HIS B CD2    1 
ATOM   3582 C CE1    . HIS B 1 121 ? 6.840  -7.185  28.897  1.00 28.70 ? 115 HIS B CE1    1 
ATOM   3583 N NE2    . HIS B 1 121 ? 6.105  -6.378  29.641  1.00 23.31 ? 115 HIS B NE2    1 
ATOM   3584 N N      . GLU B 1 122 ? 7.862  -10.290 30.837  1.00 23.21 ? 116 GLU B N      1 
ATOM   3585 C CA     . GLU B 1 122 ? 8.045  -11.332 29.831  1.00 27.67 ? 116 GLU B CA     1 
ATOM   3586 C C      . GLU B 1 122 ? 9.289  -11.102 28.970  1.00 22.52 ? 116 GLU B C      1 
ATOM   3587 O O      . GLU B 1 122 ? 9.986  -12.057 28.604  1.00 25.72 ? 116 GLU B O      1 
ATOM   3588 C CB     . GLU B 1 122 ? 6.775  -11.441 28.977  1.00 27.94 ? 116 GLU B CB     1 
ATOM   3589 C CG     . GLU B 1 122 ? 5.530  -11.875 29.782  1.00 36.21 ? 116 GLU B CG     1 
ATOM   3590 C CD     . GLU B 1 122 ? 4.743  -10.750 30.488  1.00 47.23 ? 116 GLU B CD     1 
ATOM   3591 O OE1    . GLU B 1 122 ? 5.303  -9.677  30.815  1.00 34.15 ? 116 GLU B OE1    1 
ATOM   3592 O OE2    . GLU B 1 122 ? 3.531  -10.969 30.741  1.00 46.26 ? 116 GLU B OE2    1 
ATOM   3593 N N      . VAL B 1 123 ? 9.602  -9.841  28.666  1.00 22.18 ? 117 VAL B N      1 
ATOM   3594 C CA     . VAL B 1 123 ? 10.746 -9.527  27.814  1.00 24.18 ? 117 VAL B CA     1 
ATOM   3595 C C      . VAL B 1 123 ? 12.071 -9.967  28.432  1.00 23.45 ? 117 VAL B C      1 
ATOM   3596 O O      . VAL B 1 123 ? 13.044 -10.192 27.703  1.00 24.86 ? 117 VAL B O      1 
ATOM   3597 C CB     . VAL B 1 123 ? 10.758 -8.020  27.479  1.00 22.70 ? 117 VAL B CB     1 
ATOM   3598 C CG1    . VAL B 1 123 ? 11.224 -7.205  28.694  1.00 23.81 ? 117 VAL B CG1    1 
ATOM   3599 C CG2    . VAL B 1 123 ? 11.642 -7.742  26.275  1.00 26.25 ? 117 VAL B CG2    1 
ATOM   3600 N N      . TYR B 1 124 ? 12.131 -10.092 29.760  1.00 23.13 ? 118 TYR B N      1 
ATOM   3601 C CA     . TYR B 1 124 ? 13.353 -10.431 30.484  1.00 23.79 ? 118 TYR B CA     1 
ATOM   3602 C C      . TYR B 1 124 ? 13.427 -11.903 30.859  1.00 24.76 ? 118 TYR B C      1 
ATOM   3603 O O      . TYR B 1 124 ? 14.422 -12.330 31.458  1.00 24.53 ? 118 TYR B O      1 
ATOM   3604 C CB     . TYR B 1 124 ? 13.463 -9.587  31.765  1.00 22.77 ? 118 TYR B CB     1 
ATOM   3605 C CG     . TYR B 1 124 ? 13.639 -8.116  31.492  1.00 20.43 ? 118 TYR B CG     1 
ATOM   3606 C CD1    . TYR B 1 124 ? 14.696 -7.665  30.701  1.00 20.71 ? 118 TYR B CD1    1 
ATOM   3607 C CD2    . TYR B 1 124 ? 12.745 -7.174  32.020  1.00 18.28 ? 118 TYR B CD2    1 
ATOM   3608 C CE1    . TYR B 1 124 ? 14.864 -6.329  30.440  1.00 23.69 ? 118 TYR B CE1    1 
ATOM   3609 C CE2    . TYR B 1 124 ? 12.905 -5.828  31.757  1.00 22.16 ? 118 TYR B CE2    1 
ATOM   3610 C CZ     . TYR B 1 124 ? 13.970 -5.414  30.961  1.00 22.93 ? 118 TYR B CZ     1 
ATOM   3611 O OH     . TYR B 1 124 ? 14.153 -4.078  30.676  1.00 21.33 ? 118 TYR B OH     1 
ATOM   3612 N N      . GLN B 1 125 ? 12.397 -12.677 30.546  1.00 25.21 ? 119 GLN B N      1 
ATOM   3613 C CA     . GLN B 1 125 ? 12.284 -14.062 30.954  1.00 27.25 ? 119 GLN B CA     1 
ATOM   3614 C C      . GLN B 1 125 ? 12.451 -14.991 29.759  1.00 30.16 ? 119 GLN B C      1 
ATOM   3615 O O      . GLN B 1 125 ? 11.954 -14.692 28.662  1.00 28.77 ? 119 GLN B O      1 
ATOM   3616 C CB     . GLN B 1 125 ? 10.907 -14.310 31.574  1.00 26.71 ? 119 GLN B CB     1 
ATOM   3617 C CG     . GLN B 1 125 ? 10.695 -13.670 32.942  1.00 25.16 ? 119 GLN B CG     1 
ATOM   3618 C CD     . GLN B 1 125 ? 11.699 -14.156 33.977  1.00 28.82 ? 119 GLN B CD     1 
ATOM   3619 O OE1    . GLN B 1 125 ? 11.969 -15.349 34.073  1.00 29.28 ? 119 GLN B OE1    1 
ATOM   3620 N NE2    . GLN B 1 125 ? 12.235 -13.231 34.771  1.00 23.67 ? 119 GLN B NE2    1 
ATOM   3621 N N      . PRO B 1 126 ? 13.129 -16.122 29.944  1.00 30.21 ? 120 PRO B N      1 
ATOM   3622 C CA     . PRO B 1 126 ? 13.254 -17.096 28.852  1.00 36.86 ? 120 PRO B CA     1 
ATOM   3623 C C      . PRO B 1 126 ? 11.880 -17.583 28.415  1.00 35.34 ? 120 PRO B C      1 
ATOM   3624 O O      . PRO B 1 126 ? 11.032 -17.924 29.242  1.00 36.61 ? 120 PRO B O      1 
ATOM   3625 C CB     . PRO B 1 126 ? 14.082 -18.229 29.474  1.00 38.31 ? 120 PRO B CB     1 
ATOM   3626 C CG     . PRO B 1 126 ? 14.589 -17.695 30.795  1.00 35.21 ? 120 PRO B CG     1 
ATOM   3627 C CD     . PRO B 1 126 ? 13.628 -16.649 31.224  1.00 31.27 ? 120 PRO B CD     1 
ATOM   3628 N N      . ALA B 1 127 ? 11.662 -17.591 27.099  1.00 33.69 ? 121 ALA B N      1 
ATOM   3629 C CA     . ALA B 1 127 ? 10.394 -17.998 26.493  1.00 39.41 ? 121 ALA B CA     1 
ATOM   3630 C C      . ALA B 1 127 ? 9.232  -17.073 26.854  1.00 36.47 ? 121 ALA B C      1 
ATOM   3631 O O      . ALA B 1 127 ? 8.069  -17.431 26.650  1.00 42.36 ? 121 ALA B O      1 
ATOM   3632 C CB     . ALA B 1 127 ? 10.049 -19.463 26.793  1.00 43.12 ? 121 ALA B CB     1 
ATOM   3633 N N      . GLY B 1 128 ? 9.518  -15.881 27.375  1.00 29.75 ? 122 GLY B N      1 
ATOM   3634 C CA     . GLY B 1 128 ? 8.453  -14.995 27.815  1.00 34.20 ? 122 GLY B CA     1 
ATOM   3635 C C      . GLY B 1 128 ? 7.630  -15.556 28.953  1.00 35.08 ? 122 GLY B C      1 
ATOM   3636 O O      . GLY B 1 128 ? 6.452  -15.203 29.095  1.00 38.82 ? 122 GLY B O      1 
ATOM   3637 N N      . ALA B 1 129 ? 8.221  -16.428 29.768  1.00 33.25 ? 123 ALA B N      1 
ATOM   3638 C CA     . ALA B 1 129 ? 7.525  -17.081 30.866  1.00 38.70 ? 123 ALA B CA     1 
ATOM   3639 C C      . ALA B 1 129 ? 7.262  -16.094 32.005  1.00 34.15 ? 123 ALA B C      1 
ATOM   3640 O O      . ALA B 1 129 ? 7.858  -15.019 32.088  1.00 33.94 ? 123 ALA B O      1 
ATOM   3641 C CB     . ALA B 1 129 ? 8.352  -18.255 31.388  1.00 35.35 ? 123 ALA B CB     1 
ATOM   3642 N N      . ALA B 1 130 ? 6.350  -16.475 32.890  1.00 31.50 ? 124 ALA B N      1 
ATOM   3643 C CA     . ALA B 1 130 ? 6.017  -15.622 34.023  1.00 30.80 ? 124 ALA B CA     1 
ATOM   3644 C C      . ALA B 1 130 ? 7.179  -15.572 35.015  1.00 29.18 ? 124 ALA B C      1 
ATOM   3645 O O      . ALA B 1 130 ? 7.850  -16.584 35.248  1.00 29.87 ? 124 ALA B O      1 
ATOM   3646 C CB     . ALA B 1 130 ? 4.764  -16.141 34.729  1.00 31.02 ? 124 ALA B CB     1 
ATOM   3647 N N      . PRO B 1 131 ? 7.443  -14.413 35.612  1.00 24.08 ? 125 PRO B N      1 
ATOM   3648 C CA     . PRO B 1 131 ? 8.437  -14.347 36.696  1.00 25.58 ? 125 PRO B CA     1 
ATOM   3649 C C      . PRO B 1 131 ? 7.982  -15.167 37.894  1.00 26.45 ? 125 PRO B C      1 
ATOM   3650 O O      . PRO B 1 131 ? 6.801  -15.493 38.044  1.00 29.03 ? 125 PRO B O      1 
ATOM   3651 C CB     . PRO B 1 131 ? 8.478  -12.854 37.046  1.00 23.58 ? 125 PRO B CB     1 
ATOM   3652 C CG     . PRO B 1 131 ? 7.795  -12.151 35.902  1.00 33.30 ? 125 PRO B CG     1 
ATOM   3653 C CD     . PRO B 1 131 ? 6.786  -13.119 35.383  1.00 25.76 ? 125 PRO B CD     1 
ATOM   3654 N N      . ILE B 1 132 ? 8.932  -15.482 38.780  1.00 25.47 ? 126 ILE B N      1 
ATOM   3655 C CA     . ILE B 1 132 ? 8.645  -16.288 39.967  1.00 24.06 ? 126 ILE B CA     1 
ATOM   3656 C C      . ILE B 1 132 ? 8.623  -15.410 41.209  1.00 26.30 ? 126 ILE B C      1 
ATOM   3657 O O      . ILE B 1 132 ? 9.255  -14.355 41.277  1.00 23.69 ? 126 ILE B O      1 
ATOM   3658 C CB     . ILE B 1 132 ? 9.620  -17.465 40.166  1.00 25.08 ? 126 ILE B CB     1 
ATOM   3659 C CG1    . ILE B 1 132 ? 11.042 -16.950 40.406  1.00 26.00 ? 126 ILE B CG1    1 
ATOM   3660 C CG2    . ILE B 1 132 ? 9.577  -18.399 38.972  1.00 28.46 ? 126 ILE B CG2    1 
ATOM   3661 C CD1    . ILE B 1 132 ? 11.838 -17.807 41.340  1.00 30.84 ? 126 ILE B CD1    1 
ATOM   3662 N N      . SER B 1 133 ? 7.920  -15.888 42.228  1.00 24.20 ? 127 SER B N      1 
ATOM   3663 C CA     . SER B 1 133 ? 7.829  -15.144 43.475  1.00 21.98 ? 127 SER B CA     1 
ATOM   3664 C C      . SER B 1 133 ? 7.331  -16.081 44.566  1.00 21.69 ? 127 SER B C      1 
ATOM   3665 O O      . SER B 1 133 ? 7.066  -17.263 44.332  1.00 25.39 ? 127 SER B O      1 
ATOM   3666 C CB     . SER B 1 133 ? 6.897  -13.941 43.316  1.00 23.46 ? 127 SER B CB     1 
ATOM   3667 O OG     . SER B 1 133 ? 6.950  -13.083 44.443  1.00 22.90 ? 127 SER B OG     1 
ATOM   3668 N N      . SER B 1 134 ? 7.222  -15.530 45.777  1.00 22.52 ? 128 SER B N      1 
ATOM   3669 C CA     . SER B 1 134 ? 6.550  -16.211 46.871  1.00 23.03 ? 128 SER B CA     1 
ATOM   3670 C C      . SER B 1 134 ? 5.043  -16.237 46.668  1.00 24.91 ? 128 SER B C      1 
ATOM   3671 O O      . SER B 1 134 ? 4.349  -17.063 47.281  1.00 23.81 ? 128 SER B O      1 
ATOM   3672 C CB     . SER B 1 134 ? 6.835  -15.418 48.138  1.00 23.66 ? 128 SER B CB     1 
ATOM   3673 O OG     . SER B 1 134 ? 6.371  -14.082 47.967  1.00 26.50 ? 128 SER B OG     1 
ATOM   3674 N N      . THR B 1 135 ? 4.531  -15.347 45.826  1.00 24.65 ? 129 THR B N      1 
ATOM   3675 C CA     . THR B 1 135 ? 3.117  -15.039 45.717  1.00 25.35 ? 129 THR B CA     1 
ATOM   3676 C C      . THR B 1 135 ? 2.730  -15.001 44.247  1.00 25.84 ? 129 THR B C      1 
ATOM   3677 O O      . THR B 1 135 ? 3.585  -14.979 43.355  1.00 25.59 ? 129 THR B O      1 
ATOM   3678 C CB     . THR B 1 135 ? 2.820  -13.667 46.344  1.00 29.40 ? 129 THR B CB     1 
ATOM   3679 O OG1    . THR B 1 135 ? 1.414  -13.404 46.288  1.00 29.21 ? 129 THR B OG1    1 
ATOM   3680 C CG2    . THR B 1 135 ? 3.560  -12.557 45.595  1.00 27.51 ? 129 THR B CG2    1 
ATOM   3681 N N      . GLU B 1 136 ? 1.420  -14.991 44.003  1.00 28.50 ? 130 GLU B N      1 
ATOM   3682 C CA     . GLU B 1 136 ? 0.856  -14.770 42.676  1.00 30.46 ? 130 GLU B CA     1 
ATOM   3683 C C      . GLU B 1 136 ? 0.430  -13.325 42.459  1.00 27.76 ? 130 GLU B C      1 
ATOM   3684 O O      . GLU B 1 136 ? -0.014 -12.977 41.358  1.00 29.05 ? 130 GLU B O      1 
ATOM   3685 C CB     . GLU B 1 136 ? -0.361 -15.672 42.480  1.00 35.83 ? 130 GLU B CB     1 
ATOM   3686 C CG     . GLU B 1 136 ? -0.033 -17.053 41.994  1.00 45.28 ? 130 GLU B CG     1 
ATOM   3687 C CD     . GLU B 1 136 ? -1.273 -17.815 41.577  1.00 54.29 ? 130 GLU B CD     1 
ATOM   3688 O OE1    . GLU B 1 136 ? -2.275 -17.164 41.207  1.00 61.00 ? 130 GLU B OE1    1 
ATOM   3689 O OE2    . GLU B 1 136 ? -1.244 -19.064 41.618  1.00 48.64 ? 130 GLU B OE2    1 
ATOM   3690 N N      . LYS B 1 137 ? 0.541  -12.485 43.476  1.00 26.49 ? 131 LYS B N      1 
ATOM   3691 C CA     . LYS B 1 137 ? 0.108  -11.100 43.377  1.00 26.71 ? 131 LYS B CA     1 
ATOM   3692 C C      . LYS B 1 137 ? 1.140  -10.295 42.596  1.00 31.19 ? 131 LYS B C      1 
ATOM   3693 O O      . LYS B 1 137 ? 2.337  -10.360 42.910  1.00 27.05 ? 131 LYS B O      1 
ATOM   3694 C CB     . LYS B 1 137 ? -0.023 -10.504 44.776  1.00 31.57 ? 131 LYS B CB     1 
ATOM   3695 C CG     . LYS B 1 137 ? -1.294 -10.899 45.515  1.00 36.83 ? 131 LYS B CG     1 
ATOM   3696 C CD     . LYS B 1 137 ? -1.319 -10.388 46.967  1.00 40.14 ? 131 LYS B CD     1 
ATOM   3697 C CE     . LYS B 1 137 ? 0.022  -10.587 47.708  1.00 36.94 ? 131 LYS B CE     1 
ATOM   3698 N NZ     . LYS B 1 137 ? -0.053 -10.144 49.145  1.00 42.22 ? 131 LYS B NZ     1 
ATOM   3699 N N      . PRO B 1 138 ? 0.729  -9.529  41.591  1.00 27.93 ? 132 PRO B N      1 
ATOM   3700 C CA     . PRO B 1 138 ? 1.684  -8.685  40.875  1.00 27.48 ? 132 PRO B CA     1 
ATOM   3701 C C      . PRO B 1 138 ? 1.954  -7.399  41.636  1.00 25.04 ? 132 PRO B C      1 
ATOM   3702 O O      . PRO B 1 138 ? 1.177  -6.962  42.488  1.00 26.62 ? 132 PRO B O      1 
ATOM   3703 C CB     . PRO B 1 138 ? 0.961  -8.388  39.557  1.00 27.66 ? 132 PRO B CB     1 
ATOM   3704 C CG     . PRO B 1 138 ? -0.473 -8.334  39.968  1.00 29.98 ? 132 PRO B CG     1 
ATOM   3705 C CD     . PRO B 1 138 ? -0.632 -9.410  41.031  1.00 27.13 ? 132 PRO B CD     1 
ATOM   3706 N N      . ILE B 1 139 ? 3.113  -6.808  41.335  1.00 22.72 ? 133 ILE B N      1 
ATOM   3707 C CA     . ILE B 1 139 ? 3.371  -5.446  41.780  1.00 22.58 ? 133 ILE B CA     1 
ATOM   3708 C C      . ILE B 1 139 ? 2.251  -4.556  41.250  1.00 24.85 ? 133 ILE B C      1 
ATOM   3709 O O      . ILE B 1 139 ? 1.824  -4.686  40.094  1.00 27.24 ? 133 ILE B O      1 
ATOM   3710 C CB     . ILE B 1 139 ? 4.749  -4.989  41.272  1.00 21.79 ? 133 ILE B CB     1 
ATOM   3711 C CG1    . ILE B 1 139 ? 5.860  -5.738  42.009  1.00 20.64 ? 133 ILE B CG1    1 
ATOM   3712 C CG2    . ILE B 1 139 ? 4.936  -3.500  41.491  1.00 22.62 ? 133 ILE B CG2    1 
ATOM   3713 C CD1    . ILE B 1 139 ? 7.176  -5.726  41.213  1.00 20.57 ? 133 ILE B CD1    1 
ATOM   3714 N N      . SER B 1 140 ? 1.801  -3.617  42.075  1.00 26.74 ? 134 SER B N      1 
ATOM   3715 C CA     . SER B 1 140 ? 0.676  -2.733  41.689  1.00 29.69 ? 134 SER B CA     1 
ATOM   3716 C C      . SER B 1 140 ? 1.010  -1.812  40.517  1.00 31.80 ? 134 SER B C      1 
ATOM   3717 O O      . SER B 1 140 ? 2.185  -1.622  40.225  1.00 29.96 ? 134 SER B O      1 
ATOM   3718 C CB     . SER B 1 140 ? 0.223  -1.906  42.846  1.00 34.52 ? 134 SER B CB     1 
ATOM   3719 O OG     . SER B 1 140 ? 1.149  -0.873  43.117  1.00 34.69 ? 134 SER B OG     1 
ATOM   3720 N N      . ASN B 1 141 ? -0.022 -1.202  39.932  1.00 32.89 ? 135 ASN B N      1 
ATOM   3721 C CA     . ASN B 1 141 ? 0.153  -0.323  38.744  1.00 31.90 ? 135 ASN B CA     1 
ATOM   3722 C C      . ASN B 1 141 ? 0.815  1.003   39.128  1.00 31.35 ? 135 ASN B C      1 
ATOM   3723 O O      . ASN B 1 141 ? 1.100  1.779   38.231  1.00 39.08 ? 135 ASN B O      1 
ATOM   3724 C CB     . ASN B 1 141 ? -1.178 -0.097  38.020  1.00 46.67 ? 135 ASN B CB     1 
ATOM   3725 N N      . ARG B 1 142 ? 1.061  1.222   40.413  1.00 36.41 ? 136 ARG B N      1 
ATOM   3726 C CA     . ARG B 1 142 ? 1.785  2.434   40.866  1.00 34.36 ? 136 ARG B CA     1 
ATOM   3727 C C      . ARG B 1 142 ? 3.242  2.353   40.397  1.00 38.66 ? 136 ARG B C      1 
ATOM   3728 O O      . ARG B 1 142 ? 3.900  3.389   40.349  1.00 36.37 ? 136 ARG B O      1 
ATOM   3729 C CB     . ARG B 1 142 ? 1.723  2.529   42.391  1.00 35.96 ? 136 ARG B CB     1 
ATOM   3730 N N      . TRP B 1 143 ? 3.716  1.146   40.097  1.00 29.36 ? 137 TRP B N      1 
ATOM   3731 C CA     . TRP B 1 143 ? 5.099  0.977   39.671  1.00 28.06 ? 137 TRP B CA     1 
ATOM   3732 C C      . TRP B 1 143 ? 5.131  0.450   38.246  1.00 24.59 ? 137 TRP B C      1 
ATOM   3733 O O      . TRP B 1 143 ? 4.269  -0.342  37.849  1.00 27.34 ? 137 TRP B O      1 
ATOM   3734 C CB     . TRP B 1 143 ? 5.830  -0.011  40.576  1.00 27.09 ? 137 TRP B CB     1 
ATOM   3735 C CG     . TRP B 1 143 ? 5.681  0.302   42.032  1.00 31.56 ? 137 TRP B CG     1 
ATOM   3736 C CD1    . TRP B 1 143 ? 4.687  -0.116  42.859  1.00 30.00 ? 137 TRP B CD1    1 
ATOM   3737 C CD2    . TRP B 1 143 ? 6.544  1.127   42.822  1.00 34.33 ? 137 TRP B CD2    1 
ATOM   3738 N NE1    . TRP B 1 143 ? 4.888  0.374   44.130  1.00 33.05 ? 137 TRP B NE1    1 
ATOM   3739 C CE2    . TRP B 1 143 ? 6.017  1.149   44.130  1.00 33.54 ? 137 TRP B CE2    1 
ATOM   3740 C CE3    . TRP B 1 143 ? 7.715  1.841   42.554  1.00 37.76 ? 137 TRP B CE3    1 
ATOM   3741 C CZ2    . TRP B 1 143 ? 6.619  1.860   45.165  1.00 38.34 ? 137 TRP B CZ2    1 
ATOM   3742 C CZ3    . TRP B 1 143 ? 8.313  2.546   43.588  1.00 43.60 ? 137 TRP B CZ3    1 
ATOM   3743 C CH2    . TRP B 1 143 ? 7.762  2.551   44.873  1.00 33.72 ? 137 TRP B CH2    1 
ATOM   3744 N N      . ARG B 1 144 ? 6.129  0.891   37.485  1.00 24.85 ? 138 ARG B N      1 
ATOM   3745 C CA     . ARG B 1 144 ? 6.322  0.470   36.102  1.00 22.66 ? 138 ARG B CA     1 
ATOM   3746 C C      . ARG B 1 144 ? 7.760  0.007   35.919  1.00 22.84 ? 138 ARG B C      1 
ATOM   3747 O O      . ARG B 1 144 ? 8.676  0.509   36.574  1.00 26.72 ? 138 ARG B O      1 
ATOM   3748 C CB     . ARG B 1 144 ? 6.049  1.615   35.113  1.00 29.14 ? 138 ARG B CB     1 
ATOM   3749 C CG     . ARG B 1 144 ? 4.629  2.161   35.150  1.00 39.90 ? 138 ARG B CG     1 
ATOM   3750 C CD     . ARG B 1 144 ? 3.602  1.062   34.956  1.00 41.63 ? 138 ARG B CD     1 
ATOM   3751 N NE     . ARG B 1 144 ? 2.266  1.484   35.367  1.00 53.89 ? 138 ARG B NE     1 
ATOM   3752 C CZ     . ARG B 1 144 ? 1.441  2.205   34.617  1.00 60.53 ? 138 ARG B CZ     1 
ATOM   3753 N NH1    . ARG B 1 144 ? 1.770  2.581   33.391  1.00 50.39 ? 138 ARG B NH1    1 
ATOM   3754 N NH2    . ARG B 1 144 ? 0.255  2.555   35.109  1.00 51.97 ? 138 ARG B NH2    1 
ATOM   3755 N N      . ILE B 1 145 ? 7.955  -0.952  35.014  1.00 25.98 ? 139 ILE B N      1 
ATOM   3756 C CA     . ILE B 1 145 ? 9.266  -1.559  34.799  1.00 22.44 ? 139 ILE B CA     1 
ATOM   3757 C C      . ILE B 1 145 ? 9.946  -0.919  33.594  1.00 24.21 ? 139 ILE B C      1 
ATOM   3758 O O      . ILE B 1 145 ? 9.321  -0.684  32.553  1.00 23.38 ? 139 ILE B O      1 
ATOM   3759 C CB     . ILE B 1 145 ? 9.159  -3.092  34.660  1.00 19.16 ? 139 ILE B CB     1 
ATOM   3760 C CG1    . ILE B 1 145 ? 10.554 -3.729  34.647  1.00 20.57 ? 139 ILE B CG1    1 
ATOM   3761 C CG2    . ILE B 1 145 ? 8.371  -3.494  33.397  1.00 23.97 ? 139 ILE B CG2    1 
ATOM   3762 C CD1    . ILE B 1 145 ? 10.523 -5.236  34.672  1.00 24.52 ? 139 ILE B CD1    1 
ATOM   3763 N N      . LEU B 1 146 ? 11.234 -0.625  33.734  1.00 20.31 ? 140 LEU B N      1 
ATOM   3764 C CA     . LEU B 1 146 ? 12.016 -0.153  32.595  1.00 23.06 ? 140 LEU B CA     1 
ATOM   3765 C C      . LEU B 1 146 ? 12.165 -1.272  31.571  1.00 21.64 ? 140 LEU B C      1 
ATOM   3766 O O      . LEU B 1 146 ? 12.544 -2.397  31.903  1.00 21.98 ? 140 LEU B O      1 
ATOM   3767 C CB     . LEU B 1 146 ? 13.391 0.328   33.064  1.00 20.98 ? 140 LEU B CB     1 
ATOM   3768 C CG     . LEU B 1 146 ? 14.389 0.742   31.971  1.00 22.17 ? 140 LEU B CG     1 
ATOM   3769 C CD1    . LEU B 1 146 ? 13.902 1.945   31.172  1.00 24.14 ? 140 LEU B CD1    1 
ATOM   3770 C CD2    . LEU B 1 146 ? 15.761 1.030   32.586  1.00 23.23 ? 140 LEU B CD2    1 
ATOM   3771 N N      . MET B 1 147 ? 11.870 -0.960  30.330  1.00 21.22 ? 141 MET B N      1 
ATOM   3772 C CA     . MET B 1 147 ? 11.866 -1.870  29.198  1.00 21.54 ? 141 MET B CA     1 
ATOM   3773 C C      . MET B 1 147 ? 13.173 -1.719  28.423  1.00 22.56 ? 141 MET B C      1 
ATOM   3774 O O      . MET B 1 147 ? 13.825 -0.672  28.489  1.00 22.71 ? 141 MET B O      1 
ATOM   3775 C CB     . MET B 1 147 ? 10.712 -1.437  28.291  1.00 24.83 ? 141 MET B CB     1 
ATOM   3776 C CG     . MET B 1 147 ? 9.303  -2.005  28.609  1.00 30.65 ? 141 MET B CG     1 
ATOM   3777 S SD     . MET B 1 147 ? 9.073  -3.594  29.418  1.00 27.27 ? 141 MET B SD     1 
ATOM   3778 C CE     . MET B 1 147 ? 8.977  -4.600  27.929  1.00 34.18 ? 141 MET B CE     1 
ATOM   3779 N N      . PRO B 1 148 ? 13.582 -2.734  27.650  1.00 20.91 ? 142 PRO B N      1 
ATOM   3780 C CA     . PRO B 1 148 ? 14.847 -2.615  26.894  1.00 26.91 ? 142 PRO B CA     1 
ATOM   3781 C C      . PRO B 1 148 ? 14.888 -1.447  25.918  1.00 23.81 ? 142 PRO B C      1 
ATOM   3782 O O      . PRO B 1 148 ? 15.968 -0.906  25.653  1.00 28.06 ? 142 PRO B O      1 
ATOM   3783 C CB     . PRO B 1 148 ? 14.948 -3.963  26.166  1.00 24.23 ? 142 PRO B CB     1 
ATOM   3784 C CG     . PRO B 1 148 ? 14.203 -4.911  27.056  1.00 24.51 ? 142 PRO B CG     1 
ATOM   3785 C CD     . PRO B 1 148 ? 13.055 -4.110  27.632  1.00 22.68 ? 142 PRO B CD     1 
ATOM   3786 N N      . ASP B 1 149 ? 13.744 -1.020  25.400  1.00 21.45 ? 143 ASP B N      1 
ATOM   3787 C CA     . ASP B 1 149 ? 13.680 0.129   24.509  1.00 25.89 ? 143 ASP B CA     1 
ATOM   3788 C C      . ASP B 1 149 ? 13.587 1.469   25.229  1.00 27.91 ? 143 ASP B C      1 
ATOM   3789 O O      . ASP B 1 149 ? 13.421 2.500   24.569  1.00 29.49 ? 143 ASP B O      1 
ATOM   3790 C CB     . ASP B 1 149 ? 12.576 -0.054  23.459  1.00 26.59 ? 143 ASP B CB     1 
ATOM   3791 C CG     . ASP B 1 149 ? 11.173 0.062   24.033  1.00 31.38 ? 143 ASP B CG     1 
ATOM   3792 O OD1    . ASP B 1 149 ? 11.020 0.319   25.259  1.00 28.95 ? 143 ASP B OD1    1 
ATOM   3793 O OD2    . ASP B 1 149 ? 10.211 -0.093  23.243  1.00 31.64 ? 143 ASP B OD2    1 
ATOM   3794 N N      . GLY B 1 150 ? 13.688 1.485   26.558  1.00 25.72 ? 144 GLY B N      1 
ATOM   3795 C CA     . GLY B 1 150 ? 13.683 2.724   27.296  1.00 27.39 ? 144 GLY B CA     1 
ATOM   3796 C C      . GLY B 1 150 ? 12.312 3.222   27.695  1.00 29.09 ? 144 GLY B C      1 
ATOM   3797 O O      . GLY B 1 150 ? 12.220 4.227   28.413  1.00 34.02 ? 144 GLY B O      1 
ATOM   3798 N N      . THR B 1 151 ? 11.247 2.561   27.254  1.00 27.95 ? 145 THR B N      1 
ATOM   3799 C CA     . THR B 1 151 ? 9.918  2.877   27.745  1.00 28.68 ? 145 THR B CA     1 
ATOM   3800 C C      . THR B 1 151 ? 9.676  2.150   29.067  1.00 26.23 ? 145 THR B C      1 
ATOM   3801 O O      . THR B 1 151 ? 10.518 1.394   29.558  1.00 25.09 ? 145 THR B O      1 
ATOM   3802 C CB     . THR B 1 151 ? 8.867  2.500   26.705  1.00 31.03 ? 145 THR B CB     1 
ATOM   3803 O OG1    . THR B 1 151 ? 8.863  1.078   26.507  1.00 30.75 ? 145 THR B OG1    1 
ATOM   3804 C CG2    . THR B 1 151 ? 9.148  3.194   25.379  1.00 34.00 ? 145 THR B CG2    1 
ATOM   3805 N N      . HIS B 1 152 ? 8.509  2.368   29.656  1.00 26.65 ? 146 HIS B N      1 
ATOM   3806 C CA     . HIS B 1 152 ? 8.133  1.668   30.870  1.00 26.50 ? 146 HIS B CA     1 
ATOM   3807 C C      . HIS B 1 152 ? 6.909  0.805   30.615  1.00 31.25 ? 146 HIS B C      1 
ATOM   3808 O O      . HIS B 1 152 ? 6.015  1.179   29.845  1.00 31.91 ? 146 HIS B O      1 
ATOM   3809 C CB     . HIS B 1 152 ? 7.942  2.643   32.030  1.00 29.17 ? 146 HIS B CB     1 
ATOM   3810 C CG     . HIS B 1 152 ? 9.231  3.222   32.523  1.00 30.42 ? 146 HIS B CG     1 
ATOM   3811 N ND1    . HIS B 1 152 ? 9.869  4.265   31.888  1.00 35.52 ? 146 HIS B ND1    1 
ATOM   3812 C CD2    . HIS B 1 152 ? 10.015 2.885   33.576  1.00 31.35 ? 146 HIS B CD2    1 
ATOM   3813 C CE1    . HIS B 1 152 ? 10.986 4.553   32.533  1.00 34.90 ? 146 HIS B CE1    1 
ATOM   3814 N NE2    . HIS B 1 152 ? 11.101 3.727   33.557  1.00 36.78 ? 146 HIS B NE2    1 
ATOM   3815 N N      . GLY B 1 153 ? 6.901  -0.372  31.237  1.00 26.96 ? 147 GLY B N      1 
ATOM   3816 C CA     . GLY B 1 153 ? 5.867  -1.357  31.032  1.00 29.85 ? 147 GLY B CA     1 
ATOM   3817 C C      . GLY B 1 153 ? 5.208  -1.776  32.334  1.00 27.63 ? 147 GLY B C      1 
ATOM   3818 O O      . GLY B 1 153 ? 5.520  -1.278  33.421  1.00 28.02 ? 147 GLY B O      1 
ATOM   3819 N N      . ILE B 1 154 ? 4.303  -2.736  32.199  1.00 30.12 ? 148 ILE B N      1 
ATOM   3820 C CA     . ILE B 1 154 ? 3.454  -3.192  33.292  1.00 24.63 ? 148 ILE B CA     1 
ATOM   3821 C C      . ILE B 1 154 ? 4.062  -4.447  33.900  1.00 24.06 ? 148 ILE B C      1 
ATOM   3822 O O      . ILE B 1 154 ? 4.462  -5.362  33.175  1.00 25.62 ? 148 ILE B O      1 
ATOM   3823 C CB     . ILE B 1 154 ? 2.033  -3.482  32.777  1.00 33.94 ? 148 ILE B CB     1 
ATOM   3824 C CG1    . ILE B 1 154 ? 1.404  -2.215  32.196  1.00 40.52 ? 148 ILE B CG1    1 
ATOM   3825 C CG2    . ILE B 1 154 ? 1.168  -4.021  33.908  1.00 31.03 ? 148 ILE B CG2    1 
ATOM   3826 C CD1    . ILE B 1 154 ? 1.357  -1.067  33.176  1.00 47.43 ? 148 ILE B CD1    1 
ATOM   3827 N N      . TYR B 1 155 ? 4.135  -4.499  35.233  1.00 26.25 ? 149 TYR B N      1 
ATOM   3828 C CA     . TYR B 1 155 ? 4.565  -5.725  35.906  1.00 26.65 ? 149 TYR B CA     1 
ATOM   3829 C C      . TYR B 1 155 ? 3.488  -6.800  35.787  1.00 23.67 ? 149 TYR B C      1 
ATOM   3830 O O      . TYR B 1 155 ? 2.317  -6.541  36.108  1.00 24.91 ? 149 TYR B O      1 
ATOM   3831 C CB     . TYR B 1 155 ? 4.856  -5.460  37.385  1.00 24.21 ? 149 TYR B CB     1 
ATOM   3832 C CG     . TYR B 1 155 ? 6.143  -4.712  37.653  1.00 23.24 ? 149 TYR B CG     1 
ATOM   3833 C CD1    . TYR B 1 155 ? 7.376  -5.347  37.539  1.00 22.43 ? 149 TYR B CD1    1 
ATOM   3834 C CD2    . TYR B 1 155 ? 6.125  -3.371  38.034  1.00 25.09 ? 149 TYR B CD2    1 
ATOM   3835 C CE1    . TYR B 1 155 ? 8.558  -4.668  37.796  1.00 25.22 ? 149 TYR B CE1    1 
ATOM   3836 C CE2    . TYR B 1 155 ? 7.303  -2.682  38.295  1.00 23.79 ? 149 TYR B CE2    1 
ATOM   3837 C CZ     . TYR B 1 155 ? 8.509  -3.339  38.181  1.00 22.08 ? 149 TYR B CZ     1 
ATOM   3838 O OH     . TYR B 1 155 ? 9.674  -2.663  38.411  1.00 26.50 ? 149 TYR B OH     1 
ATOM   3839 N N      . PRO B 1 156 ? 3.832  -8.004  35.338  1.00 25.41 ? 150 PRO B N      1 
ATOM   3840 C CA     . PRO B 1 156 ? 2.841  -9.070  35.169  1.00 26.97 ? 150 PRO B CA     1 
ATOM   3841 C C      . PRO B 1 156 ? 2.633  -9.847  36.465  1.00 26.60 ? 150 PRO B C      1 
ATOM   3842 O O      . PRO B 1 156 ? 3.352  -9.676  37.447  1.00 25.92 ? 150 PRO B O      1 
ATOM   3843 C CB     . PRO B 1 156 ? 3.527  -9.985  34.152  1.00 29.02 ? 150 PRO B CB     1 
ATOM   3844 C CG     . PRO B 1 156 ? 4.980  -9.855  34.506  1.00 27.55 ? 150 PRO B CG     1 
ATOM   3845 C CD     . PRO B 1 156 ? 5.164  -8.408  34.854  1.00 26.53 ? 150 PRO B CD     1 
ATOM   3846 N N      . LYS B 1 157 ? 1.649  -10.736 36.428  1.00 25.19 ? 151 LYS B N      1 
ATOM   3847 C CA     . LYS B 1 157 ? 1.421  -11.642 37.551  1.00 28.88 ? 151 LYS B CA     1 
ATOM   3848 C C      . LYS B 1 157 ? 2.552  -12.662 37.618  1.00 27.70 ? 151 LYS B C      1 
ATOM   3849 O O      . LYS B 1 157 ? 2.891  -13.279 36.599  1.00 27.67 ? 151 LYS B O      1 
ATOM   3850 C CB     . LYS B 1 157 ? 0.100  -12.378 37.336  1.00 34.07 ? 151 LYS B CB     1 
ATOM   3851 C CG     . LYS B 1 157 ? -1.060 -11.836 38.137  1.00 45.74 ? 151 LYS B CG     1 
ATOM   3852 C CD     . LYS B 1 157 ? -2.238 -12.803 38.108  1.00 49.62 ? 151 LYS B CD     1 
ATOM   3853 C CE     . LYS B 1 157 ? -3.546 -12.071 37.879  1.00 51.51 ? 151 LYS B CE     1 
ATOM   3854 N NZ     . LYS B 1 157 ? -4.653 -13.015 37.554  1.00 54.17 ? 151 LYS B NZ     1 
ATOM   3855 N N      . PRO B 1 158 ? 3.167  -12.865 38.776  1.00 26.24 ? 152 PRO B N      1 
ATOM   3856 C CA     . PRO B 1 158 ? 4.192  -13.899 38.895  1.00 26.54 ? 152 PRO B CA     1 
ATOM   3857 C C      . PRO B 1 158 ? 3.564  -15.257 39.188  1.00 27.54 ? 152 PRO B C      1 
ATOM   3858 O O      . PRO B 1 158 ? 2.370  -15.379 39.475  1.00 29.16 ? 152 PRO B O      1 
ATOM   3859 C CB     . PRO B 1 158 ? 4.991  -13.432 40.116  1.00 21.34 ? 152 PRO B CB     1 
ATOM   3860 C CG     . PRO B 1 158 ? 3.943  -12.777 40.991  1.00 23.48 ? 152 PRO B CG     1 
ATOM   3861 C CD     . PRO B 1 158 ? 3.037  -12.061 40.003  1.00 28.37 ? 152 PRO B CD     1 
ATOM   3862 N N      . ARG B 1 159 ? 4.412  -16.274 39.120  1.00 25.98 ? 153 ARG B N      1 
ATOM   3863 C CA     . ARG B 1 159 ? 4.084  -17.646 39.478  1.00 26.77 ? 153 ARG B CA     1 
ATOM   3864 C C      . ARG B 1 159 ? 4.603  -17.899 40.894  1.00 30.69 ? 153 ARG B C      1 
ATOM   3865 O O      . ARG B 1 159 ? 5.788  -17.684 41.174  1.00 29.31 ? 153 ARG B O      1 
ATOM   3866 C CB     . ARG B 1 159 ? 4.784  -18.574 38.489  1.00 28.53 ? 153 ARG B CB     1 
ATOM   3867 C CG     . ARG B 1 159 ? 4.493  -20.043 38.623  1.00 33.39 ? 153 ARG B CG     1 
ATOM   3868 C CD     . ARG B 1 159 ? 5.029  -20.789 37.391  1.00 33.89 ? 153 ARG B CD     1 
ATOM   3869 N NE     . ARG B 1 159 ? 6.470  -20.657 37.168  1.00 28.27 ? 153 ARG B NE     1 
ATOM   3870 C CZ     . ARG B 1 159 ? 7.405  -21.304 37.850  1.00 34.00 ? 153 ARG B CZ     1 
ATOM   3871 N NH1    . ARG B 1 159 ? 7.096  -22.108 38.856  1.00 32.46 ? 153 ARG B NH1    1 
ATOM   3872 N NH2    . ARG B 1 159 ? 8.681  -21.144 37.512  1.00 31.01 ? 153 ARG B NH2    1 
ATOM   3873 N N      . ALA B 1 160 ? 3.722  -18.339 41.787  1.00 26.44 ? 154 ALA B N      1 
ATOM   3874 C CA     . ALA B 1 160 ? 4.127  -18.643 43.157  1.00 28.90 ? 154 ALA B CA     1 
ATOM   3875 C C      . ALA B 1 160 ? 4.789  -20.015 43.183  1.00 29.28 ? 154 ALA B C      1 
ATOM   3876 O O      . ALA B 1 160 ? 4.182  -21.011 42.773  1.00 34.29 ? 154 ALA B O      1 
ATOM   3877 C CB     . ALA B 1 160 ? 2.918  -18.611 44.088  1.00 28.73 ? 154 ALA B CB     1 
ATOM   3878 N N      . ILE B 1 161 ? 6.027  -20.073 43.658  1.00 23.96 ? 155 ILE B N      1 
ATOM   3879 C CA     . ILE B 1 161 ? 6.823  -21.292 43.560  1.00 24.96 ? 155 ILE B CA     1 
ATOM   3880 C C      . ILE B 1 161 ? 6.579  -22.193 44.764  1.00 26.48 ? 155 ILE B C      1 
ATOM   3881 O O      . ILE B 1 161 ? 6.312  -21.729 45.877  1.00 28.62 ? 155 ILE B O      1 
ATOM   3882 C CB     . ILE B 1 161 ? 8.322  -20.978 43.361  1.00 23.03 ? 155 ILE B CB     1 
ATOM   3883 C CG1    . ILE B 1 161 ? 8.878  -20.123 44.509  1.00 26.56 ? 155 ILE B CG1    1 
ATOM   3884 C CG2    . ILE B 1 161 ? 8.544  -20.314 41.992  1.00 25.72 ? 155 ILE B CG2    1 
ATOM   3885 C CD1    . ILE B 1 161 ? 10.389 -19.942 44.441  1.00 28.31 ? 155 ILE B CD1    1 
ATOM   3886 N N      . GLY B 1 162 ? 6.685  -23.503 44.537  1.00 26.15 ? 156 GLY B N      1 
ATOM   3887 C CA     . GLY B 1 162 ? 6.616  -24.474 45.610  1.00 27.01 ? 156 GLY B CA     1 
ATOM   3888 C C      . GLY B 1 162 ? 7.956  -24.648 46.303  1.00 26.71 ? 156 GLY B C      1 
ATOM   3889 O O      . GLY B 1 162 ? 8.964  -24.037 45.951  1.00 25.52 ? 156 GLY B O      1 
ATOM   3890 N N      . THR B 1 163 ? 7.975  -25.517 47.316  1.00 27.14 ? 157 THR B N      1 
ATOM   3891 C CA     . THR B 1 163 ? 9.191  -25.613 48.123  1.00 23.13 ? 157 THR B CA     1 
ATOM   3892 C C      . THR B 1 163 ? 10.321 -26.340 47.397  1.00 24.42 ? 157 THR B C      1 
ATOM   3893 O O      . THR B 1 163 ? 11.498 -26.090 47.681  1.00 24.86 ? 157 THR B O      1 
ATOM   3894 C CB     . THR B 1 163 ? 8.898  -26.230 49.495  1.00 29.30 ? 157 THR B CB     1 
ATOM   3895 O OG1    . THR B 1 163 ? 8.420  -27.570 49.333  1.00 27.63 ? 157 THR B OG1    1 
ATOM   3896 C CG2    . THR B 1 163 ? 7.859  -25.402 50.235  1.00 28.47 ? 157 THR B CG2    1 
ATOM   3897 N N      . TYR B 1 164 ? 9.999  -27.232 46.454  1.00 26.23 ? 158 TYR B N      1 
ATOM   3898 C CA     . TYR B 1 164 ? 11.058 -27.847 45.663  1.00 26.42 ? 158 TYR B CA     1 
ATOM   3899 C C      . TYR B 1 164 ? 11.772 -26.794 44.828  1.00 22.53 ? 158 TYR B C      1 
ATOM   3900 O O      . TYR B 1 164 ? 13.007 -26.731 44.800  1.00 25.31 ? 158 TYR B O      1 
ATOM   3901 C CB     . TYR B 1 164 ? 10.484 -28.938 44.760  1.00 25.95 ? 158 TYR B CB     1 
ATOM   3902 C CG     . TYR B 1 164 ? 11.518 -29.581 43.870  1.00 25.30 ? 158 TYR B CG     1 
ATOM   3903 C CD1    . TYR B 1 164 ? 12.532 -30.365 44.407  1.00 27.92 ? 158 TYR B CD1    1 
ATOM   3904 C CD2    . TYR B 1 164 ? 11.482 -29.408 42.489  1.00 26.96 ? 158 TYR B CD2    1 
ATOM   3905 C CE1    . TYR B 1 164 ? 13.482 -30.959 43.605  1.00 32.37 ? 158 TYR B CE1    1 
ATOM   3906 C CE2    . TYR B 1 164 ? 12.425 -30.006 41.677  1.00 31.79 ? 158 TYR B CE2    1 
ATOM   3907 C CZ     . TYR B 1 164 ? 13.426 -30.777 42.243  1.00 33.69 ? 158 TYR B CZ     1 
ATOM   3908 O OH     . TYR B 1 164 ? 14.375 -31.375 41.449  1.00 36.00 ? 158 TYR B OH     1 
ATOM   3909 N N      . GLU B 1 165 ? 10.997 -25.933 44.169  1.00 24.87 ? 159 GLU B N      1 
ATOM   3910 C CA     . GLU B 1 165 ? 11.580 -24.846 43.389  1.00 26.21 ? 159 GLU B CA     1 
ATOM   3911 C C      . GLU B 1 165 ? 12.371 -23.888 44.272  1.00 24.94 ? 159 GLU B C      1 
ATOM   3912 O O      . GLU B 1 165 ? 13.418 -23.379 43.860  1.00 23.98 ? 159 GLU B O      1 
ATOM   3913 C CB     . GLU B 1 165 ? 10.479 -24.094 42.644  1.00 26.45 ? 159 GLU B CB     1 
ATOM   3914 C CG     . GLU B 1 165 ? 11.007 -22.994 41.720  1.00 30.97 ? 159 GLU B CG     1 
ATOM   3915 C CD     . GLU B 1 165 ? 10.277 -22.905 40.394  1.00 37.74 ? 159 GLU B CD     1 
ATOM   3916 O OE1    . GLU B 1 165 ? 9.192  -23.514 40.248  1.00 36.01 ? 159 GLU B OE1    1 
ATOM   3917 O OE2    . GLU B 1 165 ? 10.762 -22.158 39.520  1.00 31.81 ? 159 GLU B OE2    1 
ATOM   3918 N N      . ILE B 1 166 ? 11.887 -23.623 45.490  1.00 24.11 ? 160 ILE B N      1 
ATOM   3919 C CA     . ILE B 1 166 ? 12.648 -22.786 46.418  1.00 21.63 ? 160 ILE B CA     1 
ATOM   3920 C C      . ILE B 1 166 ? 14.043 -23.360 46.624  1.00 23.53 ? 160 ILE B C      1 
ATOM   3921 O O      . ILE B 1 166 ? 15.048 -22.635 46.593  1.00 23.36 ? 160 ILE B O      1 
ATOM   3922 C CB     . ILE B 1 166 ? 11.901 -22.637 47.757  1.00 23.93 ? 160 ILE B CB     1 
ATOM   3923 C CG1    . ILE B 1 166 ? 10.737 -21.661 47.616  1.00 24.49 ? 160 ILE B CG1    1 
ATOM   3924 C CG2    . ILE B 1 166 ? 12.857 -22.136 48.829  1.00 23.48 ? 160 ILE B CG2    1 
ATOM   3925 C CD1    . ILE B 1 166 ? 9.773  -21.685 48.816  1.00 24.64 ? 160 ILE B CD1    1 
ATOM   3926 N N      . SER B 1 167 ? 14.132 -24.677 46.846  1.00 25.54 ? 161 SER B N      1 
ATOM   3927 C CA     . SER B 1 167 ? 15.446 -25.287 47.037  1.00 28.25 ? 161 SER B CA     1 
ATOM   3928 C C      . SER B 1 167 ? 16.307 -25.193 45.778  1.00 24.73 ? 161 SER B C      1 
ATOM   3929 O O      . SER B 1 167 ? 17.533 -25.081 45.875  1.00 25.61 ? 161 SER B O      1 
ATOM   3930 C CB     . SER B 1 167 ? 15.307 -26.730 47.534  1.00 31.75 ? 161 SER B CB     1 
ATOM   3931 O OG     . SER B 1 167 ? 14.943 -27.617 46.491  1.00 37.51 ? 161 SER B OG     1 
ATOM   3932 N N      . GLN B 1 168 ? 15.689 -25.217 44.595  1.00 25.25 ? 162 GLN B N      1 
ATOM   3933 C CA     . GLN B 1 168 ? 16.458 -25.029 43.368  1.00 24.05 ? 162 GLN B CA     1 
ATOM   3934 C C      . GLN B 1 168 ? 16.994 -23.605 43.254  1.00 24.50 ? 162 GLN B C      1 
ATOM   3935 O O      . GLN B 1 168 ? 18.108 -23.396 42.758  1.00 26.03 ? 162 GLN B O      1 
ATOM   3936 C CB     . GLN B 1 168 ? 15.597 -25.377 42.155  1.00 28.51 ? 162 GLN B CB     1 
ATOM   3937 C CG     . GLN B 1 168 ? 15.206 -26.841 42.053  1.00 29.50 ? 162 GLN B CG     1 
ATOM   3938 C CD     . GLN B 1 168 ? 14.402 -27.126 40.801  1.00 35.73 ? 162 GLN B CD     1 
ATOM   3939 O OE1    . GLN B 1 168 ? 13.300 -26.598 40.636  1.00 34.15 ? 162 GLN B OE1    1 
ATOM   3940 N NE2    . GLN B 1 168 ? 14.938 -27.964 39.915  1.00 38.12 ? 162 GLN B NE2    1 
ATOM   3941 N N      . VAL B 1 169 ? 16.215 -22.611 43.696  1.00 24.63 ? 163 VAL B N      1 
ATOM   3942 C CA     . VAL B 1 169 ? 16.695 -21.230 43.662  1.00 22.52 ? 163 VAL B CA     1 
ATOM   3943 C C      . VAL B 1 169 ? 17.840 -21.043 44.646  1.00 25.17 ? 163 VAL B C      1 
ATOM   3944 O O      . VAL B 1 169 ? 18.822 -20.346 44.357  1.00 24.05 ? 163 VAL B O      1 
ATOM   3945 C CB     . VAL B 1 169 ? 15.549 -20.229 43.911  1.00 24.19 ? 163 VAL B CB     1 
ATOM   3946 C CG1    . VAL B 1 169 ? 16.091 -18.811 43.952  1.00 25.71 ? 163 VAL B CG1    1 
ATOM   3947 C CG2    . VAL B 1 169 ? 14.452 -20.361 42.862  1.00 23.50 ? 163 VAL B CG2    1 
ATOM   3948 N N      . VAL B 1 170 ? 17.719 -21.639 45.838  1.00 24.31 ? 164 VAL B N      1 
ATOM   3949 C CA     . VAL B 1 170 ? 18.826 -21.628 46.790  1.00 27.06 ? 164 VAL B CA     1 
ATOM   3950 C C      . VAL B 1 170 ? 20.086 -22.185 46.141  1.00 25.10 ? 164 VAL B C      1 
ATOM   3951 O O      . VAL B 1 170 ? 21.181 -21.624 46.279  1.00 23.64 ? 164 VAL B O      1 
ATOM   3952 C CB     . VAL B 1 170 ? 18.439 -22.407 48.062  1.00 23.38 ? 164 VAL B CB     1 
ATOM   3953 C CG1    . VAL B 1 170 ? 19.654 -22.586 48.961  1.00 27.58 ? 164 VAL B CG1    1 
ATOM   3954 C CG2    . VAL B 1 170 ? 17.303 -21.703 48.808  1.00 23.70 ? 164 VAL B CG2    1 
ATOM   3955 N N      . GLU B 1 171 ? 19.951 -23.293 45.412  1.00 24.61 ? 165 GLU B N      1 
ATOM   3956 C CA     . GLU B 1 171 ? 21.107 -23.864 44.729  1.00 26.64 ? 165 GLU B CA     1 
ATOM   3957 C C      . GLU B 1 171 ? 21.674 -22.919 43.667  1.00 22.99 ? 165 GLU B C      1 
ATOM   3958 O O      . GLU B 1 171 ? 22.888 -22.906 43.451  1.00 25.27 ? 165 GLU B O      1 
ATOM   3959 C CB     . GLU B 1 171 ? 20.755 -25.234 44.141  1.00 30.42 ? 165 GLU B CB     1 
ATOM   3960 C CG     . GLU B 1 171 ? 21.869 -25.887 43.328  1.00 33.36 ? 165 GLU B CG     1 
ATOM   3961 C CD     . GLU B 1 171 ? 23.093 -26.257 44.151  1.00 42.81 ? 165 GLU B CD     1 
ATOM   3962 O OE1    . GLU B 1 171 ? 22.994 -26.348 45.399  1.00 40.64 ? 165 GLU B OE1    1 
ATOM   3963 O OE2    . GLU B 1 171 ? 24.165 -26.460 43.538  1.00 43.25 ? 165 GLU B OE2    1 
ATOM   3964 N N      . ASP B 1 172 ? 20.822 -22.111 43.018  1.00 25.52 ? 166 ASP B N      1 
ATOM   3965 C CA     . ASP B 1 172 ? 21.326 -21.110 42.074  1.00 27.31 ? 166 ASP B CA     1 
ATOM   3966 C C      . ASP B 1 172 ? 22.212 -20.086 42.778  1.00 25.50 ? 166 ASP B C      1 
ATOM   3967 O O      . ASP B 1 172 ? 23.269 -19.706 42.261  1.00 23.31 ? 166 ASP B O      1 
ATOM   3968 C CB     . ASP B 1 172 ? 20.181 -20.413 41.327  1.00 22.97 ? 166 ASP B CB     1 
ATOM   3969 C CG     . ASP B 1 172 ? 19.495 -21.318 40.310  1.00 29.36 ? 166 ASP B CG     1 
ATOM   3970 O OD1    . ASP B 1 172 ? 20.163 -22.209 39.748  1.00 32.97 ? 166 ASP B OD1    1 
ATOM   3971 O OD2    . ASP B 1 172 ? 18.291 -21.107 40.039  1.00 27.88 ? 166 ASP B OD2    1 
ATOM   3972 N N      . TYR B 1 173 ? 21.816 -19.646 43.977  1.00 23.17 ? 167 TYR B N      1 
ATOM   3973 C CA     . TYR B 1 173 ? 22.689 -18.767 44.754  1.00 21.47 ? 167 TYR B CA     1 
ATOM   3974 C C      . TYR B 1 173 ? 24.007 -19.460 45.093  1.00 21.56 ? 167 TYR B C      1 
ATOM   3975 O O      . TYR B 1 173 ? 25.086 -18.863 44.969  1.00 23.52 ? 167 TYR B O      1 
ATOM   3976 C CB     . TYR B 1 173 ? 21.984 -18.373 46.052  1.00 20.95 ? 167 TYR B CB     1 
ATOM   3977 C CG     . TYR B 1 173 ? 20.966 -17.259 45.938  1.00 20.19 ? 167 TYR B CG     1 
ATOM   3978 C CD1    . TYR B 1 173 ? 21.366 -15.926 45.863  1.00 23.16 ? 167 TYR B CD1    1 
ATOM   3979 C CD2    . TYR B 1 173 ? 19.611 -17.540 45.914  1.00 20.70 ? 167 TYR B CD2    1 
ATOM   3980 C CE1    . TYR B 1 173 ? 20.431 -14.897 45.788  1.00 22.29 ? 167 TYR B CE1    1 
ATOM   3981 C CE2    . TYR B 1 173 ? 18.666 -16.526 45.828  1.00 23.30 ? 167 TYR B CE2    1 
ATOM   3982 C CZ     . TYR B 1 173 ? 19.088 -15.206 45.754  1.00 20.08 ? 167 TYR B CZ     1 
ATOM   3983 O OH     . TYR B 1 173 ? 18.157 -14.199 45.685  1.00 22.50 ? 167 TYR B OH     1 
ATOM   3984 N N      . ARG B 1 174 ? 23.935 -20.720 45.531  1.00 22.74 ? 168 ARG B N      1 
ATOM   3985 C CA     . ARG B 1 174 ? 25.141 -21.462 45.895  1.00 23.37 ? 168 ARG B CA     1 
ATOM   3986 C C      . ARG B 1 174 ? 26.096 -21.575 44.713  1.00 24.75 ? 168 ARG B C      1 
ATOM   3987 O O      . ARG B 1 174 ? 27.296 -21.309 44.838  1.00 25.02 ? 168 ARG B O      1 
ATOM   3988 C CB     . ARG B 1 174 ? 24.757 -22.857 46.397  1.00 26.73 ? 168 ARG B CB     1 
ATOM   3989 C CG     . ARG B 1 174 ? 25.849 -23.540 47.210  1.00 30.53 ? 168 ARG B CG     1 
ATOM   3990 C CD     . ARG B 1 174 ? 25.521 -25.003 47.482  1.00 38.04 ? 168 ARG B CD     1 
ATOM   3991 N NE     . ARG B 1 174 ? 25.636 -25.819 46.280  1.00 42.21 ? 168 ARG B NE     1 
ATOM   3992 C CZ     . ARG B 1 174 ? 26.768 -26.366 45.856  1.00 51.67 ? 168 ARG B CZ     1 
ATOM   3993 N NH1    . ARG B 1 174 ? 27.900 -26.223 46.528  1.00 53.50 ? 168 ARG B NH1    1 
ATOM   3994 N NH2    . ARG B 1 174 ? 26.765 -27.074 44.729  1.00 55.93 ? 168 ARG B NH2    1 
ATOM   3995 N N      . ARG B 1 175 ? 25.571 -21.955 43.549  1.00 23.45 ? 169 ARG B N      1 
ATOM   3996 C CA     . ARG B 1 175 ? 26.418 -22.114 42.371  1.00 23.07 ? 169 ARG B CA     1 
ATOM   3997 C C      . ARG B 1 175 ? 27.013 -20.778 41.938  1.00 23.45 ? 169 ARG B C      1 
ATOM   3998 O O      . ARG B 1 175 ? 28.182 -20.705 41.531  1.00 24.34 ? 169 ARG B O      1 
ATOM   3999 C CB     . ARG B 1 175 ? 25.601 -22.763 41.248  1.00 29.47 ? 169 ARG B CB     1 
ATOM   4000 N N      . SER B 1 176 ? 26.217 -19.707 42.007  1.00 24.90 ? 170 SER B N      1 
ATOM   4001 C CA     . SER B 1 176 ? 26.714 -18.387 41.634  1.00 27.75 ? 170 SER B CA     1 
ATOM   4002 C C      . SER B 1 176 ? 27.793 -17.903 42.599  1.00 26.54 ? 170 SER B C      1 
ATOM   4003 O O      . SER B 1 176 ? 28.740 -17.228 42.183  1.00 24.38 ? 170 SER B O      1 
ATOM   4004 C CB     . SER B 1 176 ? 25.554 -17.391 41.568  1.00 26.97 ? 170 SER B CB     1 
ATOM   4005 O OG     . SER B 1 176 ? 24.730 -17.667 40.443  1.00 28.08 ? 170 SER B OG     1 
ATOM   4006 N N      . ALA B 1 177 ? 27.664 -18.225 43.894  1.00 22.54 ? 171 ALA B N      1 
ATOM   4007 C CA     . ALA B 1 177 ? 28.700 -17.851 44.851  1.00 20.93 ? 171 ALA B CA     1 
ATOM   4008 C C      . ALA B 1 177 ? 30.021 -18.547 44.532  1.00 22.60 ? 171 ALA B C      1 
ATOM   4009 O O      . ALA B 1 177 ? 31.089 -17.918 44.559  1.00 24.16 ? 171 ALA B O      1 
ATOM   4010 C CB     . ALA B 1 177 ? 28.222 -18.158 46.278  1.00 21.48 ? 171 ALA B CB     1 
ATOM   4011 N N      . LEU B 1 178 ? 29.966 -19.835 44.181  1.00 26.43 ? 172 LEU B N      1 
ATOM   4012 C CA     . LEU B 1 178 ? 31.181 -20.541 43.771  1.00 27.03 ? 172 LEU B CA     1 
ATOM   4013 C C      . LEU B 1 178 ? 31.766 -19.953 42.492  1.00 28.15 ? 172 LEU B C      1 
ATOM   4014 O O      . LEU B 1 178 ? 32.987 -19.804 42.369  1.00 26.60 ? 172 LEU B O      1 
ATOM   4015 C CB     . LEU B 1 178 ? 30.894 -22.034 43.605  1.00 25.23 ? 172 LEU B CB     1 
ATOM   4016 C CG     . LEU B 1 178 ? 30.592 -22.758 44.924  1.00 27.69 ? 172 LEU B CG     1 
ATOM   4017 C CD1    . LEU B 1 178 ? 29.874 -24.087 44.699  1.00 30.72 ? 172 LEU B CD1    1 
ATOM   4018 C CD2    . LEU B 1 178 ? 31.869 -22.956 45.735  1.00 26.23 ? 172 LEU B CD2    1 
ATOM   4019 N N      . ASN B 1 179 ? 30.909 -19.611 41.529  1.00 25.05 ? 173 ASN B N      1 
ATOM   4020 C CA     . ASN B 1 179 ? 31.381 -18.973 40.305  1.00 24.53 ? 173 ASN B CA     1 
ATOM   4021 C C      . ASN B 1 179 ? 32.064 -17.644 40.600  1.00 25.27 ? 173 ASN B C      1 
ATOM   4022 O O      . ASN B 1 179 ? 33.054 -17.290 39.952  1.00 25.10 ? 173 ASN B O      1 
ATOM   4023 C CB     . ASN B 1 179 ? 30.200 -18.766 39.354  1.00 24.49 ? 173 ASN B CB     1 
ATOM   4024 C CG     . ASN B 1 179 ? 29.770 -20.047 38.675  1.00 35.20 ? 173 ASN B CG     1 
ATOM   4025 O OD1    . ASN B 1 179 ? 30.408 -21.089 38.829  1.00 30.80 ? 173 ASN B OD1    1 
ATOM   4026 N ND2    . ASN B 1 179 ? 28.668 -19.982 37.930  1.00 33.09 ? 173 ASN B ND2    1 
ATOM   4027 N N      . ALA B 1 180 ? 31.542 -16.883 41.567  1.00 24.05 ? 174 ALA B N      1 
ATOM   4028 C CA     . ALA B 1 180 ? 32.166 -15.606 41.904  1.00 21.91 ? 174 ALA B CA     1 
ATOM   4029 C C      . ALA B 1 180 ? 33.563 -15.806 42.489  1.00 24.97 ? 174 ALA B C      1 
ATOM   4030 O O      . ALA B 1 180 ? 34.491 -15.057 42.163  1.00 24.40 ? 174 ALA B O      1 
ATOM   4031 C CB     . ALA B 1 180 ? 31.275 -14.821 42.868  1.00 23.54 ? 174 ALA B CB     1 
ATOM   4032 N N      . ILE B 1 181 ? 33.729 -16.813 43.349  1.00 23.95 ? 175 ILE B N      1 
ATOM   4033 C CA     . ILE B 1 181 ? 35.059 -17.157 43.847  1.00 25.38 ? 175 ILE B CA     1 
ATOM   4034 C C      . ILE B 1 181 ? 35.965 -17.586 42.699  1.00 26.32 ? 175 ILE B C      1 
ATOM   4035 O O      . ILE B 1 181 ? 37.149 -17.222 42.649  1.00 25.93 ? 175 ILE B O      1 
ATOM   4036 C CB     . ILE B 1 181 ? 34.961 -18.240 44.939  1.00 24.47 ? 175 ILE B CB     1 
ATOM   4037 C CG1    . ILE B 1 181 ? 34.241 -17.706 46.186  1.00 27.55 ? 175 ILE B CG1    1 
ATOM   4038 C CG2    . ILE B 1 181 ? 36.354 -18.755 45.309  1.00 26.67 ? 175 ILE B CG2    1 
ATOM   4039 C CD1    . ILE B 1 181 ? 34.660 -16.302 46.590  1.00 27.32 ? 175 ILE B CD1    1 
ATOM   4040 N N      . GLU B 1 182 ? 35.422 -18.355 41.755  1.00 25.44 ? 176 GLU B N      1 
ATOM   4041 C CA     . GLU B 1 182 ? 36.223 -18.795 40.618  1.00 27.46 ? 176 GLU B CA     1 
ATOM   4042 C C      . GLU B 1 182 ? 36.715 -17.607 39.799  1.00 32.86 ? 176 GLU B C      1 
ATOM   4043 O O      . GLU B 1 182 ? 37.835 -17.624 39.273  1.00 30.21 ? 176 GLU B O      1 
ATOM   4044 C CB     . GLU B 1 182 ? 35.411 -19.758 39.752  1.00 27.95 ? 176 GLU B CB     1 
ATOM   4045 C CG     . GLU B 1 182 ? 36.178 -20.255 38.533  1.00 36.04 ? 176 GLU B CG     1 
ATOM   4046 C CD     . GLU B 1 182 ? 35.340 -21.133 37.617  1.00 45.35 ? 176 GLU B CD     1 
ATOM   4047 O OE1    . GLU B 1 182 ? 34.212 -21.512 38.001  1.00 45.32 ? 176 GLU B OE1    1 
ATOM   4048 O OE2    . GLU B 1 182 ? 35.815 -21.442 36.503  1.00 53.95 ? 176 GLU B OE2    1 
ATOM   4049 N N      . ALA B 1 183 ? 35.894 -16.561 39.680  1.00 26.80 ? 177 ALA B N      1 
ATOM   4050 C CA     . ALA B 1 183 ? 36.299 -15.367 38.945  1.00 27.11 ? 177 ALA B CA     1 
ATOM   4051 C C      . ALA B 1 183 ? 37.282 -14.508 39.725  1.00 27.61 ? 177 ALA B C      1 
ATOM   4052 O O      . ALA B 1 183 ? 37.801 -13.530 39.172  1.00 28.69 ? 177 ALA B O      1 
ATOM   4053 C CB     . ALA B 1 183 ? 35.069 -14.534 38.579  1.00 25.88 ? 177 ALA B CB     1 
ATOM   4054 N N      . GLY B 1 184 ? 37.542 -14.839 40.989  1.00 24.85 ? 178 GLY B N      1 
ATOM   4055 C CA     . GLY B 1 184 ? 38.488 -14.099 41.794  1.00 25.43 ? 178 GLY B CA     1 
ATOM   4056 C C      . GLY B 1 184 ? 37.873 -13.108 42.759  1.00 24.27 ? 178 GLY B C      1 
ATOM   4057 O O      . GLY B 1 184 ? 38.620 -12.415 43.461  1.00 25.02 ? 178 GLY B O      1 
ATOM   4058 N N      . PHE B 1 185 ? 36.542 -13.007 42.811  1.00 21.83 ? 179 PHE B N      1 
ATOM   4059 C CA     . PHE B 1 185 ? 35.921 -12.096 43.762  1.00 22.18 ? 179 PHE B CA     1 
ATOM   4060 C C      . PHE B 1 185 ? 36.345 -12.443 45.190  1.00 23.79 ? 179 PHE B C      1 
ATOM   4061 O O      . PHE B 1 185 ? 36.533 -13.611 45.542  1.00 26.30 ? 179 PHE B O      1 
ATOM   4062 C CB     . PHE B 1 185 ? 34.395 -12.163 43.649  1.00 22.49 ? 179 PHE B CB     1 
ATOM   4063 C CG     . PHE B 1 185 ? 33.823 -11.347 42.515  1.00 24.69 ? 179 PHE B CG     1 
ATOM   4064 C CD1    . PHE B 1 185 ? 33.771 -9.962  42.602  1.00 22.00 ? 179 PHE B CD1    1 
ATOM   4065 C CD2    . PHE B 1 185 ? 33.335 -11.966 41.367  1.00 21.17 ? 179 PHE B CD2    1 
ATOM   4066 C CE1    . PHE B 1 185 ? 33.245 -9.202  41.572  1.00 20.78 ? 179 PHE B CE1    1 
ATOM   4067 C CE2    . PHE B 1 185 ? 32.794 -11.211 40.317  1.00 22.58 ? 179 PHE B CE2    1 
ATOM   4068 C CZ     . PHE B 1 185 ? 32.752 -9.826  40.422  1.00 22.93 ? 179 PHE B CZ     1 
ATOM   4069 N N      . ASP B 1 186 ? 36.493 -11.414 46.018  1.00 21.99 ? 180 ASP B N      1 
ATOM   4070 C CA     . ASP B 1 186 ? 36.817 -11.635 47.425  1.00 23.23 ? 180 ASP B CA     1 
ATOM   4071 C C      . ASP B 1 186 ? 35.637 -12.206 48.202  1.00 27.52 ? 180 ASP B C      1 
ATOM   4072 O O      . ASP B 1 186 ? 35.841 -12.892 49.209  1.00 25.18 ? 180 ASP B O      1 
ATOM   4073 C CB     . ASP B 1 186 ? 37.317 -10.331 48.033  1.00 22.39 ? 180 ASP B CB     1 
ATOM   4074 C CG     . ASP B 1 186 ? 38.557 -9.805  47.318  1.00 30.63 ? 180 ASP B CG     1 
ATOM   4075 O OD1    . ASP B 1 186 ? 39.625 -10.461 47.390  1.00 30.68 ? 180 ASP B OD1    1 
ATOM   4076 O OD2    . ASP B 1 186 ? 38.461 -8.748  46.663  1.00 26.71 ? 180 ASP B OD2    1 
ATOM   4077 N N      . GLY B 1 187 ? 34.416 -11.945 47.751  1.00 24.83 ? 181 GLY B N      1 
ATOM   4078 C CA     . GLY B 1 187 ? 33.247 -12.543 48.351  1.00 22.45 ? 181 GLY B CA     1 
ATOM   4079 C C      . GLY B 1 187 ? 32.015 -12.148 47.570  1.00 19.44 ? 181 GLY B C      1 
ATOM   4080 O O      . GLY B 1 187 ? 32.107 -11.612 46.462  1.00 22.10 ? 181 GLY B O      1 
ATOM   4081 N N      . ILE B 1 188 ? 30.851 -12.421 48.167  1.00 20.37 ? 182 ILE B N      1 
ATOM   4082 C CA     . ILE B 1 188 ? 29.569 -12.080 47.567  1.00 21.35 ? 182 ILE B CA     1 
ATOM   4083 C C      . ILE B 1 188 ? 28.696 -11.372 48.596  1.00 22.65 ? 182 ILE B C      1 
ATOM   4084 O O      . ILE B 1 188 ? 28.846 -11.548 49.808  1.00 21.25 ? 182 ILE B O      1 
ATOM   4085 C CB     . ILE B 1 188 ? 28.824 -13.307 46.994  1.00 19.83 ? 182 ILE B CB     1 
ATOM   4086 C CG1    . ILE B 1 188 ? 28.440 -14.309 48.094  1.00 24.50 ? 182 ILE B CG1    1 
ATOM   4087 C CG2    . ILE B 1 188 ? 29.641 -13.978 45.888  1.00 21.59 ? 182 ILE B CG2    1 
ATOM   4088 C CD1    . ILE B 1 188 ? 27.015 -14.129 48.682  1.00 26.26 ? 182 ILE B CD1    1 
ATOM   4089 N N      . GLU B 1 189 ? 27.737 -10.600 48.090  1.00 18.95 ? 183 GLU B N      1 
ATOM   4090 C CA     . GLU B 1 189 ? 26.696 -9.997  48.911  1.00 18.96 ? 183 GLU B CA     1 
ATOM   4091 C C      . GLU B 1 189 ? 25.354 -10.537 48.450  1.00 20.14 ? 183 GLU B C      1 
ATOM   4092 O O      . GLU B 1 189 ? 25.065 -10.549 47.247  1.00 21.06 ? 183 GLU B O      1 
ATOM   4093 C CB     . GLU B 1 189 ? 26.691 -8.471  48.783  1.00 20.25 ? 183 GLU B CB     1 
ATOM   4094 C CG     . GLU B 1 189 ? 25.585 -7.821  49.634  1.00 20.56 ? 183 GLU B CG     1 
ATOM   4095 C CD     . GLU B 1 189 ? 25.611 -6.311  49.557  1.00 25.26 ? 183 GLU B CD     1 
ATOM   4096 O OE1    . GLU B 1 189 ? 26.407 -5.696  50.281  1.00 24.59 ? 183 GLU B OE1    1 
ATOM   4097 O OE2    . GLU B 1 189 ? 24.856 -5.728  48.756  1.00 22.65 ? 183 GLU B OE2    1 
ATOM   4098 N N      . ILE B 1 190 ? 24.533 -10.974 49.396  1.00 20.49 ? 184 ILE B N      1 
ATOM   4099 C CA     . ILE B 1 190 ? 23.187 -11.437 49.083  1.00 22.27 ? 184 ILE B CA     1 
ATOM   4100 C C      . ILE B 1 190 ? 22.272 -10.220 49.025  1.00 20.66 ? 184 ILE B C      1 
ATOM   4101 O O      . ILE B 1 190 ? 22.111 -9.506  50.022  1.00 21.59 ? 184 ILE B O      1 
ATOM   4102 C CB     . ILE B 1 190 ? 22.696 -12.431 50.145  1.00 18.88 ? 184 ILE B CB     1 
ATOM   4103 C CG1    . ILE B 1 190 ? 23.487 -13.743 50.060  1.00 22.07 ? 184 ILE B CG1    1 
ATOM   4104 C CG2    . ILE B 1 190 ? 21.211 -12.682 49.975  1.00 21.48 ? 184 ILE B CG2    1 
ATOM   4105 C CD1    . ILE B 1 190 ? 23.388 -14.438 48.709  1.00 23.70 ? 184 ILE B CD1    1 
ATOM   4106 N N      . HIS B 1 191 ? 21.655 -9.990  47.869  1.00 21.04 ? 185 HIS B N      1 
ATOM   4107 C CA     . HIS B 1 191 ? 20.702 -8.890  47.722  1.00 21.04 ? 185 HIS B CA     1 
ATOM   4108 C C      . HIS B 1 191 ? 19.362 -9.339  48.294  1.00 20.56 ? 185 HIS B C      1 
ATOM   4109 O O      . HIS B 1 191 ? 18.587 -10.027 47.631  1.00 21.71 ? 185 HIS B O      1 
ATOM   4110 C CB     . HIS B 1 191 ? 20.572 -8.491  46.254  1.00 19.48 ? 185 HIS B CB     1 
ATOM   4111 C CG     . HIS B 1 191 ? 19.820 -7.209  46.039  1.00 18.80 ? 185 HIS B CG     1 
ATOM   4112 N ND1    . HIS B 1 191 ? 18.944 -6.691  46.972  1.00 21.67 ? 185 HIS B ND1    1 
ATOM   4113 C CD2    . HIS B 1 191 ? 19.800 -6.353  44.989  1.00 20.84 ? 185 HIS B CD2    1 
ATOM   4114 C CE1    . HIS B 1 191 ? 18.423 -5.567  46.507  1.00 21.82 ? 185 HIS B CE1    1 
ATOM   4115 N NE2    . HIS B 1 191 ? 18.932 -5.335  45.308  1.00 19.98 ? 185 HIS B NE2    1 
ATOM   4116 N N      . GLY B 1 192 ? 19.091 -8.966  49.544  1.00 18.55 ? 186 GLY B N      1 
ATOM   4117 C CA     . GLY B 1 192 ? 17.814 -9.273  50.164  1.00 22.54 ? 186 GLY B CA     1 
ATOM   4118 C C      . GLY B 1 192 ? 16.973 -8.040  50.425  1.00 21.89 ? 186 GLY B C      1 
ATOM   4119 O O      . GLY B 1 192 ? 16.179 -8.021  51.369  1.00 24.02 ? 186 GLY B O      1 
ATOM   4120 N N      . ALA B 1 193 ? 17.125 -7.020  49.585  1.00 21.20 ? 187 ALA B N      1 
ATOM   4121 C CA     . ALA B 1 193 ? 16.535 -5.703  49.779  1.00 20.01 ? 187 ALA B CA     1 
ATOM   4122 C C      . ALA B 1 193 ? 15.604 -5.317  48.622  1.00 21.22 ? 187 ALA B C      1 
ATOM   4123 O O      . ALA B 1 193 ? 15.437 -6.052  47.639  1.00 19.54 ? 187 ALA B O      1 
ATOM   4124 C CB     . ALA B 1 193 ? 17.638 -4.648  49.908  1.00 22.73 ? 187 ALA B CB     1 
ATOM   4125 N N      . HIS B 1 194 ? 14.985 -4.139  48.782  1.00 22.65 ? 188 HIS B N      1 
ATOM   4126 C CA     . HIS B 1 194 ? 14.343 -3.363  47.713  1.00 22.41 ? 188 HIS B CA     1 
ATOM   4127 C C      . HIS B 1 194 ? 13.168 -4.053  47.032  1.00 20.66 ? 188 HIS B C      1 
ATOM   4128 O O      . HIS B 1 194 ? 12.850 -3.721  45.880  1.00 21.38 ? 188 HIS B O      1 
ATOM   4129 C CB     . HIS B 1 194 ? 15.350 -2.848  46.669  1.00 21.21 ? 188 HIS B CB     1 
ATOM   4130 C CG     . HIS B 1 194 ? 16.474 -2.058  47.263  1.00 24.27 ? 188 HIS B CG     1 
ATOM   4131 N ND1    . HIS B 1 194 ? 17.790 -2.213  46.879  1.00 23.62 ? 188 HIS B ND1    1 
ATOM   4132 C CD2    . HIS B 1 194 ? 16.480 -1.130  48.249  1.00 34.00 ? 188 HIS B CD2    1 
ATOM   4133 C CE1    . HIS B 1 194 ? 18.553 -1.392  47.576  1.00 28.31 ? 188 HIS B CE1    1 
ATOM   4134 N NE2    . HIS B 1 194 ? 17.782 -0.725  48.417  1.00 34.39 ? 188 HIS B NE2    1 
ATOM   4135 N N      . GLY B 1 195 ? 12.501 -4.998  47.685  1.00 22.18 ? 189 GLY B N      1 
ATOM   4136 C CA     . GLY B 1 195 ? 11.330 -5.609  47.076  1.00 21.64 ? 189 GLY B CA     1 
ATOM   4137 C C      . GLY B 1 195 ? 11.604 -6.699  46.063  1.00 20.33 ? 189 GLY B C      1 
ATOM   4138 O O      . GLY B 1 195 ? 10.694 -7.083  45.323  1.00 21.30 ? 189 GLY B O      1 
ATOM   4139 N N      . TYR B 1 196 ? 12.821 -7.218  46.010  1.00 17.85 ? 190 TYR B N      1 
ATOM   4140 C CA     . TYR B 1 196 ? 13.188 -8.247  45.042  1.00 16.82 ? 190 TYR B CA     1 
ATOM   4141 C C      . TYR B 1 196 ? 12.853 -9.614  45.647  1.00 18.96 ? 190 TYR B C      1 
ATOM   4142 O O      . TYR B 1 196 ? 12.089 -9.678  46.609  1.00 19.59 ? 190 TYR B O      1 
ATOM   4143 C CB     . TYR B 1 196 ? 14.614 -7.985  44.529  1.00 19.84 ? 190 TYR B CB     1 
ATOM   4144 C CG     . TYR B 1 196 ? 14.687 -6.713  43.708  1.00 19.02 ? 190 TYR B CG     1 
ATOM   4145 C CD1    . TYR B 1 196 ? 13.939 -6.566  42.535  1.00 20.78 ? 190 TYR B CD1    1 
ATOM   4146 C CD2    . TYR B 1 196 ? 15.452 -5.639  44.128  1.00 17.91 ? 190 TYR B CD2    1 
ATOM   4147 C CE1    . TYR B 1 196 ? 13.996 -5.389  41.785  1.00 21.51 ? 190 TYR B CE1    1 
ATOM   4148 C CE2    . TYR B 1 196 ? 15.503 -4.466  43.413  1.00 21.13 ? 190 TYR B CE2    1 
ATOM   4149 C CZ     . TYR B 1 196 ? 14.771 -4.341  42.246  1.00 22.76 ? 190 TYR B CZ     1 
ATOM   4150 O OH     . TYR B 1 196 ? 14.834 -3.173  41.527  1.00 28.02 ? 190 TYR B OH     1 
ATOM   4151 N N      . LEU B 1 197 ? 13.392 -10.712 45.108  1.00 20.79 ? 191 LEU B N      1 
ATOM   4152 C CA     . LEU B 1 197 ? 12.873 -12.041 45.447  1.00 18.94 ? 191 LEU B CA     1 
ATOM   4153 C C      . LEU B 1 197 ? 12.920 -12.320 46.951  1.00 20.99 ? 191 LEU B C      1 
ATOM   4154 O O      . LEU B 1 197 ? 11.926 -12.765 47.537  1.00 21.96 ? 191 LEU B O      1 
ATOM   4155 C CB     . LEU B 1 197 ? 13.608 -13.135 44.671  1.00 21.20 ? 191 LEU B CB     1 
ATOM   4156 C CG     . LEU B 1 197 ? 13.099 -14.544 44.999  1.00 20.26 ? 191 LEU B CG     1 
ATOM   4157 C CD1    . LEU B 1 197 ? 11.631 -14.718 44.589  1.00 23.16 ? 191 LEU B CD1    1 
ATOM   4158 C CD2    . LEU B 1 197 ? 13.977 -15.617 44.370  1.00 22.05 ? 191 LEU B CD2    1 
ATOM   4159 N N      . ILE B 1 198 ? 14.073 -12.087 47.592  1.00 19.01 ? 192 ILE B N      1 
ATOM   4160 C CA     . ILE B 1 198 ? 14.184 -12.358 49.031  1.00 19.10 ? 192 ILE B CA     1 
ATOM   4161 C C      . ILE B 1 198 ? 13.225 -11.487 49.825  1.00 21.38 ? 192 ILE B C      1 
ATOM   4162 O O      . ILE B 1 198 ? 12.550 -11.965 50.749  1.00 21.25 ? 192 ILE B O      1 
ATOM   4163 C CB     . ILE B 1 198 ? 15.636 -12.215 49.508  1.00 19.48 ? 192 ILE B CB     1 
ATOM   4164 C CG1    . ILE B 1 198 ? 16.473 -13.340 48.909  1.00 20.53 ? 192 ILE B CG1    1 
ATOM   4165 C CG2    . ILE B 1 198 ? 15.707 -12.257 51.036  1.00 20.87 ? 192 ILE B CG2    1 
ATOM   4166 C CD1    . ILE B 1 198 ? 17.957 -13.120 49.076  1.00 18.77 ? 192 ILE B CD1    1 
ATOM   4167 N N      . ASP B 1 199 ? 13.144 -10.201 49.477  1.00 23.80 ? 193 ASP B N      1 
ATOM   4168 C CA     . ASP B 1 199 ? 12.203 -9.305  50.144  1.00 22.76 ? 193 ASP B CA     1 
ATOM   4169 C C      . ASP B 1 199 ? 10.753 -9.743  49.929  1.00 19.96 ? 193 ASP B C      1 
ATOM   4170 O O      . ASP B 1 199 ? 9.895  -9.489  50.784  1.00 22.18 ? 193 ASP B O      1 
ATOM   4171 C CB     . ASP B 1 199 ? 12.393 -7.874  49.634  1.00 26.99 ? 193 ASP B CB     1 
ATOM   4172 C CG     . ASP B 1 199 ? 12.274 -6.828  50.737  1.00 22.71 ? 193 ASP B CG     1 
ATOM   4173 O OD1    . ASP B 1 199 ? 12.426 -7.169  51.934  1.00 24.04 ? 193 ASP B OD1    1 
ATOM   4174 O OD2    . ASP B 1 199 ? 12.088 -5.635  50.412  1.00 27.92 ? 193 ASP B OD2    1 
ATOM   4175 N N      . GLN B 1 200 ? 10.456 -10.400 48.803  1.00 20.67 ? 194 GLN B N      1 
ATOM   4176 C CA     . GLN B 1 200 ? 9.103  -10.890 48.575  1.00 18.63 ? 194 GLN B CA     1 
ATOM   4177 C C      . GLN B 1 200 ? 8.731  -12.035 49.515  1.00 21.00 ? 194 GLN B C      1 
ATOM   4178 O O      . GLN B 1 200 ? 7.538  -12.300 49.708  1.00 24.02 ? 194 GLN B O      1 
ATOM   4179 C CB     . GLN B 1 200 ? 8.930  -11.302 47.108  1.00 17.89 ? 194 GLN B CB     1 
ATOM   4180 C CG     . GLN B 1 200 ? 9.014  -10.128 46.138  1.00 21.59 ? 194 GLN B CG     1 
ATOM   4181 C CD     . GLN B 1 200 ? 9.459  -10.527 44.733  1.00 20.09 ? 194 GLN B CD     1 
ATOM   4182 O OE1    . GLN B 1 200 ? 9.222  -11.646 44.275  1.00 21.49 ? 194 GLN B OE1    1 
ATOM   4183 N NE2    . GLN B 1 200 ? 10.138 -9.609  44.057  1.00 22.28 ? 194 GLN B NE2    1 
ATOM   4184 N N      . PHE B 1 201 ? 9.719  -12.730 50.082  1.00 19.97 ? 195 PHE B N      1 
ATOM   4185 C CA     . PHE B 1 201 ? 9.464  -13.670 51.170  1.00 21.70 ? 195 PHE B CA     1 
ATOM   4186 C C      . PHE B 1 201 ? 9.456  -12.982 52.533  1.00 22.65 ? 195 PHE B C      1 
ATOM   4187 O O      . PHE B 1 201 ? 8.646  -13.337 53.394  1.00 23.55 ? 195 PHE B O      1 
ATOM   4188 C CB     . PHE B 1 201 ? 10.495 -14.806 51.140  1.00 23.02 ? 195 PHE B CB     1 
ATOM   4189 C CG     . PHE B 1 201 ? 10.194 -15.866 50.109  1.00 23.39 ? 195 PHE B CG     1 
ATOM   4190 C CD1    . PHE B 1 201 ? 10.628 -15.722 48.787  1.00 21.59 ? 195 PHE B CD1    1 
ATOM   4191 C CD2    . PHE B 1 201 ? 9.434  -16.983 50.444  1.00 26.87 ? 195 PHE B CD2    1 
ATOM   4192 C CE1    . PHE B 1 201 ? 10.342 -16.684 47.848  1.00 23.51 ? 195 PHE B CE1    1 
ATOM   4193 C CE2    . PHE B 1 201 ? 9.136  -17.950 49.487  1.00 23.91 ? 195 PHE B CE2    1 
ATOM   4194 C CZ     . PHE B 1 201 ? 9.590  -17.797 48.189  1.00 22.04 ? 195 PHE B CZ     1 
ATOM   4195 N N      . LEU B 1 202 ? 10.323 -11.985 52.744  1.00 20.48 ? 196 LEU B N      1 
ATOM   4196 C CA     . LEU B 1 202 ? 10.444 -11.386 54.081  1.00 19.91 ? 196 LEU B CA     1 
ATOM   4197 C C      . LEU B 1 202 ? 9.214  -10.574 54.458  1.00 20.05 ? 196 LEU B C      1 
ATOM   4198 O O      . LEU B 1 202 ? 8.753  -10.634 55.611  1.00 22.82 ? 196 LEU B O      1 
ATOM   4199 C CB     . LEU B 1 202 ? 11.666 -10.470 54.135  1.00 22.43 ? 196 LEU B CB     1 
ATOM   4200 C CG     . LEU B 1 202 ? 13.030 -11.137 54.153  1.00 19.14 ? 196 LEU B CG     1 
ATOM   4201 C CD1    . LEU B 1 202 ? 14.105 -10.082 53.988  1.00 23.82 ? 196 LEU B CD1    1 
ATOM   4202 C CD2    . LEU B 1 202 ? 13.192 -11.896 55.459  1.00 22.73 ? 196 LEU B CD2    1 
ATOM   4203 N N      . LYS B 1 203 ? 8.665  -9.814  53.514  1.00 24.10 ? 197 LYS B N      1 
ATOM   4204 C CA     . LYS B 1 203 ? 7.696  -8.762  53.803  1.00 21.75 ? 197 LYS B CA     1 
ATOM   4205 C C      . LYS B 1 203 ? 6.279  -9.325  53.844  1.00 25.26 ? 197 LYS B C      1 
ATOM   4206 O O      . LYS B 1 203 ? 5.808  -9.907  52.858  1.00 25.23 ? 197 LYS B O      1 
ATOM   4207 C CB     . LYS B 1 203 ? 7.803  -7.659  52.753  1.00 23.42 ? 197 LYS B CB     1 
ATOM   4208 C CG     . LYS B 1 203 ? 9.132  -6.911  52.722  1.00 27.73 ? 197 LYS B CG     1 
ATOM   4209 C CD     . LYS B 1 203 ? 9.349  -6.019  53.911  1.00 28.14 ? 197 LYS B CD     1 
ATOM   4210 C CE     . LYS B 1 203 ? 10.715 -5.336  53.841  1.00 25.03 ? 197 LYS B CE     1 
ATOM   4211 N NZ     . LYS B 1 203 ? 10.843 -4.303  52.776  1.00 28.30 ? 197 LYS B NZ     1 
ATOM   4212 N N      . ASP B 1 204 ? 5.587  -9.117  54.973  1.00 23.88 ? 198 ASP B N      1 
ATOM   4213 C CA     . ASP B 1 204 ? 4.211  -9.593  55.098  1.00 25.45 ? 198 ASP B CA     1 
ATOM   4214 C C      . ASP B 1 204 ? 3.222  -8.850  54.205  1.00 28.60 ? 198 ASP B C      1 
ATOM   4215 O O      . ASP B 1 204 ? 2.104  -9.339  54.024  1.00 27.54 ? 198 ASP B O      1 
ATOM   4216 C CB     . ASP B 1 204 ? 3.738  -9.681  56.568  1.00 20.69 ? 198 ASP B CB     1 
ATOM   4217 C CG     . ASP B 1 204 ? 3.586  -8.318  57.247  1.00 29.01 ? 198 ASP B CG     1 
ATOM   4218 O OD1    . ASP B 1 204 ? 3.757  -7.258  56.619  1.00 28.52 ? 198 ASP B OD1    1 
ATOM   4219 O OD2    . ASP B 1 204 ? 3.309  -8.308  58.467  1.00 33.71 ? 198 ASP B OD2    1 
ATOM   4220 N N      . GLY B 1 205 ? 3.600  -7.708  53.626  1.00 25.26 ? 199 GLY B N      1 
ATOM   4221 C CA     . GLY B 1 205 ? 2.755  -7.113  52.599  1.00 24.81 ? 199 GLY B CA     1 
ATOM   4222 C C      . GLY B 1 205 ? 2.813  -7.802  51.251  1.00 29.60 ? 199 GLY B C      1 
ATOM   4223 O O      . GLY B 1 205 ? 2.015  -7.477  50.365  1.00 30.76 ? 199 GLY B O      1 
ATOM   4224 N N      . ILE B 1 206 ? 3.744  -8.739  51.075  1.00 25.53 ? 200 ILE B N      1 
ATOM   4225 C CA     . ILE B 1 206 ? 3.888  -9.506  49.844  1.00 22.88 ? 200 ILE B CA     1 
ATOM   4226 C C      . ILE B 1 206 ? 3.621  -10.985 50.077  1.00 25.70 ? 200 ILE B C      1 
ATOM   4227 O O      . ILE B 1 206 ? 2.888  -11.627 49.314  1.00 27.91 ? 200 ILE B O      1 
ATOM   4228 C CB     . ILE B 1 206 ? 5.277  -9.302  49.201  1.00 22.38 ? 200 ILE B CB     1 
ATOM   4229 C CG1    . ILE B 1 206 ? 5.575  -7.817  48.995  1.00 24.97 ? 200 ILE B CG1    1 
ATOM   4230 C CG2    . ILE B 1 206 ? 5.365  -10.084 47.883  1.00 23.11 ? 200 ILE B CG2    1 
ATOM   4231 C CD1    . ILE B 1 206 ? 6.910  -7.552  48.338  1.00 22.86 ? 200 ILE B CD1    1 
ATOM   4232 N N      . ASN B 1 207 ? 4.204  -11.543 51.132  1.00 25.31 ? 201 ASN B N      1 
ATOM   4233 C CA     . ASN B 1 207 ? 4.191  -12.983 51.359  1.00 24.09 ? 201 ASN B CA     1 
ATOM   4234 C C      . ASN B 1 207 ? 2.833  -13.353 51.934  1.00 27.69 ? 201 ASN B C      1 
ATOM   4235 O O      . ASN B 1 207 ? 2.561  -13.125 53.115  1.00 26.53 ? 201 ASN B O      1 
ATOM   4236 C CB     . ASN B 1 207 ? 5.331  -13.367 52.294  1.00 23.30 ? 201 ASN B CB     1 
ATOM   4237 C CG     . ASN B 1 207 ? 5.447  -14.862 52.506  1.00 24.75 ? 201 ASN B CG     1 
ATOM   4238 O OD1    . ASN B 1 207 ? 4.492  -15.611 52.319  1.00 25.72 ? 201 ASN B OD1    1 
ATOM   4239 N ND2    . ASN B 1 207 ? 6.622  -15.302 52.925  1.00 23.32 ? 201 ASN B ND2    1 
ATOM   4240 N N      . ASP B 1 208 ? 1.979  -13.934 51.090  1.00 26.84 ? 202 ASP B N      1 
ATOM   4241 C CA     . ASP B 1 208 ? 0.657  -14.399 51.484  1.00 32.61 ? 202 ASP B CA     1 
ATOM   4242 C C      . ASP B 1 208 ? 0.597  -15.922 51.536  1.00 33.02 ? 202 ASP B C      1 
ATOM   4243 O O      . ASP B 1 208 ? -0.483 -16.506 51.414  1.00 33.67 ? 202 ASP B O      1 
ATOM   4244 C CB     . ASP B 1 208 ? -0.409 -13.823 50.543  1.00 28.21 ? 202 ASP B CB     1 
ATOM   4245 C CG     . ASP B 1 208 ? -0.228 -14.272 49.092  1.00 37.37 ? 202 ASP B CG     1 
ATOM   4246 O OD1    . ASP B 1 208 ? 0.882  -14.690 48.718  1.00 33.22 ? 202 ASP B OD1    1 
ATOM   4247 O OD2    . ASP B 1 208 ? -1.217 -14.257 48.324  1.00 35.92 ? 202 ASP B OD2    1 
ATOM   4248 N N      . ARG B 1 209 ? 1.744  -16.575 51.708  1.00 29.78 ? 203 ARG B N      1 
ATOM   4249 C CA     . ARG B 1 209 ? 1.790  -18.029 51.686  1.00 27.63 ? 203 ARG B CA     1 
ATOM   4250 C C      . ARG B 1 209 ? 1.204  -18.606 52.964  1.00 31.11 ? 203 ARG B C      1 
ATOM   4251 O O      . ARG B 1 209 ? 1.286  -18.009 54.040  1.00 28.70 ? 203 ARG B O      1 
ATOM   4252 C CB     . ARG B 1 209 ? 3.227  -18.512 51.568  1.00 25.74 ? 203 ARG B CB     1 
ATOM   4253 C CG     . ARG B 1 209 ? 3.917  -18.092 50.283  1.00 23.11 ? 203 ARG B CG     1 
ATOM   4254 C CD     . ARG B 1 209 ? 5.359  -18.495 50.349  1.00 24.17 ? 203 ARG B CD     1 
ATOM   4255 N NE     . ARG B 1 209 ? 5.539  -19.917 50.099  1.00 24.14 ? 203 ARG B NE     1 
ATOM   4256 C CZ     . ARG B 1 209 ? 5.759  -20.419 48.891  1.00 25.32 ? 203 ARG B CZ     1 
ATOM   4257 N NH1    . ARG B 1 209 ? 5.767  -19.645 47.814  1.00 23.68 ? 203 ARG B NH1    1 
ATOM   4258 N NH2    . ARG B 1 209 ? 5.978  -21.725 48.759  1.00 24.17 ? 203 ARG B NH2    1 
ATOM   4259 N N      . THR B 1 210 ? 0.630  -19.800 52.840  1.00 36.15 ? 204 THR B N      1 
ATOM   4260 C CA     . THR B 1 210 ? 0.125  -20.535 53.991  1.00 36.51 ? 204 THR B CA     1 
ATOM   4261 C C      . THR B 1 210 ? 0.940  -21.787 54.286  1.00 40.49 ? 204 THR B C      1 
ATOM   4262 O O      . THR B 1 210 ? 0.528  -22.598 55.122  1.00 38.42 ? 204 THR B O      1 
ATOM   4263 C CB     . THR B 1 210 ? -1.346 -20.899 53.793  1.00 39.90 ? 204 THR B CB     1 
ATOM   4264 O OG1    . THR B 1 210 ? -1.493 -21.619 52.563  1.00 40.70 ? 204 THR B OG1    1 
ATOM   4265 C CG2    . THR B 1 210 ? -2.198 -19.640 53.758  1.00 44.70 ? 204 THR B CG2    1 
ATOM   4266 N N      . ASP B 1 211 ? 2.072  -21.968 53.615  1.00 28.93 ? 205 ASP B N      1 
ATOM   4267 C CA     . ASP B 1 211 ? 2.949  -23.098 53.884  1.00 30.55 ? 205 ASP B CA     1 
ATOM   4268 C C      . ASP B 1 211 ? 4.025  -22.688 54.894  1.00 26.32 ? 205 ASP B C      1 
ATOM   4269 O O      . ASP B 1 211 ? 3.911  -21.655 55.562  1.00 33.39 ? 205 ASP B O      1 
ATOM   4270 C CB     . ASP B 1 211 ? 3.467  -23.707 52.572  1.00 28.60 ? 205 ASP B CB     1 
ATOM   4271 C CG     . ASP B 1 211 ? 4.525  -22.845 51.878  1.00 33.23 ? 205 ASP B CG     1 
ATOM   4272 O OD1    . ASP B 1 211 ? 4.783  -21.699 52.307  1.00 26.10 ? 205 ASP B OD1    1 
ATOM   4273 O OD2    . ASP B 1 211 ? 5.103  -23.324 50.876  1.00 28.72 ? 205 ASP B OD2    1 
ATOM   4274 N N      . GLU B 1 212 ? 5.086  -23.487 55.008  1.00 25.58 ? 206 GLU B N      1 
ATOM   4275 C CA     . GLU B 1 212 ? 6.124  -23.242 56.001  1.00 28.13 ? 206 GLU B CA     1 
ATOM   4276 C C      . GLU B 1 212 ? 7.029  -22.069 55.653  1.00 29.05 ? 206 GLU B C      1 
ATOM   4277 O O      . GLU B 1 212 ? 7.943  -21.776 56.431  1.00 28.43 ? 206 GLU B O      1 
ATOM   4278 C CB     . GLU B 1 212 ? 6.922  -24.527 56.250  1.00 30.72 ? 206 GLU B CB     1 
ATOM   4279 C CG     . GLU B 1 212 ? 7.907  -24.863 55.146  1.00 32.00 ? 206 GLU B CG     1 
ATOM   4280 C CD     . GLU B 1 212 ? 7.323  -25.878 54.166  1.00 38.77 ? 206 GLU B CD     1 
ATOM   4281 O OE1    . GLU B 1 212 ? 6.086  -25.858 53.966  1.00 37.29 ? 206 GLU B OE1    1 
ATOM   4282 O OE2    . GLU B 1 212 ? 8.091  -26.686 53.597  1.00 39.07 ? 206 GLU B OE2    1 
ATOM   4283 N N      . TYR B 1 213 ? 6.807  -21.397 54.519  1.00 26.32 ? 207 TYR B N      1 
ATOM   4284 C CA     . TYR B 1 213 ? 7.576  -20.215 54.149  1.00 27.03 ? 207 TYR B CA     1 
ATOM   4285 C C      . TYR B 1 213 ? 6.788  -18.925 54.333  1.00 26.70 ? 207 TYR B C      1 
ATOM   4286 O O      . TYR B 1 213 ? 7.250  -17.860 53.902  1.00 27.47 ? 207 TYR B O      1 
ATOM   4287 C CB     . TYR B 1 213 ? 8.090  -20.328 52.706  1.00 23.41 ? 207 TYR B CB     1 
ATOM   4288 C CG     . TYR B 1 213 ? 9.263  -21.268 52.565  1.00 22.92 ? 207 TYR B CG     1 
ATOM   4289 C CD1    . TYR B 1 213 ? 9.061  -22.638 52.421  1.00 25.05 ? 207 TYR B CD1    1 
ATOM   4290 C CD2    . TYR B 1 213 ? 10.574 -20.795 52.583  1.00 22.28 ? 207 TYR B CD2    1 
ATOM   4291 C CE1    . TYR B 1 213 ? 10.120 -23.508 52.297  1.00 26.36 ? 207 TYR B CE1    1 
ATOM   4292 C CE2    . TYR B 1 213 ? 11.644 -21.659 52.456  1.00 25.21 ? 207 TYR B CE2    1 
ATOM   4293 C CZ     . TYR B 1 213 ? 11.410 -23.016 52.313  1.00 27.29 ? 207 TYR B CZ     1 
ATOM   4294 O OH     . TYR B 1 213 ? 12.465 -23.887 52.194  1.00 30.57 ? 207 TYR B OH     1 
ATOM   4295 N N      . GLY B 1 214 ? 5.604  -18.994 54.957  1.00 30.20 ? 208 GLY B N      1 
ATOM   4296 C CA     . GLY B 1 214 ? 4.767  -17.826 55.123  1.00 25.72 ? 208 GLY B CA     1 
ATOM   4297 C C      . GLY B 1 214 ? 4.144  -17.788 56.506  1.00 27.69 ? 208 GLY B C      1 
ATOM   4298 O O      . GLY B 1 214 ? 4.174  -18.767 57.254  1.00 28.51 ? 208 GLY B O      1 
ATOM   4299 N N      . GLY B 1 215 ? 3.569  -16.633 56.825  1.00 25.43 ? 209 GLY B N      1 
ATOM   4300 C CA     . GLY B 1 215 ? 2.934  -16.417 58.111  1.00 25.54 ? 209 GLY B CA     1 
ATOM   4301 C C      . GLY B 1 215 ? 3.859  -15.806 59.145  1.00 30.41 ? 209 GLY B C      1 
ATOM   4302 O O      . GLY B 1 215 ? 4.125  -14.598 59.124  1.00 26.95 ? 209 GLY B O      1 
ATOM   4303 N N      . SER B 1 216 ? 4.378  -16.647 60.035  1.00 24.55 ? 210 SER B N      1 
ATOM   4304 C CA     . SER B 1 216 ? 5.181  -16.178 61.156  1.00 25.79 ? 210 SER B CA     1 
ATOM   4305 C C      . SER B 1 216 ? 6.487  -15.552 60.673  1.00 25.95 ? 210 SER B C      1 
ATOM   4306 O O      . SER B 1 216 ? 6.947  -15.786 59.548  1.00 24.83 ? 210 SER B O      1 
ATOM   4307 C CB     . SER B 1 216 ? 5.527  -17.353 62.069  1.00 27.49 ? 210 SER B CB     1 
ATOM   4308 O OG     . SER B 1 216 ? 6.366  -18.275 61.378  1.00 27.83 ? 210 SER B OG     1 
ATOM   4309 N N      . LEU B 1 217 ? 7.086  -14.739 61.551  1.00 25.89 ? 211 LEU B N      1 
ATOM   4310 C CA     . LEU B 1 217 ? 8.411  -14.186 61.289  1.00 22.29 ? 211 LEU B CA     1 
ATOM   4311 C C      . LEU B 1 217 ? 9.416  -15.288 60.981  1.00 26.94 ? 211 LEU B C      1 
ATOM   4312 O O      . LEU B 1 217 ? 10.245 -15.148 60.069  1.00 23.86 ? 211 LEU B O      1 
ATOM   4313 C CB     . LEU B 1 217 ? 8.871  -13.373 62.505  1.00 24.74 ? 211 LEU B CB     1 
ATOM   4314 C CG     . LEU B 1 217 ? 8.238  -11.995 62.702  1.00 24.47 ? 211 LEU B CG     1 
ATOM   4315 C CD1    . LEU B 1 217 ? 8.598  -11.506 64.091  1.00 25.10 ? 211 LEU B CD1    1 
ATOM   4316 C CD2    . LEU B 1 217 ? 8.736  -11.000 61.663  1.00 28.07 ? 211 LEU B CD2    1 
ATOM   4317 N N      . ALA B 1 218 ? 9.343  -16.405 61.708  1.00 22.40 ? 212 ALA B N      1 
ATOM   4318 C CA     . ALA B 1 218 ? 10.281 -17.500 61.483  1.00 21.84 ? 212 ALA B CA     1 
ATOM   4319 C C      . ALA B 1 218 ? 10.116 -18.085 60.086  1.00 25.82 ? 212 ALA B C      1 
ATOM   4320 O O      . ALA B 1 218 ? 11.107 -18.388 59.406  1.00 25.39 ? 212 ALA B O      1 
ATOM   4321 C CB     . ALA B 1 218 ? 10.086 -18.587 62.541  1.00 29.74 ? 212 ALA B CB     1 
ATOM   4322 N N      . ASN B 1 219 ? 8.868  -18.261 59.652  1.00 26.38 ? 213 ASN B N      1 
ATOM   4323 C CA     . ASN B 1 219 ? 8.620  -18.803 58.321  1.00 23.09 ? 213 ASN B CA     1 
ATOM   4324 C C      . ASN B 1 219 ? 9.035  -17.815 57.241  1.00 26.11 ? 213 ASN B C      1 
ATOM   4325 O O      . ASN B 1 219 ? 9.614  -18.211 56.224  1.00 24.96 ? 213 ASN B O      1 
ATOM   4326 C CB     . ASN B 1 219 ? 7.145  -19.170 58.174  1.00 23.35 ? 213 ASN B CB     1 
ATOM   4327 C CG     . ASN B 1 219 ? 6.778  -20.431 58.945  1.00 29.43 ? 213 ASN B CG     1 
ATOM   4328 O OD1    . ASN B 1 219 ? 7.621  -21.022 59.620  1.00 29.29 ? 213 ASN B OD1    1 
ATOM   4329 N ND2    . ASN B 1 219 ? 5.520  -20.851 58.837  1.00 26.34 ? 213 ASN B ND2    1 
ATOM   4330 N N      . ARG B 1 220 ? 8.750  -16.524 57.442  1.00 22.39 ? 214 ARG B N      1 
ATOM   4331 C CA     . ARG B 1 220 ? 9.108  -15.536 56.429  1.00 23.04 ? 214 ARG B CA     1 
ATOM   4332 C C      . ARG B 1 220 ? 10.612 -15.349 56.314  1.00 23.28 ? 214 ARG B C      1 
ATOM   4333 O O      . ARG B 1 220 ? 11.100 -14.951 55.245  1.00 23.57 ? 214 ARG B O      1 
ATOM   4334 C CB     . ARG B 1 220 ? 8.390  -14.211 56.696  1.00 21.57 ? 214 ARG B CB     1 
ATOM   4335 C CG     . ARG B 1 220 ? 6.876  -14.359 56.536  1.00 23.67 ? 214 ARG B CG     1 
ATOM   4336 C CD     . ARG B 1 220 ? 6.110  -13.061 56.412  1.00 29.03 ? 214 ARG B CD     1 
ATOM   4337 N NE     . ARG B 1 220 ? 6.827  -11.881 56.871  1.00 35.66 ? 214 ARG B NE     1 
ATOM   4338 C CZ     . ARG B 1 220 ? 6.625  -11.285 58.038  1.00 25.46 ? 214 ARG B CZ     1 
ATOM   4339 N NH1    . ARG B 1 220 ? 5.804  -11.792 58.943  1.00 44.72 ? 214 ARG B NH1    1 
ATOM   4340 N NH2    . ARG B 1 220 ? 7.266  -10.154 58.304  1.00 38.99 ? 214 ARG B NH2    1 
ATOM   4341 N N      . CYS B 1 221 ? 11.353 -15.668 57.368  1.00 23.25 ? 215 CYS B N      1 
ATOM   4342 C CA     . CYS B 1 221 ? 12.799 -15.546 57.386  1.00 24.67 ? 215 CYS B CA     1 
ATOM   4343 C C      . CYS B 1 221 ? 13.482 -16.803 56.872  1.00 23.96 ? 215 CYS B C      1 
ATOM   4344 O O      . CYS B 1 221 ? 14.709 -16.820 56.739  1.00 24.25 ? 215 CYS B O      1 
ATOM   4345 C CB     . CYS B 1 221 ? 13.248 -15.281 58.829  1.00 22.83 ? 215 CYS B CB     1 
ATOM   4346 S SG     . CYS B 1 221 ? 13.049 -13.555 59.316  1.00 27.08 ? 215 CYS B SG     1 
ATOM   4347 N N      . LYS B 1 222 ? 12.713 -17.855 56.589  1.00 22.48 ? 216 LYS B N      1 
ATOM   4348 C CA     . LYS B 1 222 ? 13.302 -19.138 56.228  1.00 24.50 ? 216 LYS B CA     1 
ATOM   4349 C C      . LYS B 1 222 ? 14.066 -19.047 54.909  1.00 22.08 ? 216 LYS B C      1 
ATOM   4350 O O      . LYS B 1 222 ? 15.165 -19.599 54.785  1.00 24.41 ? 216 LYS B O      1 
ATOM   4351 C CB     . LYS B 1 222 ? 12.191 -20.183 56.131  1.00 26.18 ? 216 LYS B CB     1 
ATOM   4352 C CG     . LYS B 1 222 ? 12.636 -21.594 55.820  1.00 31.34 ? 216 LYS B CG     1 
ATOM   4353 C CD     . LYS B 1 222 ? 11.524 -22.587 56.175  1.00 37.34 ? 216 LYS B CD     1 
ATOM   4354 C CE     . LYS B 1 222 ? 11.098 -22.418 57.635  1.00 39.75 ? 216 LYS B CE     1 
ATOM   4355 N NZ     . LYS B 1 222 ? 9.889  -23.208 58.069  1.00 40.66 ? 216 LYS B NZ     1 
ATOM   4356 N N      . PHE B 1 223 ? 13.505 -18.353 53.914  1.00 24.01 ? 217 PHE B N      1 
ATOM   4357 C CA     . PHE B 1 223 ? 14.167 -18.288 52.614  1.00 21.86 ? 217 PHE B CA     1 
ATOM   4358 C C      . PHE B 1 223 ? 15.526 -17.609 52.715  1.00 19.76 ? 217 PHE B C      1 
ATOM   4359 O O      . PHE B 1 223 ? 16.531 -18.146 52.235  1.00 23.78 ? 217 PHE B O      1 
ATOM   4360 C CB     . PHE B 1 223 ? 13.273 -17.593 51.583  1.00 20.06 ? 217 PHE B CB     1 
ATOM   4361 C CG     . PHE B 1 223 ? 13.842 -17.621 50.180  1.00 22.24 ? 217 PHE B CG     1 
ATOM   4362 C CD1    . PHE B 1 223 ? 14.189 -18.825 49.594  1.00 25.40 ? 217 PHE B CD1    1 
ATOM   4363 C CD2    . PHE B 1 223 ? 14.047 -16.448 49.475  1.00 23.66 ? 217 PHE B CD2    1 
ATOM   4364 C CE1    . PHE B 1 223 ? 14.724 -18.863 48.298  1.00 27.79 ? 217 PHE B CE1    1 
ATOM   4365 C CE2    . PHE B 1 223 ? 14.575 -16.476 48.182  1.00 22.45 ? 217 PHE B CE2    1 
ATOM   4366 C CZ     . PHE B 1 223 ? 14.916 -17.686 47.602  1.00 24.32 ? 217 PHE B CZ     1 
ATOM   4367 N N      . ILE B 1 224 ? 15.582 -16.421 53.329  1.00 22.12 ? 218 ILE B N      1 
ATOM   4368 C CA     . ILE B 1 224 ? 16.868 -15.732 53.452  1.00 22.70 ? 218 ILE B CA     1 
ATOM   4369 C C      . ILE B 1 224 ? 17.858 -16.554 54.265  1.00 25.04 ? 218 ILE B C      1 
ATOM   4370 O O      . ILE B 1 224 ? 19.049 -16.598 53.942  1.00 21.73 ? 218 ILE B O      1 
ATOM   4371 C CB     . ILE B 1 224 ? 16.727 -14.281 53.960  1.00 18.25 ? 218 ILE B CB     1 
ATOM   4372 C CG1    . ILE B 1 224 ? 18.046 -13.526 53.739  1.00 22.22 ? 218 ILE B CG1    1 
ATOM   4373 C CG2    . ILE B 1 224 ? 16.290 -14.236 55.435  1.00 23.01 ? 218 ILE B CG2    1 
ATOM   4374 C CD1    . ILE B 1 224 ? 17.980 -12.026 54.023  1.00 22.94 ? 218 ILE B CD1    1 
ATOM   4375 N N      . THR B 1 225 ? 17.385 -17.228 55.321  1.00 24.12 ? 219 THR B N      1 
ATOM   4376 C CA     . THR B 1 225 ? 18.273 -18.070 56.124  1.00 23.99 ? 219 THR B CA     1 
ATOM   4377 C C      . THR B 1 225 ? 18.869 -19.193 55.280  1.00 22.70 ? 219 THR B C      1 
ATOM   4378 O O      . THR B 1 225 ? 20.081 -19.457 55.330  1.00 24.81 ? 219 THR B O      1 
ATOM   4379 C CB     . THR B 1 225 ? 17.503 -18.636 57.320  1.00 28.05 ? 219 THR B CB     1 
ATOM   4380 O OG1    . THR B 1 225 ? 16.992 -17.558 58.115  1.00 27.73 ? 219 THR B OG1    1 
ATOM   4381 C CG2    . THR B 1 225 ? 18.413 -19.495 58.188  1.00 26.93 ? 219 THR B CG2    1 
ATOM   4382 N N      . GLN B 1 226 ? 18.027 -19.856 54.480  1.00 22.85 ? 220 GLN B N      1 
ATOM   4383 C CA     . GLN B 1 226 ? 18.509 -20.936 53.622  1.00 24.05 ? 220 GLN B CA     1 
ATOM   4384 C C      . GLN B 1 226 ? 19.467 -20.424 52.552  1.00 25.74 ? 220 GLN B C      1 
ATOM   4385 O O      . GLN B 1 226 ? 20.465 -21.085 52.238  1.00 24.38 ? 220 GLN B O      1 
ATOM   4386 C CB     . GLN B 1 226 ? 17.328 -21.688 53.009  1.00 25.54 ? 220 GLN B CB     1 
ATOM   4387 C CG     . GLN B 1 226 ? 16.693 -22.673 53.981  1.00 31.29 ? 220 GLN B CG     1 
ATOM   4388 C CD     . GLN B 1 226 ? 15.313 -23.127 53.552  1.00 34.45 ? 220 GLN B CD     1 
ATOM   4389 O OE1    . GLN B 1 226 ? 14.882 -22.870 52.431  1.00 31.72 ? 220 GLN B OE1    1 
ATOM   4390 N NE2    . GLN B 1 226 ? 14.612 -23.813 54.449  1.00 45.29 ? 220 GLN B NE2    1 
ATOM   4391 N N      . VAL B 1 227 ? 19.192 -19.249 51.986  1.00 22.76 ? 221 VAL B N      1 
ATOM   4392 C CA     . VAL B 1 227 ? 20.108 -18.682 51.000  1.00 24.69 ? 221 VAL B CA     1 
ATOM   4393 C C      . VAL B 1 227 ? 21.464 -18.404 51.637  1.00 23.49 ? 221 VAL B C      1 
ATOM   4394 O O      . VAL B 1 227 ? 22.515 -18.803 51.116  1.00 22.72 ? 221 VAL B O      1 
ATOM   4395 C CB     . VAL B 1 227 ? 19.503 -17.418 50.362  1.00 22.91 ? 221 VAL B CB     1 
ATOM   4396 C CG1    . VAL B 1 227 ? 20.569 -16.685 49.534  1.00 25.04 ? 221 VAL B CG1    1 
ATOM   4397 C CG2    . VAL B 1 227 ? 18.302 -17.781 49.492  1.00 22.70 ? 221 VAL B CG2    1 
ATOM   4398 N N      . VAL B 1 228 ? 21.458 -17.721 52.784  1.00 22.90 ? 222 VAL B N      1 
ATOM   4399 C CA     . VAL B 1 228 ? 22.711 -17.359 53.440  1.00 20.68 ? 222 VAL B CA     1 
ATOM   4400 C C      . VAL B 1 228 ? 23.473 -18.603 53.879  1.00 23.11 ? 222 VAL B C      1 
ATOM   4401 O O      . VAL B 1 228 ? 24.691 -18.693 53.697  1.00 23.70 ? 222 VAL B O      1 
ATOM   4402 C CB     . VAL B 1 228 ? 22.449 -16.392 54.611  1.00 24.43 ? 222 VAL B CB     1 
ATOM   4403 C CG1    . VAL B 1 228 ? 23.732 -16.174 55.408  1.00 22.85 ? 222 VAL B CG1    1 
ATOM   4404 C CG2    . VAL B 1 228 ? 21.917 -15.071 54.094  1.00 23.76 ? 222 VAL B CG2    1 
ATOM   4405 N N      . GLN B 1 229 ? 22.774 -19.580 54.465  1.00 25.71 ? 223 GLN B N      1 
ATOM   4406 C CA     . GLN B 1 229 ? 23.432 -20.816 54.881  1.00 27.23 ? 223 GLN B CA     1 
ATOM   4407 C C      . GLN B 1 229 ? 24.073 -21.535 53.700  1.00 27.59 ? 223 GLN B C      1 
ATOM   4408 O O      . GLN B 1 229 ? 25.182 -22.071 53.817  1.00 28.93 ? 223 GLN B O      1 
ATOM   4409 C CB     . GLN B 1 229 ? 22.426 -21.736 55.563  1.00 29.60 ? 223 GLN B CB     1 
ATOM   4410 C CG     . GLN B 1 229 ? 23.050 -22.960 56.218  1.00 38.70 ? 223 GLN B CG     1 
ATOM   4411 C CD     . GLN B 1 229 ? 24.218 -22.613 57.130  1.00 40.12 ? 223 GLN B CD     1 
ATOM   4412 O OE1    . GLN B 1 229 ? 24.021 -22.199 58.274  1.00 46.48 ? 223 GLN B OE1    1 
ATOM   4413 N NE2    . GLN B 1 229 ? 25.444 -22.820 56.639  1.00 35.85 ? 223 GLN B NE2    1 
ATOM   4414 N N      . ALA B 1 230 ? 23.382 -21.574 52.560  1.00 26.33 ? 224 ALA B N      1 
ATOM   4415 C CA     . ALA B 1 230 ? 23.923 -22.263 51.393  1.00 26.77 ? 224 ALA B CA     1 
ATOM   4416 C C      . ALA B 1 230 ? 25.219 -21.617 50.925  1.00 28.85 ? 224 ALA B C      1 
ATOM   4417 O O      . ALA B 1 230 ? 26.208 -22.309 50.663  1.00 28.00 ? 224 ALA B O      1 
ATOM   4418 C CB     . ALA B 1 230 ? 22.882 -22.284 50.273  1.00 24.97 ? 224 ALA B CB     1 
ATOM   4419 N N      . VAL B 1 231 ? 25.238 -20.286 50.821  1.00 23.57 ? 225 VAL B N      1 
ATOM   4420 C CA     . VAL B 1 231 ? 26.452 -19.617 50.370  1.00 23.53 ? 225 VAL B CA     1 
ATOM   4421 C C      . VAL B 1 231 ? 27.551 -19.689 51.427  1.00 26.07 ? 225 VAL B C      1 
ATOM   4422 O O      . VAL B 1 231 ? 28.725 -19.849 51.086  1.00 27.50 ? 225 VAL B O      1 
ATOM   4423 C CB     . VAL B 1 231 ? 26.175 -18.190 49.850  1.00 25.65 ? 225 VAL B CB     1 
ATOM   4424 C CG1    . VAL B 1 231 ? 25.245 -18.250 48.636  1.00 25.07 ? 225 VAL B CG1    1 
ATOM   4425 C CG2    . VAL B 1 231 ? 25.589 -17.301 50.939  1.00 24.89 ? 225 VAL B CG2    1 
ATOM   4426 N N      . VAL B 1 232 ? 27.194 -19.607 52.713  1.00 26.74 ? 226 VAL B N      1 
ATOM   4427 C CA     . VAL B 1 232 ? 28.195 -19.734 53.774  1.00 27.56 ? 226 VAL B CA     1 
ATOM   4428 C C      . VAL B 1 232 ? 28.861 -21.104 53.725  1.00 26.01 ? 226 VAL B C      1 
ATOM   4429 O O      . VAL B 1 232 ? 30.084 -21.224 53.863  1.00 27.86 ? 226 VAL B O      1 
ATOM   4430 C CB     . VAL B 1 232 ? 27.559 -19.459 55.150  1.00 26.51 ? 226 VAL B CB     1 
ATOM   4431 C CG1    . VAL B 1 232 ? 28.467 -19.976 56.279  1.00 26.66 ? 226 VAL B CG1    1 
ATOM   4432 C CG2    . VAL B 1 232 ? 27.260 -17.967 55.319  1.00 26.88 ? 226 VAL B CG2    1 
ATOM   4433 N N      . SER B 1 233 ? 28.067 -22.160 53.533  1.00 27.36 ? 227 SER B N      1 
ATOM   4434 C CA     . SER B 1 233 ? 28.636 -23.500 53.450  1.00 30.04 ? 227 SER B CA     1 
ATOM   4435 C C      . SER B 1 233 ? 29.514 -23.667 52.222  1.00 30.57 ? 227 SER B C      1 
ATOM   4436 O O      . SER B 1 233 ? 30.469 -24.452 52.247  1.00 36.01 ? 227 SER B O      1 
ATOM   4437 C CB     . SER B 1 233 ? 27.527 -24.551 53.459  1.00 30.23 ? 227 SER B CB     1 
ATOM   4438 O OG     . SER B 1 233 ? 26.751 -24.456 54.644  1.00 44.27 ? 227 SER B OG     1 
ATOM   4439 N N      . ALA B 1 234 ? 29.215 -22.938 51.144  1.00 29.36 ? 228 ALA B N      1 
ATOM   4440 C CA     . ALA B 1 234 ? 29.955 -23.106 49.899  1.00 26.05 ? 228 ALA B CA     1 
ATOM   4441 C C      . ALA B 1 234 ? 31.284 -22.356 49.905  1.00 30.51 ? 228 ALA B C      1 
ATOM   4442 O O      . ALA B 1 234 ? 32.291 -22.876 49.408  1.00 32.11 ? 228 ALA B O      1 
ATOM   4443 C CB     . ALA B 1 234 ? 29.096 -22.654 48.716  1.00 27.09 ? 228 ALA B CB     1 
ATOM   4444 N N      . ILE B 1 235 ? 31.313 -21.131 50.431  1.00 25.01 ? 229 ILE B N      1 
ATOM   4445 C CA     . ILE B 1 235 ? 32.492 -20.284 50.263  1.00 24.48 ? 229 ILE B CA     1 
ATOM   4446 C C      . ILE B 1 235 ? 33.048 -19.749 51.578  1.00 27.59 ? 229 ILE B C      1 
ATOM   4447 O O      . ILE B 1 235 ? 34.109 -19.110 51.598  1.00 27.69 ? 229 ILE B O      1 
ATOM   4448 C CB     . ILE B 1 235 ? 32.253 -19.150 49.239  1.00 25.53 ? 229 ILE B CB     1 
ATOM   4449 C CG1    . ILE B 1 235 ? 31.277 -18.102 49.782  1.00 25.90 ? 229 ILE B CG1    1 
ATOM   4450 C CG2    . ILE B 1 235 ? 31.763 -19.711 47.891  1.00 26.89 ? 229 ILE B CG2    1 
ATOM   4451 C CD1    . ILE B 1 235 ? 31.300 -16.799 48.994  1.00 26.60 ? 229 ILE B CD1    1 
ATOM   4452 N N      . GLY B 1 236 ? 32.354 -20.007 52.684  1.00 26.45 ? 230 GLY B N      1 
ATOM   4453 C CA     . GLY B 1 236 ? 32.810 -19.519 53.972  1.00 29.49 ? 230 GLY B CA     1 
ATOM   4454 C C      . GLY B 1 236 ? 32.118 -18.240 54.401  1.00 27.42 ? 230 GLY B C      1 
ATOM   4455 O O      . GLY B 1 236 ? 31.904 -17.337 53.586  1.00 27.66 ? 230 GLY B O      1 
ATOM   4456 N N      . ALA B 1 237 ? 31.771 -18.149 55.686  1.00 25.47 ? 231 ALA B N      1 
ATOM   4457 C CA     . ALA B 1 237 ? 30.994 -17.010 56.164  1.00 24.49 ? 231 ALA B CA     1 
ATOM   4458 C C      . ALA B 1 237 ? 31.726 -15.693 55.960  1.00 24.12 ? 231 ALA B C      1 
ATOM   4459 O O      . ALA B 1 237 ? 31.089 -14.670 55.682  1.00 23.83 ? 231 ALA B O      1 
ATOM   4460 C CB     . ALA B 1 237 ? 30.639 -17.190 57.646  1.00 27.75 ? 231 ALA B CB     1 
ATOM   4461 N N      . ASP B 1 238 ? 33.055 -15.692 56.091  1.00 23.82 ? 232 ASP B N      1 
ATOM   4462 C CA     . ASP B 1 238 ? 33.822 -14.453 56.027  1.00 27.38 ? 232 ASP B CA     1 
ATOM   4463 C C      . ASP B 1 238 ? 33.798 -13.825 54.642  1.00 26.65 ? 232 ASP B C      1 
ATOM   4464 O O      . ASP B 1 238 ? 34.263 -12.691 54.482  1.00 26.97 ? 232 ASP B O      1 
ATOM   4465 C CB     . ASP B 1 238 ? 35.279 -14.727 56.391  1.00 31.86 ? 232 ASP B CB     1 
ATOM   4466 C CG     . ASP B 1 238 ? 35.783 -16.028 55.794  1.00 42.26 ? 232 ASP B CG     1 
ATOM   4467 O OD1    . ASP B 1 238 ? 35.224 -17.101 56.108  1.00 53.79 ? 232 ASP B OD1    1 
ATOM   4468 O OD2    . ASP B 1 238 ? 36.737 -15.976 54.998  1.00 59.13 ? 232 ASP B OD2    1 
ATOM   4469 N N      . ARG B 1 239 ? 33.290 -14.539 53.640  1.00 25.80 ? 233 ARG B N      1 
ATOM   4470 C CA     . ARG B 1 239 ? 33.200 -14.036 52.281  1.00 20.69 ? 233 ARG B CA     1 
ATOM   4471 C C      . ARG B 1 239 ? 31.762 -13.734 51.877  1.00 22.47 ? 233 ARG B C      1 
ATOM   4472 O O      . ARG B 1 239 ? 31.476 -13.603 50.680  1.00 22.34 ? 233 ARG B O      1 
ATOM   4473 C CB     . ARG B 1 239 ? 33.824 -15.043 51.317  1.00 23.33 ? 233 ARG B CB     1 
ATOM   4474 C CG     . ARG B 1 239 ? 35.308 -15.298 51.553  1.00 28.13 ? 233 ARG B CG     1 
ATOM   4475 C CD     . ARG B 1 239 ? 35.874 -16.214 50.464  1.00 29.56 ? 233 ARG B CD     1 
ATOM   4476 N NE     . ARG B 1 239 ? 37.288 -16.509 50.674  1.00 40.15 ? 233 ARG B NE     1 
ATOM   4477 C CZ     . ARG B 1 239 ? 38.289 -15.777 50.198  1.00 49.29 ? 233 ARG B CZ     1 
ATOM   4478 N NH1    . ARG B 1 239 ? 38.072 -14.665 49.508  1.00 35.11 ? 233 ARG B NH1    1 
ATOM   4479 N NH2    . ARG B 1 239 ? 39.543 -16.158 50.437  1.00 44.67 ? 233 ARG B NH2    1 
ATOM   4480 N N      . VAL B 1 240 ? 30.856 -13.619 52.851  1.00 22.65 ? 234 VAL B N      1 
ATOM   4481 C CA     . VAL B 1 240 ? 29.427 -13.457 52.590  1.00 23.51 ? 234 VAL B CA     1 
ATOM   4482 C C      . VAL B 1 240 ? 28.925 -12.221 53.322  1.00 22.45 ? 234 VAL B C      1 
ATOM   4483 O O      . VAL B 1 240 ? 28.959 -12.172 54.559  1.00 22.45 ? 234 VAL B O      1 
ATOM   4484 C CB     . VAL B 1 240 ? 28.608 -14.692 53.000  1.00 19.38 ? 234 VAL B CB     1 
ATOM   4485 C CG1    . VAL B 1 240 ? 27.109 -14.428 52.798  1.00 21.89 ? 234 VAL B CG1    1 
ATOM   4486 C CG2    . VAL B 1 240 ? 29.034 -15.907 52.204  1.00 23.95 ? 234 VAL B CG2    1 
ATOM   4487 N N      . GLY B 1 241 ? 28.446 -11.233 52.565  1.00 22.75 ? 235 GLY B N      1 
ATOM   4488 C CA     . GLY B 1 241 ? 27.707 -10.116 53.126  1.00 20.75 ? 235 GLY B CA     1 
ATOM   4489 C C      . GLY B 1 241 ? 26.223 -10.262 52.837  1.00 21.53 ? 235 GLY B C      1 
ATOM   4490 O O      . GLY B 1 241 ? 25.855 -10.987 51.911  1.00 19.77 ? 235 GLY B O      1 
ATOM   4491 N N      . VAL B 1 242 ? 25.363 -9.615  53.634  1.00 19.84 ? 236 VAL B N      1 
ATOM   4492 C CA     . VAL B 1 242 ? 23.910 -9.685  53.479  1.00 21.77 ? 236 VAL B CA     1 
ATOM   4493 C C      . VAL B 1 242 ? 23.348 -8.265  53.490  1.00 20.54 ? 236 VAL B C      1 
ATOM   4494 O O      . VAL B 1 242 ? 23.668 -7.475  54.382  1.00 20.59 ? 236 VAL B O      1 
ATOM   4495 C CB     . VAL B 1 242 ? 23.252 -10.530 54.593  1.00 22.91 ? 236 VAL B CB     1 
ATOM   4496 C CG1    . VAL B 1 242 ? 21.745 -10.667 54.343  1.00 21.85 ? 236 VAL B CG1    1 
ATOM   4497 C CG2    . VAL B 1 242 ? 23.904 -11.903 54.695  1.00 24.98 ? 236 VAL B CG2    1 
ATOM   4498 N N      . ARG B 1 243 ? 22.496 -7.940  52.512  1.00 21.50 ? 237 ARG B N      1 
ATOM   4499 C CA     . ARG B 1 243 ? 21.904 -6.608  52.414  1.00 18.09 ? 237 ARG B CA     1 
ATOM   4500 C C      . ARG B 1 243 ? 20.393 -6.695  52.540  1.00 19.80 ? 237 ARG B C      1 
ATOM   4501 O O      . ARG B 1 243 ? 19.755 -7.466  51.821  1.00 19.91 ? 237 ARG B O      1 
ATOM   4502 C CB     . ARG B 1 243 ? 22.240 -5.920  51.081  1.00 17.79 ? 237 ARG B CB     1 
ATOM   4503 C CG     . ARG B 1 243 ? 21.893 -4.419  51.102  1.00 20.72 ? 237 ARG B CG     1 
ATOM   4504 C CD     . ARG B 1 243 ? 22.338 -3.669  49.848  1.00 22.47 ? 237 ARG B CD     1 
ATOM   4505 N NE     . ARG B 1 243 ? 22.711 -2.291  50.163  1.00 22.62 ? 237 ARG B NE     1 
ATOM   4506 C CZ     . ARG B 1 243 ? 22.625 -1.278  49.310  1.00 24.20 ? 237 ARG B CZ     1 
ATOM   4507 N NH1    . ARG B 1 243 ? 22.069 -1.426  48.118  1.00 23.04 ? 237 ARG B NH1    1 
ATOM   4508 N NH2    . ARG B 1 243 ? 23.113 -0.090  49.656  1.00 22.22 ? 237 ARG B NH2    1 
ATOM   4509 N N      . VAL B 1 244 ? 19.817 -5.899  53.448  1.00 19.23 ? 238 VAL B N      1 
ATOM   4510 C CA     . VAL B 1 244 ? 18.369 -5.851  53.618  1.00 18.74 ? 238 VAL B CA     1 
ATOM   4511 C C      . VAL B 1 244 ? 17.915 -4.403  53.753  1.00 19.78 ? 238 VAL B C      1 
ATOM   4512 O O      . VAL B 1 244 ? 18.714 -3.489  53.959  1.00 20.47 ? 238 VAL B O      1 
ATOM   4513 C CB     . VAL B 1 244 ? 17.874 -6.666  54.835  1.00 22.17 ? 238 VAL B CB     1 
ATOM   4514 C CG1    . VAL B 1 244 ? 18.076 -8.158  54.614  1.00 22.65 ? 238 VAL B CG1    1 
ATOM   4515 C CG2    . VAL B 1 244 ? 18.560 -6.184  56.124  1.00 21.45 ? 238 VAL B CG2    1 
ATOM   4516 N N      . SER B 1 245 ? 16.597 -4.213  53.651  1.00 20.14 ? 239 SER B N      1 
ATOM   4517 C CA     . SER B 1 245 ? 15.987 -2.883  53.695  1.00 22.47 ? 239 SER B CA     1 
ATOM   4518 C C      . SER B 1 245 ? 14.585 -3.012  54.266  1.00 22.94 ? 239 SER B C      1 
ATOM   4519 O O      . SER B 1 245 ? 13.582 -2.849  53.563  1.00 22.94 ? 239 SER B O      1 
ATOM   4520 C CB     . SER B 1 245 ? 15.968 -2.245  52.306  1.00 24.23 ? 239 SER B CB     1 
ATOM   4521 O OG     . SER B 1 245 ? 15.138 -2.957  51.395  1.00 21.91 ? 239 SER B OG     1 
ATOM   4522 N N      . PRO B 1 246 ? 14.477 -3.301  55.564  1.00 21.18 ? 240 PRO B N      1 
ATOM   4523 C CA     . PRO B 1 246 ? 13.154 -3.536  56.162  1.00 20.91 ? 240 PRO B CA     1 
ATOM   4524 C C      . PRO B 1 246 ? 12.190 -2.367  56.017  1.00 21.11 ? 240 PRO B C      1 
ATOM   4525 O O      . PRO B 1 246 ? 10.976 -2.590  55.971  1.00 25.86 ? 240 PRO B O      1 
ATOM   4526 C CB     . PRO B 1 246 ? 13.463 -3.848  57.638  1.00 25.57 ? 240 PRO B CB     1 
ATOM   4527 C CG     . PRO B 1 246 ? 14.894 -3.470  57.861  1.00 24.53 ? 240 PRO B CG     1 
ATOM   4528 C CD     . PRO B 1 246 ? 15.586 -3.360  56.531  1.00 22.16 ? 240 PRO B CD     1 
ATOM   4529 N N      . ALA B 1 247 ? 12.682 -1.132  55.950  1.00 21.98 ? 241 ALA B N      1 
ATOM   4530 C CA     . ALA B 1 247 ? 11.823 0.042   55.961  1.00 28.96 ? 241 ALA B CA     1 
ATOM   4531 C C      . ALA B 1 247 ? 11.646 0.690   54.594  1.00 26.07 ? 241 ALA B C      1 
ATOM   4532 O O      . ALA B 1 247 ? 10.966 1.715   54.499  1.00 31.31 ? 241 ALA B O      1 
ATOM   4533 C CB     . ALA B 1 247 ? 12.333 1.075   56.969  1.00 31.82 ? 241 ALA B CB     1 
ATOM   4534 N N      . ILE B 1 248 ? 12.231 0.133   53.540  1.00 24.30 ? 242 ILE B N      1 
ATOM   4535 C CA     . ILE B 1 248 ? 12.018 0.646   52.190  1.00 24.30 ? 242 ILE B CA     1 
ATOM   4536 C C      . ILE B 1 248 ? 10.827 -0.086  51.583  1.00 27.16 ? 242 ILE B C      1 
ATOM   4537 O O      . ILE B 1 248 ? 10.789 -1.324  51.581  1.00 27.61 ? 242 ILE B O      1 
ATOM   4538 C CB     . ILE B 1 248 ? 13.280 0.471   51.326  1.00 22.59 ? 242 ILE B CB     1 
ATOM   4539 C CG1    . ILE B 1 248 ? 14.378 1.441   51.780  1.00 26.54 ? 242 ILE B CG1    1 
ATOM   4540 C CG2    . ILE B 1 248 ? 12.957 0.709   49.856  1.00 22.78 ? 242 ILE B CG2    1 
ATOM   4541 C CD1    . ILE B 1 248 ? 15.688 1.268   51.013  1.00 27.52 ? 242 ILE B CD1    1 
ATOM   4542 N N      . ASP B 1 249 ? 9.852  0.681   51.076  1.00 27.68 ? 243 ASP B N      1 
ATOM   4543 C CA     . ASP B 1 249 ? 8.574  0.179   50.572  1.00 30.93 ? 243 ASP B CA     1 
ATOM   4544 C C      . ASP B 1 249 ? 8.546  -0.006  49.056  1.00 33.63 ? 243 ASP B C      1 
ATOM   4545 O O      . ASP B 1 249 ? 7.466  -0.212  48.486  1.00 30.68 ? 243 ASP B O      1 
ATOM   4546 C CB     . ASP B 1 249 ? 7.441  1.133   50.969  1.00 33.60 ? 243 ASP B CB     1 
ATOM   4547 C CG     . ASP B 1 249 ? 7.224  1.196   52.461  1.00 54.20 ? 243 ASP B CG     1 
ATOM   4548 O OD1    . ASP B 1 249 ? 7.802  0.353   53.179  1.00 53.20 ? 243 ASP B OD1    1 
ATOM   4549 O OD2    . ASP B 1 249 ? 6.480  2.094   52.916  1.00 59.14 ? 243 ASP B OD2    1 
ATOM   4550 N N      . HIS B 1 250 ? 9.700  0.061   48.403  1.00 30.83 ? 244 HIS B N      1 
ATOM   4551 C CA     . HIS B 1 250 ? 9.804  -0.006  46.947  1.00 28.69 ? 244 HIS B CA     1 
ATOM   4552 C C      . HIS B 1 250 ? 9.114  -1.253  46.397  1.00 24.15 ? 244 HIS B C      1 
ATOM   4553 O O      . HIS B 1 250 ? 9.253  -2.350  46.941  1.00 26.49 ? 244 HIS B O      1 
ATOM   4554 C CB     . HIS B 1 250 ? 11.311 -0.018  46.626  1.00 24.93 ? 244 HIS B CB     1 
ATOM   4555 C CG     . HIS B 1 250 ? 11.661 -0.077  45.170  1.00 34.11 ? 244 HIS B CG     1 
ATOM   4556 N ND1    . HIS B 1 250 ? 11.156 0.825   44.253  1.00 35.29 ? 244 HIS B ND1    1 
ATOM   4557 C CD2    . HIS B 1 250 ? 12.404 -0.960  44.460  1.00 27.30 ? 244 HIS B CD2    1 
ATOM   4558 C CE1    . HIS B 1 250 ? 11.599 0.515   43.045  1.00 38.90 ? 244 HIS B CE1    1 
ATOM   4559 N NE2    . HIS B 1 250 ? 12.357 -0.562  43.144  1.00 31.15 ? 244 HIS B NE2    1 
ATOM   4560 N N      . LEU B 1 251 ? 8.369  -1.083  45.290  1.00 26.56 ? 245 LEU B N      1 
ATOM   4561 C CA     . LEU B 1 251 ? 7.719  -2.205  44.599  1.00 28.36 ? 245 LEU B CA     1 
ATOM   4562 C C      . LEU B 1 251 ? 6.724  -2.936  45.499  1.00 27.63 ? 245 LEU B C      1 
ATOM   4563 O O      . LEU B 1 251 ? 6.641  -4.168  45.491  1.00 26.21 ? 245 LEU B O      1 
ATOM   4564 C CB     . LEU B 1 251 ? 8.735  -3.183  43.999  1.00 24.86 ? 245 LEU B CB     1 
ATOM   4565 C CG     . LEU B 1 251 ? 9.818  -2.614  43.088  1.00 27.96 ? 245 LEU B CG     1 
ATOM   4566 C CD1    . LEU B 1 251 ? 10.785 -3.730  42.695  1.00 25.42 ? 245 LEU B CD1    1 
ATOM   4567 C CD2    . LEU B 1 251 ? 9.214  -1.951  41.856  1.00 28.76 ? 245 LEU B CD2    1 
ATOM   4568 N N      . ASP B 1 252 ? 5.980  -2.167  46.300  1.00 25.47 ? 246 ASP B N      1 
ATOM   4569 C CA     . ASP B 1 252 ? 4.931  -2.700  47.186  1.00 28.29 ? 246 ASP B CA     1 
ATOM   4570 C C      . ASP B 1 252 ? 5.486  -3.634  48.253  1.00 33.47 ? 246 ASP B C      1 
ATOM   4571 O O      . ASP B 1 252 ? 4.849  -4.620  48.630  1.00 44.10 ? 246 ASP B O      1 
ATOM   4572 C CB     . ASP B 1 252 ? 3.820  -3.393  46.399  1.00 37.34 ? 246 ASP B CB     1 
ATOM   4573 C CG     . ASP B 1 252 ? 3.005  -2.432  45.595  1.00 31.53 ? 246 ASP B CG     1 
ATOM   4574 O OD1    . ASP B 1 252 ? 3.035  -1.223  45.899  1.00 43.49 ? 246 ASP B OD1    1 
ATOM   4575 O OD2    . ASP B 1 252 ? 2.337  -2.890  44.656  1.00 42.25 ? 246 ASP B OD2    1 
ATOM   4576 N N      . ALA B 1 253 ? 6.670  -3.323  48.764  1.00 27.55 ? 247 ALA B N      1 
ATOM   4577 C CA     . ALA B 1 253 ? 7.336  -4.203  49.718  1.00 25.91 ? 247 ALA B CA     1 
ATOM   4578 C C      . ALA B 1 253 ? 7.239  -3.628  51.132  1.00 26.32 ? 247 ALA B C      1 
ATOM   4579 O O      . ALA B 1 253 ? 8.225  -3.250  51.757  1.00 30.64 ? 247 ALA B O      1 
ATOM   4580 C CB     . ALA B 1 253 ? 8.782  -4.438  49.296  1.00 28.70 ? 247 ALA B CB     1 
ATOM   4581 N N      . MET B 1 254 ? 6.004  -3.589  51.627  1.00 22.29 ? 248 MET B N      1 
ATOM   4582 C CA     . MET B 1 254 ? 5.678  -3.111  52.971  1.00 24.85 ? 248 MET B CA     1 
ATOM   4583 C C      . MET B 1 254 ? 5.705  -4.259  53.972  1.00 25.13 ? 248 MET B C      1 
ATOM   4584 O O      . MET B 1 254 ? 5.233  -5.361  53.688  1.00 27.57 ? 248 MET B O      1 
ATOM   4585 C CB     . MET B 1 254 ? 4.246  -2.565  52.952  1.00 32.36 ? 248 MET B CB     1 
ATOM   4586 C CG     . MET B 1 254 ? 3.841  -1.657  54.117  1.00 52.40 ? 248 MET B CG     1 
ATOM   4587 S SD     . MET B 1 254 ? 4.368  0.058   53.936  1.00 82.03 ? 248 MET B SD     1 
ATOM   4588 C CE     . MET B 1 254 ? 3.528  0.497   52.410  1.00 48.56 ? 248 MET B CE     1 
ATOM   4589 N N      . ASP B 1 255 ? 6.227  -3.982  55.166  1.00 27.14 ? 249 ASP B N      1 
ATOM   4590 C CA     . ASP B 1 255 ? 5.974  -4.807  56.340  1.00 27.07 ? 249 ASP B CA     1 
ATOM   4591 C C      . ASP B 1 255 ? 5.201  -4.012  57.381  1.00 26.59 ? 249 ASP B C      1 
ATOM   4592 O O      . ASP B 1 255 ? 5.468  -2.825  57.593  1.00 27.17 ? 249 ASP B O      1 
ATOM   4593 C CB     . ASP B 1 255 ? 7.250  -5.348  56.988  1.00 26.61 ? 249 ASP B CB     1 
ATOM   4594 C CG     . ASP B 1 255 ? 6.983  -6.583  57.851  1.00 29.62 ? 249 ASP B CG     1 
ATOM   4595 O OD1    . ASP B 1 255 ? 6.859  -7.700  57.309  1.00 26.40 ? 249 ASP B OD1    1 
ATOM   4596 O OD2    . ASP B 1 255 ? 6.853  -6.432  59.089  1.00 28.41 ? 249 ASP B OD2    1 
ATOM   4597 N N      . SER B 1 256 ? 4.254  -4.688  58.033  1.00 27.84 ? 250 SER B N      1 
ATOM   4598 C CA     . SER B 1 256 ? 3.474  -4.062  59.095  1.00 29.00 ? 250 SER B CA     1 
ATOM   4599 C C      . SER B 1 256 ? 4.337  -3.663  60.282  1.00 31.50 ? 250 SER B C      1 
ATOM   4600 O O      . SER B 1 256 ? 3.933  -2.805  61.077  1.00 28.06 ? 250 SER B O      1 
ATOM   4601 C CB     . SER B 1 256 ? 2.380  -5.019  59.570  1.00 28.57 ? 250 SER B CB     1 
ATOM   4602 O OG     . SER B 1 256 ? 2.937  -6.215  60.094  1.00 32.82 ? 250 SER B OG     1 
ATOM   4603 N N      . ASN B 1 257 ? 5.509  -4.261  60.439  1.00 25.64 ? 251 ASN B N      1 
ATOM   4604 C CA     . ASN B 1 257 ? 6.384  -3.934  61.564  1.00 26.66 ? 251 ASN B CA     1 
ATOM   4605 C C      . ASN B 1 257 ? 7.827  -4.037  61.091  1.00 24.91 ? 251 ASN B C      1 
ATOM   4606 O O      . ASN B 1 257 ? 8.523  -5.027  61.357  1.00 23.94 ? 251 ASN B O      1 
ATOM   4607 C CB     . ASN B 1 257 ? 6.102  -4.842  62.761  1.00 24.20 ? 251 ASN B CB     1 
ATOM   4608 C CG     . ASN B 1 257 ? 6.750  -4.335  64.044  1.00 28.55 ? 251 ASN B CG     1 
ATOM   4609 O OD1    . ASN B 1 257 ? 7.764  -3.629  64.015  1.00 25.47 ? 251 ASN B OD1    1 
ATOM   4610 N ND2    . ASN B 1 257 ? 6.161  -4.698  65.183  1.00 30.94 ? 251 ASN B ND2    1 
ATOM   4611 N N      . PRO B 1 258 ? 8.319  -3.008  60.391  1.00 22.82 ? 252 PRO B N      1 
ATOM   4612 C CA     . PRO B 1 258 ? 9.690  -3.091  59.834  1.00 27.03 ? 252 PRO B CA     1 
ATOM   4613 C C      . PRO B 1 258 ? 10.769 -3.353  60.864  1.00 25.32 ? 252 PRO B C      1 
ATOM   4614 O O      . PRO B 1 258 ? 11.712 -4.105  60.587  1.00 22.87 ? 252 PRO B O      1 
ATOM   4615 C CB     . PRO B 1 258 ? 9.880  -1.733  59.143  1.00 25.52 ? 252 PRO B CB     1 
ATOM   4616 C CG     . PRO B 1 258 ? 8.490  -1.290  58.799  1.00 27.00 ? 252 PRO B CG     1 
ATOM   4617 C CD     . PRO B 1 258 ? 7.605  -1.805  59.922  1.00 22.09 ? 252 PRO B CD     1 
ATOM   4618 N N      . LEU B 1 259 ? 10.659 -2.754  62.052  1.00 23.76 ? 253 LEU B N      1 
ATOM   4619 C CA     . LEU B 1 259 ? 11.675 -2.967  63.074  1.00 25.43 ? 253 LEU B CA     1 
ATOM   4620 C C      . LEU B 1 259 ? 11.705 -4.421  63.539  1.00 22.31 ? 253 LEU B C      1 
ATOM   4621 O O      . LEU B 1 259 ? 12.786 -5.010  63.675  1.00 24.35 ? 253 LEU B O      1 
ATOM   4622 C CB     . LEU B 1 259 ? 11.452 -2.008  64.243  1.00 27.17 ? 253 LEU B CB     1 
ATOM   4623 C CG     . LEU B 1 259 ? 12.521 -2.070  65.327  1.00 32.52 ? 253 LEU B CG     1 
ATOM   4624 C CD1    . LEU B 1 259 ? 13.886 -1.941  64.705  1.00 28.60 ? 253 LEU B CD1    1 
ATOM   4625 C CD2    . LEU B 1 259 ? 12.279 -0.961  66.333  1.00 32.82 ? 253 LEU B CD2    1 
ATOM   4626 N N      . SER B 1 260 ? 10.533 -5.021  63.773  1.00 20.40 ? 254 SER B N      1 
ATOM   4627 C CA     . SER B 1 260 ? 10.489 -6.413  64.207  1.00 21.94 ? 254 SER B CA     1 
ATOM   4628 C C      . SER B 1 260 ? 11.031 -7.342  63.124  1.00 20.35 ? 254 SER B C      1 
ATOM   4629 O O      . SER B 1 260 ? 11.783 -8.284  63.415  1.00 21.64 ? 254 SER B O      1 
ATOM   4630 C CB     . SER B 1 260 ? 9.053  -6.781  64.592  1.00 24.64 ? 254 SER B CB     1 
ATOM   4631 O OG     . SER B 1 260 ? 8.924  -8.156  64.892  1.00 24.90 ? 254 SER B OG     1 
ATOM   4632 N N      . LEU B 1 261 ? 10.665 -7.082  61.868  1.00 20.90 ? 255 LEU B N      1 
ATOM   4633 C CA     . LEU B 1 261 ? 11.209 -7.863  60.761  1.00 22.05 ? 255 LEU B CA     1 
ATOM   4634 C C      . LEU B 1 261 ? 12.727 -7.780  60.723  1.00 20.91 ? 255 LEU B C      1 
ATOM   4635 O O      . LEU B 1 261 ? 13.410 -8.806  60.624  1.00 19.73 ? 255 LEU B O      1 
ATOM   4636 C CB     . LEU B 1 261 ? 10.611 -7.376  59.445  1.00 20.02 ? 255 LEU B CB     1 
ATOM   4637 C CG     . LEU B 1 261 ? 11.166 -8.086  58.211  1.00 19.32 ? 255 LEU B CG     1 
ATOM   4638 C CD1    . LEU B 1 261 ? 11.023 -9.604  58.338  1.00 23.37 ? 255 LEU B CD1    1 
ATOM   4639 C CD2    . LEU B 1 261 ? 10.417 -7.558  57.000  1.00 20.42 ? 255 LEU B CD2    1 
ATOM   4640 N N      . GLY B 1 262 ? 13.270 -6.560  60.798  1.00 18.76 ? 256 GLY B N      1 
ATOM   4641 C CA     . GLY B 1 262 ? 14.713 -6.394  60.770  1.00 19.33 ? 256 GLY B CA     1 
ATOM   4642 C C      . GLY B 1 262 ? 15.414 -7.115  61.905  1.00 20.79 ? 256 GLY B C      1 
ATOM   4643 O O      . GLY B 1 262 ? 16.452 -7.751  61.705  1.00 21.37 ? 256 GLY B O      1 
ATOM   4644 N N      . LEU B 1 263 ? 14.863 -7.018  63.117  1.00 20.13 ? 257 LEU B N      1 
ATOM   4645 C CA     . LEU B 1 263 ? 15.457 -7.744  64.232  1.00 19.87 ? 257 LEU B CA     1 
ATOM   4646 C C      . LEU B 1 263 ? 15.330 -9.254  64.046  1.00 21.11 ? 257 LEU B C      1 
ATOM   4647 O O      . LEU B 1 263 ? 16.224 -10.000 64.454  1.00 21.25 ? 257 LEU B O      1 
ATOM   4648 C CB     . LEU B 1 263 ? 14.798 -7.297  65.541  1.00 22.93 ? 257 LEU B CB     1 
ATOM   4649 C CG     . LEU B 1 263 ? 15.141 -5.868  65.976  1.00 21.80 ? 257 LEU B CG     1 
ATOM   4650 C CD1    . LEU B 1 263 ? 14.275 -5.394  67.136  1.00 22.25 ? 257 LEU B CD1    1 
ATOM   4651 C CD2    . LEU B 1 263 ? 16.610 -5.777  66.361  1.00 23.01 ? 257 LEU B CD2    1 
ATOM   4652 N N      . ALA B 1 264 ? 14.244 -9.722  63.420  1.00 22.11 ? 258 ALA B N      1 
ATOM   4653 C CA     . ALA B 1 264 ? 14.099 -11.155 63.161  1.00 22.55 ? 258 ALA B CA     1 
ATOM   4654 C C      . ALA B 1 264 ? 15.176 -11.656 62.203  1.00 21.47 ? 258 ALA B C      1 
ATOM   4655 O O      . ALA B 1 264 ? 15.753 -12.733 62.400  1.00 21.96 ? 258 ALA B O      1 
ATOM   4656 C CB     . ALA B 1 264 ? 12.702 -11.450 62.604  1.00 21.06 ? 258 ALA B CB     1 
ATOM   4657 N N      . VAL B 1 265 ? 15.461 -10.891 61.154  1.00 22.29 ? 259 VAL B N      1 
ATOM   4658 C CA     . VAL B 1 265 ? 16.534 -11.282 60.248  1.00 20.92 ? 259 VAL B CA     1 
ATOM   4659 C C      . VAL B 1 265 ? 17.864 -11.315 60.981  1.00 20.50 ? 259 VAL B C      1 
ATOM   4660 O O      . VAL B 1 265 ? 18.654 -12.258 60.828  1.00 21.48 ? 259 VAL B O      1 
ATOM   4661 C CB     . VAL B 1 265 ? 16.562 -10.342 59.035  1.00 21.75 ? 259 VAL B CB     1 
ATOM   4662 C CG1    . VAL B 1 265 ? 17.795 -10.636 58.175  1.00 21.66 ? 259 VAL B CG1    1 
ATOM   4663 C CG2    . VAL B 1 265 ? 15.258 -10.487 58.240  1.00 20.79 ? 259 VAL B CG2    1 
ATOM   4664 N N      . VAL B 1 266 ? 18.128 -10.291 61.799  1.00 21.74 ? 260 VAL B N      1 
ATOM   4665 C CA     . VAL B 1 266 ? 19.392 -10.220 62.526  1.00 22.48 ? 260 VAL B CA     1 
ATOM   4666 C C      . VAL B 1 266 ? 19.546 -11.429 63.441  1.00 22.08 ? 260 VAL B C      1 
ATOM   4667 O O      . VAL B 1 266 ? 20.626 -12.031 63.525  1.00 23.10 ? 260 VAL B O      1 
ATOM   4668 C CB     . VAL B 1 266 ? 19.486 -8.886  63.293  1.00 21.03 ? 260 VAL B CB     1 
ATOM   4669 C CG1    . VAL B 1 266 ? 20.616 -8.940  64.325  1.00 24.46 ? 260 VAL B CG1    1 
ATOM   4670 C CG2    . VAL B 1 266 ? 19.686 -7.718  62.317  1.00 22.43 ? 260 VAL B CG2    1 
ATOM   4671 N N      . GLU B 1 267 ? 18.461 -11.812 64.120  1.00 23.60 ? 261 GLU B N      1 
ATOM   4672 C CA     . GLU B 1 267 ? 18.447 -13.024 64.939  1.00 24.30 ? 261 GLU B CA     1 
ATOM   4673 C C      . GLU B 1 267 ? 18.935 -14.236 64.155  1.00 27.20 ? 261 GLU B C      1 
ATOM   4674 O O      . GLU B 1 267 ? 19.789 -14.993 64.629  1.00 23.19 ? 261 GLU B O      1 
ATOM   4675 C CB     . GLU B 1 267 ? 17.032 -13.259 65.475  1.00 28.73 ? 261 GLU B CB     1 
ATOM   4676 C CG     . GLU B 1 267 ? 16.867 -14.496 66.348  1.00 33.46 ? 261 GLU B CG     1 
ATOM   4677 C CD     . GLU B 1 267 ? 15.408 -14.748 66.711  1.00 34.99 ? 261 GLU B CD     1 
ATOM   4678 O OE1    . GLU B 1 267 ? 14.714 -13.777 67.078  1.00 33.81 ? 261 GLU B OE1    1 
ATOM   4679 O OE2    . GLU B 1 267 ? 14.953 -15.914 66.636  1.00 29.40 ? 261 GLU B OE2    1 
ATOM   4680 N N      . ARG B 1 268 ? 18.426 -14.422 62.932  1.00 24.83 ? 262 ARG B N      1 
ATOM   4681 C CA     . ARG B 1 268 ? 18.826 -15.593 62.157  1.00 24.29 ? 262 ARG B CA     1 
ATOM   4682 C C      . ARG B 1 268 ? 20.271 -15.492 61.689  1.00 25.66 ? 262 ARG B C      1 
ATOM   4683 O O      . ARG B 1 268 ? 20.973 -16.507 61.617  1.00 26.37 ? 262 ARG B O      1 
ATOM   4684 C CB     . ARG B 1 268 ? 17.879 -15.824 60.978  1.00 26.34 ? 262 ARG B CB     1 
ATOM   4685 C CG     . ARG B 1 268 ? 16.672 -16.669 61.353  1.00 33.48 ? 262 ARG B CG     1 
ATOM   4686 C CD     . ARG B 1 268 ? 15.589 -15.788 61.886  1.00 30.39 ? 262 ARG B CD     1 
ATOM   4687 N NE     . ARG B 1 268 ? 14.473 -16.531 62.449  1.00 34.58 ? 262 ARG B NE     1 
ATOM   4688 C CZ     . ARG B 1 268 ? 13.571 -15.997 63.259  1.00 32.46 ? 262 ARG B CZ     1 
ATOM   4689 N NH1    . ARG B 1 268 ? 13.628 -14.721 63.608  1.00 26.45 ? 262 ARG B NH1    1 
ATOM   4690 N NH2    . ARG B 1 268 ? 12.577 -16.755 63.709  1.00 27.31 ? 262 ARG B NH2    1 
ATOM   4691 N N      . LEU B 1 269 ? 20.736 -14.281 61.360  1.00 24.67 ? 263 LEU B N      1 
ATOM   4692 C CA     . LEU B 1 269 ? 22.134 -14.114 60.982  1.00 22.79 ? 263 LEU B CA     1 
ATOM   4693 C C      . LEU B 1 269 ? 23.061 -14.388 62.161  1.00 23.91 ? 263 LEU B C      1 
ATOM   4694 O O      . LEU B 1 269 ? 24.104 -15.036 62.001  1.00 24.06 ? 263 LEU B O      1 
ATOM   4695 C CB     . LEU B 1 269 ? 22.366 -12.713 60.415  1.00 23.27 ? 263 LEU B CB     1 
ATOM   4696 C CG     . LEU B 1 269 ? 21.566 -12.394 59.145  1.00 20.77 ? 263 LEU B CG     1 
ATOM   4697 C CD1    . LEU B 1 269 ? 21.905 -11.007 58.658  1.00 26.85 ? 263 LEU B CD1    1 
ATOM   4698 C CD2    . LEU B 1 269 ? 21.850 -13.427 58.059  1.00 23.67 ? 263 LEU B CD2    1 
ATOM   4699 N N      . ASN B 1 270 ? 22.707 -13.894 63.346  1.00 23.75 ? 264 ASN B N      1 
ATOM   4700 C CA     . ASN B 1 270 ? 23.523 -14.177 64.524  1.00 27.31 ? 264 ASN B CA     1 
ATOM   4701 C C      . ASN B 1 270 ? 23.620 -15.683 64.762  1.00 21.99 ? 264 ASN B C      1 
ATOM   4702 O O      . ASN B 1 270 ? 24.698 -16.200 65.077  1.00 25.47 ? 264 ASN B O      1 
ATOM   4703 C CB     . ASN B 1 270 ? 22.920 -13.479 65.741  1.00 23.34 ? 264 ASN B CB     1 
ATOM   4704 C CG     . ASN B 1 270 ? 23.246 -11.991 65.802  1.00 23.07 ? 264 ASN B CG     1 
ATOM   4705 O OD1    . ASN B 1 270 ? 24.103 -11.487 65.076  1.00 23.57 ? 264 ASN B OD1    1 
ATOM   4706 N ND2    . ASN B 1 270 ? 22.543 -11.274 66.683  1.00 25.93 ? 264 ASN B ND2    1 
ATOM   4707 N N      . LYS B 1 271 ? 22.515 -16.405 64.542  1.00 24.44 ? 265 LYS B N      1 
ATOM   4708 C CA     . LYS B 1 271 ? 22.469 -17.852 64.746  1.00 28.17 ? 265 LYS B CA     1 
ATOM   4709 C C      . LYS B 1 271 ? 23.296 -18.599 63.699  1.00 29.80 ? 265 LYS B C      1 
ATOM   4710 O O      . LYS B 1 271 ? 23.973 -19.585 64.021  1.00 27.68 ? 265 LYS B O      1 
ATOM   4711 C CB     . LYS B 1 271 ? 21.012 -18.305 64.694  1.00 29.86 ? 265 LYS B CB     1 
ATOM   4712 C CG     . LYS B 1 271 ? 20.760 -19.782 64.914  1.00 36.82 ? 265 LYS B CG     1 
ATOM   4713 C CD     . LYS B 1 271 ? 19.284 -19.999 65.261  1.00 49.58 ? 265 LYS B CD     1 
ATOM   4714 C CE     . LYS B 1 271 ? 18.895 -21.470 65.248  1.00 47.62 ? 265 LYS B CE     1 
ATOM   4715 N NZ     . LYS B 1 271 ? 17.465 -21.664 65.632  1.00 53.45 ? 265 LYS B NZ     1 
ATOM   4716 N N      . ILE B 1 272 ? 23.239 -18.165 62.437  1.00 24.70 ? 266 ILE B N      1 
ATOM   4717 C CA     . ILE B 1 272 ? 24.099 -18.773 61.422  1.00 27.82 ? 266 ILE B CA     1 
ATOM   4718 C C      . ILE B 1 272 ? 25.563 -18.642 61.819  1.00 27.44 ? 266 ILE B C      1 
ATOM   4719 O O      . ILE B 1 272 ? 26.358 -19.576 61.647  1.00 30.06 ? 266 ILE B O      1 
ATOM   4720 C CB     . ILE B 1 272 ? 23.815 -18.174 60.032  1.00 26.41 ? 266 ILE B CB     1 
ATOM   4721 C CG1    . ILE B 1 272 ? 22.425 -18.603 59.558  1.00 27.57 ? 266 ILE B CG1    1 
ATOM   4722 C CG2    . ILE B 1 272 ? 24.902 -18.579 59.039  1.00 27.30 ? 266 ILE B CG2    1 
ATOM   4723 C CD1    . ILE B 1 272 ? 22.001 -17.998 58.238  1.00 28.78 ? 266 ILE B CD1    1 
ATOM   4724 N N      . GLN B 1 273 ? 25.936 -17.491 62.384  1.00 26.30 ? 267 GLN B N      1 
ATOM   4725 C CA     . GLN B 1 273 ? 27.324 -17.277 62.777  1.00 25.69 ? 267 GLN B CA     1 
ATOM   4726 C C      . GLN B 1 273 ? 27.752 -18.229 63.892  1.00 29.75 ? 267 GLN B C      1 
ATOM   4727 O O      . GLN B 1 273 ? 28.839 -18.810 63.822  1.00 32.73 ? 267 GLN B O      1 
ATOM   4728 C CB     . GLN B 1 273 ? 27.558 -15.810 63.149  1.00 26.63 ? 267 GLN B CB     1 
ATOM   4729 C CG     . GLN B 1 273 ? 27.392 -14.874 61.947  1.00 26.73 ? 267 GLN B CG     1 
ATOM   4730 C CD     . GLN B 1 273 ? 27.652 -13.413 62.255  1.00 28.40 ? 267 GLN B CD     1 
ATOM   4731 O OE1    . GLN B 1 273 ? 28.064 -12.651 61.377  1.00 26.82 ? 267 GLN B OE1    1 
ATOM   4732 N NE2    . GLN B 1 273 ? 27.397 -13.005 63.500  1.00 24.65 ? 267 GLN B NE2    1 
ATOM   4733 N N      . LEU B 1 274 ? 26.914 -18.415 64.919  1.00 29.51 ? 268 LEU B N      1 
ATOM   4734 C CA     . LEU B 1 274 ? 27.289 -19.342 65.991  1.00 33.09 ? 268 LEU B CA     1 
ATOM   4735 C C      . LEU B 1 274 ? 27.363 -20.786 65.506  1.00 38.99 ? 268 LEU B C      1 
ATOM   4736 O O      . LEU B 1 274 ? 28.274 -21.529 65.894  1.00 42.18 ? 268 LEU B O      1 
ATOM   4737 C CB     . LEU B 1 274 ? 26.371 -19.226 67.210  1.00 37.62 ? 268 LEU B CB     1 
ATOM   4738 C CG     . LEU B 1 274 ? 26.474 -18.058 68.202  1.00 51.24 ? 268 LEU B CG     1 
ATOM   4739 C CD1    . LEU B 1 274 ? 27.937 -17.698 68.463  1.00 50.57 ? 268 LEU B CD1    1 
ATOM   4740 C CD2    . LEU B 1 274 ? 25.660 -16.836 67.841  1.00 44.94 ? 268 LEU B CD2    1 
ATOM   4741 N N      . HIS B 1 275 ? 26.407 -21.210 64.675  1.00 38.30 ? 269 HIS B N      1 
ATOM   4742 C CA     . HIS B 1 275 ? 26.419 -22.581 64.175  1.00 44.12 ? 269 HIS B CA     1 
ATOM   4743 C C      . HIS B 1 275 ? 27.600 -22.836 63.248  1.00 42.41 ? 269 HIS B C      1 
ATOM   4744 O O      . HIS B 1 275 ? 28.104 -23.962 63.183  1.00 45.85 ? 269 HIS B O      1 
ATOM   4745 C CB     . HIS B 1 275 ? 25.106 -22.896 63.456  1.00 43.09 ? 269 HIS B CB     1 
ATOM   4746 N N      . SER B 1 276 ? 28.052 -21.818 62.525  1.00 41.09 ? 270 SER B N      1 
ATOM   4747 C CA     . SER B 1 276 ? 29.178 -21.967 61.618  1.00 45.95 ? 270 SER B CA     1 
ATOM   4748 C C      . SER B 1 276 ? 30.523 -21.715 62.285  1.00 43.41 ? 270 SER B C      1 
ATOM   4749 O O      . SER B 1 276 ? 31.559 -22.012 61.681  1.00 43.91 ? 270 SER B O      1 
ATOM   4750 C CB     . SER B 1 276 ? 29.018 -21.015 60.432  1.00 43.81 ? 270 SER B CB     1 
ATOM   4751 O OG     . SER B 1 276 ? 29.502 -19.726 60.770  1.00 48.34 ? 270 SER B OG     1 
ATOM   4752 N N      . GLY B 1 277 ? 30.536 -21.175 63.502  1.00 39.17 ? 271 GLY B N      1 
ATOM   4753 C CA     . GLY B 1 277 ? 31.785 -20.818 64.142  1.00 40.29 ? 271 GLY B CA     1 
ATOM   4754 C C      . GLY B 1 277 ? 32.563 -19.720 63.452  1.00 42.16 ? 271 GLY B C      1 
ATOM   4755 O O      . GLY B 1 277 ? 33.779 -19.631 63.629  1.00 38.67 ? 271 GLY B O      1 
ATOM   4756 N N      . SER B 1 278 ? 31.902 -18.881 62.657  1.00 36.62 ? 272 SER B N      1 
ATOM   4757 C CA     . SER B 1 278 ? 32.588 -17.788 61.987  1.00 33.20 ? 272 SER B CA     1 
ATOM   4758 C C      . SER B 1 278 ? 31.596 -16.663 61.738  1.00 33.73 ? 272 SER B C      1 
ATOM   4759 O O      . SER B 1 278 ? 30.380 -16.868 61.724  1.00 38.69 ? 272 SER B O      1 
ATOM   4760 C CB     . SER B 1 278 ? 33.230 -18.233 60.668  1.00 43.58 ? 272 SER B CB     1 
ATOM   4761 O OG     . SER B 1 278 ? 32.444 -19.231 60.042  1.00 55.09 ? 272 SER B OG     1 
ATOM   4762 N N      . LYS B 1 279 ? 32.132 -15.468 61.544  1.00 32.95 ? 273 LYS B N      1 
ATOM   4763 C CA     . LYS B 1 279 ? 31.313 -14.289 61.336  1.00 28.78 ? 273 LYS B CA     1 
ATOM   4764 C C      . LYS B 1 279 ? 31.153 -14.039 59.846  1.00 25.15 ? 273 LYS B C      1 
ATOM   4765 O O      . LYS B 1 279 ? 32.068 -14.295 59.053  1.00 26.24 ? 273 LYS B O      1 
ATOM   4766 C CB     . LYS B 1 279 ? 31.943 -13.071 62.008  1.00 33.75 ? 273 LYS B CB     1 
ATOM   4767 C CG     . LYS B 1 279 ? 31.844 -13.121 63.533  1.00 35.94 ? 273 LYS B CG     1 
ATOM   4768 C CD     . LYS B 1 279 ? 31.387 -11.792 64.104  1.00 40.91 ? 273 LYS B CD     1 
ATOM   4769 C CE     . LYS B 1 279 ? 31.520 -11.766 65.613  1.00 43.95 ? 273 LYS B CE     1 
ATOM   4770 N NZ     . LYS B 1 279 ? 30.382 -12.488 66.239  1.00 40.67 ? 273 LYS B NZ     1 
ATOM   4771 N N      . LEU B 1 280 ? 29.975 -13.558 59.471  1.00 23.35 ? 274 LEU B N      1 
ATOM   4772 C CA     . LEU B 1 280 ? 29.776 -13.084 58.112  1.00 19.16 ? 274 LEU B CA     1 
ATOM   4773 C C      . LEU B 1 280 ? 30.697 -11.899 57.853  1.00 21.63 ? 274 LEU B C      1 
ATOM   4774 O O      . LEU B 1 280 ? 31.251 -11.293 58.775  1.00 23.26 ? 274 LEU B O      1 
ATOM   4775 C CB     . LEU B 1 280 ? 28.322 -12.641 57.940  1.00 24.12 ? 274 LEU B CB     1 
ATOM   4776 C CG     . LEU B 1 280 ? 27.254 -13.732 58.078  1.00 25.49 ? 274 LEU B CG     1 
ATOM   4777 C CD1    . LEU B 1 280 ? 25.865 -13.117 58.311  1.00 26.80 ? 274 LEU B CD1    1 
ATOM   4778 C CD2    . LEU B 1 280 ? 27.245 -14.590 56.837  1.00 25.63 ? 274 LEU B CD2    1 
ATOM   4779 N N      . ALA B 1 281 ? 30.874 -11.569 56.576  1.00 22.18 ? 275 ALA B N      1 
ATOM   4780 C CA     . ALA B 1 281 ? 31.655 -10.385 56.244  1.00 19.55 ? 275 ALA B CA     1 
ATOM   4781 C C      . ALA B 1 281 ? 31.013 -9.130  56.826  1.00 19.66 ? 275 ALA B C      1 
ATOM   4782 O O      . ALA B 1 281 ? 31.710 -8.260  57.364  1.00 24.29 ? 275 ALA B O      1 
ATOM   4783 C CB     . ALA B 1 281 ? 31.807 -10.271 54.725  1.00 20.27 ? 275 ALA B CB     1 
ATOM   4784 N N      . TYR B 1 282 ? 29.684 -9.026  56.745  1.00 22.10 ? 276 TYR B N      1 
ATOM   4785 C CA     . TYR B 1 282 ? 28.968 -7.855  57.237  1.00 21.28 ? 276 TYR B CA     1 
ATOM   4786 C C      . TYR B 1 282 ? 27.477 -8.030  57.025  1.00 22.01 ? 276 TYR B C      1 
ATOM   4787 O O      . TYR B 1 282 ? 27.031 -8.863  56.229  1.00 22.05 ? 276 TYR B O      1 
ATOM   4788 C CB     . TYR B 1 282 ? 29.406 -6.580  56.508  1.00 20.37 ? 276 TYR B CB     1 
ATOM   4789 C CG     . TYR B 1 282 ? 29.202 -6.624  55.009  1.00 20.07 ? 276 TYR B CG     1 
ATOM   4790 C CD1    . TYR B 1 282 ? 27.941 -6.432  54.429  1.00 21.02 ? 276 TYR B CD1    1 
ATOM   4791 C CD2    . TYR B 1 282 ? 30.273 -6.907  54.171  1.00 22.40 ? 276 TYR B CD2    1 
ATOM   4792 C CE1    . TYR B 1 282 ? 27.784 -6.491  53.043  1.00 20.52 ? 276 TYR B CE1    1 
ATOM   4793 C CE2    . TYR B 1 282 ? 30.126 -6.967  52.795  1.00 21.54 ? 276 TYR B CE2    1 
ATOM   4794 C CZ     . TYR B 1 282 ? 28.878 -6.755  52.246  1.00 21.36 ? 276 TYR B CZ     1 
ATOM   4795 O OH     . TYR B 1 282 ? 28.722 -6.814  50.887  1.00 18.63 ? 276 TYR B OH     1 
ATOM   4796 N N      . LEU B 1 283 ? 26.720 -7.199  57.737  1.00 21.48 ? 277 LEU B N      1 
ATOM   4797 C CA     . LEU B 1 283 ? 25.335 -6.872  57.434  1.00 19.50 ? 277 LEU B CA     1 
ATOM   4798 C C      . LEU B 1 283 ? 25.292 -5.450  56.886  1.00 21.49 ? 277 LEU B C      1 
ATOM   4799 O O      . LEU B 1 283 ? 25.914 -4.539  57.444  1.00 21.12 ? 277 LEU B O      1 
ATOM   4800 C CB     . LEU B 1 283 ? 24.472 -6.966  58.694  1.00 19.12 ? 277 LEU B CB     1 
ATOM   4801 C CG     . LEU B 1 283 ? 23.036 -6.435  58.626  1.00 18.09 ? 277 LEU B CG     1 
ATOM   4802 C CD1    . LEU B 1 283 ? 22.148 -7.332  57.790  1.00 20.77 ? 277 LEU B CD1    1 
ATOM   4803 C CD2    . LEU B 1 283 ? 22.497 -6.334  60.059  1.00 21.75 ? 277 LEU B CD2    1 
ATOM   4804 N N      . HIS B 1 284 ? 24.531 -5.262  55.811  1.00 19.37 ? 278 HIS B N      1 
ATOM   4805 C CA     . HIS B 1 284 ? 24.454 -4.010  55.073  1.00 19.44 ? 278 HIS B CA     1 
ATOM   4806 C C      . HIS B 1 284 ? 22.983 -3.628  55.052  1.00 18.45 ? 278 HIS B C      1 
ATOM   4807 O O      . HIS B 1 284 ? 22.159 -4.385  54.531  1.00 20.26 ? 278 HIS B O      1 
ATOM   4808 C CB     . HIS B 1 284 ? 24.971 -4.279  53.652  1.00 20.23 ? 278 HIS B CB     1 
ATOM   4809 C CG     . HIS B 1 284 ? 25.165 -3.062  52.803  1.00 18.94 ? 278 HIS B CG     1 
ATOM   4810 N ND1    . HIS B 1 284 ? 25.690 -3.140  51.527  1.00 22.25 ? 278 HIS B ND1    1 
ATOM   4811 C CD2    . HIS B 1 284 ? 24.919 -1.751  53.030  1.00 18.51 ? 278 HIS B CD2    1 
ATOM   4812 C CE1    . HIS B 1 284 ? 25.778 -1.927  51.015  1.00 21.41 ? 278 HIS B CE1    1 
ATOM   4813 N NE2    . HIS B 1 284 ? 25.311 -1.067  51.901  1.00 20.30 ? 278 HIS B NE2    1 
ATOM   4814 N N      . VAL B 1 285 ? 22.642 -2.500  55.675  1.00 20.50 ? 279 VAL B N      1 
ATOM   4815 C CA     . VAL B 1 285 ? 21.250 -2.068  55.799  1.00 19.93 ? 279 VAL B CA     1 
ATOM   4816 C C      . VAL B 1 285 ? 21.086 -0.749  55.066  1.00 19.19 ? 279 VAL B C      1 
ATOM   4817 O O      . VAL B 1 285 ? 21.879 0.179   55.248  1.00 21.96 ? 279 VAL B O      1 
ATOM   4818 C CB     . VAL B 1 285 ? 20.793 -1.938  57.263  1.00 19.59 ? 279 VAL B CB     1 
ATOM   4819 C CG1    . VAL B 1 285 ? 19.358 -1.404  57.304  1.00 23.15 ? 279 VAL B CG1    1 
ATOM   4820 C CG2    . VAL B 1 285 ? 20.846 -3.288  57.930  1.00 23.96 ? 279 VAL B CG2    1 
ATOM   4821 N N      . THR B 1 286 ? 20.071 -0.671  54.220  1.00 22.55 ? 280 THR B N      1 
ATOM   4822 C CA     . THR B 1 286 ? 19.802 0.559   53.507  1.00 19.88 ? 280 THR B CA     1 
ATOM   4823 C C      . THR B 1 286 ? 18.444 1.091   53.938  1.00 27.13 ? 280 THR B C      1 
ATOM   4824 O O      . THR B 1 286 ? 17.532 0.319   54.255  1.00 27.93 ? 280 THR B O      1 
ATOM   4825 C CB     . THR B 1 286 ? 19.944 0.340   51.992  1.00 30.52 ? 280 THR B CB     1 
ATOM   4826 O OG1    . THR B 1 286 ? 20.144 1.596   51.327  1.00 33.08 ? 280 THR B OG1    1 
ATOM   4827 C CG2    . THR B 1 286 ? 18.767 -0.403  51.439  1.00 29.41 ? 280 THR B CG2    1 
ATOM   4828 N N      . GLN B 1 287 ? 18.340 2.407   54.005  1.00 25.48 ? 281 GLN B N      1 
ATOM   4829 C CA     . GLN B 1 287 ? 17.170 3.094   54.522  1.00 29.61 ? 281 GLN B CA     1 
ATOM   4830 C C      . GLN B 1 287 ? 16.595 4.001   53.439  1.00 28.19 ? 281 GLN B C      1 
ATOM   4831 O O      . GLN B 1 287 ? 17.300 4.380   52.494  1.00 28.46 ? 281 GLN B O      1 
ATOM   4832 C CB     . GLN B 1 287 ? 17.588 3.923   55.744  1.00 26.10 ? 281 GLN B CB     1 
ATOM   4833 C CG     . GLN B 1 287 ? 18.470 5.108   55.424  1.00 27.34 ? 281 GLN B CG     1 
ATOM   4834 C CD     . GLN B 1 287 ? 19.053 5.758   56.664  1.00 27.70 ? 281 GLN B CD     1 
ATOM   4835 O OE1    . GLN B 1 287 ? 18.603 5.510   57.798  1.00 30.14 ? 281 GLN B OE1    1 
ATOM   4836 N NE2    . GLN B 1 287 ? 20.039 6.613   56.463  1.00 29.06 ? 281 GLN B NE2    1 
ATOM   4837 N N      . PRO B 1 288 ? 15.298 4.348   53.526  1.00 31.44 ? 282 PRO B N      1 
ATOM   4838 C CA     . PRO B 1 288 ? 14.662 5.197   52.508  1.00 36.12 ? 282 PRO B CA     1 
ATOM   4839 C C      . PRO B 1 288 ? 15.077 6.663   52.621  1.00 45.03 ? 282 PRO B C      1 
ATOM   4840 O O      . PRO B 1 288 ? 15.719 7.024   53.611  1.00 44.32 ? 282 PRO B O      1 
ATOM   4841 C CB     . PRO B 1 288 ? 13.167 5.042   52.814  1.00 36.54 ? 282 PRO B CB     1 
ATOM   4842 C CG     . PRO B 1 288 ? 13.122 4.758   54.257  1.00 36.36 ? 282 PRO B CG     1 
ATOM   4843 C CD     . PRO B 1 288 ? 14.341 3.930   54.567  1.00 34.55 ? 282 PRO B CD     1 
ATOM   4844 N N      . ALA B 1 308 ? 14.405 6.906   62.346  1.00 64.54 ? 302 ALA B N      1 
ATOM   4845 C CA     . ALA B 1 308 ? 15.776 6.635   61.850  1.00 66.06 ? 302 ALA B CA     1 
ATOM   4846 C C      . ALA B 1 308 ? 16.655 6.115   62.989  1.00 62.09 ? 302 ALA B C      1 
ATOM   4847 O O      . ALA B 1 308 ? 17.872 6.273   62.877  1.00 54.66 ? 302 ALA B O      1 
ATOM   4848 C CB     . ALA B 1 308 ? 16.369 7.869   61.214  1.00 61.03 ? 302 ALA B CB     1 
ATOM   4849 N N      . ARG B 1 309 ? 16.054 5.580   64.058  1.00 54.59 ? 303 ARG B N      1 
ATOM   4850 C CA     . ARG B 1 309 ? 16.828 4.909   65.130  1.00 45.08 ? 303 ARG B CA     1 
ATOM   4851 C C      . ARG B 1 309 ? 16.839 3.433   64.737  1.00 41.34 ? 303 ARG B C      1 
ATOM   4852 O O      . ARG B 1 309 ? 17.469 2.652   65.439  1.00 45.87 ? 303 ARG B O      1 
ATOM   4853 C CB     . ARG B 1 309 ? 16.145 5.049   66.490  1.00 46.15 ? 303 ARG B CB     1 
ATOM   4854 C CG     . ARG B 1 309 ? 16.709 6.166   67.355  1.00 52.70 ? 303 ARG B CG     1 
ATOM   4855 C CD     . ARG B 1 309 ? 16.979 5.725   68.778  1.00 56.38 ? 303 ARG B CD     1 
ATOM   4856 N NE     . ARG B 1 309 ? 15.961 4.808   69.260  1.00 58.30 ? 303 ARG B NE     1 
ATOM   4857 C CZ     . ARG B 1 309 ? 15.017 5.124   70.139  1.00 54.71 ? 303 ARG B CZ     1 
ATOM   4858 N NH1    . ARG B 1 309 ? 14.219 6.151   69.914  1.00 56.12 ? 303 ARG B NH1    1 
ATOM   4859 N NH2    . ARG B 1 309 ? 14.874 4.407   71.238  1.00 52.31 ? 303 ARG B NH2    1 
ATOM   4860 N N      . LEU B 1 310 ? 16.148 3.102   63.642  1.00 42.51 ? 304 LEU B N      1 
ATOM   4861 C CA     . LEU B 1 310 ? 16.072 1.703   63.152  1.00 38.54 ? 304 LEU B CA     1 
ATOM   4862 C C      . LEU B 1 310 ? 17.481 1.227   62.785  1.00 29.39 ? 304 LEU B C      1 
ATOM   4863 O O      . LEU B 1 310 ? 17.850 0.126   63.172  1.00 29.53 ? 304 LEU B O      1 
ATOM   4864 C CB     . LEU B 1 310 ? 15.119 1.683   61.955  1.00 34.71 ? 304 LEU B CB     1 
ATOM   4865 C CG     . LEU B 1 310 ? 15.137 0.465   61.031  1.00 43.26 ? 304 LEU B CG     1 
ATOM   4866 C CD1    . LEU B 1 310 ? 15.063 -0.828  61.809  1.00 46.89 ? 304 LEU B CD1    1 
ATOM   4867 C CD2    . LEU B 1 310 ? 13.969 0.521   60.064  1.00 44.16 ? 304 LEU B CD2    1 
ATOM   4868 N N      . MET B 1 311 ? 18.219 2.062   62.071  1.00 31.96 ? 305 MET B N      1 
ATOM   4869 C CA     . MET B 1 311 ? 19.590 1.688   61.658  1.00 26.30 ? 305 MET B CA     1 
ATOM   4870 C C      . MET B 1 311 ? 20.410 1.314   62.902  1.00 29.45 ? 305 MET B C      1 
ATOM   4871 O O      . MET B 1 311 ? 21.016 0.247   62.898  1.00 24.64 ? 305 MET B O      1 
ATOM   4872 C CB     . MET B 1 311 ? 20.237 2.843   60.884  1.00 29.11 ? 305 MET B CB     1 
ATOM   4873 C CG     . MET B 1 311 ? 21.527 2.470   60.185  1.00 25.61 ? 305 MET B CG     1 
ATOM   4874 S SD     . MET B 1 311 ? 21.263 1.504   58.678  1.00 35.46 ? 305 MET B SD     1 
ATOM   4875 C CE     . MET B 1 311 ? 20.932 2.807   57.496  1.00 28.03 ? 305 MET B CE     1 
ATOM   4876 N N      . ARG B 1 312 ? 20.426 2.187   63.906  1.00 29.47 ? 306 ARG B N      1 
ATOM   4877 C CA     . ARG B 1 312 ? 21.209 1.903   65.109  1.00 28.33 ? 306 ARG B CA     1 
ATOM   4878 C C      . ARG B 1 312 ? 20.679 0.675   65.841  1.00 24.00 ? 306 ARG B C      1 
ATOM   4879 O O      . ARG B 1 312 ? 21.463 -0.133  66.356  1.00 23.71 ? 306 ARG B O      1 
ATOM   4880 C CB     . ARG B 1 312 ? 21.210 3.125   66.032  1.00 34.15 ? 306 ARG B CB     1 
ATOM   4881 C CG     . ARG B 1 312 ? 22.066 2.965   67.274  1.00 33.57 ? 306 ARG B CG     1 
ATOM   4882 C CD     . ARG B 1 312 ? 23.498 2.656   66.894  1.00 35.92 ? 306 ARG B CD     1 
ATOM   4883 N NE     . ARG B 1 312 ? 24.322 2.367   68.062  1.00 29.84 ? 306 ARG B NE     1 
ATOM   4884 C CZ     . ARG B 1 312 ? 25.277 3.163   68.526  1.00 41.30 ? 306 ARG B CZ     1 
ATOM   4885 N NH1    . ARG B 1 312 ? 25.558 4.319   67.945  1.00 40.99 ? 306 ARG B NH1    1 
ATOM   4886 N NH2    . ARG B 1 312 ? 25.962 2.795   69.606  1.00 45.71 ? 306 ARG B NH2    1 
ATOM   4887 N N      . THR B 1 313 ? 19.356 0.503   65.872  1.00 25.70 ? 307 THR B N      1 
ATOM   4888 C CA     . THR B 1 313 ? 18.771 -0.653  66.543  1.00 25.80 ? 307 THR B CA     1 
ATOM   4889 C C      . THR B 1 313 ? 19.212 -1.965  65.899  1.00 24.47 ? 307 THR B C      1 
ATOM   4890 O O      . THR B 1 313 ? 19.581 -2.914  66.596  1.00 24.61 ? 307 THR B O      1 
ATOM   4891 C CB     . THR B 1 313 ? 17.248 -0.536  66.566  1.00 33.33 ? 307 THR B CB     1 
ATOM   4892 O OG1    . THR B 1 313 ? 16.875 0.669   67.247  1.00 39.78 ? 307 THR B OG1    1 
ATOM   4893 C CG2    . THR B 1 313 ? 16.660 -1.733  67.293  1.00 30.89 ? 307 THR B CG2    1 
ATOM   4894 N N      . LEU B 1 314 ? 19.189 -2.044  64.564  1.00 21.08 ? 308 LEU B N      1 
ATOM   4895 C CA     . LEU B 1 314 ? 19.666 -3.270  63.928  1.00 20.13 ? 308 LEU B CA     1 
ATOM   4896 C C      . LEU B 1 314 ? 21.166 -3.456  64.142  1.00 20.56 ? 308 LEU B C      1 
ATOM   4897 O O      . LEU B 1 314 ? 21.628 -4.576  64.389  1.00 22.79 ? 308 LEU B O      1 
ATOM   4898 C CB     . LEU B 1 314 ? 19.309 -3.288  62.441  1.00 22.68 ? 308 LEU B CB     1 
ATOM   4899 C CG     . LEU B 1 314 ? 17.830 -3.097  62.120  1.00 22.16 ? 308 LEU B CG     1 
ATOM   4900 C CD1    . LEU B 1 314 ? 17.675 -3.050  60.592  1.00 26.39 ? 308 LEU B CD1    1 
ATOM   4901 C CD2    . LEU B 1 314 ? 16.963 -4.177  62.753  1.00 25.05 ? 308 LEU B CD2    1 
ATOM   4902 N N      . ARG B 1 315 ? 21.940 -2.370  64.076  1.00 20.30 ? 309 ARG B N      1 
ATOM   4903 C CA     . ARG B 1 315 ? 23.377 -2.467  64.317  1.00 21.81 ? 309 ARG B CA     1 
ATOM   4904 C C      . ARG B 1 315 ? 23.651 -3.010  65.714  1.00 21.79 ? 309 ARG B C      1 
ATOM   4905 O O      . ARG B 1 315 ? 24.476 -3.913  65.898  1.00 22.15 ? 309 ARG B O      1 
ATOM   4906 C CB     . ARG B 1 315 ? 24.023 -1.094  64.131  1.00 23.24 ? 309 ARG B CB     1 
ATOM   4907 C CG     . ARG B 1 315 ? 25.562 -1.112  64.114  1.00 23.94 ? 309 ARG B CG     1 
ATOM   4908 C CD     . ARG B 1 315 ? 26.209 -1.077  65.512  1.00 21.25 ? 309 ARG B CD     1 
ATOM   4909 N NE     . ARG B 1 315 ? 27.499 -0.400  65.440  1.00 25.90 ? 309 ARG B NE     1 
ATOM   4910 C CZ     . ARG B 1 315 ? 28.577 -0.874  64.823  1.00 26.37 ? 309 ARG B CZ     1 
ATOM   4911 N NH1    . ARG B 1 315 ? 28.615 -2.102  64.328  1.00 22.73 ? 309 ARG B NH1    1 
ATOM   4912 N NH2    . ARG B 1 315 ? 29.644 -0.095  64.697  1.00 24.73 ? 309 ARG B NH2    1 
ATOM   4913 N N      . ASN B 1 316 ? 22.956 -2.471  66.713  1.00 23.70 ? 310 ASN B N      1 
ATOM   4914 C CA     . ASN B 1 316 ? 23.167 -2.916  68.090  1.00 23.82 ? 310 ASN B CA     1 
ATOM   4915 C C      . ASN B 1 316 ? 22.827 -4.391  68.265  1.00 26.28 ? 310 ASN B C      1 
ATOM   4916 O O      . ASN B 1 316 ? 23.407 -5.070  69.122  1.00 26.48 ? 310 ASN B O      1 
ATOM   4917 C CB     . ASN B 1 316 ? 22.297 -2.084  69.024  1.00 25.76 ? 310 ASN B CB     1 
ATOM   4918 C CG     . ASN B 1 316 ? 22.877 -0.710  69.310  1.00 24.23 ? 310 ASN B CG     1 
ATOM   4919 O OD1    . ASN B 1 316 ? 24.038 -0.429  69.028  1.00 24.98 ? 310 ASN B OD1    1 
ATOM   4920 N ND2    . ASN B 1 316 ? 22.048 0.161   69.888  1.00 26.25 ? 310 ASN B ND2    1 
ATOM   4921 N N      . ALA B 1 317 ? 21.884 -4.904  67.479  1.00 20.82 ? 311 ALA B N      1 
ATOM   4922 C CA     . ALA B 1 317 ? 21.462 -6.292  67.610  1.00 20.86 ? 311 ALA B CA     1 
ATOM   4923 C C      . ALA B 1 317 ? 22.360 -7.259  66.866  1.00 22.58 ? 311 ALA B C      1 
ATOM   4924 O O      . ALA B 1 317 ? 22.382 -8.444  67.208  1.00 23.36 ? 311 ALA B O      1 
ATOM   4925 C CB     . ALA B 1 317 ? 20.033 -6.456  67.094  1.00 22.95 ? 311 ALA B CB     1 
ATOM   4926 N N      . TYR B 1 318 ? 23.073 -6.795  65.836  1.00 22.33 ? 312 TYR B N      1 
ATOM   4927 C CA     . TYR B 1 318 ? 23.853 -7.674  64.983  1.00 21.27 ? 312 TYR B CA     1 
ATOM   4928 C C      . TYR B 1 318 ? 25.251 -7.852  65.571  1.00 22.15 ? 312 TYR B C      1 
ATOM   4929 O O      . TYR B 1 318 ? 25.934 -6.869  65.881  1.00 22.85 ? 312 TYR B O      1 
ATOM   4930 C CB     . TYR B 1 318 ? 23.991 -7.046  63.591  1.00 21.77 ? 312 TYR B CB     1 
ATOM   4931 C CG     . TYR B 1 318 ? 24.832 -7.897  62.689  1.00 22.18 ? 312 TYR B CG     1 
ATOM   4932 C CD1    . TYR B 1 318 ? 24.684 -9.281  62.666  1.00 22.23 ? 312 TYR B CD1    1 
ATOM   4933 C CD2    . TYR B 1 318 ? 25.947 -7.356  62.084  1.00 19.13 ? 312 TYR B CD2    1 
ATOM   4934 C CE1    . TYR B 1 318 ? 25.510 -10.079 61.903  1.00 24.22 ? 312 TYR B CE1    1 
ATOM   4935 C CE2    . TYR B 1 318 ? 26.798 -8.145  61.346  1.00 18.36 ? 312 TYR B CE2    1 
ATOM   4936 C CZ     . TYR B 1 318 ? 26.583 -9.504  61.260  1.00 24.23 ? 312 TYR B CZ     1 
ATOM   4937 O OH     . TYR B 1 318 ? 27.454 -10.266 60.506  1.00 27.37 ? 312 TYR B OH     1 
ATOM   4938 N N      . GLN B 1 319 ? 25.696 -9.107  65.676  1.00 21.93 ? 313 GLN B N      1 
ATOM   4939 C CA     . GLN B 1 319 ? 27.053 -9.427  66.144  1.00 26.27 ? 313 GLN B CA     1 
ATOM   4940 C C      . GLN B 1 319 ? 28.033 -9.466  64.975  1.00 22.79 ? 313 GLN B C      1 
ATOM   4941 O O      . GLN B 1 319 ? 28.375 -10.526 64.451  1.00 27.12 ? 313 GLN B O      1 
ATOM   4942 C CB     . GLN B 1 319 ? 27.048 -10.745 66.910  1.00 25.95 ? 313 GLN B CB     1 
ATOM   4943 C CG     . GLN B 1 319 ? 25.976 -10.798 67.994  1.00 24.09 ? 313 GLN B CG     1 
ATOM   4944 C CD     . GLN B 1 319 ? 25.877 -12.142 68.671  1.00 31.30 ? 313 GLN B CD     1 
ATOM   4945 O OE1    . GLN B 1 319 ? 26.618 -13.065 68.357  1.00 32.16 ? 313 GLN B OE1    1 
ATOM   4946 N NE2    . GLN B 1 319 ? 24.972 -12.248 69.645  1.00 32.79 ? 313 GLN B NE2    1 
ATOM   4947 N N      . GLY B 1 320 ? 28.514 -8.290  64.583  1.00 23.49 ? 314 GLY B N      1 
ATOM   4948 C CA     . GLY B 1 320 ? 29.499 -8.220  63.516  1.00 22.98 ? 314 GLY B CA     1 
ATOM   4949 C C      . GLY B 1 320 ? 29.548 -6.842  62.868  1.00 23.80 ? 314 GLY B C      1 
ATOM   4950 O O      . GLY B 1 320 ? 29.040 -5.859  63.411  1.00 22.95 ? 314 GLY B O      1 
ATOM   4951 N N      . THR B 1 321 ? 30.175 -6.813  61.691  1.00 22.03 ? 315 THR B N      1 
ATOM   4952 C CA     . THR B 1 321 ? 30.420 -5.580  60.958  1.00 20.70 ? 315 THR B CA     1 
ATOM   4953 C C      . THR B 1 321 ? 29.135 -5.083  60.307  1.00 23.57 ? 315 THR B C      1 
ATOM   4954 O O      . THR B 1 321 ? 28.366 -5.863  59.738  1.00 21.46 ? 315 THR B O      1 
ATOM   4955 C CB     . THR B 1 321 ? 31.463 -5.849  59.872  1.00 27.57 ? 315 THR B CB     1 
ATOM   4956 O OG1    . THR B 1 321 ? 32.719 -6.140  60.499  1.00 24.71 ? 315 THR B OG1    1 
ATOM   4957 C CG2    . THR B 1 321 ? 31.616 -4.640  58.950  1.00 24.34 ? 315 THR B CG2    1 
ATOM   4958 N N      . PHE B 1 322 ? 28.906 -3.775  60.390  1.00 23.11 ? 316 PHE B N      1 
ATOM   4959 C CA     . PHE B 1 322 ? 27.667 -3.167  59.916  1.00 21.11 ? 316 PHE B CA     1 
ATOM   4960 C C      . PHE B 1 322 ? 27.982 -2.076  58.900  1.00 22.95 ? 316 PHE B C      1 
ATOM   4961 O O      . PHE B 1 322 ? 28.779 -1.176  59.184  1.00 20.89 ? 316 PHE B O      1 
ATOM   4962 C CB     . PHE B 1 322 ? 26.928 -2.559  61.110  1.00 21.78 ? 316 PHE B CB     1 
ATOM   4963 C CG     . PHE B 1 322 ? 25.520 -2.144  60.811  1.00 21.60 ? 316 PHE B CG     1 
ATOM   4964 C CD1    . PHE B 1 322 ? 24.486 -3.059  60.896  1.00 21.17 ? 316 PHE B CD1    1 
ATOM   4965 C CD2    . PHE B 1 322 ? 25.236 -0.832  60.472  1.00 22.43 ? 316 PHE B CD2    1 
ATOM   4966 C CE1    . PHE B 1 322 ? 23.184 -2.679  60.623  1.00 20.97 ? 316 PHE B CE1    1 
ATOM   4967 C CE2    . PHE B 1 322 ? 23.928 -0.442  60.209  1.00 24.36 ? 316 PHE B CE2    1 
ATOM   4968 C CZ     . PHE B 1 322 ? 22.905 -1.368  60.293  1.00 22.50 ? 316 PHE B CZ     1 
ATOM   4969 N N      . ILE B 1 323 ? 27.347 -2.141  57.725  1.00 20.20 ? 317 ILE B N      1 
ATOM   4970 C CA     . ILE B 1 323 ? 27.469 -1.107  56.701  1.00 19.50 ? 317 ILE B CA     1 
ATOM   4971 C C      . ILE B 1 323 ? 26.144 -0.368  56.601  1.00 22.20 ? 317 ILE B C      1 
ATOM   4972 O O      . ILE B 1 323 ? 25.108 -0.987  56.332  1.00 21.46 ? 317 ILE B O      1 
ATOM   4973 C CB     . ILE B 1 323 ? 27.805 -1.701  55.329  1.00 19.94 ? 317 ILE B CB     1 
ATOM   4974 C CG1    . ILE B 1 323 ? 28.994 -2.662  55.419  1.00 21.59 ? 317 ILE B CG1    1 
ATOM   4975 C CG2    . ILE B 1 323 ? 28.049 -0.565  54.343  1.00 21.20 ? 317 ILE B CG2    1 
ATOM   4976 C CD1    . ILE B 1 323 ? 29.404 -3.220  54.043  1.00 21.29 ? 317 ILE B CD1    1 
ATOM   4977 N N      . CYS B 1 324 ? 26.168 0.947   56.802  1.00 20.70 ? 318 CYS B N      1 
ATOM   4978 C CA     . CYS B 1 324 ? 24.956 1.743   56.658  1.00 23.60 ? 318 CYS B CA     1 
ATOM   4979 C C      . CYS B 1 324 ? 24.935 2.389   55.279  1.00 23.21 ? 318 CYS B C      1 
ATOM   4980 O O      . CYS B 1 324 ? 25.982 2.631   54.670  1.00 21.96 ? 318 CYS B O      1 
ATOM   4981 C CB     . CYS B 1 324 ? 24.841 2.826   57.735  1.00 22.02 ? 318 CYS B CB     1 
ATOM   4982 S SG     . CYS B 1 324 ? 26.208 4.004   57.776  1.00 26.75 ? 318 CYS B SG     1 
ATOM   4983 N N      . SER B 1 325 ? 23.725 2.663   54.793  1.00 22.84 ? 319 SER B N      1 
ATOM   4984 C CA     . SER B 1 325 ? 23.541 3.092   53.418  1.00 20.13 ? 319 SER B CA     1 
ATOM   4985 C C      . SER B 1 325 ? 22.227 3.851   53.296  1.00 22.15 ? 319 SER B C      1 
ATOM   4986 O O      . SER B 1 325 ? 21.239 3.522   53.956  1.00 22.73 ? 319 SER B O      1 
ATOM   4987 C CB     . SER B 1 325 ? 23.491 1.864   52.510  1.00 25.96 ? 319 SER B CB     1 
ATOM   4988 O OG     . SER B 1 325 ? 22.877 2.179   51.275  1.00 31.66 ? 319 SER B OG     1 
ATOM   4989 N N      . GLY B 1 326 ? 22.222 4.848   52.413  1.00 23.18 ? 320 GLY B N      1 
ATOM   4990 C CA     . GLY B 1 326 ? 21.006 5.568   52.080  1.00 24.36 ? 320 GLY B CA     1 
ATOM   4991 C C      . GLY B 1 326 ? 21.019 7.013   52.530  1.00 28.21 ? 320 GLY B C      1 
ATOM   4992 O O      . GLY B 1 326 ? 20.789 7.306   53.708  1.00 25.93 ? 320 GLY B O      1 
ATOM   4993 N N      . GLY B 1 327 ? 21.287 7.931   51.607  1.00 27.18 ? 321 GLY B N      1 
ATOM   4994 C CA     . GLY B 1 327 ? 21.271 9.339   51.945  1.00 28.68 ? 321 GLY B CA     1 
ATOM   4995 C C      . GLY B 1 327 ? 22.482 9.840   52.694  1.00 33.34 ? 321 GLY B C      1 
ATOM   4996 O O      . GLY B 1 327 ? 22.461 10.975  53.185  1.00 35.04 ? 321 GLY B O      1 
ATOM   4997 N N      . TYR B 1 328 ? 23.538 9.041   52.807  1.00 29.86 ? 322 TYR B N      1 
ATOM   4998 C CA     . TYR B 1 328 ? 24.711 9.509   53.527  1.00 28.77 ? 322 TYR B CA     1 
ATOM   4999 C C      . TYR B 1 328 ? 25.474 10.550  52.719  1.00 28.83 ? 322 TYR B C      1 
ATOM   5000 O O      . TYR B 1 328 ? 25.588 10.463  51.491  1.00 29.27 ? 322 TYR B O      1 
ATOM   5001 C CB     . TYR B 1 328 ? 25.594 8.338   53.974  1.00 29.83 ? 322 TYR B CB     1 
ATOM   5002 C CG     . TYR B 1 328 ? 24.941 7.611   55.123  1.00 27.32 ? 322 TYR B CG     1 
ATOM   5003 C CD1    . TYR B 1 328 ? 24.028 6.593   54.890  1.00 26.23 ? 322 TYR B CD1    1 
ATOM   5004 C CD2    . TYR B 1 328 ? 25.183 7.985   56.448  1.00 29.37 ? 322 TYR B CD2    1 
ATOM   5005 C CE1    . TYR B 1 328 ? 23.389 5.944   55.936  1.00 25.49 ? 322 TYR B CE1    1 
ATOM   5006 C CE2    . TYR B 1 328 ? 24.557 7.335   57.505  1.00 26.86 ? 322 TYR B CE2    1 
ATOM   5007 C CZ     . TYR B 1 328 ? 23.656 6.319   57.242  1.00 29.37 ? 322 TYR B CZ     1 
ATOM   5008 O OH     . TYR B 1 328 ? 23.019 5.664   58.269  1.00 32.18 ? 322 TYR B OH     1 
ATOM   5009 N N      . THR B 1 329 ? 25.930 11.577  53.418  1.00 29.14 ? 323 THR B N      1 
ATOM   5010 C CA     . THR B 1 329 ? 26.836 12.594  52.919  1.00 32.18 ? 323 THR B CA     1 
ATOM   5011 C C      . THR B 1 329 ? 28.193 12.376  53.574  1.00 31.49 ? 323 THR B C      1 
ATOM   5012 O O      . THR B 1 329 ? 28.369 11.467  54.389  1.00 29.19 ? 323 THR B O      1 
ATOM   5013 C CB     . THR B 1 329 ? 26.283 13.983  53.244  1.00 33.10 ? 323 THR B CB     1 
ATOM   5014 O OG1    . THR B 1 329 ? 26.160 14.134  54.668  1.00 33.66 ? 323 THR B OG1    1 
ATOM   5015 C CG2    . THR B 1 329 ? 24.911 14.180  52.589  1.00 38.14 ? 323 THR B CG2    1 
ATOM   5016 N N      . ARG B 1 330 ? 29.166 13.209  53.203  1.00 27.78 ? 324 ARG B N      1 
ATOM   5017 C CA     . ARG B 1 330 ? 30.439 13.192  53.912  1.00 27.32 ? 324 ARG B CA     1 
ATOM   5018 C C      . ARG B 1 330 ? 30.218 13.379  55.411  1.00 27.90 ? 324 ARG B C      1 
ATOM   5019 O O      . ARG B 1 330 ? 30.697 12.589  56.230  1.00 27.82 ? 324 ARG B O      1 
ATOM   5020 C CB     . ARG B 1 330 ? 31.351 14.287  53.364  1.00 30.22 ? 324 ARG B CB     1 
ATOM   5021 C CG     . ARG B 1 330 ? 32.687 14.352  54.064  1.00 32.51 ? 324 ARG B CG     1 
ATOM   5022 C CD     . ARG B 1 330 ? 33.545 15.469  53.518  1.00 29.57 ? 324 ARG B CD     1 
ATOM   5023 N NE     . ARG B 1 330 ? 34.855 15.482  54.155  1.00 31.67 ? 324 ARG B NE     1 
ATOM   5024 C CZ     . ARG B 1 330 ? 35.125 16.137  55.277  1.00 38.77 ? 324 ARG B CZ     1 
ATOM   5025 N NH1    . ARG B 1 330 ? 34.204 16.865  55.888  1.00 31.64 ? 324 ARG B NH1    1 
ATOM   5026 N NH2    . ARG B 1 330 ? 36.347 16.067  55.791  1.00 38.29 ? 324 ARG B NH2    1 
ATOM   5027 N N      . GLU B 1 331 ? 29.442 14.397  55.775  1.00 28.70 ? 325 GLU B N      1 
ATOM   5028 C CA     . GLU B 1 331 ? 29.271 14.745  57.182  1.00 31.78 ? 325 GLU B CA     1 
ATOM   5029 C C      . GLU B 1 331 ? 28.491 13.667  57.928  1.00 29.68 ? 325 GLU B C      1 
ATOM   5030 O O      . GLU B 1 331 ? 28.867 13.282  59.043  1.00 30.15 ? 325 GLU B O      1 
ATOM   5031 C CB     . GLU B 1 331 ? 28.583 16.108  57.281  1.00 34.74 ? 325 GLU B CB     1 
ATOM   5032 C CG     . GLU B 1 331 ? 29.457 17.269  56.775  1.00 48.02 ? 325 GLU B CG     1 
ATOM   5033 C CD     . GLU B 1 331 ? 29.662 17.283  55.243  1.00 53.96 ? 325 GLU B CD     1 
ATOM   5034 O OE1    . GLU B 1 331 ? 28.831 16.704  54.487  1.00 42.88 ? 325 GLU B OE1    1 
ATOM   5035 O OE2    . GLU B 1 331 ? 30.690 17.855  54.801  1.00 49.64 ? 325 GLU B OE2    1 
ATOM   5036 N N      . LEU B 1 332 ? 27.417 13.151  57.323  1.00 30.51 ? 326 LEU B N      1 
ATOM   5037 C CA     . LEU B 1 332 ? 26.653 12.085  57.967  1.00 29.79 ? 326 LEU B CA     1 
ATOM   5038 C C      . LEU B 1 332 ? 27.440 10.781  58.043  1.00 31.08 ? 326 LEU B C      1 
ATOM   5039 O O      . LEU B 1 332 ? 27.286 10.030  59.012  1.00 28.18 ? 326 LEU B O      1 
ATOM   5040 C CB     . LEU B 1 332 ? 25.311 11.879  57.261  1.00 28.98 ? 326 LEU B CB     1 
ATOM   5041 C CG     . LEU B 1 332 ? 24.332 13.049  57.365  1.00 30.02 ? 326 LEU B CG     1 
ATOM   5042 C CD1    . LEU B 1 332 ? 23.189 12.879  56.374  1.00 34.47 ? 326 LEU B CD1    1 
ATOM   5043 C CD2    . LEU B 1 332 ? 23.812 13.207  58.804  1.00 34.20 ? 326 LEU B CD2    1 
ATOM   5044 N N      . GLY B 1 333 ? 28.277 10.489  57.041  1.00 28.62 ? 327 GLY B N      1 
ATOM   5045 C CA     . GLY B 1 333 ? 29.140 9.319   57.136  1.00 25.33 ? 327 GLY B CA     1 
ATOM   5046 C C      . GLY B 1 333 ? 30.172 9.437   58.243  1.00 30.37 ? 327 GLY B C      1 
ATOM   5047 O O      . GLY B 1 333 ? 30.425 8.475   58.977  1.00 25.83 ? 327 GLY B O      1 
ATOM   5048 N N      . ILE B 1 334 ? 30.792 10.611  58.374  1.00 26.60 ? 328 ILE B N      1 
ATOM   5049 C CA     . ILE B 1 334 ? 31.740 10.822  59.463  1.00 26.50 ? 328 ILE B CA     1 
ATOM   5050 C C      . ILE B 1 334 ? 31.047 10.621  60.802  1.00 26.97 ? 328 ILE B C      1 
ATOM   5051 O O      . ILE B 1 334 ? 31.567 9.940   61.692  1.00 30.65 ? 328 ILE B O      1 
ATOM   5052 C CB     . ILE B 1 334 ? 32.384 12.218  59.361  1.00 29.44 ? 328 ILE B CB     1 
ATOM   5053 C CG1    . ILE B 1 334 ? 33.363 12.272  58.187  1.00 29.95 ? 328 ILE B CG1    1 
ATOM   5054 C CG2    . ILE B 1 334 ? 33.108 12.571  60.662  1.00 31.41 ? 328 ILE B CG2    1 
ATOM   5055 C CD1    . ILE B 1 334 ? 33.798 13.679  57.811  1.00 32.65 ? 328 ILE B CD1    1 
ATOM   5056 N N      . GLU B 1 335 ? 29.846 11.185  60.947  1.00 28.70 ? 329 GLU B N      1 
ATOM   5057 C CA     . GLU B 1 335 ? 29.108 11.092  62.205  1.00 31.48 ? 329 GLU B CA     1 
ATOM   5058 C C      . GLU B 1 335 ? 28.732 9.647   62.523  1.00 30.20 ? 329 GLU B C      1 
ATOM   5059 O O      . GLU B 1 335 ? 28.820 9.215   63.679  1.00 30.30 ? 329 GLU B O      1 
ATOM   5060 C CB     . GLU B 1 335 ? 27.866 11.980  62.118  1.00 30.09 ? 329 GLU B CB     1 
ATOM   5061 C CG     . GLU B 1 335 ? 27.003 12.022  63.357  1.00 46.71 ? 329 GLU B CG     1 
ATOM   5062 C CD     . GLU B 1 335 ? 25.731 12.835  63.158  1.00 61.50 ? 329 GLU B CD     1 
ATOM   5063 O OE1    . GLU B 1 335 ? 24.870 12.423  62.349  1.00 50.72 ? 329 GLU B OE1    1 
ATOM   5064 O OE2    . GLU B 1 335 ? 25.585 13.882  63.827  1.00 65.54 ? 329 GLU B OE2    1 
ATOM   5065 N N      . ALA B 1 336 ? 28.310 8.884   61.509  1.00 28.68 ? 330 ALA B N      1 
ATOM   5066 C CA     . ALA B 1 336 ? 27.911 7.496   61.735  1.00 26.24 ? 330 ALA B CA     1 
ATOM   5067 C C      . ALA B 1 336 ? 29.057 6.675   62.313  1.00 28.95 ? 330 ALA B C      1 
ATOM   5068 O O      . ALA B 1 336 ? 28.861 5.893   63.250  1.00 31.26 ? 330 ALA B O      1 
ATOM   5069 C CB     . ALA B 1 336 ? 27.425 6.872   60.425  1.00 27.13 ? 330 ALA B CB     1 
ATOM   5070 N N      . VAL B 1 337 ? 30.260 6.827   61.762  1.00 27.52 ? 331 VAL B N      1 
ATOM   5071 C CA     . VAL B 1 337 ? 31.390 6.058   62.268  1.00 26.28 ? 331 VAL B CA     1 
ATOM   5072 C C      . VAL B 1 337 ? 31.848 6.592   63.623  1.00 32.77 ? 331 VAL B C      1 
ATOM   5073 O O      . VAL B 1 337 ? 32.172 5.816   64.531  1.00 30.19 ? 331 VAL B O      1 
ATOM   5074 C CB     . VAL B 1 337 ? 32.523 6.016   61.232  1.00 27.04 ? 331 VAL B CB     1 
ATOM   5075 C CG1    . VAL B 1 337 ? 33.695 5.228   61.771  1.00 29.76 ? 331 VAL B CG1    1 
ATOM   5076 C CG2    . VAL B 1 337 ? 32.002 5.396   59.923  1.00 25.86 ? 331 VAL B CG2    1 
ATOM   5077 N N      . ALA B 1 338 ? 31.875 7.918   63.785  1.00 27.87 ? 332 ALA B N      1 
ATOM   5078 C CA     . ALA B 1 338 ? 32.332 8.499   65.047  1.00 29.43 ? 332 ALA B CA     1 
ATOM   5079 C C      . ALA B 1 338 ? 31.419 8.114   66.205  1.00 33.78 ? 332 ALA B C      1 
ATOM   5080 O O      . ALA B 1 338 ? 31.891 7.871   67.324  1.00 36.10 ? 332 ALA B O      1 
ATOM   5081 C CB     . ALA B 1 338 ? 32.425 10.019  64.922  1.00 33.43 ? 332 ALA B CB     1 
ATOM   5082 N N      . GLN B 1 339 ? 30.113 8.058   65.961  1.00 29.74 ? 333 GLN B N      1 
ATOM   5083 C CA     . GLN B 1 339 ? 29.130 7.764   66.999  1.00 35.17 ? 333 GLN B CA     1 
ATOM   5084 C C      . GLN B 1 339 ? 28.894 6.274   67.206  1.00 34.54 ? 333 GLN B C      1 
ATOM   5085 O O      . GLN B 1 339 ? 28.074 5.904   68.058  1.00 33.44 ? 333 GLN B O      1 
ATOM   5086 C CB     . GLN B 1 339 ? 27.806 8.457   66.677  1.00 34.52 ? 333 GLN B CB     1 
ATOM   5087 C CG     . GLN B 1 339 ? 27.880 9.967   66.731  1.00 35.93 ? 333 GLN B CG     1 
ATOM   5088 C CD     . GLN B 1 339 ? 26.559 10.623  66.375  1.00 57.73 ? 333 GLN B CD     1 
ATOM   5089 O OE1    . GLN B 1 339 ? 25.603 9.948   65.988  1.00 59.26 ? 333 GLN B OE1    1 
ATOM   5090 N NE2    . GLN B 1 339 ? 26.491 11.944  66.529  1.00 56.19 ? 333 GLN B NE2    1 
ATOM   5091 N N      . GLY B 1 340 ? 29.595 5.416   66.467  1.00 32.71 ? 334 GLY B N      1 
ATOM   5092 C CA     . GLY B 1 340 ? 29.409 3.985   66.563  1.00 29.08 ? 334 GLY B CA     1 
ATOM   5093 C C      . GLY B 1 340 ? 28.170 3.445   65.891  1.00 30.20 ? 334 GLY B C      1 
ATOM   5094 O O      . GLY B 1 340 ? 27.796 2.296   66.152  1.00 33.80 ? 334 GLY B O      1 
ATOM   5095 N N      . ASP B 1 341 ? 27.511 4.235   65.033  1.00 28.62 ? 335 ASP B N      1 
ATOM   5096 C CA     . ASP B 1 341 ? 26.308 3.767   64.351  1.00 26.76 ? 335 ASP B CA     1 
ATOM   5097 C C      . ASP B 1 341 ? 26.615 2.763   63.240  1.00 31.74 ? 335 ASP B C      1 
ATOM   5098 O O      . ASP B 1 341 ? 25.715 2.027   62.818  1.00 30.11 ? 335 ASP B O      1 
ATOM   5099 C CB     . ASP B 1 341 ? 25.564 4.946   63.725  1.00 37.47 ? 335 ASP B CB     1 
ATOM   5100 C CG     . ASP B 1 341 ? 24.938 5.864   64.752  1.00 43.39 ? 335 ASP B CG     1 
ATOM   5101 O OD1    . ASP B 1 341 ? 24.816 5.466   65.933  1.00 45.28 ? 335 ASP B OD1    1 
ATOM   5102 O OD2    . ASP B 1 341 ? 24.572 6.998   64.372  1.00 47.15 ? 335 ASP B OD2    1 
ATOM   5103 N N      . ALA B 1 342 ? 27.845 2.735   62.736  1.00 24.21 ? 336 ALA B N      1 
ATOM   5104 C CA     . ALA B 1 342 ? 28.219 1.798   61.687  1.00 23.00 ? 336 ALA B CA     1 
ATOM   5105 C C      . ALA B 1 342 ? 29.731 1.700   61.634  1.00 23.95 ? 336 ALA B C      1 
ATOM   5106 O O      . ALA B 1 342 ? 30.447 2.598   62.085  1.00 27.71 ? 336 ALA B O      1 
ATOM   5107 C CB     . ALA B 1 342 ? 27.688 2.236   60.319  1.00 26.71 ? 336 ALA B CB     1 
ATOM   5108 N N      . ASP B 1 343 ? 30.207 0.594   61.065  1.00 21.58 ? 337 ASP B N      1 
ATOM   5109 C CA     . ASP B 1 343 ? 31.637 0.427   60.835  1.00 20.64 ? 337 ASP B CA     1 
ATOM   5110 C C      . ASP B 1 343 ? 32.061 0.931   59.470  1.00 21.11 ? 337 ASP B C      1 
ATOM   5111 O O      . ASP B 1 343 ? 33.190 1.418   59.319  1.00 20.74 ? 337 ASP B O      1 
ATOM   5112 C CB     . ASP B 1 343 ? 32.016 -1.048  60.966  1.00 22.49 ? 337 ASP B CB     1 
ATOM   5113 C CG     . ASP B 1 343 ? 31.567 -1.631  62.283  1.00 23.39 ? 337 ASP B CG     1 
ATOM   5114 O OD1    . ASP B 1 343 ? 32.086 -1.185  63.330  1.00 26.59 ? 337 ASP B OD1    1 
ATOM   5115 O OD2    . ASP B 1 343 ? 30.676 -2.508  62.284  1.00 22.73 ? 337 ASP B OD2    1 
ATOM   5116 N N      . LEU B 1 344 ? 31.181 0.821   58.478  1.00 22.12 ? 338 LEU B N      1 
ATOM   5117 C CA     . LEU B 1 344 ? 31.470 1.241   57.112  1.00 19.68 ? 338 LEU B CA     1 
ATOM   5118 C C      . LEU B 1 344 ? 30.237 1.956   56.580  1.00 19.79 ? 338 LEU B C      1 
ATOM   5119 O O      . LEU B 1 344 ? 29.116 1.693   57.023  1.00 20.72 ? 338 LEU B O      1 
ATOM   5120 C CB     . LEU B 1 344 ? 31.779 0.031   56.213  1.00 23.12 ? 338 LEU B CB     1 
ATOM   5121 C CG     . LEU B 1 344 ? 32.919 -0.892  56.667  1.00 21.92 ? 338 LEU B CG     1 
ATOM   5122 C CD1    . LEU B 1 344 ? 32.883 -2.221  55.923  1.00 25.19 ? 338 LEU B CD1    1 
ATOM   5123 C CD2    . LEU B 1 344 ? 34.286 -0.224  56.530  1.00 25.38 ? 338 LEU B CD2    1 
ATOM   5124 N N      . VAL B 1 345 ? 30.448 2.850   55.612  1.00 20.19 ? 339 VAL B N      1 
ATOM   5125 C CA     . VAL B 1 345 ? 29.385 3.678   55.050  1.00 21.72 ? 339 VAL B CA     1 
ATOM   5126 C C      . VAL B 1 345 ? 29.444 3.518   53.535  1.00 18.56 ? 339 VAL B C      1 
ATOM   5127 O O      . VAL B 1 345 ? 30.489 3.780   52.922  1.00 19.83 ? 339 VAL B O      1 
ATOM   5128 C CB     . VAL B 1 345 ? 29.556 5.161   55.432  1.00 19.58 ? 339 VAL B CB     1 
ATOM   5129 C CG1    . VAL B 1 345 ? 28.430 6.000   54.844  1.00 23.84 ? 339 VAL B CG1    1 
ATOM   5130 C CG2    . VAL B 1 345 ? 29.643 5.341   56.970  1.00 19.30 ? 339 VAL B CG2    1 
ATOM   5131 N N      . SER B 1 346 ? 28.342 3.094   52.926  1.00 20.06 ? 340 SER B N      1 
ATOM   5132 C CA     . SER B 1 346 ? 28.316 2.926   51.479  1.00 17.11 ? 340 SER B CA     1 
ATOM   5133 C C      . SER B 1 346 ? 27.619 4.105   50.812  1.00 20.49 ? 340 SER B C      1 
ATOM   5134 O O      . SER B 1 346 ? 26.638 4.648   51.335  1.00 21.68 ? 340 SER B O      1 
ATOM   5135 C CB     . SER B 1 346 ? 27.709 1.584   51.062  1.00 22.74 ? 340 SER B CB     1 
ATOM   5136 O OG     . SER B 1 346 ? 26.309 1.542   51.276  1.00 23.97 ? 340 SER B OG     1 
ATOM   5137 N N      . TYR B 1 347 ? 28.170 4.525   49.676  1.00 21.90 ? 341 TYR B N      1 
ATOM   5138 C CA     . TYR B 1 347 ? 27.657 5.641   48.895  1.00 21.51 ? 341 TYR B CA     1 
ATOM   5139 C C      . TYR B 1 347 ? 27.275 5.129   47.518  1.00 21.21 ? 341 TYR B C      1 
ATOM   5140 O O      . TYR B 1 347 ? 28.050 4.405   46.879  1.00 21.30 ? 341 TYR B O      1 
ATOM   5141 C CB     . TYR B 1 347 ? 28.698 6.755   48.773  1.00 19.81 ? 341 TYR B CB     1 
ATOM   5142 C CG     . TYR B 1 347 ? 29.025 7.413   50.100  1.00 21.76 ? 341 TYR B CG     1 
ATOM   5143 C CD1    . TYR B 1 347 ? 29.985 6.876   50.954  1.00 22.69 ? 341 TYR B CD1    1 
ATOM   5144 C CD2    . TYR B 1 347 ? 28.369 8.572   50.489  1.00 24.39 ? 341 TYR B CD2    1 
ATOM   5145 C CE1    . TYR B 1 347 ? 30.278 7.489   52.176  1.00 22.86 ? 341 TYR B CE1    1 
ATOM   5146 C CE2    . TYR B 1 347 ? 28.645 9.185   51.708  1.00 23.74 ? 341 TYR B CE2    1 
ATOM   5147 C CZ     . TYR B 1 347 ? 29.604 8.643   52.542  1.00 22.17 ? 341 TYR B CZ     1 
ATOM   5148 O OH     . TYR B 1 347 ? 29.885 9.252   53.753  1.00 24.02 ? 341 TYR B OH     1 
ATOM   5149 N N      . GLY B 1 348 ? 26.074 5.491   47.079  1.00 19.56 ? 342 GLY B N      1 
ATOM   5150 C CA     . GLY B 1 348 ? 25.598 5.135   45.757  1.00 22.42 ? 342 GLY B CA     1 
ATOM   5151 C C      . GLY B 1 348 ? 25.672 6.267   44.750  1.00 21.51 ? 342 GLY B C      1 
ATOM   5152 O O      . GLY B 1 348 ? 26.629 6.361   43.980  1.00 21.95 ? 342 GLY B O      1 
ATOM   5153 N N      . ARG B 1 349 ? 24.666 7.146   44.759  1.00 24.15 ? 343 ARG B N      1 
ATOM   5154 C CA     . ARG B 1 349 ? 24.538 8.141   43.695  1.00 23.39 ? 343 ARG B CA     1 
ATOM   5155 C C      . ARG B 1 349 ? 25.773 9.034   43.572  1.00 23.35 ? 343 ARG B C      1 
ATOM   5156 O O      . ARG B 1 349 ? 26.192 9.363   42.457  1.00 22.16 ? 343 ARG B O      1 
ATOM   5157 C CB     . ARG B 1 349 ? 23.255 8.955   43.884  1.00 22.27 ? 343 ARG B CB     1 
ATOM   5158 C CG     . ARG B 1 349 ? 22.005 8.154   43.534  1.00 25.87 ? 343 ARG B CG     1 
ATOM   5159 C CD     . ARG B 1 349 ? 20.747 8.782   44.094  1.00 28.27 ? 343 ARG B CD     1 
ATOM   5160 N NE     . ARG B 1 349 ? 20.728 8.749   45.549  1.00 27.76 ? 343 ARG B NE     1 
ATOM   5161 C CZ     . ARG B 1 349 ? 19.820 9.370   46.285  1.00 31.78 ? 343 ARG B CZ     1 
ATOM   5162 N NH1    . ARG B 1 349 ? 18.843 10.069  45.727  1.00 33.60 ? 343 ARG B NH1    1 
ATOM   5163 N NH2    . ARG B 1 349 ? 19.890 9.285   47.611  1.00 31.97 ? 343 ARG B NH2    1 
ATOM   5164 N N      . LEU B 1 350 ? 26.375 9.445   44.694  1.00 24.55 ? 344 LEU B N      1 
ATOM   5165 C CA     . LEU B 1 350 ? 27.558 10.299  44.588  1.00 20.25 ? 344 LEU B CA     1 
ATOM   5166 C C      . LEU B 1 350 ? 28.753 9.560   43.997  1.00 19.99 ? 344 LEU B C      1 
ATOM   5167 O O      . LEU B 1 350 ? 29.636 10.194  43.408  1.00 22.24 ? 344 LEU B O      1 
ATOM   5168 C CB     . LEU B 1 350 ? 27.927 10.906  45.939  1.00 26.16 ? 344 LEU B CB     1 
ATOM   5169 C CG     . LEU B 1 350 ? 26.936 11.917  46.509  1.00 30.46 ? 344 LEU B CG     1 
ATOM   5170 C CD1    . LEU B 1 350 ? 27.347 12.258  47.924  1.00 27.62 ? 344 LEU B CD1    1 
ATOM   5171 C CD2    . LEU B 1 350 ? 26.887 13.164  45.657  1.00 31.24 ? 344 LEU B CD2    1 
ATOM   5172 N N      . PHE B 1 351 ? 28.799 8.233   44.143  1.00 21.71 ? 345 PHE B N      1 
ATOM   5173 C CA     . PHE B 1 351 ? 29.865 7.451   43.527  1.00 22.30 ? 345 PHE B CA     1 
ATOM   5174 C C      . PHE B 1 351 ? 29.662 7.302   42.024  1.00 24.05 ? 345 PHE B C      1 
ATOM   5175 O O      . PHE B 1 351 ? 30.637 7.060   41.302  1.00 23.25 ? 345 PHE B O      1 
ATOM   5176 C CB     . PHE B 1 351 ? 29.947 6.073   44.188  1.00 25.40 ? 345 PHE B CB     1 
ATOM   5177 C CG     . PHE B 1 351 ? 31.297 5.746   44.782  1.00 22.31 ? 345 PHE B CG     1 
ATOM   5178 C CD1    . PHE B 1 351 ? 32.461 5.952   44.064  1.00 21.36 ? 345 PHE B CD1    1 
ATOM   5179 C CD2    . PHE B 1 351 ? 31.390 5.210   46.061  1.00 21.25 ? 345 PHE B CD2    1 
ATOM   5180 C CE1    . PHE B 1 351 ? 33.711 5.637   44.628  1.00 21.90 ? 345 PHE B CE1    1 
ATOM   5181 C CE2    . PHE B 1 351 ? 32.631 4.891   46.621  1.00 22.91 ? 345 PHE B CE2    1 
ATOM   5182 C CZ     . PHE B 1 351 ? 33.784 5.099   45.898  1.00 23.03 ? 345 PHE B CZ     1 
ATOM   5183 N N      . ILE B 1 352 ? 28.420 7.436   41.540  1.00 21.47 ? 346 ILE B N      1 
ATOM   5184 C CA     . ILE B 1 352 ? 28.183 7.467   40.097  1.00 21.59 ? 346 ILE B CA     1 
ATOM   5185 C C      . ILE B 1 352 ? 28.964 8.606   39.454  1.00 22.46 ? 346 ILE B C      1 
ATOM   5186 O O      . ILE B 1 352 ? 29.655 8.421   38.442  1.00 23.62 ? 346 ILE B O      1 
ATOM   5187 C CB     . ILE B 1 352 ? 26.676 7.580   39.798  1.00 20.62 ? 346 ILE B CB     1 
ATOM   5188 C CG1    . ILE B 1 352 ? 25.954 6.280   40.147  1.00 25.95 ? 346 ILE B CG1    1 
ATOM   5189 C CG2    . ILE B 1 352 ? 26.462 7.953   38.319  1.00 22.36 ? 346 ILE B CG2    1 
ATOM   5190 C CD1    . ILE B 1 352 ? 24.434 6.346   39.976  1.00 26.70 ? 346 ILE B CD1    1 
ATOM   5191 N N      . SER B 1 353 ? 28.883 9.799   40.044  1.00 21.76 ? 347 SER B N      1 
ATOM   5192 C CA     . SER B 1 353 ? 29.397 11.003  39.405  1.00 21.50 ? 347 SER B CA     1 
ATOM   5193 C C      . SER B 1 353 ? 30.744 11.455  39.947  1.00 22.58 ? 347 SER B C      1 
ATOM   5194 O O      . SER B 1 353 ? 31.322 12.410  39.412  1.00 23.17 ? 347 SER B O      1 
ATOM   5195 C CB     . SER B 1 353 ? 28.391 12.151  39.536  1.00 22.86 ? 347 SER B CB     1 
ATOM   5196 O OG     . SER B 1 353 ? 28.042 12.353  40.889  1.00 23.45 ? 347 SER B OG     1 
ATOM   5197 N N      . ASN B 1 354 ? 31.263 10.801  40.983  1.00 24.37 ? 348 ASN B N      1 
ATOM   5198 C CA     . ASN B 1 354 ? 32.557 11.156  41.561  1.00 22.86 ? 348 ASN B CA     1 
ATOM   5199 C C      . ASN B 1 354 ? 33.399 9.893   41.595  1.00 24.85 ? 348 ASN B C      1 
ATOM   5200 O O      . ASN B 1 354 ? 33.368 9.143   42.582  1.00 23.48 ? 348 ASN B O      1 
ATOM   5201 C CB     . ASN B 1 354 ? 32.387 11.759  42.953  1.00 20.72 ? 348 ASN B CB     1 
ATOM   5202 C CG     . ASN B 1 354 ? 31.636 13.063  42.909  1.00 22.27 ? 348 ASN B CG     1 
ATOM   5203 O OD1    . ASN B 1 354 ? 32.228 14.118  42.712  1.00 24.07 ? 348 ASN B OD1    1 
ATOM   5204 N ND2    . ASN B 1 354 ? 30.310 12.993  43.043  1.00 22.09 ? 348 ASN B ND2    1 
ATOM   5205 N N      . PRO B 1 355 ? 34.151 9.613   40.528  1.00 24.10 ? 349 PRO B N      1 
ATOM   5206 C CA     . PRO B 1 355 ? 34.942 8.376   40.519  1.00 21.04 ? 349 PRO B CA     1 
ATOM   5207 C C      . PRO B 1 355 ? 35.933 8.343   41.658  1.00 24.91 ? 349 PRO B C      1 
ATOM   5208 O O      . PRO B 1 355 ? 36.175 7.283   42.241  1.00 23.20 ? 349 PRO B O      1 
ATOM   5209 C CB     . PRO B 1 355 ? 35.634 8.399   39.145  1.00 24.32 ? 349 PRO B CB     1 
ATOM   5210 C CG     . PRO B 1 355 ? 35.593 9.845   38.714  1.00 26.20 ? 349 PRO B CG     1 
ATOM   5211 C CD     . PRO B 1 355 ? 34.285 10.357  39.259  1.00 22.54 ? 349 PRO B CD     1 
ATOM   5212 N N      . ASP B 1 356 ? 36.485 9.502   42.006  1.00 22.41 ? 350 ASP B N      1 
ATOM   5213 C CA     . ASP B 1 356 ? 37.382 9.655   43.144  1.00 22.73 ? 350 ASP B CA     1 
ATOM   5214 C C      . ASP B 1 356 ? 36.642 10.129  44.391  1.00 25.05 ? 350 ASP B C      1 
ATOM   5215 O O      . ASP B 1 356 ? 37.134 10.992  45.118  1.00 24.84 ? 350 ASP B O      1 
ATOM   5216 C CB     . ASP B 1 356 ? 38.548 10.579  42.790  1.00 25.74 ? 350 ASP B CB     1 
ATOM   5217 C CG     . ASP B 1 356 ? 38.103 11.891  42.145  1.00 28.29 ? 350 ASP B CG     1 
ATOM   5218 O OD1    . ASP B 1 356 ? 36.889 12.072  41.878  1.00 26.40 ? 350 ASP B OD1    1 
ATOM   5219 O OD2    . ASP B 1 356 ? 38.991 12.740  41.883  1.00 29.01 ? 350 ASP B OD2    1 
ATOM   5220 N N      . LEU B 1 357 ? 35.451 9.574   44.652  1.00 23.04 ? 351 LEU B N      1 
ATOM   5221 C CA     . LEU B 1 357 ? 34.670 9.975   45.823  1.00 23.43 ? 351 LEU B CA     1 
ATOM   5222 C C      . LEU B 1 357 ? 35.470 9.832   47.111  1.00 24.09 ? 351 LEU B C      1 
ATOM   5223 O O      . LEU B 1 357 ? 35.377 10.687  47.998  1.00 25.65 ? 351 LEU B O      1 
ATOM   5224 C CB     . LEU B 1 357 ? 33.361 9.184   45.910  1.00 22.59 ? 351 LEU B CB     1 
ATOM   5225 C CG     . LEU B 1 357 ? 32.472 9.594   47.096  1.00 23.10 ? 351 LEU B CG     1 
ATOM   5226 C CD1    . LEU B 1 357 ? 32.116 11.074  47.046  1.00 25.33 ? 351 LEU B CD1    1 
ATOM   5227 C CD2    . LEU B 1 357 ? 31.215 8.740   47.185  1.00 23.32 ? 351 LEU B CD2    1 
ATOM   5228 N N      . VAL B 1 358 ? 36.262 8.764   47.236  1.00 22.58 ? 352 VAL B N      1 
ATOM   5229 C CA     . VAL B 1 358 ? 37.022 8.560   48.473  1.00 26.17 ? 352 VAL B CA     1 
ATOM   5230 C C      . VAL B 1 358 ? 37.959 9.736   48.713  1.00 27.58 ? 352 VAL B C      1 
ATOM   5231 O O      . VAL B 1 358 ? 37.993 10.318  49.806  1.00 25.68 ? 352 VAL B O      1 
ATOM   5232 C CB     . VAL B 1 358 ? 37.784 7.222   48.430  1.00 25.83 ? 352 VAL B CB     1 
ATOM   5233 C CG1    . VAL B 1 358 ? 38.592 7.020   49.716  1.00 26.76 ? 352 VAL B CG1    1 
ATOM   5234 C CG2    . VAL B 1 358 ? 36.825 6.055   48.192  1.00 27.31 ? 352 VAL B CG2    1 
ATOM   5235 N N      . MET B 1 359 ? 38.711 10.120  47.679  1.00 25.28 ? 353 MET B N      1 
ATOM   5236 C CA     . MET B 1 359 ? 39.652 11.226  47.807  1.00 26.24 ? 353 MET B CA     1 
ATOM   5237 C C      . MET B 1 359 ? 38.924 12.541  48.073  1.00 29.77 ? 353 MET B C      1 
ATOM   5238 O O      . MET B 1 359 ? 39.396 13.369  48.858  1.00 29.56 ? 353 MET B O      1 
ATOM   5239 C CB     . MET B 1 359 ? 40.505 11.311  46.537  1.00 29.46 ? 353 MET B CB     1 
ATOM   5240 C CG     . MET B 1 359 ? 41.479 12.468  46.490  1.00 32.58 ? 353 MET B CG     1 
ATOM   5241 S SD     . MET B 1 359 ? 42.793 12.324  47.728  1.00 50.54 ? 353 MET B SD     1 
ATOM   5242 C CE     . MET B 1 359 ? 43.084 10.552  47.766  1.00 43.58 ? 353 MET B CE     1 
ATOM   5243 N N      . ARG B 1 360 ? 37.765 12.749  47.440  1.00 26.20 ? 354 ARG B N      1 
ATOM   5244 C CA     . ARG B 1 360 ? 37.006 13.970  47.696  1.00 25.41 ? 354 ARG B CA     1 
ATOM   5245 C C      . ARG B 1 360 ? 36.498 14.018  49.134  1.00 28.31 ? 354 ARG B C      1 
ATOM   5246 O O      . ARG B 1 360 ? 36.458 15.089  49.752  1.00 29.58 ? 354 ARG B O      1 
ATOM   5247 C CB     . ARG B 1 360 ? 35.852 14.086  46.705  1.00 23.99 ? 354 ARG B CB     1 
ATOM   5248 C CG     . ARG B 1 360 ? 36.313 14.366  45.285  1.00 24.72 ? 354 ARG B CG     1 
ATOM   5249 C CD     . ARG B 1 360 ? 35.130 14.632  44.388  1.00 26.74 ? 354 ARG B CD     1 
ATOM   5250 N NE     . ARG B 1 360 ? 35.485 14.391  42.997  1.00 26.13 ? 354 ARG B NE     1 
ATOM   5251 C CZ     . ARG B 1 360 ? 35.247 15.227  41.997  1.00 27.53 ? 354 ARG B CZ     1 
ATOM   5252 N NH1    . ARG B 1 360 ? 34.658 16.395  42.194  1.00 27.90 ? 354 ARG B NH1    1 
ATOM   5253 N NH2    . ARG B 1 360 ? 35.610 14.881  40.767  1.00 25.83 ? 354 ARG B NH2    1 
ATOM   5254 N N      . ILE B 1 361 ? 36.098 12.871  49.683  1.00 24.19 ? 355 ILE B N      1 
ATOM   5255 C CA     . ILE B 1 361 ? 35.699 12.842  51.086  1.00 26.48 ? 355 ILE B CA     1 
ATOM   5256 C C      . ILE B 1 361 ? 36.896 13.156  51.978  1.00 26.30 ? 355 ILE B C      1 
ATOM   5257 O O      . ILE B 1 361 ? 36.777 13.899  52.963  1.00 29.69 ? 355 ILE B O      1 
ATOM   5258 C CB     . ILE B 1 361 ? 35.021 11.498  51.418  1.00 23.90 ? 355 ILE B CB     1 
ATOM   5259 C CG1    . ILE B 1 361 ? 33.620 11.460  50.800  1.00 26.13 ? 355 ILE B CG1    1 
ATOM   5260 C CG2    . ILE B 1 361 ? 34.924 11.279  52.930  1.00 25.75 ? 355 ILE B CG2    1 
ATOM   5261 C CD1    . ILE B 1 361 ? 32.974 10.084  50.813  1.00 27.74 ? 355 ILE B CD1    1 
ATOM   5262 N N      . LYS B 1 362 ? 38.078 12.641  51.622  1.00 27.20 ? 356 LYS B N      1 
ATOM   5263 C CA     . LYS B 1 362 ? 39.256 12.878  52.456  1.00 27.90 ? 356 LYS B CA     1 
ATOM   5264 C C      . LYS B 1 362 ? 39.671 14.344  52.430  1.00 35.26 ? 356 LYS B C      1 
ATOM   5265 O O      . LYS B 1 362 ? 40.052 14.907  53.464  1.00 34.54 ? 356 LYS B O      1 
ATOM   5266 C CB     . LYS B 1 362 ? 40.400 11.959  52.030  1.00 34.08 ? 356 LYS B CB     1 
ATOM   5267 C CG     . LYS B 1 362 ? 41.617 11.997  52.956  1.00 37.55 ? 356 LYS B CG     1 
ATOM   5268 C CD     . LYS B 1 362 ? 42.897 11.934  52.159  1.00 42.33 ? 356 LYS B CD     1 
ATOM   5269 C CE     . LYS B 1 362 ? 43.390 13.318  51.783  1.00 59.12 ? 356 LYS B CE     1 
ATOM   5270 N NZ     . LYS B 1 362 ? 44.834 13.327  51.403  1.00 64.42 ? 356 LYS B NZ     1 
ATOM   5271 N N      . LEU B 1 363 ? 39.578 14.983  51.268  1.00 29.58 ? 357 LEU B N      1 
ATOM   5272 C CA     . LEU B 1 363 ? 39.942 16.382  51.092  1.00 29.46 ? 357 LEU B CA     1 
ATOM   5273 C C      . LEU B 1 363 ? 38.808 17.345  51.403  1.00 31.36 ? 357 LEU B C      1 
ATOM   5274 O O      . LEU B 1 363 ? 39.050 18.557  51.456  1.00 35.07 ? 357 LEU B O      1 
ATOM   5275 C CB     . LEU B 1 363 ? 40.373 16.614  49.640  1.00 26.92 ? 357 LEU B CB     1 
ATOM   5276 C CG     . LEU B 1 363 ? 41.653 15.892  49.239  1.00 31.16 ? 357 LEU B CG     1 
ATOM   5277 C CD1    . LEU B 1 363 ? 41.966 16.139  47.769  1.00 34.76 ? 357 LEU B CD1    1 
ATOM   5278 C CD2    . LEU B 1 363 ? 42.799 16.376  50.108  1.00 39.38 ? 357 LEU B CD2    1 
ATOM   5279 N N      . ASN B 1 364 ? 37.587 16.845  51.596  1.00 28.32 ? 358 ASN B N      1 
ATOM   5280 C CA     . ASN B 1 364 ? 36.396 17.692  51.629  1.00 28.55 ? 358 ASN B CA     1 
ATOM   5281 C C      . ASN B 1 364 ? 36.325 18.566  50.379  1.00 30.53 ? 358 ASN B C      1 
ATOM   5282 O O      . ASN B 1 364 ? 36.027 19.762  50.439  1.00 31.84 ? 358 ASN B O      1 
ATOM   5283 C CB     . ASN B 1 364 ? 36.295 18.521  52.913  1.00 32.69 ? 358 ASN B CB     1 
ATOM   5284 C CG     . ASN B 1 364 ? 34.894 19.061  53.145  1.00 35.73 ? 358 ASN B CG     1 
ATOM   5285 O OD1    . ASN B 1 364 ? 33.943 18.668  52.465  1.00 36.28 ? 358 ASN B OD1    1 
ATOM   5286 N ND2    . ASN B 1 364 ? 34.761 19.977  54.095  1.00 42.59 ? 358 ASN B ND2    1 
ATOM   5287 N N      . ALA B 1 365 ? 36.619 17.953  49.232  1.00 30.03 ? 359 ALA B N      1 
ATOM   5288 C CA     . ALA B 1 365 ? 36.546 18.618  47.946  1.00 29.78 ? 359 ALA B CA     1 
ATOM   5289 C C      . ALA B 1 365 ? 35.110 18.599  47.431  1.00 28.08 ? 359 ALA B C      1 
ATOM   5290 O O      . ALA B 1 365 ? 34.345 17.683  47.743  1.00 29.59 ? 359 ALA B O      1 
ATOM   5291 C CB     . ALA B 1 365 ? 37.446 17.900  46.944  1.00 28.01 ? 359 ALA B CB     1 
ATOM   5292 N N      . PRO B 1 366 ? 34.717 19.605  46.645  1.00 29.74 ? 360 PRO B N      1 
ATOM   5293 C CA     . PRO B 1 366 ? 33.338 19.652  46.137  1.00 28.66 ? 360 PRO B CA     1 
ATOM   5294 C C      . PRO B 1 366 ? 33.029 18.476  45.216  1.00 30.32 ? 360 PRO B C      1 
ATOM   5295 O O      . PRO B 1 366 ? 33.890 17.988  44.482  1.00 32.61 ? 360 PRO B O      1 
ATOM   5296 C CB     . PRO B 1 366 ? 33.285 20.979  45.368  1.00 31.00 ? 360 PRO B CB     1 
ATOM   5297 C CG     . PRO B 1 366 ? 34.466 21.768  45.842  1.00 37.12 ? 360 PRO B CG     1 
ATOM   5298 C CD     . PRO B 1 366 ? 35.508 20.778  46.237  1.00 32.26 ? 360 PRO B CD     1 
ATOM   5299 N N      . LEU B 1 367 ? 31.773 18.040  45.244  1.00 27.07 ? 361 LEU B N      1 
ATOM   5300 C CA     . LEU B 1 367 ? 31.335 16.857  44.515  1.00 25.44 ? 361 LEU B CA     1 
ATOM   5301 C C      . LEU B 1 367 ? 30.640 17.230  43.211  1.00 26.32 ? 361 LEU B C      1 
ATOM   5302 O O      . LEU B 1 367 ? 30.026 18.296  43.094  1.00 24.84 ? 361 LEU B O      1 
ATOM   5303 C CB     . LEU B 1 367 ? 30.369 16.027  45.364  1.00 26.10 ? 361 LEU B CB     1 
ATOM   5304 C CG     . LEU B 1 367 ? 30.843 15.694  46.782  1.00 23.79 ? 361 LEU B CG     1 
ATOM   5305 C CD1    . LEU B 1 367 ? 29.777 14.912  47.521  1.00 30.45 ? 361 LEU B CD1    1 
ATOM   5306 C CD2    . LEU B 1 367 ? 32.158 14.927  46.741  1.00 29.33 ? 361 LEU B CD2    1 
ATOM   5307 N N      . ASN B 1 368 ? 30.722 16.317  42.241  1.00 25.21 ? 362 ASN B N      1 
ATOM   5308 C CA     . ASN B 1 368 ? 30.055 16.480  40.953  1.00 23.19 ? 362 ASN B CA     1 
ATOM   5309 C C      . ASN B 1 368 ? 28.606 16.034  41.031  1.00 25.57 ? 362 ASN B C      1 
ATOM   5310 O O      . ASN B 1 368 ? 28.276 15.051  41.704  1.00 22.62 ? 362 ASN B O      1 
ATOM   5311 C CB     . ASN B 1 368 ? 30.704 15.580  39.907  1.00 24.02 ? 362 ASN B CB     1 
ATOM   5312 C CG     . ASN B 1 368 ? 32.138 15.933  39.618  1.00 25.04 ? 362 ASN B CG     1 
ATOM   5313 O OD1    . ASN B 1 368 ? 32.582 17.060  39.836  1.00 32.35 ? 362 ASN B OD1    1 
ATOM   5314 N ND2    . ASN B 1 368 ? 32.880 14.956  39.108  1.00 28.33 ? 362 ASN B ND2    1 
ATOM   5315 N N      . LYS B 1 369 ? 27.748 16.718  40.278  1.00 24.51 ? 363 LYS B N      1 
ATOM   5316 C CA     . LYS B 1 369 ? 26.369 16.278  40.140  1.00 25.45 ? 363 LYS B CA     1 
ATOM   5317 C C      . LYS B 1 369 ? 26.287 15.013  39.287  1.00 27.57 ? 363 LYS B C      1 
ATOM   5318 O O      . LYS B 1 369 ? 27.135 14.760  38.425  1.00 28.24 ? 363 LYS B O      1 
ATOM   5319 C CB     . LYS B 1 369 ? 25.519 17.389  39.526  1.00 26.74 ? 363 LYS B CB     1 
ATOM   5320 C CG     . LYS B 1 369 ? 25.629 17.527  38.022  1.00 34.64 ? 363 LYS B CG     1 
ATOM   5321 C CD     . LYS B 1 369 ? 24.254 17.839  37.442  1.00 41.35 ? 363 LYS B CD     1 
ATOM   5322 C CE     . LYS B 1 369 ? 24.098 19.314  37.125  1.00 55.03 ? 363 LYS B CE     1 
ATOM   5323 N NZ     . LYS B 1 369 ? 22.907 19.566  36.257  1.00 53.94 ? 363 LYS B NZ     1 
ATOM   5324 N N      . TYR B 1 370 ? 25.260 14.207  39.549  1.00 26.61 ? 364 TYR B N      1 
ATOM   5325 C CA     . TYR B 1 370 ? 24.990 13.012  38.765  1.00 26.12 ? 364 TYR B CA     1 
ATOM   5326 C C      . TYR B 1 370 ? 23.781 13.247  37.866  1.00 28.89 ? 364 TYR B C      1 
ATOM   5327 O O      . TYR B 1 370 ? 22.929 14.095  38.144  1.00 31.44 ? 364 TYR B O      1 
ATOM   5328 C CB     . TYR B 1 370 ? 24.753 11.797  39.666  1.00 28.81 ? 364 TYR B CB     1 
ATOM   5329 C CG     . TYR B 1 370 ? 23.786 12.008  40.809  1.00 30.92 ? 364 TYR B CG     1 
ATOM   5330 C CD1    . TYR B 1 370 ? 22.411 11.921  40.610  1.00 34.63 ? 364 TYR B CD1    1 
ATOM   5331 C CD2    . TYR B 1 370 ? 24.246 12.270  42.100  1.00 29.37 ? 364 TYR B CD2    1 
ATOM   5332 C CE1    . TYR B 1 370 ? 21.520 12.096  41.665  1.00 30.34 ? 364 TYR B CE1    1 
ATOM   5333 C CE2    . TYR B 1 370 ? 23.358 12.453  43.163  1.00 28.63 ? 364 TYR B CE2    1 
ATOM   5334 C CZ     . TYR B 1 370 ? 21.997 12.366  42.930  1.00 30.18 ? 364 TYR B CZ     1 
ATOM   5335 O OH     . TYR B 1 370 ? 21.110 12.539  43.977  1.00 37.25 ? 364 TYR B OH     1 
ATOM   5336 N N      . ASN B 1 371 ? 23.716 12.481  36.778  1.00 27.07 ? 365 ASN B N      1 
ATOM   5337 C CA     . ASN B 1 371 ? 22.680 12.645  35.759  1.00 27.51 ? 365 ASN B CA     1 
ATOM   5338 C C      . ASN B 1 371 ? 21.810 11.391  35.738  1.00 25.63 ? 365 ASN B C      1 
ATOM   5339 O O      . ASN B 1 371 ? 22.205 10.356  35.189  1.00 25.35 ? 365 ASN B O      1 
ATOM   5340 C CB     . ASN B 1 371 ? 23.321 12.932  34.408  1.00 29.32 ? 365 ASN B CB     1 
ATOM   5341 C CG     . ASN B 1 371 ? 24.307 14.083  34.482  1.00 39.82 ? 365 ASN B CG     1 
ATOM   5342 O OD1    . ASN B 1 371 ? 23.969 15.174  34.949  1.00 48.32 ? 365 ASN B OD1    1 
ATOM   5343 N ND2    . ASN B 1 371 ? 25.546 13.830  34.078  1.00 43.87 ? 365 ASN B ND2    1 
ATOM   5344 N N      . ARG B 1 372 ? 20.621 11.494  36.335  1.00 25.68 ? 366 ARG B N      1 
ATOM   5345 C CA     . ARG B 1 372 ? 19.714 10.353  36.403  1.00 23.50 ? 366 ARG B CA     1 
ATOM   5346 C C      . ARG B 1 372 ? 19.391 9.796   35.016  1.00 23.94 ? 366 ARG B C      1 
ATOM   5347 O O      . ARG B 1 372 ? 19.189 8.584   34.869  1.00 24.18 ? 366 ARG B O      1 
ATOM   5348 C CB     . ARG B 1 372 ? 18.444 10.759  37.155  1.00 28.03 ? 366 ARG B CB     1 
ATOM   5349 C CG     . ARG B 1 372 ? 17.389 9.678   37.285  1.00 29.54 ? 366 ARG B CG     1 
ATOM   5350 C CD     . ARG B 1 372 ? 16.309 10.114  38.286  1.00 39.43 ? 366 ARG B CD     1 
ATOM   5351 N NE     . ARG B 1 372 ? 16.808 10.121  39.659  1.00 47.51 ? 366 ARG B NE     1 
ATOM   5352 C CZ     . ARG B 1 372 ? 16.928 9.038   40.417  1.00 36.14 ? 366 ARG B CZ     1 
ATOM   5353 N NH1    . ARG B 1 372 ? 16.532 7.848   39.990  1.00 45.59 ? 366 ARG B NH1    1 
ATOM   5354 N NH2    . ARG B 1 372 ? 17.451 9.150   41.637  1.00 37.95 ? 366 ARG B NH2    1 
ATOM   5355 N N      . LYS B 1 373 ? 19.378 10.650  33.986  1.00 24.94 ? 367 LYS B N      1 
ATOM   5356 C CA     . LYS B 1 373 ? 19.020 10.194  32.647  1.00 27.52 ? 367 LYS B CA     1 
ATOM   5357 C C      . LYS B 1 373 ? 19.936 9.079   32.150  1.00 29.45 ? 367 LYS B C      1 
ATOM   5358 O O      . LYS B 1 373 ? 19.503 8.234   31.361  1.00 28.82 ? 367 LYS B O      1 
ATOM   5359 C CB     . LYS B 1 373 ? 19.026 11.374  31.674  1.00 29.26 ? 367 LYS B CB     1 
ATOM   5360 N N      . THR B 1 374 ? 21.191 9.041   32.608  1.00 24.35 ? 368 THR B N      1 
ATOM   5361 C CA     . THR B 1 374 ? 22.148 8.036   32.151  1.00 21.41 ? 368 THR B CA     1 
ATOM   5362 C C      . THR B 1 374 ? 22.465 6.976   33.210  1.00 23.70 ? 368 THR B C      1 
ATOM   5363 O O      . THR B 1 374 ? 23.494 6.297   33.120  1.00 21.84 ? 368 THR B O      1 
ATOM   5364 C CB     . THR B 1 374 ? 23.414 8.692   31.593  1.00 23.26 ? 368 THR B CB     1 
ATOM   5365 O OG1    . THR B 1 374 ? 23.926 9.641   32.537  1.00 26.95 ? 368 THR B OG1    1 
ATOM   5366 C CG2    . THR B 1 374 ? 23.110 9.401   30.259  1.00 24.26 ? 368 THR B CG2    1 
ATOM   5367 N N      . PHE B 1 375 ? 21.585 6.806   34.204  1.00 23.80 ? 369 PHE B N      1 
ATOM   5368 C CA     . PHE B 1 375 ? 21.772 5.738   35.186  1.00 22.85 ? 369 PHE B CA     1 
ATOM   5369 C C      . PHE B 1 375 ? 21.735 4.362   34.530  1.00 21.89 ? 369 PHE B C      1 
ATOM   5370 O O      . PHE B 1 375 ? 22.568 3.501   34.835  1.00 21.11 ? 369 PHE B O      1 
ATOM   5371 C CB     . PHE B 1 375 ? 20.681 5.809   36.255  1.00 21.51 ? 369 PHE B CB     1 
ATOM   5372 C CG     . PHE B 1 375 ? 20.944 6.814   37.350  1.00 24.87 ? 369 PHE B CG     1 
ATOM   5373 C CD1    . PHE B 1 375 ? 22.057 7.644   37.317  1.00 27.71 ? 369 PHE B CD1    1 
ATOM   5374 C CD2    . PHE B 1 375 ? 20.061 6.920   38.419  1.00 25.95 ? 369 PHE B CD2    1 
ATOM   5375 C CE1    . PHE B 1 375 ? 22.280 8.568   38.335  1.00 29.07 ? 369 PHE B CE1    1 
ATOM   5376 C CE2    . PHE B 1 375 ? 20.287 7.836   39.441  1.00 23.08 ? 369 PHE B CE2    1 
ATOM   5377 C CZ     . PHE B 1 375 ? 21.392 8.658   39.399  1.00 26.86 ? 369 PHE B CZ     1 
ATOM   5378 N N      . TYR B 1 376 ? 20.777 4.137   33.618  1.00 20.31 ? 370 TYR B N      1 
ATOM   5379 C CA     . TYR B 1 376 ? 20.448 2.797   33.132  1.00 20.15 ? 370 TYR B CA     1 
ATOM   5380 C C      . TYR B 1 376 ? 20.589 2.672   31.622  1.00 21.25 ? 370 TYR B C      1 
ATOM   5381 O O      . TYR B 1 376 ? 20.066 1.717   31.038  1.00 20.97 ? 370 TYR B O      1 
ATOM   5382 C CB     . TYR B 1 376 ? 19.040 2.369   33.542  1.00 20.65 ? 370 TYR B CB     1 
ATOM   5383 C CG     . TYR B 1 376 ? 18.754 2.520   35.018  1.00 21.16 ? 370 TYR B CG     1 
ATOM   5384 C CD1    . TYR B 1 376 ? 19.435 1.743   35.938  1.00 21.49 ? 370 TYR B CD1    1 
ATOM   5385 C CD2    . TYR B 1 376 ? 17.779 3.393   35.480  1.00 24.84 ? 370 TYR B CD2    1 
ATOM   5386 C CE1    . TYR B 1 376 ? 19.194 1.850   37.287  1.00 24.27 ? 370 TYR B CE1    1 
ATOM   5387 C CE2    . TYR B 1 376 ? 17.513 3.500   36.849  1.00 21.62 ? 370 TYR B CE2    1 
ATOM   5388 C CZ     . TYR B 1 376 ? 18.231 2.721   37.735  1.00 21.90 ? 370 TYR B CZ     1 
ATOM   5389 O OH     . TYR B 1 376 ? 17.999 2.808   39.093  1.00 23.70 ? 370 TYR B OH     1 
ATOM   5390 N N      . THR B 1 377 ? 21.258 3.623   30.991  1.00 19.59 ? 371 THR B N      1 
ATOM   5391 C CA     . THR B 1 377 ? 21.486 3.578   29.552  1.00 22.06 ? 371 THR B CA     1 
ATOM   5392 C C      . THR B 1 377 ? 22.656 2.640   29.237  1.00 20.36 ? 371 THR B C      1 
ATOM   5393 O O      . THR B 1 377 ? 23.334 2.135   30.138  1.00 22.63 ? 371 THR B O      1 
ATOM   5394 C CB     . THR B 1 377 ? 21.704 4.994   29.031  1.00 21.05 ? 371 THR B CB     1 
ATOM   5395 O OG1    . THR B 1 377 ? 22.624 5.677   29.886  1.00 24.68 ? 371 THR B OG1    1 
ATOM   5396 C CG2    . THR B 1 377 ? 20.381 5.757   29.012  1.00 23.97 ? 371 THR B CG2    1 
ATOM   5397 N N      . GLN B 1 378 ? 22.891 2.380   27.936  1.00 19.35 ? 372 GLN B N      1 
ATOM   5398 C CA     . GLN B 1 378 ? 23.819 1.316   27.545  1.00 21.87 ? 372 GLN B CA     1 
ATOM   5399 C C      . GLN B 1 378 ? 25.178 1.803   27.057  1.00 24.09 ? 372 GLN B C      1 
ATOM   5400 O O      . GLN B 1 378 ? 26.042 0.965   26.766  1.00 25.80 ? 372 GLN B O      1 
ATOM   5401 C CB     . GLN B 1 378 ? 23.204 0.407   26.470  1.00 22.69 ? 372 GLN B CB     1 
ATOM   5402 C CG     . GLN B 1 378 ? 22.283 -0.651  27.027  1.00 20.77 ? 372 GLN B CG     1 
ATOM   5403 C CD     . GLN B 1 378 ? 21.138 -0.031  27.764  1.00 22.44 ? 372 GLN B CD     1 
ATOM   5404 O OE1    . GLN B 1 378 ? 20.224 0.530   27.163  1.00 24.58 ? 372 GLN B OE1    1 
ATOM   5405 N NE2    . GLN B 1 378 ? 21.192 -0.094  29.089  1.00 19.82 ? 372 GLN B NE2    1 
ATOM   5406 N N      . ASP B 1 379 ? 25.392 3.109   26.940  1.00 25.38 ? 373 ASP B N      1 
ATOM   5407 C CA     . ASP B 1 379 ? 26.668 3.598   26.411  1.00 26.23 ? 373 ASP B CA     1 
ATOM   5408 C C      . ASP B 1 379 ? 27.827 3.226   27.326  1.00 20.88 ? 373 ASP B C      1 
ATOM   5409 O O      . ASP B 1 379 ? 27.729 3.390   28.549  1.00 24.09 ? 373 ASP B O      1 
ATOM   5410 C CB     . ASP B 1 379 ? 26.637 5.104   26.143  1.00 28.03 ? 373 ASP B CB     1 
ATOM   5411 C CG     . ASP B 1 379 ? 27.720 5.543   25.171  1.00 26.07 ? 373 ASP B CG     1 
ATOM   5412 O OD1    . ASP B 1 379 ? 28.890 5.672   25.602  1.00 23.78 ? 373 ASP B OD1    1 
ATOM   5413 O OD2    . ASP B 1 379 ? 27.401 5.817   23.988  1.00 27.47 ? 373 ASP B OD2    1 
ATOM   5414 N N      . PRO B 1 380 ? 28.944 2.728   26.781  1.00 19.74 ? 374 PRO B N      1 
ATOM   5415 C CA     . PRO B 1 380 ? 30.054 2.316   27.651  1.00 24.40 ? 374 PRO B CA     1 
ATOM   5416 C C      . PRO B 1 380 ? 30.825 3.476   28.251  1.00 23.99 ? 374 PRO B C      1 
ATOM   5417 O O      . PRO B 1 380 ? 31.641 3.241   29.150  1.00 25.72 ? 374 PRO B O      1 
ATOM   5418 C CB     . PRO B 1 380 ? 30.944 1.479   26.720  1.00 23.67 ? 374 PRO B CB     1 
ATOM   5419 C CG     . PRO B 1 380 ? 30.627 1.992   25.320  1.00 25.15 ? 374 PRO B CG     1 
ATOM   5420 C CD     . PRO B 1 380 ? 29.171 2.391   25.361  1.00 21.23 ? 374 PRO B CD     1 
ATOM   5421 N N      . VAL B 1 381 ? 30.605 4.710   27.787  1.00 21.74 ? 375 VAL B N      1 
ATOM   5422 C CA     . VAL B 1 381 ? 31.330 5.885   28.261  1.00 23.08 ? 375 VAL B CA     1 
ATOM   5423 C C      . VAL B 1 381 ? 30.385 6.942   28.824  1.00 25.80 ? 375 VAL B C      1 
ATOM   5424 O O      . VAL B 1 381 ? 30.565 7.413   29.954  1.00 25.06 ? 375 VAL B O      1 
ATOM   5425 C CB     . VAL B 1 381 ? 32.225 6.484   27.152  1.00 23.92 ? 375 VAL B CB     1 
ATOM   5426 C CG1    . VAL B 1 381 ? 32.870 7.778   27.632  1.00 26.64 ? 375 VAL B CG1    1 
ATOM   5427 C CG2    . VAL B 1 381 ? 33.282 5.473   26.720  1.00 25.91 ? 375 VAL B CG2    1 
ATOM   5428 N N      . VAL B 1 382 ? 29.358 7.311   28.057  1.00 22.61 ? 376 VAL B N      1 
ATOM   5429 C CA     . VAL B 1 382 ? 28.545 8.485   28.354  1.00 22.36 ? 376 VAL B CA     1 
ATOM   5430 C C      . VAL B 1 382 ? 27.730 8.236   29.617  1.00 24.56 ? 376 VAL B C      1 
ATOM   5431 O O      . VAL B 1 382 ? 26.914 7.310   29.675  1.00 25.61 ? 376 VAL B O      1 
ATOM   5432 C CB     . VAL B 1 382 ? 27.625 8.815   27.172  1.00 23.17 ? 376 VAL B CB     1 
ATOM   5433 C CG1    . VAL B 1 382 ? 26.564 9.823   27.585  1.00 23.21 ? 376 VAL B CG1    1 
ATOM   5434 C CG2    . VAL B 1 382 ? 28.438 9.303   25.972  1.00 25.05 ? 376 VAL B CG2    1 
ATOM   5435 N N      . GLY B 1 383 ? 27.921 9.089   30.621  1.00 22.29 ? 377 GLY B N      1 
ATOM   5436 C CA     . GLY B 1 383 ? 27.244 8.908   31.892  1.00 22.00 ? 377 GLY B CA     1 
ATOM   5437 C C      . GLY B 1 383 ? 27.714 7.723   32.692  1.00 24.18 ? 377 GLY B C      1 
ATOM   5438 O O      . GLY B 1 383 ? 27.043 7.348   33.663  1.00 23.94 ? 377 GLY B O      1 
ATOM   5439 N N      . TYR B 1 384 ? 28.865 7.145   32.343  1.00 23.39 ? 378 TYR B N      1 
ATOM   5440 C CA     . TYR B 1 384 ? 29.383 5.945   32.989  1.00 20.81 ? 378 TYR B CA     1 
ATOM   5441 C C      . TYR B 1 384 ? 30.826 6.148   33.436  1.00 22.56 ? 378 TYR B C      1 
ATOM   5442 O O      . TYR B 1 384 ? 31.121 6.138   34.637  1.00 25.54 ? 378 TYR B O      1 
ATOM   5443 C CB     . TYR B 1 384 ? 29.262 4.747   32.043  1.00 22.17 ? 378 TYR B CB     1 
ATOM   5444 C CG     . TYR B 1 384 ? 29.396 3.386   32.697  1.00 24.05 ? 378 TYR B CG     1 
ATOM   5445 C CD1    . TYR B 1 384 ? 28.666 3.060   33.843  1.00 23.20 ? 378 TYR B CD1    1 
ATOM   5446 C CD2    . TYR B 1 384 ? 30.259 2.426   32.170  1.00 24.20 ? 378 TYR B CD2    1 
ATOM   5447 C CE1    . TYR B 1 384 ? 28.782 1.804   34.433  1.00 23.41 ? 378 TYR B CE1    1 
ATOM   5448 C CE2    . TYR B 1 384 ? 30.380 1.174   32.750  1.00 22.83 ? 378 TYR B CE2    1 
ATOM   5449 C CZ     . TYR B 1 384 ? 29.651 0.872   33.884  1.00 22.47 ? 378 TYR B CZ     1 
ATOM   5450 O OH     . TYR B 1 384 ? 29.780 -0.374  34.457  1.00 25.45 ? 378 TYR B OH     1 
ATOM   5451 N N      . THR B 1 385 ? 31.736 6.343   32.483  1.00 22.29 ? 379 THR B N      1 
ATOM   5452 C CA     . THR B 1 385 ? 33.140 6.571   32.802  1.00 25.71 ? 379 THR B CA     1 
ATOM   5453 C C      . THR B 1 385 ? 33.619 7.982   32.481  1.00 21.73 ? 379 THR B C      1 
ATOM   5454 O O      . THR B 1 385 ? 34.804 8.273   32.676  1.00 26.37 ? 379 THR B O      1 
ATOM   5455 C CB     . THR B 1 385 ? 34.036 5.558   32.073  1.00 26.88 ? 379 THR B CB     1 
ATOM   5456 O OG1    . THR B 1 385 ? 33.808 5.664   30.671  1.00 25.19 ? 379 THR B OG1    1 
ATOM   5457 C CG2    . THR B 1 385 ? 33.747 4.136   32.515  1.00 29.48 ? 379 THR B CG2    1 
ATOM   5458 N N      . ASP B 1 386 ? 32.739 8.871   32.021  1.00 23.41 ? 380 ASP B N      1 
ATOM   5459 C CA     . ASP B 1 386 ? 33.145 10.215  31.625  1.00 26.99 ? 380 ASP B CA     1 
ATOM   5460 C C      . ASP B 1 386 ? 32.874 11.277  32.693  1.00 26.65 ? 380 ASP B C      1 
ATOM   5461 O O      . ASP B 1 386 ? 33.013 12.472  32.420  1.00 24.53 ? 380 ASP B O      1 
ATOM   5462 C CB     . ASP B 1 386 ? 32.539 10.598  30.265  1.00 24.11 ? 380 ASP B CB     1 
ATOM   5463 C CG     . ASP B 1 386 ? 31.021 10.669  30.284  1.00 27.72 ? 380 ASP B CG     1 
ATOM   5464 O OD1    . ASP B 1 386 ? 30.391 10.306  31.303  1.00 29.42 ? 380 ASP B OD1    1 
ATOM   5465 O OD2    . ASP B 1 386 ? 30.444 11.094  29.255  1.00 32.71 ? 380 ASP B OD2    1 
ATOM   5466 N N      . TYR B 1 387 ? 32.504 10.878  33.898  1.00 24.36 ? 381 TYR B N      1 
ATOM   5467 C CA     . TYR B 1 387 ? 32.443 11.841  34.988  1.00 22.30 ? 381 TYR B CA     1 
ATOM   5468 C C      . TYR B 1 387 ? 33.868 12.166  35.427  1.00 23.83 ? 381 TYR B C      1 
ATOM   5469 O O      . TYR B 1 387 ? 34.675 11.247  35.621  1.00 26.78 ? 381 TYR B O      1 
ATOM   5470 C CB     . TYR B 1 387 ? 31.681 11.244  36.159  1.00 22.88 ? 381 TYR B CB     1 
ATOM   5471 C CG     . TYR B 1 387 ? 30.178 11.189  36.012  1.00 24.06 ? 381 TYR B CG     1 
ATOM   5472 C CD1    . TYR B 1 387 ? 29.398 12.324  36.207  1.00 23.04 ? 381 TYR B CD1    1 
ATOM   5473 C CD2    . TYR B 1 387 ? 29.535 9.988   35.729  1.00 20.70 ? 381 TYR B CD2    1 
ATOM   5474 C CE1    . TYR B 1 387 ? 28.024 12.271  36.109  1.00 24.66 ? 381 TYR B CE1    1 
ATOM   5475 C CE2    . TYR B 1 387 ? 28.145 9.922   35.638  1.00 23.00 ? 381 TYR B CE2    1 
ATOM   5476 C CZ     . TYR B 1 387 ? 27.399 11.069  35.837  1.00 23.22 ? 381 TYR B CZ     1 
ATOM   5477 O OH     . TYR B 1 387 ? 26.026 11.016  35.753  1.00 26.70 ? 381 TYR B OH     1 
ATOM   5478 N N      . PRO B 1 388 ? 34.225 13.439  35.564  1.00 28.48 ? 382 PRO B N      1 
ATOM   5479 C CA     . PRO B 1 388 ? 35.638 13.804  35.715  1.00 27.83 ? 382 PRO B CA     1 
ATOM   5480 C C      . PRO B 1 388 ? 36.166 13.586  37.126  1.00 26.08 ? 382 PRO B C      1 
ATOM   5481 O O      . PRO B 1 388 ? 35.432 13.588  38.114  1.00 28.05 ? 382 PRO B O      1 
ATOM   5482 C CB     . PRO B 1 388 ? 35.661 15.297  35.368  1.00 30.91 ? 382 PRO B CB     1 
ATOM   5483 C CG     . PRO B 1 388 ? 34.275 15.775  35.624  1.00 36.41 ? 382 PRO B CG     1 
ATOM   5484 C CD     . PRO B 1 388 ? 33.357 14.614  35.371  1.00 33.35 ? 382 PRO B CD     1 
ATOM   5485 N N      . PHE B 1 389 ? 37.481 13.396  37.189  1.00 29.88 ? 383 PHE B N      1 
ATOM   5486 C CA     . PHE B 1 389 ? 38.227 13.384  38.434  1.00 27.41 ? 383 PHE B CA     1 
ATOM   5487 C C      . PHE B 1 389 ? 38.507 14.819  38.876  1.00 29.60 ? 383 PHE B C      1 
ATOM   5488 O O      . PHE B 1 389 ? 38.305 15.780  38.125  1.00 33.07 ? 383 PHE B O      1 
ATOM   5489 C CB     . PHE B 1 389 ? 39.547 12.637  38.232  1.00 26.26 ? 383 PHE B CB     1 
ATOM   5490 C CG     . PHE B 1 389 ? 39.390 11.142  38.120  1.00 28.58 ? 383 PHE B CG     1 
ATOM   5491 C CD1    . PHE B 1 389 ? 38.990 10.557  36.922  1.00 34.53 ? 383 PHE B CD1    1 
ATOM   5492 C CD2    . PHE B 1 389 ? 39.675 10.321  39.200  1.00 26.24 ? 383 PHE B CD2    1 
ATOM   5493 C CE1    . PHE B 1 389 ? 38.850 9.179   36.816  1.00 28.91 ? 383 PHE B CE1    1 
ATOM   5494 C CE2    . PHE B 1 389 ? 39.537 8.943   39.104  1.00 29.73 ? 383 PHE B CE2    1 
ATOM   5495 C CZ     . PHE B 1 389 ? 39.122 8.372   37.908  1.00 31.78 ? 383 PHE B CZ     1 
ATOM   5496 N N      . LEU B 1 390 ? 38.972 14.962  40.115  1.00 29.35 ? 384 LEU B N      1 
ATOM   5497 C CA     . LEU B 1 390 ? 39.464 16.255  40.597  1.00 31.80 ? 384 LEU B CA     1 
ATOM   5498 C C      . LEU B 1 390 ? 40.566 16.805  39.692  1.00 34.95 ? 384 LEU B C      1 
ATOM   5499 O O      . LEU B 1 390 ? 40.508 17.960  39.269  1.00 48.16 ? 384 LEU B O      1 
ATOM   5500 C CB     . LEU B 1 390 ? 40.003 16.127  42.018  1.00 34.26 ? 384 LEU B CB     1 
ATOM   5501 C CG     . LEU B 1 390 ? 38.958 16.126  43.122  1.00 31.79 ? 384 LEU B CG     1 
ATOM   5502 C CD1    . LEU B 1 390 ? 39.640 15.917  44.472  1.00 31.89 ? 384 LEU B CD1    1 
ATOM   5503 C CD2    . LEU B 1 390 ? 38.169 17.427  43.109  1.00 38.66 ? 384 LEU B CD2    1 
HETATM 5504 N N1     . FMN C 2 .   ? 22.225 -6.673  0.508   1.00 17.60 ? 401 FMN A N1     1 
HETATM 5505 C C2     . FMN C 2 .   ? 21.981 -5.323  0.404   1.00 21.82 ? 401 FMN A C2     1 
HETATM 5506 O O2     . FMN C 2 .   ? 21.714 -4.680  1.420   1.00 19.16 ? 401 FMN A O2     1 
HETATM 5507 N N3     . FMN C 2 .   ? 21.992 -4.706  -0.835  1.00 18.19 ? 401 FMN A N3     1 
HETATM 5508 C C4     . FMN C 2 .   ? 22.274 -5.435  -1.972  1.00 21.49 ? 401 FMN A C4     1 
HETATM 5509 O O4     . FMN C 2 .   ? 22.284 -4.874  -3.086  1.00 20.39 ? 401 FMN A O4     1 
HETATM 5510 C C4A    . FMN C 2 .   ? 22.504 -6.806  -1.853  1.00 19.80 ? 401 FMN A C4A    1 
HETATM 5511 N N5     . FMN C 2 .   ? 22.815 -7.559  -2.974  1.00 21.53 ? 401 FMN A N5     1 
HETATM 5512 C C5A    . FMN C 2 .   ? 23.011 -8.920  -2.867  1.00 20.04 ? 401 FMN A C5A    1 
HETATM 5513 C C6     . FMN C 2 .   ? 23.279 -9.669  -4.020  1.00 19.97 ? 401 FMN A C6     1 
HETATM 5514 C C7     . FMN C 2 .   ? 23.490 -11.041 -3.913  1.00 18.81 ? 401 FMN A C7     1 
HETATM 5515 C C7M    . FMN C 2 .   ? 23.767 -11.846 -5.162  1.00 22.04 ? 401 FMN A C7M    1 
HETATM 5516 C C8     . FMN C 2 .   ? 23.444 -11.658 -2.665  1.00 25.69 ? 401 FMN A C8     1 
HETATM 5517 C C8M    . FMN C 2 .   ? 23.679 -13.131 -2.521  1.00 24.45 ? 401 FMN A C8M    1 
HETATM 5518 C C9     . FMN C 2 .   ? 23.181 -10.902 -1.529  1.00 23.69 ? 401 FMN A C9     1 
HETATM 5519 C C9A    . FMN C 2 .   ? 22.958 -9.537  -1.625  1.00 21.44 ? 401 FMN A C9A    1 
HETATM 5520 N N10    . FMN C 2 .   ? 22.713 -8.781  -0.487  1.00 20.54 ? 401 FMN A N10    1 
HETATM 5521 C C10    . FMN C 2 .   ? 22.485 -7.426  -0.612  1.00 20.68 ? 401 FMN A C10    1 
HETATM 5522 C "C1'"  . FMN C 2 .   ? 22.602 -9.438  0.869   1.00 20.00 ? 401 FMN A "C1'"  1 
HETATM 5523 C "C2'"  . FMN C 2 .   ? 21.158 -10.000 0.936   1.00 23.33 ? 401 FMN A "C2'"  1 
HETATM 5524 O "O2'"  . FMN C 2 .   ? 20.165 -8.974  0.904   1.00 20.77 ? 401 FMN A "O2'"  1 
HETATM 5525 C "C3'"  . FMN C 2 .   ? 20.866 -10.889 2.150   1.00 22.27 ? 401 FMN A "C3'"  1 
HETATM 5526 O "O3'"  . FMN C 2 .   ? 20.995 -10.095 3.311   1.00 20.98 ? 401 FMN A "O3'"  1 
HETATM 5527 C "C4'"  . FMN C 2 .   ? 21.813 -12.092 2.195   1.00 24.46 ? 401 FMN A "C4'"  1 
HETATM 5528 O "O4'"  . FMN C 2 .   ? 21.728 -12.817 0.975   1.00 25.79 ? 401 FMN A "O4'"  1 
HETATM 5529 C "C5'"  . FMN C 2 .   ? 21.549 -13.072 3.335   1.00 24.97 ? 401 FMN A "C5'"  1 
HETATM 5530 O "O5'"  . FMN C 2 .   ? 20.219 -13.552 3.257   1.00 22.23 ? 401 FMN A "O5'"  1 
HETATM 5531 P P      . FMN C 2 .   ? 19.840 -15.004 2.665   1.00 22.76 ? 401 FMN A P      1 
HETATM 5532 O O1P    . FMN C 2 .   ? 20.433 -15.085 1.272   1.00 22.00 ? 401 FMN A O1P    1 
HETATM 5533 O O2P    . FMN C 2 .   ? 18.334 -15.066 2.647   1.00 21.24 ? 401 FMN A O2P    1 
HETATM 5534 O O3P    . FMN C 2 .   ? 20.401 -16.100 3.537   1.00 26.98 ? 401 FMN A O3P    1 
HETATM 5535 O O7N    . WI6 D 3 .   ? 25.196 -5.217  -0.008  0.91 21.70 ? 402 WI6 A O7N    1 
HETATM 5536 C C7N    . WI6 D 3 .   ? 25.448 -5.619  -1.149  0.91 24.35 ? 402 WI6 A C7N    1 
HETATM 5537 N N7N    . WI6 D 3 .   ? 25.349 -4.852  -2.245  0.91 22.84 ? 402 WI6 A N7N    1 
HETATM 5538 C C3N    . WI6 D 3 .   ? 25.824 -7.077  -1.430  0.91 28.06 ? 402 WI6 A C3N    1 
HETATM 5539 C C2N    . WI6 D 3 .   ? 26.472 -7.698  -0.201  0.91 34.45 ? 402 WI6 A C2N    1 
HETATM 5540 C C4N    . WI6 D 3 .   ? 26.676 -7.366  -2.632  0.91 31.93 ? 402 WI6 A C4N    1 
HETATM 5541 C C5N    . WI6 D 3 .   ? 27.252 -8.566  -2.652  0.91 32.50 ? 402 WI6 A C5N    1 
HETATM 5542 C C6N    . WI6 D 3 .   ? 27.023 -9.622  -1.601  0.91 35.71 ? 402 WI6 A C6N    1 
HETATM 5543 N N1N    . WI6 D 3 .   ? 26.500 -9.137  -0.327  0.91 36.00 ? 402 WI6 A N1N    1 
HETATM 5544 C "C1'A" . WI6 D 3 .   ? 26.977 -9.742  0.890   0.91 39.01 ? 402 WI6 A "C1'A" 1 
HETATM 5545 O "O4'A" . WI6 D 3 .   ? 28.383 -9.826  0.882   0.91 47.56 ? 402 WI6 A "O4'A" 1 
HETATM 5546 C "C2'A" . WI6 D 3 .   ? 26.541 -11.160 1.318   0.91 46.77 ? 402 WI6 A "C2'A" 1 
HETATM 5547 O "O2'A" . WI6 D 3 .   ? 25.212 -11.267 1.735   0.91 36.35 ? 402 WI6 A "O2'A" 1 
HETATM 5548 C "C3'A" . WI6 D 3 .   ? 27.579 -11.451 2.418   0.91 42.01 ? 402 WI6 A "C3'A" 1 
HETATM 5549 O "O3'A" . WI6 D 3 .   ? 27.155 -11.003 3.693   0.91 49.20 ? 402 WI6 A "O3'A" 1 
HETATM 5550 C "C4'A" . WI6 D 3 .   ? 28.819 -10.729 1.899   0.91 49.02 ? 402 WI6 A "C4'A" 1 
HETATM 5551 C "C5'A" . WI6 D 3 .   ? 29.816 -11.751 1.382   0.91 52.78 ? 402 WI6 A "C5'A" 1 
HETATM 5552 O "O5'A" . WI6 D 3 .   ? 29.301 -12.317 0.203   0.91 57.11 ? 402 WI6 A "O5'A" 1 
HETATM 5553 P PN     . WI6 D 3 .   ? 29.655 -13.882 -0.155  0.91 66.23 ? 402 WI6 A PN     1 
HETATM 5554 O O1N    . WI6 D 3 .   ? 29.730 -14.596 1.158   0.91 58.73 ? 402 WI6 A O1N    1 
HETATM 5555 O O2N    . WI6 D 3 .   ? 28.744 -14.336 -1.253  0.91 61.90 ? 402 WI6 A O2N    1 
HETATM 5556 O O3     . WI6 D 3 .   ? 31.174 -13.644 -0.751  0.91 68.86 ? 402 WI6 A O3     1 
HETATM 5557 P PA     . WI6 D 3 .   ? 31.563 -13.309 -2.316  0.91 79.27 ? 402 WI6 A PA     1 
HETATM 5558 O O2P    . WI6 D 3 .   ? 32.941 -12.726 -2.379  0.91 75.94 ? 402 WI6 A O2P    1 
HETATM 5559 O O1     . WI6 D 3 .   ? 30.399 -12.643 -2.990  0.91 67.45 ? 402 WI6 A O1     1 
HETATM 5560 O "O5'"  . WI6 D 3 .   ? 31.589 -14.862 -2.862  0.91 68.58 ? 402 WI6 A "O5'"  1 
HETATM 5561 N N1     . FMN E 2 .   ? 21.028 -1.516  45.462  1.00 18.90 ? 401 FMN B N1     1 
HETATM 5562 C C2     . FMN E 2 .   ? 21.276 -2.866  45.418  1.00 20.39 ? 401 FMN B C2     1 
HETATM 5563 O O2     . FMN E 2 .   ? 21.260 -3.503  46.474  1.00 19.58 ? 401 FMN B O2     1 
HETATM 5564 N N3     . FMN E 2 .   ? 21.584 -3.476  44.202  1.00 16.93 ? 401 FMN B N3     1 
HETATM 5565 C C4     . FMN E 2 .   ? 21.604 -2.744  43.031  1.00 22.33 ? 401 FMN B C4     1 
HETATM 5566 O O4     . FMN E 2 .   ? 21.876 -3.289  41.942  1.00 20.19 ? 401 FMN B O4     1 
HETATM 5567 C C4A    . FMN E 2 .   ? 21.350 -1.379  43.090  1.00 19.59 ? 401 FMN B C4A    1 
HETATM 5568 N N5     . FMN E 2 .   ? 21.349 -0.630  41.925  1.00 21.14 ? 401 FMN B N5     1 
HETATM 5569 C C5A    . FMN E 2 .   ? 21.135 0.727   41.979  1.00 17.97 ? 401 FMN B C5A    1 
HETATM 5570 C C6     . FMN E 2 .   ? 21.187 1.474   40.807  1.00 20.29 ? 401 FMN B C6     1 
HETATM 5571 C C7     . FMN E 2 .   ? 20.949 2.839   40.858  1.00 18.72 ? 401 FMN B C7     1 
HETATM 5572 C C7M    . FMN E 2 .   ? 21.016 3.640   39.583  1.00 24.72 ? 401 FMN B C7M    1 
HETATM 5573 C C8     . FMN E 2 .   ? 20.682 3.459   42.076  1.00 26.06 ? 401 FMN B C8     1 
HETATM 5574 C C8M    . FMN E 2 .   ? 20.417 4.936   42.137  1.00 26.49 ? 401 FMN B C8M    1 
HETATM 5575 C C9     . FMN E 2 .   ? 20.635 2.707   43.243  1.00 23.82 ? 401 FMN B C9     1 
HETATM 5576 C C9A    . FMN E 2 .   ? 20.873 1.342   43.201  1.00 21.18 ? 401 FMN B C9A    1 
HETATM 5577 N N10    . FMN E 2 .   ? 20.811 0.580   44.354  1.00 20.12 ? 401 FMN B N10    1 
HETATM 5578 C C10    . FMN E 2 .   ? 21.069 -0.771  44.308  1.00 21.11 ? 401 FMN B C10    1 
HETATM 5579 C "C1'"  . FMN E 2 .   ? 20.566 1.239   45.677  1.00 21.27 ? 401 FMN B "C1'"  1 
HETATM 5580 C "C2'"  . FMN E 2 .   ? 21.959 1.733   46.097  1.00 20.77 ? 401 FMN B "C2'"  1 
HETATM 5581 O "O2'"  . FMN E 2 .   ? 22.904 0.712   46.363  1.00 20.22 ? 401 FMN B "O2'"  1 
HETATM 5582 C "C3'"  . FMN E 2 .   ? 21.955 2.530   47.375  1.00 24.72 ? 401 FMN B "C3'"  1 
HETATM 5583 O "O3'"  . FMN E 2 .   ? 21.463 1.812   48.490  1.00 20.47 ? 401 FMN B "O3'"  1 
HETATM 5584 C "C4'"  . FMN E 2 .   ? 21.328 3.895   47.292  1.00 26.41 ? 401 FMN B "C4'"  1 
HETATM 5585 O "O4'"  . FMN E 2 .   ? 21.337 4.528   46.028  1.00 25.50 ? 401 FMN B "O4'"  1 
HETATM 5586 C "C5'"  . FMN E 2 .   ? 22.552 4.446   47.952  1.00 41.91 ? 401 FMN B "C5'"  1 
HETATM 5587 O "O5'"  . FMN E 2 .   ? 22.169 5.528   48.688  1.00 23.93 ? 401 FMN B "O5'"  1 
HETATM 5588 P P      . FMN E 2 .   ? 22.774 6.902   48.185  1.00 22.28 ? 401 FMN B P      1 
HETATM 5589 O O1P    . FMN E 2 .   ? 24.223 6.879   48.600  1.00 21.19 ? 401 FMN B O1P    1 
HETATM 5590 O O2P    . FMN E 2 .   ? 22.000 8.000   48.875  1.00 26.62 ? 401 FMN B O2P    1 
HETATM 5591 O O3P    . FMN E 2 .   ? 22.583 6.972   46.688  1.00 22.10 ? 401 FMN B O3P    1 
HETATM 5592 O O7N    . WI6 F 3 .   ? 18.277 -2.896  44.139  0.80 20.82 ? 402 WI6 B O7N    1 
HETATM 5593 C C7N    . WI6 F 3 .   ? 18.329 -2.484  42.987  0.80 22.67 ? 402 WI6 B C7N    1 
HETATM 5594 N N7N    . WI6 F 3 .   ? 18.697 -3.254  41.956  0.80 20.68 ? 402 WI6 B N7N    1 
HETATM 5595 C C3N    . WI6 F 3 .   ? 18.055 -1.024  42.625  0.80 27.61 ? 402 WI6 B C3N    1 
HETATM 5596 C C2N    . WI6 F 3 .   ? 17.150 -0.389  43.665  0.80 30.43 ? 402 WI6 B C2N    1 
HETATM 5597 C C4N    . WI6 F 3 .   ? 17.497 -0.751  41.258  0.80 28.92 ? 402 WI6 B C4N    1 
HETATM 5598 C C5N    . WI6 F 3 .   ? 16.922 0.436   41.092  0.80 29.18 ? 402 WI6 B C5N    1 
HETATM 5599 C C6N    . WI6 F 3 .   ? 16.952 1.519   42.132  0.80 31.24 ? 402 WI6 B C6N    1 
HETATM 5600 N N1N    . WI6 F 3 .   ? 17.096 1.045   43.504  0.80 31.02 ? 402 WI6 B N1N    1 
HETATM 5601 C "C1'A" . WI6 F 3 .   ? 16.268 1.624   44.528  0.80 35.25 ? 402 WI6 B "C1'A" 1 
HETATM 5602 O "O4'A" . WI6 F 3 .   ? 14.942 1.783   44.082  0.80 41.44 ? 402 WI6 B "O4'A" 1 
HETATM 5603 C "C2'A" . WI6 F 3 .   ? 16.607 3.000   45.138  0.80 39.90 ? 402 WI6 B "C2'A" 1 
HETATM 5604 O "O2'A" . WI6 F 3 .   ? 17.759 3.019   45.929  0.80 33.17 ? 402 WI6 B "O2'A" 1 
HETATM 5605 C "C3'A" . WI6 F 3 .   ? 15.295 3.303   45.885  0.80 31.54 ? 402 WI6 B "C3'A" 1 
HETATM 5606 O "O3'A" . WI6 F 3 .   ? 15.312 2.823   47.215  0.80 42.66 ? 402 WI6 B "O3'A" 1 
HETATM 5607 C "C4'A" . WI6 F 3 .   ? 14.247 2.645   44.986  0.80 41.78 ? 402 WI6 B "C4'A" 1 
HETATM 5608 C "C5'A" . WI6 F 3 .   ? 13.485 3.723   44.239  0.80 43.58 ? 402 WI6 B "C5'A" 1 
HETATM 5609 O "O5'A" . WI6 F 3 .   ? 14.306 4.128   43.176  0.80 46.84 ? 402 WI6 B "O5'A" 1 
HETATM 5610 P PN     . WI6 F 3 .   ? 14.156 5.631   42.528  0.80 53.55 ? 402 WI6 B PN     1 
HETATM 5611 O O1N    . WI6 F 3 .   ? 13.581 6.497   43.603  0.80 47.63 ? 402 WI6 B O1N    1 
HETATM 5612 O O2N    . WI6 F 3 .   ? 15.435 5.977   41.832  0.80 46.37 ? 402 WI6 B O2N    1 
HETATM 5613 O O3     . WI6 F 3 .   ? 13.002 5.268   41.414  0.80 54.84 ? 402 WI6 B O3     1 
HETATM 5614 P PA     . WI6 F 3 .   ? 12.322 6.314   40.344  0.80 63.31 ? 402 WI6 B PA     1 
HETATM 5615 O O2P    . WI6 F 3 .   ? 12.152 5.647   39.013  0.80 57.41 ? 402 WI6 B O2P    1 
HETATM 5616 O O1     . WI6 F 3 .   ? 12.980 7.651   40.458  0.80 58.32 ? 402 WI6 B O1     1 
HETATM 5617 O "O5'"  . WI6 F 3 .   ? 10.877 6.455   41.114  0.80 56.07 ? 402 WI6 B "O5'"  1 
HETATM 5618 O O      . HOH G 4 .   ? 46.880 7.472   3.827   1.00 52.96 ? 501 HOH A O      1 
HETATM 5619 O O      . HOH G 4 .   ? 3.508  -8.172  -16.922 1.00 46.32 ? 502 HOH A O      1 
HETATM 5620 O O      . HOH G 4 .   ? 17.981 -11.716 3.890   1.00 32.10 ? 503 HOH A O      1 
HETATM 5621 O O      . HOH G 4 .   ? 26.772 -21.956 -9.530  1.00 46.27 ? 504 HOH A O      1 
HETATM 5622 O O      . HOH G 4 .   ? 10.646 -7.289  22.216  1.00 42.04 ? 505 HOH A O      1 
HETATM 5623 O O      . HOH G 4 .   ? 32.599 -5.636  -3.817  1.00 34.28 ? 506 HOH A O      1 
HETATM 5624 O O      . HOH G 4 .   ? -1.776 -9.276  12.176  1.00 41.03 ? 507 HOH A O      1 
HETATM 5625 O O      . HOH G 4 .   ? 2.040  -22.665 5.660   1.00 41.60 ? 508 HOH A O      1 
HETATM 5626 O O      . HOH G 4 .   ? 5.682  7.136   -4.430  1.00 34.72 ? 509 HOH A O      1 
HETATM 5627 O O      . HOH G 4 .   ? 17.525 -7.160  -9.822  1.00 30.02 ? 510 HOH A O      1 
HETATM 5628 O O      . HOH G 4 .   ? 31.572 12.925  -3.238  1.00 37.67 ? 511 HOH A O      1 
HETATM 5629 O O      . HOH G 4 .   ? 12.793 7.446   -20.409 1.00 53.29 ? 512 HOH A O      1 
HETATM 5630 O O      . HOH G 4 .   ? -0.892 -10.122 -7.206  1.00 40.64 ? 513 HOH A O      1 
HETATM 5631 O O      . HOH G 4 .   ? 21.143 11.758  -6.263  1.00 46.12 ? 514 HOH A O      1 
HETATM 5632 O O      . HOH G 4 .   ? 40.271 2.126   12.094  1.00 42.68 ? 515 HOH A O      1 
HETATM 5633 O O      . HOH G 4 .   ? 5.699  9.590   8.695   1.00 40.59 ? 516 HOH A O      1 
HETATM 5634 O O      . HOH G 4 .   ? 36.656 -6.839  20.220  1.00 50.96 ? 517 HOH A O      1 
HETATM 5635 O O      . HOH G 4 .   ? 7.025  -11.171 -15.139 1.00 37.40 ? 518 HOH A O      1 
HETATM 5636 O O      . HOH G 4 .   ? 37.748 -3.248  9.978   1.00 41.62 ? 519 HOH A O      1 
HETATM 5637 O O      . HOH G 4 .   ? 21.049 -20.811 1.051   1.00 46.70 ? 520 HOH A O      1 
HETATM 5638 O O      . HOH G 4 .   ? 42.581 11.362  1.210   1.00 41.49 ? 521 HOH A O      1 
HETATM 5639 O O      . HOH G 4 .   ? 26.280 -14.890 -0.730  1.00 42.21 ? 522 HOH A O      1 
HETATM 5640 O O      . HOH G 4 .   ? 19.321 -21.018 -17.475 1.00 42.80 ? 523 HOH A O      1 
HETATM 5641 O O      . HOH G 4 .   ? 44.004 8.465   -0.925  1.00 42.40 ? 524 HOH A O      1 
HETATM 5642 O O      . HOH G 4 .   ? 32.565 0.110   19.267  1.00 33.86 ? 525 HOH A O      1 
HETATM 5643 O O      . HOH G 4 .   ? 22.555 -16.046 -22.998 1.00 29.17 ? 526 HOH A O      1 
HETATM 5644 O O      . HOH G 4 .   ? 3.326  -20.634 -7.962  1.00 39.96 ? 527 HOH A O      1 
HETATM 5645 O O      . HOH G 4 .   ? 28.517 14.069  -3.501  1.00 46.94 ? 528 HOH A O      1 
HETATM 5646 O O      . HOH G 4 .   ? 6.057  -5.312  16.649  1.00 41.75 ? 529 HOH A O      1 
HETATM 5647 O O      . HOH G 4 .   ? 29.939 -7.467  -15.875 1.00 41.08 ? 530 HOH A O      1 
HETATM 5648 O O      . HOH G 4 .   ? 8.367  14.168  -0.454  1.00 47.03 ? 531 HOH A O      1 
HETATM 5649 O O      . HOH G 4 .   ? 15.921 -24.257 9.286   1.00 39.31 ? 532 HOH A O      1 
HETATM 5650 O O      . HOH G 4 .   ? 17.233 -23.902 -10.064 1.00 30.75 ? 533 HOH A O      1 
HETATM 5651 O O      . HOH G 4 .   ? 26.506 0.505   23.842  1.00 29.17 ? 534 HOH A O      1 
HETATM 5652 O O      . HOH G 4 .   ? 19.051 -9.338  24.753  1.00 39.67 ? 535 HOH A O      1 
HETATM 5653 O O      . HOH G 4 .   ? 36.564 16.094  0.601   1.00 27.78 ? 536 HOH A O      1 
HETATM 5654 O O      . HOH G 4 .   ? 30.258 10.388  -3.689  1.00 30.67 ? 537 HOH A O      1 
HETATM 5655 O O      . HOH G 4 .   ? 42.025 -5.987  -3.223  1.00 29.32 ? 538 HOH A O      1 
HETATM 5656 O O      . HOH G 4 .   ? 0.262  -0.092  -11.912 1.00 34.58 ? 539 HOH A O      1 
HETATM 5657 O O      . HOH G 4 .   ? 28.603 4.176   -14.130 1.00 36.65 ? 540 HOH A O      1 
HETATM 5658 O O      . HOH G 4 .   ? 43.671 5.563   -5.269  1.00 34.00 ? 541 HOH A O      1 
HETATM 5659 O O      . HOH G 4 .   ? 6.370  0.135   10.295  1.00 22.69 ? 542 HOH A O      1 
HETATM 5660 O O      . HOH G 4 .   ? -3.246 -6.576  2.702   1.00 39.20 ? 543 HOH A O      1 
HETATM 5661 O O      . HOH G 4 .   ? 23.891 3.615   1.051   1.00 21.34 ? 544 HOH A O      1 
HETATM 5662 O O      . HOH G 4 .   ? 21.361 -17.010 -10.707 1.00 28.70 ? 545 HOH A O      1 
HETATM 5663 O O      . HOH G 4 .   ? 45.051 5.081   10.454  1.00 40.95 ? 546 HOH A O      1 
HETATM 5664 O O      . HOH G 4 .   ? 5.199  4.465   -10.734 1.00 38.96 ? 547 HOH A O      1 
HETATM 5665 O O      . HOH G 4 .   ? 23.358 -14.653 -16.924 1.00 27.71 ? 548 HOH A O      1 
HETATM 5666 O O      . HOH G 4 .   ? 36.887 6.040   14.929  1.00 37.68 ? 549 HOH A O      1 
HETATM 5667 O O      . HOH G 4 .   ? 33.928 20.310  9.995   1.00 34.54 ? 550 HOH A O      1 
HETATM 5668 O O      . HOH G 4 .   ? 27.558 10.594  -3.662  1.00 27.15 ? 551 HOH A O      1 
HETATM 5669 O O      . HOH G 4 .   ? 22.007 -19.939 -14.132 1.00 41.37 ? 552 HOH A O      1 
HETATM 5670 O O      . HOH G 4 .   ? 29.822 -16.562 -13.808 1.00 37.55 ? 553 HOH A O      1 
HETATM 5671 O O      . HOH G 4 .   ? 42.466 7.050   -9.596  1.00 42.35 ? 554 HOH A O      1 
HETATM 5672 O O      . HOH G 4 .   ? 34.496 -7.834  16.727  1.00 45.75 ? 555 HOH A O      1 
HETATM 5673 O O      . HOH G 4 .   ? 31.855 12.360  21.217  1.00 33.40 ? 556 HOH A O      1 
HETATM 5674 O O      . HOH G 4 .   ? 31.983 -5.313  -8.321  1.00 24.43 ? 557 HOH A O      1 
HETATM 5675 O O      . HOH G 4 .   ? -0.830 -1.592  -5.752  1.00 41.13 ? 558 HOH A O      1 
HETATM 5676 O O      . HOH G 4 .   ? 28.939 -5.142  7.614   1.00 33.33 ? 559 HOH A O      1 
HETATM 5677 O O      . HOH G 4 .   ? 8.635  -29.472 1.427   1.00 41.51 ? 560 HOH A O      1 
HETATM 5678 O O      . HOH G 4 .   ? 41.059 -7.900  -13.842 1.00 51.83 ? 561 HOH A O      1 
HETATM 5679 O O      . HOH G 4 .   ? 43.137 -3.746  -1.923  1.00 27.69 ? 562 HOH A O      1 
HETATM 5680 O O      . HOH G 4 .   ? 19.617 -5.883  -12.023 1.00 21.07 ? 563 HOH A O      1 
HETATM 5681 O O      . HOH G 4 .   ? 15.118 -13.545 14.261  1.00 41.32 ? 564 HOH A O      1 
HETATM 5682 O O      . HOH G 4 .   ? 36.763 4.692   17.461  1.00 36.36 ? 565 HOH A O      1 
HETATM 5683 O O      . HOH G 4 .   ? 29.189 12.192  -7.402  1.00 38.42 ? 566 HOH A O      1 
HETATM 5684 O O      . HOH G 4 .   ? 33.230 -14.144 -13.003 1.00 46.11 ? 567 HOH A O      1 
HETATM 5685 O O      . HOH G 4 .   ? 10.576 -1.957  21.067  1.00 39.08 ? 568 HOH A O      1 
HETATM 5686 O O      . HOH G 4 .   ? 13.883 -10.617 -18.774 1.00 35.68 ? 569 HOH A O      1 
HETATM 5687 O O      . HOH G 4 .   ? 35.142 -8.427  -2.386  1.00 35.50 ? 570 HOH A O      1 
HETATM 5688 O O      . HOH G 4 .   ? 13.828 -15.412 21.035  1.00 40.72 ? 571 HOH A O      1 
HETATM 5689 O O      . HOH G 4 .   ? 6.103  -10.819 -2.828  1.00 23.72 ? 572 HOH A O      1 
HETATM 5690 O O      . HOH G 4 .   ? 40.819 -9.424  -18.252 1.00 41.06 ? 573 HOH A O      1 
HETATM 5691 O O      . HOH G 4 .   ? 17.898 -20.216 -13.827 1.00 33.48 ? 574 HOH A O      1 
HETATM 5692 O O      . HOH G 4 .   ? 22.566 -3.323  -7.255  1.00 19.53 ? 575 HOH A O      1 
HETATM 5693 O O      . HOH G 4 .   ? 38.191 16.729  16.224  1.00 52.29 ? 576 HOH A O      1 
HETATM 5694 O O      . HOH G 4 .   ? 44.080 -2.714  3.832   1.00 44.74 ? 577 HOH A O      1 
HETATM 5695 O O      . HOH G 4 .   ? 23.489 -10.007 4.311   1.00 29.10 ? 578 HOH A O      1 
HETATM 5696 O O      . HOH G 4 .   ? 41.755 13.605  2.248   1.00 38.29 ? 579 HOH A O      1 
HETATM 5697 O O      . HOH G 4 .   ? 35.027 9.064   -6.379  1.00 37.72 ? 580 HOH A O      1 
HETATM 5698 O O      . HOH G 4 .   ? 20.873 8.468   -17.022 1.00 34.60 ? 581 HOH A O      1 
HETATM 5699 O O      . HOH G 4 .   ? 4.826  -14.153 -7.356  1.00 39.80 ? 582 HOH A O      1 
HETATM 5700 O O      . HOH G 4 .   ? 25.385 10.423  16.931  1.00 35.95 ? 583 HOH A O      1 
HETATM 5701 O O      . HOH G 4 .   ? 31.735 -3.034  -4.739  1.00 26.21 ? 584 HOH A O      1 
HETATM 5702 O O      . HOH G 4 .   ? 21.566 6.314   25.437  1.00 39.23 ? 585 HOH A O      1 
HETATM 5703 O O      . HOH G 4 .   ? 37.269 17.498  9.403   1.00 31.92 ? 586 HOH A O      1 
HETATM 5704 O O      . HOH G 4 .   ? 22.017 -4.701  -9.623  1.00 22.53 ? 587 HOH A O      1 
HETATM 5705 O O      . HOH G 4 .   ? 2.923  3.042   -9.484  1.00 36.43 ? 588 HOH A O      1 
HETATM 5706 O O      . HOH G 4 .   ? 9.340  1.110   12.525  1.00 26.38 ? 589 HOH A O      1 
HETATM 5707 O O      . HOH G 4 .   ? 45.103 -0.980  -2.655  1.00 41.85 ? 590 HOH A O      1 
HETATM 5708 O O      . HOH G 4 .   ? 35.535 -1.450  22.026  1.00 38.48 ? 591 HOH A O      1 
HETATM 5709 O O      . HOH G 4 .   ? 6.858  -11.216 15.968  1.00 29.95 ? 592 HOH A O      1 
HETATM 5710 O O      . HOH G 4 .   ? 17.168 -8.394  -6.665  1.00 23.59 ? 593 HOH A O      1 
HETATM 5711 O O      . HOH G 4 .   ? 5.563  2.930   7.339   1.00 35.77 ? 594 HOH A O      1 
HETATM 5712 O O      . HOH G 4 .   ? 33.468 18.754  -2.822  1.00 38.75 ? 595 HOH A O      1 
HETATM 5713 O O      . HOH G 4 .   ? 4.829  -8.833  14.768  1.00 27.97 ? 596 HOH A O      1 
HETATM 5714 O O      . HOH G 4 .   ? 4.464  5.888   -0.107  1.00 32.59 ? 597 HOH A O      1 
HETATM 5715 O O      . HOH G 4 .   ? 21.933 2.945   23.584  1.00 32.32 ? 598 HOH A O      1 
HETATM 5716 O O      . HOH G 4 .   ? -1.102 3.211   1.985   1.00 41.10 ? 599 HOH A O      1 
HETATM 5717 O O      . HOH G 4 .   ? 28.418 0.629   -12.485 1.00 22.07 ? 600 HOH A O      1 
HETATM 5718 O O      . HOH G 4 .   ? 27.602 6.554   10.337  1.00 24.35 ? 601 HOH A O      1 
HETATM 5719 O O      . HOH G 4 .   ? 31.915 1.853   -15.008 1.00 28.32 ? 602 HOH A O      1 
HETATM 5720 O O      . HOH G 4 .   ? 41.686 10.692  -15.321 1.00 53.11 ? 603 HOH A O      1 
HETATM 5721 O O      . HOH G 4 .   ? 8.106  6.305   -17.497 1.00 33.00 ? 604 HOH A O      1 
HETATM 5722 O O      . HOH G 4 .   ? 36.638 2.215   19.366  1.00 39.58 ? 605 HOH A O      1 
HETATM 5723 O O      . HOH G 4 .   ? 34.774 9.048   -17.157 1.00 42.73 ? 606 HOH A O      1 
HETATM 5724 O O      . HOH G 4 .   ? 11.208 6.376   18.908  1.00 26.09 ? 607 HOH A O      1 
HETATM 5725 O O      . HOH G 4 .   ? 42.977 -0.821  -8.241  1.00 32.24 ? 608 HOH A O      1 
HETATM 5726 O O      . HOH G 4 .   ? 40.037 13.217  10.908  1.00 42.10 ? 609 HOH A O      1 
HETATM 5727 O O      . HOH G 4 .   ? 20.794 17.369  2.492   1.00 38.68 ? 610 HOH A O      1 
HETATM 5728 O O      . HOH G 4 .   ? 7.693  -10.275 -0.673  1.00 22.87 ? 611 HOH A O      1 
HETATM 5729 O O      . HOH G 4 .   ? 18.027 -4.752  23.971  1.00 26.04 ? 612 HOH A O      1 
HETATM 5730 O O      . HOH G 4 .   ? 5.257  10.105  4.191   1.00 40.53 ? 613 HOH A O      1 
HETATM 5731 O O      . HOH G 4 .   ? 15.956 -7.402  -4.389  1.00 23.15 ? 614 HOH A O      1 
HETATM 5732 O O      . HOH G 4 .   ? 7.941  -3.386  17.483  1.00 37.39 ? 615 HOH A O      1 
HETATM 5733 O O      . HOH G 4 .   ? 2.942  4.842   -1.886  1.00 36.93 ? 616 HOH A O      1 
HETATM 5734 O O      . HOH G 4 .   ? 29.106 7.022   -13.011 1.00 35.13 ? 617 HOH A O      1 
HETATM 5735 O O      . HOH G 4 .   ? 24.373 -13.810 1.083   1.00 31.81 ? 618 HOH A O      1 
HETATM 5736 O O      . HOH G 4 .   ? 0.883  -1.261  -3.462  1.00 36.87 ? 619 HOH A O      1 
HETATM 5737 O O      . HOH G 4 .   ? 1.921  -6.483  -13.399 1.00 31.74 ? 620 HOH A O      1 
HETATM 5738 O O      . HOH G 4 .   ? 25.177 4.984   22.437  1.00 29.56 ? 621 HOH A O      1 
HETATM 5739 O O      . HOH G 4 .   ? 38.378 11.080  -5.986  1.00 35.51 ? 622 HOH A O      1 
HETATM 5740 O O      . HOH G 4 .   ? 26.208 -1.825  9.518   1.00 23.50 ? 623 HOH A O      1 
HETATM 5741 O O      . HOH G 4 .   ? 12.672 -16.625 -12.171 1.00 24.32 ? 624 HOH A O      1 
HETATM 5742 O O      . HOH G 4 .   ? 31.838 -6.128  13.135  1.00 29.43 ? 625 HOH A O      1 
HETATM 5743 O O      . HOH G 4 .   ? 17.250 -17.196 1.258   1.00 25.68 ? 626 HOH A O      1 
HETATM 5744 O O      . HOH G 4 .   ? 4.083  9.481   -2.989  1.00 44.18 ? 627 HOH A O      1 
HETATM 5745 O O      . HOH G 4 .   ? 9.244  -24.992 1.746   1.00 35.36 ? 628 HOH A O      1 
HETATM 5746 O O      . HOH G 4 .   ? 20.039 1.567   22.269  1.00 25.95 ? 629 HOH A O      1 
HETATM 5747 O O      . HOH G 4 .   ? 30.567 5.101   -9.277  1.00 24.32 ? 630 HOH A O      1 
HETATM 5748 O O      . HOH G 4 .   ? 44.106 -7.708  -3.803  1.00 33.04 ? 631 HOH A O      1 
HETATM 5749 O O      . HOH G 4 .   ? 38.931 -6.251  -20.026 1.00 37.48 ? 632 HOH A O      1 
HETATM 5750 O O      . HOH G 4 .   ? 16.531 -19.466 -20.260 1.00 33.23 ? 633 HOH A O      1 
HETATM 5751 O O      . HOH G 4 .   ? 23.353 17.822  3.432   1.00 35.20 ? 634 HOH A O      1 
HETATM 5752 O O      . HOH G 4 .   ? 3.549  -17.307 19.082  1.00 49.26 ? 635 HOH A O      1 
HETATM 5753 O O      . HOH G 4 .   ? 39.400 3.491   14.834  1.00 47.58 ? 636 HOH A O      1 
HETATM 5754 O O      . HOH G 4 .   ? 28.760 -7.927  -19.444 1.00 25.85 ? 637 HOH A O      1 
HETATM 5755 O O      . HOH G 4 .   ? 39.058 14.572  0.036   1.00 35.84 ? 638 HOH A O      1 
HETATM 5756 O O      . HOH G 4 .   ? 6.861  -14.707 -4.439  1.00 27.07 ? 639 HOH A O      1 
HETATM 5757 O O      . HOH G 4 .   ? 18.598 -15.063 -22.890 1.00 29.16 ? 640 HOH A O      1 
HETATM 5758 O O      . HOH G 4 .   ? 22.477 -11.959 15.000  1.00 34.11 ? 641 HOH A O      1 
HETATM 5759 O O      . HOH G 4 .   ? 27.878 -14.129 -11.137 1.00 24.19 ? 642 HOH A O      1 
HETATM 5760 O O      . HOH G 4 .   ? 34.878 -1.559  3.422   1.00 21.63 ? 643 HOH A O      1 
HETATM 5761 O O      . HOH G 4 .   ? 27.623 14.064  -6.162  1.00 42.19 ? 644 HOH A O      1 
HETATM 5762 O O      . HOH G 4 .   ? 17.401 -14.590 5.237   1.00 24.65 ? 645 HOH A O      1 
HETATM 5763 O O      . HOH G 4 .   ? 34.412 -10.409 -5.460  1.00 39.93 ? 646 HOH A O      1 
HETATM 5764 O O      . HOH G 4 .   ? 34.925 18.204  2.215   1.00 28.64 ? 647 HOH A O      1 
HETATM 5765 O O      . HOH G 4 .   ? 31.055 -11.666 8.975   1.00 41.12 ? 648 HOH A O      1 
HETATM 5766 O O      . HOH G 4 .   ? 5.763  -9.012  2.729   1.00 24.26 ? 649 HOH A O      1 
HETATM 5767 O O      . HOH G 4 .   ? 10.192 17.294  0.464   1.00 41.02 ? 650 HOH A O      1 
HETATM 5768 O O      . HOH G 4 .   ? 22.843 12.874  -6.798  1.00 42.02 ? 651 HOH A O      1 
HETATM 5769 O O      . HOH G 4 .   ? 26.105 16.655  6.916   1.00 35.16 ? 652 HOH A O      1 
HETATM 5770 O O      . HOH G 4 .   ? 24.854 -8.108  12.167  1.00 28.12 ? 653 HOH A O      1 
HETATM 5771 O O      . HOH G 4 .   ? 16.940 -14.671 -10.324 1.00 22.71 ? 654 HOH A O      1 
HETATM 5772 O O      . HOH G 4 .   ? 9.409  13.504  -5.092  1.00 37.37 ? 655 HOH A O      1 
HETATM 5773 O O      . HOH G 4 .   ? 36.828 4.714   -15.483 1.00 37.40 ? 656 HOH A O      1 
HETATM 5774 O O      . HOH G 4 .   ? 31.463 -9.778  -18.040 1.00 31.53 ? 657 HOH A O      1 
HETATM 5775 O O      . HOH G 4 .   ? 45.307 2.803   -4.964  1.00 34.30 ? 658 HOH A O      1 
HETATM 5776 O O      . HOH G 4 .   ? 28.326 -0.318  -15.064 1.00 24.21 ? 659 HOH A O      1 
HETATM 5777 O O      . HOH G 4 .   ? 25.932 1.799   -5.871  1.00 22.16 ? 660 HOH A O      1 
HETATM 5778 O O      . HOH G 4 .   ? -3.075 3.299   4.391   1.00 39.01 ? 661 HOH A O      1 
HETATM 5779 O O      . HOH G 4 .   ? 29.914 9.291   11.267  1.00 23.56 ? 662 HOH A O      1 
HETATM 5780 O O      . HOH G 4 .   ? 24.637 8.539   24.029  1.00 32.86 ? 663 HOH A O      1 
HETATM 5781 O O      . HOH G 4 .   ? 24.972 -15.136 12.747  1.00 47.90 ? 664 HOH A O      1 
HETATM 5782 O O      . HOH G 4 .   ? 30.147 -5.867  -18.408 1.00 23.40 ? 665 HOH A O      1 
HETATM 5783 O O      . HOH G 4 .   ? 41.440 1.564   -9.336  1.00 31.72 ? 666 HOH A O      1 
HETATM 5784 O O      . HOH G 4 .   ? 8.223  12.161  9.130   1.00 36.74 ? 667 HOH A O      1 
HETATM 5785 O O      . HOH G 4 .   ? 24.204 -12.269 5.511   1.00 39.03 ? 668 HOH A O      1 
HETATM 5786 O O      . HOH G 4 .   ? 12.171 -0.005  -17.225 1.00 28.58 ? 669 HOH A O      1 
HETATM 5787 O O      . HOH G 4 .   ? 25.365 16.833  -3.624  1.00 38.84 ? 670 HOH A O      1 
HETATM 5788 O O      . HOH G 4 .   ? 35.008 2.643   -17.189 1.00 35.89 ? 671 HOH A O      1 
HETATM 5789 O O      . HOH G 4 .   ? 17.107 7.249   21.890  1.00 34.93 ? 672 HOH A O      1 
HETATM 5790 O O      . HOH G 4 .   ? 26.551 2.679   2.336   1.00 24.13 ? 673 HOH A O      1 
HETATM 5791 O O      . HOH G 4 .   ? 24.540 15.676  13.317  1.00 47.27 ? 674 HOH A O      1 
HETATM 5792 O O      . HOH G 4 .   ? 12.748 -24.671 6.817   1.00 33.93 ? 675 HOH A O      1 
HETATM 5793 O O      . HOH G 4 .   ? 1.232  1.300   -3.291  1.00 35.85 ? 676 HOH A O      1 
HETATM 5794 O O      . HOH G 4 .   ? 3.040  -27.544 -10.835 1.00 61.06 ? 677 HOH A O      1 
HETATM 5795 O O      . HOH G 4 .   ? 29.614 -10.658 -13.895 1.00 27.92 ? 678 HOH A O      1 
HETATM 5796 O O      . HOH G 4 .   ? 40.357 9.321   7.916   1.00 32.28 ? 679 HOH A O      1 
HETATM 5797 O O      . HOH G 4 .   ? 33.203 5.960   -3.931  1.00 23.26 ? 680 HOH A O      1 
HETATM 5798 O O      . HOH G 4 .   ? 10.373 -18.489 -14.984 1.00 34.98 ? 681 HOH A O      1 
HETATM 5799 O O      . HOH G 4 .   ? 9.248  -23.318 12.667  1.00 41.75 ? 682 HOH A O      1 
HETATM 5800 O O      . HOH G 4 .   ? 30.265 2.761   -12.658 1.00 27.86 ? 683 HOH A O      1 
HETATM 5801 O O      . HOH G 4 .   ? 39.370 0.127   -0.969  1.00 24.48 ? 684 HOH A O      1 
HETATM 5802 O O      . HOH G 4 .   ? 37.056 12.637  17.491  1.00 40.15 ? 685 HOH A O      1 
HETATM 5803 O O      . HOH G 4 .   ? 12.939 -27.891 -6.904  1.00 28.92 ? 686 HOH A O      1 
HETATM 5804 O O      . HOH G 4 .   ? 39.849 -1.314  6.865   1.00 37.86 ? 687 HOH A O      1 
HETATM 5805 O O      . HOH G 4 .   ? 25.255 -22.136 -6.706  1.00 39.80 ? 688 HOH A O      1 
HETATM 5806 O O      . HOH G 4 .   ? 16.567 17.767  8.276   1.00 52.50 ? 689 HOH A O      1 
HETATM 5807 O O      . HOH G 4 .   ? -2.185 -0.583  2.965   1.00 45.24 ? 690 HOH A O      1 
HETATM 5808 O O      . HOH G 4 .   ? 43.563 6.900   6.791   1.00 37.17 ? 691 HOH A O      1 
HETATM 5809 O O      . HOH G 4 .   ? 18.570 -18.684 3.427   1.00 37.38 ? 692 HOH A O      1 
HETATM 5810 O O      . HOH G 4 .   ? 9.925  -27.858 -6.156  1.00 40.37 ? 693 HOH A O      1 
HETATM 5811 O O      . HOH G 4 .   ? 4.924  -0.311  -16.890 1.00 37.58 ? 694 HOH A O      1 
HETATM 5812 O O      . HOH G 4 .   ? 20.079 -7.179  -18.668 1.00 22.27 ? 695 HOH A O      1 
HETATM 5813 O O      . HOH G 4 .   ? 22.471 5.592   -16.492 1.00 36.99 ? 696 HOH A O      1 
HETATM 5814 O O      . HOH G 4 .   ? 27.239 0.757   4.280   1.00 19.83 ? 697 HOH A O      1 
HETATM 5815 O O      . HOH G 4 .   ? 19.332 10.870  16.524  1.00 35.38 ? 698 HOH A O      1 
HETATM 5816 O O      . HOH G 4 .   ? 20.759 15.777  7.832   1.00 38.50 ? 699 HOH A O      1 
HETATM 5817 O O      . HOH G 4 .   ? 10.070 -25.373 -9.559  1.00 35.01 ? 700 HOH A O      1 
HETATM 5818 O O      . HOH G 4 .   ? 39.579 7.406   15.530  1.00 44.49 ? 701 HOH A O      1 
HETATM 5819 O O      . HOH G 4 .   ? 14.569 -17.967 14.077  1.00 31.56 ? 702 HOH A O      1 
HETATM 5820 O O      . HOH G 4 .   ? 13.278 -23.443 3.979   1.00 32.17 ? 703 HOH A O      1 
HETATM 5821 O O      . HOH G 4 .   ? 18.885 14.015  -15.035 1.00 44.08 ? 704 HOH A O      1 
HETATM 5822 O O      . HOH G 4 .   ? 11.730 -3.869  17.000  1.00 23.60 ? 705 HOH A O      1 
HETATM 5823 O O      . HOH G 4 .   ? 30.215 -2.372  25.982  1.00 28.78 ? 706 HOH A O      1 
HETATM 5824 O O      . HOH G 4 .   ? 25.254 6.270   -14.955 1.00 48.66 ? 707 HOH A O      1 
HETATM 5825 O O      . HOH G 4 .   ? 5.359  -14.700 21.214  1.00 48.27 ? 708 HOH A O      1 
HETATM 5826 O O      . HOH G 4 .   ? 30.466 -6.004  6.304   1.00 37.53 ? 709 HOH A O      1 
HETATM 5827 O O      . HOH G 4 .   ? 4.468  2.365   -16.984 1.00 41.60 ? 710 HOH A O      1 
HETATM 5828 O O      . HOH G 4 .   ? 15.472 -3.703  -21.645 1.00 40.26 ? 711 HOH A O      1 
HETATM 5829 O O      . HOH G 4 .   ? 25.778 -19.681 -1.056  1.00 40.92 ? 712 HOH A O      1 
HETATM 5830 O O      . HOH G 4 .   ? 11.625 -3.025  24.828  1.00 28.10 ? 713 HOH A O      1 
HETATM 5831 O O      . HOH G 4 .   ? 29.123 -15.125 -8.515  1.00 33.13 ? 714 HOH A O      1 
HETATM 5832 O O      . HOH G 4 .   ? 29.499 8.697   22.147  1.00 24.96 ? 715 HOH A O      1 
HETATM 5833 O O      . HOH G 4 .   ? 27.409 -0.389  -6.713  1.00 21.58 ? 716 HOH A O      1 
HETATM 5834 O O      . HOH G 4 .   ? 32.606 -7.031  -6.264  1.00 24.41 ? 717 HOH A O      1 
HETATM 5835 O O      . HOH G 4 .   ? 0.527  4.953   1.184   1.00 46.75 ? 718 HOH A O      1 
HETATM 5836 O O      . HOH G 4 .   ? 33.665 -13.259 -18.019 1.00 37.04 ? 719 HOH A O      1 
HETATM 5837 O O      . HOH G 4 .   ? 8.405  6.875   18.528  1.00 40.44 ? 720 HOH A O      1 
HETATM 5838 O O      . HOH G 4 .   ? 16.418 4.688   22.624  1.00 37.50 ? 721 HOH A O      1 
HETATM 5839 O O      . HOH G 4 .   ? 29.251 -7.718  20.314  1.00 39.42 ? 722 HOH A O      1 
HETATM 5840 O O      . HOH G 4 .   ? 1.731  -2.589  13.219  1.00 41.25 ? 723 HOH A O      1 
HETATM 5841 O O      . HOH G 4 .   ? 2.484  5.526   8.782   1.00 45.13 ? 724 HOH A O      1 
HETATM 5842 O O      . HOH G 4 .   ? 31.880 -13.648 -5.543  1.00 44.08 ? 725 HOH A O      1 
HETATM 5843 O O      . HOH G 4 .   ? 31.511 0.476   21.852  1.00 29.33 ? 726 HOH A O      1 
HETATM 5844 O O      . HOH G 4 .   ? -0.579 -12.454 -5.158  1.00 37.72 ? 727 HOH A O      1 
HETATM 5845 O O      . HOH G 4 .   ? 7.829  -21.718 -14.659 1.00 34.42 ? 728 HOH A O      1 
HETATM 5846 O O      . HOH G 4 .   ? 15.769 -5.719  -20.548 1.00 27.29 ? 729 HOH A O      1 
HETATM 5847 O O      . HOH G 4 .   ? 42.855 -4.311  -10.368 1.00 29.27 ? 730 HOH A O      1 
HETATM 5848 O O      . HOH G 4 .   ? 21.264 -23.678 -4.130  1.00 35.67 ? 731 HOH A O      1 
HETATM 5849 O O      . HOH G 4 .   ? 6.426  -9.013  18.404  1.00 52.53 ? 732 HOH A O      1 
HETATM 5850 O O      . HOH G 4 .   ? 5.897  3.701   10.130  1.00 29.77 ? 733 HOH A O      1 
HETATM 5851 O O      . HOH G 4 .   ? 27.494 -11.703 -18.204 1.00 25.88 ? 734 HOH A O      1 
HETATM 5852 O O      . HOH G 4 .   ? 4.698  -16.375 -4.334  1.00 27.40 ? 735 HOH A O      1 
HETATM 5853 O O      . HOH G 4 .   ? 35.207 17.289  -3.577  1.00 44.44 ? 736 HOH A O      1 
HETATM 5854 O O      . HOH G 4 .   ? 7.286  -15.274 -15.793 1.00 42.94 ? 737 HOH A O      1 
HETATM 5855 O O      . HOH G 4 .   ? 0.205  -4.900  12.516  1.00 29.76 ? 738 HOH A O      1 
HETATM 5856 O O      . HOH G 4 .   ? 3.603  5.766   -4.581  1.00 44.59 ? 739 HOH A O      1 
HETATM 5857 O O      . HOH G 4 .   ? 16.139 17.147  4.024   1.00 42.75 ? 740 HOH A O      1 
HETATM 5858 O O      . HOH G 4 .   ? 44.209 -8.501  5.487   1.00 44.35 ? 741 HOH A O      1 
HETATM 5859 O O      . HOH G 4 .   ? 19.472 -24.755 -11.679 1.00 46.52 ? 742 HOH A O      1 
HETATM 5860 O O      . HOH G 4 .   ? 18.662 -13.259 18.752  1.00 41.91 ? 743 HOH A O      1 
HETATM 5861 O O      . HOH G 4 .   ? 32.452 5.601   22.374  1.00 27.93 ? 744 HOH A O      1 
HETATM 5862 O O      . HOH G 4 .   ? 36.300 19.165  10.870  1.00 44.38 ? 745 HOH A O      1 
HETATM 5863 O O      . HOH G 4 .   ? 17.047 11.796  -21.166 1.00 53.90 ? 746 HOH A O      1 
HETATM 5864 O O      . HOH G 4 .   ? 35.639 11.142  19.713  1.00 33.13 ? 747 HOH A O      1 
HETATM 5865 O O      . HOH G 4 .   ? 13.154 -27.370 -0.068  1.00 33.21 ? 748 HOH A O      1 
HETATM 5866 O O      . HOH G 4 .   ? 34.605 3.483   20.320  1.00 36.90 ? 749 HOH A O      1 
HETATM 5867 O O      . HOH G 4 .   ? 37.876 -3.059  15.079  1.00 42.15 ? 750 HOH A O      1 
HETATM 5868 O O      . HOH G 4 .   ? 48.765 -3.332  -0.867  1.00 53.11 ? 751 HOH A O      1 
HETATM 5869 O O      . HOH G 4 .   ? 24.723 11.567  20.517  1.00 43.70 ? 752 HOH A O      1 
HETATM 5870 O O      . HOH G 4 .   ? 36.836 -11.470 -2.675  1.00 37.73 ? 753 HOH A O      1 
HETATM 5871 O O      . HOH G 4 .   ? 34.977 11.666  -6.316  1.00 43.15 ? 754 HOH A O      1 
HETATM 5872 O O      . HOH G 4 .   ? 7.606  8.657   17.245  1.00 43.87 ? 755 HOH A O      1 
HETATM 5873 O O      . HOH G 4 .   ? 7.612  10.134  -12.923 1.00 45.26 ? 756 HOH A O      1 
HETATM 5874 O O      . HOH G 4 .   ? 17.119 -6.951  25.147  1.00 27.52 ? 757 HOH A O      1 
HETATM 5875 O O      . HOH G 4 .   ? 47.216 -3.375  -3.136  1.00 46.42 ? 758 HOH A O      1 
HETATM 5876 O O      . HOH G 4 .   ? 40.310 -13.010 -11.714 1.00 40.41 ? 759 HOH A O      1 
HETATM 5877 O O      . HOH G 4 .   ? 17.350 2.056   22.505  1.00 32.70 ? 760 HOH A O      1 
HETATM 5878 O O      . HOH G 4 .   ? 15.675 15.290  -6.517  1.00 41.46 ? 761 HOH A O      1 
HETATM 5879 O O      . HOH G 4 .   ? 18.608 -17.432 11.233  1.00 49.86 ? 762 HOH A O      1 
HETATM 5880 O O      . HOH G 4 .   ? 15.105 -22.410 -17.707 1.00 52.28 ? 763 HOH A O      1 
HETATM 5881 O O      . HOH G 4 .   ? 29.809 -15.216 -6.159  1.00 47.84 ? 764 HOH A O      1 
HETATM 5882 O O      . HOH G 4 .   ? 2.232  -8.396  15.052  1.00 46.43 ? 765 HOH A O      1 
HETATM 5883 O O      . HOH G 4 .   ? 39.319 -5.695  -16.002 1.00 44.08 ? 766 HOH A O      1 
HETATM 5884 O O      . HOH G 4 .   ? 17.075 17.103  -6.351  1.00 56.64 ? 767 HOH A O      1 
HETATM 5885 O O      . HOH G 4 .   ? 8.406  -3.162  -16.157 1.00 38.48 ? 768 HOH A O      1 
HETATM 5886 O O      . HOH G 4 .   ? 33.267 -0.822  23.438  1.00 38.58 ? 769 HOH A O      1 
HETATM 5887 O O      . HOH G 4 .   ? 30.490 15.826  -4.124  1.00 47.86 ? 770 HOH A O      1 
HETATM 5888 O O      . HOH G 4 .   ? 17.234 14.091  -11.110 1.00 48.62 ? 771 HOH A O      1 
HETATM 5889 O O      . HOH G 4 .   ? 18.621 14.241  13.240  1.00 44.44 ? 772 HOH A O      1 
HETATM 5890 O O      . HOH G 4 .   ? -3.251 0.307   5.091   1.00 45.76 ? 773 HOH A O      1 
HETATM 5891 O O      . HOH G 4 .   ? 10.239 -4.334  20.258  1.00 43.10 ? 774 HOH A O      1 
HETATM 5892 O O      . HOH G 4 .   ? 32.715 -9.423  -1.806  1.00 40.87 ? 775 HOH A O      1 
HETATM 5893 O O      . HOH G 4 .   ? 29.019 -7.642  23.082  1.00 48.58 ? 776 HOH A O      1 
HETATM 5894 O O      . HOH G 4 .   ? 17.921 0.704   -22.637 1.00 44.85 ? 777 HOH A O      1 
HETATM 5895 O O      . HOH G 4 .   ? 29.816 -11.475 -16.668 1.00 29.16 ? 778 HOH A O      1 
HETATM 5896 O O      . HOH G 4 .   ? 5.682  5.453   -17.562 1.00 42.83 ? 779 HOH A O      1 
HETATM 5897 O O      . HOH G 4 .   ? 26.109 -1.453  12.342  1.00 38.35 ? 780 HOH A O      1 
HETATM 5898 O O      . HOH G 4 .   ? 3.279  -13.030 16.848  1.00 59.76 ? 781 HOH A O      1 
HETATM 5899 O O      . HOH G 4 .   ? 14.491 14.916  -11.216 1.00 52.97 ? 782 HOH A O      1 
HETATM 5900 O O      . HOH G 4 .   ? 33.311 -15.294 -10.373 1.00 48.98 ? 783 HOH A O      1 
HETATM 5901 O O      . HOH G 4 .   ? 5.488  -12.401 -14.071 1.00 51.35 ? 784 HOH A O      1 
HETATM 5902 O O      . HOH G 4 .   ? 32.054 -12.046 -7.677  1.00 30.85 ? 785 HOH A O      1 
HETATM 5903 O O      . HOH G 4 .   ? 7.084  3.271   21.274  1.00 54.85 ? 786 HOH A O      1 
HETATM 5904 O O      . HOH G 4 .   ? 1.764  -2.081  -15.315 1.00 44.56 ? 787 HOH A O      1 
HETATM 5905 O O      . HOH G 4 .   ? 38.216 -14.046 -11.525 1.00 48.99 ? 788 HOH A O      1 
HETATM 5906 O O      . HOH G 4 .   ? 24.708 2.166   23.071  1.00 33.79 ? 789 HOH A O      1 
HETATM 5907 O O      . HOH G 4 .   ? 7.937  -1.348  19.510  1.00 47.66 ? 790 HOH A O      1 
HETATM 5908 O O      . HOH G 4 .   ? 14.167 18.141  2.811   1.00 42.57 ? 791 HOH A O      1 
HETATM 5909 O O      . HOH G 4 .   ? 7.445  1.005   19.670  1.00 44.39 ? 792 HOH A O      1 
HETATM 5910 O O      . HOH G 4 .   ? 42.517 9.504   6.527   1.00 43.75 ? 793 HOH A O      1 
HETATM 5911 O O      . HOH G 4 .   ? 14.794 8.566   22.039  1.00 33.58 ? 794 HOH A O      1 
HETATM 5912 O O      . HOH G 4 .   ? 16.452 -13.388 17.022  1.00 46.49 ? 795 HOH A O      1 
HETATM 5913 O O      . HOH G 4 .   ? 7.059  13.192  -6.509  1.00 43.54 ? 796 HOH A O      1 
HETATM 5914 O O      . HOH G 4 .   ? 44.534 7.978   -3.743  1.00 51.24 ? 797 HOH A O      1 
HETATM 5915 O O      . HOH G 4 .   ? 20.270 14.712  11.792  1.00 38.80 ? 798 HOH A O      1 
HETATM 5916 O O      . HOH G 4 .   ? 32.818 13.408  -6.120  1.00 49.90 ? 799 HOH A O      1 
HETATM 5917 O O      . HOH G 4 .   ? 41.753 -12.923 -9.351  1.00 55.77 ? 800 HOH A O      1 
HETATM 5918 O O      . HOH G 4 .   ? 34.184 12.558  21.931  1.00 55.69 ? 801 HOH A O      1 
HETATM 5919 O O      . HOH G 4 .   ? 36.492 -13.888 -5.564  1.00 52.47 ? 802 HOH A O      1 
HETATM 5920 O O      . HOH G 4 .   ? 17.131 16.323  -8.122  1.00 53.84 ? 803 HOH A O      1 
HETATM 5921 O O      . HOH G 4 .   ? 8.749  -27.305 -8.627  1.00 44.37 ? 804 HOH A O      1 
HETATM 5922 O O      . HOH G 4 .   ? 18.815 9.158   22.986  1.00 46.58 ? 805 HOH A O      1 
HETATM 5923 O O      . HOH G 4 .   ? 6.719  10.930  18.814  1.00 48.45 ? 806 HOH A O      1 
HETATM 5924 O O      . HOH G 4 .   ? -0.304 5.488   9.368   1.00 45.09 ? 807 HOH A O      1 
HETATM 5925 O O      . HOH G 4 .   ? 46.046 5.490   5.931   1.00 44.46 ? 808 HOH A O      1 
HETATM 5926 O O      . HOH G 4 .   ? 28.836 -17.648 -16.132 1.00 48.53 ? 809 HOH A O      1 
HETATM 5927 O O      . HOH G 4 .   ? 24.084 12.745  15.249  1.00 38.12 ? 810 HOH A O      1 
HETATM 5928 O O      . HOH G 4 .   ? 22.839 6.165   -21.015 1.00 56.14 ? 811 HOH A O      1 
HETATM 5929 O O      . HOH G 4 .   ? 30.135 11.214  23.090  1.00 34.92 ? 812 HOH A O      1 
HETATM 5930 O O      . HOH G 4 .   ? 39.198 10.972  17.866  1.00 53.37 ? 813 HOH A O      1 
HETATM 5931 O O      . HOH G 4 .   ? 17.746 13.276  16.020  1.00 46.45 ? 814 HOH A O      1 
HETATM 5932 O O      . HOH G 4 .   ? 5.354  -7.438  18.761  1.00 45.93 ? 815 HOH A O      1 
HETATM 5933 O O      . HOH G 4 .   ? 5.163  7.775   16.511  1.00 46.51 ? 816 HOH A O      1 
HETATM 5934 O O      . HOH G 4 .   ? 14.476 -7.896  -21.712 1.00 39.87 ? 817 HOH A O      1 
HETATM 5935 O O      . HOH G 4 .   ? 42.125 5.083   -7.640  1.00 43.77 ? 818 HOH A O      1 
HETATM 5936 O O      . HOH G 4 .   ? 18.926 17.343  6.716   1.00 45.00 ? 819 HOH A O      1 
HETATM 5937 O O      . HOH G 4 .   ? 11.843 -13.467 -21.625 1.00 52.57 ? 820 HOH A O      1 
HETATM 5938 O O      . HOH G 4 .   ? 10.295 -1.808  -18.037 1.00 45.54 ? 821 HOH A O      1 
HETATM 5939 O O      . HOH G 4 .   ? 36.659 -8.192  17.280  1.00 49.91 ? 822 HOH A O      1 
HETATM 5940 O O      . HOH G 4 .   ? 23.538 8.031   26.462  1.00 30.99 ? 823 HOH A O      1 
HETATM 5941 O O      . HOH G 4 .   ? 25.490 -21.862 -4.488  1.00 53.45 ? 824 HOH A O      1 
HETATM 5942 O O      . HOH G 4 .   ? 16.558 2.383   -21.858 1.00 41.89 ? 825 HOH A O      1 
HETATM 5943 O O      . HOH G 4 .   ? 25.033 11.032  23.625  1.00 46.51 ? 826 HOH A O      1 
HETATM 5944 O O      . HOH G 4 .   ? 17.156 -10.996 25.713  1.00 40.07 ? 827 HOH A O      1 
HETATM 5945 O O      . HOH G 4 .   ? 27.989 16.551  -5.233  1.00 50.90 ? 828 HOH A O      1 
HETATM 5946 O O      . HOH G 4 .   ? 30.048 -12.638 -12.323 1.00 26.81 ? 829 HOH A O      1 
HETATM 5947 O O      . HOH G 4 .   ? 3.798  5.317   10.873  1.00 42.41 ? 830 HOH A O      1 
HETATM 5948 O O      . HOH G 4 .   ? 35.080 12.429  -9.453  1.00 54.41 ? 831 HOH A O      1 
HETATM 5949 O O      . HOH G 4 .   ? 24.180 -20.483 -16.993 1.00 48.74 ? 832 HOH A O      1 
HETATM 5950 O O      . HOH G 4 .   ? 11.636 -25.157 2.858   1.00 36.98 ? 833 HOH A O      1 
HETATM 5951 O O      . HOH G 4 .   ? 8.752  9.748   -14.458 1.00 46.72 ? 834 HOH A O      1 
HETATM 5952 O O      . HOH G 4 .   ? 10.665 15.829  -6.300  1.00 44.87 ? 835 HOH A O      1 
HETATM 5953 O O      . HOH G 4 .   ? 38.159 9.833   20.371  1.00 48.31 ? 836 HOH A O      1 
HETATM 5954 O O      . HOH G 4 .   ? 24.125 13.408  -8.962  1.00 42.49 ? 837 HOH A O      1 
HETATM 5955 O O      . HOH G 4 .   ? 39.811 17.241  10.075  1.00 49.21 ? 838 HOH A O      1 
HETATM 5956 O O      . HOH G 4 .   ? 18.129 -15.207 20.387  1.00 51.77 ? 839 HOH A O      1 
HETATM 5957 O O      . HOH G 4 .   ? 45.126 0.057   -6.896  1.00 44.18 ? 840 HOH A O      1 
HETATM 5958 O O      . HOH G 4 .   ? 31.728 -9.747  -5.958  1.00 31.16 ? 841 HOH A O      1 
HETATM 5959 O O      . HOH G 4 .   ? 30.915 -13.233 -9.813  1.00 32.86 ? 842 HOH A O      1 
HETATM 5960 O O      . HOH G 4 .   ? 34.716 6.679   22.990  1.00 37.63 ? 843 HOH A O      1 
HETATM 5961 O O      . HOH G 4 .   ? 31.242 -14.363 -14.113 1.00 35.31 ? 844 HOH A O      1 
HETATM 5962 O O      . HOH G 4 .   ? 1.178  -4.640  -15.470 1.00 39.41 ? 845 HOH A O      1 
HETATM 5963 O O      . HOH G 4 .   ? 6.817  7.425   20.880  1.00 45.31 ? 846 HOH A O      1 
HETATM 5964 O O      . HOH G 4 .   ? -0.708 2.568   -2.456  1.00 48.17 ? 847 HOH A O      1 
HETATM 5965 O O      . HOH G 4 .   ? 19.071 7.415   25.627  1.00 45.28 ? 848 HOH A O      1 
HETATM 5966 O O      . HOH G 4 .   ? 33.788 22.695  -3.282  1.00 39.20 ? 849 HOH A O      1 
HETATM 5967 O O      . HOH G 4 .   ? 18.990 18.041  4.408   1.00 47.92 ? 850 HOH A O      1 
HETATM 5968 O O      . HOH G 4 .   ? 24.428 -10.477 13.978  1.00 36.38 ? 851 HOH A O      1 
HETATM 5969 O O      . HOH G 4 .   ? 20.975 16.405  10.177  1.00 45.15 ? 852 HOH A O      1 
HETATM 5970 O O      . HOH G 4 .   ? 19.073 -16.832 21.393  1.00 56.67 ? 853 HOH A O      1 
HETATM 5971 O O      . HOH G 4 .   ? 21.600 12.215  17.160  1.00 41.54 ? 854 HOH A O      1 
HETATM 5972 O O      . HOH G 4 .   ? 38.894 -14.317 -6.735  1.00 53.77 ? 855 HOH A O      1 
HETATM 5973 O O      . HOH G 4 .   ? 23.429 17.250  6.384   1.00 43.98 ? 856 HOH A O      1 
HETATM 5974 O O      . HOH G 4 .   ? 2.441  -17.961 -8.275  1.00 49.82 ? 857 HOH A O      1 
HETATM 5975 O O      . HOH G 4 .   ? 15.333 -25.062 11.663  1.00 47.96 ? 858 HOH A O      1 
HETATM 5976 O O      . HOH G 4 .   ? 43.180 3.115   -9.125  1.00 45.31 ? 859 HOH A O      1 
HETATM 5977 O O      . HOH G 4 .   ? 30.924 -1.124  -15.470 1.00 26.97 ? 860 HOH A O      1 
HETATM 5978 O O      . HOH G 4 .   ? 0.739  -14.557 -5.934  1.00 41.42 ? 861 HOH A O      1 
HETATM 5979 O O      . HOH G 4 .   ? 17.206 -17.642 -22.346 1.00 30.66 ? 862 HOH A O      1 
HETATM 5980 O O      . HOH G 4 .   ? 7.728  9.119   -16.855 1.00 44.28 ? 863 HOH A O      1 
HETATM 5981 O O      . HOH G 4 .   ? 7.965  14.223  -3.088  1.00 41.28 ? 864 HOH A O      1 
HETATM 5982 O O      . HOH G 4 .   ? 8.935  17.498  -2.246  1.00 49.77 ? 865 HOH A O      1 
HETATM 5983 O O      . HOH G 4 .   ? 41.312 -13.895 -7.581  1.00 58.76 ? 866 HOH A O      1 
HETATM 5984 O O      . HOH G 4 .   ? 2.931  -1.275  -17.379 1.00 44.86 ? 867 HOH A O      1 
HETATM 5985 O O      . HOH G 4 .   ? 35.015 20.720  -1.741  1.00 41.35 ? 868 HOH A O      1 
HETATM 5986 O O      . HOH G 4 .   ? 3.053  -16.050 -6.536  1.00 34.37 ? 869 HOH A O      1 
HETATM 5987 O O      . HOH G 4 .   ? 47.731 3.733   -4.260  1.00 45.70 ? 870 HOH A O      1 
HETATM 5988 O O      . HOH G 4 .   ? 31.282 -13.556 -16.712 1.00 35.24 ? 871 HOH A O      1 
HETATM 5989 O O      . HOH G 4 .   ? 32.899 2.940   22.553  1.00 30.81 ? 872 HOH A O      1 
HETATM 5990 O O      . HOH G 4 .   ? 34.673 9.277   23.968  1.00 43.80 ? 873 HOH A O      1 
HETATM 5991 O O      . HOH G 4 .   ? 20.881 -22.169 -19.694 1.00 46.82 ? 874 HOH A O      1 
HETATM 5992 O O      . HOH G 4 .   ? 45.324 2.346   -7.564  1.00 42.23 ? 875 HOH A O      1 
HETATM 5993 O O      . HOH G 4 .   ? 22.316 10.148  26.931  1.00 39.85 ? 876 HOH A O      1 
HETATM 5994 O O      . HOH G 4 .   ? 2.506  5.410   12.800  1.00 47.76 ? 877 HOH A O      1 
HETATM 5995 O O      . HOH G 4 .   ? 2.814  -16.837 -11.099 1.00 51.75 ? 878 HOH A O      1 
HETATM 5996 O O      . HOH G 4 .   ? 18.632 18.135  10.809  1.00 55.61 ? 879 HOH A O      1 
HETATM 5997 O O      . HOH G 4 .   ? 3.285  -11.122 19.109  1.00 51.12 ? 880 HOH A O      1 
HETATM 5998 O O      . HOH G 4 .   ? 14.651 -10.588 -23.179 1.00 38.44 ? 881 HOH A O      1 
HETATM 5999 O O      . HOH G 4 .   ? 27.924 12.372  23.615  1.00 45.31 ? 882 HOH A O      1 
HETATM 6000 O O      . HOH G 4 .   ? 30.705 12.727  -12.361 1.00 49.12 ? 883 HOH A O      1 
HETATM 6001 O O      . HOH G 4 .   ? 29.728 11.603  -14.275 1.00 51.32 ? 884 HOH A O      1 
HETATM 6002 O O      . HOH G 4 .   ? 3.578  -17.923 -13.125 1.00 47.13 ? 885 HOH A O      1 
HETATM 6003 O O      . HOH G 4 .   ? 36.325 5.110   24.461  1.00 38.28 ? 886 HOH A O      1 
HETATM 6004 O O      . HOH H 4 .   ? 12.764 -21.260 39.344  1.00 40.41 ? 501 HOH B O      1 
HETATM 6005 O O      . HOH H 4 .   ? 24.493 7.679   62.214  1.00 46.29 ? 502 HOH B O      1 
HETATM 6006 O O      . HOH H 4 .   ? 26.185 -1.142  69.480  1.00 47.19 ? 503 HOH B O      1 
HETATM 6007 O O      . HOH H 4 .   ? 19.597 5.055   63.834  1.00 42.41 ? 504 HOH B O      1 
HETATM 6008 O O      . HOH H 4 .   ? 16.341 -17.756 66.304  1.00 45.61 ? 505 HOH B O      1 
HETATM 6009 O O      . HOH H 4 .   ? 20.926 12.725  53.066  1.00 44.71 ? 506 HOH B O      1 
HETATM 6010 O O      . HOH H 4 .   ? 32.274 -13.575 25.704  1.00 54.01 ? 507 HOH B O      1 
HETATM 6011 O O      . HOH H 4 .   ? 13.742 5.064   37.289  1.00 47.51 ? 508 HOH B O      1 
HETATM 6012 O O      . HOH H 4 .   ? 43.649 -0.156  33.614  1.00 48.55 ? 509 HOH B O      1 
HETATM 6013 O O      . HOH H 4 .   ? 41.321 1.279   62.893  1.00 43.08 ? 510 HOH B O      1 
HETATM 6014 O O      . HOH H 4 .   ? 12.113 -2.453  38.385  1.00 32.97 ? 511 HOH B O      1 
HETATM 6015 O O      . HOH H 4 .   ? 24.307 3.606   49.869  1.00 33.30 ? 512 HOH B O      1 
HETATM 6016 O O      . HOH H 4 .   ? 12.685 -3.226  50.474  1.00 34.04 ? 513 HOH B O      1 
HETATM 6017 O O      . HOH H 4 .   ? 42.742 -13.809 35.243  1.00 51.71 ? 514 HOH B O      1 
HETATM 6018 O O      . HOH H 4 .   ? 27.030 7.920   22.671  1.00 29.64 ? 515 HOH B O      1 
HETATM 6019 O O      . HOH H 4 .   ? 28.391 -0.986  36.746  1.00 28.10 ? 516 HOH B O      1 
HETATM 6020 O O      . HOH H 4 .   ? 6.692  -0.229  26.607  1.00 49.96 ? 517 HOH B O      1 
HETATM 6021 O O      . HOH H 4 .   ? 40.485 -12.656 38.951  1.00 41.83 ? 518 HOH B O      1 
HETATM 6022 O O      . HOH H 4 .   ? 42.014 -9.553  47.370  1.00 40.47 ? 519 HOH B O      1 
HETATM 6023 O O      . HOH H 4 .   ? 32.157 -2.683  65.415  1.00 41.81 ? 520 HOH B O      1 
HETATM 6024 O O      . HOH H 4 .   ? 16.186 0.334   28.633  1.00 40.27 ? 521 HOH B O      1 
HETATM 6025 O O      . HOH H 4 .   ? 15.112 -24.039 56.961  1.00 48.22 ? 522 HOH B O      1 
HETATM 6026 O O      . HOH H 4 .   ? 10.777 1.984   36.419  1.00 37.45 ? 523 HOH B O      1 
HETATM 6027 O O      . HOH H 4 .   ? 18.003 11.110  43.218  1.00 40.81 ? 524 HOH B O      1 
HETATM 6028 O O      . HOH H 4 .   ? 24.579 6.416   28.369  1.00 26.65 ? 525 HOH B O      1 
HETATM 6029 O O      . HOH H 4 .   ? 26.664 18.054  54.029  1.00 50.93 ? 526 HOH B O      1 
HETATM 6030 O O      . HOH H 4 .   ? 42.427 -10.952 40.943  1.00 35.56 ? 527 HOH B O      1 
HETATM 6031 O O      . HOH H 4 .   ? 34.171 2.635   29.067  1.00 38.62 ? 528 HOH B O      1 
HETATM 6032 O O      . HOH H 4 .   ? 29.516 -14.941 66.403  1.00 41.26 ? 529 HOH B O      1 
HETATM 6033 O O      . HOH H 4 .   ? 4.120  -25.582 50.020  1.00 30.25 ? 530 HOH B O      1 
HETATM 6034 O O      . HOH H 4 .   ? 0.368  -16.314 38.083  1.00 42.27 ? 531 HOH B O      1 
HETATM 6035 O O      . HOH H 4 .   ? 17.003 -18.705 39.990  1.00 26.38 ? 532 HOH B O      1 
HETATM 6036 O O      . HOH H 4 .   ? 17.404 6.855   43.321  1.00 40.98 ? 533 HOH B O      1 
HETATM 6037 O O      . HOH H 4 .   ? 41.573 12.416  42.202  1.00 40.74 ? 534 HOH B O      1 
HETATM 6038 O O      . HOH H 4 .   ? 28.554 12.904  29.008  1.00 43.18 ? 535 HOH B O      1 
HETATM 6039 O O      . HOH H 4 .   ? 33.671 -8.339  59.123  1.00 25.81 ? 536 HOH B O      1 
HETATM 6040 O O      . HOH H 4 .   ? 13.710 6.163   29.403  1.00 38.80 ? 537 HOH B O      1 
HETATM 6041 O O      . HOH H 4 .   ? 19.207 -11.785 45.526  1.00 23.19 ? 538 HOH B O      1 
HETATM 6042 O O      . HOH H 4 .   ? 31.641 2.973   64.407  1.00 34.11 ? 539 HOH B O      1 
HETATM 6043 O O      . HOH H 4 .   ? 23.950 -3.505  35.757  1.00 22.35 ? 540 HOH B O      1 
HETATM 6044 O O      . HOH H 4 .   ? 2.967  -2.282  36.614  1.00 37.24 ? 541 HOH B O      1 
HETATM 6045 O O      . HOH H 4 .   ? 45.286 2.244   44.120  1.00 43.15 ? 542 HOH B O      1 
HETATM 6046 O O      . HOH H 4 .   ? 6.454  -20.509 62.794  1.00 34.22 ? 543 HOH B O      1 
HETATM 6047 O O      . HOH H 4 .   ? 7.260  -28.472 51.537  1.00 33.56 ? 544 HOH B O      1 
HETATM 6048 O O      . HOH H 4 .   ? 2.890  -14.092 55.562  1.00 37.34 ? 545 HOH B O      1 
HETATM 6049 O O      . HOH H 4 .   ? 9.310  0.243   39.135  1.00 32.85 ? 546 HOH B O      1 
HETATM 6050 O O      . HOH H 4 .   ? 43.420 4.285   49.694  1.00 41.14 ? 547 HOH B O      1 
HETATM 6051 O O      . HOH H 4 .   ? 35.309 2.096   48.232  1.00 23.95 ? 548 HOH B O      1 
HETATM 6052 O O      . HOH H 4 .   ? 2.548  -12.890 57.844  1.00 36.30 ? 549 HOH B O      1 
HETATM 6053 O O      . HOH H 4 .   ? 23.778 7.285   67.563  1.00 46.46 ? 550 HOH B O      1 
HETATM 6054 O O      . HOH H 4 .   ? 34.002 0.580   63.882  1.00 29.24 ? 551 HOH B O      1 
HETATM 6055 O O      . HOH H 4 .   ? 2.126  -10.368 59.672  1.00 43.72 ? 552 HOH B O      1 
HETATM 6056 O O      . HOH H 4 .   ? 27.789 0.198   39.845  1.00 23.91 ? 553 HOH B O      1 
HETATM 6057 O O      . HOH H 4 .   ? 24.875 8.748   34.953  1.00 27.46 ? 554 HOH B O      1 
HETATM 6058 O O      . HOH H 4 .   ? -1.187 -5.836  42.992  1.00 41.19 ? 555 HOH B O      1 
HETATM 6059 O O      . HOH H 4 .   ? 5.041  -0.192  57.603  1.00 49.29 ? 556 HOH B O      1 
HETATM 6060 O O      . HOH H 4 .   ? 35.419 -11.087 56.555  1.00 40.11 ? 557 HOH B O      1 
HETATM 6061 O O      . HOH H 4 .   ? 1.798  -13.536 34.178  1.00 41.18 ? 558 HOH B O      1 
HETATM 6062 O O      . HOH H 4 .   ? 44.702 -2.224  53.859  1.00 45.86 ? 559 HOH B O      1 
HETATM 6063 O O      . HOH H 4 .   ? 28.886 15.709  36.636  1.00 32.77 ? 560 HOH B O      1 
HETATM 6064 O O      . HOH H 4 .   ? 14.367 -18.466 39.337  1.00 29.65 ? 561 HOH B O      1 
HETATM 6065 O O      . HOH H 4 .   ? 37.471 2.595   46.493  1.00 24.84 ? 562 HOH B O      1 
HETATM 6066 O O      . HOH H 4 .   ? 38.642 14.677  55.831  1.00 41.86 ? 563 HOH B O      1 
HETATM 6067 O O      . HOH H 4 .   ? 13.173 -14.736 53.553  1.00 25.88 ? 564 HOH B O      1 
HETATM 6068 O O      . HOH H 4 .   ? 35.596 -16.083 27.747  1.00 49.24 ? 565 HOH B O      1 
HETATM 6069 O O      . HOH H 4 .   ? 18.673 -12.451 29.880  1.00 34.86 ? 566 HOH B O      1 
HETATM 6070 O O      . HOH H 4 .   ? 17.338 8.331   29.771  1.00 37.34 ? 567 HOH B O      1 
HETATM 6071 O O      . HOH H 4 .   ? 1.299  -4.289  37.487  1.00 32.08 ? 568 HOH B O      1 
HETATM 6072 O O      . HOH H 4 .   ? 17.763 -22.089 37.592  1.00 40.17 ? 569 HOH B O      1 
HETATM 6073 O O      . HOH H 4 .   ? 13.184 -5.107  37.953  1.00 27.01 ? 570 HOH B O      1 
HETATM 6074 O O      . HOH H 4 .   ? 27.074 -16.530 28.903  1.00 35.73 ? 571 HOH B O      1 
HETATM 6075 O O      . HOH H 4 .   ? 0.484  -15.702 55.169  1.00 44.32 ? 572 HOH B O      1 
HETATM 6076 O O      . HOH H 4 .   ? 18.517 -8.715  31.332  1.00 21.43 ? 573 HOH B O      1 
HETATM 6077 O O      . HOH H 4 .   ? 12.368 -13.263 65.851  1.00 30.16 ? 574 HOH B O      1 
HETATM 6078 O O      . HOH H 4 .   ? 44.366 -1.563  37.487  1.00 37.33 ? 575 HOH B O      1 
HETATM 6079 O O      . HOH H 4 .   ? 14.407 -29.387 37.681  1.00 53.97 ? 576 HOH B O      1 
HETATM 6080 O O      . HOH H 4 .   ? 5.974  -8.312  60.821  1.00 33.53 ? 577 HOH B O      1 
HETATM 6081 O O      . HOH H 4 .   ? 1.260  -19.726 40.844  1.00 38.53 ? 578 HOH B O      1 
HETATM 6082 O O      . HOH H 4 .   ? 22.787 -4.784  37.871  1.00 21.02 ? 579 HOH B O      1 
HETATM 6083 O O      . HOH H 4 .   ? 34.140 -17.323 26.679  1.00 45.41 ? 580 HOH B O      1 
HETATM 6084 O O      . HOH H 4 .   ? 10.726 -8.590  66.864  1.00 31.19 ? 581 HOH B O      1 
HETATM 6085 O O      . HOH H 4 .   ? 8.007  1.263   22.440  1.00 41.76 ? 582 HOH B O      1 
HETATM 6086 O O      . HOH H 4 .   ? 13.907 -2.745  34.347  1.00 24.18 ? 583 HOH B O      1 
HETATM 6087 O O      . HOH H 4 .   ? 42.692 -6.864  47.174  1.00 39.06 ? 584 HOH B O      1 
HETATM 6088 O O      . HOH H 4 .   ? 28.388 -0.759  42.416  1.00 22.73 ? 585 HOH B O      1 
HETATM 6089 O O      . HOH H 4 .   ? 26.749 -14.508 66.057  1.00 27.78 ? 586 HOH B O      1 
HETATM 6090 O O      . HOH H 4 .   ? 17.809 1.273   69.729  1.00 37.67 ? 587 HOH B O      1 
HETATM 6091 O O      . HOH H 4 .   ? 38.221 -15.633 44.859  1.00 35.74 ? 588 HOH B O      1 
HETATM 6092 O O      . HOH H 4 .   ? 18.835 -3.384  69.174  1.00 26.93 ? 589 HOH B O      1 
HETATM 6093 O O      . HOH H 4 .   ? 33.180 16.852  50.062  1.00 34.98 ? 590 HOH B O      1 
HETATM 6094 O O      . HOH H 4 .   ? 26.905 -2.179  34.071  1.00 21.99 ? 591 HOH B O      1 
HETATM 6095 O O      . HOH H 4 .   ? 39.371 -14.509 31.754  1.00 35.48 ? 592 HOH B O      1 
HETATM 6096 O O      . HOH H 4 .   ? 10.586 -17.185 35.557  1.00 39.18 ? 593 HOH B O      1 
HETATM 6097 O O      . HOH H 4 .   ? 7.029  -24.314 41.722  1.00 30.39 ? 594 HOH B O      1 
HETATM 6098 O O      . HOH H 4 .   ? 4.033  -13.170 32.289  1.00 40.17 ? 595 HOH B O      1 
HETATM 6099 O O      . HOH H 4 .   ? 24.730 16.282  55.583  1.00 44.37 ? 596 HOH B O      1 
HETATM 6100 O O      . HOH H 4 .   ? 39.996 5.897   42.527  1.00 38.56 ? 597 HOH B O      1 
HETATM 6101 O O      . HOH H 4 .   ? 13.609 -18.583 60.507  1.00 39.52 ? 598 HOH B O      1 
HETATM 6102 O O      . HOH H 4 .   ? 45.539 -8.194  39.141  1.00 33.32 ? 599 HOH B O      1 
HETATM 6103 O O      . HOH H 4 .   ? 2.494  -6.486  62.786  1.00 40.18 ? 600 HOH B O      1 
HETATM 6104 O O      . HOH H 4 .   ? 28.972 12.069  32.851  1.00 35.03 ? 601 HOH B O      1 
HETATM 6105 O O      . HOH H 4 .   ? 25.316 11.796  31.563  1.00 43.51 ? 602 HOH B O      1 
HETATM 6106 O O      . HOH H 4 .   ? 44.263 3.875   56.831  1.00 43.66 ? 603 HOH B O      1 
HETATM 6107 O O      . HOH H 4 .   ? 18.731 1.886   48.750  1.00 29.37 ? 604 HOH B O      1 
HETATM 6108 O O      . HOH H 4 .   ? 15.556 -13.172 33.813  1.00 27.26 ? 605 HOH B O      1 
HETATM 6109 O O      . HOH H 4 .   ? 32.649 -25.515 48.706  1.00 42.28 ? 606 HOH B O      1 
HETATM 6110 O O      . HOH H 4 .   ? 15.441 -0.097  56.002  1.00 27.68 ? 607 HOH B O      1 
HETATM 6111 O O      . HOH H 4 .   ? 19.126 -26.062 47.902  1.00 34.68 ? 608 HOH B O      1 
HETATM 6112 O O      . HOH H 4 .   ? 14.801 -6.312  53.045  1.00 23.47 ? 609 HOH B O      1 
HETATM 6113 O O      . HOH H 4 .   ? 24.426 6.429   51.317  1.00 24.81 ? 610 HOH B O      1 
HETATM 6114 O O      . HOH H 4 .   ? 3.355  -7.237  31.475  1.00 31.93 ? 611 HOH B O      1 
HETATM 6115 O O      . HOH H 4 .   ? 33.750 21.268  50.011  1.00 45.74 ? 612 HOH B O      1 
HETATM 6116 O O      . HOH H 4 .   ? 14.992 -14.510 69.730  1.00 35.16 ? 613 HOH B O      1 
HETATM 6117 O O      . HOH H 4 .   ? 0.677  -11.633 54.622  1.00 43.07 ? 614 HOH B O      1 
HETATM 6118 O O      . HOH H 4 .   ? 28.451 -22.098 31.360  1.00 41.03 ? 615 HOH B O      1 
HETATM 6119 O O      . HOH H 4 .   ? 7.248  -19.342 34.860  1.00 39.10 ? 616 HOH B O      1 
HETATM 6120 O O      . HOH H 4 .   ? 15.794 -9.958  27.916  1.00 25.74 ? 617 HOH B O      1 
HETATM 6121 O O      . HOH H 4 .   ? 4.015  -15.382 30.396  1.00 43.22 ? 618 HOH B O      1 
HETATM 6122 O O      . HOH H 4 .   ? 33.373 -8.795  27.641  1.00 41.53 ? 619 HOH B O      1 
HETATM 6123 O O      . HOH H 4 .   ? 1.612  -21.546 41.879  1.00 43.37 ? 620 HOH B O      1 
HETATM 6124 O O      . HOH H 4 .   ? 10.959 -27.071 39.220  1.00 37.14 ? 621 HOH B O      1 
HETATM 6125 O O      . HOH H 4 .   ? 36.441 10.427  33.638  1.00 32.81 ? 622 HOH B O      1 
HETATM 6126 O O      . HOH H 4 .   ? 43.044 -2.419  57.919  1.00 37.69 ? 623 HOH B O      1 
HETATM 6127 O O      . HOH H 4 .   ? 25.660 9.000   47.521  1.00 25.07 ? 624 HOH B O      1 
HETATM 6128 O O      . HOH H 4 .   ? 36.245 0.826   51.948  1.00 25.60 ? 625 HOH B O      1 
HETATM 6129 O O      . HOH H 4 .   ? 17.372 -9.716  66.972  1.00 26.04 ? 626 HOH B O      1 
HETATM 6130 O O      . HOH H 4 .   ? 21.702 -25.508 47.721  1.00 39.44 ? 627 HOH B O      1 
HETATM 6131 O O      . HOH H 4 .   ? 22.510 -20.994 38.275  1.00 29.92 ? 628 HOH B O      1 
HETATM 6132 O O      . HOH H 4 .   ? 30.176 -9.304  60.432  1.00 27.10 ? 629 HOH B O      1 
HETATM 6133 O O      . HOH H 4 .   ? 33.575 8.416   35.748  1.00 24.59 ? 630 HOH B O      1 
HETATM 6134 O O      . HOH H 4 .   ? 35.460 -8.233  31.013  1.00 29.23 ? 631 HOH B O      1 
HETATM 6135 O O      . HOH H 4 .   ? 30.667 6.974   23.885  1.00 25.55 ? 632 HOH B O      1 
HETATM 6136 O O      . HOH H 4 .   ? 11.596 -14.046 38.259  1.00 23.05 ? 633 HOH B O      1 
HETATM 6137 O O      . HOH H 4 .   ? 10.694 -17.449 53.760  1.00 25.19 ? 634 HOH B O      1 
HETATM 6138 O O      . HOH H 4 .   ? 29.212 20.307  44.867  1.00 29.28 ? 635 HOH B O      1 
HETATM 6139 O O      . HOH H 4 .   ? 29.003 6.559   36.426  1.00 23.26 ? 636 HOH B O      1 
HETATM 6140 O O      . HOH H 4 .   ? 32.027 19.676  40.681  1.00 28.46 ? 637 HOH B O      1 
HETATM 6141 O O      . HOH H 4 .   ? 20.058 -0.249  24.473  1.00 26.89 ? 638 HOH B O      1 
HETATM 6142 O O      . HOH H 4 .   ? 7.945  -6.578  44.888  1.00 22.57 ? 639 HOH B O      1 
HETATM 6143 O O      . HOH H 4 .   ? 4.649  4.693   42.719  1.00 53.96 ? 640 HOH B O      1 
HETATM 6144 O O      . HOH H 4 .   ? 15.489 -24.868 50.555  1.00 38.53 ? 641 HOH B O      1 
HETATM 6145 O O      . HOH H 4 .   ? 13.235 -10.815 24.972  1.00 33.85 ? 642 HOH B O      1 
HETATM 6146 O O      . HOH H 4 .   ? 36.982 -5.642  63.012  1.00 42.73 ? 643 HOH B O      1 
HETATM 6147 O O      . HOH H 4 .   ? -0.935 -15.436 45.789  1.00 36.34 ? 644 HOH B O      1 
HETATM 6148 O O      . HOH H 4 .   ? 19.116 -9.943  38.295  1.00 21.94 ? 645 HOH B O      1 
HETATM 6149 O O      . HOH H 4 .   ? 22.233 -14.359 29.784  1.00 48.77 ? 646 HOH B O      1 
HETATM 6150 O O      . HOH H 4 .   ? 17.700 3.996   49.734  1.00 39.60 ? 647 HOH B O      1 
HETATM 6151 O O      . HOH H 4 .   ? 37.160 6.661   44.806  1.00 26.84 ? 648 HOH B O      1 
HETATM 6152 O O      . HOH H 4 .   ? 9.439  -25.269 38.058  1.00 46.39 ? 649 HOH B O      1 
HETATM 6153 O O      . HOH H 4 .   ? 8.367  -2.009  55.080  1.00 32.32 ? 650 HOH B O      1 
HETATM 6154 O O      . HOH H 4 .   ? 16.993 1.667   25.134  1.00 36.12 ? 651 HOH B O      1 
HETATM 6155 O O      . HOH H 4 .   ? 42.350 -7.716  33.308  1.00 39.35 ? 652 HOH B O      1 
HETATM 6156 O O      . HOH H 4 .   ? 30.178 15.140  60.720  1.00 40.67 ? 653 HOH B O      1 
HETATM 6157 O O      . HOH H 4 .   ? 4.923  -22.760 40.542  1.00 36.67 ? 654 HOH B O      1 
HETATM 6158 O O      . HOH H 4 .   ? 38.328 0.135   46.068  1.00 29.92 ? 655 HOH B O      1 
HETATM 6159 O O      . HOH H 4 .   ? 18.724 5.624   45.379  1.00 31.53 ? 656 HOH B O      1 
HETATM 6160 O O      . HOH H 4 .   ? 17.536 12.688  40.608  1.00 50.75 ? 657 HOH B O      1 
HETATM 6161 O O      . HOH H 4 .   ? 18.714 5.849   32.704  1.00 25.35 ? 658 HOH B O      1 
HETATM 6162 O O      . HOH H 4 .   ? 16.727 -10.918 30.610  1.00 29.17 ? 659 HOH B O      1 
HETATM 6163 O O      . HOH H 4 .   ? 21.251 -22.263 58.865  1.00 39.68 ? 660 HOH B O      1 
HETATM 6164 O O      . HOH H 4 .   ? 17.906 -14.971 30.540  1.00 35.24 ? 661 HOH B O      1 
HETATM 6165 O O      . HOH H 4 .   ? 15.703 -22.269 39.996  1.00 45.11 ? 662 HOH B O      1 
HETATM 6166 O O      . HOH H 4 .   ? 30.397 -4.835  65.683  1.00 34.63 ? 663 HOH B O      1 
HETATM 6167 O O      . HOH H 4 .   ? 34.722 -21.755 43.482  1.00 38.92 ? 664 HOH B O      1 
HETATM 6168 O O      . HOH H 4 .   ? 17.715 2.403   29.601  1.00 27.54 ? 665 HOH B O      1 
HETATM 6169 O O      . HOH H 4 .   ? 11.086 -12.837 26.105  1.00 34.42 ? 666 HOH B O      1 
HETATM 6170 O O      . HOH H 4 .   ? 26.751 -4.354  64.172  1.00 23.74 ? 667 HOH B O      1 
HETATM 6171 O O      . HOH H 4 .   ? 0.878  -10.304 31.524  1.00 42.31 ? 668 HOH B O      1 
HETATM 6172 O O      . HOH H 4 .   ? 15.662 7.024   37.405  1.00 48.99 ? 669 HOH B O      1 
HETATM 6173 O O      . HOH H 4 .   ? 1.120  -21.185 50.398  1.00 39.32 ? 670 HOH B O      1 
HETATM 6174 O O      . HOH H 4 .   ? 40.235 -13.047 48.421  1.00 39.57 ? 671 HOH B O      1 
HETATM 6175 O O      . HOH H 4 .   ? 24.881 9.801   60.525  1.00 37.45 ? 672 HOH B O      1 
HETATM 6176 O O      . HOH H 4 .   ? 36.018 -19.461 49.508  1.00 37.75 ? 673 HOH B O      1 
HETATM 6177 O O      . HOH H 4 .   ? 15.195 -8.896  47.746  1.00 19.53 ? 674 HOH B O      1 
HETATM 6178 O O      . HOH H 4 .   ? 28.190 -1.033  27.512  1.00 23.00 ? 675 HOH B O      1 
HETATM 6179 O O      . HOH H 4 .   ? 4.856  -8.305  39.458  1.00 24.34 ? 676 HOH B O      1 
HETATM 6180 O O      . HOH H 4 .   ? 32.146 -20.406 57.404  1.00 36.80 ? 677 HOH B O      1 
HETATM 6181 O O      . HOH H 4 .   ? 16.889 3.833   59.362  1.00 32.81 ? 678 HOH B O      1 
HETATM 6182 O O      . HOH H 4 .   ? 32.512 -22.639 40.013  1.00 50.31 ? 679 HOH B O      1 
HETATM 6183 O O      . HOH H 4 .   ? 16.473 -20.446 35.826  1.00 35.58 ? 680 HOH B O      1 
HETATM 6184 O O      . HOH H 4 .   ? 41.865 12.940  62.541  1.00 59.57 ? 681 HOH B O      1 
HETATM 6185 O O      . HOH H 4 .   ? 16.307 -10.841 46.094  1.00 23.87 ? 682 HOH B O      1 
HETATM 6186 O O      . HOH H 4 .   ? 36.231 -18.267 53.334  1.00 41.50 ? 683 HOH B O      1 
HETATM 6187 O O      . HOH H 4 .   ? 16.792 7.008   34.884  1.00 34.24 ? 684 HOH B O      1 
HETATM 6188 O O      . HOH H 4 .   ? 0.107  -11.257 34.065  1.00 34.68 ? 685 HOH B O      1 
HETATM 6189 O O      . HOH H 4 .   ? 19.211 -7.840  28.799  1.00 23.60 ? 686 HOH B O      1 
HETATM 6190 O O      . HOH H 4 .   ? 2.154  -20.728 57.832  1.00 38.52 ? 687 HOH B O      1 
HETATM 6191 O O      . HOH H 4 .   ? 8.880  -0.601  62.740  1.00 40.66 ? 688 HOH B O      1 
HETATM 6192 O O      . HOH H 4 .   ? 8.153  -21.958 62.290  1.00 49.23 ? 689 HOH B O      1 
HETATM 6193 O O      . HOH H 4 .   ? 13.759 -17.064 25.197  1.00 40.73 ? 690 HOH B O      1 
HETATM 6194 O O      . HOH H 4 .   ? 24.669 20.492  34.155  1.00 48.29 ? 691 HOH B O      1 
HETATM 6195 O O      . HOH H 4 .   ? 14.876 5.002   24.629  1.00 35.88 ? 692 HOH B O      1 
HETATM 6196 O O      . HOH H 4 .   ? 28.603 -14.105 23.476  1.00 49.11 ? 693 HOH B O      1 
HETATM 6197 O O      . HOH H 4 .   ? 34.576 8.709   68.038  1.00 49.69 ? 694 HOH B O      1 
HETATM 6198 O O      . HOH H 4 .   ? 33.573 -5.451  25.974  1.00 37.07 ? 695 HOH B O      1 
HETATM 6199 O O      . HOH H 4 .   ? -0.528 -7.104  35.910  1.00 39.84 ? 696 HOH B O      1 
HETATM 6200 O O      . HOH H 4 .   ? 32.043 11.393  26.843  1.00 35.14 ? 697 HOH B O      1 
HETATM 6201 O O      . HOH H 4 .   ? 31.422 6.713   69.953  1.00 47.98 ? 698 HOH B O      1 
HETATM 6202 O O      . HOH H 4 .   ? 12.768 -1.047  36.172  1.00 23.24 ? 699 HOH B O      1 
HETATM 6203 O O      . HOH H 4 .   ? 10.192 3.568   51.290  1.00 41.53 ? 700 HOH B O      1 
HETATM 6204 O O      . HOH H 4 .   ? 15.165 -10.987 67.811  1.00 31.08 ? 701 HOH B O      1 
HETATM 6205 O O      . HOH H 4 .   ? 2.248  -6.824  47.051  1.00 43.73 ? 702 HOH B O      1 
HETATM 6206 O O      . HOH H 4 .   ? 18.474 -2.314  25.113  1.00 24.18 ? 703 HOH B O      1 
HETATM 6207 O O      . HOH H 4 .   ? 39.972 -9.299  26.466  1.00 55.50 ? 704 HOH B O      1 
HETATM 6208 O O      . HOH H 4 .   ? 1.515  -17.512 47.849  1.00 31.80 ? 705 HOH B O      1 
HETATM 6209 O O      . HOH H 4 .   ? 17.890 -7.696  37.143  1.00 21.16 ? 706 HOH B O      1 
HETATM 6210 O O      . HOH H 4 .   ? 34.632 19.735  42.254  1.00 42.19 ? 707 HOH B O      1 
HETATM 6211 O O      . HOH H 4 .   ? 6.442  -8.704  63.440  1.00 31.74 ? 708 HOH B O      1 
HETATM 6212 O O      . HOH H 4 .   ? 42.837 -10.640 33.316  1.00 42.56 ? 709 HOH B O      1 
HETATM 6213 O O      . HOH H 4 .   ? 39.758 6.944   33.791  1.00 42.48 ? 710 HOH B O      1 
HETATM 6214 O O      . HOH H 4 .   ? 25.311 -13.691 29.126  1.00 34.81 ? 711 HOH B O      1 
HETATM 6215 O O      . HOH H 4 .   ? 20.169 -15.472 67.505  1.00 34.44 ? 712 HOH B O      1 
HETATM 6216 O O      . HOH H 4 .   ? 3.087  -19.270 60.366  1.00 37.71 ? 713 HOH B O      1 
HETATM 6217 O O      . HOH H 4 .   ? 35.461 17.185  38.940  1.00 34.65 ? 714 HOH B O      1 
HETATM 6218 O O      . HOH H 4 .   ? 3.926  -11.813 61.211  1.00 37.71 ? 715 HOH B O      1 
HETATM 6219 O O      . HOH H 4 .   ? 29.468 -20.118 28.848  1.00 39.03 ? 716 HOH B O      1 
HETATM 6220 O O      . HOH H 4 .   ? 32.908 -2.327  26.848  1.00 28.02 ? 717 HOH B O      1 
HETATM 6221 O O      . HOH H 4 .   ? 5.249  -14.208 26.588  1.00 51.74 ? 718 HOH B O      1 
HETATM 6222 O O      . HOH H 4 .   ? 23.633 10.437  49.230  1.00 29.92 ? 719 HOH B O      1 
HETATM 6223 O O      . HOH H 4 .   ? 24.793 -5.098  71.732  1.00 28.76 ? 720 HOH B O      1 
HETATM 6224 O O      . HOH H 4 .   ? 8.198  -16.829 64.403  1.00 27.28 ? 721 HOH B O      1 
HETATM 6225 O O      . HOH H 4 .   ? 4.200  -3.877  29.469  1.00 32.81 ? 722 HOH B O      1 
HETATM 6226 O O      . HOH H 4 .   ? 20.583 -12.622 68.447  1.00 42.12 ? 723 HOH B O      1 
HETATM 6227 O O      . HOH H 4 .   ? 24.095 -25.711 54.267  1.00 52.94 ? 724 HOH B O      1 
HETATM 6228 O O      . HOH H 4 .   ? 19.946 14.014  37.738  1.00 38.90 ? 725 HOH B O      1 
HETATM 6229 O O      . HOH H 4 .   ? 10.961 -20.725 30.206  1.00 52.67 ? 726 HOH B O      1 
HETATM 6230 O O      . HOH H 4 .   ? 36.122 7.214   29.643  1.00 36.74 ? 727 HOH B O      1 
HETATM 6231 O O      . HOH H 4 .   ? 26.110 -25.260 50.331  1.00 43.90 ? 728 HOH B O      1 
HETATM 6232 O O      . HOH H 4 .   ? 5.342  -13.876 63.802  1.00 27.36 ? 729 HOH B O      1 
HETATM 6233 O O      . HOH H 4 .   ? 12.249 -16.791 67.547  1.00 35.55 ? 730 HOH B O      1 
HETATM 6234 O O      . HOH H 4 .   ? 38.984 13.648  34.622  1.00 29.80 ? 731 HOH B O      1 
HETATM 6235 O O      . HOH H 4 .   ? 15.811 1.603   71.663  1.00 38.51 ? 732 HOH B O      1 
HETATM 6236 O O      . HOH H 4 .   ? 19.486 -19.100 61.582  1.00 39.11 ? 733 HOH B O      1 
HETATM 6237 O O      . HOH H 4 .   ? 30.083 19.305  47.362  1.00 34.72 ? 734 HOH B O      1 
HETATM 6238 O O      . HOH H 4 .   ? 39.163 8.236   45.399  1.00 27.05 ? 735 HOH B O      1 
HETATM 6239 O O      . HOH H 4 .   ? 6.775  4.623   28.703  1.00 36.92 ? 736 HOH B O      1 
HETATM 6240 O O      . HOH H 4 .   ? 39.073 -3.293  62.873  1.00 33.08 ? 737 HOH B O      1 
HETATM 6241 O O      . HOH H 4 .   ? 23.149 15.452  41.286  1.00 34.02 ? 738 HOH B O      1 
HETATM 6242 O O      . HOH H 4 .   ? 20.879 3.571   26.046  1.00 27.56 ? 739 HOH B O      1 
HETATM 6243 O O      . HOH H 4 .   ? 28.695 15.391  51.184  1.00 34.15 ? 740 HOH B O      1 
HETATM 6244 O O      . HOH H 4 .   ? 4.561  -27.540 51.984  1.00 44.33 ? 741 HOH B O      1 
HETATM 6245 O O      . HOH H 4 .   ? 16.776 10.758  47.810  1.00 52.64 ? 742 HOH B O      1 
HETATM 6246 O O      . HOH H 4 .   ? 6.477  -5.886  67.939  1.00 28.50 ? 743 HOH B O      1 
HETATM 6247 O O      . HOH H 4 .   ? 20.296 -24.071 52.647  1.00 37.27 ? 744 HOH B O      1 
HETATM 6248 O O      . HOH H 4 .   ? 19.097 -25.289 40.623  1.00 38.87 ? 745 HOH B O      1 
HETATM 6249 O O      . HOH H 4 .   ? 13.769 3.890   34.966  1.00 32.61 ? 746 HOH B O      1 
HETATM 6250 O O      . HOH H 4 .   ? 4.611  0.435   49.240  1.00 49.34 ? 747 HOH B O      1 
HETATM 6251 O O      . HOH H 4 .   ? 15.193 6.854   56.589  1.00 46.67 ? 748 HOH B O      1 
HETATM 6252 O O      . HOH H 4 .   ? 44.409 4.426   45.866  1.00 39.76 ? 749 HOH B O      1 
HETATM 6253 O O      . HOH H 4 .   ? 42.293 11.970  59.008  1.00 51.63 ? 750 HOH B O      1 
HETATM 6254 O O      . HOH H 4 .   ? 34.208 -11.984 59.018  1.00 32.22 ? 751 HOH B O      1 
HETATM 6255 O O      . HOH H 4 .   ? 34.920 -22.218 48.010  1.00 41.53 ? 752 HOH B O      1 
HETATM 6256 O O      . HOH H 4 .   ? 24.806 -22.204 33.014  1.00 49.89 ? 753 HOH B O      1 
HETATM 6257 O O      . HOH H 4 .   ? 7.779  3.199   38.701  1.00 38.62 ? 754 HOH B O      1 
HETATM 6258 O O      . HOH H 4 .   ? 13.240 -19.761 63.975  1.00 47.41 ? 755 HOH B O      1 
HETATM 6259 O O      . HOH H 4 .   ? 19.343 -1.204  70.588  1.00 28.91 ? 756 HOH B O      1 
HETATM 6260 O O      . HOH H 4 .   ? 30.692 -16.784 65.294  1.00 43.97 ? 757 HOH B O      1 
HETATM 6261 O O      . HOH H 4 .   ? -0.849 0.196   45.260  1.00 44.75 ? 758 HOH B O      1 
HETATM 6262 O O      . HOH H 4 .   ? 28.764 -22.079 35.531  1.00 49.75 ? 759 HOH B O      1 
HETATM 6263 O O      . HOH H 4 .   ? 19.844 -10.255 67.940  1.00 31.10 ? 760 HOH B O      1 
HETATM 6264 O O      . HOH H 4 .   ? 10.561 -19.770 35.373  1.00 42.28 ? 761 HOH B O      1 
HETATM 6265 O O      . HOH H 4 .   ? 18.016 11.011  49.503  1.00 46.11 ? 762 HOH B O      1 
HETATM 6266 O O      . HOH H 4 .   ? 31.390 -22.494 56.507  1.00 52.35 ? 763 HOH B O      1 
HETATM 6267 O O      . HOH H 4 .   ? 28.167 -26.233 49.734  1.00 40.86 ? 764 HOH B O      1 
HETATM 6268 O O      . HOH H 4 .   ? 28.208 -9.266  24.625  1.00 49.03 ? 765 HOH B O      1 
HETATM 6269 O O      . HOH H 4 .   ? 8.820  -2.555  24.788  1.00 42.97 ? 766 HOH B O      1 
HETATM 6270 O O      . HOH H 4 .   ? 18.318 3.157   26.940  1.00 31.36 ? 767 HOH B O      1 
HETATM 6271 O O      . HOH H 4 .   ? 29.015 -23.699 40.228  1.00 43.90 ? 768 HOH B O      1 
HETATM 6272 O O      . HOH H 4 .   ? 38.874 -4.843  33.021  1.00 41.93 ? 769 HOH B O      1 
HETATM 6273 O O      . HOH H 4 .   ? -1.939 1.183   41.874  1.00 46.08 ? 770 HOH B O      1 
HETATM 6274 O O      . HOH H 4 .   ? 4.203  -7.368  64.752  1.00 39.24 ? 771 HOH B O      1 
HETATM 6275 O O      . HOH H 4 .   ? 1.992  -13.884 61.601  1.00 50.86 ? 772 HOH B O      1 
HETATM 6276 O O      . HOH H 4 .   ? 28.067 -14.427 71.085  1.00 45.97 ? 773 HOH B O      1 
HETATM 6277 O O      . HOH H 4 .   ? 11.358 1.322   40.503  1.00 40.28 ? 774 HOH B O      1 
HETATM 6278 O O      . HOH H 4 .   ? 17.066 -26.031 55.294  1.00 51.33 ? 775 HOH B O      1 
HETATM 6279 O O      . HOH H 4 .   ? 20.260 -9.726  27.231  1.00 34.87 ? 776 HOH B O      1 
HETATM 6280 O O      . HOH H 4 .   ? 30.153 -11.183 69.474  1.00 53.76 ? 777 HOH B O      1 
HETATM 6281 O O      . HOH H 4 .   ? 22.413 -16.689 68.058  1.00 36.27 ? 778 HOH B O      1 
HETATM 6282 O O      . HOH H 4 .   ? 12.646 -10.344 66.533  1.00 33.10 ? 779 HOH B O      1 
HETATM 6283 O O      . HOH H 4 .   ? 15.996 -14.598 28.368  1.00 48.16 ? 780 HOH B O      1 
HETATM 6284 O O      . HOH H 4 .   ? 12.618 -21.582 36.441  1.00 41.73 ? 781 HOH B O      1 
HETATM 6285 O O      . HOH H 4 .   ? 19.785 -22.747 56.882  1.00 42.06 ? 782 HOH B O      1 
HETATM 6286 O O      . HOH H 4 .   ? 42.539 14.186  40.064  1.00 47.63 ? 783 HOH B O      1 
HETATM 6287 O O      . HOH H 4 .   ? 37.513 -21.219 42.645  1.00 45.89 ? 784 HOH B O      1 
HETATM 6288 O O      . HOH H 4 .   ? 15.375 -20.562 59.564  1.00 42.27 ? 785 HOH B O      1 
HETATM 6289 O O      . HOH H 4 .   ? 27.669 -3.530  67.824  1.00 45.77 ? 786 HOH B O      1 
HETATM 6290 O O      . HOH H 4 .   ? 2.393  -1.450  49.586  1.00 53.94 ? 787 HOH B O      1 
HETATM 6291 O O      . HOH H 4 .   ? 3.528  -20.028 63.122  1.00 50.61 ? 788 HOH B O      1 
HETATM 6292 O O      . HOH H 4 .   ? 36.436 19.243  40.386  1.00 41.26 ? 789 HOH B O      1 
HETATM 6293 O O      . HOH H 4 .   ? 7.262  -19.361 65.009  1.00 34.42 ? 790 HOH B O      1 
HETATM 6294 O O      . HOH H 4 .   ? 17.117 6.512   47.927  1.00 44.72 ? 791 HOH B O      1 
HETATM 6295 O O      . HOH H 4 .   ? 31.093 -19.171 67.306  1.00 48.92 ? 792 HOH B O      1 
HETATM 6296 O O      . HOH H 4 .   ? 21.018 -21.344 61.693  1.00 44.15 ? 793 HOH B O      1 
HETATM 6297 O O      . HOH H 4 .   ? 19.417 9.681   27.686  1.00 51.76 ? 794 HOH B O      1 
HETATM 6298 O O      . HOH H 4 .   ? 45.175 -10.272 40.901  1.00 41.75 ? 795 HOH B O      1 
HETATM 6299 O O      . HOH H 4 .   ? 37.415 -6.198  30.832  1.00 44.01 ? 796 HOH B O      1 
HETATM 6300 O O      . HOH H 4 .   ? 22.579 -25.500 52.343  1.00 44.19 ? 797 HOH B O      1 
HETATM 6301 O O      . HOH H 4 .   ? 30.157 -15.347 69.050  1.00 46.02 ? 798 HOH B O      1 
HETATM 6302 O O      . HOH H 4 .   ? 12.878 -16.205 70.069  1.00 30.07 ? 799 HOH B O      1 
HETATM 6303 O O      . HOH H 4 .   ? 34.446 -0.378  26.005  1.00 36.82 ? 800 HOH B O      1 
HETATM 6304 O O      . HOH H 4 .   ? 19.093 2.659   71.048  1.00 43.67 ? 801 HOH B O      1 
HETATM 6305 O O      . HOH H 4 .   ? 15.346 9.603   34.149  1.00 46.62 ? 802 HOH B O      1 
HETATM 6306 O O      . HOH H 4 .   ? 17.107 -20.342 61.782  1.00 42.88 ? 803 HOH B O      1 
HETATM 6307 O O      . HOH H 4 .   ? 34.685 1.507   27.009  1.00 29.92 ? 804 HOH B O      1 
HETATM 6308 O O      . HOH H 4 .   ? 46.445 -8.301  36.584  1.00 44.95 ? 805 HOH B O      1 
HETATM 6309 O O      . HOH H 4 .   ? 18.632 -17.060 68.182  1.00 48.05 ? 806 HOH B O      1 
HETATM 6310 O O      . HOH H 4 .   ? 19.597 -22.542 35.633  1.00 47.93 ? 807 HOH B O      1 
HETATM 6311 O O      . HOH H 4 .   ? 16.919 4.466   31.057  1.00 27.28 ? 808 HOH B O      1 
HETATM 6312 O O      . HOH H 4 .   ? -2.494 -12.499 34.008  1.00 47.24 ? 809 HOH B O      1 
HETATM 6313 O O      . HOH H 4 .   ? 1.085  -7.763  31.892  1.00 48.79 ? 810 HOH B O      1 
HETATM 6314 O O      . HOH H 4 .   ? 5.203  -2.202  27.485  1.00 39.45 ? 811 HOH B O      1 
HETATM 6315 O O      . HOH H 4 .   ? 29.461 -23.691 57.777  1.00 53.27 ? 812 HOH B O      1 
HETATM 6316 O O      . HOH H 4 .   ? 30.573 16.961  50.563  1.00 35.96 ? 813 HOH B O      1 
HETATM 6317 O O      . HOH H 4 .   ? 21.544 -21.541 35.738  1.00 43.95 ? 814 HOH B O      1 
HETATM 6318 O O      . HOH H 4 .   ? 13.517 1.556   36.664  1.00 31.11 ? 815 HOH B O      1 
HETATM 6319 O O      . HOH H 4 .   ? 35.059 -3.150  65.893  1.00 54.72 ? 816 HOH B O      1 
HETATM 6320 O O      . HOH H 4 .   ? 16.630 9.389   57.742  1.00 54.86 ? 817 HOH B O      1 
HETATM 6321 O O      . HOH H 4 .   ? 23.239 -26.214 49.899  1.00 43.38 ? 818 HOH B O      1 
HETATM 6322 O O      . HOH H 4 .   ? 19.258 21.252  38.005  1.00 40.64 ? 819 HOH B O      1 
HETATM 6323 O O      . HOH H 4 .   ? 16.168 6.135   29.030  1.00 32.96 ? 820 HOH B O      1 
HETATM 6324 O O      . HOH H 4 .   ? 15.305 5.156   33.244  1.00 31.78 ? 821 HOH B O      1 
HETATM 6325 O O      . HOH H 4 .   ? 2.806  -14.858 63.808  1.00 38.32 ? 822 HOH B O      1 
HETATM 6326 O O      . HOH H 4 .   ? 15.411 2.185   57.777  1.00 38.98 ? 823 HOH B O      1 
HETATM 6327 O O      . HOH H 4 .   ? 41.721 -13.542 32.402  1.00 40.14 ? 824 HOH B O      1 
HETATM 6328 O O      . HOH H 4 .   ? 42.344 9.725   42.375  1.00 46.12 ? 825 HOH B O      1 
HETATM 6329 O O      . HOH H 4 .   ? 45.816 -3.617  35.850  1.00 42.24 ? 826 HOH B O      1 
HETATM 6330 O O      . HOH H 4 .   ? 15.253 9.821   31.162  1.00 54.57 ? 827 HOH B O      1 
HETATM 6331 O O      . HOH H 4 .   ? 17.385 -15.694 70.506  1.00 45.65 ? 828 HOH B O      1 
HETATM 6332 O O      . HOH H 4 .   ? 39.526 -17.203 32.755  1.00 40.84 ? 829 HOH B O      1 
HETATM 6333 O O      . HOH H 4 .   ? 16.877 -7.005  27.771  1.00 27.00 ? 830 HOH B O      1 
HETATM 6334 O O      . HOH H 4 .   ? 11.262 -20.723 32.893  1.00 52.75 ? 831 HOH B O      1 
HETATM 6335 O O      . HOH H 4 .   ? 31.904 9.294   24.750  1.00 31.84 ? 832 HOH B O      1 
HETATM 6336 O O      . HOH H 4 .   ? 46.000 1.611   56.708  1.00 57.44 ? 833 HOH B O      1 
HETATM 6337 O O      . HOH H 4 .   ? 10.689 -30.819 38.663  1.00 38.37 ? 834 HOH B O      1 
HETATM 6338 O O      . HOH H 4 .   ? 44.439 12.599  60.743  1.00 63.76 ? 835 HOH B O      1 
HETATM 6339 O O      . HOH H 4 .   ? 19.482 -24.640 55.242  1.00 43.89 ? 836 HOH B O      1 
HETATM 6340 O O      . HOH H 4 .   ? 27.030 -3.348  71.767  1.00 46.01 ? 837 HOH B O      1 
HETATM 6341 O O      . HOH H 4 .   ? 22.006 -21.837 33.142  1.00 49.17 ? 838 HOH B O      1 
HETATM 6342 O O      . HOH H 4 .   ? 24.400 16.919  58.170  1.00 50.53 ? 839 HOH B O      1 
HETATM 6343 O O      . HOH H 4 .   ? 4.826  -11.187 63.890  1.00 30.78 ? 840 HOH B O      1 
HETATM 6344 O O      . HOH H 4 .   ? 41.463 7.943   43.680  1.00 35.24 ? 841 HOH B O      1 
HETATM 6345 O O      . HOH H 4 .   ? 14.875 8.479   74.105  1.00 50.80 ? 842 HOH B O      1 
HETATM 6346 O O      . HOH H 4 .   ? 43.512 6.709   44.780  1.00 42.61 ? 843 HOH B O      1 
HETATM 6347 O O      . HOH H 4 .   ? -2.043 -12.567 54.615  1.00 50.73 ? 844 HOH B O      1 
HETATM 6348 O O      . HOH H 4 .   ? 13.910 -18.251 70.855  1.00 35.76 ? 845 HOH B O      1 
HETATM 6349 O O      . HOH H 4 .   ? 16.861 5.553   26.423  1.00 35.40 ? 846 HOH B O      1 
HETATM 6350 O O      . HOH H 4 .   ? 2.569  -16.824 64.658  1.00 48.45 ? 847 HOH B O      1 
HETATM 6351 O O      . HOH H 4 .   ? 20.573 -16.669 29.924  1.00 46.97 ? 848 HOH B O      1 
HETATM 6352 O O      . HOH H 4 .   ? 35.684 -22.544 45.681  1.00 41.14 ? 849 HOH B O      1 
HETATM 6353 O O      . HOH H 4 .   ? 24.779 -20.966 28.777  1.00 54.59 ? 850 HOH B O      1 
HETATM 6354 O O      . HOH H 4 .   ? 31.254 -16.766 69.627  1.00 54.90 ? 851 HOH B O      1 
HETATM 6355 O O      . HOH H 4 .   ? 21.528 -20.940 30.705  1.00 55.67 ? 852 HOH B O      1 
HETATM 6356 O O      . HOH H 4 .   ? 34.685 2.352   24.607  1.00 40.51 ? 853 HOH B O      1 
HETATM 6357 O O      . HOH H 4 .   ? 9.166  -20.471 66.076  1.00 44.09 ? 854 HOH B O      1 
HETATM 6358 O O      . HOH H 4 .   ? 24.108 -22.609 30.185  1.00 55.27 ? 855 HOH B O      1 
HETATM 6359 O O      . HOH H 4 .   ? 0.961  -13.358 64.809  1.00 51.08 ? 856 HOH B O      1 
HETATM 6360 O O      . HOH H 4 .   ? 0.522  -17.191 66.319  1.00 52.70 ? 857 HOH B O      1 
# 
