data_8QNX
# 
_entry.id   8QNX 
# 
_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   8QNX         pdb_00008qnx 10.2210/pdb8qnx/pdb 
WWPDB D_1292133636 ?            ?                   
# 
_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                        8QNX 
_pdbx_database_status.recvd_initial_deposition_date   2023-09-27 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB . 8QNA unspecified 
PDB . 8QN1 unspecified 
PDB . 8QN9 unspecified 
PDB . 8QMX unspecified 
PDB . 8QN3 unspecified 
PDB . 8QNE unspecified 
PDB . 8QNK unspecified 
PDB . 8QNP unspecified 
PDB . 8QNM unspecified 
PDB . 8QNW 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'                     43609.312 1   ? ? ? ? 
2 non-polymer syn 'FLAVIN MONONUCLEOTIDE'                               456.344   1   ? ? ? ? 
3 non-polymer syn '1,4,5,6-Tetrahydronicotinamide adenine dinucleotide' 667.457   1   ? ? ? ? 
4 non-polymer syn 'SULFATE ION'                                         96.063    1   ? ? ? ? 
5 water       nat water                                                 18.015    466 ? ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MASHHHHHHMASSAQDGNNPLFSPYKMGKFNLSHRVVLAPMTRCRALNNIPQAALGEYYEQRATAGGFLITEGTMISPTS
AGFPHVPGIFTKEQVREWKKIVDVVHAKGAVIFCQLWHVGRASHEVYQPAGAAPISSTEKPISNRWRILMPDGTHGIYPK
PRAIGTYEISQVVEDYRRSALNAIEAGFDGIEIHGAHGYLIDQFLKDGINDRTDEYGGSLANRCKFITQVVQAVVSAIGA
DRVGVRVSPAIDHLDAMDSNPLSLGLAVVERLNKIQLHSGSKLAYLHVTQPGDGRGSEEEEARLMRTLRNAYQGTFICSG
GYTRELGIEAVAQGDADLVSYGRLFISNPDLVMRIKLNAPLNKYNRKTFYTQDPVVGYTDYPFLQGNGSNGPLSRL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MASHHHHHHMASSAQDGNNPLFSPYKMGKFNLSHRVVLAPMTRCRALNNIPQAALGEYYEQRATAGGFLITEGTMISPTS
AGFPHVPGIFTKEQVREWKKIVDVVHAKGAVIFCQLWHVGRASHEVYQPAGAAPISSTEKPISNRWRILMPDGTHGIYPK
PRAIGTYEISQVVEDYRRSALNAIEAGFDGIEIHGAHGYLIDQFLKDGINDRTDEYGGSLANRCKFITQVVQAVVSAIGA
DRVGVRVSPAIDHLDAMDSNPLSLGLAVVERLNKIQLHSGSKLAYLHVTQPGDGRGSEEEEARLMRTLRNAYQGTFICSG
GYTRELGIEAVAQGDADLVSYGRLFISNPDLVMRIKLNAPLNKYNRKTFYTQDPVVGYTDYPFLQGNGSNGPLSRL
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'FLAVIN MONONUCLEOTIDE'                               FMN 
3 '1,4,5,6-Tetrahydronicotinamide adenine dinucleotide' WI6 
4 'SULFATE ION'                                         SO4 
5 water                                                 HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ALA n 
1 3   SER n 
1 4   HIS n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   HIS n 
1 10  MET n 
1 11  ALA n 
1 12  SER n 
1 13  SER n 
1 14  ALA n 
1 15  GLN n 
1 16  ASP n 
1 17  GLY n 
1 18  ASN n 
1 19  ASN n 
1 20  PRO n 
1 21  LEU n 
1 22  PHE n 
1 23  SER n 
1 24  PRO n 
1 25  TYR n 
1 26  LYS n 
1 27  MET n 
1 28  GLY n 
1 29  LYS n 
1 30  PHE n 
1 31  ASN n 
1 32  LEU n 
1 33  SER n 
1 34  HIS n 
1 35  ARG n 
1 36  VAL n 
1 37  VAL n 
1 38  LEU n 
1 39  ALA n 
1 40  PRO n 
1 41  MET n 
1 42  THR n 
1 43  ARG n 
1 44  CYS n 
1 45  ARG n 
1 46  ALA n 
1 47  LEU n 
1 48  ASN n 
1 49  ASN n 
1 50  ILE n 
1 51  PRO n 
1 52  GLN n 
1 53  ALA n 
1 54  ALA n 
1 55  LEU n 
1 56  GLY n 
1 57  GLU n 
1 58  TYR n 
1 59  TYR n 
1 60  GLU n 
1 61  GLN n 
1 62  ARG n 
1 63  ALA n 
1 64  THR n 
1 65  ALA n 
1 66  GLY n 
1 67  GLY n 
1 68  PHE n 
1 69  LEU n 
1 70  ILE n 
1 71  THR n 
1 72  GLU n 
1 73  GLY n 
1 74  THR n 
1 75  MET n 
1 76  ILE n 
1 77  SER n 
1 78  PRO n 
1 79  THR n 
1 80  SER n 
1 81  ALA n 
1 82  GLY n 
1 83  PHE n 
1 84  PRO n 
1 85  HIS n 
1 86  VAL n 
1 87  PRO n 
1 88  GLY n 
1 89  ILE n 
1 90  PHE n 
1 91  THR n 
1 92  LYS n 
1 93  GLU n 
1 94  GLN n 
1 95  VAL n 
1 96  ARG n 
1 97  GLU n 
1 98  TRP n 
1 99  LYS n 
1 100 LYS n 
1 101 ILE n 
1 102 VAL n 
1 103 ASP n 
1 104 VAL n 
1 105 VAL n 
1 106 HIS n 
1 107 ALA n 
1 108 LYS n 
1 109 GLY n 
1 110 ALA n 
1 111 VAL n 
1 112 ILE n 
1 113 PHE n 
1 114 CYS n 
1 115 GLN n 
1 116 LEU n 
1 117 TRP n 
1 118 HIS n 
1 119 VAL n 
1 120 GLY n 
1 121 ARG n 
1 122 ALA n 
1 123 SER n 
1 124 HIS n 
1 125 GLU n 
1 126 VAL n 
1 127 TYR n 
1 128 GLN n 
1 129 PRO n 
1 130 ALA n 
1 131 GLY n 
1 132 ALA n 
1 133 ALA n 
1 134 PRO n 
1 135 ILE n 
1 136 SER n 
1 137 SER n 
1 138 THR n 
1 139 GLU n 
1 140 LYS n 
1 141 PRO n 
1 142 ILE n 
1 143 SER n 
1 144 ASN n 
1 145 ARG n 
1 146 TRP n 
1 147 ARG n 
1 148 ILE n 
1 149 LEU n 
1 150 MET n 
1 151 PRO n 
1 152 ASP n 
1 153 GLY n 
1 154 THR n 
1 155 HIS n 
1 156 GLY n 
1 157 ILE n 
1 158 TYR n 
1 159 PRO n 
1 160 LYS n 
1 161 PRO n 
1 162 ARG n 
1 163 ALA n 
1 164 ILE n 
1 165 GLY n 
1 166 THR n 
1 167 TYR n 
1 168 GLU n 
1 169 ILE n 
1 170 SER n 
1 171 GLN n 
1 172 VAL n 
1 173 VAL n 
1 174 GLU n 
1 175 ASP n 
1 176 TYR n 
1 177 ARG n 
1 178 ARG n 
1 179 SER n 
1 180 ALA n 
1 181 LEU n 
1 182 ASN n 
1 183 ALA n 
1 184 ILE n 
1 185 GLU n 
1 186 ALA n 
1 187 GLY n 
1 188 PHE n 
1 189 ASP n 
1 190 GLY n 
1 191 ILE n 
1 192 GLU n 
1 193 ILE n 
1 194 HIS n 
1 195 GLY n 
1 196 ALA n 
1 197 HIS n 
1 198 GLY n 
1 199 TYR n 
1 200 LEU n 
1 201 ILE n 
1 202 ASP n 
1 203 GLN n 
1 204 PHE n 
1 205 LEU n 
1 206 LYS n 
1 207 ASP n 
1 208 GLY n 
1 209 ILE n 
1 210 ASN n 
1 211 ASP n 
1 212 ARG n 
1 213 THR n 
1 214 ASP n 
1 215 GLU n 
1 216 TYR n 
1 217 GLY n 
1 218 GLY n 
1 219 SER n 
1 220 LEU n 
1 221 ALA n 
1 222 ASN n 
1 223 ARG n 
1 224 CYS n 
1 225 LYS n 
1 226 PHE n 
1 227 ILE n 
1 228 THR n 
1 229 GLN n 
1 230 VAL n 
1 231 VAL n 
1 232 GLN n 
1 233 ALA n 
1 234 VAL n 
1 235 VAL n 
1 236 SER n 
1 237 ALA n 
1 238 ILE n 
1 239 GLY n 
1 240 ALA n 
1 241 ASP n 
1 242 ARG n 
1 243 VAL n 
1 244 GLY n 
1 245 VAL n 
1 246 ARG n 
1 247 VAL n 
1 248 SER n 
1 249 PRO n 
1 250 ALA n 
1 251 ILE n 
1 252 ASP n 
1 253 HIS n 
1 254 LEU n 
1 255 ASP n 
1 256 ALA n 
1 257 MET n 
1 258 ASP n 
1 259 SER n 
1 260 ASN n 
1 261 PRO n 
1 262 LEU n 
1 263 SER n 
1 264 LEU n 
1 265 GLY n 
1 266 LEU n 
1 267 ALA n 
1 268 VAL n 
1 269 VAL n 
1 270 GLU n 
1 271 ARG n 
1 272 LEU n 
1 273 ASN n 
1 274 LYS n 
1 275 ILE n 
1 276 GLN n 
1 277 LEU n 
1 278 HIS n 
1 279 SER n 
1 280 GLY n 
1 281 SER n 
1 282 LYS n 
1 283 LEU n 
1 284 ALA n 
1 285 TYR n 
1 286 LEU n 
1 287 HIS n 
1 288 VAL n 
1 289 THR n 
1 290 GLN n 
1 291 PRO n 
1 292 GLY n 
1 293 ASP n 
1 294 GLY n 
1 295 ARG n 
1 296 GLY n 
1 297 SER n 
1 298 GLU n 
1 299 GLU n 
1 300 GLU n 
1 301 GLU n 
1 302 ALA n 
1 303 ARG n 
1 304 LEU n 
1 305 MET n 
1 306 ARG n 
1 307 THR n 
1 308 LEU n 
1 309 ARG n 
1 310 ASN n 
1 311 ALA n 
1 312 TYR n 
1 313 GLN n 
1 314 GLY n 
1 315 THR n 
1 316 PHE n 
1 317 ILE n 
1 318 CYS n 
1 319 SER n 
1 320 GLY n 
1 321 GLY n 
1 322 TYR n 
1 323 THR n 
1 324 ARG n 
1 325 GLU n 
1 326 LEU n 
1 327 GLY n 
1 328 ILE n 
1 329 GLU n 
1 330 ALA n 
1 331 VAL n 
1 332 ALA n 
1 333 GLN n 
1 334 GLY n 
1 335 ASP n 
1 336 ALA n 
1 337 ASP n 
1 338 LEU n 
1 339 VAL n 
1 340 SER n 
1 341 TYR n 
1 342 GLY n 
1 343 ARG n 
1 344 LEU n 
1 345 PHE n 
1 346 ILE n 
1 347 SER n 
1 348 ASN n 
1 349 PRO n 
1 350 ASP n 
1 351 LEU n 
1 352 VAL n 
1 353 MET n 
1 354 ARG n 
1 355 ILE n 
1 356 LYS n 
1 357 LEU n 
1 358 ASN n 
1 359 ALA n 
1 360 PRO n 
1 361 LEU n 
1 362 ASN n 
1 363 LYS n 
1 364 TYR n 
1 365 ASN n 
1 366 ARG n 
1 367 LYS n 
1 368 THR n 
1 369 PHE n 
1 370 TYR n 
1 371 THR n 
1 372 GLN n 
1 373 ASP n 
1 374 PRO n 
1 375 VAL n 
1 376 VAL n 
1 377 GLY n 
1 378 TYR n 
1 379 THR n 
1 380 ASP n 
1 381 TYR n 
1 382 PRO n 
1 383 PHE n 
1 384 LEU n 
1 385 GLN n 
1 386 GLY n 
1 387 ASN n 
1 388 GLY n 
1 389 SER n 
1 390 ASN n 
1 391 GLY n 
1 392 PRO n 
1 393 LEU n 
1 394 SER n 
1 395 ARG n 
1 396 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                   396 
_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 
SO4 non-polymer         . 'SULFATE ION'                                         ? 'O4 S -2'           96.063  
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   MET 1   -8  ?   ?   ?   A . n 
A 1 2   ALA 2   -7  ?   ?   ?   A . n 
A 1 3   SER 3   -6  ?   ?   ?   A . n 
A 1 4   HIS 4   -5  ?   ?   ?   A . n 
A 1 5   HIS 5   -4  ?   ?   ?   A . n 
A 1 6   HIS 6   -3  ?   ?   ?   A . n 
A 1 7   HIS 7   -2  ?   ?   ?   A . n 
A 1 8   HIS 8   -1  ?   ?   ?   A . n 
A 1 9   HIS 9   0   ?   ?   ?   A . n 
A 1 10  MET 10  1   ?   ?   ?   A . n 
A 1 11  ALA 11  2   ?   ?   ?   A . n 
A 1 12  SER 12  3   ?   ?   ?   A . n 
A 1 13  SER 13  4   ?   ?   ?   A . n 
A 1 14  ALA 14  5   ?   ?   ?   A . n 
A 1 15  GLN 15  6   ?   ?   ?   A . n 
A 1 16  ASP 16  7   ?   ?   ?   A . n 
A 1 17  GLY 17  8   ?   ?   ?   A . n 
A 1 18  ASN 18  9   ?   ?   ?   A . n 
A 1 19  ASN 19  10  10  ASN ASN A . n 
A 1 20  PRO 20  11  11  PRO PRO A . n 
A 1 21  LEU 21  12  12  LEU LEU A . n 
A 1 22  PHE 22  13  13  PHE PHE A . n 
A 1 23  SER 23  14  14  SER SER A . n 
A 1 24  PRO 24  15  15  PRO PRO A . n 
A 1 25  TYR 25  16  16  TYR TYR A . n 
A 1 26  LYS 26  17  17  LYS LYS A . n 
A 1 27  MET 27  18  18  MET MET A . n 
A 1 28  GLY 28  19  19  GLY GLY A . n 
A 1 29  LYS 29  20  20  LYS LYS A . n 
A 1 30  PHE 30  21  21  PHE PHE A . n 
A 1 31  ASN 31  22  22  ASN ASN A . n 
A 1 32  LEU 32  23  23  LEU LEU A . n 
A 1 33  SER 33  24  24  SER SER A . n 
A 1 34  HIS 34  25  25  HIS HIS A . n 
A 1 35  ARG 35  26  26  ARG ARG A . n 
A 1 36  VAL 36  27  27  VAL VAL A . n 
A 1 37  VAL 37  28  28  VAL VAL A . n 
A 1 38  LEU 38  29  29  LEU LEU A . n 
A 1 39  ALA 39  30  30  ALA ALA A . n 
A 1 40  PRO 40  31  31  PRO PRO A . n 
A 1 41  MET 41  32  32  MET MET A . n 
A 1 42  THR 42  33  33  THR THR A . n 
A 1 43  ARG 43  34  34  ARG ARG A . n 
A 1 44  CYS 44  35  35  CYS CYS A . n 
A 1 45  ARG 45  36  36  ARG ARG A . n 
A 1 46  ALA 46  37  37  ALA ALA A . n 
A 1 47  LEU 47  38  38  LEU LEU A . n 
A 1 48  ASN 48  39  39  ASN ASN A . n 
A 1 49  ASN 49  40  40  ASN ASN A . n 
A 1 50  ILE 50  41  41  ILE ILE A . n 
A 1 51  PRO 51  42  42  PRO PRO A . n 
A 1 52  GLN 52  43  43  GLN GLN A . n 
A 1 53  ALA 53  44  44  ALA ALA A . n 
A 1 54  ALA 54  45  45  ALA ALA A . n 
A 1 55  LEU 55  46  46  LEU LEU A . n 
A 1 56  GLY 56  47  47  GLY GLY A . n 
A 1 57  GLU 57  48  48  GLU GLU A . n 
A 1 58  TYR 58  49  49  TYR TYR A . n 
A 1 59  TYR 59  50  50  TYR TYR A . n 
A 1 60  GLU 60  51  51  GLU GLU A . n 
A 1 61  GLN 61  52  52  GLN GLN A . n 
A 1 62  ARG 62  53  53  ARG ARG A . n 
A 1 63  ALA 63  54  54  ALA ALA A . n 
A 1 64  THR 64  55  55  THR THR A . n 
A 1 65  ALA 65  56  56  ALA ALA A . n 
A 1 66  GLY 66  57  57  GLY GLY A . n 
A 1 67  GLY 67  58  58  GLY GLY A . n 
A 1 68  PHE 68  59  59  PHE PHE A . n 
A 1 69  LEU 69  60  60  LEU LEU A . n 
A 1 70  ILE 70  61  61  ILE ILE A . n 
A 1 71  THR 71  62  62  THR THR A . n 
A 1 72  GLU 72  63  63  GLU GLU A . n 
A 1 73  GLY 73  64  64  GLY GLY A . n 
A 1 74  THR 74  65  65  THR THR A . n 
A 1 75  MET 75  66  66  MET MET A . n 
A 1 76  ILE 76  67  67  ILE ILE A . n 
A 1 77  SER 77  68  68  SER SER A . n 
A 1 78  PRO 78  69  69  PRO PRO A . n 
A 1 79  THR 79  70  70  THR THR A . n 
A 1 80  SER 80  71  71  SER SER A . n 
A 1 81  ALA 81  72  72  ALA ALA A . n 
A 1 82  GLY 82  73  73  GLY GLY A . n 
A 1 83  PHE 83  74  74  PHE PHE A . n 
A 1 84  PRO 84  75  75  PRO PRO A . n 
A 1 85  HIS 85  76  76  HIS HIS A . n 
A 1 86  VAL 86  77  77  VAL VAL A . n 
A 1 87  PRO 87  78  78  PRO PRO A . n 
A 1 88  GLY 88  79  79  GLY GLY A . n 
A 1 89  ILE 89  80  80  ILE ILE A . n 
A 1 90  PHE 90  81  81  PHE PHE A . n 
A 1 91  THR 91  82  82  THR THR A . n 
A 1 92  LYS 92  83  83  LYS LYS A . n 
A 1 93  GLU 93  84  84  GLU GLU A . n 
A 1 94  GLN 94  85  85  GLN GLN A . n 
A 1 95  VAL 95  86  86  VAL VAL A . n 
A 1 96  ARG 96  87  87  ARG ARG A . n 
A 1 97  GLU 97  88  88  GLU GLU A . n 
A 1 98  TRP 98  89  89  TRP TRP A . n 
A 1 99  LYS 99  90  90  LYS LYS A . n 
A 1 100 LYS 100 91  91  LYS LYS A . n 
A 1 101 ILE 101 92  92  ILE ILE A . n 
A 1 102 VAL 102 93  93  VAL VAL A . n 
A 1 103 ASP 103 94  94  ASP ASP A . n 
A 1 104 VAL 104 95  95  VAL VAL A . n 
A 1 105 VAL 105 96  96  VAL VAL A . n 
A 1 106 HIS 106 97  97  HIS HIS A . n 
A 1 107 ALA 107 98  98  ALA ALA A . n 
A 1 108 LYS 108 99  99  LYS LYS A . n 
A 1 109 GLY 109 100 100 GLY GLY A . n 
A 1 110 ALA 110 101 101 ALA ALA A . n 
A 1 111 VAL 111 102 102 VAL VAL A . n 
A 1 112 ILE 112 103 103 ILE ILE A . n 
A 1 113 PHE 113 104 104 PHE PHE A . n 
A 1 114 CYS 114 105 105 CYS CYS A . n 
A 1 115 GLN 115 106 106 GLN GLN A . n 
A 1 116 LEU 116 107 107 LEU LEU A . n 
A 1 117 TRP 117 108 108 TRP TRP A . n 
A 1 118 HIS 118 109 109 HIS HIS A . n 
A 1 119 VAL 119 110 110 VAL VAL A . n 
A 1 120 GLY 120 111 111 GLY GLY A . n 
A 1 121 ARG 121 112 112 ARG ARG A . n 
A 1 122 ALA 122 113 113 ALA ALA A . n 
A 1 123 SER 123 114 114 SER SER A . n 
A 1 124 HIS 124 115 115 HIS HIS A . n 
A 1 125 GLU 125 116 116 GLU GLU A . n 
A 1 126 VAL 126 117 117 VAL VAL A . n 
A 1 127 TYR 127 118 118 TYR TYR A . n 
A 1 128 GLN 128 119 119 GLN GLN A . n 
A 1 129 PRO 129 120 120 PRO PRO A . n 
A 1 130 ALA 130 121 121 ALA ALA A . n 
A 1 131 GLY 131 122 122 GLY GLY A . n 
A 1 132 ALA 132 123 123 ALA ALA A . n 
A 1 133 ALA 133 124 124 ALA ALA A . n 
A 1 134 PRO 134 125 125 PRO PRO A . n 
A 1 135 ILE 135 126 126 ILE ILE A . n 
A 1 136 SER 136 127 127 SER SER A . n 
A 1 137 SER 137 128 128 SER SER A . n 
A 1 138 THR 138 129 129 THR THR A . n 
A 1 139 GLU 139 130 130 GLU GLU A . n 
A 1 140 LYS 140 131 131 LYS LYS A . n 
A 1 141 PRO 141 132 132 PRO PRO A . n 
A 1 142 ILE 142 133 133 ILE ILE A . n 
A 1 143 SER 143 134 134 SER SER A . n 
A 1 144 ASN 144 135 135 ASN ASN A . n 
A 1 145 ARG 145 136 136 ARG ARG A . n 
A 1 146 TRP 146 137 137 TRP TRP A . n 
A 1 147 ARG 147 138 138 ARG ARG A . n 
A 1 148 ILE 148 139 139 ILE ILE A . n 
A 1 149 LEU 149 140 140 LEU LEU A . n 
A 1 150 MET 150 141 141 MET MET A . n 
A 1 151 PRO 151 142 142 PRO PRO A . n 
A 1 152 ASP 152 143 143 ASP ASP A . n 
A 1 153 GLY 153 144 144 GLY GLY A . n 
A 1 154 THR 154 145 145 THR THR A . n 
A 1 155 HIS 155 146 146 HIS HIS A . n 
A 1 156 GLY 156 147 147 GLY GLY A . n 
A 1 157 ILE 157 148 148 ILE ILE A . n 
A 1 158 TYR 158 149 149 TYR TYR A . n 
A 1 159 PRO 159 150 150 PRO PRO A . n 
A 1 160 LYS 160 151 151 LYS LYS A . n 
A 1 161 PRO 161 152 152 PRO PRO A . n 
A 1 162 ARG 162 153 153 ARG ARG A . n 
A 1 163 ALA 163 154 154 ALA ALA A . n 
A 1 164 ILE 164 155 155 ILE ILE A . n 
A 1 165 GLY 165 156 156 GLY GLY A . n 
A 1 166 THR 166 157 157 THR THR A . n 
A 1 167 TYR 167 158 158 TYR TYR A . n 
A 1 168 GLU 168 159 159 GLU GLU A . n 
A 1 169 ILE 169 160 160 ILE ILE A . n 
A 1 170 SER 170 161 161 SER SER A . n 
A 1 171 GLN 171 162 162 GLN GLN A . n 
A 1 172 VAL 172 163 163 VAL VAL A . n 
A 1 173 VAL 173 164 164 VAL VAL A . n 
A 1 174 GLU 174 165 165 GLU GLU A . n 
A 1 175 ASP 175 166 166 ASP ASP A . n 
A 1 176 TYR 176 167 167 TYR TYR A . n 
A 1 177 ARG 177 168 168 ARG ARG A . n 
A 1 178 ARG 178 169 169 ARG ARG A . n 
A 1 179 SER 179 170 170 SER SER A . n 
A 1 180 ALA 180 171 171 ALA ALA A . n 
A 1 181 LEU 181 172 172 LEU LEU A . n 
A 1 182 ASN 182 173 173 ASN ASN A . n 
A 1 183 ALA 183 174 174 ALA ALA A . n 
A 1 184 ILE 184 175 175 ILE ILE A . n 
A 1 185 GLU 185 176 176 GLU GLU A . n 
A 1 186 ALA 186 177 177 ALA ALA A . n 
A 1 187 GLY 187 178 178 GLY GLY A . n 
A 1 188 PHE 188 179 179 PHE PHE A . n 
A 1 189 ASP 189 180 180 ASP ASP A . n 
A 1 190 GLY 190 181 181 GLY GLY A . n 
A 1 191 ILE 191 182 182 ILE ILE A . n 
A 1 192 GLU 192 183 183 GLU GLU A . n 
A 1 193 ILE 193 184 184 ILE ILE A . n 
A 1 194 HIS 194 185 185 HIS HIS A . n 
A 1 195 GLY 195 186 186 GLY GLY A . n 
A 1 196 ALA 196 187 187 ALA ALA A . n 
A 1 197 HIS 197 188 188 HIS HIS A . n 
A 1 198 GLY 198 189 189 GLY GLY A . n 
A 1 199 TYR 199 190 190 TYR TYR A . n 
A 1 200 LEU 200 191 191 LEU LEU A . n 
A 1 201 ILE 201 192 192 ILE ILE A . n 
A 1 202 ASP 202 193 193 ASP ASP A . n 
A 1 203 GLN 203 194 194 GLN GLN A . n 
A 1 204 PHE 204 195 195 PHE PHE A . n 
A 1 205 LEU 205 196 196 LEU LEU A . n 
A 1 206 LYS 206 197 197 LYS LYS A . n 
A 1 207 ASP 207 198 198 ASP ASP A . n 
A 1 208 GLY 208 199 199 GLY GLY A . n 
A 1 209 ILE 209 200 200 ILE ILE A . n 
A 1 210 ASN 210 201 201 ASN ASN A . n 
A 1 211 ASP 211 202 202 ASP ASP A . n 
A 1 212 ARG 212 203 203 ARG ARG A . n 
A 1 213 THR 213 204 204 THR THR A . n 
A 1 214 ASP 214 205 205 ASP ASP A . n 
A 1 215 GLU 215 206 206 GLU GLU A . n 
A 1 216 TYR 216 207 207 TYR TYR A . n 
A 1 217 GLY 217 208 208 GLY GLY A . n 
A 1 218 GLY 218 209 209 GLY GLY A . n 
A 1 219 SER 219 210 210 SER SER A . n 
A 1 220 LEU 220 211 211 LEU LEU A . n 
A 1 221 ALA 221 212 212 ALA ALA A . n 
A 1 222 ASN 222 213 213 ASN ASN A . n 
A 1 223 ARG 223 214 214 ARG ARG A . n 
A 1 224 CYS 224 215 215 CYS CYS A . n 
A 1 225 LYS 225 216 216 LYS LYS A . n 
A 1 226 PHE 226 217 217 PHE PHE A . n 
A 1 227 ILE 227 218 218 ILE ILE A . n 
A 1 228 THR 228 219 219 THR THR A . n 
A 1 229 GLN 229 220 220 GLN GLN A . n 
A 1 230 VAL 230 221 221 VAL VAL A . n 
A 1 231 VAL 231 222 222 VAL VAL A . n 
A 1 232 GLN 232 223 223 GLN GLN A . n 
A 1 233 ALA 233 224 224 ALA ALA A . n 
A 1 234 VAL 234 225 225 VAL VAL A . n 
A 1 235 VAL 235 226 226 VAL VAL A . n 
A 1 236 SER 236 227 227 SER SER A . n 
A 1 237 ALA 237 228 228 ALA ALA A . n 
A 1 238 ILE 238 229 229 ILE ILE A . n 
A 1 239 GLY 239 230 230 GLY GLY A . n 
A 1 240 ALA 240 231 231 ALA ALA A . n 
A 1 241 ASP 241 232 232 ASP ASP A . n 
A 1 242 ARG 242 233 233 ARG ARG A . n 
A 1 243 VAL 243 234 234 VAL VAL A . n 
A 1 244 GLY 244 235 235 GLY GLY A . n 
A 1 245 VAL 245 236 236 VAL VAL A . n 
A 1 246 ARG 246 237 237 ARG ARG A . n 
A 1 247 VAL 247 238 238 VAL VAL A . n 
A 1 248 SER 248 239 239 SER SER A . n 
A 1 249 PRO 249 240 240 PRO PRO A . n 
A 1 250 ALA 250 241 241 ALA ALA A . n 
A 1 251 ILE 251 242 242 ILE ILE A . n 
A 1 252 ASP 252 243 243 ASP ASP A . n 
A 1 253 HIS 253 244 244 HIS HIS A . n 
A 1 254 LEU 254 245 245 LEU LEU A . n 
A 1 255 ASP 255 246 246 ASP ASP A . n 
A 1 256 ALA 256 247 247 ALA ALA A . n 
A 1 257 MET 257 248 248 MET MET A . n 
A 1 258 ASP 258 249 249 ASP ASP A . n 
A 1 259 SER 259 250 250 SER SER A . n 
A 1 260 ASN 260 251 251 ASN ASN A . n 
A 1 261 PRO 261 252 252 PRO PRO A . n 
A 1 262 LEU 262 253 253 LEU LEU A . n 
A 1 263 SER 263 254 254 SER SER A . n 
A 1 264 LEU 264 255 255 LEU LEU A . n 
A 1 265 GLY 265 256 256 GLY GLY A . n 
A 1 266 LEU 266 257 257 LEU LEU A . n 
A 1 267 ALA 267 258 258 ALA ALA A . n 
A 1 268 VAL 268 259 259 VAL VAL A . n 
A 1 269 VAL 269 260 260 VAL VAL A . n 
A 1 270 GLU 270 261 261 GLU GLU A . n 
A 1 271 ARG 271 262 262 ARG ARG A . n 
A 1 272 LEU 272 263 263 LEU LEU A . n 
A 1 273 ASN 273 264 264 ASN ASN A . n 
A 1 274 LYS 274 265 265 LYS LYS A . n 
A 1 275 ILE 275 266 266 ILE ILE A . n 
A 1 276 GLN 276 267 267 GLN GLN A . n 
A 1 277 LEU 277 268 268 LEU LEU A . n 
A 1 278 HIS 278 269 269 HIS HIS A . n 
A 1 279 SER 279 270 270 SER SER A . n 
A 1 280 GLY 280 271 271 GLY GLY A . n 
A 1 281 SER 281 272 272 SER SER A . n 
A 1 282 LYS 282 273 273 LYS LYS A . n 
A 1 283 LEU 283 274 274 LEU LEU A . n 
A 1 284 ALA 284 275 275 ALA ALA A . n 
A 1 285 TYR 285 276 276 TYR TYR A . n 
A 1 286 LEU 286 277 277 LEU LEU A . n 
A 1 287 HIS 287 278 278 HIS HIS A . n 
A 1 288 VAL 288 279 279 VAL VAL A . n 
A 1 289 THR 289 280 280 THR THR A . n 
A 1 290 GLN 290 281 281 GLN GLN A . n 
A 1 291 PRO 291 282 282 PRO PRO A . n 
A 1 292 GLY 292 283 283 GLY GLY A . n 
A 1 293 ASP 293 284 284 ASP ASP A . n 
A 1 294 GLY 294 285 285 GLY GLY A . n 
A 1 295 ARG 295 286 ?   ?   ?   A . n 
A 1 296 GLY 296 287 ?   ?   ?   A . n 
A 1 297 SER 297 288 288 SER SER A . n 
A 1 298 GLU 298 289 289 GLU GLU A . n 
A 1 299 GLU 299 290 290 GLU GLU A . n 
A 1 300 GLU 300 291 291 GLU GLU A . n 
A 1 301 GLU 301 292 292 GLU GLU A . n 
A 1 302 ALA 302 293 293 ALA ALA A . n 
A 1 303 ARG 303 294 294 ARG ARG A . n 
A 1 304 LEU 304 295 295 LEU LEU A . n 
A 1 305 MET 305 296 296 MET MET A . n 
A 1 306 ARG 306 297 297 ARG ARG A . n 
A 1 307 THR 307 298 298 THR THR A . n 
A 1 308 LEU 308 299 299 LEU LEU A . n 
A 1 309 ARG 309 300 300 ARG ARG A . n 
A 1 310 ASN 310 301 301 ASN ASN A . n 
A 1 311 ALA 311 302 302 ALA ALA A . n 
A 1 312 TYR 312 303 303 TYR TYR A . n 
A 1 313 GLN 313 304 304 GLN GLN A . n 
A 1 314 GLY 314 305 305 GLY GLY A . n 
A 1 315 THR 315 306 306 THR THR A . n 
A 1 316 PHE 316 307 307 PHE PHE A . n 
A 1 317 ILE 317 308 308 ILE ILE A . n 
A 1 318 CYS 318 309 309 CYS CYS A . n 
A 1 319 SER 319 310 310 SER SER A . n 
A 1 320 GLY 320 311 311 GLY GLY A . n 
A 1 321 GLY 321 312 312 GLY GLY A . n 
A 1 322 TYR 322 313 313 TYR TYR A . n 
A 1 323 THR 323 314 314 THR THR A . n 
A 1 324 ARG 324 315 315 ARG ARG A . n 
A 1 325 GLU 325 316 316 GLU GLU A . n 
A 1 326 LEU 326 317 317 LEU LEU A . n 
A 1 327 GLY 327 318 318 GLY GLY A . n 
A 1 328 ILE 328 319 319 ILE ILE A . n 
A 1 329 GLU 329 320 320 GLU GLU A . n 
A 1 330 ALA 330 321 321 ALA ALA A . n 
A 1 331 VAL 331 322 322 VAL VAL A . n 
A 1 332 ALA 332 323 323 ALA ALA A . n 
A 1 333 GLN 333 324 324 GLN GLN A . n 
A 1 334 GLY 334 325 325 GLY GLY A . n 
A 1 335 ASP 335 326 326 ASP ASP A . n 
A 1 336 ALA 336 327 327 ALA ALA A . n 
A 1 337 ASP 337 328 328 ASP ASP A . n 
A 1 338 LEU 338 329 329 LEU LEU A . n 
A 1 339 VAL 339 330 330 VAL VAL A . n 
A 1 340 SER 340 331 331 SER SER A . n 
A 1 341 TYR 341 332 332 TYR TYR A . n 
A 1 342 GLY 342 333 333 GLY GLY A . n 
A 1 343 ARG 343 334 334 ARG ARG A . n 
A 1 344 LEU 344 335 335 LEU LEU A . n 
A 1 345 PHE 345 336 336 PHE PHE A . n 
A 1 346 ILE 346 337 337 ILE ILE A . n 
A 1 347 SER 347 338 338 SER SER A . n 
A 1 348 ASN 348 339 339 ASN ASN A . n 
A 1 349 PRO 349 340 340 PRO PRO A . n 
A 1 350 ASP 350 341 341 ASP ASP A . n 
A 1 351 LEU 351 342 342 LEU LEU A . n 
A 1 352 VAL 352 343 343 VAL VAL A . n 
A 1 353 MET 353 344 344 MET MET A . n 
A 1 354 ARG 354 345 345 ARG ARG A . n 
A 1 355 ILE 355 346 346 ILE ILE A . n 
A 1 356 LYS 356 347 347 LYS LYS A . n 
A 1 357 LEU 357 348 348 LEU LEU A . n 
A 1 358 ASN 358 349 349 ASN ASN A . n 
A 1 359 ALA 359 350 350 ALA ALA A . n 
A 1 360 PRO 360 351 351 PRO PRO A . n 
A 1 361 LEU 361 352 352 LEU LEU A . n 
A 1 362 ASN 362 353 353 ASN ASN A . n 
A 1 363 LYS 363 354 354 LYS LYS A . n 
A 1 364 TYR 364 355 355 TYR TYR A . n 
A 1 365 ASN 365 356 356 ASN ASN A . n 
A 1 366 ARG 366 357 357 ARG ARG A . n 
A 1 367 LYS 367 358 358 LYS LYS A . n 
A 1 368 THR 368 359 359 THR THR A . n 
A 1 369 PHE 369 360 360 PHE PHE A . n 
A 1 370 TYR 370 361 361 TYR TYR A . n 
A 1 371 THR 371 362 362 THR THR A . n 
A 1 372 GLN 372 363 363 GLN GLN A . n 
A 1 373 ASP 373 364 364 ASP ASP A . n 
A 1 374 PRO 374 365 365 PRO PRO A . n 
A 1 375 VAL 375 366 366 VAL VAL A . n 
A 1 376 VAL 376 367 367 VAL VAL A . n 
A 1 377 GLY 377 368 368 GLY GLY A . n 
A 1 378 TYR 378 369 369 TYR TYR A . n 
A 1 379 THR 379 370 370 THR THR A . n 
A 1 380 ASP 380 371 371 ASP ASP A . n 
A 1 381 TYR 381 372 372 TYR TYR A . n 
A 1 382 PRO 382 373 373 PRO PRO A . n 
A 1 383 PHE 383 374 374 PHE PHE A . n 
A 1 384 LEU 384 375 375 LEU LEU A . n 
A 1 385 GLN 385 376 ?   ?   ?   A . n 
A 1 386 GLY 386 377 ?   ?   ?   A . n 
A 1 387 ASN 387 378 ?   ?   ?   A . n 
A 1 388 GLY 388 379 ?   ?   ?   A . n 
A 1 389 SER 389 380 ?   ?   ?   A . n 
A 1 390 ASN 390 381 ?   ?   ?   A . n 
A 1 391 GLY 391 382 ?   ?   ?   A . n 
A 1 392 PRO 392 383 ?   ?   ?   A . n 
A 1 393 LEU 393 384 ?   ?   ?   A . n 
A 1 394 SER 394 385 ?   ?   ?   A . n 
A 1 395 ARG 395 386 ?   ?   ?   A . n 
A 1 396 LEU 396 387 ?   ?   ?   A . 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 
B 2 FMN 1   401 401 FMN FMN A . 
C 3 WI6 1   402 402 WI6 TXD A . 
D 4 SO4 1   403 1   SO4 SO4 A . 
E 5 HOH 1   501 292 HOH HOH A . 
E 5 HOH 2   502 219 HOH HOH A . 
E 5 HOH 3   503 344 HOH HOH A . 
E 5 HOH 4   504 280 HOH HOH A . 
E 5 HOH 5   505 212 HOH HOH A . 
E 5 HOH 6   506 457 HOH HOH A . 
E 5 HOH 7   507 343 HOH HOH A . 
E 5 HOH 8   508 257 HOH HOH A . 
E 5 HOH 9   509 500 HOH HOH A . 
E 5 HOH 10  510 388 HOH HOH A . 
E 5 HOH 11  511 501 HOH HOH A . 
E 5 HOH 12  512 333 HOH HOH A . 
E 5 HOH 13  513 399 HOH HOH A . 
E 5 HOH 14  514 247 HOH HOH A . 
E 5 HOH 15  515 180 HOH HOH A . 
E 5 HOH 16  516 210 HOH HOH A . 
E 5 HOH 17  517 361 HOH HOH A . 
E 5 HOH 18  518 414 HOH HOH A . 
E 5 HOH 19  519 129 HOH HOH A . 
E 5 HOH 20  520 107 HOH HOH A . 
E 5 HOH 21  521 222 HOH HOH A . 
E 5 HOH 22  522 53  HOH HOH A . 
E 5 HOH 23  523 301 HOH HOH A . 
E 5 HOH 24  524 245 HOH HOH A . 
E 5 HOH 25  525 220 HOH HOH A . 
E 5 HOH 26  526 28  HOH HOH A . 
E 5 HOH 27  527 425 HOH HOH A . 
E 5 HOH 28  528 61  HOH HOH A . 
E 5 HOH 29  529 217 HOH HOH A . 
E 5 HOH 30  530 332 HOH HOH A . 
E 5 HOH 31  531 120 HOH HOH A . 
E 5 HOH 32  532 321 HOH HOH A . 
E 5 HOH 33  533 125 HOH HOH A . 
E 5 HOH 34  534 108 HOH HOH A . 
E 5 HOH 35  535 39  HOH HOH A . 
E 5 HOH 36  536 142 HOH HOH A . 
E 5 HOH 37  537 252 HOH HOH A . 
E 5 HOH 38  538 181 HOH HOH A . 
E 5 HOH 39  539 179 HOH HOH A . 
E 5 HOH 40  540 214 HOH HOH A . 
E 5 HOH 41  541 192 HOH HOH A . 
E 5 HOH 42  542 45  HOH HOH A . 
E 5 HOH 43  543 48  HOH HOH A . 
E 5 HOH 44  544 160 HOH HOH A . 
E 5 HOH 45  545 25  HOH HOH A . 
E 5 HOH 46  546 403 HOH HOH A . 
E 5 HOH 47  547 88  HOH HOH A . 
E 5 HOH 48  548 177 HOH HOH A . 
E 5 HOH 49  549 152 HOH HOH A . 
E 5 HOH 50  550 475 HOH HOH A . 
E 5 HOH 51  551 147 HOH HOH A . 
E 5 HOH 52  552 472 HOH HOH A . 
E 5 HOH 53  553 151 HOH HOH A . 
E 5 HOH 54  554 426 HOH HOH A . 
E 5 HOH 55  555 264 HOH HOH A . 
E 5 HOH 56  556 216 HOH HOH A . 
E 5 HOH 57  557 326 HOH HOH A . 
E 5 HOH 58  558 443 HOH HOH A . 
E 5 HOH 59  559 502 HOH HOH A . 
E 5 HOH 60  560 74  HOH HOH A . 
E 5 HOH 61  561 32  HOH HOH A . 
E 5 HOH 62  562 373 HOH HOH A . 
E 5 HOH 63  563 51  HOH HOH A . 
E 5 HOH 64  564 205 HOH HOH A . 
E 5 HOH 65  565 20  HOH HOH A . 
E 5 HOH 66  566 63  HOH HOH A . 
E 5 HOH 67  567 334 HOH HOH A . 
E 5 HOH 68  568 4   HOH HOH A . 
E 5 HOH 69  569 153 HOH HOH A . 
E 5 HOH 70  570 66  HOH HOH A . 
E 5 HOH 71  571 65  HOH HOH A . 
E 5 HOH 72  572 92  HOH HOH A . 
E 5 HOH 73  573 46  HOH HOH A . 
E 5 HOH 74  574 164 HOH HOH A . 
E 5 HOH 75  575 168 HOH HOH A . 
E 5 HOH 76  576 307 HOH HOH A . 
E 5 HOH 77  577 145 HOH HOH A . 
E 5 HOH 78  578 62  HOH HOH A . 
E 5 HOH 79  579 119 HOH HOH A . 
E 5 HOH 80  580 499 HOH HOH A . 
E 5 HOH 81  581 27  HOH HOH A . 
E 5 HOH 82  582 157 HOH HOH A . 
E 5 HOH 83  583 22  HOH HOH A . 
E 5 HOH 84  584 230 HOH HOH A . 
E 5 HOH 85  585 9   HOH HOH A . 
E 5 HOH 86  586 354 HOH HOH A . 
E 5 HOH 87  587 68  HOH HOH A . 
E 5 HOH 88  588 67  HOH HOH A . 
E 5 HOH 89  589 5   HOH HOH A . 
E 5 HOH 90  590 232 HOH HOH A . 
E 5 HOH 91  591 97  HOH HOH A . 
E 5 HOH 92  592 422 HOH HOH A . 
E 5 HOH 93  593 40  HOH HOH A . 
E 5 HOH 94  594 167 HOH HOH A . 
E 5 HOH 95  595 155 HOH HOH A . 
E 5 HOH 96  596 183 HOH HOH A . 
E 5 HOH 97  597 23  HOH HOH A . 
E 5 HOH 98  598 47  HOH HOH A . 
E 5 HOH 99  599 288 HOH HOH A . 
E 5 HOH 100 600 258 HOH HOH A . 
E 5 HOH 101 601 96  HOH HOH A . 
E 5 HOH 102 602 237 HOH HOH A . 
E 5 HOH 103 603 71  HOH HOH A . 
E 5 HOH 104 604 8   HOH HOH A . 
E 5 HOH 105 605 6   HOH HOH A . 
E 5 HOH 106 606 174 HOH HOH A . 
E 5 HOH 107 607 328 HOH HOH A . 
E 5 HOH 108 608 173 HOH HOH A . 
E 5 HOH 109 609 234 HOH HOH A . 
E 5 HOH 110 610 49  HOH HOH A . 
E 5 HOH 111 611 506 HOH HOH A . 
E 5 HOH 112 612 139 HOH HOH A . 
E 5 HOH 113 613 126 HOH HOH A . 
E 5 HOH 114 614 478 HOH HOH A . 
E 5 HOH 115 615 276 HOH HOH A . 
E 5 HOH 116 616 432 HOH HOH A . 
E 5 HOH 117 617 293 HOH HOH A . 
E 5 HOH 118 618 248 HOH HOH A . 
E 5 HOH 119 619 76  HOH HOH A . 
E 5 HOH 120 620 14  HOH HOH A . 
E 5 HOH 121 621 477 HOH HOH A . 
E 5 HOH 122 622 364 HOH HOH A . 
E 5 HOH 123 623 29  HOH HOH A . 
E 5 HOH 124 624 161 HOH HOH A . 
E 5 HOH 125 625 64  HOH HOH A . 
E 5 HOH 126 626 90  HOH HOH A . 
E 5 HOH 127 627 60  HOH HOH A . 
E 5 HOH 128 628 98  HOH HOH A . 
E 5 HOH 129 629 3   HOH HOH A . 
E 5 HOH 130 630 203 HOH HOH A . 
E 5 HOH 131 631 479 HOH HOH A . 
E 5 HOH 132 632 229 HOH HOH A . 
E 5 HOH 133 633 196 HOH HOH A . 
E 5 HOH 134 634 54  HOH HOH A . 
E 5 HOH 135 635 200 HOH HOH A . 
E 5 HOH 136 636 19  HOH HOH A . 
E 5 HOH 137 637 384 HOH HOH A . 
E 5 HOH 138 638 188 HOH HOH A . 
E 5 HOH 139 639 400 HOH HOH A . 
E 5 HOH 140 640 87  HOH HOH A . 
E 5 HOH 141 641 102 HOH HOH A . 
E 5 HOH 142 642 100 HOH HOH A . 
E 5 HOH 143 643 398 HOH HOH A . 
E 5 HOH 144 644 31  HOH HOH A . 
E 5 HOH 145 645 132 HOH HOH A . 
E 5 HOH 146 646 118 HOH HOH A . 
E 5 HOH 147 647 263 HOH HOH A . 
E 5 HOH 148 648 122 HOH HOH A . 
E 5 HOH 149 649 244 HOH HOH A . 
E 5 HOH 150 650 266 HOH HOH A . 
E 5 HOH 151 651 36  HOH HOH A . 
E 5 HOH 152 652 12  HOH HOH A . 
E 5 HOH 153 653 73  HOH HOH A . 
E 5 HOH 154 654 58  HOH HOH A . 
E 5 HOH 155 655 91  HOH HOH A . 
E 5 HOH 156 656 99  HOH HOH A . 
E 5 HOH 157 657 311 HOH HOH A . 
E 5 HOH 158 658 17  HOH HOH A . 
E 5 HOH 159 659 15  HOH HOH A . 
E 5 HOH 160 660 84  HOH HOH A . 
E 5 HOH 161 661 30  HOH HOH A . 
E 5 HOH 162 662 16  HOH HOH A . 
E 5 HOH 163 663 363 HOH HOH A . 
E 5 HOH 164 664 56  HOH HOH A . 
E 5 HOH 165 665 324 HOH HOH A . 
E 5 HOH 166 666 494 HOH HOH A . 
E 5 HOH 167 667 171 HOH HOH A . 
E 5 HOH 168 668 26  HOH HOH A . 
E 5 HOH 169 669 209 HOH HOH A . 
E 5 HOH 170 670 496 HOH HOH A . 
E 5 HOH 171 671 243 HOH HOH A . 
E 5 HOH 172 672 273 HOH HOH A . 
E 5 HOH 173 673 140 HOH HOH A . 
E 5 HOH 174 674 123 HOH HOH A . 
E 5 HOH 175 675 262 HOH HOH A . 
E 5 HOH 176 676 135 HOH HOH A . 
E 5 HOH 177 677 38  HOH HOH A . 
E 5 HOH 178 678 430 HOH HOH A . 
E 5 HOH 179 679 341 HOH HOH A . 
E 5 HOH 180 680 246 HOH HOH A . 
E 5 HOH 181 681 82  HOH HOH A . 
E 5 HOH 182 682 134 HOH HOH A . 
E 5 HOH 183 683 59  HOH HOH A . 
E 5 HOH 184 684 481 HOH HOH A . 
E 5 HOH 185 685 242 HOH HOH A . 
E 5 HOH 186 686 86  HOH HOH A . 
E 5 HOH 187 687 492 HOH HOH A . 
E 5 HOH 188 688 78  HOH HOH A . 
E 5 HOH 189 689 178 HOH HOH A . 
E 5 HOH 190 690 265 HOH HOH A . 
E 5 HOH 191 691 2   HOH HOH A . 
E 5 HOH 192 692 186 HOH HOH A . 
E 5 HOH 193 693 268 HOH HOH A . 
E 5 HOH 194 694 75  HOH HOH A . 
E 5 HOH 195 695 7   HOH HOH A . 
E 5 HOH 196 696 335 HOH HOH A . 
E 5 HOH 197 697 162 HOH HOH A . 
E 5 HOH 198 698 170 HOH HOH A . 
E 5 HOH 199 699 348 HOH HOH A . 
E 5 HOH 200 700 34  HOH HOH A . 
E 5 HOH 201 701 503 HOH HOH A . 
E 5 HOH 202 702 255 HOH HOH A . 
E 5 HOH 203 703 269 HOH HOH A . 
E 5 HOH 204 704 279 HOH HOH A . 
E 5 HOH 205 705 194 HOH HOH A . 
E 5 HOH 206 706 376 HOH HOH A . 
E 5 HOH 207 707 191 HOH HOH A . 
E 5 HOH 208 708 10  HOH HOH A . 
E 5 HOH 209 709 81  HOH HOH A . 
E 5 HOH 210 710 228 HOH HOH A . 
E 5 HOH 211 711 128 HOH HOH A . 
E 5 HOH 212 712 154 HOH HOH A . 
E 5 HOH 213 713 89  HOH HOH A . 
E 5 HOH 214 714 465 HOH HOH A . 
E 5 HOH 215 715 44  HOH HOH A . 
E 5 HOH 216 716 201 HOH HOH A . 
E 5 HOH 217 717 137 HOH HOH A . 
E 5 HOH 218 718 77  HOH HOH A . 
E 5 HOH 219 719 35  HOH HOH A . 
E 5 HOH 220 720 33  HOH HOH A . 
E 5 HOH 221 721 149 HOH HOH A . 
E 5 HOH 222 722 113 HOH HOH A . 
E 5 HOH 223 723 111 HOH HOH A . 
E 5 HOH 224 724 24  HOH HOH A . 
E 5 HOH 225 725 286 HOH HOH A . 
E 5 HOH 226 726 146 HOH HOH A . 
E 5 HOH 227 727 130 HOH HOH A . 
E 5 HOH 228 728 37  HOH HOH A . 
E 5 HOH 229 729 93  HOH HOH A . 
E 5 HOH 230 730 350 HOH HOH A . 
E 5 HOH 231 731 199 HOH HOH A . 
E 5 HOH 232 732 116 HOH HOH A . 
E 5 HOH 233 733 497 HOH HOH A . 
E 5 HOH 234 734 136 HOH HOH A . 
E 5 HOH 235 735 261 HOH HOH A . 
E 5 HOH 236 736 50  HOH HOH A . 
E 5 HOH 237 737 41  HOH HOH A . 
E 5 HOH 238 738 250 HOH HOH A . 
E 5 HOH 239 739 114 HOH HOH A . 
E 5 HOH 240 740 55  HOH HOH A . 
E 5 HOH 241 741 489 HOH HOH A . 
E 5 HOH 242 742 352 HOH HOH A . 
E 5 HOH 243 743 106 HOH HOH A . 
E 5 HOH 244 744 410 HOH HOH A . 
E 5 HOH 245 745 95  HOH HOH A . 
E 5 HOH 246 746 208 HOH HOH A . 
E 5 HOH 247 747 43  HOH HOH A . 
E 5 HOH 248 748 369 HOH HOH A . 
E 5 HOH 249 749 225 HOH HOH A . 
E 5 HOH 250 750 377 HOH HOH A . 
E 5 HOH 251 751 127 HOH HOH A . 
E 5 HOH 252 752 406 HOH HOH A . 
E 5 HOH 253 753 1   HOH HOH A . 
E 5 HOH 254 754 421 HOH HOH A . 
E 5 HOH 255 755 165 HOH HOH A . 
E 5 HOH 256 756 18  HOH HOH A . 
E 5 HOH 257 757 148 HOH HOH A . 
E 5 HOH 258 758 412 HOH HOH A . 
E 5 HOH 259 759 21  HOH HOH A . 
E 5 HOH 260 760 226 HOH HOH A . 
E 5 HOH 261 761 218 HOH HOH A . 
E 5 HOH 262 762 315 HOH HOH A . 
E 5 HOH 263 763 156 HOH HOH A . 
E 5 HOH 264 764 80  HOH HOH A . 
E 5 HOH 265 765 175 HOH HOH A . 
E 5 HOH 266 766 110 HOH HOH A . 
E 5 HOH 267 767 72  HOH HOH A . 
E 5 HOH 268 768 131 HOH HOH A . 
E 5 HOH 269 769 240 HOH HOH A . 
E 5 HOH 270 770 172 HOH HOH A . 
E 5 HOH 271 771 308 HOH HOH A . 
E 5 HOH 272 772 117 HOH HOH A . 
E 5 HOH 273 773 42  HOH HOH A . 
E 5 HOH 274 774 459 HOH HOH A . 
E 5 HOH 275 775 202 HOH HOH A . 
E 5 HOH 276 776 259 HOH HOH A . 
E 5 HOH 277 777 138 HOH HOH A . 
E 5 HOH 278 778 290 HOH HOH A . 
E 5 HOH 279 779 70  HOH HOH A . 
E 5 HOH 280 780 371 HOH HOH A . 
E 5 HOH 281 781 163 HOH HOH A . 
E 5 HOH 282 782 150 HOH HOH A . 
E 5 HOH 283 783 11  HOH HOH A . 
E 5 HOH 284 784 337 HOH HOH A . 
E 5 HOH 285 785 365 HOH HOH A . 
E 5 HOH 286 786 281 HOH HOH A . 
E 5 HOH 287 787 124 HOH HOH A . 
E 5 HOH 288 788 83  HOH HOH A . 
E 5 HOH 289 789 271 HOH HOH A . 
E 5 HOH 290 790 94  HOH HOH A . 
E 5 HOH 291 791 221 HOH HOH A . 
E 5 HOH 292 792 487 HOH HOH A . 
E 5 HOH 293 793 101 HOH HOH A . 
E 5 HOH 294 794 330 HOH HOH A . 
E 5 HOH 295 795 447 HOH HOH A . 
E 5 HOH 296 796 378 HOH HOH A . 
E 5 HOH 297 797 445 HOH HOH A . 
E 5 HOH 298 798 433 HOH HOH A . 
E 5 HOH 299 799 442 HOH HOH A . 
E 5 HOH 300 800 195 HOH HOH A . 
E 5 HOH 301 801 313 HOH HOH A . 
E 5 HOH 302 802 115 HOH HOH A . 
E 5 HOH 303 803 211 HOH HOH A . 
E 5 HOH 304 804 306 HOH HOH A . 
E 5 HOH 305 805 52  HOH HOH A . 
E 5 HOH 306 806 254 HOH HOH A . 
E 5 HOH 307 807 498 HOH HOH A . 
E 5 HOH 308 808 395 HOH HOH A . 
E 5 HOH 309 809 274 HOH HOH A . 
E 5 HOH 310 810 223 HOH HOH A . 
E 5 HOH 311 811 416 HOH HOH A . 
E 5 HOH 312 812 367 HOH HOH A . 
E 5 HOH 313 813 362 HOH HOH A . 
E 5 HOH 314 814 189 HOH HOH A . 
E 5 HOH 315 815 484 HOH HOH A . 
E 5 HOH 316 816 295 HOH HOH A . 
E 5 HOH 317 817 452 HOH HOH A . 
E 5 HOH 318 818 428 HOH HOH A . 
E 5 HOH 319 819 309 HOH HOH A . 
E 5 HOH 320 820 103 HOH HOH A . 
E 5 HOH 321 821 338 HOH HOH A . 
E 5 HOH 322 822 407 HOH HOH A . 
E 5 HOH 323 823 294 HOH HOH A . 
E 5 HOH 324 824 340 HOH HOH A . 
E 5 HOH 325 825 310 HOH HOH A . 
E 5 HOH 326 826 404 HOH HOH A . 
E 5 HOH 327 827 236 HOH HOH A . 
E 5 HOH 328 828 385 HOH HOH A . 
E 5 HOH 329 829 434 HOH HOH A . 
E 5 HOH 330 830 169 HOH HOH A . 
E 5 HOH 331 831 355 HOH HOH A . 
E 5 HOH 332 832 359 HOH HOH A . 
E 5 HOH 333 833 143 HOH HOH A . 
E 5 HOH 334 834 249 HOH HOH A . 
E 5 HOH 335 835 389 HOH HOH A . 
E 5 HOH 336 836 417 HOH HOH A . 
E 5 HOH 337 837 444 HOH HOH A . 
E 5 HOH 338 838 239 HOH HOH A . 
E 5 HOH 339 839 418 HOH HOH A . 
E 5 HOH 340 840 323 HOH HOH A . 
E 5 HOH 341 841 357 HOH HOH A . 
E 5 HOH 342 842 383 HOH HOH A . 
E 5 HOH 343 843 463 HOH HOH A . 
E 5 HOH 344 844 461 HOH HOH A . 
E 5 HOH 345 845 185 HOH HOH A . 
E 5 HOH 346 846 379 HOH HOH A . 
E 5 HOH 347 847 448 HOH HOH A . 
E 5 HOH 348 848 302 HOH HOH A . 
E 5 HOH 349 849 505 HOH HOH A . 
E 5 HOH 350 850 197 HOH HOH A . 
E 5 HOH 351 851 458 HOH HOH A . 
E 5 HOH 352 852 342 HOH HOH A . 
E 5 HOH 353 853 351 HOH HOH A . 
E 5 HOH 354 854 366 HOH HOH A . 
E 5 HOH 355 855 437 HOH HOH A . 
E 5 HOH 356 856 190 HOH HOH A . 
E 5 HOH 357 857 300 HOH HOH A . 
E 5 HOH 358 858 312 HOH HOH A . 
E 5 HOH 359 859 402 HOH HOH A . 
E 5 HOH 360 860 159 HOH HOH A . 
E 5 HOH 361 861 424 HOH HOH A . 
E 5 HOH 362 862 278 HOH HOH A . 
E 5 HOH 363 863 79  HOH HOH A . 
E 5 HOH 364 864 270 HOH HOH A . 
E 5 HOH 365 865 298 HOH HOH A . 
E 5 HOH 366 866 454 HOH HOH A . 
E 5 HOH 367 867 495 HOH HOH A . 
E 5 HOH 368 868 260 HOH HOH A . 
E 5 HOH 369 869 193 HOH HOH A . 
E 5 HOH 370 870 370 HOH HOH A . 
E 5 HOH 371 871 429 HOH HOH A . 
E 5 HOH 372 872 327 HOH HOH A . 
E 5 HOH 373 873 482 HOH HOH A . 
E 5 HOH 374 874 449 HOH HOH A . 
E 5 HOH 375 875 176 HOH HOH A . 
E 5 HOH 376 876 204 HOH HOH A . 
E 5 HOH 377 877 314 HOH HOH A . 
E 5 HOH 378 878 109 HOH HOH A . 
E 5 HOH 379 879 256 HOH HOH A . 
E 5 HOH 380 880 353 HOH HOH A . 
E 5 HOH 381 881 235 HOH HOH A . 
E 5 HOH 382 882 207 HOH HOH A . 
E 5 HOH 383 883 112 HOH HOH A . 
E 5 HOH 384 884 476 HOH HOH A . 
E 5 HOH 385 885 277 HOH HOH A . 
E 5 HOH 386 886 380 HOH HOH A . 
E 5 HOH 387 887 198 HOH HOH A . 
E 5 HOH 388 888 238 HOH HOH A . 
E 5 HOH 389 889 386 HOH HOH A . 
E 5 HOH 390 890 297 HOH HOH A . 
E 5 HOH 391 891 438 HOH HOH A . 
E 5 HOH 392 892 287 HOH HOH A . 
E 5 HOH 393 893 304 HOH HOH A . 
E 5 HOH 394 894 504 HOH HOH A . 
E 5 HOH 395 895 317 HOH HOH A . 
E 5 HOH 396 896 480 HOH HOH A . 
E 5 HOH 397 897 184 HOH HOH A . 
E 5 HOH 398 898 397 HOH HOH A . 
E 5 HOH 399 899 206 HOH HOH A . 
E 5 HOH 400 900 144 HOH HOH A . 
E 5 HOH 401 901 431 HOH HOH A . 
E 5 HOH 402 902 427 HOH HOH A . 
E 5 HOH 403 903 133 HOH HOH A . 
E 5 HOH 404 904 329 HOH HOH A . 
E 5 HOH 405 905 488 HOH HOH A . 
E 5 HOH 406 906 105 HOH HOH A . 
E 5 HOH 407 907 284 HOH HOH A . 
E 5 HOH 408 908 285 HOH HOH A . 
E 5 HOH 409 909 455 HOH HOH A . 
E 5 HOH 410 910 325 HOH HOH A . 
E 5 HOH 411 911 339 HOH HOH A . 
E 5 HOH 412 912 446 HOH HOH A . 
E 5 HOH 413 913 158 HOH HOH A . 
E 5 HOH 414 914 381 HOH HOH A . 
E 5 HOH 415 915 450 HOH HOH A . 
E 5 HOH 416 916 409 HOH HOH A . 
E 5 HOH 417 917 316 HOH HOH A . 
E 5 HOH 418 918 474 HOH HOH A . 
E 5 HOH 419 919 413 HOH HOH A . 
E 5 HOH 420 920 289 HOH HOH A . 
E 5 HOH 421 921 331 HOH HOH A . 
E 5 HOH 422 922 486 HOH HOH A . 
E 5 HOH 423 923 272 HOH HOH A . 
E 5 HOH 424 924 305 HOH HOH A . 
E 5 HOH 425 925 347 HOH HOH A . 
E 5 HOH 426 926 267 HOH HOH A . 
E 5 HOH 427 927 453 HOH HOH A . 
E 5 HOH 428 928 253 HOH HOH A . 
E 5 HOH 429 929 439 HOH HOH A . 
E 5 HOH 430 930 291 HOH HOH A . 
E 5 HOH 431 931 224 HOH HOH A . 
E 5 HOH 432 932 231 HOH HOH A . 
E 5 HOH 433 933 401 HOH HOH A . 
E 5 HOH 434 934 85  HOH HOH A . 
E 5 HOH 435 935 215 HOH HOH A . 
E 5 HOH 436 936 336 HOH HOH A . 
E 5 HOH 437 937 374 HOH HOH A . 
E 5 HOH 438 938 187 HOH HOH A . 
E 5 HOH 439 939 493 HOH HOH A . 
E 5 HOH 440 940 166 HOH HOH A . 
E 5 HOH 441 941 360 HOH HOH A . 
E 5 HOH 442 942 372 HOH HOH A . 
E 5 HOH 443 943 466 HOH HOH A . 
E 5 HOH 444 944 473 HOH HOH A . 
E 5 HOH 445 945 387 HOH HOH A . 
E 5 HOH 446 946 299 HOH HOH A . 
E 5 HOH 447 947 320 HOH HOH A . 
E 5 HOH 448 948 469 HOH HOH A . 
E 5 HOH 449 949 296 HOH HOH A . 
E 5 HOH 450 950 227 HOH HOH A . 
E 5 HOH 451 951 483 HOH HOH A . 
E 5 HOH 452 952 460 HOH HOH A . 
E 5 HOH 453 953 440 HOH HOH A . 
E 5 HOH 454 954 368 HOH HOH A . 
E 5 HOH 455 955 375 HOH HOH A . 
E 5 HOH 456 956 356 HOH HOH A . 
E 5 HOH 457 957 303 HOH HOH A . 
E 5 HOH 458 958 411 HOH HOH A . 
E 5 HOH 459 959 233 HOH HOH A . 
E 5 HOH 460 960 390 HOH HOH A . 
E 5 HOH 461 961 467 HOH HOH A . 
E 5 HOH 462 962 318 HOH HOH A . 
E 5 HOH 463 963 322 HOH HOH A . 
E 5 HOH 464 964 283 HOH HOH A . 
E 5 HOH 465 965 441 HOH HOH A . 
E 5 HOH 466 966 470 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 20  ? CG    ? A LYS 29  CG    
2  1 Y 1 A LYS 20  ? CD    ? A LYS 29  CD    
3  1 Y 1 A LYS 20  ? CE    ? A LYS 29  CE    
4  1 Y 1 A LYS 20  ? NZ    ? A LYS 29  NZ    
5  1 Y 1 A GLU 116 ? CG    ? A GLU 125 CG    
6  1 Y 1 A GLU 116 ? CD    ? A GLU 125 CD    
7  1 Y 1 A GLU 116 ? OE1   ? A GLU 125 OE1   
8  1 Y 1 A GLU 116 ? OE2   ? A GLU 125 OE2   
9  1 Y 1 A GLU 130 ? CG    ? A GLU 139 CG    
10 1 Y 1 A GLU 130 ? CD    ? A GLU 139 CD    
11 1 Y 1 A GLU 130 ? OE1   ? A GLU 139 OE1   
12 1 Y 1 A GLU 130 ? OE2   ? A GLU 139 OE2   
13 1 Y 1 A ASP 284 ? CG    ? A ASP 293 CG    
14 1 Y 1 A ASP 284 ? OD1   ? A ASP 293 OD1   
15 1 Y 1 A ASP 284 ? OD2   ? A ASP 293 OD2   
16 1 Y 1 A GLU 289 ? CG    ? A GLU 298 CG    
17 1 Y 1 A GLU 289 ? CD    ? A GLU 298 CD    
18 1 Y 1 A GLU 289 ? OE1   ? A GLU 298 OE1   
19 1 Y 1 A GLU 289 ? OE2   ? A GLU 298 OE2   
20 1 Y 1 A GLU 290 ? CG    ? A GLU 299 CG    
21 1 Y 1 A GLU 290 ? CD    ? A GLU 299 CD    
22 1 Y 1 A GLU 290 ? OE1   ? A GLU 299 OE1   
23 1 Y 1 A GLU 290 ? OE2   ? A GLU 299 OE2   
24 1 Y 1 A GLU 291 ? CG    ? A GLU 300 CG    
25 1 Y 1 A GLU 291 ? CD    ? A GLU 300 CD    
26 1 Y 1 A GLU 291 ? OE1   ? A GLU 300 OE1   
27 1 Y 1 A GLU 291 ? OE2   ? A GLU 300 OE2   
28 1 Y 1 A GLU 316 ? CG    ? A GLU 325 CG    
29 1 Y 1 A GLU 316 ? CD    ? A GLU 325 CD    
30 1 Y 1 A GLU 316 ? OE1   ? A GLU 325 OE1   
31 1 Y 1 A GLU 316 ? OE2   ? A GLU 325 OE2   
32 1 Y 1 A GLU 320 ? CG    ? A GLU 329 CG    
33 1 Y 1 A GLU 320 ? CD    ? A GLU 329 CD    
34 1 Y 1 A GLU 320 ? OE1   ? A GLU 329 OE1   
35 1 Y 1 A GLU 320 ? OE2   ? A GLU 329 OE2   
36 1 Y 1 A LYS 358 ? CG    ? A LYS 367 CG    
37 1 Y 1 A LYS 358 ? CD    ? A LYS 367 CD    
38 1 Y 1 A LYS 358 ? CE    ? A LYS 367 CE    
39 1 Y 1 A LYS 358 ? NZ    ? A LYS 367 NZ    
40 1 N 0 A WI6 402 ? "C5'" B C WI6 ?   "C5'" 
41 1 N 0 A WI6 402 ? "C4'" B C WI6 ?   "C4'" 
42 1 N 0 A WI6 402 ? "O4'" B C WI6 ?   "O4'" 
43 1 N 0 A WI6 402 ? "C3'" B C WI6 ?   "C3'" 
44 1 N 0 A WI6 402 ? "O2'" B C WI6 ?   "O2'" 
45 1 N 0 A WI6 402 ? "O3'" B C WI6 ?   "O3'" 
# 
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                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8QNX 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     88.010 
_cell.length_a_esd                 ? 
_cell.length_b                     89.620 
_cell.length_b_esd                 ? 
_cell.length_c                     49.400 
_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                         8QNX 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 2' 
_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                   8QNX 
_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             2.23 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          44.93 
_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 MES/Tris, 50 mM ammonium sulfate, 8% 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   1.033 
_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        1.033 
_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                                       8QNX 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.45 
_reflns.d_resolution_low                               44.01 
_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                                     1752169 
_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                           93.36 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                26.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          23.80 
_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                                   0.999 
_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                                    1.45 
_reflns_shell.d_res_low                                     1.47 
_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                             41437 
_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                                  0.862 
_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                                 8QNX 
_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                            1.45 
_refine.ls_d_res_low                             44.01 
_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                     65357 
_refine.ls_number_reflns_R_free                  3269 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    93.36 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1484 
_refine.ls_R_factor_R_free                       0.1722 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1471 
_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                          1.36 
_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                 16.63 
_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                            0.12 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.45 
_refine_hist.d_res_low                        44.01 
_refine_hist.number_atoms_solvent             466 
_refine_hist.number_atoms_total               3340 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        2794 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         80 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.015  ? 2990 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.494  ? 4083 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 15.267 ? 1072 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.117  ? 447  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.018  ? 518  ? 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' 1.45 1.47  . . 91  1711 60.00 . . . . 0.2025 . . . . . . . . . . . 0.2549 
'X-RAY DIFFRACTION' 1.47 1.49  . . 101 1936 68.00 . . . . 0.1849 . . . . . . . . . . . 0.2176 
'X-RAY DIFFRACTION' 1.49 1.52  . . 117 2205 78.00 . . . . 0.1683 . . . . . . . . . . . 0.1667 
'X-RAY DIFFRACTION' 1.52 1.55  . . 137 2604 91.00 . . . . 0.1610 . . . . . . . . . . . 0.2145 
'X-RAY DIFFRACTION' 1.55 1.57  . . 143 2734 96.00 . . . . 0.1459 . . . . . . . . . . . 0.1953 
'X-RAY DIFFRACTION' 1.57 1.60  . . 146 2763 97.00 . . . . 0.1484 . . . . . . . . . . . 0.1916 
'X-RAY DIFFRACTION' 1.60 1.64  . . 145 2750 97.00 . . . . 0.1396 . . . . . . . . . . . 0.1801 
'X-RAY DIFFRACTION' 1.64 1.67  . . 145 2760 97.00 . . . . 0.1407 . . . . . . . . . . . 0.1807 
'X-RAY DIFFRACTION' 1.67 1.71  . . 148 2808 97.00 . . . . 0.1387 . . . . . . . . . . . 0.1963 
'X-RAY DIFFRACTION' 1.71 1.75  . . 146 2784 97.00 . . . . 0.1437 . . . . . . . . . . . 0.1659 
'X-RAY DIFFRACTION' 1.75 1.80  . . 147 2780 97.00 . . . . 0.1402 . . . . . . . . . . . 0.1860 
'X-RAY DIFFRACTION' 1.80 1.85  . . 147 2796 97.00 . . . . 0.1454 . . . . . . . . . . . 0.1752 
'X-RAY DIFFRACTION' 1.85 1.91  . . 142 2700 94.00 . . . . 0.1452 . . . . . . . . . . . 0.1747 
'X-RAY DIFFRACTION' 1.91 1.98  . . 149 2831 98.00 . . . . 0.1439 . . . . . . . . . . . 0.1732 
'X-RAY DIFFRACTION' 1.98 2.06  . . 149 2826 98.00 . . . . 0.1454 . . . . . . . . . . . 0.1726 
'X-RAY DIFFRACTION' 2.06 2.16  . . 149 2835 98.00 . . . . 0.1433 . . . . . . . . . . . 0.1854 
'X-RAY DIFFRACTION' 2.16 2.27  . . 149 2842 98.00 . . . . 0.1472 . . . . . . . . . . . 0.1707 
'X-RAY DIFFRACTION' 2.27 2.41  . . 151 2862 99.00 . . . . 0.1448 . . . . . . . . . . . 0.1847 
'X-RAY DIFFRACTION' 2.41 2.60  . . 151 2867 98.00 . . . . 0.1570 . . . . . . . . . . . 0.1658 
'X-RAY DIFFRACTION' 2.60 2.86  . . 147 2785 95.00 . . . . 0.1547 . . . . . . . . . . . 0.1681 
'X-RAY DIFFRACTION' 2.86 3.27  . . 153 2917 99.00 . . . . 0.1479 . . . . . . . . . . . 0.1807 
'X-RAY DIFFRACTION' 3.27 4.12  . . 156 2970 99.00 . . . . 0.1324 . . . . . . . . . . . 0.1563 
'X-RAY DIFFRACTION' 4.12 44.01 . . 160 3022 97.00 . . . . 0.1530 . . . . . . . . . . . 0.1530 
# 
_struct.entry_id                     8QNX 
_struct.title                        'OPR3 variant with redesigned loop 6 (8aa) 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        8QNX 
_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 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
# 
_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 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8QNX 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 10 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 396 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q9FEW9 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  396 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       387 
# 
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 8QNX MET A 1   ? UNP Q9FEW9 ?   ?   'initiating methionine' -8  1  
1 8QNX ALA A 2   ? UNP Q9FEW9 ?   ?   'expression tag'        -7  2  
1 8QNX SER A 3   ? UNP Q9FEW9 ?   ?   'expression tag'        -6  3  
1 8QNX HIS A 4   ? UNP Q9FEW9 ?   ?   'expression tag'        -5  4  
1 8QNX HIS A 5   ? UNP Q9FEW9 ?   ?   'expression tag'        -4  5  
1 8QNX HIS A 6   ? UNP Q9FEW9 ?   ?   'expression tag'        -3  6  
1 8QNX HIS A 7   ? UNP Q9FEW9 ?   ?   'expression tag'        -2  7  
1 8QNX HIS A 8   ? UNP Q9FEW9 ?   ?   'expression tag'        -1  8  
1 8QNX HIS A 9   ? UNP Q9FEW9 ?   ?   'expression tag'        0   9  
1 8QNX GLY A 292 ? UNP Q9FEW9 ARG 283 'engineered mutation'   283 10 
1 8QNX ASP A 293 ? UNP Q9FEW9 TYR 284 'engineered mutation'   284 11 
1 8QNX GLY A 294 ? UNP Q9FEW9 VAL 285 'engineered mutation'   285 12 
1 8QNX ARG A 295 ? UNP Q9FEW9 ALA 286 'engineered mutation'   286 13 
1 8QNX ?   A ?   ? UNP Q9FEW9 TYR 287 deletion                ?   14 
1 8QNX ?   A ?   ? UNP Q9FEW9 GLY 288 deletion                ?   15 
1 8QNX ?   A ?   ? UNP Q9FEW9 GLN 289 deletion                ?   16 
1 8QNX ?   A ?   ? UNP Q9FEW9 THR 290 deletion                ?   17 
1 8QNX ?   A ?   ? UNP Q9FEW9 GLU 291 deletion                ?   18 
1 8QNX ?   A ?   ? UNP Q9FEW9 ALA 292 deletion                ?   19 
1 8QNX ?   A ?   ? UNP Q9FEW9 GLY 293 deletion                ?   20 
1 8QNX ?   A ?   ? UNP Q9FEW9 ARG 294 deletion                ?   21 
1 8QNX ?   A ?   ? UNP Q9FEW9 LEU 295 deletion                ?   22 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASN A 19  ? SER A 23  ? ASN A 10  SER A 14  5 ? 5  
HELX_P HELX_P2  AA2 ALA A 46  ? ILE A 50  ? ALA A 37  ILE A 41  5 ? 5  
HELX_P HELX_P3  AA3 GLN A 52  ? ALA A 63  ? GLN A 43  ALA A 54  1 ? 12 
HELX_P HELX_P4  AA4 THR A 91  ? LYS A 108 ? THR A 82  LYS A 99  1 ? 18 
HELX_P HELX_P5  AA5 HIS A 124 ? ALA A 132 ? HIS A 115 ALA A 123 5 ? 9  
HELX_P HELX_P6  AA6 GLY A 165 ? ALA A 186 ? GLY A 156 ALA A 177 1 ? 22 
HELX_P HELX_P7  AA7 TYR A 199 ? LYS A 206 ? TYR A 190 LYS A 197 1 ? 8  
HELX_P HELX_P8  AA8 SER A 219 ? CYS A 224 ? SER A 210 CYS A 215 1 ? 6  
HELX_P HELX_P9  AA9 CYS A 224 ? GLY A 239 ? CYS A 215 GLY A 230 1 ? 16 
HELX_P HELX_P10 AB1 ASP A 252 ? ALA A 256 ? ASP A 243 ALA A 247 5 ? 5  
HELX_P HELX_P11 AB2 ASN A 260 ? GLY A 280 ? ASN A 251 GLY A 271 1 ? 21 
HELX_P HELX_P12 AB3 GLU A 298 ? TYR A 312 ? GLU A 289 TYR A 303 1 ? 15 
HELX_P HELX_P13 AB4 THR A 323 ? GLN A 333 ? THR A 314 GLN A 324 1 ? 11 
HELX_P HELX_P14 AB5 GLY A 342 ? ASN A 348 ? GLY A 333 ASN A 339 1 ? 7  
HELX_P HELX_P15 AB6 ASP A 350 ? ASN A 358 ? ASP A 341 ASN A 349 1 ? 9  
HELX_P HELX_P16 AB7 ASN A 365 ? PHE A 369 ? ASN A 356 PHE A 360 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 ? 
# 
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 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 TYR A 25  ? MET A 27  ? TYR A 16  MET A 18  
AA1 2 PHE A 30  ? LEU A 32  ? PHE A 21  LEU A 23  
AA2 1 VAL A 36  ? LEU A 38  ? VAL A 27  LEU A 29  
AA2 2 PHE A 68  ? MET A 75  ? PHE A 59  MET A 66  
AA2 3 VAL A 111 ? TRP A 117 ? VAL A 102 TRP A 108 
AA2 4 GLY A 190 ? GLY A 195 ? GLY A 181 GLY A 186 
AA2 5 VAL A 243 ? VAL A 247 ? VAL A 234 VAL A 238 
AA2 6 TYR A 285 ? THR A 289 ? TYR A 276 THR A 280 
AA2 7 PHE A 316 ? SER A 319 ? PHE A 307 SER A 310 
AA2 8 LEU A 338 ? TYR A 341 ? LEU A 329 TYR A 332 
AA2 9 VAL A 36  ? LEU A 38  ? VAL A 27  LEU A 29  
AA3 1 ILE A 135 ? SER A 136 ? ILE A 126 SER A 127 
AA3 2 ARG A 162 ? ALA A 163 ? ARG A 153 ALA A 154 
AA4 1 ILE A 148 ? LEU A 149 ? ILE A 139 LEU A 140 
AA4 2 HIS A 155 ? GLY A 156 ? HIS A 146 GLY A 147 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N TYR A 25  ? N TYR A 16  O LEU A 32  ? O LEU A 23  
AA2 1 2 N LEU A 38  ? N LEU A 29  O PHE A 68  ? O PHE A 59  
AA2 2 3 N THR A 74  ? N THR A 65  O TRP A 117 ? O TRP A 108 
AA2 3 4 N LEU A 116 ? N LEU A 107 O GLU A 192 ? O GLU A 183 
AA2 4 5 N ILE A 193 ? N ILE A 184 O ARG A 246 ? O ARG A 237 
AA2 5 6 N VAL A 245 ? N VAL A 236 O HIS A 287 ? O HIS A 278 
AA2 6 7 N LEU A 286 ? N LEU A 277 O ILE A 317 ? O ILE A 308 
AA2 7 8 N CYS A 318 ? N CYS A 309 O SER A 340 ? O SER A 331 
AA2 8 9 O VAL A 339 ? O VAL A 330 N VAL A 37  ? N VAL A 28  
AA3 1 2 N SER A 136 ? N SER A 127 O ARG A 162 ? O ARG A 153 
AA4 1 2 N ILE A 148 ? N ILE A 139 O GLY A 156 ? O GLY A 147 
# 
_pdbx_entry_details.entry_id                   8QNX 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 O   A HOH 530 ? ? O A HOH 693 ? ? 2.03 
2  1 O   A HOH 851 ? ? O A HOH 948 ? ? 2.05 
3  1 ND2 A ASN 251 ? B O A HOH 501 ? ? 2.06 
4  1 OE1 A GLU 261 ? ? O A HOH 502 ? ? 2.09 
5  1 O   A HOH 670 ? ? O A HOH 911 ? ? 2.09 
6  1 O   A HOH 554 ? ? O A HOH 829 ? ? 2.09 
7  1 O   A HOH 716 ? ? O A HOH 919 ? ? 2.11 
8  1 OE1 A GLU 261 ? ? O A HOH 503 ? ? 2.13 
9  1 O   A HOH 855 ? ? O A HOH 866 ? ? 2.14 
10 1 O   A HOH 704 ? ? O A HOH 808 ? ? 2.16 
11 1 OD1 A ASP 232 ? ? O A HOH 504 ? ? 2.17 
12 1 O   A HOH 678 ? ? O A HOH 844 ? ? 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 GLU A 63  ? ? -49.45  151.77 
2 1 ALA A 121 ? ? 59.77   18.42  
3 1 ASP A 341 ? ? -91.71  42.00  
4 1 TYR A 369 ? ? -130.49 -61.04 
# 
_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    A 
_pdbx_validate_planes.auth_seq_id     26 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.100 
_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 963 ? 6.01 . 
2 1 O ? A HOH 964 ? 6.16 . 
3 1 O ? A HOH 965 ? 6.21 . 
4 1 O ? A HOH 966 ? 6.88 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET -8  ? A MET 1   
2  1 Y 1 A ALA -7  ? A ALA 2   
3  1 Y 1 A SER -6  ? A SER 3   
4  1 Y 1 A HIS -5  ? A HIS 4   
5  1 Y 1 A HIS -4  ? A HIS 5   
6  1 Y 1 A HIS -3  ? A HIS 6   
7  1 Y 1 A HIS -2  ? A HIS 7   
8  1 Y 1 A HIS -1  ? A HIS 8   
9  1 Y 1 A HIS 0   ? A HIS 9   
10 1 Y 1 A MET 1   ? A MET 10  
11 1 Y 1 A ALA 2   ? A ALA 11  
12 1 Y 1 A SER 3   ? A SER 12  
13 1 Y 1 A SER 4   ? A SER 13  
14 1 Y 1 A ALA 5   ? A ALA 14  
15 1 Y 1 A GLN 6   ? A GLN 15  
16 1 Y 1 A ASP 7   ? A ASP 16  
17 1 Y 1 A GLY 8   ? A GLY 17  
18 1 Y 1 A ASN 9   ? A ASN 18  
19 1 Y 1 A ARG 286 ? A ARG 295 
20 1 Y 1 A GLY 287 ? A GLY 296 
21 1 Y 1 A GLN 376 ? A GLN 385 
22 1 Y 1 A GLY 377 ? A GLY 386 
23 1 Y 1 A ASN 378 ? A ASN 387 
24 1 Y 1 A GLY 379 ? A GLY 388 
25 1 Y 1 A SER 380 ? A SER 389 
26 1 Y 1 A ASN 381 ? A ASN 390 
27 1 Y 1 A GLY 382 ? A GLY 391 
28 1 Y 1 A PRO 383 ? A PRO 392 
29 1 Y 1 A LEU 384 ? A LEU 393 
30 1 Y 1 A SER 385 ? A SER 394 
31 1 Y 1 A ARG 386 ? A ARG 395 
32 1 Y 1 A LEU 387 ? A LEU 396 
# 
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 
SO4 S      S N N 356 
SO4 O1     O N N 357 
SO4 O2     O N N 358 
SO4 O3     O N N 359 
SO4 O4     O N N 360 
THR N      N N N 361 
THR CA     C N S 362 
THR C      C N N 363 
THR O      O N N 364 
THR CB     C N R 365 
THR OG1    O N N 366 
THR CG2    C N N 367 
THR OXT    O N N 368 
THR H      H N N 369 
THR H2     H N N 370 
THR HA     H N N 371 
THR HB     H N N 372 
THR HG1    H N N 373 
THR HG21   H N N 374 
THR HG22   H N N 375 
THR HG23   H N N 376 
THR HXT    H N N 377 
TRP N      N N N 378 
TRP CA     C N S 379 
TRP C      C N N 380 
TRP O      O N N 381 
TRP CB     C N N 382 
TRP CG     C Y N 383 
TRP CD1    C Y N 384 
TRP CD2    C Y N 385 
TRP NE1    N Y N 386 
TRP CE2    C Y N 387 
TRP CE3    C Y N 388 
TRP CZ2    C Y N 389 
TRP CZ3    C Y N 390 
TRP CH2    C Y N 391 
TRP OXT    O N N 392 
TRP H      H N N 393 
TRP H2     H N N 394 
TRP HA     H N N 395 
TRP HB2    H N N 396 
TRP HB3    H N N 397 
TRP HD1    H N N 398 
TRP HE1    H N N 399 
TRP HE3    H N N 400 
TRP HZ2    H N N 401 
TRP HZ3    H N N 402 
TRP HH2    H N N 403 
TRP HXT    H N N 404 
TYR N      N N N 405 
TYR CA     C N S 406 
TYR C      C N N 407 
TYR O      O N N 408 
TYR CB     C N N 409 
TYR CG     C Y N 410 
TYR CD1    C Y N 411 
TYR CD2    C Y N 412 
TYR CE1    C Y N 413 
TYR CE2    C Y N 414 
TYR CZ     C Y N 415 
TYR OH     O N N 416 
TYR OXT    O N N 417 
TYR H      H N N 418 
TYR H2     H N N 419 
TYR HA     H N N 420 
TYR HB2    H N N 421 
TYR HB3    H N N 422 
TYR HD1    H N N 423 
TYR HD2    H N N 424 
TYR HE1    H N N 425 
TYR HE2    H N N 426 
TYR HH     H N N 427 
TYR HXT    H N N 428 
VAL N      N N N 429 
VAL CA     C N S 430 
VAL C      C N N 431 
VAL O      O N N 432 
VAL CB     C N N 433 
VAL CG1    C N N 434 
VAL CG2    C N N 435 
VAL OXT    O N N 436 
VAL H      H N N 437 
VAL H2     H N N 438 
VAL HA     H N N 439 
VAL HB     H N N 440 
VAL HG11   H N N 441 
VAL HG12   H N N 442 
VAL HG13   H N N 443 
VAL HG21   H N N 444 
VAL HG22   H N N 445 
VAL HG23   H N N 446 
VAL HXT    H N N 447 
WI6 O7N    O N N 448 
WI6 C7N    C N N 449 
WI6 N7N    N N N 450 
WI6 C3N    C N S 451 
WI6 C2N    C N N 452 
WI6 C4N    C N N 453 
WI6 C5N    C N N 454 
WI6 C6N    C N N 455 
WI6 N1N    N N N 456 
WI6 "C1'A" C N R 457 
WI6 "O4'A" O N N 458 
WI6 "C2'A" C N R 459 
WI6 "O2'A" O N N 460 
WI6 "C3'A" C N S 461 
WI6 "O3'A" O N N 462 
WI6 "C4'A" C N R 463 
WI6 "C5'A" C N N 464 
WI6 "O5'A" O N N 465 
WI6 PN     P N N 466 
WI6 O1N    O N N 467 
WI6 O2N    O N N 468 
WI6 O3     O N N 469 
WI6 PA     P N N 470 
WI6 O2P    O N N 471 
WI6 O1     O N N 472 
WI6 "O5'"  O N N 473 
WI6 H7N1   H N N 474 
WI6 H7N2   H N N 475 
WI6 H3N    H N N 476 
WI6 H2N1   H N N 477 
WI6 H2N2   H N N 478 
WI6 H4N    H N N 479 
WI6 H5N    H N N 480 
WI6 H6N1   H N N 481 
WI6 H6N2   H N N 482 
WI6 "H1'A" H N N 483 
WI6 "H2'A" H N N 484 
WI6 HO2A   H N N 485 
WI6 "H3'A" H N N 486 
WI6 HO3A   H N N 487 
WI6 "H4'A" H N N 488 
WI6 "H5'1" H N N 489 
WI6 "H5'2" H N N 490 
WI6 HO2N   H N N 491 
WI6 HO2P   H N N 492 
WI6 "C5'"  C N N 493 
WI6 "C4'"  C N N 494 
WI6 "O4'"  O N N 495 
WI6 "C1'"  C N N 496 
WI6 "C2'"  C N N 497 
WI6 "C3'"  C N N 498 
WI6 N9A    N Y N 499 
WI6 C4A    C Y N 500 
WI6 C5A    C Y N 501 
WI6 N7A    N Y N 502 
WI6 C8A    C Y N 503 
WI6 C6A    C Y N 504 
WI6 N1A    N Y N 505 
WI6 C2A    C Y N 506 
WI6 N3A    N Y N 507 
WI6 "O2'"  O N N 508 
WI6 "O3'"  O N N 509 
WI6 "H5'A" H N N 510 
WI6 "H5'B" H N N 511 
WI6 "H4'"  H N N 512 
WI6 "H1'"  H N N 513 
WI6 "H2'"  H N N 514 
WI6 "H3'"  H N N 515 
WI6 H8A    H N N 516 
WI6 H2A    H N N 517 
WI6 "HO2'" H N N 518 
WI6 "HO3'" H N N 519 
WI6 N6A    N N N 520 
WI6 H6A1   H N N 521 
WI6 H6A2   H N N 522 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
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 
SO4 S      O1     doub N N 344 
SO4 S      O2     doub N N 345 
SO4 S      O3     sing N N 346 
SO4 S      O4     sing N N 347 
THR N      CA     sing N N 348 
THR N      H      sing N N 349 
THR N      H2     sing N N 350 
THR CA     C      sing N N 351 
THR CA     CB     sing N N 352 
THR CA     HA     sing N N 353 
THR C      O      doub N N 354 
THR C      OXT    sing N N 355 
THR CB     OG1    sing N N 356 
THR CB     CG2    sing N N 357 
THR CB     HB     sing N N 358 
THR OG1    HG1    sing N N 359 
THR CG2    HG21   sing N N 360 
THR CG2    HG22   sing N N 361 
THR CG2    HG23   sing N N 362 
THR OXT    HXT    sing N N 363 
TRP N      CA     sing N N 364 
TRP N      H      sing N N 365 
TRP N      H2     sing N N 366 
TRP CA     C      sing N N 367 
TRP CA     CB     sing N N 368 
TRP CA     HA     sing N N 369 
TRP C      O      doub N N 370 
TRP C      OXT    sing N N 371 
TRP CB     CG     sing N N 372 
TRP CB     HB2    sing N N 373 
TRP CB     HB3    sing N N 374 
TRP CG     CD1    doub Y N 375 
TRP CG     CD2    sing Y N 376 
TRP CD1    NE1    sing Y N 377 
TRP CD1    HD1    sing N N 378 
TRP CD2    CE2    doub Y N 379 
TRP CD2    CE3    sing Y N 380 
TRP NE1    CE2    sing Y N 381 
TRP NE1    HE1    sing N N 382 
TRP CE2    CZ2    sing Y N 383 
TRP CE3    CZ3    doub Y N 384 
TRP CE3    HE3    sing N N 385 
TRP CZ2    CH2    doub Y N 386 
TRP CZ2    HZ2    sing N N 387 
TRP CZ3    CH2    sing Y N 388 
TRP CZ3    HZ3    sing N N 389 
TRP CH2    HH2    sing N N 390 
TRP OXT    HXT    sing N N 391 
TYR N      CA     sing N N 392 
TYR N      H      sing N N 393 
TYR N      H2     sing N N 394 
TYR CA     C      sing N N 395 
TYR CA     CB     sing N N 396 
TYR CA     HA     sing N N 397 
TYR C      O      doub N N 398 
TYR C      OXT    sing N N 399 
TYR CB     CG     sing N N 400 
TYR CB     HB2    sing N N 401 
TYR CB     HB3    sing N N 402 
TYR CG     CD1    doub Y N 403 
TYR CG     CD2    sing Y N 404 
TYR CD1    CE1    sing Y N 405 
TYR CD1    HD1    sing N N 406 
TYR CD2    CE2    doub Y N 407 
TYR CD2    HD2    sing N N 408 
TYR CE1    CZ     doub Y N 409 
TYR CE1    HE1    sing N N 410 
TYR CE2    CZ     sing Y N 411 
TYR CE2    HE2    sing N N 412 
TYR CZ     OH     sing N N 413 
TYR OH     HH     sing N N 414 
TYR OXT    HXT    sing N N 415 
VAL N      CA     sing N N 416 
VAL N      H      sing N N 417 
VAL N      H2     sing N N 418 
VAL CA     C      sing N N 419 
VAL CA     CB     sing N N 420 
VAL CA     HA     sing N N 421 
VAL C      O      doub N N 422 
VAL C      OXT    sing N N 423 
VAL CB     CG1    sing N N 424 
VAL CB     CG2    sing N N 425 
VAL CB     HB     sing N N 426 
VAL CG1    HG11   sing N N 427 
VAL CG1    HG12   sing N N 428 
VAL CG1    HG13   sing N N 429 
VAL CG2    HG21   sing N N 430 
VAL CG2    HG22   sing N N 431 
VAL CG2    HG23   sing N N 432 
VAL OXT    HXT    sing N N 433 
WI6 "O3'A" "C3'A" sing N N 434 
WI6 "O2'A" "C2'A" sing N N 435 
WI6 "C3'A" "C4'A" sing N N 436 
WI6 "C3'A" "C2'A" sing N N 437 
WI6 "C4'A" "C5'A" sing N N 438 
WI6 "C4'A" "O4'A" sing N N 439 
WI6 "C2'A" "C1'A" sing N N 440 
WI6 "C1'A" "O4'A" sing N N 441 
WI6 "C1'A" N1N    sing N N 442 
WI6 "C5'A" "O5'A" sing N N 443 
WI6 O7N    C7N    doub N N 444 
WI6 C2N    N1N    sing N N 445 
WI6 C2N    C3N    sing N N 446 
WI6 N1N    C6N    sing N N 447 
WI6 O1N    PN     doub N N 448 
WI6 "O5'A" PN     sing N N 449 
WI6 C7N    C3N    sing N N 450 
WI6 C7N    N7N    sing N N 451 
WI6 PN     O2N    sing N N 452 
WI6 PN     O3     sing N N 453 
WI6 C3N    C4N    sing N N 454 
WI6 C6N    C5N    sing N N 455 
WI6 O2P    PA     doub N N 456 
WI6 C4N    C5N    doub N N 457 
WI6 O3     PA     sing N N 458 
WI6 "O5'"  PA     sing N N 459 
WI6 PA     O1     sing N N 460 
WI6 N7N    H7N1   sing N N 461 
WI6 N7N    H7N2   sing N N 462 
WI6 C3N    H3N    sing N N 463 
WI6 C2N    H2N1   sing N N 464 
WI6 C2N    H2N2   sing N N 465 
WI6 C4N    H4N    sing N N 466 
WI6 C5N    H5N    sing N N 467 
WI6 C6N    H6N1   sing N N 468 
WI6 C6N    H6N2   sing N N 469 
WI6 "C1'A" "H1'A" sing N N 470 
WI6 "C2'A" "H2'A" sing N N 471 
WI6 "O2'A" HO2A   sing N N 472 
WI6 "C3'A" "H3'A" sing N N 473 
WI6 "O3'A" HO3A   sing N N 474 
WI6 "C4'A" "H4'A" sing N N 475 
WI6 "C5'A" "H5'1" sing N N 476 
WI6 "C5'A" "H5'2" sing N N 477 
WI6 O2N    HO2N   sing N N 478 
WI6 O1     HO2P   sing N N 479 
WI6 "O5'"  "C5'"  sing N N 480 
WI6 "C5'"  "C4'"  sing N N 481 
WI6 "C4'"  "O4'"  sing N N 482 
WI6 "O4'"  "C1'"  sing N N 483 
WI6 "C1'"  "C2'"  sing N N 484 
WI6 "C2'"  "C3'"  sing N N 485 
WI6 "C3'"  "C4'"  sing N N 486 
WI6 "C1'"  N9A    sing N N 487 
WI6 N9A    C4A    sing Y N 488 
WI6 C4A    C5A    doub Y N 489 
WI6 C5A    N7A    sing Y N 490 
WI6 N7A    C8A    doub Y N 491 
WI6 C8A    N9A    sing Y N 492 
WI6 C5A    C6A    sing Y N 493 
WI6 C6A    N1A    doub Y N 494 
WI6 N1A    C2A    sing Y N 495 
WI6 C2A    N3A    doub Y N 496 
WI6 N3A    C4A    sing Y N 497 
WI6 "C2'"  "O2'"  sing N N 498 
WI6 "C3'"  "O3'"  sing N N 499 
WI6 "C5'"  "H5'A" sing N N 500 
WI6 "C5'"  "H5'B" sing N N 501 
WI6 "C4'"  "H4'"  sing N N 502 
WI6 "C1'"  "H1'"  sing N N 503 
WI6 "C2'"  "H2'"  sing N N 504 
WI6 "C3'"  "H3'"  sing N N 505 
WI6 C8A    H8A    sing N N 506 
WI6 C2A    H2A    sing N N 507 
WI6 "O2'"  "HO2'" sing N N 508 
WI6 "O3'"  "HO3'" sing N N 509 
WI6 C6A    N6A    sing N N 510 
WI6 N6A    H6A1   sing N N 511 
WI6 N6A    H6A2   sing N N 512 
# 
_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                    8QNX 
_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]   0.011362 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011158 
_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]   0.020243 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
P 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N      . ASN A 1 19  ? 7.763  35.768 0.338  1.00 31.19 ? 10  ASN A N      1 
ATOM   2    C CA     . ASN A 1 19  ? 8.044  35.328 1.713  1.00 23.46 ? 10  ASN A CA     1 
ATOM   3    C C      . ASN A 1 19  ? 9.535  35.597 1.998  1.00 21.26 ? 10  ASN A C      1 
ATOM   4    O O      . ASN A 1 19  ? 10.442 35.039 1.352  1.00 21.45 ? 10  ASN A O      1 
ATOM   5    C CB     . ASN A 1 19  ? 7.677  33.840 1.849  1.00 24.03 ? 10  ASN A CB     1 
ATOM   6    C CG     . ASN A 1 19  ? 7.966  33.270 3.217  1.00 25.90 ? 10  ASN A CG     1 
ATOM   7    O OD1    . ASN A 1 19  ? 8.690  33.875 4.015  1.00 23.42 ? 10  ASN A OD1    1 
ATOM   8    N ND2    . ASN A 1 19  ? 7.434  32.074 3.478  1.00 25.46 ? 10  ASN A ND2    1 
ATOM   9    N N      . PRO A 1 20  ? 9.813  36.513 2.928  1.00 20.29 ? 11  PRO A N      1 
ATOM   10   C CA     . PRO A 1 20  ? 11.217 36.882 3.187  1.00 19.25 ? 11  PRO A CA     1 
ATOM   11   C C      . PRO A 1 20  ? 12.046 35.738 3.781  1.00 18.06 ? 11  PRO A C      1 
ATOM   12   O O      . PRO A 1 20  ? 13.291 35.822 3.765  1.00 17.36 ? 11  PRO A O      1 
ATOM   13   C CB     . PRO A 1 20  ? 11.105 38.047 4.186  1.00 25.63 ? 11  PRO A CB     1 
ATOM   14   C CG     . PRO A 1 20  ? 9.839  37.676 4.958  1.00 25.96 ? 11  PRO A CG     1 
ATOM   15   C CD     . PRO A 1 20  ? 8.881  37.137 3.885  1.00 23.16 ? 11  PRO A CD     1 
ATOM   16   N N      . LEU A 1 21  ? 11.408 34.690 4.313  1.00 17.67 ? 12  LEU A N      1 
ATOM   17   C CA     . LEU A 1 21  ? 12.183 33.511 4.734  1.00 17.53 ? 12  LEU A CA     1 
ATOM   18   C C      . LEU A 1 21  ? 12.851 32.848 3.551  1.00 19.26 ? 12  LEU A C      1 
ATOM   19   O O      . LEU A 1 21  ? 13.784 32.062 3.721  1.00 17.36 ? 12  LEU A O      1 
ATOM   20   C CB     . LEU A 1 21  ? 11.317 32.457 5.435  1.00 19.78 ? 12  LEU A CB     1 
ATOM   21   C CG     . LEU A 1 21  ? 10.936 32.777 6.887  1.00 18.02 ? 12  LEU A CG     1 
ATOM   22   C CD1    . LEU A 1 21  ? 9.990  31.668 7.338  1.00 16.04 ? 12  LEU A CD1    1 
ATOM   23   C CD2    . LEU A 1 21  ? 12.136 32.915 7.810  1.00 18.31 ? 12  LEU A CD2    1 
ATOM   24   N N      . PHE A 1 22  ? 12.392 33.133 2.340  1.00 16.45 ? 13  PHE A N      1 
ATOM   25   C CA     . PHE A 1 22  ? 12.980 32.562 1.130  1.00 16.75 ? 13  PHE A CA     1 
ATOM   26   C C      . PHE A 1 22  ? 13.798 33.549 0.344  1.00 20.11 ? 13  PHE A C      1 
ATOM   27   O O      . PHE A 1 22  ? 14.043 33.345 -0.853 1.00 24.01 ? 13  PHE A O      1 
ATOM   28   C CB     . PHE A 1 22  ? 11.920 31.825 0.292  1.00 15.67 ? 13  PHE A CB     1 
ATOM   29   C CG     . PHE A 1 22  ? 11.465 30.613 1.002  1.00 18.13 ? 13  PHE A CG     1 
ATOM   30   C CD1    . PHE A 1 22  ? 12.193 29.424 0.870  1.00 21.66 ? 13  PHE A CD1    1 
ATOM   31   C CD2    . PHE A 1 22  ? 10.438 30.693 1.919  1.00 18.48 ? 13  PHE A CD2    1 
ATOM   32   C CE1    . PHE A 1 22  ? 11.866 28.315 1.649  1.00 21.86 ? 13  PHE A CE1    1 
ATOM   33   C CE2    . PHE A 1 22  ? 10.084 29.588 2.704  1.00 22.51 ? 13  PHE A CE2    1 
ATOM   34   C CZ     . PHE A 1 22  ? 10.819 28.396 2.570  1.00 20.82 ? 13  PHE A CZ     1 
ATOM   35   N N      . SER A 1 23  ? 14.241 34.574 0.983  1.00 17.54 ? 14  SER A N      1 
ATOM   36   C CA     . SER A 1 23  ? 15.227 35.393 0.313  1.00 17.93 ? 14  SER A CA     1 
ATOM   37   C C      . SER A 1 23  ? 16.617 34.924 0.701  1.00 17.89 ? 14  SER A C      1 
ATOM   38   O O      . SER A 1 23  ? 16.814 34.463 1.833  1.00 17.08 ? 14  SER A O      1 
ATOM   39   C CB     . SER A 1 23  ? 15.027 36.844 0.685  1.00 21.33 ? 14  SER A CB     1 
ATOM   40   O OG     . SER A 1 23  ? 15.134 37.033 2.072  1.00 25.51 ? 14  SER A OG     1 
ATOM   41   N N      . PRO A 1 24  ? 17.581 34.973 -0.226 1.00 14.84 ? 15  PRO A N      1 
ATOM   42   C CA     . PRO A 1 24  ? 18.942 34.515 0.061  1.00 15.49 ? 15  PRO A CA     1 
ATOM   43   C C      . PRO A 1 24  ? 19.640 35.377 1.104  1.00 17.12 ? 15  PRO A C      1 
ATOM   44   O O      . PRO A 1 24  ? 19.273 36.522 1.407  1.00 17.77 ? 15  PRO A O      1 
ATOM   45   C CB     . PRO A 1 24  ? 19.641 34.640 -1.306 1.00 18.67 ? 15  PRO A CB     1 
ATOM   46   C CG     . PRO A 1 24  ? 18.825 35.693 -2.030 1.00 21.97 ? 15  PRO A CG     1 
ATOM   47   C CD     . PRO A 1 24  ? 17.410 35.347 -1.646 1.00 21.10 ? 15  PRO A CD     1 
ATOM   48   N N      . TYR A 1 25  ? 20.641 34.772 1.718  1.00 15.73 ? 16  TYR A N      1 
ATOM   49   C CA     . TYR A 1 25  ? 21.401 35.451 2.742  1.00 13.14 ? 16  TYR A CA     1 
ATOM   50   C C      . TYR A 1 25  ? 22.838 34.966 2.718  1.00 15.39 ? 16  TYR A C      1 
ATOM   51   O O      . TYR A 1 25  ? 23.108 33.756 2.625  1.00 16.17 ? 16  TYR A O      1 
ATOM   52   C CB     . TYR A 1 25  ? 20.796 35.132 4.144  1.00 15.96 ? 16  TYR A CB     1 
ATOM   53   C CG     . TYR A 1 25  ? 21.467 35.952 5.204  1.00 13.70 ? 16  TYR A CG     1 
ATOM   54   C CD1    . TYR A 1 25  ? 21.197 37.313 5.320  1.00 16.01 ? 16  TYR A CD1    1 
ATOM   55   C CD2    . TYR A 1 25  ? 22.443 35.396 6.014  1.00 14.65 ? 16  TYR A CD2    1 
ATOM   56   C CE1    . TYR A 1 25  ? 21.845 38.109 6.287  1.00 13.17 ? 16  TYR A CE1    1 
ATOM   57   C CE2    . TYR A 1 25  ? 23.114 36.170 6.931  1.00 15.40 ? 16  TYR A CE2    1 
ATOM   58   C CZ     . TYR A 1 25  ? 22.828 37.514 7.058  1.00 14.39 ? 16  TYR A CZ     1 
ATOM   59   O OH     . TYR A 1 25  ? 23.515 38.249 7.991  1.00 16.38 ? 16  TYR A OH     1 
ATOM   60   N N      . LYS A 1 26  ? 23.783 35.898 2.844  1.00 16.41 ? 17  LYS A N      1 
ATOM   61   C CA     . LYS A 1 26  ? 25.197 35.553 2.849  1.00 17.43 ? 17  LYS A CA     1 
ATOM   62   C C      . LYS A 1 26  ? 25.650 35.475 4.299  1.00 16.66 ? 17  LYS A C      1 
ATOM   63   O O      . LYS A 1 26  ? 25.753 36.496 4.984  1.00 19.94 ? 17  LYS A O      1 
ATOM   64   C CB     . LYS A 1 26  ? 26.007 36.582 2.051  1.00 20.62 ? 17  LYS A CB     1 
ATOM   65   C CG     . LYS A 1 26  ? 27.447 36.171 1.880  1.00 27.14 ? 17  LYS A CG     1 
ATOM   66   C CD     . LYS A 1 26  ? 28.157 37.004 0.822  1.00 39.17 ? 17  LYS A CD     1 
ATOM   67   C CE     . LYS A 1 26  ? 29.594 36.497 0.632  1.00 39.57 ? 17  LYS A CE     1 
ATOM   68   N NZ     . LYS A 1 26  ? 29.514 35.077 0.192  1.00 43.36 ? 17  LYS A NZ     1 
ATOM   69   N N      . MET A 1 27  ? 25.824 34.261 4.798  1.00 16.65 ? 18  MET A N      1 
ATOM   70   C CA     . MET A 1 27  ? 26.350 34.018 6.150  1.00 16.94 ? 18  MET A CA     1 
ATOM   71   C C      . MET A 1 27  ? 27.846 33.851 5.978  1.00 19.23 ? 18  MET A C      1 
ATOM   72   O O      . MET A 1 27  ? 28.351 32.725 5.832  1.00 20.40 ? 18  MET A O      1 
ATOM   73   C CB     . MET A 1 27  ? 25.781 32.734 6.694  1.00 17.43 ? 18  MET A CB     1 
ATOM   74   C CG     . MET A 1 27  ? 26.066 32.517 8.178  1.00 19.02 ? 18  MET A CG     1 
ATOM   75   S SD     . MET A 1 27  ? 25.061 31.171 8.852  1.00 20.82 ? 18  MET A SD     1 
ATOM   76   C CE     . MET A 1 27  ? 25.765 29.729 7.907  1.00 20.62 ? 18  MET A CE     1 
ATOM   77   N N      . GLY A 1 28  ? 28.503 35.010 5.771  1.00 27.28 ? 19  GLY A N      1 
ATOM   78   C CA     . GLY A 1 28  ? 29.935 35.127 5.532  1.00 26.70 ? 19  GLY A CA     1 
ATOM   79   C C      . GLY A 1 28  ? 30.293 34.394 4.280  1.00 17.95 ? 19  GLY A C      1 
ATOM   80   O O      . GLY A 1 28  ? 29.849 34.812 3.211  1.00 29.28 ? 19  GLY A O      1 
ATOM   81   N N      . LYS A 1 29  ? 31.049 33.280 4.364  1.00 23.01 ? 20  LYS A N      1 
ATOM   82   C CA     . LYS A 1 29  ? 31.406 32.642 3.094  1.00 20.35 ? 20  LYS A CA     1 
ATOM   83   C C      . LYS A 1 29  ? 30.295 31.794 2.505  1.00 16.62 ? 20  LYS A C      1 
ATOM   84   O O      . LYS A 1 29  ? 30.369 31.455 1.304  1.00 20.97 ? 20  LYS A O      1 
ATOM   85   C CB     . LYS A 1 29  ? 32.729 31.843 3.167  1.00 28.59 ? 20  LYS A CB     1 
ATOM   86   N N      . PHE A 1 30  ? 29.224 31.537 3.230  1.00 16.03 ? 21  PHE A N      1 
ATOM   87   C CA     . PHE A 1 30  ? 28.197 30.614 2.772  1.00 16.51 ? 21  PHE A CA     1 
ATOM   88   C C      . PHE A 1 30  ? 27.015 31.364 2.172  1.00 15.31 ? 21  PHE A C      1 
ATOM   89   O O      . PHE A 1 30  ? 26.422 32.245 2.798  1.00 17.46 ? 21  PHE A O      1 
ATOM   90   C CB     . PHE A 1 30  ? 27.740 29.761 3.955  1.00 18.23 ? 21  PHE A CB     1 
ATOM   91   C CG     . PHE A 1 30  ? 28.912 29.122 4.700  1.00 19.83 ? 21  PHE A CG     1 
ATOM   92   C CD1    . PHE A 1 30  ? 29.629 28.105 4.088  1.00 21.21 ? 21  PHE A CD1    1 
ATOM   93   C CD2    . PHE A 1 30  ? 29.358 29.604 5.936  1.00 18.21 ? 21  PHE A CD2    1 
ATOM   94   C CE1    . PHE A 1 30  ? 30.745 27.528 4.757  1.00 19.40 ? 21  PHE A CE1    1 
ATOM   95   C CE2    . PHE A 1 30  ? 30.458 29.029 6.557  1.00 21.19 ? 21  PHE A CE2    1 
ATOM   96   C CZ     . PHE A 1 30  ? 31.133 28.002 5.956  1.00 22.40 ? 21  PHE A CZ     1 
ATOM   97   N N      . ASN A 1 31  ? 26.656 31.008 0.962  1.00 13.30 ? 22  ASN A N      1 
ATOM   98   C CA     . ASN A 1 31  ? 25.501 31.593 0.308  1.00 13.88 ? 22  ASN A CA     1 
ATOM   99   C C      . ASN A 1 31  ? 24.278 30.724 0.581  1.00 15.49 ? 22  ASN A C      1 
ATOM   100  O O      . ASN A 1 31  ? 24.116 29.642 -0.006 1.00 19.83 ? 22  ASN A O      1 
ATOM   101  C CB     . ASN A 1 31  ? 25.799 31.640 -1.191 1.00 14.62 ? 22  ASN A CB     1 
ATOM   102  C CG     . ASN A 1 31  ? 27.067 32.445 -1.493 1.00 19.09 ? 22  ASN A CG     1 
ATOM   103  O OD1    . ASN A 1 31  ? 27.174 33.606 -1.134 1.00 19.85 ? 22  ASN A OD1    1 
ATOM   104  N ND2    . ASN A 1 31  ? 28.025 31.826 -2.160 1.00 19.88 ? 22  ASN A ND2    1 
ATOM   105  N N      . LEU A 1 32  ? 23.418 31.179 1.493  1.00 13.77 ? 23  LEU A N      1 
ATOM   106  C CA     . LEU A 1 32  ? 22.218 30.433 1.842  1.00 14.88 ? 23  LEU A CA     1 
ATOM   107  C C      . LEU A 1 32  ? 21.074 30.854 0.932  1.00 13.85 ? 23  LEU A C      1 
ATOM   108  O O      . LEU A 1 32  ? 20.964 32.037 0.545  1.00 15.06 ? 23  LEU A O      1 
ATOM   109  C CB     . LEU A 1 32  ? 21.815 30.696 3.298  1.00 14.01 ? 23  LEU A CB     1 
ATOM   110  C CG     . LEU A 1 32  ? 22.904 30.361 4.292  1.00 12.13 ? 23  LEU A CG     1 
ATOM   111  C CD1    . LEU A 1 32  ? 22.365 30.575 5.723  1.00 13.93 ? 23  LEU A CD1    1 
ATOM   112  C CD2    . LEU A 1 32  ? 23.401 28.912 4.149  1.00 15.37 ? 23  LEU A CD2    1 
ATOM   113  N N      . SER A 1 33  ? 20.217 29.896 0.604  1.00 14.56 ? 24  SER A N      1 
ATOM   114  C CA     A SER A 1 33  ? 19.092 30.168 -0.290 0.56 14.70 ? 24  SER A CA     1 
ATOM   115  C CA     B SER A 1 33  ? 19.099 30.178 -0.293 0.44 14.71 ? 24  SER A CA     1 
ATOM   116  C C      . SER A 1 33  ? 17.840 30.554 0.460  1.00 16.96 ? 24  SER A C      1 
ATOM   117  O O      . SER A 1 33  ? 16.888 31.075 -0.158 1.00 16.48 ? 24  SER A O      1 
ATOM   118  C CB     A SER A 1 33  ? 18.778 28.923 -1.126 0.56 14.49 ? 24  SER A CB     1 
ATOM   119  C CB     B SER A 1 33  ? 18.792 28.956 -1.168 0.44 14.58 ? 24  SER A CB     1 
ATOM   120  O OG     A SER A 1 33  ? 19.854 28.693 -2.000 0.56 22.42 ? 24  SER A OG     1 
ATOM   121  O OG     B SER A 1 33  ? 18.335 27.886 -0.369 0.44 12.99 ? 24  SER A OG     1 
ATOM   122  N N      . HIS A 1 34  ? 17.793 30.293 1.774  1.00 13.47 ? 25  HIS A N      1 
ATOM   123  C CA     . HIS A 1 34  ? 16.628 30.591 2.566  1.00 13.16 ? 25  HIS A CA     1 
ATOM   124  C C      . HIS A 1 34  ? 17.108 30.676 4.003  1.00 12.42 ? 25  HIS A C      1 
ATOM   125  O O      . HIS A 1 34  ? 18.246 30.326 4.312  1.00 13.83 ? 25  HIS A O      1 
ATOM   126  C CB     . HIS A 1 34  ? 15.519 29.560 2.331  1.00 11.93 ? 25  HIS A CB     1 
ATOM   127  C CG     . HIS A 1 34  ? 15.875 28.196 2.796  1.00 12.39 ? 25  HIS A CG     1 
ATOM   128  N ND1    . HIS A 1 34  ? 15.900 27.853 4.140  1.00 12.65 ? 25  HIS A ND1    1 
ATOM   129  C CD2    . HIS A 1 34  ? 16.256 27.095 2.104  1.00 13.81 ? 25  HIS A CD2    1 
ATOM   130  C CE1    . HIS A 1 34  ? 16.297 26.599 4.247  1.00 11.95 ? 25  HIS A CE1    1 
ATOM   131  N NE2    . HIS A 1 34  ? 16.507 26.102 3.023  1.00 12.02 ? 25  HIS A NE2    1 
ATOM   132  N N      . ARG A 1 35  ? 16.209 31.097 4.874  1.00 12.82 ? 26  ARG A N      1 
ATOM   133  C CA     . ARG A 1 35  ? 16.562 31.504 6.225  1.00 12.21 ? 26  ARG A CA     1 
ATOM   134  C C      . ARG A 1 35  ? 16.041 30.541 7.261  1.00 13.44 ? 26  ARG A C      1 
ATOM   135  O O      . ARG A 1 35  ? 16.139 30.858 8.451  1.00 13.29 ? 26  ARG A O      1 
ATOM   136  C CB     . ARG A 1 35  ? 16.085 32.929 6.460  1.00 13.83 ? 26  ARG A CB     1 
ATOM   137  C CG     . ARG A 1 35  ? 16.801 33.896 5.440  1.00 16.22 ? 26  ARG A CG     1 
ATOM   138  C CD     . ARG A 1 35  ? 16.172 35.116 5.366  1.00 21.92 ? 26  ARG A CD     1 
ATOM   139  N NE     . ARG A 1 35  ? 16.882 35.960 4.398  1.00 18.01 ? 26  ARG A NE     1 
ATOM   140  C CZ     . ARG A 1 35  ? 17.454 37.097 4.744  1.00 17.10 ? 26  ARG A CZ     1 
ATOM   141  N NH1    . ARG A 1 35  ? 17.705 37.391 6.007  1.00 14.78 ? 26  ARG A NH1    1 
ATOM   142  N NH2    . ARG A 1 35  ? 17.716 38.000 3.810  1.00 16.03 ? 26  ARG A NH2    1 
ATOM   143  N N      . VAL A 1 36  ? 15.511 29.368 6.866  1.00 12.28 ? 27  VAL A N      1 
ATOM   144  C CA     . VAL A 1 36  ? 14.984 28.406 7.837  1.00 12.94 ? 27  VAL A CA     1 
ATOM   145  C C      . VAL A 1 36  ? 16.143 27.506 8.217  1.00 12.81 ? 27  VAL A C      1 
ATOM   146  O O      . VAL A 1 36  ? 16.674 26.783 7.362  1.00 12.17 ? 27  VAL A O      1 
ATOM   147  C CB     . VAL A 1 36  ? 13.845 27.573 7.208  1.00 14.00 ? 27  VAL A CB     1 
ATOM   148  C CG1    . VAL A 1 36  ? 13.316 26.532 8.182  1.00 14.68 ? 27  VAL A CG1    1 
ATOM   149  C CG2    . VAL A 1 36  ? 12.705 28.512 6.735  1.00 14.80 ? 27  VAL A CG2    1 
ATOM   150  N N      . VAL A 1 37  ? 16.496 27.470 9.514  1.00 10.60 ? 28  VAL A N      1 
ATOM   151  C CA     . VAL A 1 37  ? 17.665 26.744 9.997  1.00 10.20 ? 28  VAL A CA     1 
ATOM   152  C C      . VAL A 1 37  ? 17.201 25.549 10.839 1.00 10.99 ? 28  VAL A C      1 
ATOM   153  O O      . VAL A 1 37  ? 16.270 25.686 11.640 1.00 11.22 ? 28  VAL A O      1 
ATOM   154  C CB     . VAL A 1 37  ? 18.545 27.694 10.840 1.00 10.40 ? 28  VAL A CB     1 
ATOM   155  C CG1    . VAL A 1 37  ? 19.730 26.948 11.434 1.00 10.84 ? 28  VAL A CG1    1 
ATOM   156  C CG2    . VAL A 1 37  ? 19.026 28.880 9.963  1.00 12.23 ? 28  VAL A CG2    1 
ATOM   157  N N      . LEU A 1 38  ? 17.864 24.412 10.712 1.00 9.79  ? 29  LEU A N      1 
ATOM   158  C CA     . LEU A 1 38  ? 17.649 23.309 11.661 1.00 10.13 ? 29  LEU A CA     1 
ATOM   159  C C      . LEU A 1 38  ? 18.389 23.566 12.956 1.00 9.62  ? 29  LEU A C      1 
ATOM   160  O O      . LEU A 1 38  ? 19.622 23.656 12.979 1.00 11.00 ? 29  LEU A O      1 
ATOM   161  C CB     . LEU A 1 38  ? 18.139 21.987 11.044 1.00 9.71  ? 29  LEU A CB     1 
ATOM   162  C CG     . LEU A 1 38  ? 18.227 20.822 12.024 1.00 11.38 ? 29  LEU A CG     1 
ATOM   163  C CD1    . LEU A 1 38  ? 16.835 20.418 12.524 1.00 13.47 ? 29  LEU A CD1    1 
ATOM   164  C CD2    . LEU A 1 38  ? 18.914 19.634 11.375 1.00 12.46 ? 29  LEU A CD2    1 
ATOM   165  N N      . ALA A 1 39  ? 17.652 23.791 14.027 1.00 10.36 ? 30  ALA A N      1 
ATOM   166  C CA     . ALA A 1 39  ? 18.278 23.988 15.343 1.00 9.49  ? 30  ALA A CA     1 
ATOM   167  C C      . ALA A 1 39  ? 18.936 22.702 15.819 1.00 10.83 ? 30  ALA A C      1 
ATOM   168  O O      . ALA A 1 39  ? 18.504 21.602 15.482 1.00 11.58 ? 30  ALA A O      1 
ATOM   169  C CB     . ALA A 1 39  ? 17.190 24.349 16.336 1.00 10.18 ? 30  ALA A CB     1 
ATOM   170  N N      . PRO A 1 40  ? 19.977 22.829 16.639 1.00 9.79  ? 31  PRO A N      1 
ATOM   171  C CA     . PRO A 1 40  ? 20.683 21.644 17.153 1.00 10.15 ? 31  PRO A CA     1 
ATOM   172  C C      . PRO A 1 40  ? 19.771 20.866 18.099 1.00 10.14 ? 31  PRO A C      1 
ATOM   173  O O      . PRO A 1 40  ? 19.193 21.453 19.035 1.00 10.57 ? 31  PRO A O      1 
ATOM   174  C CB     . PRO A 1 40  ? 21.857 22.242 17.938 1.00 9.99  ? 31  PRO A CB     1 
ATOM   175  C CG     . PRO A 1 40  ? 21.358 23.666 18.311 1.00 10.98 ? 31  PRO A CG     1 
ATOM   176  C CD     . PRO A 1 40  ? 20.522 24.106 17.148 1.00 8.50  ? 31  PRO A CD     1 
ATOM   177  N N      . MET A 1 41  ? 19.669 19.556 17.888 1.00 9.81  ? 32  MET A N      1 
ATOM   178  C CA     . MET A 1 41  ? 18.827 18.739 18.759 1.00 9.63  ? 32  MET A CA     1 
ATOM   179  C C      . MET A 1 41  ? 19.448 17.387 19.038 1.00 9.94  ? 32  MET A C      1 
ATOM   180  O O      . MET A 1 41  ? 19.588 16.571 18.136 1.00 11.60 ? 32  MET A O      1 
ATOM   181  C CB     . MET A 1 41  ? 17.417 18.523 18.218 1.00 12.79 ? 32  MET A CB     1 
ATOM   182  C CG     . MET A 1 41  ? 16.603 19.839 18.197 1.00 13.52 ? 32  MET A CG     1 
ATOM   183  S SD     . MET A 1 41  ? 14.989 19.505 17.507 1.00 14.90 ? 32  MET A SD     1 
ATOM   184  C CE     . MET A 1 41  ? 15.486 19.348 15.742 1.00 15.10 ? 32  MET A CE     1 
ATOM   185  N N      . THR A 1 42  ? 19.729 17.172 20.325 1.00 9.92  ? 33  THR A N      1 
ATOM   186  C CA     . THR A 1 42  ? 20.130 15.863 20.845 1.00 10.32 ? 33  THR A CA     1 
ATOM   187  C C      . THR A 1 42  ? 19.032 14.849 20.626 1.00 12.13 ? 33  THR A C      1 
ATOM   188  O O      . THR A 1 42  ? 17.897 15.056 21.072 1.00 11.25 ? 33  THR A O      1 
ATOM   189  C CB     . THR A 1 42  ? 20.398 16.035 22.332 1.00 11.06 ? 33  THR A CB     1 
ATOM   190  O OG1    . THR A 1 42  ? 21.552 16.871 22.488 1.00 12.90 ? 33  THR A OG1    1 
ATOM   191  C CG2    . THR A 1 42  ? 20.657 14.733 23.044 1.00 11.63 ? 33  THR A CG2    1 
ATOM   192  N N      . ARG A 1 43  ? 19.388 13.732 19.983 1.00 10.60 ? 34  ARG A N      1 
ATOM   193  C CA     . ARG A 1 43  ? 18.419 12.651 19.712 1.00 10.48 ? 34  ARG A CA     1 
ATOM   194  C C      . ARG A 1 43  ? 18.896 11.282 20.187 1.00 10.46 ? 34  ARG A C      1 
ATOM   195  O O      . ARG A 1 43  ? 18.074 10.348 20.247 1.00 11.38 ? 34  ARG A O      1 
ATOM   196  C CB     . ARG A 1 43  ? 18.079 12.546 18.217 1.00 10.44 ? 34  ARG A CB     1 
ATOM   197  C CG     . ARG A 1 43  ? 17.565 13.901 17.652 1.00 11.80 ? 34  ARG A CG     1 
ATOM   198  C CD     . ARG A 1 43  ? 16.269 14.419 18.258 1.00 11.31 ? 34  ARG A CD     1 
ATOM   199  N NE     . ARG A 1 43  ? 15.213 13.439 18.329 1.00 10.91 ? 34  ARG A NE     1 
ATOM   200  C CZ     . ARG A 1 43  ? 14.492 13.067 17.291 1.00 10.88 ? 34  ARG A CZ     1 
ATOM   201  N NH1    . ARG A 1 43  ? 14.623 13.659 16.112 1.00 12.56 ? 34  ARG A NH1    1 
ATOM   202  N NH2    . ARG A 1 43  ? 13.562 12.119 17.465 1.00 12.74 ? 34  ARG A NH2    1 
ATOM   203  N N      . CYS A 1 44  ? 20.139 11.127 20.583 1.00 9.99  ? 35  CYS A N      1 
ATOM   204  C CA     . CYS A 1 44  ? 20.587 9.921  21.293 1.00 11.48 ? 35  CYS A CA     1 
ATOM   205  C C      . CYS A 1 44  ? 20.555 8.661  20.417 1.00 11.81 ? 35  CYS A C      1 
ATOM   206  O O      . CYS A 1 44  ? 20.417 7.548  20.930 1.00 11.70 ? 35  CYS A O      1 
ATOM   207  C CB     . CYS A 1 44  ? 19.812 9.669  22.617 1.00 10.38 ? 35  CYS A CB     1 
ATOM   208  S SG     . CYS A 1 44  ? 19.804 11.125 23.674 1.00 12.78 ? 35  CYS A SG     1 
ATOM   209  N N      . ARG A 1 45  ? 20.817 8.816  19.117 1.00 10.99 ? 36  ARG A N      1 
ATOM   210  C CA     . ARG A 1 45  ? 20.925 7.646  18.230 1.00 12.25 ? 36  ARG A CA     1 
ATOM   211  C C      . ARG A 1 45  ? 22.374 7.283  17.918 1.00 12.25 ? 36  ARG A C      1 
ATOM   212  O O      . ARG A 1 45  ? 22.612 6.306  17.204 1.00 12.57 ? 36  ARG A O      1 
ATOM   213  C CB     . ARG A 1 45  ? 20.138 7.863  16.897 1.00 11.67 ? 36  ARG A CB     1 
ATOM   214  C CG     . ARG A 1 45  ? 18.690 7.334  16.946 1.00 11.83 ? 36  ARG A CG     1 
ATOM   215  C CD     . ARG A 1 45  ? 17.798 8.251  17.790 1.00 12.07 ? 36  ARG A CD     1 
ATOM   216  N NE     . ARG A 1 45  ? 16.414 7.796  17.743 1.00 11.12 ? 36  ARG A NE     1 
ATOM   217  C CZ     . ARG A 1 45  ? 15.423 8.479  18.292 1.00 12.21 ? 36  ARG A CZ     1 
ATOM   218  N NH1    . ARG A 1 45  ? 15.659 9.592  19.001 1.00 12.29 ? 36  ARG A NH1    1 
ATOM   219  N NH2    . ARG A 1 45  ? 14.159 8.051  18.124 1.00 12.18 ? 36  ARG A NH2    1 
ATOM   220  N N      . ALA A 1 46  ? 23.359 8.049  18.432 1.00 12.13 ? 37  ALA A N      1 
ATOM   221  C CA     . ALA A 1 46  ? 24.768 7.850  18.081 1.00 11.10 ? 37  ALA A CA     1 
ATOM   222  C C      . ALA A 1 46  ? 25.370 6.859  19.068 1.00 13.27 ? 37  ALA A C      1 
ATOM   223  O O      . ALA A 1 46  ? 26.099 7.218  20.016 1.00 13.10 ? 37  ALA A O      1 
ATOM   224  C CB     . ALA A 1 46  ? 25.540 9.165  18.139 1.00 12.38 ? 37  ALA A CB     1 
ATOM   225  N N      . LEU A 1 47  ? 25.015 5.596  18.847 1.00 11.16 ? 38  LEU A N      1 
ATOM   226  C CA     . LEU A 1 47  ? 25.379 4.528  19.794 1.00 12.61 ? 38  LEU A CA     1 
ATOM   227  C C      . LEU A 1 47  ? 26.880 4.524  20.097 1.00 14.51 ? 38  LEU A C      1 
ATOM   228  O O      . LEU A 1 47  ? 27.724 4.638  19.199 1.00 15.56 ? 38  LEU A O      1 
ATOM   229  C CB     . LEU A 1 47  ? 24.923 3.187  19.225 1.00 13.34 ? 38  LEU A CB     1 
ATOM   230  C CG     . LEU A 1 47  ? 23.444 3.111  18.867 1.00 13.48 ? 38  LEU A CG     1 
ATOM   231  C CD1    . LEU A 1 47  ? 23.152 1.653  18.496 1.00 16.35 ? 38  LEU A CD1    1 
ATOM   232  C CD2    . LEU A 1 47  ? 22.536 3.500  20.087 1.00 14.39 ? 38  LEU A CD2    1 
ATOM   233  N N      . ASN A 1 48  ? 27.191 4.471  21.402 1.00 14.93 ? 39  ASN A N      1 
ATOM   234  C CA     . ASN A 1 48  ? 28.571 4.498  21.902 1.00 18.22 ? 39  ASN A CA     1 
ATOM   235  C C      . ASN A 1 48  ? 29.350 5.716  21.480 1.00 14.17 ? 39  ASN A C      1 
ATOM   236  O O      . ASN A 1 48  ? 30.589 5.712  21.396 1.00 15.70 ? 39  ASN A O      1 
ATOM   237  C CB     . ASN A 1 48  ? 29.333 3.227  21.600 1.00 23.26 ? 39  ASN A CB     1 
ATOM   238  C CG     . ASN A 1 48  ? 28.846 2.069  22.436 1.00 21.79 ? 39  ASN A CG     1 
ATOM   239  O OD1    . ASN A 1 48  ? 28.368 2.164  23.647 1.00 24.81 ? 39  ASN A OD1    1 
ATOM   240  N ND2    . ASN A 1 48  ? 28.947 0.958  21.820 1.00 17.24 ? 39  ASN A ND2    1 
ATOM   241  N N      . ASN A 1 49  ? 28.603 6.779  21.292 1.00 12.53 ? 40  ASN A N      1 
ATOM   242  C CA     . ASN A 1 49  ? 29.153 8.088  20.922 1.00 11.44 ? 40  ASN A CA     1 
ATOM   243  C C      . ASN A 1 49  ? 29.739 8.118  19.533 1.00 12.98 ? 40  ASN A C      1 
ATOM   244  O O      . ASN A 1 49  ? 30.439 9.077  19.161 1.00 13.21 ? 40  ASN A O      1 
ATOM   245  C CB     . ASN A 1 49  ? 30.181 8.641  21.928 1.00 12.07 ? 40  ASN A CB     1 
ATOM   246  C CG     . ASN A 1 49  ? 29.713 8.519  23.378 1.00 12.02 ? 40  ASN A CG     1 
ATOM   247  O OD1    . ASN A 1 49  ? 30.460 7.986  24.204 1.00 17.08 ? 40  ASN A OD1    1 
ATOM   248  N ND2    . ASN A 1 49  ? 28.536 9.037  23.722 1.00 13.12 ? 40  ASN A ND2    1 
ATOM   249  N N      . ILE A 1 50  ? 29.427 7.127  18.725 1.00 12.11 ? 41  ILE A N      1 
ATOM   250  C CA     . ILE A 1 50  ? 29.900 7.072  17.352 1.00 14.30 ? 41  ILE A CA     1 
ATOM   251  C C      . ILE A 1 50  ? 28.738 7.450  16.448 1.00 13.75 ? 41  ILE A C      1 
ATOM   252  O O      . ILE A 1 50  ? 27.665 6.851  16.562 1.00 13.20 ? 41  ILE A O      1 
ATOM   253  C CB     . ILE A 1 50  ? 30.407 5.664  17.018 1.00 13.62 ? 41  ILE A CB     1 
ATOM   254  C CG1    . ILE A 1 50  ? 31.524 5.277  18.001 1.00 18.26 ? 41  ILE A CG1    1 
ATOM   255  C CG2    . ILE A 1 50  ? 30.865 5.601  15.556 1.00 18.24 ? 41  ILE A CG2    1 
ATOM   256  C CD1    . ILE A 1 50  ? 31.849 3.782  17.944 1.00 24.65 ? 41  ILE A CD1    1 
ATOM   257  N N      . PRO A 1 51  ? 28.900 8.433  15.561 1.00 12.39 ? 42  PRO A N      1 
ATOM   258  C CA     . PRO A 1 51  ? 27.840 8.724  14.598 1.00 12.66 ? 42  PRO A CA     1 
ATOM   259  C C      . PRO A 1 51  ? 27.483 7.452  13.828 1.00 16.23 ? 42  PRO A C      1 
ATOM   260  O O      . PRO A 1 51  ? 28.345 6.644  13.494 1.00 17.49 ? 42  PRO A O      1 
ATOM   261  C CB     . PRO A 1 51  ? 28.472 9.789  13.710 1.00 14.17 ? 42  PRO A CB     1 
ATOM   262  C CG     . PRO A 1 51  ? 29.530 10.412 14.540 1.00 15.39 ? 42  PRO A CG     1 
ATOM   263  C CD     . PRO A 1 51  ? 30.053 9.325  15.419 1.00 12.85 ? 42  PRO A CD     1 
ATOM   264  N N      . GLN A 1 52  ? 26.198 7.246  13.604 1.00 13.98 ? 43  GLN A N      1 
ATOM   265  C CA     . GLN A 1 52  ? 25.668 6.028  12.999 1.00 15.13 ? 43  GLN A CA     1 
ATOM   266  C C      . GLN A 1 52  ? 25.054 6.359  11.657 1.00 15.55 ? 43  GLN A C      1 
ATOM   267  O O      . GLN A 1 52  ? 24.659 7.493  11.391 1.00 15.11 ? 43  GLN A O      1 
ATOM   268  C CB     . GLN A 1 52  ? 24.578 5.430  13.905 1.00 15.31 ? 43  GLN A CB     1 
ATOM   269  C CG     . GLN A 1 52  ? 25.094 5.034  15.278 1.00 16.08 ? 43  GLN A CG     1 
ATOM   270  C CD     . GLN A 1 52  ? 25.967 3.819  15.282 1.00 20.43 ? 43  GLN A CD     1 
ATOM   271  O OE1    . GLN A 1 52  ? 25.688 2.833  14.568 1.00 25.17 ? 43  GLN A OE1    1 
ATOM   272  N NE2    . GLN A 1 52  ? 27.064 3.853  16.052 1.00 17.38 ? 43  GLN A NE2    1 
ATOM   273  N N      . ALA A 1 53  ? 24.885 5.321  10.822 1.00 15.93 ? 44  ALA A N      1 
ATOM   274  C CA     . ALA A 1 53  ? 24.173 5.523  9.563  1.00 15.85 ? 44  ALA A CA     1 
ATOM   275  C C      . ALA A 1 53  ? 22.811 6.201  9.735  1.00 14.79 ? 44  ALA A C      1 
ATOM   276  O O      . ALA A 1 53  ? 22.377 6.977  8.863  1.00 16.10 ? 44  ALA A O      1 
ATOM   277  C CB     . ALA A 1 53  ? 23.976 4.159  8.870  1.00 17.96 ? 44  ALA A CB     1 
ATOM   278  N N      . ALA A 1 54  ? 22.095 5.899  10.818 1.00 14.61 ? 45  ALA A N      1 
ATOM   279  C CA     . ALA A 1 54  ? 20.791 6.530  11.016 1.00 14.44 ? 45  ALA A CA     1 
ATOM   280  C C      . ALA A 1 54  ? 20.895 8.054  11.040 1.00 14.26 ? 45  ALA A C      1 
ATOM   281  O O      . ALA A 1 54  ? 19.999 8.734  10.514 1.00 13.95 ? 45  ALA A O      1 
ATOM   282  C CB     . ALA A 1 54  ? 20.166 6.031  12.317 1.00 16.28 ? 45  ALA A CB     1 
ATOM   283  N N      . LEU A 1 55  ? 21.992 8.615  11.601 1.00 13.20 ? 46  LEU A N      1 
ATOM   284  C CA     . LEU A 1 55  ? 22.153 10.079 11.597 1.00 13.04 ? 46  LEU A CA     1 
ATOM   285  C C      . LEU A 1 55  ? 22.276 10.603 10.182 1.00 13.45 ? 46  LEU A C      1 
ATOM   286  O O      . LEU A 1 55  ? 21.765 11.679 9.861  1.00 11.99 ? 46  LEU A O      1 
ATOM   287  C CB     . LEU A 1 55  ? 23.389 10.485 12.384 1.00 12.52 ? 46  LEU A CB     1 
ATOM   288  C CG     . LEU A 1 55  ? 23.234 10.640 13.904 1.00 12.02 ? 46  LEU A CG     1 
ATOM   289  C CD1    . LEU A 1 55  ? 22.933 9.283  14.584 1.00 13.47 ? 46  LEU A CD1    1 
ATOM   290  C CD2    . LEU A 1 55  ? 24.525 11.292 14.483 1.00 13.34 ? 46  LEU A CD2    1 
ATOM   291  N N      . GLY A 1 56  ? 22.953 9.847  9.300  1.00 13.14 ? 47  GLY A N      1 
ATOM   292  C CA     . GLY A 1 56  ? 23.062 10.273 7.915  1.00 13.69 ? 47  GLY A CA     1 
ATOM   293  C C      . GLY A 1 56  ? 21.699 10.361 7.255  1.00 11.84 ? 47  GLY A C      1 
ATOM   294  O O      . GLY A 1 56  ? 21.390 11.329 6.571  1.00 14.23 ? 47  GLY A O      1 
ATOM   295  N N      . GLU A 1 57  ? 20.854 9.355  7.476  1.00 13.26 ? 48  GLU A N      1 
ATOM   296  C CA     . GLU A 1 57  ? 19.499 9.402  6.932  1.00 14.69 ? 48  GLU A CA     1 
ATOM   297  C C      . GLU A 1 57  ? 18.691 10.562 7.492  1.00 11.79 ? 48  GLU A C      1 
ATOM   298  O O      . GLU A 1 57  ? 18.027 11.286 6.746  1.00 14.52 ? 48  GLU A O      1 
ATOM   299  C CB     . GLU A 1 57  ? 18.783 8.087  7.241  1.00 17.39 ? 48  GLU A CB     1 
ATOM   300  C CG     . GLU A 1 57  ? 17.415 8.024  6.529  1.00 21.46 ? 48  GLU A CG     1 
ATOM   301  C CD     . GLU A 1 57  ? 16.742 6.621  6.584  1.00 63.02 ? 48  GLU A CD     1 
ATOM   302  O OE1    . GLU A 1 57  ? 17.023 5.831  7.524  1.00 59.69 ? 48  GLU A OE1    1 
ATOM   303  O OE2    . GLU A 1 57  ? 15.935 6.307  5.672  1.00 58.22 ? 48  GLU A OE2    1 
ATOM   304  N N      . TYR A 1 58  ? 18.816 10.806 8.805  1.00 12.71 ? 49  TYR A N      1 
ATOM   305  C CA     . TYR A 1 58  ? 18.083 11.890 9.459  1.00 11.07 ? 49  TYR A CA     1 
ATOM   306  C C      . TYR A 1 58  ? 18.457 13.266 8.934  1.00 11.41 ? 49  TYR A C      1 
ATOM   307  O O      . TYR A 1 58  ? 17.577 14.087 8.615  1.00 11.58 ? 49  TYR A O      1 
ATOM   308  C CB     . TYR A 1 58  ? 18.365 11.783 10.935 1.00 12.65 ? 49  TYR A CB     1 
ATOM   309  C CG     . TYR A 1 58  ? 17.836 12.903 11.789 1.00 12.30 ? 49  TYR A CG     1 
ATOM   310  C CD1    . TYR A 1 58  ? 16.517 12.929 12.229 1.00 12.45 ? 49  TYR A CD1    1 
ATOM   311  C CD2    . TYR A 1 58  ? 18.694 13.892 12.233 1.00 12.27 ? 49  TYR A CD2    1 
ATOM   312  C CE1    . TYR A 1 58  ? 16.055 13.923 13.092 1.00 11.85 ? 49  TYR A CE1    1 
ATOM   313  C CE2    . TYR A 1 58  ? 18.247 14.889 13.098 1.00 13.60 ? 49  TYR A CE2    1 
ATOM   314  C CZ     . TYR A 1 58  ? 16.930 14.851 13.535 1.00 12.66 ? 49  TYR A CZ     1 
ATOM   315  O OH     . TYR A 1 58  ? 16.506 15.807 14.471 1.00 15.15 ? 49  TYR A OH     1 
ATOM   316  N N      . TYR A 1 59  ? 19.764 13.550 8.871  1.00 10.81 ? 50  TYR A N      1 
ATOM   317  C CA     . TYR A 1 59  ? 20.173 14.865 8.381  1.00 11.13 ? 50  TYR A CA     1 
ATOM   318  C C      . TYR A 1 59  ? 19.910 15.008 6.882  1.00 10.99 ? 50  TYR A C      1 
ATOM   319  O O      . TYR A 1 59  ? 19.538 16.098 6.431  1.00 12.77 ? 50  TYR A O      1 
ATOM   320  C CB     . TYR A 1 59  ? 21.638 15.148 8.744  1.00 12.17 ? 50  TYR A CB     1 
ATOM   321  C CG     . TYR A 1 59  ? 21.859 15.412 10.212 1.00 11.39 ? 50  TYR A CG     1 
ATOM   322  C CD1    . TYR A 1 59  ? 21.353 16.571 10.813 1.00 12.42 ? 50  TYR A CD1    1 
ATOM   323  C CD2    . TYR A 1 59  ? 22.549 14.508 10.988 1.00 11.67 ? 50  TYR A CD2    1 
ATOM   324  C CE1    . TYR A 1 59  ? 21.538 16.804 12.184 1.00 12.59 ? 50  TYR A CE1    1 
ATOM   325  C CE2    . TYR A 1 59  ? 22.744 14.742 12.373 1.00 12.06 ? 50  TYR A CE2    1 
ATOM   326  C CZ     . TYR A 1 59  ? 22.187 15.867 12.928 1.00 12.63 ? 50  TYR A CZ     1 
ATOM   327  O OH     . TYR A 1 59  ? 22.429 16.084 14.264 1.00 14.35 ? 50  TYR A OH     1 
ATOM   328  N N      . GLU A 1 60  ? 20.096 13.913 6.091  1.00 11.57 ? 51  GLU A N      1 
ATOM   329  C CA     . GLU A 1 60  ? 19.827 14.014 4.660  1.00 12.91 ? 51  GLU A CA     1 
ATOM   330  C C      . GLU A 1 60  ? 18.355 14.349 4.420  1.00 12.21 ? 51  GLU A C      1 
ATOM   331  O O      . GLU A 1 60  ? 18.034 15.169 3.539  1.00 14.98 ? 51  GLU A O      1 
ATOM   332  C CB     . GLU A 1 60  ? 20.215 12.695 3.994  1.00 13.95 ? 51  GLU A CB     1 
ATOM   333  C CG     . GLU A 1 60  ? 19.938 12.661 2.471  1.00 17.34 ? 51  GLU A CG     1 
ATOM   334  C CD     . GLU A 1 60  ? 20.275 11.277 1.897  1.00 30.82 ? 51  GLU A CD     1 
ATOM   335  O OE1    . GLU A 1 60  ? 19.796 10.258 2.464  1.00 31.96 ? 51  GLU A OE1    1 
ATOM   336  O OE2    . GLU A 1 60  ? 20.959 11.201 0.847  1.00 37.19 ? 51  GLU A OE2    1 
ATOM   337  N N      . GLN A 1 61  ? 17.443 13.756 5.202  1.00 13.22 ? 52  GLN A N      1 
ATOM   338  C CA     . GLN A 1 61  ? 16.021 14.056 5.021  1.00 11.80 ? 52  GLN A CA     1 
ATOM   339  C C      . GLN A 1 61  ? 15.707 15.515 5.207  1.00 12.64 ? 52  GLN A C      1 
ATOM   340  O O      . GLN A 1 61  ? 14.789 16.043 4.550  1.00 15.04 ? 52  GLN A O      1 
ATOM   341  C CB     . GLN A 1 61  ? 15.213 13.301 6.068  1.00 12.98 ? 52  GLN A CB     1 
ATOM   342  C CG     . GLN A 1 61  ? 15.054 11.804 5.766  1.00 13.19 ? 52  GLN A CG     1 
ATOM   343  C CD     . GLN A 1 61  ? 14.179 11.077 6.786  1.00 14.06 ? 52  GLN A CD     1 
ATOM   344  O OE1    . GLN A 1 61  ? 13.932 11.551 7.917  1.00 15.15 ? 52  GLN A OE1    1 
ATOM   345  N NE2    . GLN A 1 61  ? 13.688 9.921  6.390  1.00 18.13 ? 52  GLN A NE2    1 
ATOM   346  N N      . ARG A 1 62  ? 16.438 16.185 6.096  1.00 12.36 ? 53  ARG A N      1 
ATOM   347  C CA     . ARG A 1 62  ? 16.141 17.552 6.466  1.00 13.27 ? 53  ARG A CA     1 
ATOM   348  C C      . ARG A 1 62  ? 16.923 18.573 5.656  1.00 12.54 ? 53  ARG A C      1 
ATOM   349  O O      . ARG A 1 62  ? 16.543 19.751 5.617  1.00 14.57 ? 53  ARG A O      1 
ATOM   350  C CB     . ARG A 1 62  ? 16.360 17.714 7.981  1.00 13.85 ? 53  ARG A CB     1 
ATOM   351  C CG     . ARG A 1 62  ? 15.209 16.974 8.734  1.00 12.76 ? 53  ARG A CG     1 
ATOM   352  C CD     . ARG A 1 62  ? 15.557 16.531 10.153 1.00 12.53 ? 53  ARG A CD     1 
ATOM   353  N NE     . ARG A 1 62  ? 14.377 15.823 10.685 1.00 11.51 ? 53  ARG A NE     1 
ATOM   354  C CZ     . ARG A 1 62  ? 13.980 14.639 10.257 1.00 12.09 ? 53  ARG A CZ     1 
ATOM   355  N NH1    . ARG A 1 62  ? 14.769 13.891 9.475  1.00 12.74 ? 53  ARG A NH1    1 
ATOM   356  N NH2    . ARG A 1 62  ? 12.777 14.170 10.626 1.00 13.66 ? 53  ARG A NH2    1 
ATOM   357  N N      . ALA A 1 63  ? 17.989 18.139 4.984  1.00 11.71 ? 54  ALA A N      1 
ATOM   358  C CA     . ALA A 1 63  ? 18.838 19.036 4.198  1.00 12.58 ? 54  ALA A CA     1 
ATOM   359  C C      . ALA A 1 63  ? 18.122 19.524 2.947  1.00 14.45 ? 54  ALA A C      1 
ATOM   360  O O      . ALA A 1 63  ? 17.393 18.783 2.285  1.00 16.73 ? 54  ALA A O      1 
ATOM   361  C CB     . ALA A 1 63  ? 20.075 18.254 3.764  1.00 14.02 ? 54  ALA A CB     1 
ATOM   362  N N      . THR A 1 64  ? 18.377 20.781 2.601  1.00 13.06 ? 55  THR A N      1 
ATOM   363  C CA     . THR A 1 64  ? 17.871 21.393 1.383  1.00 12.79 ? 55  THR A CA     1 
ATOM   364  C C      . THR A 1 64  ? 18.995 22.162 0.725  1.00 13.41 ? 55  THR A C      1 
ATOM   365  O O      . THR A 1 64  ? 19.977 22.543 1.356  1.00 13.99 ? 55  THR A O      1 
ATOM   366  C CB     . THR A 1 64  ? 16.706 22.370 1.683  1.00 13.55 ? 55  THR A CB     1 
ATOM   367  O OG1    . THR A 1 64  ? 17.112 23.327 2.682  1.00 14.29 ? 55  THR A OG1    1 
ATOM   368  C CG2    . THR A 1 64  ? 15.473 21.613 2.214  1.00 13.54 ? 55  THR A CG2    1 
ATOM   369  N N      . ALA A 1 65  ? 18.842 22.385 -0.588 1.00 14.22 ? 56  ALA A N      1 
ATOM   370  C CA     . ALA A 1 65  ? 19.825 23.134 -1.336 1.00 12.85 ? 56  ALA A CA     1 
ATOM   371  C C      . ALA A 1 65  ? 19.904 24.570 -0.806 1.00 14.92 ? 56  ALA A C      1 
ATOM   372  O O      . ALA A 1 65  ? 18.891 25.288 -0.761 1.00 16.83 ? 56  ALA A O      1 
ATOM   373  C CB     . ALA A 1 65  ? 19.420 23.120 -2.826 1.00 15.81 ? 56  ALA A CB     1 
ATOM   374  N N      . GLY A 1 66  ? 21.093 24.969 -0.383 1.00 13.59 ? 57  GLY A N      1 
ATOM   375  C CA     . GLY A 1 66  ? 21.276 26.275 0.196  1.00 14.13 ? 57  GLY A CA     1 
ATOM   376  C C      . GLY A 1 66  ? 20.746 26.438 1.609  1.00 14.14 ? 57  GLY A C      1 
ATOM   377  O O      . GLY A 1 66  ? 20.670 27.566 2.076  1.00 15.47 ? 57  GLY A O      1 
ATOM   378  N N      . GLY A 1 67  ? 20.319 25.367 2.273  1.00 12.38 ? 58  GLY A N      1 
ATOM   379  C CA     . GLY A 1 67  ? 19.811 25.502 3.631  1.00 10.89 ? 58  GLY A CA     1 
ATOM   380  C C      . GLY A 1 67  ? 20.901 25.197 4.642  1.00 13.95 ? 58  GLY A C      1 
ATOM   381  O O      . GLY A 1 67  ? 21.809 24.408 4.386  1.00 14.81 ? 58  GLY A O      1 
ATOM   382  N N      . PHE A 1 68  ? 20.766 25.773 5.835  1.00 12.08 ? 59  PHE A N      1 
ATOM   383  C CA     . PHE A 1 68  ? 21.754 25.598 6.897  1.00 10.83 ? 59  PHE A CA     1 
ATOM   384  C C      . PHE A 1 68  ? 21.230 24.682 8.011  1.00 10.86 ? 59  PHE A C      1 
ATOM   385  O O      . PHE A 1 68  ? 20.094 24.844 8.484  1.00 11.07 ? 59  PHE A O      1 
ATOM   386  C CB     . PHE A 1 68  ? 22.028 26.986 7.467  1.00 10.94 ? 59  PHE A CB     1 
ATOM   387  C CG     . PHE A 1 68  ? 23.045 27.013 8.623  1.00 11.91 ? 59  PHE A CG     1 
ATOM   388  C CD1    . PHE A 1 68  ? 24.149 26.197 8.617  1.00 12.66 ? 59  PHE A CD1    1 
ATOM   389  C CD2    . PHE A 1 68  ? 22.848 27.869 9.723  1.00 12.67 ? 59  PHE A CD2    1 
ATOM   390  C CE1    . PHE A 1 68  ? 25.028 26.225 9.669  1.00 12.40 ? 59  PHE A CE1    1 
ATOM   391  C CE2    . PHE A 1 68  ? 23.764 27.881 10.802 1.00 12.06 ? 59  PHE A CE2    1 
ATOM   392  C CZ     . PHE A 1 68  ? 24.842 27.065 10.735 1.00 11.79 ? 59  PHE A CZ     1 
ATOM   393  N N      . LEU A 1 69  ? 22.051 23.716 8.387  1.00 10.54 ? 60  LEU A N      1 
ATOM   394  C CA     . LEU A 1 69  ? 21.727 22.741 9.438  1.00 9.83  ? 60  LEU A CA     1 
ATOM   395  C C      . LEU A 1 69  ? 22.754 22.854 10.540 1.00 11.36 ? 60  LEU A C      1 
ATOM   396  O O      . LEU A 1 69  ? 23.944 22.980 10.274 1.00 11.63 ? 60  LEU A O      1 
ATOM   397  C CB     . LEU A 1 69  ? 21.854 21.289 8.893  1.00 11.29 ? 60  LEU A CB     1 
ATOM   398  C CG     . LEU A 1 69  ? 21.023 20.932 7.686  1.00 13.75 ? 60  LEU A CG     1 
ATOM   399  C CD1    . LEU A 1 69  ? 21.266 19.440 7.390  1.00 16.70 ? 60  LEU A CD1    1 
ATOM   400  C CD2    . LEU A 1 69  ? 19.571 21.213 7.884  1.00 18.21 ? 60  LEU A CD2    1 
ATOM   401  N N      . ILE A 1 70  ? 22.327 22.729 11.800 1.00 10.10 ? 61  ILE A N      1 
ATOM   402  C CA     . ILE A 1 70  ? 23.253 22.634 12.915 1.00 9.90  ? 61  ILE A CA     1 
ATOM   403  C C      . ILE A 1 70  ? 23.018 21.257 13.548 1.00 10.56 ? 61  ILE A C      1 
ATOM   404  O O      . ILE A 1 70  ? 21.866 20.883 13.801 1.00 11.38 ? 61  ILE A O      1 
ATOM   405  C CB     . ILE A 1 70  ? 22.951 23.739 13.940 1.00 9.74  ? 61  ILE A CB     1 
ATOM   406  C CG1    . ILE A 1 70  ? 23.022 25.099 13.243 1.00 9.97  ? 61  ILE A CG1    1 
ATOM   407  C CG2    . ILE A 1 70  ? 24.014 23.677 15.082 1.00 10.37 ? 61  ILE A CG2    1 
ATOM   408  C CD1    . ILE A 1 70  ? 22.354 26.190 14.074 1.00 12.33 ? 61  ILE A CD1    1 
ATOM   409  N N      . THR A 1 71  ? 24.084 20.505 13.776 1.00 10.26 ? 62  THR A N      1 
ATOM   410  C CA     . THR A 1 71  ? 23.914 19.180 14.376 1.00 10.25 ? 62  THR A CA     1 
ATOM   411  C C      . THR A 1 71  ? 23.511 19.261 15.851 1.00 9.96  ? 62  THR A C      1 
ATOM   412  O O      . THR A 1 71  ? 23.712 20.243 16.563 1.00 11.62 ? 62  THR A O      1 
ATOM   413  C CB     . THR A 1 71  ? 25.180 18.323 14.375 1.00 11.29 ? 62  THR A CB     1 
ATOM   414  O OG1    . THR A 1 71  ? 26.160 18.842 15.296 1.00 10.55 ? 62  THR A OG1    1 
ATOM   415  C CG2    . THR A 1 71  ? 25.771 18.200 12.942 1.00 13.42 ? 62  THR A CG2    1 
ATOM   416  N N      . GLU A 1 72  ? 23.041 18.104 16.311 1.00 10.48 ? 63  GLU A N      1 
ATOM   417  C CA     . GLU A 1 72  ? 22.916 17.819 17.730 1.00 9.91  ? 63  GLU A CA     1 
ATOM   418  C C      . GLU A 1 72  ? 24.226 18.156 18.445 1.00 11.45 ? 63  GLU A C      1 
ATOM   419  O O      . GLU A 1 72  ? 25.320 18.089 17.870 1.00 10.46 ? 63  GLU A O      1 
ATOM   420  C CB     . GLU A 1 72  ? 22.673 16.316 17.903 1.00 11.03 ? 63  GLU A CB     1 
ATOM   421  C CG     . GLU A 1 72  ? 23.787 15.402 17.388 1.00 11.98 ? 63  GLU A CG     1 
ATOM   422  C CD     . GLU A 1 72  ? 23.225 14.079 16.882 1.00 16.00 ? 63  GLU A CD     1 
ATOM   423  O OE1    . GLU A 1 72  ? 22.812 13.997 15.696 1.00 16.90 ? 63  GLU A OE1    1 
ATOM   424  O OE2    . GLU A 1 72  ? 23.199 13.100 17.638 1.00 15.80 ? 63  GLU A OE2    1 
ATOM   425  N N      . GLY A 1 73  ? 24.141 18.511 19.726 1.00 10.04 ? 64  GLY A N      1 
ATOM   426  C CA     . GLY A 1 73  ? 25.356 18.730 20.483 1.00 10.57 ? 64  GLY A CA     1 
ATOM   427  C C      . GLY A 1 73  ? 26.267 17.516 20.414 1.00 9.96  ? 64  GLY A C      1 
ATOM   428  O O      . GLY A 1 73  ? 25.836 16.370 20.525 1.00 10.88 ? 64  GLY A O      1 
ATOM   429  N N      . THR A 1 74  ? 27.563 17.799 20.295 1.00 9.92  ? 65  THR A N      1 
ATOM   430  C CA     . THR A 1 74  ? 28.588 16.785 20.064 1.00 11.06 ? 65  THR A CA     1 
ATOM   431  C C      . THR A 1 74  ? 29.697 16.925 21.101 1.00 10.64 ? 65  THR A C      1 
ATOM   432  O O      . THR A 1 74  ? 30.203 18.031 21.325 1.00 10.99 ? 65  THR A O      1 
ATOM   433  C CB     . THR A 1 74  ? 29.089 16.949 18.605 1.00 10.94 ? 65  THR A CB     1 
ATOM   434  O OG1    . THR A 1 74  ? 27.978 16.715 17.722 1.00 12.50 ? 65  THR A OG1    1 
ATOM   435  C CG2    . THR A 1 74  ? 30.124 15.954 18.226 1.00 11.28 ? 65  THR A CG2    1 
ATOM   436  N N      . MET A 1 75  ? 30.089 15.797 21.689 1.00 11.32 ? 66  MET A N      1 
ATOM   437  C CA     . MET A 1 75  ? 31.049 15.767 22.776 1.00 11.46 ? 66  MET A CA     1 
ATOM   438  C C      . MET A 1 75  ? 32.407 16.292 22.283 1.00 11.07 ? 66  MET A C      1 
ATOM   439  O O      . MET A 1 75  ? 32.880 15.935 21.184 1.00 12.08 ? 66  MET A O      1 
ATOM   440  C CB     . MET A 1 75  ? 31.210 14.274 23.114 1.00 12.93 ? 66  MET A CB     1 
ATOM   441  C CG     . MET A 1 75  ? 30.098 13.777 24.011 1.00 13.46 ? 66  MET A CG     1 
ATOM   442  S SD     . MET A 1 75  ? 30.413 12.005 24.340 1.00 14.18 ? 66  MET A SD     1 
ATOM   443  C CE     . MET A 1 75  ? 31.591 12.050 25.717 1.00 12.42 ? 66  MET A CE     1 
ATOM   444  N N      . ILE A 1 76  ? 33.076 17.080 23.130 1.00 11.33 ? 67  ILE A N      1 
ATOM   445  C CA     . ILE A 1 76  ? 34.431 17.554 22.860 1.00 11.85 ? 67  ILE A CA     1 
ATOM   446  C C      . ILE A 1 76  ? 35.503 16.756 23.595 1.00 11.68 ? 67  ILE A C      1 
ATOM   447  O O      . ILE A 1 76  ? 36.699 17.038 23.407 1.00 13.00 ? 67  ILE A O      1 
ATOM   448  C CB     . ILE A 1 76  ? 34.590 19.037 23.201 1.00 10.26 ? 67  ILE A CB     1 
ATOM   449  C CG1    . ILE A 1 76  ? 34.346 19.279 24.701 1.00 11.16 ? 67  ILE A CG1    1 
ATOM   450  C CG2    . ILE A 1 76  ? 33.596 19.879 22.390 1.00 12.44 ? 67  ILE A CG2    1 
ATOM   451  C CD1    . ILE A 1 76  ? 34.822 20.675 25.143 1.00 13.28 ? 67  ILE A CD1    1 
ATOM   452  N N      . SER A 1 77  ? 35.113 15.812 24.456 1.00 10.96 ? 68  SER A N      1 
ATOM   453  C CA     . SER A 1 77  ? 36.075 15.050 25.252 1.00 13.77 ? 68  SER A CA     1 
ATOM   454  C C      . SER A 1 77  ? 35.332 13.936 25.952 1.00 14.65 ? 68  SER A C      1 
ATOM   455  O O      . SER A 1 77  ? 34.091 13.948 25.997 1.00 12.99 ? 68  SER A O      1 
ATOM   456  C CB     . SER A 1 77  ? 36.684 15.958 26.317 1.00 14.08 ? 68  SER A CB     1 
ATOM   457  O OG     . SER A 1 77  ? 35.700 16.216 27.344 1.00 15.70 ? 68  SER A OG     1 
ATOM   458  N N      . PRO A 1 78  ? 36.042 12.956 26.524 1.00 14.02 ? 69  PRO A N      1 
ATOM   459  C CA     . PRO A 1 78  ? 35.356 11.866 27.229 1.00 14.90 ? 69  PRO A CA     1 
ATOM   460  C C      . PRO A 1 78  ? 34.529 12.284 28.439 1.00 14.83 ? 69  PRO A C      1 
ATOM   461  O O      . PRO A 1 78  ? 33.677 11.485 28.858 1.00 16.47 ? 69  PRO A O      1 
ATOM   462  C CB     . PRO A 1 78  ? 36.519 10.947 27.665 1.00 17.12 ? 69  PRO A CB     1 
ATOM   463  C CG     . PRO A 1 78  ? 37.603 11.240 26.678 1.00 19.20 ? 69  PRO A CG     1 
ATOM   464  C CD     . PRO A 1 78  ? 37.496 12.708 26.376 1.00 16.43 ? 69  PRO A CD     1 
ATOM   465  N N      . THR A 1 79  ? 34.716 13.470 28.996 1.00 13.16 ? 70  THR A N      1 
ATOM   466  C CA     . THR A 1 79  ? 34.028 13.897 30.208 1.00 13.93 ? 70  THR A CA     1 
ATOM   467  C C      . THR A 1 79  ? 32.899 14.867 29.905 1.00 13.70 ? 70  THR A C      1 
ATOM   468  O O      . THR A 1 79  ? 32.265 15.394 30.830 1.00 15.27 ? 70  THR A O      1 
ATOM   469  C CB     . THR A 1 79  ? 35.025 14.499 31.203 1.00 16.74 ? 70  THR A CB     1 
ATOM   470  O OG1    . THR A 1 79  ? 35.870 15.428 30.493 1.00 20.54 ? 70  THR A OG1    1 
ATOM   471  C CG2    . THR A 1 79  ? 35.926 13.422 31.792 1.00 23.07 ? 70  THR A CG2    1 
ATOM   472  N N      . SER A 1 80  ? 32.618 15.125 28.615 1.00 11.28 ? 71  SER A N      1 
ATOM   473  C CA     . SER A 1 80  ? 31.700 16.177 28.232 1.00 11.78 ? 71  SER A CA     1 
ATOM   474  C C      . SER A 1 80  ? 30.214 15.794 28.124 1.00 12.95 ? 71  SER A C      1 
ATOM   475  O O      . SER A 1 80  ? 29.373 16.687 27.837 1.00 12.64 ? 71  SER A O      1 
ATOM   476  C CB     . SER A 1 80  ? 32.177 16.822 26.921 1.00 14.81 ? 71  SER A CB     1 
ATOM   477  O OG     . SER A 1 80  ? 32.121 15.881 25.931 1.00 16.30 ? 71  SER A OG     1 
ATOM   478  N N      . ALA A 1 81  ? 29.846 14.527 28.303 1.00 11.69 ? 72  ALA A N      1 
ATOM   479  C CA     . ALA A 1 81  ? 28.492 14.072 28.056 1.00 12.53 ? 72  ALA A CA     1 
ATOM   480  C C      . ALA A 1 81  ? 27.651 13.945 29.315 1.00 11.50 ? 72  ALA A C      1 
ATOM   481  O O      . ALA A 1 81  ? 28.145 13.580 30.392 1.00 12.45 ? 72  ALA A O      1 
ATOM   482  C CB     . ALA A 1 81  ? 28.504 12.670 27.384 1.00 11.55 ? 72  ALA A CB     1 
ATOM   483  N N      . GLY A 1 82  ? 26.361 14.167 29.127 1.00 10.76 ? 73  GLY A N      1 
ATOM   484  C CA     . GLY A 1 82  ? 25.344 13.990 30.143 1.00 12.16 ? 73  GLY A CA     1 
ATOM   485  C C      . GLY A 1 82  ? 24.039 13.454 29.616 1.00 11.56 ? 73  GLY A C      1 
ATOM   486  O O      . GLY A 1 82  ? 23.011 13.592 30.282 1.00 12.74 ? 73  GLY A O      1 
ATOM   487  N N      . PHE A 1 83  ? 24.084 12.814 28.439 1.00 12.51 ? 74  PHE A N      1 
ATOM   488  C CA     . PHE A 1 83  ? 22.963 12.149 27.770 1.00 11.01 ? 74  PHE A CA     1 
ATOM   489  C C      . PHE A 1 83  ? 23.536 10.882 27.151 1.00 11.61 ? 74  PHE A C      1 
ATOM   490  O O      . PHE A 1 83  ? 24.740 10.811 26.871 1.00 12.54 ? 74  PHE A O      1 
ATOM   491  C CB     . PHE A 1 83  ? 22.367 12.980 26.624 1.00 10.48 ? 74  PHE A CB     1 
ATOM   492  C CG     . PHE A 1 83  ? 21.344 13.972 27.018 1.00 9.86  ? 74  PHE A CG     1 
ATOM   493  C CD1    . PHE A 1 83  ? 21.704 15.159 27.643 1.00 12.26 ? 74  PHE A CD1    1 
ATOM   494  C CD2    . PHE A 1 83  ? 19.996 13.748 26.759 1.00 12.77 ? 74  PHE A CD2    1 
ATOM   495  C CE1    . PHE A 1 83  ? 20.691 16.106 28.017 1.00 12.47 ? 74  PHE A CE1    1 
ATOM   496  C CE2    . PHE A 1 83  ? 19.010 14.693 27.128 1.00 12.76 ? 74  PHE A CE2    1 
ATOM   497  C CZ     . PHE A 1 83  ? 19.387 15.888 27.752 1.00 11.77 ? 74  PHE A CZ     1 
ATOM   498  N N      . PRO A 1 84  ? 22.709 9.849  26.962 1.00 11.58 ? 75  PRO A N      1 
ATOM   499  C CA     . PRO A 1 84  ? 23.204 8.592  26.375 1.00 12.62 ? 75  PRO A CA     1 
ATOM   500  C C      . PRO A 1 84  ? 23.329 8.678  24.860 1.00 11.27 ? 75  PRO A C      1 
ATOM   501  O O      . PRO A 1 84  ? 22.503 9.311  24.191 1.00 11.12 ? 75  PRO A O      1 
ATOM   502  C CB     . PRO A 1 84  ? 22.111 7.578  26.765 1.00 13.08 ? 75  PRO A CB     1 
ATOM   503  C CG     . PRO A 1 84  ? 20.837 8.423  26.774 1.00 14.92 ? 75  PRO A CG     1 
ATOM   504  C CD     . PRO A 1 84  ? 21.262 9.837  27.228 1.00 12.48 ? 75  PRO A CD     1 
ATOM   505  N N      . HIS A 1 85  ? 24.380 8.033  24.330 1.00 10.79 ? 76  HIS A N      1 
ATOM   506  C CA     . HIS A 1 85  ? 24.497 7.808  22.864 1.00 10.32 ? 76  HIS A CA     1 
ATOM   507  C C      . HIS A 1 85  ? 24.427 9.125  22.104 1.00 11.22 ? 76  HIS A C      1 
ATOM   508  O O      . HIS A 1 85  ? 23.776 9.219  21.063 1.00 11.44 ? 76  HIS A O      1 
ATOM   509  C CB     . HIS A 1 85  ? 23.469 6.789  22.407 1.00 13.16 ? 76  HIS A CB     1 
ATOM   510  C CG     . HIS A 1 85  ? 23.560 5.538  23.209 1.00 13.66 ? 76  HIS A CG     1 
ATOM   511  N ND1    . HIS A 1 85  ? 24.721 4.797  23.243 1.00 16.03 ? 76  HIS A ND1    1 
ATOM   512  C CD2    . HIS A 1 85  ? 22.711 4.978  24.104 1.00 20.60 ? 76  HIS A CD2    1 
ATOM   513  C CE1    . HIS A 1 85  ? 24.568 3.799  24.106 1.00 19.68 ? 76  HIS A CE1    1 
ATOM   514  N NE2    . HIS A 1 85  ? 23.350 3.883  24.618 1.00 16.58 ? 76  HIS A NE2    1 
ATOM   515  N N      . VAL A 1 86  ? 25.141 10.127 22.635 1.00 11.32 ? 77  VAL A N      1 
ATOM   516  C CA     . VAL A 1 86  ? 25.340 11.361 21.886 1.00 12.32 ? 77  VAL A CA     1 
ATOM   517  C C      . VAL A 1 86  ? 26.676 11.286 21.165 1.00 13.20 ? 77  VAL A C      1 
ATOM   518  O O      . VAL A 1 86  ? 27.627 10.651 21.641 1.00 12.14 ? 77  VAL A O      1 
ATOM   519  C CB     . VAL A 1 86  ? 25.261 12.578 22.803 1.00 12.89 ? 77  VAL A CB     1 
ATOM   520  C CG1    . VAL A 1 86  ? 23.880 12.616 23.468 1.00 16.44 ? 77  VAL A CG1    1 
ATOM   521  C CG2    . VAL A 1 86  ? 26.308 12.507 23.856 1.00 14.59 ? 77  VAL A CG2    1 
ATOM   522  N N      . PRO A 1 87  ? 26.779 11.857 19.975 1.00 10.07 ? 78  PRO A N      1 
ATOM   523  C CA     . PRO A 1 87  ? 28.017 11.684 19.226 1.00 10.09 ? 78  PRO A CA     1 
ATOM   524  C C      . PRO A 1 87  ? 29.122 12.520 19.835 1.00 11.57 ? 78  PRO A C      1 
ATOM   525  O O      . PRO A 1 87  ? 28.905 13.547 20.486 1.00 13.36 ? 78  PRO A O      1 
ATOM   526  C CB     . PRO A 1 87  ? 27.667 12.221 17.841 1.00 10.52 ? 78  PRO A CB     1 
ATOM   527  C CG     . PRO A 1 87  ? 26.523 13.207 18.073 1.00 9.94  ? 78  PRO A CG     1 
ATOM   528  C CD     . PRO A 1 87  ? 25.774 12.659 19.260 1.00 9.90  ? 78  PRO A CD     1 
ATOM   529  N N      . GLY A 1 88  ? 30.343 12.059 19.575 1.00 12.37 ? 79  GLY A N      1 
ATOM   530  C CA     . GLY A 1 88  ? 31.540 12.840 19.845 1.00 12.10 ? 79  GLY A CA     1 
ATOM   531  C C      . GLY A 1 88  ? 32.234 13.267 18.560 1.00 11.76 ? 79  GLY A C      1 
ATOM   532  O O      . GLY A 1 88  ? 31.925 12.791 17.472 1.00 12.16 ? 79  GLY A O      1 
ATOM   533  N N      . ILE A 1 89  ? 33.179 14.187 18.710 1.00 11.48 ? 80  ILE A N      1 
ATOM   534  C CA     . ILE A 1 89  ? 34.086 14.515 17.613 1.00 10.79 ? 80  ILE A CA     1 
ATOM   535  C C      . ILE A 1 89  ? 35.492 14.688 18.157 1.00 13.26 ? 80  ILE A C      1 
ATOM   536  O O      . ILE A 1 89  ? 36.292 15.449 17.590 1.00 15.39 ? 80  ILE A O      1 
ATOM   537  C CB     . ILE A 1 89  ? 33.578 15.709 16.788 1.00 13.23 ? 80  ILE A CB     1 
ATOM   538  C CG1    . ILE A 1 89  ? 34.238 15.731 15.375 1.00 16.25 ? 80  ILE A CG1    1 
ATOM   539  C CG2    . ILE A 1 89  ? 33.631 17.062 17.548 1.00 13.46 ? 80  ILE A CG2    1 
ATOM   540  C CD1    . ILE A 1 89  ? 33.357 16.340 14.349 1.00 23.94 ? 80  ILE A CD1    1 
ATOM   541  N N      . PHE A 1 90  ? 35.822 13.960 19.211 1.00 13.75 ? 81  PHE A N      1 
ATOM   542  C CA     . PHE A 1 90  ? 37.158 14.021 19.812 1.00 13.24 ? 81  PHE A CA     1 
ATOM   543  C C      . PHE A 1 90  ? 38.047 12.842 19.449 1.00 16.30 ? 81  PHE A C      1 
ATOM   544  O O      . PHE A 1 90  ? 39.218 12.839 19.845 1.00 18.48 ? 81  PHE A O      1 
ATOM   545  C CB     . PHE A 1 90  ? 37.061 14.180 21.353 1.00 14.31 ? 81  PHE A CB     1 
ATOM   546  C CG     . PHE A 1 90  ? 36.307 13.070 22.035 1.00 15.21 ? 81  PHE A CG     1 
ATOM   547  C CD1    . PHE A 1 90  ? 34.928 13.154 22.208 1.00 13.44 ? 81  PHE A CD1    1 
ATOM   548  C CD2    . PHE A 1 90  ? 36.971 11.919 22.541 1.00 15.16 ? 81  PHE A CD2    1 
ATOM   549  C CE1    . PHE A 1 90  ? 34.207 12.135 22.803 1.00 13.49 ? 81  PHE A CE1    1 
ATOM   550  C CE2    . PHE A 1 90  ? 36.257 10.901 23.147 1.00 16.96 ? 81  PHE A CE2    1 
ATOM   551  C CZ     . PHE A 1 90  ? 34.869 11.001 23.292 1.00 14.98 ? 81  PHE A CZ     1 
ATOM   552  N N      . THR A 1 91  ? 37.542 11.843 18.722 1.00 14.28 ? 82  THR A N      1 
ATOM   553  C CA     . THR A 1 91  ? 38.370 10.732 18.248 1.00 15.95 ? 82  THR A CA     1 
ATOM   554  C C      . THR A 1 91  ? 38.371 10.706 16.733 1.00 15.84 ? 82  THR A C      1 
ATOM   555  O O      . THR A 1 91  ? 37.438 11.175 16.077 1.00 15.76 ? 82  THR A O      1 
ATOM   556  C CB     . THR A 1 91  ? 37.878 9.360  18.740 1.00 14.69 ? 82  THR A CB     1 
ATOM   557  O OG1    . THR A 1 91  ? 36.696 8.961  18.056 1.00 16.17 ? 82  THR A OG1    1 
ATOM   558  C CG2    . THR A 1 91  ? 37.654 9.357  20.257 1.00 19.16 ? 82  THR A CG2    1 
ATOM   559  N N      . LYS A 1 92  ? 39.418 10.110 16.170 1.00 17.10 ? 83  LYS A N      1 
ATOM   560  C CA     . LYS A 1 92  ? 39.465 9.998  14.721 1.00 17.24 ? 83  LYS A CA     1 
ATOM   561  C C      . LYS A 1 92  ? 38.449 9.000  14.182 1.00 16.03 ? 83  LYS A C      1 
ATOM   562  O O      . LYS A 1 92  ? 37.985 9.189  13.060 1.00 16.03 ? 83  LYS A O      1 
ATOM   563  C CB     . LYS A 1 92  ? 40.886 9.679  14.237 1.00 21.79 ? 83  LYS A CB     1 
ATOM   564  C CG     . LYS A 1 92  ? 41.937 10.685 14.693 1.00 21.22 ? 83  LYS A CG     1 
ATOM   565  C CD     . LYS A 1 92  ? 41.621 12.120 14.165 1.00 26.92 ? 83  LYS A CD     1 
ATOM   566  C CE     . LYS A 1 92  ? 42.823 13.038 14.358 1.00 27.25 ? 83  LYS A CE     1 
ATOM   567  N NZ     . LYS A 1 92  ? 42.513 14.497 14.070 1.00 25.65 ? 83  LYS A NZ     1 
ATOM   568  N N      . GLU A 1 93  ? 38.055 7.970  14.953 1.00 15.52 ? 84  GLU A N      1 
ATOM   569  C CA     . GLU A 1 93  ? 36.952 7.127  14.513 1.00 15.37 ? 84  GLU A CA     1 
ATOM   570  C C      . GLU A 1 93  ? 35.664 7.938  14.363 1.00 13.97 ? 84  GLU A C      1 
ATOM   571  O O      . GLU A 1 93  ? 34.864 7.714  13.439 1.00 15.84 ? 84  GLU A O      1 
ATOM   572  C CB     . GLU A 1 93  ? 36.752 6.003  15.528 1.00 18.17 ? 84  GLU A CB     1 
ATOM   573  C CG     . GLU A 1 93  ? 35.468 5.250  15.338 1.00 20.09 ? 84  GLU A CG     1 
ATOM   574  C CD     . GLU A 1 93  ? 35.262 4.129  16.361 1.00 36.80 ? 84  GLU A CD     1 
ATOM   575  O OE1    . GLU A 1 93  ? 35.443 4.354  17.584 1.00 33.37 ? 84  GLU A OE1    1 
ATOM   576  O OE2    . GLU A 1 93  ? 34.899 3.017  15.934 1.00 35.50 ? 84  GLU A OE2    1 
ATOM   577  N N      . GLN A 1 94  ? 35.418 8.854  15.301 1.00 13.46 ? 85  GLN A N      1 
ATOM   578  C CA     . GLN A 1 94  ? 34.223 9.670  15.192 1.00 14.13 ? 85  GLN A CA     1 
ATOM   579  C C      . GLN A 1 94  ? 34.315 10.582 13.987 1.00 12.38 ? 85  GLN A C      1 
ATOM   580  O O      . GLN A 1 94  ? 33.309 10.800 13.293 1.00 13.74 ? 85  GLN A O      1 
ATOM   581  C CB     . GLN A 1 94  ? 34.059 10.532 16.455 1.00 14.12 ? 85  GLN A CB     1 
ATOM   582  C CG     . GLN A 1 94  ? 33.616 9.697  17.658 1.00 14.34 ? 85  GLN A CG     1 
ATOM   583  C CD     . GLN A 1 94  ? 33.980 10.375 18.975 1.00 13.99 ? 85  GLN A CD     1 
ATOM   584  O OE1    . GLN A 1 94  ? 34.643 11.409 19.041 1.00 13.13 ? 85  GLN A OE1    1 
ATOM   585  N NE2    . GLN A 1 94  ? 33.565 9.732  20.088 1.00 15.01 ? 85  GLN A NE2    1 
ATOM   586  N N      . VAL A 1 95  ? 35.504 11.132 13.710 1.00 12.72 ? 86  VAL A N      1 
ATOM   587  C CA     . VAL A 1 95  ? 35.688 11.974 12.536 1.00 13.13 ? 86  VAL A CA     1 
ATOM   588  C C      . VAL A 1 95  ? 35.355 11.192 11.260 1.00 14.23 ? 86  VAL A C      1 
ATOM   589  O O      . VAL A 1 95  ? 34.669 11.700 10.351 1.00 14.52 ? 86  VAL A O      1 
ATOM   590  C CB     . VAL A 1 95  ? 37.129 12.507 12.474 1.00 13.04 ? 86  VAL A CB     1 
ATOM   591  C CG1    . VAL A 1 95  ? 37.436 13.153 11.082 1.00 16.43 ? 86  VAL A CG1    1 
ATOM   592  C CG2    . VAL A 1 95  ? 37.402 13.485 13.580 1.00 15.61 ? 86  VAL A CG2    1 
ATOM   593  N N      . ARG A 1 96  ? 35.867 9.947  11.145 1.00 14.30 ? 87  ARG A N      1 
ATOM   594  C CA     . ARG A 1 96  ? 35.594 9.156  9.935  1.00 13.74 ? 87  ARG A CA     1 
ATOM   595  C C      . ARG A 1 96  ? 34.106 8.918  9.763  1.00 14.09 ? 87  ARG A C      1 
ATOM   596  O O      . ARG A 1 96  ? 33.591 8.918  8.618  1.00 15.75 ? 87  ARG A O      1 
ATOM   597  C CB     . ARG A 1 96  ? 36.317 7.794  10.044 1.00 17.87 ? 87  ARG A CB     1 
ATOM   598  C CG     . ARG A 1 96  ? 37.822 7.910  9.926  1.00 23.38 ? 87  ARG A CG     1 
ATOM   599  C CD     . ARG A 1 96  ? 38.452 6.496  9.735  1.00 24.54 ? 87  ARG A CD     1 
ATOM   600  N NE     . ARG A 1 96  ? 38.379 5.668  10.933 1.00 25.39 ? 87  ARG A NE     1 
ATOM   601  C CZ     . ARG A 1 96  ? 39.231 5.721  11.951 1.00 24.11 ? 87  ARG A CZ     1 
ATOM   602  N NH1    . ARG A 1 96  ? 40.219 6.592  11.985 1.00 25.61 ? 87  ARG A NH1    1 
ATOM   603  N NH2    . ARG A 1 96  ? 39.068 4.887  12.971 1.00 26.86 ? 87  ARG A NH2    1 
ATOM   604  N N      . GLU A 1 97  ? 33.388 8.660  10.877 1.00 13.11 ? 88  GLU A N      1 
ATOM   605  C CA     . GLU A 1 97  ? 31.970 8.394  10.710 1.00 11.99 ? 88  GLU A CA     1 
ATOM   606  C C      . GLU A 1 97  ? 31.171 9.670  10.423 1.00 15.48 ? 88  GLU A C      1 
ATOM   607  O O      . GLU A 1 97  ? 30.209 9.650  9.645  1.00 13.83 ? 88  GLU A O      1 
ATOM   608  C CB     . GLU A 1 97  ? 31.438 7.669  11.937 1.00 14.53 ? 88  GLU A CB     1 
ATOM   609  C CG     . GLU A 1 97  ? 32.104 6.261  12.129 1.00 17.30 ? 88  GLU A CG     1 
ATOM   610  C CD     . GLU A 1 97  ? 32.145 5.435  10.840 1.00 21.53 ? 88  GLU A CD     1 
ATOM   611  O OE1    . GLU A 1 97  ? 31.077 5.187  10.277 1.00 22.20 ? 88  GLU A OE1    1 
ATOM   612  O OE2    . GLU A 1 97  ? 33.259 5.013  10.431 1.00 28.63 ? 88  GLU A OE2    1 
ATOM   613  N N      . TRP A 1 98  ? 31.535 10.785 11.067 1.00 12.51 ? 89  TRP A N      1 
ATOM   614  C CA     . TRP A 1 98  ? 30.915 12.056 10.708 1.00 12.17 ? 89  TRP A CA     1 
ATOM   615  C C      . TRP A 1 98  ? 31.124 12.419 9.252  1.00 13.16 ? 89  TRP A C      1 
ATOM   616  O O      . TRP A 1 98  ? 30.228 12.976 8.651  1.00 13.34 ? 89  TRP A O      1 
ATOM   617  C CB     . TRP A 1 98  ? 31.465 13.191 11.569 1.00 12.27 ? 89  TRP A CB     1 
ATOM   618  C CG     . TRP A 1 98  ? 30.769 13.411 12.886 1.00 11.60 ? 89  TRP A CG     1 
ATOM   619  C CD1    . TRP A 1 98  ? 31.369 13.356 14.108 1.00 11.49 ? 89  TRP A CD1    1 
ATOM   620  C CD2    . TRP A 1 98  ? 29.414 13.807 13.099 1.00 11.65 ? 89  TRP A CD2    1 
ATOM   621  N NE1    . TRP A 1 98  ? 30.460 13.696 15.084 1.00 12.05 ? 89  TRP A NE1    1 
ATOM   622  C CE2    . TRP A 1 98  ? 29.264 13.986 14.495 1.00 11.64 ? 89  TRP A CE2    1 
ATOM   623  C CE3    . TRP A 1 98  ? 28.305 14.018 12.246 1.00 12.49 ? 89  TRP A CE3    1 
ATOM   624  C CZ2    . TRP A 1 98  ? 28.046 14.377 15.071 1.00 12.76 ? 89  TRP A CZ2    1 
ATOM   625  C CZ3    . TRP A 1 98  ? 27.082 14.432 12.824 1.00 13.25 ? 89  TRP A CZ3    1 
ATOM   626  C CH2    . TRP A 1 98  ? 26.957 14.584 14.225 1.00 13.12 ? 89  TRP A CH2    1 
ATOM   627  N N      . LYS A 1 99  ? 32.305 12.138 8.679  1.00 12.16 ? 90  LYS A N      1 
ATOM   628  C CA     . LYS A 1 99  ? 32.541 12.467 7.268  1.00 13.56 ? 90  LYS A CA     1 
ATOM   629  C C      . LYS A 1 99  ? 31.472 11.851 6.367  1.00 15.08 ? 90  LYS A C      1 
ATOM   630  O O      . LYS A 1 99  ? 31.011 12.510 5.427  1.00 14.60 ? 90  LYS A O      1 
ATOM   631  C CB     . LYS A 1 99  ? 33.940 11.999 6.877  1.00 16.14 ? 90  LYS A CB     1 
ATOM   632  C CG     . LYS A 1 99  ? 34.182 12.366 5.423  1.00 20.11 ? 90  LYS A CG     1 
ATOM   633  C CD     . LYS A 1 99  ? 35.625 12.070 5.041  1.00 28.87 ? 90  LYS A CD     1 
ATOM   634  C CE     . LYS A 1 99  ? 35.928 12.504 3.588  1.00 43.64 ? 90  LYS A CE     1 
ATOM   635  N NZ     . LYS A 1 99  ? 34.940 11.887 2.643  1.00 41.40 ? 90  LYS A NZ     1 
ATOM   636  N N      . LYS A 1 100 ? 31.011 10.630 6.663  1.00 15.17 ? 91  LYS A N      1 
ATOM   637  C CA     . LYS A 1 100 ? 30.011 10.032 5.801  1.00 15.94 ? 91  LYS A CA     1 
ATOM   638  C C      . LYS A 1 100 ? 28.698 10.798 5.854  1.00 16.21 ? 91  LYS A C      1 
ATOM   639  O O      . LYS A 1 100 ? 27.975 10.888 4.851  1.00 17.52 ? 91  LYS A O      1 
ATOM   640  C CB     . LYS A 1 100 ? 29.753 8.607  6.227  1.00 18.03 ? 91  LYS A CB     1 
ATOM   641  C CG     . LYS A 1 100 ? 30.972 7.760  6.116  1.00 20.23 ? 91  LYS A CG     1 
ATOM   642  C CD     . LYS A 1 100 ? 30.728 6.395  6.747  1.00 25.58 ? 91  LYS A CD     1 
ATOM   643  C CE     . LYS A 1 100 ? 31.964 5.558  6.717  1.00 30.07 ? 91  LYS A CE     1 
ATOM   644  N NZ     . LYS A 1 100 ? 31.749 4.388  7.631  1.00 40.05 ? 91  LYS A NZ     1 
ATOM   645  N N      . ILE A 1 101 ? 28.362 11.324 7.020  1.00 13.76 ? 92  ILE A N      1 
ATOM   646  C CA     . ILE A 1 101 ? 27.133 12.079 7.215  1.00 13.44 ? 92  ILE A CA     1 
ATOM   647  C C      . ILE A 1 101 ? 27.234 13.443 6.547  1.00 13.90 ? 92  ILE A C      1 
ATOM   648  O O      . ILE A 1 101 ? 26.315 13.896 5.852  1.00 14.00 ? 92  ILE A O      1 
ATOM   649  C CB     . ILE A 1 101 ? 26.856 12.208 8.730  1.00 13.01 ? 92  ILE A CB     1 
ATOM   650  C CG1    . ILE A 1 101 ? 26.506 10.808 9.234  1.00 14.18 ? 92  ILE A CG1    1 
ATOM   651  C CG2    . ILE A 1 101 ? 25.789 13.265 8.974  1.00 16.31 ? 92  ILE A CG2    1 
ATOM   652  C CD1    . ILE A 1 101 ? 26.783 10.702 10.770 1.00 16.32 ? 92  ILE A CD1    1 
ATOM   653  N N      . VAL A 1 102 ? 28.363 14.121 6.750  1.00 12.08 ? 93  VAL A N      1 
ATOM   654  C CA     . VAL A 1 102 ? 28.578 15.436 6.133  1.00 12.36 ? 93  VAL A CA     1 
ATOM   655  C C      . VAL A 1 102 ? 28.521 15.305 4.610  1.00 13.00 ? 93  VAL A C      1 
ATOM   656  O O      . VAL A 1 102 ? 27.923 16.142 3.919  1.00 15.40 ? 93  VAL A O      1 
ATOM   657  C CB     . VAL A 1 102 ? 29.931 16.000 6.589  1.00 12.76 ? 93  VAL A CB     1 
ATOM   658  C CG1    . VAL A 1 102 ? 30.244 17.242 5.819  1.00 17.61 ? 93  VAL A CG1    1 
ATOM   659  C CG2    . VAL A 1 102 ? 29.840 16.381 8.088  1.00 15.15 ? 93  VAL A CG2    1 
ATOM   660  N N      . ASP A 1 103 ? 29.027 14.189 4.082  1.00 13.68 ? 94  ASP A N      1 
ATOM   661  C CA     . ASP A 1 103 ? 29.051 14.056 2.615  1.00 15.19 ? 94  ASP A CA     1 
ATOM   662  C C      . ASP A 1 103 ? 27.632 13.936 2.060  1.00 14.43 ? 94  ASP A C      1 
ATOM   663  O O      . ASP A 1 103 ? 27.309 14.544 1.038  1.00 16.23 ? 94  ASP A O      1 
ATOM   664  C CB     . ASP A 1 103 ? 29.824 12.795 2.261  1.00 17.35 ? 94  ASP A CB     1 
ATOM   665  C CG     . ASP A 1 103 ? 31.315 13.029 2.295  1.00 24.44 ? 94  ASP A CG     1 
ATOM   666  O OD1    . ASP A 1 103 ? 31.712 14.222 2.405  1.00 25.93 ? 94  ASP A OD1    1 
ATOM   667  O OD2    . ASP A 1 103 ? 32.089 12.057 2.070  1.00 27.98 ? 94  ASP A OD2    1 
ATOM   668  N N      . VAL A 1 104 ? 26.739 13.191 2.720  1.00 12.94 ? 95  VAL A N      1 
ATOM   669  C CA     . VAL A 1 104 ? 25.371 13.092 2.214  1.00 12.77 ? 95  VAL A CA     1 
ATOM   670  C C      . VAL A 1 104 ? 24.638 14.425 2.319  1.00 16.19 ? 95  VAL A C      1 
ATOM   671  O O      . VAL A 1 104 ? 23.805 14.775 1.466  1.00 15.77 ? 95  VAL A O      1 
ATOM   672  C CB     . VAL A 1 104 ? 24.545 11.922 2.784  1.00 17.53 ? 95  VAL A CB     1 
ATOM   673  C CG1    . VAL A 1 104 ? 25.202 10.612 2.451  1.00 18.67 ? 95  VAL A CG1    1 
ATOM   674  C CG2    . VAL A 1 104 ? 24.218 12.078 4.277  1.00 19.46 ? 95  VAL A CG2    1 
ATOM   675  N N      . VAL A 1 105 ? 24.924 15.211 3.359  1.00 13.76 ? 96  VAL A N      1 
ATOM   676  C CA     . VAL A 1 105 ? 24.291 16.509 3.468  1.00 13.55 ? 96  VAL A CA     1 
ATOM   677  C C      . VAL A 1 105 ? 24.795 17.447 2.368  1.00 13.47 ? 96  VAL A C      1 
ATOM   678  O O      . VAL A 1 105 ? 24.018 18.173 1.742  1.00 12.43 ? 96  VAL A O      1 
ATOM   679  C CB     . VAL A 1 105 ? 24.542 17.058 4.893  1.00 13.64 ? 96  VAL A CB     1 
ATOM   680  C CG1    . VAL A 1 105 ? 24.217 18.524 4.996  1.00 16.51 ? 96  VAL A CG1    1 
ATOM   681  C CG2    . VAL A 1 105 ? 23.752 16.191 5.912  1.00 15.86 ? 96  VAL A CG2    1 
ATOM   682  N N      . HIS A 1 106 ? 26.121 17.479 2.154  1.00 13.47 ? 97  HIS A N      1 
ATOM   683  C CA     . HIS A 1 106 ? 26.670 18.304 1.075  1.00 14.64 ? 97  HIS A CA     1 
ATOM   684  C C      . HIS A 1 106 ? 26.192 17.841 -0.290 1.00 14.88 ? 97  HIS A C      1 
ATOM   685  O O      . HIS A 1 106 ? 26.069 18.670 -1.190 1.00 15.00 ? 97  HIS A O      1 
ATOM   686  C CB     . HIS A 1 106 ? 28.176 18.239 1.152  1.00 13.03 ? 97  HIS A CB     1 
ATOM   687  C CG     . HIS A 1 106 ? 28.715 19.087 2.249  1.00 13.33 ? 97  HIS A CG     1 
ATOM   688  N ND1    . HIS A 1 106 ? 30.007 18.994 2.689  1.00 16.41 ? 97  HIS A ND1    1 
ATOM   689  C CD2    . HIS A 1 106 ? 28.135 20.099 2.937  1.00 15.31 ? 97  HIS A CD2    1 
ATOM   690  C CE1    . HIS A 1 106 ? 30.197 19.895 3.654  1.00 16.16 ? 97  HIS A CE1    1 
ATOM   691  N NE2    . HIS A 1 106 ? 29.078 20.592 3.800  1.00 16.15 ? 97  HIS A NE2    1 
ATOM   692  N N      . ALA A 1 107 ? 25.881 16.548 -0.451 1.00 14.91 ? 98  ALA A N      1 
ATOM   693  C CA     . ALA A 1 107 ? 25.320 16.089 -1.721 1.00 15.94 ? 98  ALA A CA     1 
ATOM   694  C C      . ALA A 1 107 ? 23.937 16.677 -2.021 1.00 18.57 ? 98  ALA A C      1 
ATOM   695  O O      . ALA A 1 107 ? 23.531 16.722 -3.200 1.00 18.83 ? 98  ALA A O      1 
ATOM   696  C CB     . ALA A 1 107 ? 25.302 14.561 -1.753 1.00 15.27 ? 98  ALA A CB     1 
ATOM   697  N N      . LYS A 1 108 ? 23.216 17.174 -1.025 1.00 15.88 ? 99  LYS A N      1 
ATOM   698  C CA     . LYS A 1 108 ? 21.974 17.892 -1.222 1.00 17.58 ? 99  LYS A CA     1 
ATOM   699  C C      . LYS A 1 108 ? 22.168 19.397 -1.310 1.00 16.61 ? 99  LYS A C      1 
ATOM   700  O O      . LYS A 1 108 ? 21.181 20.112 -1.493 1.00 20.90 ? 99  LYS A O      1 
ATOM   701  C CB     . LYS A 1 108 ? 20.965 17.511 -0.135 1.00 22.51 ? 99  LYS A CB     1 
ATOM   702  C CG     . LYS A 1 108 ? 20.527 16.056 -0.380 1.00 34.07 ? 99  LYS A CG     1 
ATOM   703  C CD     . LYS A 1 108 ? 19.413 15.626 0.456  1.00 31.29 ? 99  LYS A CD     1 
ATOM   704  C CE     . LYS A 1 108 ? 18.127 16.258 0.048  1.00 30.15 ? 99  LYS A CE     1 
ATOM   705  N NZ     . LYS A 1 108 ? 17.113 15.871 1.042  1.00 27.37 ? 99  LYS A NZ     1 
ATOM   706  N N      . GLY A 1 109 ? 23.413 19.889 -1.236 1.00 15.41 ? 100 GLY A N      1 
ATOM   707  C CA     . GLY A 1 109 ? 23.716 21.309 -1.350 1.00 15.06 ? 100 GLY A CA     1 
ATOM   708  C C      . GLY A 1 109 ? 23.517 22.112 -0.079 1.00 15.31 ? 100 GLY A C      1 
ATOM   709  O O      . GLY A 1 109 ? 23.429 23.340 -0.151 1.00 14.68 ? 100 GLY A O      1 
ATOM   710  N N      . ALA A 1 110 ? 23.396 21.447 1.066  1.00 13.45 ? 101 ALA A N      1 
ATOM   711  C CA     . ALA A 1 110 ? 23.199 22.148 2.339  1.00 12.56 ? 101 ALA A CA     1 
ATOM   712  C C      . ALA A 1 110 ? 24.530 22.494 2.983  1.00 12.87 ? 101 ALA A C      1 
ATOM   713  O O      . ALA A 1 110 ? 25.586 21.951 2.629  1.00 14.27 ? 101 ALA A O      1 
ATOM   714  C CB     . ALA A 1 110 ? 22.395 21.241 3.265  1.00 14.68 ? 101 ALA A CB     1 
ATOM   715  N N      . VAL A 1 111 ? 24.474 23.443 3.922  1.00 11.76 ? 102 VAL A N      1 
ATOM   716  C CA     . VAL A 1 111 ? 25.625 23.840 4.760  1.00 11.10 ? 102 VAL A CA     1 
ATOM   717  C C      . VAL A 1 111 ? 25.390 23.280 6.158  1.00 12.07 ? 102 VAL A C      1 
ATOM   718  O O      . VAL A 1 111 ? 24.258 23.332 6.660  1.00 12.50 ? 102 VAL A O      1 
ATOM   719  C CB     . VAL A 1 111 ? 25.689 25.373 4.820  1.00 12.03 ? 102 VAL A CB     1 
ATOM   720  C CG1    . VAL A 1 111 ? 26.808 25.901 5.756  1.00 13.08 ? 102 VAL A CG1    1 
ATOM   721  C CG2    . VAL A 1 111 ? 25.963 25.886 3.388  1.00 13.42 ? 102 VAL A CG2    1 
ATOM   722  N N      . ILE A 1 112 ? 26.413 22.696 6.764  1.00 10.40 ? 103 ILE A N      1 
ATOM   723  C CA     . ILE A 1 112 ? 26.208 22.060 8.081  1.00 10.03 ? 103 ILE A CA     1 
ATOM   724  C C      . ILE A 1 112 ? 27.324 22.427 9.041  1.00 11.19 ? 103 ILE A C      1 
ATOM   725  O O      . ILE A 1 112 ? 28.513 22.333 8.714  1.00 11.27 ? 103 ILE A O      1 
ATOM   726  C CB     . ILE A 1 112 ? 25.976 20.539 7.973  1.00 10.52 ? 103 ILE A CB     1 
ATOM   727  C CG1    . ILE A 1 112 ? 25.699 19.894 9.340  1.00 12.30 ? 103 ILE A CG1    1 
ATOM   728  C CG2    . ILE A 1 112 ? 27.146 19.850 7.222  1.00 13.44 ? 103 ILE A CG2    1 
ATOM   729  C CD1    . ILE A 1 112 ? 25.091 18.473 9.121  1.00 14.77 ? 103 ILE A CD1    1 
ATOM   730  N N      . PHE A 1 113 ? 26.928 22.833 10.236 1.00 10.20 ? 104 PHE A N      1 
ATOM   731  C CA     . PHE A 1 113 ? 27.844 23.112 11.337 1.00 10.13 ? 104 PHE A CA     1 
ATOM   732  C C      . PHE A 1 113 ? 27.672 22.075 12.442 1.00 10.85 ? 104 PHE A C      1 
ATOM   733  O O      . PHE A 1 113 ? 26.547 21.624 12.716 1.00 11.23 ? 104 PHE A O      1 
ATOM   734  C CB     . PHE A 1 113 ? 27.590 24.503 11.976 1.00 10.22 ? 104 PHE A CB     1 
ATOM   735  C CG     . PHE A 1 113 ? 28.258 25.668 11.254 1.00 10.01 ? 104 PHE A CG     1 
ATOM   736  C CD1    . PHE A 1 113 ? 28.543 25.693 9.862  1.00 11.90 ? 104 PHE A CD1    1 
ATOM   737  C CD2    . PHE A 1 113 ? 28.538 26.819 12.018 1.00 12.05 ? 104 PHE A CD2    1 
ATOM   738  C CE1    . PHE A 1 113 ? 29.094 26.845 9.300  1.00 11.36 ? 104 PHE A CE1    1 
ATOM   739  C CE2    . PHE A 1 113 ? 29.107 27.972 11.457 1.00 11.63 ? 104 PHE A CE2    1 
ATOM   740  C CZ     . PHE A 1 113 ? 29.378 27.989 10.074 1.00 11.75 ? 104 PHE A CZ     1 
ATOM   741  N N      . CYS A 1 114 ? 28.769 21.683 13.064 1.00 9.57  ? 105 CYS A N      1 
ATOM   742  C CA     . CYS A 1 114 ? 28.757 20.760 14.211 1.00 10.96 ? 105 CYS A CA     1 
ATOM   743  C C      . CYS A 1 114 ? 28.697 21.566 15.511 1.00 10.85 ? 105 CYS A C      1 
ATOM   744  O O      . CYS A 1 114 ? 29.563 22.405 15.750 1.00 11.34 ? 105 CYS A O      1 
ATOM   745  C CB     . CYS A 1 114 ? 30.051 19.906 14.176 1.00 10.49 ? 105 CYS A CB     1 
ATOM   746  S SG     . CYS A 1 114 ? 30.122 18.730 15.563 1.00 13.05 ? 105 CYS A SG     1 
ATOM   747  N N      . GLN A 1 115 ? 27.685 21.292 16.339 1.00 9.94  ? 106 GLN A N      1 
ATOM   748  C CA     . GLN A 1 115 ? 27.630 21.963 17.639 1.00 9.16  ? 106 GLN A CA     1 
ATOM   749  C C      . GLN A 1 115 ? 28.507 21.260 18.658 1.00 11.11 ? 106 GLN A C      1 
ATOM   750  O O      . GLN A 1 115 ? 28.318 20.065 18.901 1.00 11.92 ? 106 GLN A O      1 
ATOM   751  C CB     . GLN A 1 115 ? 26.181 22.008 18.127 1.00 9.94  ? 106 GLN A CB     1 
ATOM   752  C CG     . GLN A 1 115 ? 26.122 22.914 19.384 1.00 11.52 ? 106 GLN A CG     1 
ATOM   753  C CD     . GLN A 1 115 ? 24.809 22.861 20.125 1.00 9.73  ? 106 GLN A CD     1 
ATOM   754  O OE1    . GLN A 1 115 ? 24.430 21.782 20.641 1.00 10.28 ? 106 GLN A OE1    1 
ATOM   755  N NE2    . GLN A 1 115 ? 24.154 24.037 20.260 1.00 10.02 ? 106 GLN A NE2    1 
ATOM   756  N N      . LEU A 1 116 ? 29.434 22.023 19.265 1.00 9.40  ? 107 LEU A N      1 
ATOM   757  C CA     . LEU A 1 116 ? 30.387 21.467 20.242 1.00 10.12 ? 107 LEU A CA     1 
ATOM   758  C C      . LEU A 1 116 ? 29.823 21.685 21.654 1.00 9.24  ? 107 LEU A C      1 
ATOM   759  O O      . LEU A 1 116 ? 29.581 22.829 22.093 1.00 10.12 ? 107 LEU A O      1 
ATOM   760  C CB     . LEU A 1 116 ? 31.729 22.187 20.092 1.00 10.62 ? 107 LEU A CB     1 
ATOM   761  C CG     . LEU A 1 116 ? 32.374 22.090 18.717 1.00 10.38 ? 107 LEU A CG     1 
ATOM   762  C CD1    . LEU A 1 116 ? 33.750 22.684 18.812 1.00 12.81 ? 107 LEU A CD1    1 
ATOM   763  C CD2    . LEU A 1 116 ? 32.442 20.646 18.258 1.00 12.35 ? 107 LEU A CD2    1 
ATOM   764  N N      . TRP A 1 117 ? 29.629 20.585 22.383 1.00 10.29 ? 108 TRP A N      1 
ATOM   765  C CA     . TRP A 1 117 ? 28.828 20.592 23.614 1.00 10.26 ? 108 TRP A CA     1 
ATOM   766  C C      . TRP A 1 117 ? 29.541 19.940 24.779 1.00 12.49 ? 108 TRP A C      1 
ATOM   767  O O      . TRP A 1 117 ? 29.948 18.770 24.693 1.00 13.34 ? 108 TRP A O      1 
ATOM   768  C CB     . TRP A 1 117 ? 27.560 19.794 23.336 1.00 11.77 ? 108 TRP A CB     1 
ATOM   769  C CG     . TRP A 1 117 ? 26.533 19.721 24.463 1.00 10.31 ? 108 TRP A CG     1 
ATOM   770  C CD1    . TRP A 1 117 ? 26.284 20.671 25.469 1.00 11.48 ? 108 TRP A CD1    1 
ATOM   771  C CD2    . TRP A 1 117 ? 25.526 18.718 24.575 1.00 10.19 ? 108 TRP A CD2    1 
ATOM   772  N NE1    . TRP A 1 117 ? 25.185 20.243 26.210 1.00 10.70 ? 108 TRP A NE1    1 
ATOM   773  C CE2    . TRP A 1 117 ? 24.718 19.062 25.666 1.00 10.28 ? 108 TRP A CE2    1 
ATOM   774  C CE3    . TRP A 1 117 ? 25.257 17.522 23.867 1.00 11.35 ? 108 TRP A CE3    1 
ATOM   775  C CZ2    . TRP A 1 117 ? 23.612 18.260 26.039 1.00 13.02 ? 108 TRP A CZ2    1 
ATOM   776  C CZ3    . TRP A 1 117 ? 24.164 16.731 24.224 1.00 12.03 ? 108 TRP A CZ3    1 
ATOM   777  C CH2    . TRP A 1 117 ? 23.365 17.101 25.308 1.00 11.18 ? 108 TRP A CH2    1 
ATOM   778  N N      . HIS A 1 118 ? 29.680 20.704 25.870 1.00 9.96  ? 109 HIS A N      1 
ATOM   779  C CA     . HIS A 1 118 ? 30.119 20.154 27.147 1.00 10.68 ? 109 HIS A CA     1 
ATOM   780  C C      . HIS A 1 118 ? 29.043 20.456 28.163 1.00 10.14 ? 109 HIS A C      1 
ATOM   781  O O      . HIS A 1 118 ? 28.666 21.623 28.346 1.00 10.49 ? 109 HIS A O      1 
ATOM   782  C CB     . HIS A 1 118 ? 31.459 20.772 27.558 1.00 9.99  ? 109 HIS A CB     1 
ATOM   783  C CG     . HIS A 1 118 ? 32.153 19.998 28.637 1.00 10.21 ? 109 HIS A CG     1 
ATOM   784  N ND1    . HIS A 1 118 ? 31.565 19.708 29.863 1.00 10.79 ? 109 HIS A ND1    1 
ATOM   785  C CD2    . HIS A 1 118 ? 33.412 19.503 28.695 1.00 11.96 ? 109 HIS A CD2    1 
ATOM   786  C CE1    . HIS A 1 118 ? 32.437 19.078 30.619 1.00 12.14 ? 109 HIS A CE1    1 
ATOM   787  N NE2    . HIS A 1 118 ? 33.567 18.925 29.935 1.00 13.01 ? 109 HIS A NE2    1 
ATOM   788  N N      . VAL A 1 119 ? 28.591 19.404 28.844 1.00 9.65  ? 110 VAL A N      1 
ATOM   789  C CA     . VAL A 1 119 ? 27.498 19.565 29.815 1.00 10.17 ? 110 VAL A CA     1 
ATOM   790  C C      . VAL A 1 119 ? 27.924 20.060 31.194 1.00 9.03  ? 110 VAL A C      1 
ATOM   791  O O      . VAL A 1 119 ? 27.033 20.447 31.973 1.00 10.05 ? 110 VAL A O      1 
ATOM   792  C CB     . VAL A 1 119 ? 26.719 18.253 30.068 1.00 9.84  ? 110 VAL A CB     1 
ATOM   793  C CG1    . VAL A 1 119 ? 26.086 17.747 28.730 1.00 10.84 ? 110 VAL A CG1    1 
ATOM   794  C CG2    . VAL A 1 119 ? 27.612 17.190 30.680 1.00 11.73 ? 110 VAL A CG2    1 
ATOM   795  N N      . GLY A 1 120 ? 29.215 20.073 31.507 1.00 10.06 ? 111 GLY A N      1 
ATOM   796  C CA     . GLY A 1 120 ? 29.629 20.492 32.854 1.00 10.41 ? 111 GLY A CA     1 
ATOM   797  C C      . GLY A 1 120 ? 28.954 19.638 33.909 1.00 11.46 ? 111 GLY A C      1 
ATOM   798  O O      . GLY A 1 120 ? 28.960 18.416 33.842 1.00 11.72 ? 111 GLY A O      1 
ATOM   799  N N      . ARG A 1 121 ? 28.348 20.323 34.889 1.00 10.27 ? 112 ARG A N      1 
ATOM   800  C CA     . ARG A 1 121 ? 27.784 19.573 36.030 1.00 11.19 ? 112 ARG A CA     1 
ATOM   801  C C      . ARG A 1 121 ? 26.524 18.800 35.692 1.00 11.76 ? 112 ARG A C      1 
ATOM   802  O O      . ARG A 1 121 ? 26.051 18.033 36.545 1.00 12.01 ? 112 ARG A O      1 
ATOM   803  C CB     . ARG A 1 121 ? 27.525 20.544 37.200 1.00 10.27 ? 112 ARG A CB     1 
ATOM   804  C CG     . ARG A 1 121 ? 26.377 21.501 36.967 1.00 9.82  ? 112 ARG A CG     1 
ATOM   805  C CD     . ARG A 1 121 ? 26.240 22.406 38.204 1.00 10.94 ? 112 ARG A CD     1 
ATOM   806  N NE     . ARG A 1 121 ? 25.146 23.334 37.998 1.00 11.54 ? 112 ARG A NE     1 
ATOM   807  C CZ     . ARG A 1 121 ? 24.547 24.009 38.964 1.00 11.89 ? 112 ARG A CZ     1 
ATOM   808  N NH1    . ARG A 1 121 ? 24.990 23.958 40.244 1.00 13.24 ? 112 ARG A NH1    1 
ATOM   809  N NH2    . ARG A 1 121 ? 23.482 24.712 38.665 1.00 13.59 ? 112 ARG A NH2    1 
ATOM   810  N N      . ALA A 1 122 ? 25.968 18.967 34.508 1.00 10.37 ? 113 ALA A N      1 
ATOM   811  C CA     . ALA A 1 122 ? 24.729 18.304 34.113 1.00 10.40 ? 113 ALA A CA     1 
ATOM   812  C C      . ALA A 1 122 ? 25.045 16.925 33.563 1.00 10.97 ? 113 ALA A C      1 
ATOM   813  O O      . ALA A 1 122 ? 24.851 16.627 32.369 1.00 12.04 ? 113 ALA A O      1 
ATOM   814  C CB     . ALA A 1 122 ? 23.956 19.156 33.111 1.00 11.17 ? 113 ALA A CB     1 
ATOM   815  N N      . SER A 1 123 ? 25.598 16.097 34.459 1.00 11.46 ? 114 SER A N      1 
ATOM   816  C CA     . SER A 1 123 ? 26.047 14.755 34.104 1.00 12.19 ? 114 SER A CA     1 
ATOM   817  C C      . SER A 1 123 ? 25.805 13.844 35.295 1.00 11.73 ? 114 SER A C      1 
ATOM   818  O O      . SER A 1 123 ? 25.102 14.211 36.236 1.00 14.28 ? 114 SER A O      1 
ATOM   819  C CB     . SER A 1 123 ? 27.495 14.792 33.611 1.00 12.74 ? 114 SER A CB     1 
ATOM   820  O OG     . SER A 1 123 ? 27.850 13.510 33.030 1.00 12.32 ? 114 SER A OG     1 
ATOM   821  N N      . HIS A 1 124 ? 26.389 12.661 35.218 1.00 13.06 ? 115 HIS A N      1 
ATOM   822  C CA     . HIS A 1 124 ? 26.198 11.639 36.261 1.00 11.57 ? 115 HIS A CA     1 
ATOM   823  C C      . HIS A 1 124 ? 27.355 10.687 36.110 1.00 12.79 ? 115 HIS A C      1 
ATOM   824  O O      . HIS A 1 124 ? 27.935 10.551 35.031 1.00 13.06 ? 115 HIS A O      1 
ATOM   825  C CB     . HIS A 1 124 ? 24.863 10.908 36.000 1.00 13.75 ? 115 HIS A CB     1 
ATOM   826  C CG     . HIS A 1 124 ? 24.428 9.928  37.053 1.00 13.21 ? 115 HIS A CG     1 
ATOM   827  N ND1    . HIS A 1 124 ? 24.904 8.635  37.120 1.00 15.05 ? 115 HIS A ND1    1 
ATOM   828  C CD2    . HIS A 1 124 ? 23.478 10.051 38.007 1.00 16.07 ? 115 HIS A CD2    1 
ATOM   829  C CE1    . HIS A 1 124 ? 24.319 8.023  38.150 1.00 16.88 ? 115 HIS A CE1    1 
ATOM   830  N NE2    . HIS A 1 124 ? 23.450 8.863  38.700 1.00 17.89 ? 115 HIS A NE2    1 
ATOM   831  N N      . GLU A 1 125 ? 27.664 9.958  37.194 1.00 14.28 ? 116 GLU A N      1 
ATOM   832  C CA     . GLU A 1 125 ? 28.766 9.001  37.118 1.00 16.34 ? 116 GLU A CA     1 
ATOM   833  C C      . GLU A 1 125 ? 28.589 7.992  35.982 1.00 13.97 ? 116 GLU A C      1 
ATOM   834  O O      . GLU A 1 125 ? 29.596 7.554  35.398 1.00 16.56 ? 116 GLU A O      1 
ATOM   835  C CB     . GLU A 1 125 ? 28.865 8.256  38.474 1.00 18.42 ? 116 GLU A CB     1 
ATOM   836  N N      . VAL A 1 126 ? 27.339 7.631  35.640 1.00 14.22 ? 117 VAL A N      1 
ATOM   837  C CA     . VAL A 1 126 ? 27.117 6.634  34.578 1.00 13.28 ? 117 VAL A CA     1 
ATOM   838  C C      . VAL A 1 126 ? 27.675 7.131  33.246 1.00 13.39 ? 117 VAL A C      1 
ATOM   839  O O      . VAL A 1 126 ? 27.991 6.324  32.346 1.00 15.92 ? 117 VAL A O      1 
ATOM   840  C CB     . VAL A 1 126 ? 25.620 6.244  34.494 1.00 14.10 ? 117 VAL A CB     1 
ATOM   841  C CG1    . VAL A 1 126 ? 24.765 7.326  33.801 1.00 14.29 ? 117 VAL A CG1    1 
ATOM   842  C CG2    . VAL A 1 126 ? 25.460 4.939  33.733 1.00 14.92 ? 117 VAL A CG2    1 
ATOM   843  N N      . TYR A 1 127 ? 27.785 8.457  33.095 1.00 14.06 ? 118 TYR A N      1 
ATOM   844  C CA     . TYR A 1 127 ? 28.228 9.092  31.851 1.00 11.83 ? 118 TYR A CA     1 
ATOM   845  C C      . TYR A 1 127 ? 29.697 9.470  31.885 1.00 14.62 ? 118 TYR A C      1 
ATOM   846  O O      . TYR A 1 127 ? 30.219 9.948  30.868 1.00 15.35 ? 118 TYR A O      1 
ATOM   847  C CB     . TYR A 1 127 ? 27.376 10.362 31.590 1.00 12.68 ? 118 TYR A CB     1 
ATOM   848  C CG     . TYR A 1 127 ? 25.951 10.066 31.268 1.00 10.69 ? 118 TYR A CG     1 
ATOM   849  C CD1    . TYR A 1 127 ? 25.618 9.210  30.212 1.00 10.60 ? 118 TYR A CD1    1 
ATOM   850  C CD2    . TYR A 1 127 ? 24.913 10.647 32.003 1.00 11.26 ? 118 TYR A CD2    1 
ATOM   851  C CE1    . TYR A 1 127 ? 24.311 8.919  29.941 1.00 11.80 ? 118 TYR A CE1    1 
ATOM   852  C CE2    . TYR A 1 127 ? 23.594 10.362 31.729 1.00 12.25 ? 118 TYR A CE2    1 
ATOM   853  C CZ     . TYR A 1 127 ? 23.282 9.458  30.694 1.00 11.48 ? 118 TYR A CZ     1 
ATOM   854  O OH     . TYR A 1 127 ? 21.973 9.174  30.415 1.00 12.52 ? 118 TYR A OH     1 
ATOM   855  N N      . GLN A 1 128 ? 30.390 9.288  33.022 1.00 15.49 ? 119 GLN A N      1 
ATOM   856  C CA     . GLN A 1 128 ? 31.755 9.757  33.145 1.00 14.33 ? 119 GLN A CA     1 
ATOM   857  C C      . GLN A 1 128 ? 32.714 8.588  33.178 1.00 19.37 ? 119 GLN A C      1 
ATOM   858  O O      . GLN A 1 128 ? 32.392 7.536  33.733 1.00 18.91 ? 119 GLN A O      1 
ATOM   859  C CB     . GLN A 1 128 ? 31.904 10.516 34.472 1.00 15.30 ? 119 GLN A CB     1 
ATOM   860  C CG     . GLN A 1 128 ? 31.124 11.835 34.501 1.00 14.72 ? 119 GLN A CG     1 
ATOM   861  C CD     . GLN A 1 128 ? 31.700 12.808 33.480 1.00 14.12 ? 119 GLN A CD     1 
ATOM   862  O OE1    . GLN A 1 128 ? 32.902 12.876 33.314 1.00 16.52 ? 119 GLN A OE1    1 
ATOM   863  N NE2    . GLN A 1 128 ? 30.840 13.549 32.821 1.00 13.96 ? 119 GLN A NE2    1 
ATOM   864  N N      . PRO A 1 129 ? 33.883 8.767  32.604 1.00 19.26 ? 120 PRO A N      1 
ATOM   865  C CA     . PRO A 1 129 ? 34.912 7.718  32.646 1.00 22.28 ? 120 PRO A CA     1 
ATOM   866  C C      . PRO A 1 129 ? 35.275 7.428  34.088 1.00 22.41 ? 120 PRO A C      1 
ATOM   867  O O      . PRO A 1 129 ? 35.444 8.346  34.899 1.00 22.34 ? 120 PRO A O      1 
ATOM   868  C CB     . PRO A 1 129 ? 36.091 8.349  31.881 1.00 26.36 ? 120 PRO A CB     1 
ATOM   869  C CG     . PRO A 1 129 ? 35.734 9.769  31.599 1.00 31.10 ? 120 PRO A CG     1 
ATOM   870  C CD     . PRO A 1 129 ? 34.228 9.879  31.696 1.00 22.73 ? 120 PRO A CD     1 
ATOM   871  N N      . ALA A 1 130 ? 35.366 6.134  34.410 1.00 26.10 ? 121 ALA A N      1 
ATOM   872  C CA     . ALA A 1 130 ? 35.687 5.649  35.757 1.00 29.07 ? 121 ALA A CA     1 
ATOM   873  C C      . ALA A 1 130 ? 34.681 6.110  36.787 1.00 29.47 ? 121 ALA A C      1 
ATOM   874  O O      . ALA A 1 130 ? 34.957 6.090  37.993 1.00 32.10 ? 121 ALA A O      1 
ATOM   875  C CB     . ALA A 1 130 ? 37.105 6.014  36.199 1.00 32.02 ? 121 ALA A CB     1 
ATOM   876  N N      . GLY A 1 131 ? 33.501 6.530  36.345 1.00 24.92 ? 122 GLY A N      1 
ATOM   877  C CA     . GLY A 1 131 ? 32.504 7.057  37.251 1.00 24.00 ? 122 GLY A CA     1 
ATOM   878  C C      . GLY A 1 131 ? 32.973 8.264  38.032 1.00 24.77 ? 122 GLY A C      1 
ATOM   879  O O      . GLY A 1 131 ? 32.506 8.476  39.161 1.00 24.77 ? 122 GLY A O      1 
ATOM   880  N N      . ALA A 1 132 ? 33.869 9.073  37.461 1.00 23.69 ? 123 ALA A N      1 
ATOM   881  C CA     . ALA A 1 132 ? 34.351 10.274 38.141 1.00 24.11 ? 123 ALA A CA     1 
ATOM   882  C C      . ALA A 1 132 ? 33.268 11.350 38.193 1.00 20.42 ? 123 ALA A C      1 
ATOM   883  O O      . ALA A 1 132 ? 32.294 11.313 37.436 1.00 20.75 ? 123 ALA A O      1 
ATOM   884  C CB     . ALA A 1 132 ? 35.542 10.869 37.413 1.00 27.27 ? 123 ALA A CB     1 
ATOM   885  N N      . ALA A 1 133 ? 33.443 12.296 39.112 1.00 19.53 ? 124 ALA A N      1 
ATOM   886  C CA     . ALA A 1 133 ? 32.506 13.399 39.234 1.00 18.55 ? 124 ALA A CA     1 
ATOM   887  C C      . ALA A 1 133 ? 32.565 14.303 38.000 1.00 16.90 ? 124 ALA A C      1 
ATOM   888  O O      . ALA A 1 133 ? 33.638 14.576 37.472 1.00 17.57 ? 124 ALA A O      1 
ATOM   889  C CB     . ALA A 1 133 ? 32.808 14.244 40.491 1.00 18.49 ? 124 ALA A CB     1 
ATOM   890  N N      . PRO A 1 134 ? 31.429 14.818 37.555 1.00 14.60 ? 125 PRO A N      1 
ATOM   891  C CA     . PRO A 1 134 ? 31.432 15.821 36.469 1.00 13.46 ? 125 PRO A CA     1 
ATOM   892  C C      . PRO A 1 134 ? 32.124 17.108 36.883 1.00 15.36 ? 125 PRO A C      1 
ATOM   893  O O      . PRO A 1 134 ? 32.289 17.381 38.070 1.00 15.71 ? 125 PRO A O      1 
ATOM   894  C CB     . PRO A 1 134 ? 29.945 16.070 36.191 1.00 18.37 ? 125 PRO A CB     1 
ATOM   895  C CG     . PRO A 1 134 ? 29.186 15.391 37.228 1.00 25.84 ? 125 PRO A CG     1 
ATOM   896  C CD     . PRO A 1 134 ? 30.090 14.474 38.032 1.00 15.55 ? 125 PRO A CD     1 
ATOM   897  N N      . ILE A 1 135 ? 32.549 17.920 35.901 1.00 13.43 ? 126 ILE A N      1 
ATOM   898  C CA     . ILE A 1 135 ? 33.291 19.154 36.183 1.00 12.66 ? 126 ILE A CA     1 
ATOM   899  C C      . ILE A 1 135 ? 32.395 20.380 36.019 1.00 12.85 ? 126 ILE A C      1 
ATOM   900  O O      . ILE A 1 135 ? 31.438 20.363 35.237 1.00 14.69 ? 126 ILE A O      1 
ATOM   901  C CB     . ILE A 1 135 ? 34.561 19.336 35.335 1.00 13.23 ? 126 ILE A CB     1 
ATOM   902  C CG1    . ILE A 1 135 ? 34.188 19.417 33.830 1.00 16.93 ? 126 ILE A CG1    1 
ATOM   903  C CG2    . ILE A 1 135 ? 35.563 18.218 35.613 1.00 19.70 ? 126 ILE A CG2    1 
ATOM   904  C CD1    . ILE A 1 135 ? 35.144 20.319 33.042 1.00 19.84 ? 126 ILE A CD1    1 
ATOM   905  N N      . SER A 1 136 ? 32.735 21.473 36.709 1.00 12.60 ? 127 SER A N      1 
ATOM   906  C CA     . SER A 1 136 ? 31.942 22.686 36.574 1.00 11.61 ? 127 SER A CA     1 
ATOM   907  C C      . SER A 1 136 ? 32.747 23.916 37.007 1.00 11.47 ? 127 SER A C      1 
ATOM   908  O O      . SER A 1 136 ? 33.883 23.809 37.487 1.00 13.12 ? 127 SER A O      1 
ATOM   909  C CB     . SER A 1 136 ? 30.682 22.580 37.407 1.00 12.11 ? 127 SER A CB     1 
ATOM   910  O OG     . SER A 1 136 ? 29.767 23.670 37.198 1.00 12.81 ? 127 SER A OG     1 
ATOM   911  N N      . SER A 1 137 ? 32.120 25.089 36.889 1.00 11.50 ? 128 SER A N      1 
ATOM   912  C CA     . SER A 1 137 ? 32.628 26.293 37.555 1.00 12.54 ? 128 SER A CA     1 
ATOM   913  C C      . SER A 1 137 ? 32.537 26.189 39.067 1.00 12.32 ? 128 SER A C      1 
ATOM   914  O O      . SER A 1 137 ? 33.318 26.823 39.782 1.00 12.96 ? 128 SER A O      1 
ATOM   915  C CB     . SER A 1 137 ? 31.814 27.527 37.170 1.00 14.37 ? 128 SER A CB     1 
ATOM   916  O OG     . SER A 1 137 ? 30.418 27.264 37.452 1.00 12.46 ? 128 SER A OG     1 
ATOM   917  N N      . THR A 1 138 ? 31.561 25.421 39.567 1.00 11.07 ? 129 THR A N      1 
ATOM   918  C CA     . THR A 1 138 ? 31.131 25.407 40.951 1.00 11.94 ? 129 THR A CA     1 
ATOM   919  C C      . THR A 1 138 ? 31.224 23.974 41.493 1.00 12.66 ? 129 THR A C      1 
ATOM   920  O O      . THR A 1 138 ? 31.282 22.984 40.738 1.00 14.08 ? 129 THR A O      1 
ATOM   921  C CB     . THR A 1 138 ? 29.668 25.907 40.995 1.00 13.16 ? 129 THR A CB     1 
ATOM   922  O OG1    . THR A 1 138 ? 29.259 25.954 42.372 1.00 13.72 ? 129 THR A OG1    1 
ATOM   923  C CG2    . THR A 1 138 ? 28.686 25.006 40.258 1.00 13.78 ? 129 THR A CG2    1 
ATOM   924  N N      . GLU A 1 139 ? 31.211 23.859 42.829 1.00 14.29 ? 130 GLU A N      1 
ATOM   925  C CA     . GLU A 1 139 ? 31.101 22.563 43.513 1.00 14.57 ? 130 GLU A CA     1 
ATOM   926  C C      . GLU A 1 139 ? 29.657 22.237 43.892 1.00 13.82 ? 130 GLU A C      1 
ATOM   927  O O      . GLU A 1 139 ? 29.406 21.139 44.421 1.00 16.18 ? 130 GLU A O      1 
ATOM   928  C CB     . GLU A 1 139 ? 32.003 22.520 44.764 1.00 19.00 ? 130 GLU A CB     1 
ATOM   929  N N      . LYS A 1 140 ? 28.692 23.118 43.594 1.00 13.72 ? 131 LYS A N      1 
ATOM   930  C CA     . LYS A 1 140 ? 27.303 22.848 43.957 1.00 13.63 ? 131 LYS A CA     1 
ATOM   931  C C      . LYS A 1 140 ? 26.609 21.985 42.906 1.00 14.80 ? 131 LYS A C      1 
ATOM   932  O O      . LYS A 1 140 ? 26.725 22.236 41.703 1.00 14.10 ? 131 LYS A O      1 
ATOM   933  C CB     . LYS A 1 140 ? 26.522 24.149 44.053 1.00 15.24 ? 131 LYS A CB     1 
ATOM   934  C CG     . LYS A 1 140 ? 27.021 25.109 45.158 1.00 14.11 ? 131 LYS A CG     1 
ATOM   935  C CD     . LYS A 1 140 ? 26.763 24.499 46.590 1.00 21.34 ? 131 LYS A CD     1 
ATOM   936  C CE     . LYS A 1 140 ? 26.689 25.594 47.612 1.00 33.78 ? 131 LYS A CE     1 
ATOM   937  N NZ     . LYS A 1 140 ? 25.930 25.038 48.787 1.00 33.21 ? 131 LYS A NZ     1 
ATOM   938  N N      . PRO A 1 141 ? 25.830 21.008 43.330 1.00 13.27 ? 132 PRO A N      1 
ATOM   939  C CA     . PRO A 1 141 ? 25.016 20.227 42.391 1.00 13.21 ? 132 PRO A CA     1 
ATOM   940  C C      . PRO A 1 141 ? 23.848 21.010 41.870 1.00 13.79 ? 132 PRO A C      1 
ATOM   941  O O      . PRO A 1 141 ? 23.358 21.953 42.503 1.00 15.26 ? 132 PRO A O      1 
ATOM   942  C CB     . PRO A 1 141 ? 24.495 19.072 43.249 1.00 13.72 ? 132 PRO A CB     1 
ATOM   943  C CG     . PRO A 1 141 ? 24.439 19.671 44.672 1.00 18.09 ? 132 PRO A CG     1 
ATOM   944  C CD     . PRO A 1 141 ? 25.584 20.657 44.762 1.00 14.29 ? 132 PRO A CD     1 
ATOM   945  N N      . ILE A 1 142 ? 23.378 20.628 40.653 1.00 12.59 ? 133 ILE A N      1 
ATOM   946  C CA     . ILE A 1 142 ? 22.068 21.094 40.229 1.00 11.23 ? 133 ILE A CA     1 
ATOM   947  C C      . ILE A 1 142 ? 21.068 20.661 41.319 1.00 13.71 ? 133 ILE A C      1 
ATOM   948  O O      . ILE A 1 142 ? 21.191 19.554 41.868 1.00 16.16 ? 133 ILE A O      1 
ATOM   949  C CB     . ILE A 1 142 ? 21.731 20.473 38.858 1.00 14.00 ? 133 ILE A CB     1 
ATOM   950  C CG1    . ILE A 1 142 ? 22.659 21.055 37.802 1.00 12.85 ? 133 ILE A CG1    1 
ATOM   951  C CG2    . ILE A 1 142 ? 20.311 20.728 38.488 1.00 14.29 ? 133 ILE A CG2    1 
ATOM   952  C CD1    . ILE A 1 142 ? 22.762 20.142 36.555 1.00 14.14 ? 133 ILE A CD1    1 
ATOM   953  N N      . SER A 1 143 ? 20.090 21.519 41.622 1.00 13.83 ? 134 SER A N      1 
ATOM   954  C CA     . SER A 1 143 ? 19.138 21.154 42.685 1.00 14.69 ? 134 SER A CA     1 
ATOM   955  C C      . SER A 1 143 ? 18.221 20.002 42.257 1.00 20.92 ? 134 SER A C      1 
ATOM   956  O O      . SER A 1 143 ? 18.007 19.714 41.068 1.00 17.02 ? 134 SER A O      1 
ATOM   957  C CB     . SER A 1 143 ? 18.294 22.353 43.095 1.00 17.51 ? 134 SER A CB     1 
ATOM   958  O OG     . SER A 1 143 ? 17.489 22.835 42.034 1.00 21.51 ? 134 SER A OG     1 
ATOM   959  N N      . ASN A 1 144 ? 17.626 19.348 43.268 1.00 19.07 ? 135 ASN A N      1 
ATOM   960  C CA     . ASN A 1 144 ? 16.730 18.238 42.926 1.00 21.08 ? 135 ASN A CA     1 
ATOM   961  C C      . ASN A 1 144 ? 15.376 18.699 42.341 1.00 19.50 ? 135 ASN A C      1 
ATOM   962  O O      . ASN A 1 144 ? 14.539 17.806 42.091 1.00 25.82 ? 135 ASN A O      1 
ATOM   963  C CB     . ASN A 1 144 ? 16.591 17.233 44.073 1.00 33.79 ? 135 ASN A CB     1 
ATOM   964  C CG     . ASN A 1 144 ? 15.919 17.822 45.274 1.00 35.26 ? 135 ASN A CG     1 
ATOM   965  O OD1    . ASN A 1 144 ? 15.381 18.927 45.211 1.00 34.79 ? 135 ASN A OD1    1 
ATOM   966  N ND2    . ASN A 1 144 ? 15.907 17.075 46.380 1.00 40.51 ? 135 ASN A ND2    1 
ATOM   967  N N      . ARG A 1 145 ? 15.135 19.971 42.019 1.00 19.38 ? 136 ARG A N      1 
ATOM   968  C CA     . ARG A 1 145 ? 14.059 20.326 41.106 1.00 21.42 ? 136 ARG A CA     1 
ATOM   969  C C      . ARG A 1 145 ? 14.247 19.661 39.738 1.00 22.04 ? 136 ARG A C      1 
ATOM   970  O O      . ARG A 1 145 ? 13.280 19.487 38.998 1.00 25.87 ? 136 ARG A O      1 
ATOM   971  C CB     . ARG A 1 145 ? 14.042 21.865 40.958 1.00 25.05 ? 136 ARG A CB     1 
ATOM   972  C CG     . ARG A 1 145 ? 13.379 22.423 39.704 1.00 32.91 ? 136 ARG A CG     1 
ATOM   973  C CD     . ARG A 1 145 ? 13.350 23.974 39.690 1.00 39.83 ? 136 ARG A CD     1 
ATOM   974  N NE     . ARG A 1 145 ? 12.494 24.472 38.609 1.00 51.07 ? 136 ARG A NE     1 
ATOM   975  C CZ     . ARG A 1 145 ? 12.675 25.620 37.957 1.00 57.20 ? 136 ARG A CZ     1 
ATOM   976  N NH1    . ARG A 1 145 ? 13.635 26.474 38.294 1.00 50.23 ? 136 ARG A NH1    1 
ATOM   977  N NH2    . ARG A 1 145 ? 11.878 25.915 36.933 1.00 45.12 ? 136 ARG A NH2    1 
ATOM   978  N N      . TRP A 1 146 ? 15.472 19.298 39.386 1.00 16.76 ? 137 TRP A N      1 
ATOM   979  C CA     . TRP A 1 146 ? 15.759 18.765 38.056 1.00 14.95 ? 137 TRP A CA     1 
ATOM   980  C C      . TRP A 1 146 ? 16.293 17.363 38.214 1.00 17.58 ? 137 TRP A C      1 
ATOM   981  O O      . TRP A 1 146 ? 16.958 17.036 39.184 1.00 17.05 ? 137 TRP A O      1 
ATOM   982  C CB     . TRP A 1 146 ? 16.822 19.618 37.333 1.00 15.94 ? 137 TRP A CB     1 
ATOM   983  C CG     . TRP A 1 146 ? 16.530 21.082 37.381 1.00 16.71 ? 137 TRP A CG     1 
ATOM   984  C CD1    . TRP A 1 146 ? 16.915 21.965 38.376 1.00 18.35 ? 137 TRP A CD1    1 
ATOM   985  C CD2    . TRP A 1 146 ? 15.842 21.845 36.404 1.00 15.97 ? 137 TRP A CD2    1 
ATOM   986  N NE1    . TRP A 1 146 ? 16.463 23.236 38.078 1.00 19.00 ? 137 TRP A NE1    1 
ATOM   987  C CE2    . TRP A 1 146 ? 15.787 23.196 36.889 1.00 17.47 ? 137 TRP A CE2    1 
ATOM   988  C CE3    . TRP A 1 146 ? 15.231 21.531 35.173 1.00 21.06 ? 137 TRP A CE3    1 
ATOM   989  C CZ2    . TRP A 1 146 ? 15.167 24.226 36.153 1.00 22.31 ? 137 TRP A CZ2    1 
ATOM   990  C CZ3    . TRP A 1 146 ? 14.581 22.578 34.464 1.00 23.07 ? 137 TRP A CZ3    1 
ATOM   991  C CH2    . TRP A 1 146 ? 14.573 23.899 34.969 1.00 21.85 ? 137 TRP A CH2    1 
ATOM   992  N N      . ARG A 1 147 ? 16.029 16.543 37.198 1.00 16.11 ? 138 ARG A N      1 
ATOM   993  C CA     . ARG A 1 147 ? 16.516 15.183 37.156 1.00 15.10 ? 138 ARG A CA     1 
ATOM   994  C C      . ARG A 1 147 ? 17.142 14.889 35.814 1.00 13.88 ? 138 ARG A C      1 
ATOM   995  O O      . ARG A 1 147 ? 16.759 15.458 34.806 1.00 17.49 ? 138 ARG A O      1 
ATOM   996  C CB     . ARG A 1 147 ? 15.442 14.120 37.490 1.00 19.73 ? 138 ARG A CB     1 
ATOM   997  C CG     . ARG A 1 147 ? 14.523 14.501 38.638 1.00 25.07 ? 138 ARG A CG     1 
ATOM   998  C CD     . ARG A 1 147 ? 14.518 13.388 39.666 1.00 43.85 ? 138 ARG A CD     1 
ATOM   999  N NE     . ARG A 1 147 ? 13.795 13.748 40.880 1.00 59.14 ? 138 ARG A NE     1 
ATOM   1000 C CZ     . ARG A 1 147 ? 14.282 14.499 41.853 1.00 50.90 ? 138 ARG A CZ     1 
ATOM   1001 N NH1    . ARG A 1 147 ? 15.535 14.926 41.832 1.00 46.27 ? 138 ARG A NH1    1 
ATOM   1002 N NH2    . ARG A 1 147 ? 13.492 14.829 42.876 1.00 46.27 ? 138 ARG A NH2    1 
ATOM   1003 N N      . ILE A 1 148 ? 18.123 14.000 35.815 1.00 13.89 ? 139 ILE A N      1 
ATOM   1004 C CA     . ILE A 1 148 ? 18.849 13.671 34.589 1.00 12.59 ? 139 ILE A CA     1 
ATOM   1005 C C      . ILE A 1 148 ? 18.255 12.413 33.961 1.00 14.12 ? 139 ILE A C      1 
ATOM   1006 O O      . ILE A 1 148 ? 17.907 11.451 34.655 1.00 14.17 ? 139 ILE A O      1 
ATOM   1007 C CB     . ILE A 1 148 ? 20.336 13.477 34.918 1.00 11.62 ? 139 ILE A CB     1 
ATOM   1008 C CG1    . ILE A 1 148 ? 21.172 13.419 33.622 1.00 11.89 ? 139 ILE A CG1    1 
ATOM   1009 C CG2    . ILE A 1 148 ? 20.627 12.196 35.785 1.00 15.49 ? 139 ILE A CG2    1 
ATOM   1010 C CD1    . ILE A 1 148 ? 22.638 13.402 33.833 1.00 12.38 ? 139 ILE A CD1    1 
ATOM   1011 N N      . LEU A 1 149 ? 18.120 12.413 32.649 1.00 14.29 ? 140 LEU A N      1 
ATOM   1012 C CA     . LEU A 1 149 ? 17.732 11.180 31.964 1.00 13.18 ? 140 LEU A CA     1 
ATOM   1013 C C      . LEU A 1 149 ? 18.889 10.185 32.036 1.00 12.27 ? 140 LEU A C      1 
ATOM   1014 O O      . LEU A 1 149 ? 20.012 10.510 31.643 1.00 12.89 ? 140 LEU A O      1 
ATOM   1015 C CB     . LEU A 1 149 ? 17.441 11.537 30.503 1.00 14.74 ? 140 LEU A CB     1 
ATOM   1016 C CG     . LEU A 1 149 ? 17.122 10.304 29.608 1.00 15.97 ? 140 LEU A CG     1 
ATOM   1017 C CD1    . LEU A 1 149 ? 15.833 9.626  30.061 1.00 17.87 ? 140 LEU A CD1    1 
ATOM   1018 C CD2    . LEU A 1 149 ? 16.987 10.754 28.183 1.00 16.46 ? 140 LEU A CD2    1 
ATOM   1019 N N      . MET A 1 150 ? 18.593 8.961  32.529 1.00 12.43 ? 141 MET A N      1 
ATOM   1020 C CA     . MET A 1 150 ? 19.561 7.885  32.631 1.00 12.66 ? 141 MET A CA     1 
ATOM   1021 C C      . MET A 1 150 ? 19.515 6.986  31.404 1.00 12.66 ? 141 MET A C      1 
ATOM   1022 O O      . MET A 1 150 ? 18.547 7.014  30.656 1.00 14.97 ? 141 MET A O      1 
ATOM   1023 C CB     . MET A 1 150 ? 19.247 7.033  33.891 1.00 13.34 ? 141 MET A CB     1 
ATOM   1024 C CG     . MET A 1 150 ? 19.311 7.875  35.173 1.00 15.09 ? 141 MET A CG     1 
ATOM   1025 S SD     . MET A 1 150 ? 20.995 8.393  35.581 1.00 16.45 ? 141 MET A SD     1 
ATOM   1026 C CE     . MET A 1 150 ? 21.754 6.839  36.075 1.00 17.63 ? 141 MET A CE     1 
ATOM   1027 N N      . PRO A 1 151 ? 20.566 6.204  31.176 1.00 12.33 ? 142 PRO A N      1 
ATOM   1028 C CA     . PRO A 1 151 ? 20.572 5.327  29.991 1.00 13.60 ? 142 PRO A CA     1 
ATOM   1029 C C      . PRO A 1 151 ? 19.453 4.323  29.979 1.00 15.32 ? 142 PRO A C      1 
ATOM   1030 O O      . PRO A 1 151 ? 19.101 3.831  28.890 1.00 16.17 ? 142 PRO A O      1 
ATOM   1031 C CB     . PRO A 1 151 ? 21.937 4.655  30.046 1.00 14.26 ? 142 PRO A CB     1 
ATOM   1032 C CG     . PRO A 1 151 ? 22.800 5.591  30.858 1.00 15.47 ? 142 PRO A CG     1 
ATOM   1033 C CD     . PRO A 1 151 ? 21.871 6.223  31.860 1.00 14.50 ? 142 PRO A CD     1 
ATOM   1034 N N      . ASP A 1 152 ? 18.884 3.980  31.122 1.00 14.15 ? 143 ASP A N      1 
ATOM   1035 C CA     . ASP A 1 152 ? 17.807 2.991  31.156 1.00 14.99 ? 143 ASP A CA     1 
ATOM   1036 C C      . ASP A 1 152 ? 16.440 3.630  31.007 1.00 16.07 ? 143 ASP A C      1 
ATOM   1037 O O      . ASP A 1 152 ? 15.434 2.927  31.141 1.00 18.50 ? 143 ASP A O      1 
ATOM   1038 C CB     . ASP A 1 152 ? 17.895 2.107  32.422 1.00 15.21 ? 143 ASP A CB     1 
ATOM   1039 C CG     . ASP A 1 152 ? 17.655 2.866  33.719 1.00 19.80 ? 143 ASP A CG     1 
ATOM   1040 O OD1    . ASP A 1 152 ? 17.381 4.075  33.694 1.00 19.55 ? 143 ASP A OD1    1 
ATOM   1041 O OD2    . ASP A 1 152 ? 17.762 2.215  34.783 1.00 22.77 ? 143 ASP A OD2    1 
ATOM   1042 N N      . GLY A 1 153 ? 16.385 4.954  30.746 1.00 16.79 ? 144 GLY A N      1 
ATOM   1043 C CA     . GLY A 1 153 ? 15.144 5.679  30.592 1.00 20.61 ? 144 GLY A CA     1 
ATOM   1044 C C      . GLY A 1 153 ? 14.519 6.178  31.876 1.00 19.81 ? 144 GLY A C      1 
ATOM   1045 O O      . GLY A 1 153 ? 13.453 6.809  31.803 1.00 25.27 ? 144 GLY A O      1 
ATOM   1046 N N      . THR A 1 154 ? 15.077 5.845  33.042 1.00 16.05 ? 145 THR A N      1 
ATOM   1047 C CA     . THR A 1 154 ? 14.617 6.447  34.278 1.00 17.41 ? 145 THR A CA     1 
ATOM   1048 C C      . THR A 1 154 ? 15.242 7.823  34.434 1.00 16.43 ? 145 THR A C      1 
ATOM   1049 O O      . THR A 1 154 ? 16.079 8.244  33.652 1.00 15.81 ? 145 THR A O      1 
ATOM   1050 C CB     . THR A 1 154 ? 14.991 5.597  35.479 1.00 18.76 ? 145 THR A CB     1 
ATOM   1051 O OG1    . THR A 1 154 ? 16.410 5.561  35.663 1.00 20.73 ? 145 THR A OG1    1 
ATOM   1052 C CG2    . THR A 1 154 ? 14.422 4.164  35.352 1.00 25.32 ? 145 THR A CG2    1 
ATOM   1053 N N      . HIS A 1 155 ? 14.866 8.511  35.513 1.00 17.24 ? 146 HIS A N      1 
ATOM   1054 C CA     . HIS A 1 155 ? 15.387 9.844  35.782 1.00 16.06 ? 146 HIS A CA     1 
ATOM   1055 C C      . HIS A 1 155 ? 16.113 9.798  37.105 1.00 21.51 ? 146 HIS A C      1 
ATOM   1056 O O      . HIS A 1 155 ? 15.601 9.253  38.077 1.00 24.64 ? 146 HIS A O      1 
ATOM   1057 C CB     . HIS A 1 155 ? 14.263 10.871 35.751 1.00 18.40 ? 146 HIS A CB     1 
ATOM   1058 C CG     . HIS A 1 155 ? 13.813 11.162 34.359 1.00 20.99 ? 146 HIS A CG     1 
ATOM   1059 N ND1    . HIS A 1 155 ? 14.301 12.213 33.611 1.00 32.12 ? 146 HIS A ND1    1 
ATOM   1060 C CD2    . HIS A 1 155 ? 13.001 10.464 33.538 1.00 26.21 ? 146 HIS A CD2    1 
ATOM   1061 C CE1    . HIS A 1 155 ? 13.759 12.178 32.405 1.00 31.34 ? 146 HIS A CE1    1 
ATOM   1062 N NE2    . HIS A 1 155 ? 12.971 11.122 32.333 1.00 35.99 ? 146 HIS A NE2    1 
ATOM   1063 N N      . GLY A 1 156 ? 17.346 10.289 37.119 1.00 16.62 ? 147 GLY A N      1 
ATOM   1064 C CA     . GLY A 1 156 ? 18.212 10.171 38.269 1.00 16.11 ? 147 GLY A CA     1 
ATOM   1065 C C      . GLY A 1 156 ? 18.574 11.537 38.854 1.00 15.36 ? 147 GLY A C      1 
ATOM   1066 O O      . GLY A 1 156 ? 18.134 12.581 38.395 1.00 15.14 ? 147 GLY A O      1 
ATOM   1067 N N      . ILE A 1 157 ? 19.433 11.474 39.841 1.00 16.74 ? 148 ILE A N      1 
ATOM   1068 C CA     . ILE A 1 157 ? 19.868 12.639 40.607 1.00 16.96 ? 148 ILE A CA     1 
ATOM   1069 C C      . ILE A 1 157 ? 21.186 13.153 40.082 1.00 14.40 ? 148 ILE A C      1 
ATOM   1070 O O      . ILE A 1 157 ? 22.175 12.410 40.002 1.00 16.61 ? 148 ILE A O      1 
ATOM   1071 C CB     . ILE A 1 157 ? 19.980 12.288 42.104 1.00 20.68 ? 148 ILE A CB     1 
ATOM   1072 C CG1    . ILE A 1 157 ? 18.779 11.480 42.541 1.00 23.91 ? 148 ILE A CG1    1 
ATOM   1073 C CG2    . ILE A 1 157 ? 20.364 13.496 42.987 1.00 17.23 ? 148 ILE A CG2    1 
ATOM   1074 C CD1    . ILE A 1 157 ? 17.575 12.357 42.537 1.00 30.33 ? 148 ILE A CD1    1 
ATOM   1075 N N      . TYR A 1 158 ? 21.232 14.475 39.806 1.00 14.27 ? 149 TYR A N      1 
ATOM   1076 C CA     . TYR A 1 158 ? 22.517 15.068 39.460 1.00 14.35 ? 149 TYR A CA     1 
ATOM   1077 C C      . TYR A 1 158 ? 23.455 15.067 40.665 1.00 14.38 ? 149 TYR A C      1 
ATOM   1078 O O      . TYR A 1 158 ? 23.066 15.532 41.752 1.00 16.17 ? 149 TYR A O      1 
ATOM   1079 C CB     . TYR A 1 158 ? 22.313 16.523 39.013 1.00 14.72 ? 149 TYR A CB     1 
ATOM   1080 C CG     . TYR A 1 158 ? 21.641 16.695 37.649 1.00 13.02 ? 149 TYR A CG     1 
ATOM   1081 C CD1    . TYR A 1 158 ? 22.349 16.448 36.476 1.00 12.18 ? 149 TYR A CD1    1 
ATOM   1082 C CD2    . TYR A 1 158 ? 20.320 17.089 37.554 1.00 12.33 ? 149 TYR A CD2    1 
ATOM   1083 C CE1    . TYR A 1 158 ? 21.718 16.656 35.205 1.00 12.36 ? 149 TYR A CE1    1 
ATOM   1084 C CE2    . TYR A 1 158 ? 19.682 17.260 36.344 1.00 14.12 ? 149 TYR A CE2    1 
ATOM   1085 C CZ     . TYR A 1 158 ? 20.415 17.047 35.176 1.00 13.23 ? 149 TYR A CZ     1 
ATOM   1086 O OH     . TYR A 1 158 ? 19.720 17.224 33.963 1.00 15.56 ? 149 TYR A OH     1 
ATOM   1087 N N      . PRO A 1 159 ? 24.701 14.672 40.490 1.00 15.27 ? 150 PRO A N      1 
ATOM   1088 C CA     . PRO A 1 159 ? 25.643 14.588 41.609 1.00 14.78 ? 150 PRO A CA     1 
ATOM   1089 C C      . PRO A 1 159 ? 26.370 15.907 41.806 1.00 14.71 ? 150 PRO A C      1 
ATOM   1090 O O      . PRO A 1 159 ? 26.256 16.841 41.010 1.00 15.79 ? 150 PRO A O      1 
ATOM   1091 C CB     . PRO A 1 159 ? 26.615 13.510 41.145 1.00 18.18 ? 150 PRO A CB     1 
ATOM   1092 C CG     . PRO A 1 159 ? 26.729 13.821 39.599 1.00 16.50 ? 150 PRO A CG     1 
ATOM   1093 C CD     . PRO A 1 159 ? 25.276 14.116 39.233 1.00 15.96 ? 150 PRO A CD     1 
ATOM   1094 N N      . LYS A 1 160 ? 27.083 15.983 42.929 1.00 16.68 ? 151 LYS A N      1 
ATOM   1095 C CA     . LYS A 1 160 ? 28.003 17.095 43.182 1.00 16.91 ? 151 LYS A CA     1 
ATOM   1096 C C      . LYS A 1 160 ? 29.116 17.115 42.132 1.00 14.70 ? 151 LYS A C      1 
ATOM   1097 O O      . LYS A 1 160 ? 29.825 16.118 41.959 1.00 16.76 ? 151 LYS A O      1 
ATOM   1098 C CB     . LYS A 1 160 ? 28.630 16.869 44.562 1.00 20.54 ? 151 LYS A CB     1 
ATOM   1099 C CG     . LYS A 1 160 ? 29.353 18.108 45.032 1.00 22.20 ? 151 LYS A CG     1 
ATOM   1100 C CD     . LYS A 1 160 ? 29.723 17.967 46.486 1.00 22.30 ? 151 LYS A CD     1 
ATOM   1101 C CE     . LYS A 1 160 ? 30.891 17.009 46.684 1.00 36.68 ? 151 LYS A CE     1 
ATOM   1102 N NZ     . LYS A 1 160 ? 31.173 16.866 48.200 1.00 43.94 ? 151 LYS A NZ     1 
ATOM   1103 N N      . PRO A 1 161 ? 29.331 18.235 41.449 1.00 13.79 ? 152 PRO A N      1 
ATOM   1104 C CA     . PRO A 1 161 ? 30.446 18.334 40.513 1.00 12.88 ? 152 PRO A CA     1 
ATOM   1105 C C      . PRO A 1 161 ? 31.720 18.751 41.238 1.00 15.13 ? 152 PRO A C      1 
ATOM   1106 O O      . PRO A 1 161 ? 31.704 19.145 42.412 1.00 17.36 ? 152 PRO A O      1 
ATOM   1107 C CB     . PRO A 1 161 ? 29.989 19.441 39.537 1.00 16.63 ? 152 PRO A CB     1 
ATOM   1108 C CG     . PRO A 1 161 ? 29.187 20.417 40.470 1.00 13.46 ? 152 PRO A CG     1 
ATOM   1109 C CD     . PRO A 1 161 ? 28.469 19.441 41.449 1.00 14.36 ? 152 PRO A CD     1 
ATOM   1110 N N      . ARG A 1 162 ? 32.832 18.663 40.508 1.00 14.91 ? 153 ARG A N      1 
ATOM   1111 C CA     . ARG A 1 162 ? 34.122 19.178 40.951 1.00 15.55 ? 153 ARG A CA     1 
ATOM   1112 C C      . ARG A 1 162 ? 34.380 20.543 40.287 1.00 13.45 ? 153 ARG A C      1 
ATOM   1113 O O      . ARG A 1 162 ? 34.283 20.668 39.053 1.00 14.64 ? 153 ARG A O      1 
ATOM   1114 C CB     . ARG A 1 162 ? 35.179 18.149 40.528 1.00 19.14 ? 153 ARG A CB     1 
ATOM   1115 C CG     . ARG A 1 162 ? 36.610 18.485 40.797 1.00 22.89 ? 153 ARG A CG     1 
ATOM   1116 C CD     . ARG A 1 162 ? 37.504 17.234 40.508 1.00 21.25 ? 153 ARG A CD     1 
ATOM   1117 N NE     . ARG A 1 162 ? 37.570 16.802 39.111 1.00 22.24 ? 153 ARG A NE     1 
ATOM   1118 C CZ     . ARG A 1 162 ? 38.290 17.431 38.187 1.00 18.53 ? 153 ARG A CZ     1 
ATOM   1119 N NH1    . ARG A 1 162 ? 38.959 18.512 38.483 1.00 21.70 ? 153 ARG A NH1    1 
ATOM   1120 N NH2    . ARG A 1 162 ? 38.355 16.938 36.953 1.00 19.24 ? 153 ARG A NH2    1 
ATOM   1121 N N      . ALA A 1 163 ? 34.664 21.581 41.088 1.00 14.73 ? 154 ALA A N      1 
ATOM   1122 C CA     . ALA A 1 163 ? 34.969 22.894 40.554 1.00 14.77 ? 154 ALA A CA     1 
ATOM   1123 C C      . ALA A 1 163 ? 36.387 22.868 40.032 1.00 17.46 ? 154 ALA A C      1 
ATOM   1124 O O      . ALA A 1 163 ? 37.308 22.502 40.755 1.00 21.56 ? 154 ALA A O      1 
ATOM   1125 C CB     . ALA A 1 163 ? 34.829 23.939 41.664 1.00 16.95 ? 154 ALA A CB     1 
ATOM   1126 N N      . ILE A 1 164 ? 36.576 23.235 38.791 1.00 13.78 ? 155 ILE A N      1 
ATOM   1127 C CA     . ILE A 1 164 ? 37.904 23.118 38.186 1.00 12.88 ? 155 ILE A CA     1 
ATOM   1128 C C      . ILE A 1 164 ? 38.734 24.364 38.407 1.00 13.34 ? 155 ILE A C      1 
ATOM   1129 O O      . ILE A 1 164 ? 38.225 25.501 38.489 1.00 13.83 ? 155 ILE A O      1 
ATOM   1130 C CB     . ILE A 1 164 ? 37.786 22.793 36.689 1.00 12.66 ? 155 ILE A CB     1 
ATOM   1131 C CG1    . ILE A 1 164 ? 37.015 23.858 35.924 1.00 13.50 ? 155 ILE A CG1    1 
ATOM   1132 C CG2    . ILE A 1 164 ? 37.173 21.413 36.546 1.00 17.52 ? 155 ILE A CG2    1 
ATOM   1133 C CD1    . ILE A 1 164 ? 37.066 23.558 34.400 1.00 14.23 ? 155 ILE A CD1    1 
ATOM   1134 N N      . GLY A 1 165 ? 40.043 24.149 38.480 1.00 12.09 ? 156 GLY A N      1 
ATOM   1135 C CA     . GLY A 1 165 ? 40.992 25.249 38.546 1.00 12.73 ? 156 GLY A CA     1 
ATOM   1136 C C      . GLY A 1 165 ? 41.258 25.849 37.173 1.00 11.37 ? 156 GLY A C      1 
ATOM   1137 O O      . GLY A 1 165 ? 40.755 25.384 36.141 1.00 11.92 ? 156 GLY A O      1 
ATOM   1138 N N      . THR A 1 166 ? 42.067 26.928 37.146 1.00 11.85 ? 157 THR A N      1 
ATOM   1139 C CA     . THR A 1 166 ? 42.219 27.649 35.895 1.00 10.50 ? 157 THR A CA     1 
ATOM   1140 C C      . THR A 1 166 ? 43.098 26.911 34.883 1.00 11.56 ? 157 THR A C      1 
ATOM   1141 O O      . THR A 1 166 ? 42.851 27.036 33.674 1.00 12.01 ? 157 THR A O      1 
ATOM   1142 C CB     . THR A 1 166 ? 42.662 29.104 36.089 1.00 11.66 ? 157 THR A CB     1 
ATOM   1143 O OG1    . THR A 1 166 ? 43.999 29.084 36.623 1.00 12.28 ? 157 THR A OG1    1 
ATOM   1144 C CG2    . THR A 1 166 ? 41.711 29.805 37.051 1.00 12.78 ? 157 THR A CG2    1 
ATOM   1145 N N      . TYR A 1 167 ? 44.050 26.053 35.356 1.00 11.85 ? 158 TYR A N      1 
ATOM   1146 C CA     . TYR A 1 167 ? 44.747 25.249 34.370 1.00 12.48 ? 158 TYR A CA     1 
ATOM   1147 C C      . TYR A 1 167 ? 43.764 24.312 33.688 1.00 10.95 ? 158 TYR A C      1 
ATOM   1148 O O      . TYR A 1 167 ? 43.796 24.149 32.457 1.00 12.00 ? 158 TYR A O      1 
ATOM   1149 C CB     . TYR A 1 167 ? 45.879 24.470 35.037 1.00 13.36 ? 158 TYR A CB     1 
ATOM   1150 C CG     . TYR A 1 167 ? 46.510 23.485 34.075 1.00 13.37 ? 158 TYR A CG     1 
ATOM   1151 C CD1    . TYR A 1 167 ? 47.239 23.933 32.995 1.00 13.87 ? 158 TYR A CD1    1 
ATOM   1152 C CD2    . TYR A 1 167 ? 46.318 22.130 34.256 1.00 12.41 ? 158 TYR A CD2    1 
ATOM   1153 C CE1    . TYR A 1 167 ? 47.795 23.037 32.119 1.00 15.38 ? 158 TYR A CE1    1 
ATOM   1154 C CE2    . TYR A 1 167 ? 46.899 21.186 33.384 1.00 13.74 ? 158 TYR A CE2    1 
ATOM   1155 C CZ     . TYR A 1 167 ? 47.633 21.683 32.311 1.00 14.68 ? 158 TYR A CZ     1 
ATOM   1156 O OH     . TYR A 1 167 ? 48.241 20.792 31.418 1.00 18.03 ? 158 TYR A OH     1 
ATOM   1157 N N      . GLU A 1 168 ? 42.910 23.663 34.470 1.00 11.65 ? 159 GLU A N      1 
ATOM   1158 C CA     . GLU A 1 168 ? 41.937 22.756 33.857 1.00 11.69 ? 159 GLU A CA     1 
ATOM   1159 C C      . GLU A 1 168 ? 40.970 23.514 32.938 1.00 11.13 ? 159 GLU A C      1 
ATOM   1160 O O      . GLU A 1 168 ? 40.618 22.996 31.862 1.00 11.53 ? 159 GLU A O      1 
ATOM   1161 C CB     . GLU A 1 168 ? 41.164 21.989 34.925 1.00 13.58 ? 159 GLU A CB     1 
ATOM   1162 C CG     . GLU A 1 168 ? 40.546 20.774 34.306 1.00 18.69 ? 159 GLU A CG     1 
ATOM   1163 C CD     . GLU A 1 168 ? 39.970 19.820 35.335 1.00 24.60 ? 159 GLU A CD     1 
ATOM   1164 O OE1    . GLU A 1 168 ? 40.524 19.674 36.469 1.00 22.84 ? 159 GLU A OE1    1 
ATOM   1165 O OE2    . GLU A 1 168 ? 39.163 18.969 34.874 1.00 20.57 ? 159 GLU A OE2    1 
ATOM   1166 N N      . ILE A 1 169 ? 40.575 24.747 33.290 1.00 11.59 ? 160 ILE A N      1 
ATOM   1167 C CA     . ILE A 1 169 ? 39.827 25.572 32.325 1.00 11.88 ? 160 ILE A CA     1 
ATOM   1168 C C      . ILE A 1 169 ? 40.557 25.664 30.999 1.00 11.04 ? 160 ILE A C      1 
ATOM   1169 O O      . ILE A 1 169 ? 39.964 25.452 29.940 1.00 11.96 ? 160 ILE A O      1 
ATOM   1170 C CB     . ILE A 1 169 ? 39.535 26.957 32.922 1.00 11.97 ? 160 ILE A CB     1 
ATOM   1171 C CG1    . ILE A 1 169 ? 38.509 26.821 34.028 1.00 14.39 ? 160 ILE A CG1    1 
ATOM   1172 C CG2    . ILE A 1 169 ? 39.002 27.882 31.839 1.00 14.62 ? 160 ILE A CG2    1 
ATOM   1173 C CD1    . ILE A 1 169 ? 38.320 28.143 34.796 1.00 13.61 ? 160 ILE A CD1    1 
ATOM   1174 N N      . SER A 1 170 ? 41.873 25.960 31.022 1.00 11.46 ? 161 SER A N      1 
ATOM   1175 C CA     . SER A 1 170 ? 42.623 26.077 29.768 1.00 11.85 ? 161 SER A CA     1 
ATOM   1176 C C      . SER A 1 170 ? 42.691 24.737 29.008 1.00 11.73 ? 161 SER A C      1 
ATOM   1177 O O      . SER A 1 170 ? 42.717 24.724 27.772 1.00 13.22 ? 161 SER A O      1 
ATOM   1178 C CB     . SER A 1 170 ? 44.031 26.669 30.037 1.00 12.03 ? 161 SER A CB     1 
ATOM   1179 O OG     . SER A 1 170 ? 44.930 25.693 30.654 1.00 13.85 ? 161 SER A OG     1 
ATOM   1180 N N      . GLN A 1 171 ? 42.657 23.620 29.726 1.00 10.31 ? 162 GLN A N      1 
ATOM   1181 C CA     . GLN A 1 171 ? 42.601 22.306 29.064 1.00 11.91 ? 162 GLN A CA     1 
ATOM   1182 C C      . GLN A 1 171 ? 41.259 22.101 28.374 1.00 11.56 ? 162 GLN A C      1 
ATOM   1183 O O      . GLN A 1 171 ? 41.198 21.494 27.283 1.00 12.27 ? 162 GLN A O      1 
ATOM   1184 C CB     . GLN A 1 171 ? 42.844 21.183 30.076 1.00 13.93 ? 162 GLN A CB     1 
ATOM   1185 C CG     . GLN A 1 171 ? 44.240 21.122 30.722 1.00 15.21 ? 162 GLN A CG     1 
ATOM   1186 C CD     . GLN A 1 171 ? 44.275 19.937 31.649 1.00 17.43 ? 162 GLN A CD     1 
ATOM   1187 O OE1    . GLN A 1 171 ? 43.589 19.889 32.710 1.00 21.78 ? 162 GLN A OE1    1 
ATOM   1188 N NE2    . GLN A 1 171 ? 45.050 18.928 31.250 1.00 21.15 ? 162 GLN A NE2    1 
ATOM   1189 N N      . VAL A 1 172 ? 40.160 22.522 29.026 1.00 11.58 ? 163 VAL A N      1 
ATOM   1190 C CA     . VAL A 1 172 ? 38.874 22.385 28.362 1.00 11.63 ? 163 VAL A CA     1 
ATOM   1191 C C      . VAL A 1 172 ? 38.834 23.248 27.103 1.00 11.36 ? 163 VAL A C      1 
ATOM   1192 O O      . VAL A 1 172 ? 38.272 22.840 26.081 1.00 12.07 ? 163 VAL A O      1 
ATOM   1193 C CB     . VAL A 1 172 ? 37.756 22.722 29.354 1.00 11.88 ? 163 VAL A CB     1 
ATOM   1194 C CG1    . VAL A 1 172 ? 36.419 22.716 28.597 1.00 13.95 ? 163 VAL A CG1    1 
ATOM   1195 C CG2    . VAL A 1 172 ? 37.743 21.778 30.559 1.00 13.39 ? 163 VAL A CG2    1 
ATOM   1196 N N      . VAL A 1 173 ? 39.377 24.478 27.179 1.00 11.43 ? 164 VAL A N      1 
ATOM   1197 C CA     . VAL A 1 173 ? 39.456 25.317 25.990 1.00 10.22 ? 164 VAL A CA     1 
ATOM   1198 C C      . VAL A 1 173 ? 40.183 24.580 24.875 1.00 10.69 ? 164 VAL A C      1 
ATOM   1199 O O      . VAL A 1 173 ? 39.728 24.578 23.718 1.00 12.44 ? 164 VAL A O      1 
ATOM   1200 C CB     . VAL A 1 173 ? 40.140 26.651 26.326 1.00 11.99 ? 164 VAL A CB     1 
ATOM   1201 C CG1    . VAL A 1 173 ? 40.446 27.435 25.056 1.00 12.99 ? 164 VAL A CG1    1 
ATOM   1202 C CG2    . VAL A 1 173 ? 39.272 27.514 27.271 1.00 12.75 ? 164 VAL A CG2    1 
ATOM   1203 N N      . GLU A 1 174 ? 41.295 23.902 25.214 1.00 11.48 ? 165 GLU A N      1 
ATOM   1204 C CA     . GLU A 1 174 ? 41.998 23.121 24.198 1.00 12.76 ? 165 GLU A CA     1 
ATOM   1205 C C      . GLU A 1 174 ? 41.139 21.985 23.647 1.00 11.77 ? 165 GLU A C      1 
ATOM   1206 O O      . GLU A 1 174 ? 41.262 21.645 22.458 1.00 12.66 ? 165 GLU A O      1 
ATOM   1207 C CB     . GLU A 1 174 ? 43.328 22.633 24.791 1.00 14.36 ? 165 GLU A CB     1 
ATOM   1208 C CG     . GLU A 1 174 ? 44.140 21.758 23.816 1.00 15.16 ? 165 GLU A CG     1 
ATOM   1209 C CD     . GLU A 1 174 ? 44.675 22.534 22.594 1.00 20.55 ? 165 GLU A CD     1 
ATOM   1210 O OE1    . GLU A 1 174 ? 44.532 23.758 22.478 1.00 22.09 ? 165 GLU A OE1    1 
ATOM   1211 O OE2    . GLU A 1 174 ? 45.191 21.859 21.660 1.00 21.41 ? 165 GLU A OE2    1 
ATOM   1212 N N      . ASP A 1 175 ? 40.284 21.373 24.474 1.00 11.62 ? 166 ASP A N      1 
ATOM   1213 C CA     . ASP A 1 175 ? 39.409 20.321 23.933 1.00 11.02 ? 166 ASP A CA     1 
ATOM   1214 C C      . ASP A 1 175 ? 38.433 20.915 22.923 1.00 11.30 ? 166 ASP A C      1 
ATOM   1215 O O      . ASP A 1 175 ? 38.141 20.299 21.876 1.00 11.83 ? 166 ASP A O      1 
ATOM   1216 C CB     . ASP A 1 175 ? 38.597 19.672 25.054 1.00 11.16 ? 166 ASP A CB     1 
ATOM   1217 C CG     . ASP A 1 175 ? 39.408 18.715 25.932 1.00 17.58 ? 166 ASP A CG     1 
ATOM   1218 O OD1    . ASP A 1 175 ? 40.287 17.972 25.394 1.00 21.71 ? 166 ASP A OD1    1 
ATOM   1219 O OD2    . ASP A 1 175 ? 39.098 18.646 27.182 1.00 18.61 ? 166 ASP A OD2    1 
ATOM   1220 N N      . TYR A 1 176 ? 37.915 22.131 23.173 1.00 11.39 ? 167 TYR A N      1 
ATOM   1221 C CA     . TYR A 1 176 ? 37.111 22.794 22.147 1.00 10.83 ? 167 TYR A CA     1 
ATOM   1222 C C      . TYR A 1 176 ? 37.921 23.013 20.868 1.00 10.80 ? 167 TYR A C      1 
ATOM   1223 O O      . TYR A 1 176 ? 37.418 22.750 19.764 1.00 11.67 ? 167 TYR A O      1 
ATOM   1224 C CB     . TYR A 1 176 ? 36.551 24.125 22.649 1.00 11.64 ? 167 TYR A CB     1 
ATOM   1225 C CG     . TYR A 1 176 ? 35.328 24.044 23.553 1.00 10.32 ? 167 TYR A CG     1 
ATOM   1226 C CD1    . TYR A 1 176 ? 34.044 23.863 23.013 1.00 11.69 ? 167 TYR A CD1    1 
ATOM   1227 C CD2    . TYR A 1 176 ? 35.460 24.198 24.912 1.00 10.15 ? 167 TYR A CD2    1 
ATOM   1228 C CE1    . TYR A 1 176 ? 32.926 23.828 23.835 1.00 11.00 ? 167 TYR A CE1    1 
ATOM   1229 C CE2    . TYR A 1 176 ? 34.371 24.136 25.736 1.00 11.44 ? 167 TYR A CE2    1 
ATOM   1230 C CZ     . TYR A 1 176 ? 33.108 23.993 25.179 1.00 10.50 ? 167 TYR A CZ     1 
ATOM   1231 O OH     . TYR A 1 176 ? 31.994 23.976 26.014 1.00 11.98 ? 167 TYR A OH     1 
ATOM   1232 N N      . ARG A 1 177 ? 39.171 23.485 21.016 1.00 12.14 ? 168 ARG A N      1 
ATOM   1233 C CA     . ARG A 1 177 ? 39.987 23.804 19.857 1.00 12.57 ? 168 ARG A CA     1 
ATOM   1234 C C      . ARG A 1 177 ? 40.247 22.551 19.034 1.00 11.95 ? 168 ARG A C      1 
ATOM   1235 O O      . ARG A 1 177 ? 40.109 22.578 17.795 1.00 11.82 ? 168 ARG A O      1 
ATOM   1236 C CB     . ARG A 1 177 ? 41.280 24.480 20.325 1.00 11.73 ? 168 ARG A CB     1 
ATOM   1237 C CG     . ARG A 1 177 ? 42.001 25.090 19.141 1.00 15.15 ? 168 ARG A CG     1 
ATOM   1238 C CD     . ARG A 1 177 ? 43.307 25.680 19.616 1.00 20.63 ? 168 ARG A CD     1 
ATOM   1239 N NE     . ARG A 1 177 ? 44.199 24.563 19.778 1.00 20.17 ? 168 ARG A NE     1 
ATOM   1240 C CZ     . ARG A 1 177 ? 44.931 24.045 18.801 1.00 23.40 ? 168 ARG A CZ     1 
ATOM   1241 N NH1    . ARG A 1 177 ? 45.037 24.653 17.622 1.00 23.92 ? 168 ARG A NH1    1 
ATOM   1242 N NH2    . ARG A 1 177 ? 45.555 22.893 19.012 1.00 24.01 ? 168 ARG A NH2    1 
ATOM   1243 N N      . ARG A 1 178 ? 40.611 21.453 19.701 1.00 11.87 ? 169 ARG A N      1 
ATOM   1244 C CA     . ARG A 1 178 ? 40.896 20.207 18.980 1.00 11.48 ? 169 ARG A CA     1 
ATOM   1245 C C      . ARG A 1 178 ? 39.643 19.646 18.341 1.00 12.69 ? 169 ARG A C      1 
ATOM   1246 O O      . ARG A 1 178 ? 39.690 19.087 17.237 1.00 12.68 ? 169 ARG A O      1 
ATOM   1247 C CB     . ARG A 1 178 ? 41.509 19.153 19.903 1.00 13.42 ? 169 ARG A CB     1 
ATOM   1248 C CG     . ARG A 1 178 ? 42.945 19.515 20.243 1.00 18.60 ? 169 ARG A CG     1 
ATOM   1249 C CD     . ARG A 1 178 ? 43.542 18.640 21.265 1.00 28.95 ? 169 ARG A CD     1 
ATOM   1250 N NE     . ARG A 1 178 ? 44.912 19.092 21.511 1.00 27.56 ? 169 ARG A NE     1 
ATOM   1251 C CZ     . ARG A 1 178 ? 45.860 18.363 22.088 1.00 46.76 ? 169 ARG A CZ     1 
ATOM   1252 N NH1    . ARG A 1 178 ? 45.637 17.108 22.458 1.00 33.99 ? 169 ARG A NH1    1 
ATOM   1253 N NH2    . ARG A 1 178 ? 47.048 18.922 22.333 1.00 39.49 ? 169 ARG A NH2    1 
ATOM   1254 N N      . SER A 1 179 ? 38.496 19.769 19.022 1.00 11.67 ? 170 SER A N      1 
ATOM   1255 C CA     . SER A 1 179 ? 37.262 19.298 18.425 1.00 11.83 ? 170 SER A CA     1 
ATOM   1256 C C      . SER A 1 179 ? 36.883 20.110 17.207 1.00 12.23 ? 170 SER A C      1 
ATOM   1257 O O      . SER A 1 179 ? 36.323 19.551 16.251 1.00 11.84 ? 170 SER A O      1 
ATOM   1258 C CB     . SER A 1 179 ? 36.151 19.295 19.474 1.00 11.52 ? 170 SER A CB     1 
ATOM   1259 O OG     . SER A 1 179 ? 36.391 18.303 20.438 1.00 14.96 ? 170 SER A OG     1 
ATOM   1260 N N      . ALA A 1 180 ? 37.139 21.420 17.227 1.00 11.76 ? 171 ALA A N      1 
ATOM   1261 C CA     . ALA A 1 180 ? 36.817 22.253 16.064 1.00 11.53 ? 171 ALA A CA     1 
ATOM   1262 C C      . ALA A 1 180 ? 37.670 21.837 14.872 1.00 11.58 ? 171 ALA A C      1 
ATOM   1263 O O      . ALA A 1 180 ? 37.172 21.747 13.741 1.00 12.11 ? 171 ALA A O      1 
ATOM   1264 C CB     . ALA A 1 180 ? 37.023 23.724 16.364 1.00 11.47 ? 171 ALA A CB     1 
ATOM   1265 N N      . LEU A 1 181 ? 38.957 21.558 15.129 1.00 12.08 ? 172 LEU A N      1 
ATOM   1266 C CA     . LEU A 1 181 ? 39.831 21.114 14.034 1.00 11.91 ? 172 LEU A CA     1 
ATOM   1267 C C      . LEU A 1 181 ? 39.355 19.773 13.517 1.00 13.20 ? 172 LEU A C      1 
ATOM   1268 O O      . LEU A 1 181 ? 39.370 19.538 12.300 1.00 13.93 ? 172 LEU A O      1 
ATOM   1269 C CB     . LEU A 1 181 ? 41.255 20.998 14.563 1.00 12.99 ? 172 LEU A CB     1 
ATOM   1270 C CG     . LEU A 1 181 ? 41.910 22.373 14.740 1.00 14.90 ? 172 LEU A CG     1 
ATOM   1271 C CD1    . LEU A 1 181 ? 43.163 22.149 15.570 1.00 17.60 ? 172 LEU A CD1    1 
ATOM   1272 C CD2    . LEU A 1 181 ? 42.266 22.974 13.377 1.00 15.06 ? 172 LEU A CD2    1 
ATOM   1273 N N      . ASN A 1 182 ? 38.896 18.872 14.401 1.00 11.60 ? 173 ASN A N      1 
ATOM   1274 C CA     . ASN A 1 182 ? 38.366 17.578 13.961 1.00 12.12 ? 173 ASN A CA     1 
ATOM   1275 C C      . ASN A 1 182 ? 37.084 17.742 13.141 1.00 12.70 ? 173 ASN A C      1 
ATOM   1276 O O      . ASN A 1 182 ? 36.850 17.018 12.173 1.00 12.85 ? 173 ASN A O      1 
ATOM   1277 C CB     . ASN A 1 182 ? 38.087 16.712 15.198 1.00 12.83 ? 173 ASN A CB     1 
ATOM   1278 C CG     . ASN A 1 182 ? 39.288 15.996 15.702 1.00 18.34 ? 173 ASN A CG     1 
ATOM   1279 O OD1    . ASN A 1 182 ? 40.382 16.068 15.159 1.00 18.75 ? 173 ASN A OD1    1 
ATOM   1280 N ND2    . ASN A 1 182 ? 39.095 15.308 16.803 1.00 19.22 ? 173 ASN A ND2    1 
ATOM   1281 N N      . ALA A 1 183 ? 36.240 18.704 13.502 1.00 11.04 ? 174 ALA A N      1 
ATOM   1282 C CA     . ALA A 1 183 ? 35.048 18.938 12.701 1.00 11.25 ? 174 ALA A CA     1 
ATOM   1283 C C      . ALA A 1 183 ? 35.419 19.372 11.299 1.00 11.67 ? 174 ALA A C      1 
ATOM   1284 O O      . ALA A 1 183 ? 34.777 18.924 10.341 1.00 11.95 ? 174 ALA A O      1 
ATOM   1285 C CB     . ALA A 1 183 ? 34.163 20.021 13.340 1.00 12.42 ? 174 ALA A CB     1 
ATOM   1286 N N      . ILE A 1 184 ? 36.419 20.264 11.167 1.00 12.30 ? 175 ILE A N      1 
ATOM   1287 C CA     . ILE A 1 184 ? 36.854 20.679 9.827  1.00 14.09 ? 175 ILE A CA     1 
ATOM   1288 C C      . ILE A 1 184 ? 37.419 19.479 9.065  1.00 13.65 ? 175 ILE A C      1 
ATOM   1289 O O      . ILE A 1 184 ? 37.139 19.307 7.866  1.00 15.01 ? 175 ILE A O      1 
ATOM   1290 C CB     . ILE A 1 184 ? 37.850 21.848 9.941  1.00 15.15 ? 175 ILE A CB     1 
ATOM   1291 C CG1    . ILE A 1 184 ? 37.189 23.132 10.462 1.00 16.87 ? 175 ILE A CG1    1 
ATOM   1292 C CG2    . ILE A 1 184 ? 38.558 22.078 8.567  1.00 16.20 ? 175 ILE A CG2    1 
ATOM   1293 C CD1    . ILE A 1 184 ? 35.872 23.512 9.829  1.00 18.99 ? 175 ILE A CD1    1 
ATOM   1294 N N      . GLU A 1 185 ? 38.149 18.587 9.762  1.00 13.03 ? 176 GLU A N      1 
ATOM   1295 C CA     . GLU A 1 185 ? 38.682 17.372 9.106  1.00 12.86 ? 176 GLU A CA     1 
ATOM   1296 C C      . GLU A 1 185 ? 37.578 16.464 8.589  1.00 15.09 ? 176 GLU A C      1 
ATOM   1297 O O      . GLU A 1 185 ? 37.737 15.782 7.562  1.00 17.44 ? 176 GLU A O      1 
ATOM   1298 C CB     . GLU A 1 185 ? 39.599 16.625 10.106 1.00 15.19 ? 176 GLU A CB     1 
ATOM   1299 C CG     . GLU A 1 185 ? 40.324 15.413 9.494  1.00 20.33 ? 176 GLU A CG     1 
ATOM   1300 C CD     . GLU A 1 185 ? 41.147 14.654 10.536 1.00 33.66 ? 176 GLU A CD     1 
ATOM   1301 O OE1    . GLU A 1 185 ? 41.465 15.271 11.566 1.00 29.78 ? 176 GLU A OE1    1 
ATOM   1302 O OE2    . GLU A 1 185 ? 41.451 13.448 10.350 1.00 35.63 ? 176 GLU A OE2    1 
ATOM   1303 N N      . ALA A 1 186 ? 36.451 16.399 9.291  1.00 13.56 ? 177 ALA A N      1 
ATOM   1304 C CA     . ALA A 1 186 ? 35.307 15.619 8.845  1.00 12.18 ? 177 ALA A CA     1 
ATOM   1305 C C      . ALA A 1 186 ? 34.553 16.272 7.716  1.00 13.86 ? 177 ALA A C      1 
ATOM   1306 O O      . ALA A 1 186 ? 33.684 15.612 7.107  1.00 18.50 ? 177 ALA A O      1 
ATOM   1307 C CB     . ALA A 1 186 ? 34.345 15.433 10.018 1.00 13.14 ? 177 ALA A CB     1 
ATOM   1308 N N      . GLY A 1 187 ? 34.884 17.508 7.382  1.00 12.32 ? 178 GLY A N      1 
ATOM   1309 C CA     . GLY A 1 187 ? 34.252 18.208 6.290  1.00 13.96 ? 178 GLY A CA     1 
ATOM   1310 C C      . GLY A 1 187 ? 33.183 19.183 6.701  1.00 11.55 ? 178 GLY A C      1 
ATOM   1311 O O      . GLY A 1 187 ? 32.586 19.798 5.819  1.00 13.07 ? 178 GLY A O      1 
ATOM   1312 N N      . PHE A 1 188 ? 32.923 19.335 8.010  1.00 12.10 ? 179 PHE A N      1 
ATOM   1313 C CA     . PHE A 1 188 ? 31.909 20.320 8.396  1.00 11.56 ? 179 PHE A CA     1 
ATOM   1314 C C      . PHE A 1 188 ? 32.270 21.708 7.896  1.00 11.93 ? 179 PHE A C      1 
ATOM   1315 O O      . PHE A 1 188 ? 33.452 22.070 7.786  1.00 12.13 ? 179 PHE A O      1 
ATOM   1316 C CB     . PHE A 1 188 ? 31.801 20.368 9.933  1.00 11.05 ? 179 PHE A CB     1 
ATOM   1317 C CG     . PHE A 1 188 ? 30.973 19.241 10.520 1.00 9.74  ? 179 PHE A CG     1 
ATOM   1318 C CD1    . PHE A 1 188 ? 29.583 19.298 10.488 1.00 10.14 ? 179 PHE A CD1    1 
ATOM   1319 C CD2    . PHE A 1 188 ? 31.595 18.170 11.125 1.00 10.46 ? 179 PHE A CD2    1 
ATOM   1320 C CE1    . PHE A 1 188 ? 28.815 18.295 11.056 1.00 10.77 ? 179 PHE A CE1    1 
ATOM   1321 C CE2    . PHE A 1 188 ? 30.846 17.124 11.751 1.00 10.90 ? 179 PHE A CE2    1 
ATOM   1322 C CZ     . PHE A 1 188 ? 29.439 17.180 11.688 1.00 11.62 ? 179 PHE A CZ     1 
ATOM   1323 N N      . ASP A 1 189 ? 31.222 22.501 7.607  1.00 11.38 ? 180 ASP A N      1 
ATOM   1324 C CA     . ASP A 1 189 ? 31.468 23.865 7.152  1.00 11.02 ? 180 ASP A CA     1 
ATOM   1325 C C      . ASP A 1 189 ? 31.898 24.759 8.306  1.00 13.16 ? 180 ASP A C      1 
ATOM   1326 O O      . ASP A 1 189 ? 32.553 25.787 8.079  1.00 13.73 ? 180 ASP A O      1 
ATOM   1327 C CB     . ASP A 1 189 ? 30.198 24.397 6.519  1.00 11.87 ? 180 ASP A CB     1 
ATOM   1328 C CG     . ASP A 1 189 ? 29.824 23.579 5.285  1.00 13.97 ? 180 ASP A CG     1 
ATOM   1329 O OD1    . ASP A 1 189 ? 30.610 23.657 4.322  1.00 17.34 ? 180 ASP A OD1    1 
ATOM   1330 O OD2    . ASP A 1 189 ? 28.833 22.802 5.289  1.00 13.94 ? 180 ASP A OD2    1 
ATOM   1331 N N      . GLY A 1 190 ? 31.569 24.370 9.537  1.00 11.78 ? 181 GLY A N      1 
ATOM   1332 C CA     . GLY A 1 190 ? 31.949 25.149 10.691 1.00 11.18 ? 181 GLY A CA     1 
ATOM   1333 C C      . GLY A 1 190 ? 31.429 24.484 11.942 1.00 9.84  ? 181 GLY A C      1 
ATOM   1334 O O      . GLY A 1 190 ? 30.974 23.334 11.918 1.00 9.98  ? 181 GLY A O      1 
ATOM   1335 N N      . ILE A 1 191 ? 31.562 25.201 13.054 1.00 10.65 ? 182 ILE A N      1 
ATOM   1336 C CA     . ILE A 1 191 ? 31.102 24.675 14.338 1.00 10.62 ? 182 ILE A CA     1 
ATOM   1337 C C      . ILE A 1 191 ? 30.307 25.757 15.039 1.00 9.88  ? 182 ILE A C      1 
ATOM   1338 O O      . ILE A 1 191 ? 30.458 26.942 14.777 1.00 10.39 ? 182 ILE A O      1 
ATOM   1339 C CB     . ILE A 1 191 ? 32.264 24.208 15.245 1.00 10.63 ? 182 ILE A CB     1 
ATOM   1340 C CG1    . ILE A 1 191 ? 33.232 25.344 15.684 1.00 12.24 ? 182 ILE A CG1    1 
ATOM   1341 C CG2    . ILE A 1 191 ? 33.040 23.112 14.507 1.00 11.94 ? 182 ILE A CG2    1 
ATOM   1342 C CD1    . ILE A 1 191 ? 32.737 26.116 16.945 1.00 12.47 ? 182 ILE A CD1    1 
ATOM   1343 N N      . GLU A 1 192 ? 29.428 25.310 15.954 1.00 10.46 ? 183 GLU A N      1 
ATOM   1344 C CA     . GLU A 1 192 ? 28.695 26.199 16.856 1.00 9.95  ? 183 GLU A CA     1 
ATOM   1345 C C      . GLU A 1 192 ? 29.129 25.880 18.279 1.00 9.44  ? 183 GLU A C      1 
ATOM   1346 O O      . GLU A 1 192 ? 29.140 24.698 18.685 1.00 10.56 ? 183 GLU A O      1 
ATOM   1347 C CB     . GLU A 1 192 ? 27.192 25.973 16.694 1.00 9.84  ? 183 GLU A CB     1 
ATOM   1348 C CG     . GLU A 1 192 ? 26.391 26.912 17.657 1.00 10.69 ? 183 GLU A CG     1 
ATOM   1349 C CD     . GLU A 1 192 ? 24.897 26.781 17.493 1.00 11.62 ? 183 GLU A CD     1 
ATOM   1350 O OE1    . GLU A 1 192 ? 24.355 27.488 16.608 1.00 12.23 ? 183 GLU A OE1    1 
ATOM   1351 O OE2    . GLU A 1 192 ? 24.263 25.984 18.237 1.00 11.56 ? 183 GLU A OE2    1 
ATOM   1352 N N      . ILE A 1 193 ? 29.448 26.924 19.039 1.00 9.80  ? 184 ILE A N      1 
ATOM   1353 C CA     . ILE A 1 193 ? 29.760 26.767 20.454 1.00 10.00 ? 184 ILE A CA     1 
ATOM   1354 C C      . ILE A 1 193 ? 28.442 26.729 21.222 1.00 10.11 ? 184 ILE A C      1 
ATOM   1355 O O      . ILE A 1 193 ? 27.667 27.701 21.193 1.00 11.58 ? 184 ILE A O      1 
ATOM   1356 C CB     . ILE A 1 193 ? 30.655 27.906 20.947 1.00 10.62 ? 184 ILE A CB     1 
ATOM   1357 C CG1    . ILE A 1 193 ? 32.047 27.821 20.298 1.00 11.82 ? 184 ILE A CG1    1 
ATOM   1358 C CG2    . ILE A 1 193 ? 30.775 27.824 22.491 1.00 12.47 ? 184 ILE A CG2    1 
ATOM   1359 C CD1    . ILE A 1 193 ? 32.835 26.519 20.543 1.00 13.72 ? 184 ILE A CD1    1 
ATOM   1360 N N      . HIS A 1 194 ? 28.175 25.620 21.930 1.00 10.10 ? 185 HIS A N      1 
ATOM   1361 C CA     . HIS A 1 194 ? 26.958 25.522 22.769 1.00 11.06 ? 185 HIS A CA     1 
ATOM   1362 C C      . HIS A 1 194 ? 27.220 26.231 24.095 1.00 9.88  ? 185 HIS A C      1 
ATOM   1363 O O      . HIS A 1 194 ? 27.864 25.673 24.997 1.00 10.80 ? 185 HIS A O      1 
ATOM   1364 C CB     . HIS A 1 194 ? 26.622 24.060 22.996 1.00 10.21 ? 185 HIS A CB     1 
ATOM   1365 C CG     . HIS A 1 194 ? 25.286 23.821 23.658 1.00 9.54  ? 185 HIS A CG     1 
ATOM   1366 N ND1    . HIS A 1 194 ? 24.647 24.778 24.419 1.00 11.75 ? 185 HIS A ND1    1 
ATOM   1367 C CD2    . HIS A 1 194 ? 24.477 22.722 23.646 1.00 11.43 ? 185 HIS A CD2    1 
ATOM   1368 C CE1    . HIS A 1 194 ? 23.488 24.268 24.843 1.00 11.83 ? 185 HIS A CE1    1 
ATOM   1369 N NE2    . HIS A 1 194 ? 23.363 23.024 24.397 1.00 11.66 ? 185 HIS A NE2    1 
ATOM   1370 N N      . GLY A 1 195 ? 26.739 27.472 24.217 1.00 10.14 ? 186 GLY A N      1 
ATOM   1371 C CA     . GLY A 1 195 ? 26.887 28.212 25.456 1.00 9.93  ? 186 GLY A CA     1 
ATOM   1372 C C      . GLY A 1 195 ? 25.569 28.462 26.148 1.00 10.50 ? 186 GLY A C      1 
ATOM   1373 O O      . GLY A 1 195 ? 25.450 29.476 26.836 1.00 12.15 ? 186 GLY A O      1 
ATOM   1374 N N      . ALA A 1 196 ? 24.594 27.572 25.968 1.00 10.71 ? 187 ALA A N      1 
ATOM   1375 C CA     . ALA A 1 196 ? 23.212 27.772 26.401 1.00 9.79  ? 187 ALA A CA     1 
ATOM   1376 C C      . ALA A 1 196 ? 22.806 26.715 27.442 1.00 11.77 ? 187 ALA A C      1 
ATOM   1377 O O      . ALA A 1 196 ? 23.546 25.781 27.785 1.00 11.35 ? 187 ALA A O      1 
ATOM   1378 C CB     . ALA A 1 196 ? 22.268 27.709 25.188 1.00 11.01 ? 187 ALA A CB     1 
ATOM   1379 N N      . HIS A 1 197 ? 21.576 26.902 27.955 1.00 12.05 ? 188 HIS A N      1 
ATOM   1380 C CA     . HIS A 1 197 ? 20.792 25.863 28.671 1.00 11.47 ? 188 HIS A CA     1 
ATOM   1381 C C      . HIS A 1 197 ? 21.438 25.349 29.940 1.00 11.93 ? 188 HIS A C      1 
ATOM   1382 O O      . HIS A 1 197 ? 21.171 24.214 30.350 1.00 12.83 ? 188 HIS A O      1 
ATOM   1383 C CB     . HIS A 1 197 ? 20.468 24.684 27.756 1.00 13.23 ? 188 HIS A CB     1 
ATOM   1384 C CG     . HIS A 1 197 ? 19.762 25.084 26.510 1.00 12.41 ? 188 HIS A CG     1 
ATOM   1385 N ND1    . HIS A 1 197 ? 20.128 24.604 25.284 1.00 13.06 ? 188 HIS A ND1    1 
ATOM   1386 C CD2    . HIS A 1 197 ? 18.677 25.867 26.303 1.00 17.34 ? 188 HIS A CD2    1 
ATOM   1387 C CE1    . HIS A 1 197 ? 19.327 25.101 24.359 1.00 12.36 ? 188 HIS A CE1    1 
ATOM   1388 N NE2    . HIS A 1 197 ? 18.419 25.860 24.945 1.00 16.07 ? 188 HIS A NE2    1 
ATOM   1389 N N      . GLY A 1 198 ? 22.242 26.145 30.623 1.00 10.94 ? 189 GLY A N      1 
ATOM   1390 C CA     . GLY A 1 198 ? 22.739 25.649 31.899 1.00 11.13 ? 189 GLY A CA     1 
ATOM   1391 C C      . GLY A 1 198 ? 23.861 24.633 31.814 1.00 10.95 ? 189 GLY A C      1 
ATOM   1392 O O      . GLY A 1 198 ? 24.209 23.996 32.824 1.00 10.19 ? 189 GLY A O      1 
ATOM   1393 N N      . TYR A 1 199 ? 24.459 24.450 30.622 1.00 9.45  ? 190 TYR A N      1 
ATOM   1394 C CA     . TYR A 1 199 ? 25.569 23.526 30.466 1.00 8.66  ? 190 TYR A CA     1 
ATOM   1395 C C      . TYR A 1 199 ? 26.890 24.246 30.809 1.00 10.86 ? 190 TYR A C      1 
ATOM   1396 O O      . TYR A 1 199 ? 26.869 25.266 31.489 1.00 10.74 ? 190 TYR A O      1 
ATOM   1397 C CB     . TYR A 1 199 ? 25.485 22.884 29.059 1.00 9.77  ? 190 TYR A CB     1 
ATOM   1398 C CG     . TYR A 1 199 ? 24.249 22.012 28.930 1.00 9.85  ? 190 TYR A CG     1 
ATOM   1399 C CD1    . TYR A 1 199 ? 24.071 20.905 29.775 1.00 10.53 ? 190 TYR A CD1    1 
ATOM   1400 C CD2    . TYR A 1 199 ? 23.258 22.291 27.992 1.00 10.50 ? 190 TYR A CD2    1 
ATOM   1401 C CE1    . TYR A 1 199 ? 22.941 20.125 29.639 1.00 11.15 ? 190 TYR A CE1    1 
ATOM   1402 C CE2    . TYR A 1 199 ? 22.152 21.476 27.872 1.00 13.92 ? 190 TYR A CE2    1 
ATOM   1403 C CZ     . TYR A 1 199 ? 22.017 20.423 28.695 1.00 12.53 ? 190 TYR A CZ     1 
ATOM   1404 O OH     . TYR A 1 199 ? 20.885 19.604 28.557 1.00 16.13 ? 190 TYR A OH     1 
ATOM   1405 N N      . LEU A 1 200 ? 28.051 23.678 30.479 1.00 10.20 ? 191 LEU A N      1 
ATOM   1406 C CA     . LEU A 1 200 ? 29.282 24.158 31.108 1.00 10.89 ? 191 LEU A CA     1 
ATOM   1407 C C      . LEU A 1 200 ? 29.520 25.645 30.923 1.00 10.77 ? 191 LEU A C      1 
ATOM   1408 O O      . LEU A 1 200 ? 29.870 26.341 31.882 1.00 11.07 ? 191 LEU A O      1 
ATOM   1409 C CB     . LEU A 1 200 ? 30.494 23.399 30.541 1.00 10.61 ? 191 LEU A CB     1 
ATOM   1410 C CG     . LEU A 1 200 ? 31.843 23.800 31.170 1.00 10.92 ? 191 LEU A CG     1 
ATOM   1411 C CD1    . LEU A 1 200 ? 31.954 23.471 32.675 1.00 12.44 ? 191 LEU A CD1    1 
ATOM   1412 C CD2    . LEU A 1 200 ? 33.017 23.103 30.467 1.00 12.24 ? 191 LEU A CD2    1 
ATOM   1413 N N      . ILE A 1 201 ? 29.469 26.146 29.681 1.00 10.76 ? 192 ILE A N      1 
ATOM   1414 C CA     . ILE A 1 201 ? 29.719 27.585 29.489 1.00 10.22 ? 192 ILE A CA     1 
ATOM   1415 C C      . ILE A 1 201 ? 28.715 28.433 30.280 1.00 10.89 ? 192 ILE A C      1 
ATOM   1416 O O      . ILE A 1 201 ? 29.089 29.428 30.919 1.00 10.75 ? 192 ILE A O      1 
ATOM   1417 C CB     . ILE A 1 201 ? 29.702 27.898 27.995 1.00 10.98 ? 192 ILE A CB     1 
ATOM   1418 C CG1    . ILE A 1 201 ? 30.935 27.279 27.367 1.00 12.26 ? 192 ILE A CG1    1 
ATOM   1419 C CG2    . ILE A 1 201 ? 29.675 29.420 27.785 1.00 11.58 ? 192 ILE A CG2    1 
ATOM   1420 C CD1    . ILE A 1 201 ? 30.978 27.312 25.874 1.00 11.61 ? 192 ILE A CD1    1 
ATOM   1421 N N      . ASP A 1 202 ? 27.436 28.059 30.256 1.00 10.10 ? 193 ASP A N      1 
ATOM   1422 C CA     . ASP A 1 202 ? 26.420 28.807 30.996 1.00 11.70 ? 193 ASP A CA     1 
ATOM   1423 C C      . ASP A 1 202 ? 26.652 28.699 32.499 1.00 9.98  ? 193 ASP A C      1 
ATOM   1424 O O      . ASP A 1 202 ? 26.221 29.591 33.252 1.00 12.27 ? 193 ASP A O      1 
ATOM   1425 C CB     . ASP A 1 202 ? 25.014 28.285 30.591 1.00 13.11 ? 193 ASP A CB     1 
ATOM   1426 C CG     . ASP A 1 202 ? 23.917 29.342 30.670 1.00 14.43 ? 193 ASP A CG     1 
ATOM   1427 O OD1    . ASP A 1 202 ? 24.192 30.544 30.429 1.00 15.42 ? 193 ASP A OD1    1 
ATOM   1428 O OD2    . ASP A 1 202 ? 22.759 28.915 30.859 1.00 15.19 ? 193 ASP A OD2    1 
ATOM   1429 N N      . GLN A 1 203 ? 27.264 27.603 32.994 1.00 10.31 ? 194 GLN A N      1 
ATOM   1430 C CA     . GLN A 1 203 ? 27.610 27.523 34.418 1.00 10.09 ? 194 GLN A CA     1 
ATOM   1431 C C      . GLN A 1 203 ? 28.654 28.564 34.809 1.00 10.36 ? 194 GLN A C      1 
ATOM   1432 O O      . GLN A 1 203 ? 28.742 28.907 36.007 1.00 11.89 ? 194 GLN A O      1 
ATOM   1433 C CB     . GLN A 1 203 ? 28.123 26.121 34.713 1.00 10.44 ? 194 GLN A CB     1 
ATOM   1434 C CG     . GLN A 1 203 ? 26.985 25.082 34.661 1.00 10.72 ? 194 GLN A CG     1 
ATOM   1435 C CD     . GLN A 1 203 ? 27.466 23.676 34.367 1.00 9.88  ? 194 GLN A CD     1 
ATOM   1436 O OE1    . GLN A 1 203 ? 28.542 23.248 34.767 1.00 10.92 ? 194 GLN A OE1    1 
ATOM   1437 N NE2    . GLN A 1 203 ? 26.648 22.936 33.622 1.00 10.02 ? 194 GLN A NE2    1 
ATOM   1438 N N      . PHE A 1 204 ? 29.456 29.048 33.843 1.00 9.83  ? 195 PHE A N      1 
ATOM   1439 C CA     . PHE A 1 204 ? 30.350 30.200 34.095 1.00 9.88  ? 195 PHE A CA     1 
ATOM   1440 C C      . PHE A 1 204 ? 29.640 31.534 33.899 1.00 9.65  ? 195 PHE A C      1 
ATOM   1441 O O      . PHE A 1 204 ? 29.873 32.493 34.648 1.00 11.01 ? 195 PHE A O      1 
ATOM   1442 C CB     . PHE A 1 204 ? 31.586 30.110 33.185 1.00 10.49 ? 195 PHE A CB     1 
ATOM   1443 C CG     . PHE A 1 204 ? 32.642 29.172 33.696 1.00 10.84 ? 195 PHE A CG     1 
ATOM   1444 C CD1    . PHE A 1 204 ? 32.594 27.816 33.335 1.00 11.63 ? 195 PHE A CD1    1 
ATOM   1445 C CD2    . PHE A 1 204 ? 33.677 29.623 34.529 1.00 11.03 ? 195 PHE A CD2    1 
ATOM   1446 C CE1    . PHE A 1 204 ? 33.539 26.921 33.827 1.00 11.59 ? 195 PHE A CE1    1 
ATOM   1447 C CE2    . PHE A 1 204 ? 34.644 28.729 35.043 1.00 10.75 ? 195 PHE A CE2    1 
ATOM   1448 C CZ     . PHE A 1 204 ? 34.581 27.354 34.670 1.00 12.15 ? 195 PHE A CZ     1 
ATOM   1449 N N      . LEU A 1 205 ? 28.732 31.626 32.919 1.00 10.73 ? 196 LEU A N      1 
ATOM   1450 C CA     . LEU A 1 205 ? 28.105 32.909 32.606 1.00 10.71 ? 196 LEU A CA     1 
ATOM   1451 C C      . LEU A 1 205 ? 27.160 33.358 33.699 1.00 11.43 ? 196 LEU A C      1 
ATOM   1452 O O      . LEU A 1 205 ? 27.097 34.558 34.022 1.00 12.88 ? 196 LEU A O      1 
ATOM   1453 C CB     . LEU A 1 205 ? 27.303 32.795 31.312 1.00 10.75 ? 196 LEU A CB     1 
ATOM   1454 C CG     . LEU A 1 205 ? 28.114 32.719 30.034 1.00 9.73  ? 196 LEU A CG     1 
ATOM   1455 C CD1    . LEU A 1 205 ? 27.197 32.425 28.847 1.00 11.95 ? 196 LEU A CD1    1 
ATOM   1456 C CD2    . LEU A 1 205 ? 28.926 34.008 29.810 1.00 12.90 ? 196 LEU A CD2    1 
ATOM   1457 N N      . LYS A 1 206 ? 26.371 32.423 34.229 1.00 10.74 ? 197 LYS A N      1 
ATOM   1458 C CA     . LYS A 1 206 ? 25.186 32.796 35.020 1.00 11.66 ? 197 LYS A CA     1 
ATOM   1459 C C      . LYS A 1 206 ? 25.561 33.006 36.479 1.00 11.97 ? 197 LYS A C      1 
ATOM   1460 O O      . LYS A 1 206 ? 26.133 32.103 37.106 1.00 12.79 ? 197 LYS A O      1 
ATOM   1461 C CB     . LYS A 1 206 ? 24.112 31.699 34.946 1.00 11.14 ? 197 LYS A CB     1 
ATOM   1462 C CG     . LYS A 1 206 ? 23.515 31.491 33.509 1.00 13.99 ? 197 LYS A CG     1 
ATOM   1463 C CD     . LYS A 1 206 ? 22.559 32.648 33.140 1.00 14.59 ? 197 LYS A CD     1 
ATOM   1464 C CE     . LYS A 1 206 ? 22.159 32.633 31.643 1.00 15.48 ? 197 LYS A CE     1 
ATOM   1465 N NZ     . LYS A 1 206 ? 21.296 31.471 31.377 1.00 16.62 ? 197 LYS A NZ     1 
ATOM   1466 N N      . ASP A 1 207 ? 25.187 34.168 37.020 1.00 12.65 ? 198 ASP A N      1 
ATOM   1467 C CA     . ASP A 1 207 ? 25.518 34.400 38.414 1.00 13.07 ? 198 ASP A CA     1 
ATOM   1468 C C      . ASP A 1 207 ? 24.675 33.561 39.377 1.00 16.20 ? 198 ASP A C      1 
ATOM   1469 O O      . ASP A 1 207 ? 24.992 33.542 40.571 1.00 17.80 ? 198 ASP A O      1 
ATOM   1470 C CB     . ASP A 1 207 ? 25.529 35.878 38.869 1.00 14.80 ? 198 ASP A CB     1 
ATOM   1471 C CG     . ASP A 1 207 ? 24.190 36.586 38.772 1.00 19.69 ? 198 ASP A CG     1 
ATOM   1472 O OD1    . ASP A 1 207 ? 23.117 35.965 38.622 1.00 17.10 ? 198 ASP A OD1    1 
ATOM   1473 O OD2    . ASP A 1 207 ? 24.236 37.855 38.763 1.00 23.68 ? 198 ASP A OD2    1 
ATOM   1474 N N      . GLY A 1 208 ? 23.650 32.872 38.919 1.00 13.22 ? 199 GLY A N      1 
ATOM   1475 C CA     . GLY A 1 208 ? 22.962 31.935 39.776 1.00 14.04 ? 199 GLY A CA     1 
ATOM   1476 C C      . GLY A 1 208 ? 23.638 30.602 39.887 1.00 15.68 ? 199 GLY A C      1 
ATOM   1477 O O      . GLY A 1 208 ? 23.197 29.750 40.687 1.00 19.92 ? 199 GLY A O      1 
ATOM   1478 N N      . ILE A 1 209 ? 24.728 30.392 39.123 1.00 12.84 ? 200 ILE A N      1 
ATOM   1479 C CA     . ILE A 1 209 ? 25.539 29.181 39.215 1.00 12.37 ? 200 ILE A CA     1 
ATOM   1480 C C      . ILE A 1 209 ? 26.961 29.502 39.634 1.00 12.78 ? 200 ILE A C      1 
ATOM   1481 O O      . ILE A 1 209 ? 27.541 28.829 40.476 1.00 14.16 ? 200 ILE A O      1 
ATOM   1482 C CB     . ILE A 1 209 ? 25.545 28.416 37.873 1.00 12.16 ? 200 ILE A CB     1 
ATOM   1483 C CG1    . ILE A 1 209 ? 24.123 28.037 37.443 1.00 13.91 ? 200 ILE A CG1    1 
ATOM   1484 C CG2    . ILE A 1 209 ? 26.443 27.192 38.045 1.00 11.93 ? 200 ILE A CG2    1 
ATOM   1485 C CD1    . ILE A 1 209 ? 24.044 27.353 36.060 1.00 16.00 ? 200 ILE A CD1    1 
ATOM   1486 N N      . ASN A 1 210 ? 27.573 30.488 38.996 1.00 13.21 ? 201 ASN A N      1 
ATOM   1487 C CA     . ASN A 1 210 ? 28.993 30.776 39.197 1.00 10.77 ? 201 ASN A CA     1 
ATOM   1488 C C      . ASN A 1 210 ? 29.187 31.477 40.537 1.00 13.95 ? 201 ASN A C      1 
ATOM   1489 O O      . ASN A 1 210 ? 28.867 32.662 40.693 1.00 15.46 ? 201 ASN A O      1 
ATOM   1490 C CB     . ASN A 1 210 ? 29.481 31.649 38.040 1.00 11.08 ? 201 ASN A CB     1 
ATOM   1491 C CG     . ASN A 1 210 ? 30.973 31.865 38.069 1.00 11.56 ? 201 ASN A CG     1 
ATOM   1492 O OD1    . ASN A 1 210 ? 31.621 31.737 39.128 1.00 13.50 ? 201 ASN A OD1    1 
ATOM   1493 N ND2    . ASN A 1 210 ? 31.564 32.184 36.918 1.00 11.69 ? 201 ASN A ND2    1 
ATOM   1494 N N      . ASP A 1 211 ? 29.698 30.724 41.505 1.00 13.07 ? 202 ASP A N      1 
ATOM   1495 C CA     . ASP A 1 211 ? 30.036 31.238 42.835 1.00 11.93 ? 202 ASP A CA     1 
ATOM   1496 C C      . ASP A 1 211 ? 31.547 31.276 43.036 1.00 15.49 ? 202 ASP A C      1 
ATOM   1497 O O      . ASP A 1 211 ? 32.031 31.288 44.172 1.00 15.62 ? 202 ASP A O      1 
ATOM   1498 C CB     . ASP A 1 211 ? 29.343 30.305 43.845 1.00 14.59 ? 202 ASP A CB     1 
ATOM   1499 C CG     . ASP A 1 211 ? 29.976 28.942 43.876 1.00 17.48 ? 202 ASP A CG     1 
ATOM   1500 O OD1    . ASP A 1 211 ? 30.429 28.377 42.866 1.00 16.13 ? 202 ASP A OD1    1 
ATOM   1501 O OD2    . ASP A 1 211 ? 29.703 28.210 44.890 1.00 20.41 ? 202 ASP A OD2    1 
ATOM   1502 N N      . ARG A 1 212 ? 32.315 31.354 41.950 1.00 13.45 ? 203 ARG A N      1 
ATOM   1503 C CA     . ARG A 1 212 ? 33.769 31.408 42.076 1.00 13.35 ? 203 ARG A CA     1 
ATOM   1504 C C      . ARG A 1 212 ? 34.225 32.758 42.618 1.00 14.32 ? 203 ARG A C      1 
ATOM   1505 O O      . ARG A 1 212 ? 33.596 33.786 42.381 1.00 16.75 ? 203 ARG A O      1 
ATOM   1506 C CB     . ARG A 1 212 ? 34.414 31.243 40.694 1.00 11.98 ? 203 ARG A CB     1 
ATOM   1507 C CG     . ARG A 1 212 ? 34.128 29.898 40.055 1.00 12.75 ? 203 ARG A CG     1 
ATOM   1508 C CD     . ARG A 1 212 ? 34.779 29.848 38.683 1.00 11.31 ? 203 ARG A CD     1 
ATOM   1509 N NE     . ARG A 1 212 ? 36.228 29.654 38.754 1.00 12.32 ? 203 ARG A NE     1 
ATOM   1510 C CZ     . ARG A 1 212 ? 36.789 28.443 38.682 1.00 11.37 ? 203 ARG A CZ     1 
ATOM   1511 N NH1    . ARG A 1 212 ? 36.056 27.326 38.611 1.00 12.71 ? 203 ARG A NH1    1 
ATOM   1512 N NH2    . ARG A 1 212 ? 38.123 28.331 38.683 1.00 13.19 ? 203 ARG A NH2    1 
ATOM   1513 N N      . THR A 1 213 ? 35.359 32.732 43.322 1.00 17.06 ? 204 THR A N      1 
ATOM   1514 C CA     . THR A 1 213 ? 35.952 33.962 43.835 1.00 17.34 ? 204 THR A CA     1 
ATOM   1515 C C      . THR A 1 213 ? 37.304 34.228 43.202 1.00 18.88 ? 204 THR A C      1 
ATOM   1516 O O      . THR A 1 213 ? 38.042 35.104 43.670 1.00 23.62 ? 204 THR A O      1 
ATOM   1517 C CB     . THR A 1 213 ? 36.076 33.889 45.360 1.00 19.09 ? 204 THR A CB     1 
ATOM   1518 O OG1    . THR A 1 213 ? 36.818 32.733 45.684 1.00 23.01 ? 204 THR A OG1    1 
ATOM   1519 C CG2    . THR A 1 213 ? 34.663 33.778 46.008 1.00 22.17 ? 204 THR A CG2    1 
ATOM   1520 N N      . ASP A 1 214 ? 37.639 33.530 42.129 1.00 15.23 ? 205 ASP A N      1 
ATOM   1521 C CA     . ASP A 1 214 ? 38.847 33.799 41.361 1.00 15.17 ? 205 ASP A CA     1 
ATOM   1522 C C      . ASP A 1 214 ? 38.507 34.666 40.140 1.00 14.25 ? 205 ASP A C      1 
ATOM   1523 O O      . ASP A 1 214 ? 37.431 35.293 40.075 1.00 15.12 ? 205 ASP A O      1 
ATOM   1524 C CB     . ASP A 1 214 ? 39.584 32.502 41.000 1.00 14.13 ? 205 ASP A CB     1 
ATOM   1525 C CG     . ASP A 1 214 ? 38.869 31.664 39.926 1.00 15.46 ? 205 ASP A CG     1 
ATOM   1526 O OD1    . ASP A 1 214 ? 37.756 32.008 39.491 1.00 15.39 ? 205 ASP A OD1    1 
ATOM   1527 O OD2    . ASP A 1 214 ? 39.463 30.620 39.576 1.00 15.93 ? 205 ASP A OD2    1 
ATOM   1528 N N      . GLU A 1 215 ? 39.428 34.740 39.176 1.00 13.42 ? 206 GLU A N      1 
ATOM   1529 C CA     . GLU A 1 215 ? 39.246 35.653 38.061 1.00 14.68 ? 206 GLU A CA     1 
ATOM   1530 C C      . GLU A 1 215 ? 38.220 35.167 37.045 1.00 13.94 ? 206 GLU A C      1 
ATOM   1531 O O      . GLU A 1 215 ? 37.956 35.879 36.075 1.00 15.06 ? 206 GLU A O      1 
ATOM   1532 C CB     . GLU A 1 215 ? 40.586 35.981 37.384 1.00 16.81 ? 206 GLU A CB     1 
ATOM   1533 C CG     . GLU A 1 215 ? 41.107 34.838 36.495 1.00 18.84 ? 206 GLU A CG     1 
ATOM   1534 C CD     . GLU A 1 215 ? 42.043 33.890 37.249 1.00 22.88 ? 206 GLU A CD     1 
ATOM   1535 O OE1    . GLU A 1 215 ? 41.919 33.714 38.496 1.00 22.10 ? 206 GLU A OE1    1 
ATOM   1536 O OE2    . GLU A 1 215 ? 42.908 33.265 36.566 1.00 23.50 ? 206 GLU A OE2    1 
ATOM   1537 N N      . TYR A 1 216 ? 37.579 34.012 37.275 1.00 12.72 ? 207 TYR A N      1 
ATOM   1538 C CA     . TYR A 1 216 ? 36.493 33.554 36.425 1.00 12.19 ? 207 TYR A CA     1 
ATOM   1539 C C      . TYR A 1 216 ? 35.141 33.701 37.103 1.00 14.67 ? 207 TYR A C      1 
ATOM   1540 O O      . TYR A 1 216 ? 34.169 33.235 36.552 1.00 15.03 ? 207 TYR A O      1 
ATOM   1541 C CB     . TYR A 1 216 ? 36.713 32.077 36.042 1.00 12.57 ? 207 TYR A CB     1 
ATOM   1542 C CG     . TYR A 1 216 ? 37.795 31.898 35.003 1.00 12.63 ? 207 TYR A CG     1 
ATOM   1543 C CD1    . TYR A 1 216 ? 39.126 31.859 35.370 1.00 12.86 ? 207 TYR A CD1    1 
ATOM   1544 C CD2    . TYR A 1 216 ? 37.472 31.775 33.659 1.00 12.44 ? 207 TYR A CD2    1 
ATOM   1545 C CE1    . TYR A 1 216 ? 40.120 31.678 34.395 1.00 13.76 ? 207 TYR A CE1    1 
ATOM   1546 C CE2    . TYR A 1 216 ? 38.451 31.625 32.681 1.00 12.82 ? 207 TYR A CE2    1 
ATOM   1547 C CZ     . TYR A 1 216 ? 39.765 31.539 33.056 1.00 14.89 ? 207 TYR A CZ     1 
ATOM   1548 O OH     . TYR A 1 216 ? 40.784 31.346 32.126 1.00 15.31 ? 207 TYR A OH     1 
ATOM   1549 N N      . GLY A 1 217 ? 35.068 34.405 38.239 1.00 13.74 ? 208 GLY A N      1 
ATOM   1550 C CA     . GLY A 1 217 ? 33.805 34.595 38.924 1.00 15.94 ? 208 GLY A CA     1 
ATOM   1551 C C      . GLY A 1 217 ? 33.645 36.039 39.345 1.00 12.58 ? 208 GLY A C      1 
ATOM   1552 O O      . GLY A 1 217 ? 34.595 36.842 39.295 1.00 15.17 ? 208 GLY A O      1 
ATOM   1553 N N      . GLY A 1 218 ? 32.392 36.381 39.681 1.00 14.54 ? 209 GLY A N      1 
ATOM   1554 C CA     . GLY A 1 218 ? 32.155 37.719 40.236 1.00 13.49 ? 209 GLY A CA     1 
ATOM   1555 C C      . GLY A 1 218 ? 31.606 38.652 39.165 1.00 13.85 ? 209 GLY A C      1 
ATOM   1556 O O      . GLY A 1 218 ? 30.430 38.565 38.782 1.00 16.04 ? 209 GLY A O      1 
ATOM   1557 N N      . SER A 1 219 ? 32.463 39.541 38.700 1.00 13.81 ? 210 SER A N      1 
ATOM   1558 C CA     . SER A 1 219 ? 32.058 40.563 37.744 1.00 14.70 ? 210 SER A CA     1 
ATOM   1559 C C      . SER A 1 219 ? 31.590 39.979 36.422 1.00 15.06 ? 210 SER A C      1 
ATOM   1560 O O      . SER A 1 219 ? 31.910 38.836 36.052 1.00 15.30 ? 210 SER A O      1 
ATOM   1561 C CB     . SER A 1 219 ? 33.232 41.501 37.469 1.00 15.80 ? 210 SER A CB     1 
ATOM   1562 O OG     . SER A 1 219 ? 34.278 40.823 36.740 1.00 15.43 ? 210 SER A OG     1 
ATOM   1563 N N      . LEU A 1 220 ? 30.841 40.786 35.669 1.00 13.15 ? 211 LEU A N      1 
ATOM   1564 C CA     . LEU A 1 220 ? 30.481 40.377 34.314 1.00 13.38 ? 211 LEU A CA     1 
ATOM   1565 C C      . LEU A 1 220 ? 31.705 40.022 33.493 1.00 15.39 ? 211 LEU A C      1 
ATOM   1566 O O      . LEU A 1 220 ? 31.691 39.012 32.759 1.00 14.74 ? 211 LEU A O      1 
ATOM   1567 C CB     . LEU A 1 220 ? 29.780 41.527 33.594 1.00 17.13 ? 211 LEU A CB     1 
ATOM   1568 C CG     . LEU A 1 220 ? 28.297 41.720 33.960 1.00 16.71 ? 211 LEU A CG     1 
ATOM   1569 C CD1    . LEU A 1 220 ? 27.750 43.101 33.514 1.00 17.90 ? 211 LEU A CD1    1 
ATOM   1570 C CD2    . LEU A 1 220 ? 27.473 40.581 33.378 1.00 17.10 ? 211 LEU A CD2    1 
ATOM   1571 N N      . ALA A 1 221 ? 32.774 40.832 33.554 1.00 14.20 ? 212 ALA A N      1 
ATOM   1572 C CA     . ALA A 1 221 ? 33.948 40.486 32.749 1.00 14.26 ? 212 ALA A CA     1 
ATOM   1573 C C      . ALA A 1 221 ? 34.507 39.138 33.121 1.00 14.30 ? 212 ALA A C      1 
ATOM   1574 O O      . ALA A 1 221 ? 34.893 38.352 32.248 1.00 15.30 ? 212 ALA A O      1 
ATOM   1575 C CB     . ALA A 1 221 ? 35.016 41.557 32.896 1.00 16.44 ? 212 ALA A CB     1 
ATOM   1576 N N      . ASN A 1 222 ? 34.551 38.839 34.410 1.00 13.02 ? 213 ASN A N      1 
ATOM   1577 C CA     . ASN A 1 222 ? 35.128 37.572 34.856 1.00 12.65 ? 213 ASN A CA     1 
ATOM   1578 C C      . ASN A 1 222 ? 34.232 36.410 34.436 1.00 12.89 ? 213 ASN A C      1 
ATOM   1579 O O      . ASN A 1 222 ? 34.726 35.379 33.981 1.00 12.46 ? 213 ASN A O      1 
ATOM   1580 C CB     . ASN A 1 222 ? 35.295 37.603 36.380 1.00 12.83 ? 213 ASN A CB     1 
ATOM   1581 C CG     . ASN A 1 222 ? 36.496 38.406 36.811 1.00 16.19 ? 213 ASN A CG     1 
ATOM   1582 O OD1    . ASN A 1 222 ? 37.196 38.994 35.993 1.00 17.04 ? 213 ASN A OD1    1 
ATOM   1583 N ND2    . ASN A 1 222 ? 36.761 38.392 38.119 1.00 15.82 ? 213 ASN A ND2    1 
ATOM   1584 N N      . ARG A 1 223 ? 32.911 36.590 34.552 1.00 12.39 ? 214 ARG A N      1 
ATOM   1585 C CA     . ARG A 1 223 ? 31.989 35.515 34.165 1.00 11.22 ? 214 ARG A CA     1 
ATOM   1586 C C      . ARG A 1 223 ? 32.009 35.272 32.665 1.00 13.20 ? 214 ARG A C      1 
ATOM   1587 O O      . ARG A 1 223 ? 31.744 34.146 32.208 1.00 13.09 ? 214 ARG A O      1 
ATOM   1588 C CB     . ARG A 1 223 ? 30.558 35.812 34.609 1.00 10.89 ? 214 ARG A CB     1 
ATOM   1589 C CG     . ARG A 1 223 ? 30.478 35.733 36.141 1.00 12.76 ? 214 ARG A CG     1 
ATOM   1590 C CD     . ARG A 1 223 ? 29.060 35.763 36.578 1.00 14.05 ? 214 ARG A CD     1 
ATOM   1591 N NE     . ARG A 1 223 ? 28.706 37.185 36.720 1.00 27.75 ? 214 ARG A NE     1 
ATOM   1592 C CZ     . ARG A 1 223 ? 27.601 37.767 36.295 1.00 21.76 ? 214 ARG A CZ     1 
ATOM   1593 N NH1    . ARG A 1 223 ? 26.722 37.146 35.544 1.00 24.08 ? 214 ARG A NH1    1 
ATOM   1594 N NH2    . ARG A 1 223 ? 27.344 39.009 36.676 1.00 31.53 ? 214 ARG A NH2    1 
ATOM   1595 N N      . CYS A 1 224 ? 32.345 36.282 31.877 1.00 11.49 ? 215 CYS A N      1 
ATOM   1596 C CA     . CYS A 1 224 ? 32.440 36.127 30.418 1.00 11.95 ? 215 CYS A CA     1 
ATOM   1597 C C      . CYS A 1 224 ? 33.793 35.638 29.950 1.00 11.15 ? 215 CYS A C      1 
ATOM   1598 O O      . CYS A 1 224 ? 33.960 35.381 28.746 1.00 12.67 ? 215 CYS A O      1 
ATOM   1599 C CB     . CYS A 1 224 ? 32.133 37.447 29.666 1.00 13.48 ? 215 CYS A CB     1 
ATOM   1600 S SG     . CYS A 1 224 ? 30.376 37.904 29.834 1.00 15.61 ? 215 CYS A SG     1 
ATOM   1601 N N      . LYS A 1 225 ? 34.770 35.455 30.839 1.00 11.52 ? 216 LYS A N      1 
ATOM   1602 C CA     . LYS A 1 225 ? 36.107 35.062 30.405 1.00 11.27 ? 216 LYS A CA     1 
ATOM   1603 C C      . LYS A 1 225 ? 36.088 33.711 29.739 1.00 11.72 ? 216 LYS A C      1 
ATOM   1604 O O      . LYS A 1 225 ? 36.746 33.523 28.708 1.00 12.76 ? 216 LYS A O      1 
ATOM   1605 C CB     . LYS A 1 225 ? 37.049 35.028 31.602 1.00 13.74 ? 216 LYS A CB     1 
ATOM   1606 C CG     . LYS A 1 225 ? 37.925 36.188 31.842 1.00 24.85 ? 216 LYS A CG     1 
ATOM   1607 C CD     . LYS A 1 225 ? 39.056 35.750 32.827 1.00 23.66 ? 216 LYS A CD     1 
ATOM   1608 C CE     . LYS A 1 225 ? 39.868 36.989 33.201 1.00 33.37 ? 216 LYS A CE     1 
ATOM   1609 N NZ     . LYS A 1 225 ? 39.327 37.706 34.388 1.00 29.39 ? 216 LYS A NZ     1 
ATOM   1610 N N      . PHE A 1 226 ? 35.383 32.736 30.328 1.00 10.89 ? 217 PHE A N      1 
ATOM   1611 C CA     . PHE A 1 226 ? 35.454 31.383 29.761 1.00 11.86 ? 217 PHE A CA     1 
ATOM   1612 C C      . PHE A 1 226 ? 34.905 31.355 28.329 1.00 12.50 ? 217 PHE A C      1 
ATOM   1613 O O      . PHE A 1 226 ? 35.571 30.839 27.414 1.00 12.08 ? 217 PHE A O      1 
ATOM   1614 C CB     . PHE A 1 226 ? 34.740 30.387 30.669 1.00 12.84 ? 217 PHE A CB     1 
ATOM   1615 C CG     . PHE A 1 226 ? 34.854 28.952 30.206 1.00 12.34 ? 217 PHE A CG     1 
ATOM   1616 C CD1    . PHE A 1 226 ? 36.106 28.377 29.911 1.00 15.68 ? 217 PHE A CD1    1 
ATOM   1617 C CD2    . PHE A 1 226 ? 33.722 28.210 29.996 1.00 12.78 ? 217 PHE A CD2    1 
ATOM   1618 C CE1    . PHE A 1 226 ? 36.203 27.047 29.526 1.00 17.00 ? 217 PHE A CE1    1 
ATOM   1619 C CE2    . PHE A 1 226 ? 33.797 26.902 29.611 1.00 12.46 ? 217 PHE A CE2    1 
ATOM   1620 C CZ     . PHE A 1 226 ? 35.004 26.293 29.424 1.00 12.47 ? 217 PHE A CZ     1 
ATOM   1621 N N      . ILE A 1 227 ? 33.694 31.893 28.104 1.00 11.38 ? 218 ILE A N      1 
ATOM   1622 C CA     . ILE A 1 227 ? 33.188 31.853 26.729 1.00 11.67 ? 218 ILE A CA     1 
ATOM   1623 C C      . ILE A 1 227 ? 34.088 32.637 25.787 1.00 10.86 ? 218 ILE A C      1 
ATOM   1624 O O      . ILE A 1 227 ? 34.262 32.215 24.626 1.00 11.05 ? 218 ILE A O      1 
ATOM   1625 C CB     . ILE A 1 227 ? 31.723 32.307 26.640 1.00 11.37 ? 218 ILE A CB     1 
ATOM   1626 C CG1    . ILE A 1 227 ? 31.129 31.926 25.278 1.00 11.33 ? 218 ILE A CG1    1 
ATOM   1627 C CG2    . ILE A 1 227 ? 31.580 33.863 26.846 1.00 13.36 ? 218 ILE A CG2    1 
ATOM   1628 C CD1    . ILE A 1 227 ? 29.581 32.208 25.167 1.00 12.30 ? 218 ILE A CD1    1 
ATOM   1629 N N      . THR A 1 228 ? 34.693 33.747 26.237 1.00 10.86 ? 219 THR A N      1 
ATOM   1630 C CA     . THR A 1 228 ? 35.592 34.498 25.355 1.00 11.07 ? 219 THR A CA     1 
ATOM   1631 C C      . THR A 1 228 ? 36.796 33.660 24.984 1.00 10.97 ? 219 THR A C      1 
ATOM   1632 O O      . THR A 1 228 ? 37.171 33.630 23.795 1.00 11.82 ? 219 THR A O      1 
ATOM   1633 C CB     . THR A 1 228 ? 36.072 35.751 26.076 1.00 13.48 ? 219 THR A CB     1 
ATOM   1634 O OG1    . THR A 1 228 ? 34.944 36.566 26.441 1.00 15.32 ? 219 THR A OG1    1 
ATOM   1635 C CG2    . THR A 1 228 ? 36.929 36.582 25.121 1.00 15.75 ? 219 THR A CG2    1 
ATOM   1636 N N      . GLN A 1 229 ? 37.366 32.925 25.963 1.00 11.91 ? 220 GLN A N      1 
ATOM   1637 C CA     . GLN A 1 229 ? 38.530 32.090 25.676 1.00 11.49 ? 220 GLN A CA     1 
ATOM   1638 C C      . GLN A 1 229 ? 38.193 30.921 24.766 1.00 12.07 ? 220 GLN A C      1 
ATOM   1639 O O      . GLN A 1 229 ? 38.988 30.573 23.871 1.00 12.43 ? 220 GLN A O      1 
ATOM   1640 C CB     . GLN A 1 229 ? 39.133 31.637 26.998 1.00 13.60 ? 220 GLN A CB     1 
ATOM   1641 C CG     . GLN A 1 229 ? 39.845 32.802 27.681 1.00 13.09 ? 220 GLN A CG     1 
ATOM   1642 C CD     . GLN A 1 229 ? 40.170 32.491 29.111 1.00 16.53 ? 220 GLN A CD     1 
ATOM   1643 O OE1    . GLN A 1 229 ? 40.059 31.369 29.560 1.00 16.74 ? 220 GLN A OE1    1 
ATOM   1644 N NE2    . GLN A 1 229 ? 40.582 33.542 29.839 1.00 24.36 ? 220 GLN A NE2    1 
ATOM   1645 N N      . VAL A 1 230 ? 37.026 30.303 24.959 1.00 10.84 ? 221 VAL A N      1 
ATOM   1646 C CA     . VAL A 1 230 ? 36.614 29.218 24.074 1.00 11.55 ? 221 VAL A CA     1 
ATOM   1647 C C      . VAL A 1 230 ? 36.430 29.718 22.650 1.00 11.54 ? 221 VAL A C      1 
ATOM   1648 O O      . VAL A 1 230 ? 36.976 29.131 21.688 1.00 11.17 ? 221 VAL A O      1 
ATOM   1649 C CB     . VAL A 1 230 ? 35.308 28.606 24.608 1.00 10.50 ? 221 VAL A CB     1 
ATOM   1650 C CG1    . VAL A 1 230 ? 34.731 27.646 23.547 1.00 11.63 ? 221 VAL A CG1    1 
ATOM   1651 C CG2    . VAL A 1 230 ? 35.585 27.878 25.903 1.00 12.31 ? 221 VAL A CG2    1 
ATOM   1652 N N      . VAL A 1 231 ? 35.694 30.816 22.488 1.00 11.27 ? 222 VAL A N      1 
ATOM   1653 C CA     . VAL A 1 231 ? 35.476 31.338 21.133 1.00 11.19 ? 222 VAL A CA     1 
ATOM   1654 C C      . VAL A 1 231 ? 36.791 31.781 20.501 1.00 13.02 ? 222 VAL A C      1 
ATOM   1655 O O      . VAL A 1 231 ? 37.056 31.486 19.325 1.00 13.29 ? 222 VAL A O      1 
ATOM   1656 C CB     . VAL A 1 231 ? 34.462 32.487 21.176 1.00 11.27 ? 222 VAL A CB     1 
ATOM   1657 C CG1    . VAL A 1 231 ? 34.278 33.106 19.730 1.00 14.52 ? 222 VAL A CG1    1 
ATOM   1658 C CG2    . VAL A 1 231 ? 33.142 31.992 21.643 1.00 13.42 ? 222 VAL A CG2    1 
ATOM   1659 N N      . GLN A 1 232 ? 37.638 32.473 21.248 1.00 12.34 ? 223 GLN A N      1 
ATOM   1660 C CA     . GLN A 1 232 ? 38.917 32.921 20.663 1.00 13.00 ? 223 GLN A CA     1 
ATOM   1661 C C      . GLN A 1 232 ? 39.772 31.723 20.238 1.00 15.72 ? 223 GLN A C      1 
ATOM   1662 O O      . GLN A 1 232 ? 40.395 31.747 19.160 1.00 15.27 ? 223 GLN A O      1 
ATOM   1663 C CB     . GLN A 1 232 ? 39.697 33.732 21.699 1.00 15.38 ? 223 GLN A CB     1 
ATOM   1664 C CG     . GLN A 1 232 ? 41.027 34.260 21.182 1.00 23.95 ? 223 GLN A CG     1 
ATOM   1665 C CD     . GLN A 1 232 ? 40.901 35.072 19.901 1.00 36.53 ? 223 GLN A CD     1 
ATOM   1666 O OE1    . GLN A 1 232 ? 41.260 34.613 18.784 1.00 29.84 ? 223 GLN A OE1    1 
ATOM   1667 N NE2    . GLN A 1 232 ? 40.337 36.279 20.043 1.00 26.97 ? 223 GLN A NE2    1 
ATOM   1668 N N      . ALA A 1 233 ? 39.792 30.628 21.024 1.00 13.61 ? 224 ALA A N      1 
ATOM   1669 C CA     . ALA A 1 233 ? 40.591 29.477 20.627 1.00 11.80 ? 224 ALA A CA     1 
ATOM   1670 C C      . ALA A 1 233 ? 40.073 28.858 19.343 1.00 14.89 ? 224 ALA A C      1 
ATOM   1671 O O      . ALA A 1 233 ? 40.857 28.524 18.442 1.00 14.29 ? 224 ALA A O      1 
ATOM   1672 C CB     . ALA A 1 233 ? 40.568 28.432 21.744 1.00 14.87 ? 224 ALA A CB     1 
ATOM   1673 N N      . VAL A 1 234 ? 38.762 28.696 19.211 1.00 12.77 ? 225 VAL A N      1 
ATOM   1674 C CA     . VAL A 1 234 ? 38.260 28.074 17.987 1.00 12.01 ? 225 VAL A CA     1 
ATOM   1675 C C      . VAL A 1 234 ? 38.410 29.008 16.794 1.00 13.71 ? 225 VAL A C      1 
ATOM   1676 O O      . VAL A 1 234 ? 38.671 28.545 15.658 1.00 13.77 ? 225 VAL A O      1 
ATOM   1677 C CB     . VAL A 1 234 ? 36.835 27.517 18.151 1.00 12.02 ? 225 VAL A CB     1 
ATOM   1678 C CG1    . VAL A 1 234 ? 36.803 26.452 19.186 1.00 14.00 ? 225 VAL A CG1    1 
ATOM   1679 C CG2    . VAL A 1 234 ? 35.757 28.565 18.436 1.00 16.11 ? 225 VAL A CG2    1 
ATOM   1680 N N      . VAL A 1 235 ? 38.225 30.301 16.994 1.00 13.48 ? 226 VAL A N      1 
ATOM   1681 C CA     . VAL A 1 235 ? 38.477 31.279 15.932 1.00 13.31 ? 226 VAL A CA     1 
ATOM   1682 C C      . VAL A 1 235 ? 39.903 31.165 15.433 1.00 13.80 ? 226 VAL A C      1 
ATOM   1683 O O      . VAL A 1 235 ? 40.152 31.134 14.218 1.00 15.90 ? 226 VAL A O      1 
ATOM   1684 C CB     . VAL A 1 235 ? 38.142 32.696 16.428 1.00 13.43 ? 226 VAL A CB     1 
ATOM   1685 C CG1    . VAL A 1 235 ? 38.771 33.748 15.496 1.00 17.20 ? 226 VAL A CG1    1 
ATOM   1686 C CG2    . VAL A 1 235 ? 36.602 32.878 16.577 1.00 15.13 ? 226 VAL A CG2    1 
ATOM   1687 N N      . SER A 1 236 ? 40.859 31.092 16.355 1.00 14.15 ? 227 SER A N      1 
ATOM   1688 C CA     . SER A 1 236 ? 42.250 31.004 15.932 1.00 15.57 ? 227 SER A CA     1 
ATOM   1689 C C      . SER A 1 236 ? 42.509 29.729 15.164 1.00 18.55 ? 227 SER A C      1 
ATOM   1690 O O      . SER A 1 236 ? 43.367 29.703 14.268 1.00 19.86 ? 227 SER A O      1 
ATOM   1691 C CB     . SER A 1 236 ? 43.171 31.071 17.130 1.00 19.37 ? 227 SER A CB     1 
ATOM   1692 O OG     . SER A 1 236 ? 43.053 32.373 17.668 1.00 30.92 ? 227 SER A OG     1 
ATOM   1693 N N      . ALA A 1 237 ? 41.781 28.667 15.472 1.00 14.88 ? 228 ALA A N      1 
ATOM   1694 C CA     . ALA A 1 237 ? 42.080 27.391 14.847 1.00 14.07 ? 228 ALA A CA     1 
ATOM   1695 C C      . ALA A 1 237 ? 41.437 27.236 13.492 1.00 13.96 ? 228 ALA A C      1 
ATOM   1696 O O      . ALA A 1 237 ? 42.053 26.641 12.612 1.00 17.86 ? 228 ALA A O      1 
ATOM   1697 C CB     . ALA A 1 237 ? 41.612 26.245 15.758 1.00 18.47 ? 228 ALA A CB     1 
ATOM   1698 N N      . ILE A 1 238 ? 40.204 27.711 13.302 1.00 14.73 ? 229 ILE A N      1 
ATOM   1699 C CA     . ILE A 1 238 ? 39.459 27.423 12.080 1.00 12.56 ? 229 ILE A CA     1 
ATOM   1700 C C      . ILE A 1 238 ? 38.995 28.666 11.352 1.00 12.08 ? 229 ILE A C      1 
ATOM   1701 O O      . ILE A 1 238 ? 38.519 28.538 10.215 1.00 15.28 ? 229 ILE A O      1 
ATOM   1702 C CB     . ILE A 1 238 ? 38.288 26.426 12.292 1.00 12.69 ? 229 ILE A CB     1 
ATOM   1703 C CG1    . ILE A 1 238 ? 37.133 27.039 13.091 1.00 14.14 ? 229 ILE A CG1    1 
ATOM   1704 C CG2    . ILE A 1 238 ? 38.793 25.132 12.927 1.00 15.23 ? 229 ILE A CG2    1 
ATOM   1705 C CD1    . ILE A 1 238 ? 35.906 26.106 13.057 1.00 14.81 ? 229 ILE A CD1    1 
ATOM   1706 N N      . GLY A 1 239 ? 39.132 29.848 11.937 1.00 12.97 ? 230 GLY A N      1 
ATOM   1707 C CA     . GLY A 1 239 ? 38.680 31.073 11.273 1.00 14.68 ? 230 GLY A CA     1 
ATOM   1708 C C      . GLY A 1 239 ? 37.327 31.548 11.779 1.00 14.56 ? 230 GLY A C      1 
ATOM   1709 O O      . GLY A 1 239 ? 36.423 30.708 11.944 1.00 13.37 ? 230 GLY A O      1 
ATOM   1710 N N      . ALA A 1 240 ? 37.181 32.846 12.059 1.00 14.55 ? 231 ALA A N      1 
ATOM   1711 C CA     . ALA A 1 240 ? 35.933 33.337 12.648 1.00 13.16 ? 231 ALA A CA     1 
ATOM   1712 C C      . ALA A 1 240 ? 34.720 32.961 11.818 1.00 11.40 ? 231 ALA A C      1 
ATOM   1713 O O      . ALA A 1 240 ? 33.641 32.690 12.385 1.00 11.94 ? 231 ALA A O      1 
ATOM   1714 C CB     . ALA A 1 240 ? 36.003 34.852 12.827 1.00 16.32 ? 231 ALA A CB     1 
ATOM   1715 N N      . ASP A 1 241 ? 34.829 33.025 10.488 1.00 13.02 ? 232 ASP A N      1 
ATOM   1716 C CA     . ASP A 1 241 ? 33.680 32.831 9.625  1.00 12.89 ? 232 ASP A CA     1 
ATOM   1717 C C      . ASP A 1 241 ? 33.145 31.407 9.672  1.00 14.22 ? 232 ASP A C      1 
ATOM   1718 O O      . ASP A 1 241 ? 32.093 31.128 9.084  1.00 15.98 ? 232 ASP A O      1 
ATOM   1719 C CB     . ASP A 1 241 ? 34.057 33.129 8.172  1.00 18.07 ? 232 ASP A CB     1 
ATOM   1720 C CG     . ASP A 1 241 ? 35.253 32.332 7.738  1.00 22.01 ? 232 ASP A CG     1 
ATOM   1721 O OD1    . ASP A 1 241 ? 36.348 32.620 8.243  1.00 39.44 ? 232 ASP A OD1    1 
ATOM   1722 O OD2    . ASP A 1 241 ? 35.116 31.445 6.866  1.00 47.36 ? 232 ASP A OD2    1 
ATOM   1723 N N      . ARG A 1 242 ? 33.857 30.497 10.347 1.00 11.84 ? 233 ARG A N      1 
ATOM   1724 C CA     . ARG A 1 242 ? 33.392 29.147 10.500 1.00 12.11 ? 233 ARG A CA     1 
ATOM   1725 C C      . ARG A 1 242 ? 32.926 28.863 11.933 1.00 11.59 ? 233 ARG A C      1 
ATOM   1726 O O      . ARG A 1 242 ? 32.739 27.698 12.307 1.00 13.43 ? 233 ARG A O      1 
ATOM   1727 C CB     . ARG A 1 242 ? 34.501 28.177 10.077 1.00 13.43 ? 233 ARG A CB     1 
ATOM   1728 C CG     . ARG A 1 242 ? 34.806 28.261 8.547  1.00 13.94 ? 233 ARG A CG     1 
ATOM   1729 C CD     . ARG A 1 242 ? 35.731 27.108 8.179  1.00 15.65 ? 233 ARG A CD     1 
ATOM   1730 N NE     . ARG A 1 242 ? 36.147 27.260 6.780  1.00 24.85 ? 233 ARG A NE     1 
ATOM   1731 C CZ     . ARG A 1 242 ? 35.530 26.696 5.741  1.00 27.83 ? 233 ARG A CZ     1 
ATOM   1732 N NH1    . ARG A 1 242 ? 34.408 25.984 5.885  1.00 22.21 ? 233 ARG A NH1    1 
ATOM   1733 N NH2    . ARG A 1 242 ? 36.076 26.807 4.527  1.00 28.46 ? 233 ARG A NH2    1 
ATOM   1734 N N      . VAL A 1 243 ? 32.727 29.926 12.735 1.00 10.78 ? 234 VAL A N      1 
ATOM   1735 C CA     . VAL A 1 243 ? 32.381 29.764 14.172 1.00 10.68 ? 234 VAL A CA     1 
ATOM   1736 C C      . VAL A 1 243 ? 31.073 30.494 14.464 1.00 11.64 ? 234 VAL A C      1 
ATOM   1737 O O      . VAL A 1 243 ? 30.947 31.710 14.244 1.00 12.52 ? 234 VAL A O      1 
ATOM   1738 C CB     . VAL A 1 243 ? 33.497 30.302 15.067 1.00 11.20 ? 234 VAL A CB     1 
ATOM   1739 C CG1    . VAL A 1 243 ? 33.054 30.225 16.557 1.00 12.17 ? 234 VAL A CG1    1 
ATOM   1740 C CG2    . VAL A 1 243 ? 34.753 29.523 14.862 1.00 12.71 ? 234 VAL A CG2    1 
ATOM   1741 N N      . GLY A 1 244 ? 30.079 29.744 14.933 1.00 10.68 ? 235 GLY A N      1 
ATOM   1742 C CA     . GLY A 1 244 ? 28.873 30.367 15.482 1.00 11.14 ? 235 GLY A CA     1 
ATOM   1743 C C      . GLY A 1 244 ? 28.833 30.167 16.990 1.00 9.23  ? 235 GLY A C      1 
ATOM   1744 O O      . GLY A 1 244 ? 29.537 29.289 17.530 1.00 10.81 ? 235 GLY A O      1 
ATOM   1745 N N      . VAL A 1 245 ? 28.048 31.004 17.678 1.00 10.61 ? 236 VAL A N      1 
ATOM   1746 C CA     . VAL A 1 245 ? 27.991 30.943 19.151 1.00 10.05 ? 236 VAL A CA     1 
ATOM   1747 C C      . VAL A 1 245 ? 26.530 30.964 19.575 1.00 10.44 ? 236 VAL A C      1 
ATOM   1748 O O      . VAL A 1 245 ? 25.789 31.842 19.129 1.00 11.36 ? 236 VAL A O      1 
ATOM   1749 C CB     . VAL A 1 245 ? 28.715 32.167 19.748 1.00 10.89 ? 236 VAL A CB     1 
ATOM   1750 C CG1    . VAL A 1 245 ? 28.689 32.112 21.282 1.00 13.64 ? 236 VAL A CG1    1 
ATOM   1751 C CG2    . VAL A 1 245 ? 30.171 32.170 19.231 1.00 13.60 ? 236 VAL A CG2    1 
ATOM   1752 N N      . ARG A 1 246 ? 26.120 30.013 20.436 1.00 10.10 ? 237 ARG A N      1 
ATOM   1753 C CA     . ARG A 1 246 ? 24.744 29.926 20.917 1.00 11.67 ? 237 ARG A CA     1 
ATOM   1754 C C      . ARG A 1 246 ? 24.674 30.191 22.406 1.00 9.98  ? 237 ARG A C      1 
ATOM   1755 O O      . ARG A 1 246 ? 25.436 29.617 23.176 1.00 10.37 ? 237 ARG A O      1 
ATOM   1756 C CB     . ARG A 1 246 ? 24.127 28.550 20.608 1.00 10.50 ? 237 ARG A CB     1 
ATOM   1757 C CG     . ARG A 1 246 ? 22.599 28.571 20.800 1.00 10.65 ? 237 ARG A CG     1 
ATOM   1758 C CD     . ARG A 1 246 ? 21.945 27.256 20.401 1.00 11.47 ? 237 ARG A CD     1 
ATOM   1759 N NE     . ARG A 1 246 ? 20.586 27.475 19.909 1.00 10.77 ? 237 ARG A NE     1 
ATOM   1760 C CZ     . ARG A 1 246 ? 19.598 26.593 19.974 1.00 10.28 ? 237 ARG A CZ     1 
ATOM   1761 N NH1    . ARG A 1 246 ? 19.667 25.497 20.726 1.00 10.73 ? 237 ARG A NH1    1 
ATOM   1762 N NH2    . ARG A 1 246 ? 18.502 26.799 19.259 1.00 12.16 ? 237 ARG A NH2    1 
ATOM   1763 N N      . VAL A 1 247 ? 23.804 31.142 22.796 1.00 9.34  ? 238 VAL A N      1 
ATOM   1764 C CA     . VAL A 1 247 ? 23.588 31.445 24.219 1.00 10.41 ? 238 VAL A CA     1 
ATOM   1765 C C      . VAL A 1 247 ? 22.096 31.571 24.502 1.00 10.32 ? 238 VAL A C      1 
ATOM   1766 O O      . VAL A 1 247 ? 21.266 31.694 23.595 1.00 11.20 ? 238 VAL A O      1 
ATOM   1767 C CB     . VAL A 1 247 ? 24.306 32.756 24.667 1.00 11.23 ? 238 VAL A CB     1 
ATOM   1768 C CG1    . VAL A 1 247 ? 25.862 32.524 24.600 1.00 13.18 ? 238 VAL A CG1    1 
ATOM   1769 C CG2    . VAL A 1 247 ? 23.897 33.921 23.804 1.00 12.32 ? 238 VAL A CG2    1 
ATOM   1770 N N      . SER A 1 248 ? 21.767 31.613 25.788 1.00 10.45 ? 239 SER A N      1 
ATOM   1771 C CA     . SER A 1 248 ? 20.369 31.692 26.218 1.00 11.69 ? 239 SER A CA     1 
ATOM   1772 C C      . SER A 1 248 ? 20.301 32.453 27.529 1.00 11.39 ? 239 SER A C      1 
ATOM   1773 O O      . SER A 1 248 ? 20.120 31.873 28.603 1.00 12.44 ? 239 SER A O      1 
ATOM   1774 C CB     . SER A 1 248 ? 19.733 30.307 26.360 1.00 11.08 ? 239 SER A CB     1 
ATOM   1775 O OG     . SER A 1 248 ? 20.401 29.462 27.282 1.00 11.45 ? 239 SER A OG     1 
ATOM   1776 N N      . PRO A 1 249 ? 20.374 33.765 27.477 1.00 11.62 ? 240 PRO A N      1 
ATOM   1777 C CA     . PRO A 1 249 ? 20.410 34.550 28.731 1.00 13.95 ? 240 PRO A CA     1 
ATOM   1778 C C      . PRO A 1 249 ? 19.194 34.400 29.578 1.00 13.80 ? 240 PRO A C      1 
ATOM   1779 O O      . PRO A 1 249 ? 19.336 34.555 30.799 1.00 16.52 ? 240 PRO A O      1 
ATOM   1780 C CB     . PRO A 1 249 ? 20.514 35.998 28.226 1.00 17.45 ? 240 PRO A CB     1 
ATOM   1781 C CG     . PRO A 1 249 ? 21.046 35.902 26.850 1.00 17.04 ? 240 PRO A CG     1 
ATOM   1782 C CD     . PRO A 1 249 ? 20.587 34.607 26.290 1.00 14.67 ? 240 PRO A CD     1 
ATOM   1783 N N      . ALA A 1 250 ? 18.030 34.106 29.014 1.00 14.35 ? 241 ALA A N      1 
ATOM   1784 C CA     . ALA A 1 250 ? 16.843 34.089 29.842 1.00 19.11 ? 241 ALA A CA     1 
ATOM   1785 C C      . ALA A 1 250 ? 16.178 32.722 29.857 1.00 19.33 ? 241 ALA A C      1 
ATOM   1786 O O      . ALA A 1 250 ? 14.972 32.647 30.069 1.00 22.55 ? 241 ALA A O      1 
ATOM   1787 C CB     . ALA A 1 250 ? 15.869 35.154 29.339 1.00 32.50 ? 241 ALA A CB     1 
ATOM   1788 N N      . ILE A 1 251 ? 16.951 31.665 29.667 1.00 14.41 ? 242 ILE A N      1 
ATOM   1789 C CA     . ILE A 1 251 ? 16.427 30.295 29.865 1.00 14.69 ? 242 ILE A CA     1 
ATOM   1790 C C      . ILE A 1 251 ? 17.005 29.860 31.215 1.00 15.65 ? 242 ILE A C      1 
ATOM   1791 O O      . ILE A 1 251 ? 18.204 29.983 31.370 1.00 23.06 ? 242 ILE A O      1 
ATOM   1792 C CB     . ILE A 1 251 ? 16.840 29.352 28.725 1.00 12.98 ? 242 ILE A CB     1 
ATOM   1793 C CG1    . ILE A 1 251 ? 16.125 29.726 27.426 1.00 13.27 ? 242 ILE A CG1    1 
ATOM   1794 C CG2    . ILE A 1 251 ? 16.577 27.908 29.113 1.00 15.90 ? 242 ILE A CG2    1 
ATOM   1795 C CD1    . ILE A 1 251 ? 16.288 28.719 26.317 1.00 12.98 ? 242 ILE A CD1    1 
ATOM   1796 N N      . ASP A 1 252 ? 16.173 29.399 32.139 1.00 21.55 ? 243 ASP A N      1 
ATOM   1797 C CA     . ASP A 1 252 ? 16.662 29.077 33.514 1.00 21.61 ? 243 ASP A CA     1 
ATOM   1798 C C      . ASP A 1 252 ? 16.867 27.575 33.746 1.00 32.02 ? 243 ASP A C      1 
ATOM   1799 O O      . ASP A 1 252 ? 16.970 27.179 34.918 1.00 29.08 ? 243 ASP A O      1 
ATOM   1800 C CB     . ASP A 1 252 ? 15.731 29.677 34.569 1.00 28.55 ? 243 ASP A CB     1 
ATOM   1801 C CG     . ASP A 1 252 ? 14.406 28.945 34.680 1.00 55.21 ? 243 ASP A CG     1 
ATOM   1802 O OD1    . ASP A 1 252 ? 13.723 28.838 33.659 1.00 70.69 ? 243 ASP A OD1    1 
ATOM   1803 O OD2    . ASP A 1 252 ? 14.085 28.461 35.783 1.00 58.03 ? 243 ASP A OD2    1 
ATOM   1804 N N      . HIS A 1 253 ? 16.962 26.794 32.702 1.00 17.82 ? 244 HIS A N      1 
ATOM   1805 C CA     . HIS A 1 253 ? 17.211 25.330 32.768 1.00 16.55 ? 244 HIS A CA     1 
ATOM   1806 C C      . HIS A 1 253 ? 18.345 24.964 33.720 1.00 15.81 ? 244 HIS A C      1 
ATOM   1807 O O      . HIS A 1 253 ? 19.379 25.598 33.647 1.00 15.87 ? 244 HIS A O      1 
ATOM   1808 C CB     . HIS A 1 253 ? 17.551 24.881 31.338 1.00 15.27 ? 244 HIS A CB     1 
ATOM   1809 C CG     . HIS A 1 253 ? 17.612 23.422 31.086 1.00 15.16 ? 244 HIS A CG     1 
ATOM   1810 N ND1    . HIS A 1 253 ? 16.595 22.542 31.370 1.00 18.93 ? 244 HIS A ND1    1 
ATOM   1811 C CD2    . HIS A 1 253 ? 18.582 22.706 30.528 1.00 11.97 ? 244 HIS A CD2    1 
ATOM   1812 C CE1    . HIS A 1 253 ? 16.971 21.328 31.014 1.00 15.92 ? 244 HIS A CE1    1 
ATOM   1813 N NE2    . HIS A 1 253 ? 18.172 21.405 30.503 1.00 20.02 ? 244 HIS A NE2    1 
ATOM   1814 N N      . LEU A 1 254 ? 18.133 23.941 34.557 1.00 13.64 ? 245 LEU A N      1 
ATOM   1815 C CA     . LEU A 1 254 ? 19.204 23.406 35.399 1.00 13.15 ? 245 LEU A CA     1 
ATOM   1816 C C      . LEU A 1 254 ? 19.787 24.465 36.316 1.00 14.76 ? 245 LEU A C      1 
ATOM   1817 O O      . LEU A 1 254 ? 20.993 24.521 36.562 1.00 13.42 ? 245 LEU A O      1 
ATOM   1818 C CB     . LEU A 1 254 ? 20.287 22.728 34.566 1.00 14.19 ? 245 LEU A CB     1 
ATOM   1819 C CG     . LEU A 1 254 ? 19.775 21.648 33.627 1.00 13.50 ? 245 LEU A CG     1 
ATOM   1820 C CD1    . LEU A 1 254 ? 20.953 21.071 32.849 1.00 14.85 ? 245 LEU A CD1    1 
ATOM   1821 C CD2    . LEU A 1 254 ? 19.036 20.541 34.368 1.00 17.05 ? 245 LEU A CD2    1 
ATOM   1822 N N      . ASP A 1 255 ? 18.908 25.330 36.833 1.00 13.89 ? 246 ASP A N      1 
ATOM   1823 C CA     . ASP A 1 255 ? 19.260 26.377 37.813 1.00 14.51 ? 246 ASP A CA     1 
ATOM   1824 C C      . ASP A 1 255 ? 20.060 27.541 37.189 1.00 15.47 ? 246 ASP A C      1 
ATOM   1825 O O      . ASP A 1 255 ? 20.600 28.407 37.906 1.00 17.15 ? 246 ASP A O      1 
ATOM   1826 C CB     . ASP A 1 255 ? 19.895 25.773 39.096 1.00 17.75 ? 246 ASP A CB     1 
ATOM   1827 C CG     . ASP A 1 255 ? 18.906 24.913 39.905 1.00 17.47 ? 246 ASP A CG     1 
ATOM   1828 O OD1    . ASP A 1 255 ? 17.669 25.123 39.836 1.00 23.87 ? 246 ASP A OD1    1 
ATOM   1829 O OD2    . ASP A 1 255 ? 19.371 24.058 40.666 1.00 29.63 ? 246 ASP A OD2    1 
ATOM   1830 N N      . ALA A 1 256 ? 20.032 27.711 35.873 1.00 14.72 ? 247 ALA A N      1 
ATOM   1831 C CA     . ALA A 1 256 ? 20.828 28.727 35.191 1.00 14.21 ? 247 ALA A CA     1 
ATOM   1832 C C      . ALA A 1 256 ? 20.156 30.084 35.085 1.00 24.44 ? 247 ALA A C      1 
ATOM   1833 O O      . ALA A 1 256 ? 19.967 30.613 33.993 1.00 23.02 ? 247 ALA A O      1 
ATOM   1834 C CB     . ALA A 1 256 ? 21.063 28.276 33.759 1.00 16.37 ? 247 ALA A CB     1 
ATOM   1835 N N      . MET A 1 257 ? 20.026 30.754 36.200 1.00 16.13 ? 248 MET A N      1 
ATOM   1836 C CA     . MET A 1 257 ? 19.409 32.079 36.219 1.00 16.31 ? 248 MET A CA     1 
ATOM   1837 C C      . MET A 1 257 ? 20.515 33.122 36.397 1.00 14.50 ? 248 MET A C      1 
ATOM   1838 O O      . MET A 1 257 ? 21.573 32.849 36.989 1.00 14.41 ? 248 MET A O      1 
ATOM   1839 C CB     . MET A 1 257 ? 18.392 32.155 37.365 1.00 23.97 ? 248 MET A CB     1 
ATOM   1840 C CG     . MET A 1 257 ? 18.969 32.473 38.695 1.00 37.76 ? 248 MET A CG     1 
ATOM   1841 S SD     . MET A 1 257 ? 18.994 34.274 39.045 1.00 83.86 ? 248 MET A SD     1 
ATOM   1842 C CE     . MET A 1 257 ? 20.587 34.526 39.909 1.00 24.53 ? 248 MET A CE     1 
ATOM   1843 N N      . ASP A 1 258 ? 20.281 34.316 35.837 1.00 15.88 ? 249 ASP A N      1 
ATOM   1844 C CA     . ASP A 1 258 ? 21.062 35.489 36.128 1.00 14.94 ? 249 ASP A CA     1 
ATOM   1845 C C      . ASP A 1 258 ? 20.194 36.601 36.707 1.00 14.84 ? 249 ASP A C      1 
ATOM   1846 O O      . ASP A 1 258 ? 19.034 36.780 36.312 1.00 17.87 ? 249 ASP A O      1 
ATOM   1847 C CB     . ASP A 1 258 ? 21.811 35.995 34.879 1.00 16.42 ? 249 ASP A CB     1 
ATOM   1848 C CG     . ASP A 1 258 ? 22.991 36.871 35.254 1.00 19.52 ? 249 ASP A CG     1 
ATOM   1849 O OD1    . ASP A 1 258 ? 22.832 38.138 35.336 1.00 20.13 ? 249 ASP A OD1    1 
ATOM   1850 O OD2    . ASP A 1 258 ? 24.118 36.359 35.383 1.00 17.50 ? 249 ASP A OD2    1 
ATOM   1851 N N      . SER A 1 259 ? 20.814 37.344 37.608 1.00 16.20 ? 250 SER A N      1 
ATOM   1852 C CA     . SER A 1 259 ? 20.137 38.474 38.235 1.00 15.24 ? 250 SER A CA     1 
ATOM   1853 C C      . SER A 1 259 ? 19.812 39.576 37.234 1.00 19.71 ? 250 SER A C      1 
ATOM   1854 O O      . SER A 1 259 ? 18.895 40.375 37.477 1.00 19.26 ? 250 SER A O      1 
ATOM   1855 C CB     . SER A 1 259 ? 20.990 39.010 39.378 1.00 21.20 ? 250 SER A CB     1 
ATOM   1856 O OG     . SER A 1 259 ? 22.167 39.637 38.886 1.00 24.12 ? 250 SER A OG     1 
ATOM   1857 N N      . ASN A 1 260 ? 20.528 39.668 36.112 1.00 16.44 ? 251 ASN A N      1 
ATOM   1858 C CA     A ASN A 1 260 ? 20.237 40.679 35.091 0.70 16.18 ? 251 ASN A CA     1 
ATOM   1859 C CA     B ASN A 1 260 ? 20.284 40.697 35.104 0.30 16.29 ? 251 ASN A CA     1 
ATOM   1860 C C      . ASN A 1 260 ? 20.519 40.056 33.745 1.00 15.55 ? 251 ASN A C      1 
ATOM   1861 O O      . ASN A 1 260 ? 21.570 40.271 33.135 1.00 15.10 ? 251 ASN A O      1 
ATOM   1862 C CB     A ASN A 1 260 ? 21.057 41.948 35.282 0.70 14.27 ? 251 ASN A CB     1 
ATOM   1863 C CB     B ASN A 1 260 ? 21.263 41.857 35.319 0.30 14.26 ? 251 ASN A CB     1 
ATOM   1864 C CG     A ASN A 1 260 ? 20.507 43.147 34.436 0.70 16.17 ? 251 ASN A CG     1 
ATOM   1865 C CG     B ASN A 1 260 ? 20.901 42.744 36.507 0.30 17.90 ? 251 ASN A CG     1 
ATOM   1866 O OD1    A ASN A 1 260 ? 19.912 43.002 33.315 0.70 17.33 ? 251 ASN A OD1    1 
ATOM   1867 O OD1    B ASN A 1 260 ? 19.951 43.526 36.460 0.30 22.13 ? 251 ASN A OD1    1 
ATOM   1868 N ND2    A ASN A 1 260 ? 20.768 44.360 34.954 0.70 28.32 ? 251 ASN A ND2    1 
ATOM   1869 N ND2    B ASN A 1 260 ? 21.615 42.562 37.608 0.30 19.51 ? 251 ASN A ND2    1 
ATOM   1870 N N      . PRO A 1 261 ? 19.551 39.327 33.214 1.00 15.64 ? 252 PRO A N      1 
ATOM   1871 C CA     . PRO A 1 261 ? 19.773 38.581 31.952 1.00 14.19 ? 252 PRO A CA     1 
ATOM   1872 C C      . PRO A 1 261 ? 20.127 39.446 30.758 1.00 14.15 ? 252 PRO A C      1 
ATOM   1873 O O      . PRO A 1 261 ? 21.010 39.071 29.966 1.00 13.82 ? 252 PRO A O      1 
ATOM   1874 C CB     . PRO A 1 261 ? 18.447 37.853 31.733 1.00 16.31 ? 252 PRO A CB     1 
ATOM   1875 C CG     . PRO A 1 261 ? 17.907 37.653 33.154 1.00 17.09 ? 252 PRO A CG     1 
ATOM   1876 C CD     . PRO A 1 261 ? 18.303 38.896 33.893 1.00 17.94 ? 252 PRO A CD     1 
ATOM   1877 N N      . LEU A 1 262 ? 19.439 40.569 30.563 1.00 14.48 ? 253 LEU A N      1 
ATOM   1878 C CA     . LEU A 1 262 ? 19.830 41.418 29.437 1.00 13.37 ? 253 LEU A CA     1 
ATOM   1879 C C      . LEU A 1 262 ? 21.256 41.931 29.584 1.00 13.20 ? 253 LEU A C      1 
ATOM   1880 O O      . LEU A 1 262 ? 22.012 41.951 28.608 1.00 13.65 ? 253 LEU A O      1 
ATOM   1881 C CB     . LEU A 1 262 ? 18.816 42.564 29.290 1.00 16.88 ? 253 LEU A CB     1 
ATOM   1882 C CG     . LEU A 1 262 ? 19.252 43.568 28.235 1.00 14.29 ? 253 LEU A CG     1 
ATOM   1883 C CD1    . LEU A 1 262 ? 19.306 42.960 26.857 1.00 16.44 ? 253 LEU A CD1    1 
ATOM   1884 C CD2    . LEU A 1 262 ? 18.226 44.735 28.274 1.00 16.85 ? 253 LEU A CD2    1 
ATOM   1885 N N      . SER A 1 263 ? 21.649 42.388 30.787 1.00 13.21 ? 254 SER A N      1 
ATOM   1886 C CA     . SER A 1 263 ? 22.997 42.888 30.969 1.00 11.57 ? 254 SER A CA     1 
ATOM   1887 C C      . SER A 1 263 ? 24.017 41.789 30.670 1.00 13.13 ? 254 SER A C      1 
ATOM   1888 O O      . SER A 1 263 ? 25.054 42.040 30.056 1.00 12.74 ? 254 SER A O      1 
ATOM   1889 C CB     . SER A 1 263 ? 23.124 43.401 32.398 1.00 14.77 ? 254 SER A CB     1 
ATOM   1890 O OG     . SER A 1 263 ? 24.424 43.845 32.660 1.00 17.78 ? 254 SER A OG     1 
ATOM   1891 N N      . LEU A 1 264 ? 23.759 40.559 31.142 1.00 12.04 ? 255 LEU A N      1 
ATOM   1892 C CA     . LEU A 1 264 ? 24.663 39.446 30.854 1.00 11.48 ? 255 LEU A CA     1 
ATOM   1893 C C      . LEU A 1 264 ? 24.751 39.203 29.350 1.00 12.86 ? 255 LEU A C      1 
ATOM   1894 O O      . LEU A 1 264 ? 25.854 39.016 28.787 1.00 12.97 ? 255 LEU A O      1 
ATOM   1895 C CB     . LEU A 1 264 ? 24.174 38.189 31.600 1.00 12.47 ? 255 LEU A CB     1 
ATOM   1896 C CG     . LEU A 1 264 ? 24.992 36.920 31.236 1.00 13.74 ? 255 LEU A CG     1 
ATOM   1897 C CD1    . LEU A 1 264 ? 26.486 37.107 31.653 1.00 13.99 ? 255 LEU A CD1    1 
ATOM   1898 C CD2    . LEU A 1 264 ? 24.333 35.694 31.895 1.00 15.28 ? 255 LEU A CD2    1 
ATOM   1899 N N      . GLY A 1 265 ? 23.595 39.153 28.662 1.00 12.02 ? 256 GLY A N      1 
ATOM   1900 C CA     . GLY A 1 265 ? 23.589 38.974 27.215 1.00 12.40 ? 256 GLY A CA     1 
ATOM   1901 C C      . GLY A 1 265 ? 24.361 40.057 26.496 1.00 12.82 ? 256 GLY A C      1 
ATOM   1902 O O      . GLY A 1 265 ? 25.131 39.761 25.564 1.00 12.20 ? 256 GLY A O      1 
ATOM   1903 N N      . LEU A 1 266 ? 24.174 41.317 26.910 1.00 13.05 ? 257 LEU A N      1 
ATOM   1904 C CA     . LEU A 1 266 ? 24.917 42.394 26.264 1.00 12.04 ? 257 LEU A CA     1 
ATOM   1905 C C      . LEU A 1 266 ? 26.399 42.284 26.568 1.00 13.72 ? 257 LEU A C      1 
ATOM   1906 O O      . LEU A 1 266 ? 27.212 42.628 25.721 1.00 14.21 ? 257 LEU A O      1 
ATOM   1907 C CB     . LEU A 1 266 ? 24.362 43.730 26.750 1.00 12.40 ? 257 LEU A CB     1 
ATOM   1908 C CG     . LEU A 1 266 ? 22.966 44.069 26.241 1.00 11.68 ? 257 LEU A CG     1 
ATOM   1909 C CD1    . LEU A 1 266 ? 22.486 45.337 26.911 1.00 15.07 ? 257 LEU A CD1    1 
ATOM   1910 C CD2    . LEU A 1 266 ? 22.914 44.219 24.731 1.00 15.34 ? 257 LEU A CD2    1 
ATOM   1911 N N      . ALA A 1 267 ? 26.777 41.769 27.745 1.00 11.98 ? 258 ALA A N      1 
ATOM   1912 C CA     . ALA A 1 267 ? 28.198 41.619 28.023 1.00 10.77 ? 258 ALA A CA     1 
ATOM   1913 C C      . ALA A 1 267 ? 28.817 40.533 27.137 1.00 11.88 ? 258 ALA A C      1 
ATOM   1914 O O      . ALA A 1 267 ? 29.950 40.696 26.642 1.00 14.05 ? 258 ALA A O      1 
ATOM   1915 C CB     . ALA A 1 267 ? 28.448 41.317 29.512 1.00 13.33 ? 258 ALA A CB     1 
ATOM   1916 N N      . VAL A 1 268 ? 28.085 39.440 26.889 1.00 11.80 ? 259 VAL A N      1 
ATOM   1917 C CA     . VAL A 1 268 ? 28.584 38.414 25.961 1.00 12.23 ? 259 VAL A CA     1 
ATOM   1918 C C      . VAL A 1 268 ? 28.726 39.012 24.569 1.00 11.76 ? 259 VAL A C      1 
ATOM   1919 O O      . VAL A 1 268 ? 29.735 38.809 23.892 1.00 13.61 ? 259 VAL A O      1 
ATOM   1920 C CB     . VAL A 1 268 ? 27.667 37.177 25.955 1.00 12.72 ? 259 VAL A CB     1 
ATOM   1921 C CG1    . VAL A 1 268 ? 28.126 36.199 24.809 1.00 13.03 ? 259 VAL A CG1    1 
ATOM   1922 C CG2    . VAL A 1 268 ? 27.727 36.483 27.307 1.00 11.64 ? 259 VAL A CG2    1 
ATOM   1923 N N      . VAL A 1 269 ? 27.709 39.757 24.133 1.00 11.99 ? 260 VAL A N      1 
ATOM   1924 C CA     . VAL A 1 269 ? 27.754 40.317 22.781 1.00 11.59 ? 260 VAL A CA     1 
ATOM   1925 C C      . VAL A 1 269 ? 28.949 41.254 22.650 1.00 13.78 ? 260 VAL A C      1 
ATOM   1926 O O      . VAL A 1 269 ? 29.633 41.245 21.624 1.00 14.32 ? 260 VAL A O      1 
ATOM   1927 C CB     . VAL A 1 269 ? 26.427 41.046 22.494 1.00 12.20 ? 260 VAL A CB     1 
ATOM   1928 C CG1    . VAL A 1 269 ? 26.577 41.906 21.216 1.00 13.94 ? 260 VAL A CG1    1 
ATOM   1929 C CG2    . VAL A 1 269 ? 25.314 40.085 22.328 1.00 12.48 ? 260 VAL A CG2    1 
ATOM   1930 N N      . GLU A 1 270 ? 29.218 42.067 23.669 1.00 13.97 ? 261 GLU A N      1 
ATOM   1931 C CA     . GLU A 1 270 ? 30.374 42.957 23.579 1.00 15.07 ? 261 GLU A CA     1 
ATOM   1932 C C      . GLU A 1 270 ? 31.669 42.189 23.397 1.00 16.47 ? 261 GLU A C      1 
ATOM   1933 O O      . GLU A 1 270 ? 32.524 42.613 22.612 1.00 16.46 ? 261 GLU A O      1 
ATOM   1934 C CB     . GLU A 1 270 ? 30.452 43.833 24.817 1.00 18.19 ? 261 GLU A CB     1 
ATOM   1935 C CG     . GLU A 1 270 ? 31.612 44.810 24.729 1.00 25.83 ? 261 GLU A CG     1 
ATOM   1936 C CD     . GLU A 1 270 ? 32.343 44.832 26.046 1.00 62.86 ? 261 GLU A CD     1 
ATOM   1937 O OE1    . GLU A 1 270 ? 31.954 45.610 26.946 1.00 73.95 ? 261 GLU A OE1    1 
ATOM   1938 O OE2    . GLU A 1 270 ? 33.313 44.035 26.178 1.00 58.18 ? 261 GLU A OE2    1 
ATOM   1939 N N      . ARG A 1 271 ? 31.817 41.029 24.066 1.00 14.50 ? 262 ARG A N      1 
ATOM   1940 C CA     . ARG A 1 271 ? 33.033 40.237 23.901 1.00 14.77 ? 262 ARG A CA     1 
ATOM   1941 C C      . ARG A 1 271 ? 33.117 39.683 22.487 1.00 13.89 ? 262 ARG A C      1 
ATOM   1942 O O      . ARG A 1 271 ? 34.200 39.618 21.901 1.00 15.21 ? 262 ARG A O      1 
ATOM   1943 C CB     . ARG A 1 271 ? 33.088 39.032 24.872 1.00 17.18 ? 262 ARG A CB     1 
ATOM   1944 C CG     . ARG A 1 271 ? 32.933 39.308 26.359 1.00 25.35 ? 262 ARG A CG     1 
ATOM   1945 C CD     . ARG A 1 271 ? 33.798 40.387 26.701 1.00 24.28 ? 262 ARG A CD     1 
ATOM   1946 N NE     . ARG A 1 271 ? 35.179 39.934 26.589 1.00 33.23 ? 262 ARG A NE     1 
ATOM   1947 C CZ     . ARG A 1 271 ? 36.220 40.720 26.319 1.00 45.97 ? 262 ARG A CZ     1 
ATOM   1948 N NH1    . ARG A 1 271 ? 36.064 42.000 25.999 1.00 41.42 ? 262 ARG A NH1    1 
ATOM   1949 N NH2    . ARG A 1 271 ? 37.449 40.209 26.376 1.00 29.71 ? 262 ARG A NH2    1 
ATOM   1950 N N      . LEU A 1 272 ? 31.989 39.249 21.909 1.00 12.69 ? 263 LEU A N      1 
ATOM   1951 C CA     . LEU A 1 272 ? 32.051 38.729 20.538 1.00 12.99 ? 263 LEU A CA     1 
ATOM   1952 C C      . LEU A 1 272 ? 32.422 39.840 19.566 1.00 13.15 ? 263 LEU A C      1 
ATOM   1953 O O      . LEU A 1 272 ? 33.215 39.615 18.647 1.00 13.51 ? 263 LEU A O      1 
ATOM   1954 C CB     . LEU A 1 272 ? 30.699 38.104 20.131 1.00 12.70 ? 263 LEU A CB     1 
ATOM   1955 C CG     . LEU A 1 272 ? 30.255 36.961 21.058 1.00 12.60 ? 263 LEU A CG     1 
ATOM   1956 C CD1    . LEU A 1 272 ? 28.959 36.418 20.540 1.00 16.83 ? 263 LEU A CD1    1 
ATOM   1957 C CD2    . LEU A 1 272 ? 31.306 35.870 21.103 1.00 14.41 ? 263 LEU A CD2    1 
ATOM   1958 N N      . ASN A 1 273 ? 31.858 41.039 19.760 1.00 12.05 ? 264 ASN A N      1 
ATOM   1959 C CA     . ASN A 1 273 ? 32.243 42.174 18.918 1.00 12.65 ? 264 ASN A CA     1 
ATOM   1960 C C      . ASN A 1 273 ? 33.739 42.437 19.026 1.00 13.07 ? 264 ASN A C      1 
ATOM   1961 O O      . ASN A 1 273 ? 34.394 42.697 17.997 1.00 14.19 ? 264 ASN A O      1 
ATOM   1962 C CB     . ASN A 1 273 ? 31.453 43.431 19.285 1.00 13.79 ? 264 ASN A CB     1 
ATOM   1963 C CG     . ASN A 1 273 ? 30.001 43.376 18.872 1.00 12.10 ? 264 ASN A CG     1 
ATOM   1964 O OD1    . ASN A 1 273 ? 29.581 42.554 18.052 1.00 13.39 ? 264 ASN A OD1    1 
ATOM   1965 N ND2    . ASN A 1 273 ? 29.224 44.294 19.426 1.00 13.85 ? 264 ASN A ND2    1 
ATOM   1966 N N      . LYS A 1 274 ? 34.296 42.389 20.247 1.00 12.85 ? 265 LYS A N      1 
ATOM   1967 C CA     . LYS A 1 274 ? 35.742 42.603 20.355 1.00 14.36 ? 265 LYS A CA     1 
ATOM   1968 C C      . LYS A 1 274 ? 36.588 41.495 19.743 1.00 18.28 ? 265 LYS A C      1 
ATOM   1969 O O      . LYS A 1 274 ? 37.633 41.791 19.145 1.00 17.47 ? 265 LYS A O      1 
ATOM   1970 C CB     . LYS A 1 274 ? 36.231 42.976 21.755 1.00 20.76 ? 265 LYS A CB     1 
ATOM   1971 C CG     . LYS A 1 274 ? 35.326 43.721 22.669 1.00 31.33 ? 265 LYS A CG     1 
ATOM   1972 C CD     . LYS A 1 274 ? 36.323 44.459 23.581 1.00 52.03 ? 265 LYS A CD     1 
ATOM   1973 C CE     . LYS A 1 274 ? 35.814 45.743 24.211 1.00 57.85 ? 265 LYS A CE     1 
ATOM   1974 N NZ     . LYS A 1 274 ? 34.456 45.648 24.722 1.00 50.77 ? 265 LYS A NZ     1 
ATOM   1975 N N      . ILE A 1 275 ? 36.169 40.223 19.852 1.00 15.33 ? 266 ILE A N      1 
ATOM   1976 C CA     . ILE A 1 275 ? 36.914 39.155 19.194 1.00 15.18 ? 266 ILE A CA     1 
ATOM   1977 C C      . ILE A 1 275 ? 36.985 39.437 17.710 1.00 17.77 ? 266 ILE A C      1 
ATOM   1978 O O      . ILE A 1 275 ? 38.008 39.191 17.062 1.00 18.04 ? 266 ILE A O      1 
ATOM   1979 C CB     . ILE A 1 275 ? 36.245 37.795 19.477 1.00 15.76 ? 266 ILE A CB     1 
ATOM   1980 C CG1    . ILE A 1 275 ? 36.535 37.356 20.911 1.00 16.89 ? 266 ILE A CG1    1 
ATOM   1981 C CG2    . ILE A 1 275 ? 36.802 36.661 18.513 1.00 17.18 ? 266 ILE A CG2    1 
ATOM   1982 C CD1    . ILE A 1 275 ? 35.659 36.158 21.439 1.00 16.32 ? 266 ILE A CD1    1 
ATOM   1983 N N      . GLN A 1 276 ? 35.874 39.890 17.139 1.00 15.57 ? 267 GLN A N      1 
ATOM   1984 C CA     . GLN A 1 276 ? 35.807 40.160 15.704 1.00 13.89 ? 267 GLN A CA     1 
ATOM   1985 C C      . GLN A 1 276 ? 36.739 41.294 15.328 1.00 19.46 ? 267 GLN A C      1 
ATOM   1986 O O      . GLN A 1 276 ? 37.456 41.196 14.316 1.00 20.79 ? 267 GLN A O      1 
ATOM   1987 C CB     . GLN A 1 276 ? 34.361 40.504 15.303 1.00 13.07 ? 267 GLN A CB     1 
ATOM   1988 C CG     . GLN A 1 276 ? 33.454 39.286 15.396 1.00 14.64 ? 267 GLN A CG     1 
ATOM   1989 C CD     . GLN A 1 276 ? 32.023 39.522 15.039 1.00 13.47 ? 267 GLN A CD     1 
ATOM   1990 O OE1    . GLN A 1 276 ? 31.324 38.569 14.743 1.00 14.54 ? 267 GLN A OE1    1 
ATOM   1991 N NE2    . GLN A 1 276 ? 31.550 40.759 15.064 1.00 15.32 ? 267 GLN A NE2    1 
ATOM   1992 N N      . LEU A 1 277 ? 36.705 42.390 16.105 1.00 17.48 ? 268 LEU A N      1 
ATOM   1993 C CA     . LEU A 1 277 ? 37.606 43.522 15.844 1.00 20.21 ? 268 LEU A CA     1 
ATOM   1994 C C      . LEU A 1 277 ? 39.055 43.092 15.950 1.00 25.10 ? 268 LEU A C      1 
ATOM   1995 O O      . LEU A 1 277 ? 39.861 43.392 15.059 1.00 28.75 ? 268 LEU A O      1 
ATOM   1996 C CB     . LEU A 1 277 ? 37.289 44.697 16.768 1.00 27.42 ? 268 LEU A CB     1 
ATOM   1997 C CG     . LEU A 1 277 ? 35.894 45.269 16.491 1.00 26.91 ? 268 LEU A CG     1 
ATOM   1998 C CD1    . LEU A 1 277 ? 35.341 46.237 17.540 1.00 33.59 ? 268 LEU A CD1    1 
ATOM   1999 C CD2    . LEU A 1 277 ? 35.851 45.899 15.084 1.00 34.33 ? 268 LEU A CD2    1 
ATOM   2000 N N      . HIS A 1 278 ? 39.402 42.338 16.985 1.00 24.45 ? 269 HIS A N      1 
ATOM   2001 C CA     A HIS A 1 278 ? 40.790 41.908 17.172 0.45 28.30 ? 269 HIS A CA     1 
ATOM   2002 C CA     B HIS A 1 278 ? 40.797 41.942 17.150 0.55 28.31 ? 269 HIS A CA     1 
ATOM   2003 C C      . HIS A 1 278 ? 41.252 40.959 16.072 1.00 32.20 ? 269 HIS A C      1 
ATOM   2004 O O      . HIS A 1 278 ? 42.432 40.968 15.699 1.00 39.34 ? 269 HIS A O      1 
ATOM   2005 C CB     A HIS A 1 278 ? 40.988 41.317 18.581 0.45 30.53 ? 269 HIS A CB     1 
ATOM   2006 C CB     B HIS A 1 278 ? 41.064 41.426 18.571 0.55 30.55 ? 269 HIS A CB     1 
ATOM   2007 C CG     A HIS A 1 278 ? 42.261 40.539 18.764 0.45 30.64 ? 269 HIS A CG     1 
ATOM   2008 C CG     B HIS A 1 278 ? 40.909 42.471 19.639 0.55 30.69 ? 269 HIS A CG     1 
ATOM   2009 N ND1    A HIS A 1 278 ? 42.476 39.302 18.192 0.45 32.43 ? 269 HIS A ND1    1 
ATOM   2010 N ND1    B HIS A 1 278 ? 40.384 43.722 19.398 0.55 36.66 ? 269 HIS A ND1    1 
ATOM   2011 C CD2    A HIS A 1 278 ? 43.390 40.832 19.454 0.45 34.63 ? 269 HIS A CD2    1 
ATOM   2012 C CD2    B HIS A 1 278 ? 41.218 42.446 20.959 0.55 27.25 ? 269 HIS A CD2    1 
ATOM   2013 C CE1    A HIS A 1 278 ? 43.672 38.860 18.534 0.45 32.26 ? 269 HIS A CE1    1 
ATOM   2014 C CE1    B HIS A 1 278 ? 40.372 44.419 20.520 0.55 36.38 ? 269 HIS A CE1    1 
ATOM   2015 N NE2    A HIS A 1 278 ? 44.251 39.773 19.293 0.45 36.24 ? 269 HIS A NE2    1 
ATOM   2016 N NE2    B HIS A 1 278 ? 40.871 43.667 21.482 0.55 31.29 ? 269 HIS A NE2    1 
ATOM   2017 N N      . SER A 1 279 ? 40.359 40.121 15.544 1.00 27.52 ? 270 SER A N      1 
ATOM   2018 C CA     . SER A 1 279 ? 40.749 39.151 14.528 1.00 24.18 ? 270 SER A CA     1 
ATOM   2019 C C      . SER A 1 279 ? 40.511 39.648 13.101 1.00 30.35 ? 270 SER A C      1 
ATOM   2020 O O      . SER A 1 279 ? 40.897 38.959 12.148 1.00 34.89 ? 270 SER A O      1 
ATOM   2021 C CB     . SER A 1 279 ? 40.052 37.818 14.759 1.00 34.75 ? 270 SER A CB     1 
ATOM   2022 O OG     . SER A 1 279 ? 38.703 37.975 14.402 1.00 41.83 ? 270 SER A OG     1 
ATOM   2023 N N      . GLY A 1 280 ? 39.895 40.816 12.939 1.00 25.30 ? 271 GLY A N      1 
ATOM   2024 C CA     . GLY A 1 280 ? 39.626 41.367 11.623 1.00 25.34 ? 271 GLY A CA     1 
ATOM   2025 C C      . GLY A 1 280 ? 38.620 40.587 10.807 1.00 27.62 ? 271 GLY A C      1 
ATOM   2026 O O      . GLY A 1 280 ? 38.594 40.721 9.585  1.00 26.66 ? 271 GLY A O      1 
ATOM   2027 N N      . SER A 1 281 ? 37.785 39.752 11.436 1.00 24.56 ? 272 SER A N      1 
ATOM   2028 C CA     . SER A 1 281 ? 36.790 39.005 10.681 1.00 23.10 ? 272 SER A CA     1 
ATOM   2029 C C      . SER A 1 281 ? 35.564 38.807 11.559 1.00 20.57 ? 272 SER A C      1 
ATOM   2030 O O      . SER A 1 281 ? 35.636 38.880 12.773 1.00 26.54 ? 272 SER A O      1 
ATOM   2031 C CB     . SER A 1 281 ? 37.268 37.603 10.271 1.00 30.69 ? 272 SER A CB     1 
ATOM   2032 O OG     . SER A 1 281 ? 36.260 36.942 9.496  1.00 40.54 ? 272 SER A OG     1 
ATOM   2033 N N      . LYS A 1 282 ? 34.435 38.555 10.935 1.00 19.21 ? 273 LYS A N      1 
ATOM   2034 C CA     . LYS A 1 282 ? 33.210 38.320 11.661 1.00 18.09 ? 273 LYS A CA     1 
ATOM   2035 C C      . LYS A 1 282 ? 32.988 36.827 11.874 1.00 13.44 ? 273 LYS A C      1 
ATOM   2036 O O      . LYS A 1 282 ? 33.350 35.983 11.068 1.00 14.95 ? 273 LYS A O      1 
ATOM   2037 C CB     . LYS A 1 282 ? 31.987 38.895 10.941 1.00 20.79 ? 273 LYS A CB     1 
ATOM   2038 C CG     . LYS A 1 282 ? 31.812 40.451 11.154 1.00 28.60 ? 273 LYS A CG     1 
ATOM   2039 C CD     . LYS A 1 282 ? 30.588 40.969 10.400 1.00 40.34 ? 273 LYS A CD     1 
ATOM   2040 C CE     . LYS A 1 282 ? 30.599 42.502 10.329 1.00 39.96 ? 273 LYS A CE     1 
ATOM   2041 N NZ     . LYS A 1 282 ? 31.128 43.071 11.591 1.00 33.04 ? 273 LYS A NZ     1 
ATOM   2042 N N      . LEU A 1 283 ? 32.392 36.529 13.019 1.00 13.13 ? 274 LEU A N      1 
ATOM   2043 C CA     . LEU A 1 283 ? 31.899 35.181 13.257 1.00 11.73 ? 274 LEU A CA     1 
ATOM   2044 C C      . LEU A 1 283 ? 30.860 34.814 12.194 1.00 12.28 ? 274 LEU A C      1 
ATOM   2045 O O      . LEU A 1 283 ? 30.253 35.675 11.535 1.00 13.21 ? 274 LEU A O      1 
ATOM   2046 C CB     . LEU A 1 283 ? 31.265 35.106 14.649 1.00 12.75 ? 274 LEU A CB     1 
ATOM   2047 C CG     . LEU A 1 283 ? 32.226 35.433 15.794 1.00 14.22 ? 274 LEU A CG     1 
ATOM   2048 C CD1    . LEU A 1 283 ? 31.469 35.698 17.096 1.00 17.75 ? 274 LEU A CD1    1 
ATOM   2049 C CD2    . LEU A 1 283 ? 33.182 34.245 16.016 1.00 16.16 ? 274 LEU A CD2    1 
ATOM   2050 N N      . ALA A 1 284 ? 30.546 33.520 12.105 1.00 11.66 ? 275 ALA A N      1 
ATOM   2051 C CA     . ALA A 1 284 ? 29.451 33.121 11.254 1.00 11.76 ? 275 ALA A CA     1 
ATOM   2052 C C      . ALA A 1 284 ? 28.145 33.716 11.739 1.00 11.73 ? 275 ALA A C      1 
ATOM   2053 O O      . ALA A 1 284 ? 27.334 34.167 10.930 1.00 13.07 ? 275 ALA A O      1 
ATOM   2054 C CB     . ALA A 1 284 ? 29.395 31.582 11.192 1.00 14.18 ? 275 ALA A CB     1 
ATOM   2055 N N      . TYR A 1 285 ? 27.900 33.682 13.054 1.00 12.08 ? 276 TYR A N      1 
ATOM   2056 C CA     . TYR A 1 285 ? 26.666 34.219 13.594 1.00 10.59 ? 276 TYR A CA     1 
ATOM   2057 C C      . TYR A 1 285 ? 26.689 34.148 15.114 1.00 9.55  ? 276 TYR A C      1 
ATOM   2058 O O      . TYR A 1 285 ? 27.495 33.413 15.723 1.00 11.67 ? 276 TYR A O      1 
ATOM   2059 C CB     . TYR A 1 285 ? 25.456 33.411 13.115 1.00 11.22 ? 276 TYR A CB     1 
ATOM   2060 C CG     . TYR A 1 285 ? 25.542 31.929 13.455 1.00 9.73  ? 276 TYR A CG     1 
ATOM   2061 C CD1    . TYR A 1 285 ? 25.143 31.439 14.722 1.00 11.49 ? 276 TYR A CD1    1 
ATOM   2062 C CD2    . TYR A 1 285 ? 25.985 31.008 12.485 1.00 9.92  ? 276 TYR A CD2    1 
ATOM   2063 C CE1    . TYR A 1 285 ? 25.201 30.074 15.023 1.00 10.62 ? 276 TYR A CE1    1 
ATOM   2064 C CE2    . TYR A 1 285 ? 26.083 29.644 12.773 1.00 10.95 ? 276 TYR A CE2    1 
ATOM   2065 C CZ     . TYR A 1 285 ? 25.662 29.194 14.024 1.00 10.83 ? 276 TYR A CZ     1 
ATOM   2066 O OH     . TYR A 1 285 ? 25.726 27.872 14.313 1.00 12.20 ? 276 TYR A OH     1 
ATOM   2067 N N      . LEU A 1 286 ? 25.741 34.902 15.691 1.00 9.20  ? 277 LEU A N      1 
ATOM   2068 C CA     . LEU A 1 286 ? 25.280 34.748 17.072 1.00 9.21  ? 277 LEU A CA     1 
ATOM   2069 C C      . LEU A 1 286 ? 23.880 34.131 17.022 1.00 9.41  ? 277 LEU A C      1 
ATOM   2070 O O      . LEU A 1 286 ? 23.026 34.587 16.257 1.00 12.42 ? 277 LEU A O      1 
ATOM   2071 C CB     . LEU A 1 286 ? 25.233 36.121 17.764 1.00 11.07 ? 277 LEU A CB     1 
ATOM   2072 C CG     . LEU A 1 286 ? 24.515 36.125 19.127 1.00 11.76 ? 277 LEU A CG     1 
ATOM   2073 C CD1    . LEU A 1 286 ? 25.226 35.273 20.156 1.00 13.19 ? 277 LEU A CD1    1 
ATOM   2074 C CD2    . LEU A 1 286 ? 24.385 37.556 19.610 1.00 12.76 ? 277 LEU A CD2    1 
ATOM   2075 N N      . HIS A 1 287 ? 23.644 33.098 17.840 1.00 10.25 ? 278 HIS A N      1 
ATOM   2076 C CA     . HIS A 1 287 ? 22.381 32.350 17.865 1.00 9.35  ? 278 HIS A CA     1 
ATOM   2077 C C      . HIS A 1 287 ? 21.849 32.466 19.287 1.00 10.68 ? 278 HIS A C      1 
ATOM   2078 O O      . HIS A 1 287 ? 22.499 32.001 20.241 1.00 10.59 ? 278 HIS A O      1 
ATOM   2079 C CB     . HIS A 1 287 ? 22.728 30.884 17.485 1.00 10.02 ? 278 HIS A CB     1 
ATOM   2080 C CG     . HIS A 1 287 ? 21.578 29.935 17.326 1.00 9.73  ? 278 HIS A CG     1 
ATOM   2081 N ND1    . HIS A 1 287 ? 21.791 28.637 16.892 1.00 10.88 ? 278 HIS A ND1    1 
ATOM   2082 C CD2    . HIS A 1 287 ? 20.243 30.098 17.417 1.00 11.01 ? 278 HIS A CD2    1 
ATOM   2083 C CE1    . HIS A 1 287 ? 20.625 28.021 16.769 1.00 11.89 ? 278 HIS A CE1    1 
ATOM   2084 N NE2    . HIS A 1 287 ? 19.669 28.888 17.064 1.00 10.80 ? 278 HIS A NE2    1 
ATOM   2085 N N      . VAL A 1 288 ? 20.693 33.130 19.448 1.00 10.84 ? 279 VAL A N      1 
ATOM   2086 C CA     . VAL A 1 288 ? 20.127 33.337 20.784 1.00 11.20 ? 279 VAL A CA     1 
ATOM   2087 C C      . VAL A 1 288 ? 18.823 32.579 20.862 1.00 11.32 ? 279 VAL A C      1 
ATOM   2088 O O      . VAL A 1 288 ? 17.972 32.685 19.953 1.00 12.08 ? 279 VAL A O      1 
ATOM   2089 C CB     . VAL A 1 288 ? 19.887 34.817 21.088 1.00 10.45 ? 279 VAL A CB     1 
ATOM   2090 C CG1    . VAL A 1 288 ? 19.211 34.955 22.475 1.00 12.12 ? 279 VAL A CG1    1 
ATOM   2091 C CG2    . VAL A 1 288 ? 21.211 35.547 21.084 1.00 13.06 ? 279 VAL A CG2    1 
ATOM   2092 N N      . THR A 1 289 ? 18.698 31.765 21.894 1.00 10.79 ? 280 THR A N      1 
ATOM   2093 C CA     . THR A 1 289 ? 17.481 30.986 22.087 1.00 9.94  ? 280 THR A CA     1 
ATOM   2094 C C      . THR A 1 289 ? 16.773 31.403 23.362 1.00 11.58 ? 280 THR A C      1 
ATOM   2095 O O      . THR A 1 289 ? 17.406 31.802 24.341 1.00 13.80 ? 280 THR A O      1 
ATOM   2096 C CB     . THR A 1 289 ? 17.797 29.473 21.958 1.00 11.80 ? 280 THR A CB     1 
ATOM   2097 O OG1    . THR A 1 289 ? 16.551 28.766 21.878 1.00 13.42 ? 280 THR A OG1    1 
ATOM   2098 C CG2    . THR A 1 289 ? 18.695 28.977 23.080 1.00 14.64 ? 280 THR A CG2    1 
ATOM   2099 N N      . GLN A 1 290 ? 15.453 31.300 23.329 1.00 12.74 ? 281 GLN A N      1 
ATOM   2100 C CA     . GLN A 1 290 ? 14.607 31.781 24.414 1.00 13.14 ? 281 GLN A CA     1 
ATOM   2101 C C      . GLN A 1 290 ? 13.618 30.695 24.784 1.00 13.45 ? 281 GLN A C      1 
ATOM   2102 O O      . GLN A 1 290 ? 13.471 29.716 24.051 1.00 14.01 ? 281 GLN A O      1 
ATOM   2103 C CB     . GLN A 1 290 ? 13.840 33.002 23.913 1.00 13.71 ? 281 GLN A CB     1 
ATOM   2104 C CG     . GLN A 1 290 ? 12.851 32.658 22.813 1.00 11.98 ? 281 GLN A CG     1 
ATOM   2105 C CD     . GLN A 1 290 ? 12.141 33.836 22.210 1.00 16.06 ? 281 GLN A CD     1 
ATOM   2106 O OE1    . GLN A 1 290 ? 12.330 34.990 22.608 1.00 16.25 ? 281 GLN A OE1    1 
ATOM   2107 N NE2    . GLN A 1 290 ? 11.318 33.569 21.210 1.00 19.02 ? 281 GLN A NE2    1 
ATOM   2108 N N      . PRO A 1 291 ? 12.957 30.802 25.945 1.00 14.86 ? 282 PRO A N      1 
ATOM   2109 C CA     . PRO A 1 291 ? 11.945 29.810 26.299 1.00 16.21 ? 282 PRO A CA     1 
ATOM   2110 C C      . PRO A 1 291 ? 10.923 29.653 25.188 1.00 17.86 ? 282 PRO A C      1 
ATOM   2111 O O      . PRO A 1 291 ? 10.492 30.633 24.551 1.00 18.51 ? 282 PRO A O      1 
ATOM   2112 C CB     . PRO A 1 291 ? 11.293 30.413 27.542 1.00 16.34 ? 282 PRO A CB     1 
ATOM   2113 C CG     . PRO A 1 291 ? 12.343 31.241 28.139 1.00 15.42 ? 282 PRO A CG     1 
ATOM   2114 C CD     . PRO A 1 291 ? 13.156 31.800 26.996 1.00 15.89 ? 282 PRO A CD     1 
ATOM   2115 N N      . GLY A 1 292 ? 10.544 28.419 24.961 1.00 18.45 ? 283 GLY A N      1 
ATOM   2116 C CA     . GLY A 1 292 ? 9.905  28.089 23.712 1.00 20.24 ? 283 GLY A CA     1 
ATOM   2117 C C      . GLY A 1 292 ? 8.452  27.710 23.787 1.00 26.00 ? 283 GLY A C      1 
ATOM   2118 O O      . GLY A 1 292 ? 7.915  27.194 22.797 1.00 29.27 ? 283 GLY A O      1 
ATOM   2119 N N      . ASP A 1 293 ? 7.801  27.968 24.931 1.00 25.61 ? 284 ASP A N      1 
ATOM   2120 C CA     . ASP A 1 293 ? 6.420  27.539 25.162 1.00 30.12 ? 284 ASP A CA     1 
ATOM   2121 C C      . ASP A 1 293 ? 5.580  28.744 25.577 1.00 49.41 ? 284 ASP A C      1 
ATOM   2122 O O      . ASP A 1 293 ? 5.285  28.908 26.764 1.00 55.37 ? 284 ASP A O      1 
ATOM   2123 C CB     . ASP A 1 293 ? 6.411  26.480 26.233 1.00 35.53 ? 284 ASP A CB     1 
ATOM   2124 N N      . GLY A 1 294 ? 5.228  29.586 24.608 1.00 51.22 ? 285 GLY A N      1 
ATOM   2125 C CA     . GLY A 1 294 ? 4.263  30.668 24.805 1.00 41.70 ? 285 GLY A CA     1 
ATOM   2126 C C      . GLY A 1 294 ? 4.286  31.412 26.128 1.00 52.54 ? 285 GLY A C      1 
ATOM   2127 O O      . GLY A 1 294 ? 3.267  31.512 26.817 1.00 46.66 ? 285 GLY A O      1 
ATOM   2128 N N      . SER A 1 297 ? 5.383  38.610 28.618 1.00 46.76 ? 288 SER A N      1 
ATOM   2129 C CA     . SER A 1 297 ? 5.805  37.355 28.007 1.00 44.77 ? 288 SER A CA     1 
ATOM   2130 C C      . SER A 1 297 ? 6.184  37.651 26.554 1.00 54.13 ? 288 SER A C      1 
ATOM   2131 O O      . SER A 1 297 ? 7.375  37.736 26.250 1.00 46.79 ? 288 SER A O      1 
ATOM   2132 C CB     . SER A 1 297 ? 4.708  36.294 28.079 1.00 49.09 ? 288 SER A CB     1 
ATOM   2133 O OG     . SER A 1 297 ? 5.119  35.069 27.496 1.00 53.04 ? 288 SER A OG     1 
ATOM   2134 N N      . GLU A 1 298 ? 5.201  37.846 25.661 1.00 37.59 ? 289 GLU A N      1 
ATOM   2135 C CA     . GLU A 1 298 ? 5.547  37.924 24.245 1.00 37.45 ? 289 GLU A CA     1 
ATOM   2136 C C      . GLU A 1 298 ? 6.333  39.189 23.943 1.00 37.64 ? 289 GLU A C      1 
ATOM   2137 O O      . GLU A 1 298 ? 7.426  39.136 23.356 1.00 30.26 ? 289 GLU A O      1 
ATOM   2138 C CB     . GLU A 1 298 ? 4.316  37.841 23.354 1.00 41.13 ? 289 GLU A CB     1 
ATOM   2139 N N      . GLU A 1 299 ? 5.788  40.338 24.326 1.00 36.67 ? 290 GLU A N      1 
ATOM   2140 C CA     . GLU A 1 299 ? 6.450  41.597 24.013 1.00 36.40 ? 290 GLU A CA     1 
ATOM   2141 C C      . GLU A 1 299 ? 7.803  41.683 24.696 1.00 28.76 ? 290 GLU A C      1 
ATOM   2142 O O      . GLU A 1 299 ? 8.767  42.141 24.076 1.00 27.83 ? 290 GLU A O      1 
ATOM   2143 C CB     . GLU A 1 299 ? 5.563  42.803 24.370 1.00 36.76 ? 290 GLU A CB     1 
ATOM   2144 N N      . GLU A 1 300 ? 7.894  41.270 25.965 1.00 30.37 ? 291 GLU A N      1 
ATOM   2145 C CA     . GLU A 1 300 ? 9.157  41.352 26.700 1.00 24.25 ? 291 GLU A CA     1 
ATOM   2146 C C      . GLU A 1 300 ? 10.206 40.434 26.087 1.00 30.30 ? 291 GLU A C      1 
ATOM   2147 O O      . GLU A 1 300 ? 11.376 40.801 25.975 1.00 24.79 ? 291 GLU A O      1 
ATOM   2148 C CB     . GLU A 1 300 ? 8.936  40.985 28.180 1.00 32.32 ? 291 GLU A CB     1 
ATOM   2149 N N      . GLU A 1 301 ? 9.813  39.227 25.700 1.00 26.37 ? 292 GLU A N      1 
ATOM   2150 C CA     . GLU A 1 301 ? 10.780 38.301 25.134 1.00 23.86 ? 292 GLU A CA     1 
ATOM   2151 C C      . GLU A 1 301 ? 11.259 38.827 23.778 1.00 20.41 ? 292 GLU A C      1 
ATOM   2152 O O      . GLU A 1 301 ? 12.457 38.750 23.472 1.00 17.58 ? 292 GLU A O      1 
ATOM   2153 C CB     . GLU A 1 301 ? 10.100 36.910 25.018 1.00 27.01 ? 292 GLU A CB     1 
ATOM   2154 C CG     . GLU A 1 301 ? 10.521 35.939 26.190 1.00 33.86 ? 292 GLU A CG     1 
ATOM   2155 C CD     . GLU A 1 301 ? 10.133 34.428 26.096 1.00 55.32 ? 292 GLU A CD     1 
ATOM   2156 O OE1    . GLU A 1 301 ? 10.510 33.692 25.133 1.00 32.44 ? 292 GLU A OE1    1 
ATOM   2157 O OE2    . GLU A 1 301 ? 9.428  33.969 27.042 1.00 47.10 ? 292 GLU A OE2    1 
ATOM   2158 N N      . ALA A 1 302 ? 10.357 39.380 22.960 1.00 21.33 ? 293 ALA A N      1 
ATOM   2159 C CA     . ALA A 1 302 ? 10.763 39.919 21.670 1.00 17.79 ? 293 ALA A CA     1 
ATOM   2160 C C      . ALA A 1 302 ? 11.686 41.120 21.821 1.00 20.37 ? 293 ALA A C      1 
ATOM   2161 O O      . ALA A 1 302 ? 12.603 41.306 21.010 1.00 17.97 ? 293 ALA A O      1 
ATOM   2162 C CB     . ALA A 1 302 ? 9.552  40.331 20.825 1.00 21.57 ? 293 ALA A CB     1 
ATOM   2163 N N      . ARG A 1 303 ? 11.474 41.929 22.867 1.00 21.27 ? 294 ARG A N      1 
ATOM   2164 C CA     . ARG A 1 303 ? 12.361 43.076 23.090 1.00 18.16 ? 294 ARG A CA     1 
ATOM   2165 C C      . ARG A 1 303 ? 13.753 42.614 23.505 1.00 15.31 ? 294 ARG A C      1 
ATOM   2166 O O      . ARG A 1 303 ? 14.743 43.154 23.007 1.00 16.35 ? 294 ARG A O      1 
ATOM   2167 C CB     . ARG A 1 303 ? 11.735 44.052 24.105 1.00 17.56 ? 294 ARG A CB     1 
ATOM   2168 C CG     . ARG A 1 303 ? 12.676 45.216 24.512 1.00 22.02 ? 294 ARG A CG     1 
ATOM   2169 C CD     . ARG A 1 303 ? 11.927 46.208 25.385 1.00 21.65 ? 294 ARG A CD     1 
ATOM   2170 N NE     . ARG A 1 303 ? 11.664 45.615 26.684 1.00 26.65 ? 294 ARG A NE     1 
ATOM   2171 C CZ     . ARG A 1 303 ? 11.148 46.285 27.706 1.00 36.56 ? 294 ARG A CZ     1 
ATOM   2172 N NH1    . ARG A 1 303 ? 10.833 47.559 27.587 1.00 28.10 ? 294 ARG A NH1    1 
ATOM   2173 N NH2    . ARG A 1 303 ? 10.976 45.667 28.878 1.00 31.10 ? 294 ARG A NH2    1 
ATOM   2174 N N      . LEU A 1 304 ? 13.865 41.593 24.365 1.00 15.28 ? 295 LEU A N      1 
ATOM   2175 C CA     . LEU A 1 304 ? 15.171 41.077 24.726 1.00 13.42 ? 295 LEU A CA     1 
ATOM   2176 C C      . LEU A 1 304 ? 15.902 40.552 23.492 1.00 12.80 ? 295 LEU A C      1 
ATOM   2177 O O      . LEU A 1 304 ? 17.077 40.887 23.255 1.00 14.14 ? 295 LEU A O      1 
ATOM   2178 C CB     . LEU A 1 304 ? 14.996 39.978 25.789 1.00 16.11 ? 295 LEU A CB     1 
ATOM   2179 C CG     . LEU A 1 304 ? 16.268 39.190 26.022 1.00 19.09 ? 295 LEU A CG     1 
ATOM   2180 C CD1    . LEU A 1 304 ? 17.202 40.100 26.688 1.00 25.69 ? 295 LEU A CD1    1 
ATOM   2181 C CD2    . LEU A 1 304 ? 16.006 37.952 26.913 1.00 23.53 ? 295 LEU A CD2    1 
ATOM   2182 N N      . MET A 1 305 ? 15.200 39.803 22.651 1.00 14.48 ? 296 MET A N      1 
ATOM   2183 C CA     . MET A 1 305 ? 15.840 39.253 21.467 1.00 12.90 ? 296 MET A CA     1 
ATOM   2184 C C      . MET A 1 305 ? 16.325 40.353 20.544 1.00 13.60 ? 296 MET A C      1 
ATOM   2185 O O      . MET A 1 305 ? 17.452 40.303 20.060 1.00 13.39 ? 296 MET A O      1 
ATOM   2186 C CB     . MET A 1 305 ? 14.825 38.337 20.805 1.00 14.43 ? 296 MET A CB     1 
ATOM   2187 C CG     . MET A 1 305 ? 15.328 37.402 19.661 1.00 14.48 ? 296 MET A CG     1 
ATOM   2188 S SD     . MET A 1 305 ? 16.423 36.077 20.243 1.00 16.49 ? 296 MET A SD     1 
ATOM   2189 C CE     . MET A 1 305 ? 15.238 34.792 20.600 1.00 13.85 ? 296 MET A CE     1 
ATOM   2190 N N      . ARG A 1 306 ? 15.470 41.352 20.256 1.00 14.53 ? 297 ARG A N      1 
ATOM   2191 C CA     A ARG A 1 306 ? 15.863 42.455 19.370 0.57 14.92 ? 297 ARG A CA     1 
ATOM   2192 C CA     B ARG A 1 306 ? 15.863 42.452 19.373 0.43 14.96 ? 297 ARG A CA     1 
ATOM   2193 C C      . ARG A 1 306 ? 16.999 43.287 19.974 1.00 14.86 ? 297 ARG A C      1 
ATOM   2194 O O      . ARG A 1 306 ? 17.864 43.789 19.239 1.00 14.81 ? 297 ARG A O      1 
ATOM   2195 C CB     A ARG A 1 306 ? 14.639 43.344 19.084 0.57 17.28 ? 297 ARG A CB     1 
ATOM   2196 C CB     B ARG A 1 306 ? 14.637 43.332 19.103 0.43 17.33 ? 297 ARG A CB     1 
ATOM   2197 C CG     A ARG A 1 306 ? 14.858 44.502 18.102 0.57 25.10 ? 297 ARG A CG     1 
ATOM   2198 C CG     B ARG A 1 306 ? 14.785 44.346 17.992 0.43 24.92 ? 297 ARG A CG     1 
ATOM   2199 C CD     A ARG A 1 306 ? 14.972 44.031 16.655 0.57 21.82 ? 297 ARG A CD     1 
ATOM   2200 C CD     B ARG A 1 306 ? 13.525 45.200 17.882 0.43 22.89 ? 297 ARG A CD     1 
ATOM   2201 N NE     A ARG A 1 306 ? 15.890 44.872 15.895 0.57 26.00 ? 297 ARG A NE     1 
ATOM   2202 N NE     B ARG A 1 306 ? 12.313 44.499 18.297 0.43 25.04 ? 297 ARG A NE     1 
ATOM   2203 C CZ     A ARG A 1 306 ? 15.667 45.440 14.710 0.57 17.43 ? 297 ARG A CZ     1 
ATOM   2204 C CZ     B ARG A 1 306 ? 11.633 44.802 19.397 0.43 25.19 ? 297 ARG A CZ     1 
ATOM   2205 N NH1    A ARG A 1 306 ? 14.534 45.258 14.026 0.57 17.37 ? 297 ARG A NH1    1 
ATOM   2206 N NH1    B ARG A 1 306 ? 11.999 45.808 20.176 0.43 27.61 ? 297 ARG A NH1    1 
ATOM   2207 N NH2    A ARG A 1 306 ? 16.605 46.226 14.197 0.57 30.51 ? 297 ARG A NH2    1 
ATOM   2208 N NH2    B ARG A 1 306 ? 10.569 44.079 19.722 0.43 22.50 ? 297 ARG A NH2    1 
ATOM   2209 N N      . THR A 1 307 ? 17.020 43.460 21.297 1.00 13.46 ? 298 THR A N      1 
ATOM   2210 C CA     . THR A 1 307 ? 18.083 44.248 21.900 1.00 13.05 ? 298 THR A CA     1 
ATOM   2211 C C      . THR A 1 307 ? 19.444 43.573 21.753 1.00 13.96 ? 298 THR A C      1 
ATOM   2212 O O      . THR A 1 307 ? 20.449 44.242 21.475 1.00 13.57 ? 298 THR A O      1 
ATOM   2213 C CB     . THR A 1 307 ? 17.740 44.449 23.366 1.00 15.13 ? 298 THR A CB     1 
ATOM   2214 O OG1    . THR A 1 307 ? 16.470 45.118 23.447 1.00 16.34 ? 298 THR A OG1    1 
ATOM   2215 C CG2    . THR A 1 307 ? 18.805 45.296 24.048 1.00 15.69 ? 298 THR A CG2    1 
ATOM   2216 N N      . LEU A 1 308 ? 19.485 42.246 21.938 1.00 13.78 ? 299 LEU A N      1 
ATOM   2217 C CA     . LEU A 1 308 ? 20.719 41.505 21.714 1.00 12.51 ? 299 LEU A CA     1 
ATOM   2218 C C      . LEU A 1 308 ? 21.133 41.543 20.253 1.00 12.37 ? 299 LEU A C      1 
ATOM   2219 O O      . LEU A 1 308 ? 22.301 41.798 19.943 1.00 12.42 ? 299 LEU A O      1 
ATOM   2220 C CB     . LEU A 1 308 ? 20.561 40.048 22.212 1.00 12.46 ? 299 LEU A CB     1 
ATOM   2221 C CG     . LEU A 1 308 ? 20.260 39.981 23.708 1.00 13.80 ? 299 LEU A CG     1 
ATOM   2222 C CD1    . LEU A 1 308 ? 19.946 38.536 24.085 1.00 16.59 ? 299 LEU A CD1    1 
ATOM   2223 C CD2    . LEU A 1 308 ? 21.421 40.525 24.524 1.00 16.14 ? 299 LEU A CD2    1 
ATOM   2224 N N      . ARG A 1 309 ? 20.168 41.390 19.334 1.00 11.76 ? 300 ARG A N      1 
ATOM   2225 C CA     . ARG A 1 309 ? 20.492 41.496 17.920 1.00 12.31 ? 300 ARG A CA     1 
ATOM   2226 C C      . ARG A 1 309 ? 21.083 42.862 17.605 1.00 12.37 ? 300 ARG A C      1 
ATOM   2227 O O      . ARG A 1 309 ? 22.113 42.960 16.927 1.00 13.65 ? 300 ARG A O      1 
ATOM   2228 C CB     . ARG A 1 309 ? 19.222 41.239 17.122 1.00 11.63 ? 300 ARG A CB     1 
ATOM   2229 C CG     . ARG A 1 309 ? 19.385 41.133 15.603 1.00 12.61 ? 300 ARG A CG     1 
ATOM   2230 C CD     . ARG A 1 309 ? 19.489 42.489 14.853 1.00 13.26 ? 300 ARG A CD     1 
ATOM   2231 N NE     . ARG A 1 309 ? 18.970 42.328 13.494 1.00 14.54 ? 300 ARG A NE     1 
ATOM   2232 C CZ     . ARG A 1 309 ? 19.567 41.605 12.555 1.00 12.92 ? 300 ARG A CZ     1 
ATOM   2233 N NH1    . ARG A 1 309 ? 20.804 41.131 12.714 1.00 14.04 ? 300 ARG A NH1    1 
ATOM   2234 N NH2    . ARG A 1 309 ? 18.919 41.377 11.407 1.00 14.98 ? 300 ARG A NH2    1 
ATOM   2235 N N      . ASN A 1 310 ? 20.439 43.938 18.094 1.00 11.97 ? 301 ASN A N      1 
ATOM   2236 C CA     . ASN A 1 310 ? 20.909 45.275 17.745 1.00 12.11 ? 301 ASN A CA     1 
ATOM   2237 C C      . ASN A 1 310 ? 22.306 45.551 18.288 1.00 12.18 ? 301 ASN A C      1 
ATOM   2238 O O      . ASN A 1 310 ? 23.015 46.414 17.745 1.00 14.34 ? 301 ASN A O      1 
ATOM   2239 C CB     . ASN A 1 310 ? 19.947 46.299 18.324 1.00 12.85 ? 301 ASN A CB     1 
ATOM   2240 C CG     . ASN A 1 310 ? 18.667 46.442 17.545 1.00 14.49 ? 301 ASN A CG     1 
ATOM   2241 O OD1    . ASN A 1 310 ? 18.536 45.957 16.427 1.00 17.23 ? 301 ASN A OD1    1 
ATOM   2242 N ND2    . ASN A 1 310 ? 17.685 47.086 18.172 1.00 16.12 ? 301 ASN A ND2    1 
ATOM   2243 N N      . ALA A 1 311 ? 22.695 44.879 19.381 1.00 12.11 ? 302 ALA A N      1 
ATOM   2244 C CA     . ALA A 1 311 ? 24.007 45.111 19.981 1.00 12.38 ? 302 ALA A CA     1 
ATOM   2245 C C      . ALA A 1 311 ? 25.117 44.353 19.242 1.00 11.98 ? 302 ALA A C      1 
ATOM   2246 O O      . ALA A 1 311 ? 26.286 44.677 19.448 1.00 13.79 ? 302 ALA A O      1 
ATOM   2247 C CB     . ALA A 1 311 ? 23.983 44.659 21.446 1.00 14.19 ? 302 ALA A CB     1 
ATOM   2248 N N      . TYR A 1 312 ? 24.783 43.335 18.445 1.00 10.88 ? 303 TYR A N      1 
ATOM   2249 C CA     . TYR A 1 312 ? 25.774 42.424 17.868 1.00 11.28 ? 303 TYR A CA     1 
ATOM   2250 C C      . TYR A 1 312 ? 26.107 42.845 16.437 1.00 12.13 ? 303 TYR A C      1 
ATOM   2251 O O      . TYR A 1 312 ? 25.211 43.001 15.594 1.00 13.51 ? 303 TYR A O      1 
ATOM   2252 C CB     . TYR A 1 312 ? 25.258 40.964 17.937 1.00 11.99 ? 303 TYR A CB     1 
ATOM   2253 C CG     . TYR A 1 312 ? 26.209 40.061 17.192 1.00 11.48 ? 303 TYR A CG     1 
ATOM   2254 C CD1    . TYR A 1 312 ? 27.522 39.985 17.557 1.00 12.17 ? 303 TYR A CD1    1 
ATOM   2255 C CD2    . TYR A 1 312 ? 25.776 39.317 16.111 1.00 10.63 ? 303 TYR A CD2    1 
ATOM   2256 C CE1    . TYR A 1 312 ? 28.436 39.209 16.817 1.00 12.53 ? 303 TYR A CE1    1 
ATOM   2257 C CE2    . TYR A 1 312 ? 26.651 38.474 15.391 1.00 10.30 ? 303 TYR A CE2    1 
ATOM   2258 C CZ     . TYR A 1 312 ? 27.970 38.458 15.747 1.00 11.03 ? 303 TYR A CZ     1 
ATOM   2259 O OH     . TYR A 1 312 ? 28.834 37.740 14.961 1.00 13.68 ? 303 TYR A OH     1 
ATOM   2260 N N      . GLN A 1 313 ? 27.412 42.959 16.165 1.00 11.55 ? 304 GLN A N      1 
ATOM   2261 C CA     . GLN A 1 313 ? 27.907 43.308 14.819 1.00 13.11 ? 304 GLN A CA     1 
ATOM   2262 C C      . GLN A 1 313 ? 28.003 42.051 13.968 1.00 14.28 ? 304 GLN A C      1 
ATOM   2263 O O      . GLN A 1 313 ? 29.097 41.536 13.721 1.00 16.09 ? 304 GLN A O      1 
ATOM   2264 C CB     . GLN A 1 313 ? 29.278 43.963 14.895 1.00 14.17 ? 304 GLN A CB     1 
ATOM   2265 C CG     . GLN A 1 313 ? 29.230 45.241 15.717 1.00 16.28 ? 304 GLN A CG     1 
ATOM   2266 C CD     . GLN A 1 313 ? 30.584 45.919 15.817 1.00 20.80 ? 304 GLN A CD     1 
ATOM   2267 O OE1    . GLN A 1 313 ? 31.459 45.668 14.998 1.00 21.65 ? 304 GLN A OE1    1 
ATOM   2268 N NE2    . GLN A 1 313 ? 30.746 46.767 16.799 1.00 21.76 ? 304 GLN A NE2    1 
ATOM   2269 N N      . GLY A 1 314 ? 26.866 41.571 13.479 1.00 12.98 ? 305 GLY A N      1 
ATOM   2270 C CA     . GLY A 1 314 ? 26.923 40.444 12.580 1.00 13.24 ? 305 GLY A CA     1 
ATOM   2271 C C      . GLY A 1 314 ? 25.578 39.749 12.443 1.00 12.01 ? 305 GLY A C      1 
ATOM   2272 O O      . GLY A 1 314 ? 24.536 40.328 12.723 1.00 13.30 ? 305 GLY A O      1 
ATOM   2273 N N      . THR A 1 315 ? 25.650 38.539 11.915 1.00 11.31 ? 306 THR A N      1 
ATOM   2274 C CA     . THR A 1 315 ? 24.475 37.744 11.580 1.00 11.71 ? 306 THR A CA     1 
ATOM   2275 C C      . THR A 1 315 ? 23.844 37.167 12.826 1.00 12.22 ? 306 THR A C      1 
ATOM   2276 O O      . THR A 1 315 ? 24.547 36.731 13.729 1.00 12.01 ? 306 THR A O      1 
ATOM   2277 C CB     . THR A 1 315 ? 24.913 36.576 10.715 1.00 11.83 ? 306 THR A CB     1 
ATOM   2278 O OG1    . THR A 1 315 ? 25.444 37.107 9.478  1.00 13.91 ? 306 THR A OG1    1 
ATOM   2279 C CG2    . THR A 1 315 ? 23.759 35.554 10.428 1.00 12.10 ? 306 THR A CG2    1 
ATOM   2280 N N      . PHE A 1 316 ? 22.507 37.209 12.877 1.00 11.40 ? 307 PHE A N      1 
ATOM   2281 C CA     . PHE A 1 316 ? 21.772 36.857 14.101 1.00 10.46 ? 307 PHE A CA     1 
ATOM   2282 C C      . PHE A 1 316 ? 20.722 35.799 13.786 1.00 10.45 ? 307 PHE A C      1 
ATOM   2283 O O      . PHE A 1 316 ? 19.898 35.977 12.856 1.00 11.09 ? 307 PHE A O      1 
ATOM   2284 C CB     . PHE A 1 316 ? 21.088 38.086 14.679 1.00 10.90 ? 307 PHE A CB     1 
ATOM   2285 C CG     . PHE A 1 316 ? 20.487 37.875 16.069 1.00 10.47 ? 307 PHE A CG     1 
ATOM   2286 C CD1    . PHE A 1 316 ? 21.286 38.080 17.204 1.00 12.40 ? 307 PHE A CD1    1 
ATOM   2287 C CD2    . PHE A 1 316 ? 19.151 37.529 16.238 1.00 12.26 ? 307 PHE A CD2    1 
ATOM   2288 C CE1    . PHE A 1 316 ? 20.750 37.933 18.500 1.00 12.04 ? 307 PHE A CE1    1 
ATOM   2289 C CE2    . PHE A 1 316 ? 18.624 37.353 17.531 1.00 12.25 ? 307 PHE A CE2    1 
ATOM   2290 C CZ     . PHE A 1 316 ? 19.431 37.555 18.670 1.00 12.38 ? 307 PHE A CZ     1 
ATOM   2291 N N      . ILE A 1 317 ? 20.780 34.666 14.511 1.00 10.72 ? 308 ILE A N      1 
ATOM   2292 C CA     . ILE A 1 317 ? 19.778 33.594 14.412 1.00 10.53 ? 308 ILE A CA     1 
ATOM   2293 C C      . ILE A 1 317 ? 18.921 33.631 15.671 1.00 11.02 ? 308 ILE A C      1 
ATOM   2294 O O      . ILE A 1 317 ? 19.453 33.573 16.794 1.00 11.69 ? 308 ILE A O      1 
ATOM   2295 C CB     . ILE A 1 317 ? 20.438 32.208 14.300 1.00 10.53 ? 308 ILE A CB     1 
ATOM   2296 C CG1    . ILE A 1 317 ? 21.583 32.225 13.293 1.00 10.86 ? 308 ILE A CG1    1 
ATOM   2297 C CG2    . ILE A 1 317 ? 19.348 31.119 13.988 1.00 12.70 ? 308 ILE A CG2    1 
ATOM   2298 C CD1    . ILE A 1 317 ? 22.116 30.810 12.939 1.00 13.28 ? 308 ILE A CD1    1 
ATOM   2299 N N      . CYS A 1 318 ? 17.605 33.796 15.498 1.00 11.65 ? 309 CYS A N      1 
ATOM   2300 C CA     . CYS A 1 318 ? 16.680 33.723 16.622 1.00 12.09 ? 309 CYS A CA     1 
ATOM   2301 C C      . CYS A 1 318 ? 16.078 32.326 16.727 1.00 11.24 ? 309 CYS A C      1 
ATOM   2302 O O      . CYS A 1 318 ? 15.931 31.630 15.725 1.00 13.17 ? 309 CYS A O      1 
ATOM   2303 C CB     . CYS A 1 318 ? 15.589 34.778 16.506 1.00 11.99 ? 309 CYS A CB     1 
ATOM   2304 S SG     . CYS A 1 318 ? 14.556 34.669 15.077 1.00 15.09 ? 309 CYS A SG     1 
ATOM   2305 N N      . SER A 1 319 ? 15.692 31.943 17.934 1.00 11.62 ? 310 SER A N      1 
ATOM   2306 C CA     . SER A 1 319 ? 15.267 30.570 18.191 1.00 11.19 ? 310 SER A CA     1 
ATOM   2307 C C      . SER A 1 319 ? 14.381 30.491 19.421 1.00 11.58 ? 310 SER A C      1 
ATOM   2308 O O      . SER A 1 319 ? 14.631 31.203 20.415 1.00 11.77 ? 310 SER A O      1 
ATOM   2309 C CB     . SER A 1 319 ? 16.542 29.804 18.510 1.00 12.63 ? 310 SER A CB     1 
ATOM   2310 O OG     . SER A 1 319 ? 16.277 28.604 19.174 1.00 14.07 ? 310 SER A OG     1 
ATOM   2311 N N      . GLY A 1 320 ? 13.374 29.607 19.364 1.00 11.82 ? 311 GLY A N      1 
ATOM   2312 C CA     . GLY A 1 320 ? 12.573 29.226 20.535 1.00 11.98 ? 311 GLY A CA     1 
ATOM   2313 C C      . GLY A 1 320 ? 11.119 29.608 20.295 1.00 13.10 ? 311 GLY A C      1 
ATOM   2314 O O      . GLY A 1 320 ? 10.748 30.766 20.451 1.00 15.40 ? 311 GLY A O      1 
ATOM   2315 N N      . GLY A 1 321 ? 10.262 28.630 20.017 1.00 11.29 ? 312 GLY A N      1 
ATOM   2316 C CA     . GLY A 1 321 ? 8.848  28.894 19.848 1.00 13.52 ? 312 GLY A CA     1 
ATOM   2317 C C      . GLY A 1 321 ? 8.471  29.623 18.581 1.00 15.13 ? 312 GLY A C      1 
ATOM   2318 O O      . GLY A 1 321 ? 7.335  30.077 18.481 1.00 18.15 ? 312 GLY A O      1 
ATOM   2319 N N      . TYR A 1 322 ? 9.365  29.790 17.609 1.00 12.88 ? 313 TYR A N      1 
ATOM   2320 C CA     . TYR A 1 322 ? 8.960  30.492 16.401 1.00 13.29 ? 313 TYR A CA     1 
ATOM   2321 C C      . TYR A 1 322 ? 8.003  29.655 15.579 1.00 17.90 ? 313 TYR A C      1 
ATOM   2322 O O      . TYR A 1 322 ? 8.135  28.441 15.488 1.00 17.62 ? 313 TYR A O      1 
ATOM   2323 C CB     . TYR A 1 322 ? 10.183 30.924 15.552 1.00 15.02 ? 313 TYR A CB     1 
ATOM   2324 C CG     . TYR A 1 322 ? 10.856 32.129 16.168 1.00 13.37 ? 313 TYR A CG     1 
ATOM   2325 C CD1    . TYR A 1 322 ? 11.770 31.971 17.209 1.00 13.70 ? 313 TYR A CD1    1 
ATOM   2326 C CD2    . TYR A 1 322 ? 10.530 33.446 15.768 1.00 15.17 ? 313 TYR A CD2    1 
ATOM   2327 C CE1    . TYR A 1 322 ? 12.316 33.033 17.863 1.00 16.79 ? 313 TYR A CE1    1 
ATOM   2328 C CE2    . TYR A 1 322 ? 11.103 34.562 16.428 1.00 18.11 ? 313 TYR A CE2    1 
ATOM   2329 C CZ     . TYR A 1 322 ? 12.002 34.329 17.456 1.00 16.31 ? 313 TYR A CZ     1 
ATOM   2330 O OH     . TYR A 1 322 ? 12.581 35.382 18.122 1.00 18.12 ? 313 TYR A OH     1 
ATOM   2331 N N      . THR A 1 323 ? 7.010  30.326 15.016 1.00 21.75 ? 314 THR A N      1 
ATOM   2332 C CA     . THR A 1 323 ? 6.090  29.733 14.057 1.00 18.58 ? 314 THR A CA     1 
ATOM   2333 C C      . THR A 1 323 ? 6.510  30.159 12.648 1.00 18.02 ? 314 THR A C      1 
ATOM   2334 O O      . THR A 1 323 ? 7.439  30.972 12.456 1.00 18.64 ? 314 THR A O      1 
ATOM   2335 C CB     . THR A 1 323 ? 4.683  30.261 14.359 1.00 17.67 ? 314 THR A CB     1 
ATOM   2336 O OG1    . THR A 1 323 ? 4.733  31.686 14.218 1.00 18.66 ? 314 THR A OG1    1 
ATOM   2337 C CG2    . THR A 1 323 ? 4.322  29.908 15.779 1.00 21.18 ? 314 THR A CG2    1 
ATOM   2338 N N      . ARG A 1 324 ? 5.785  29.682 11.624 1.00 16.80 ? 315 ARG A N      1 
ATOM   2339 C CA     . ARG A 1 324 ? 5.967  30.237 10.291 1.00 16.76 ? 315 ARG A CA     1 
ATOM   2340 C C      . ARG A 1 324 ? 5.735  31.747 10.276 1.00 17.47 ? 315 ARG A C      1 
ATOM   2341 O O      . ARG A 1 324 ? 6.568  32.515 9.775  1.00 18.70 ? 315 ARG A O      1 
ATOM   2342 C CB     . ARG A 1 324 ? 5.001  29.538 9.336  1.00 17.90 ? 315 ARG A CB     1 
ATOM   2343 C CG     . ARG A 1 324 ? 5.059  30.069 7.975  1.00 18.24 ? 315 ARG A CG     1 
ATOM   2344 C CD     . ARG A 1 324 ? 4.120  29.307 7.034  1.00 19.51 ? 315 ARG A CD     1 
ATOM   2345 N NE     . ARG A 1 324 ? 4.184  29.774 5.651  1.00 19.43 ? 315 ARG A NE     1 
ATOM   2346 C CZ     . ARG A 1 324 ? 3.570  30.870 5.221  1.00 21.07 ? 315 ARG A CZ     1 
ATOM   2347 N NH1    . ARG A 1 324 ? 2.779  31.565 6.024  1.00 23.05 ? 315 ARG A NH1    1 
ATOM   2348 N NH2    . ARG A 1 324 ? 3.748  31.262 3.965  1.00 28.57 ? 315 ARG A NH2    1 
ATOM   2349 N N      . GLU A 1 325 ? 4.630  32.205 10.880 1.00 18.36 ? 316 GLU A N      1 
ATOM   2350 C CA     . GLU A 1 325 ? 4.310  33.631 10.817 1.00 19.61 ? 316 GLU A CA     1 
ATOM   2351 C C      . GLU A 1 325 ? 5.304  34.481 11.597 1.00 15.26 ? 316 GLU A C      1 
ATOM   2352 O O      . GLU A 1 325 ? 5.691  35.560 11.124 1.00 18.57 ? 316 GLU A O      1 
ATOM   2353 C CB     . GLU A 1 325 ? 2.890  33.893 11.320 1.00 22.09 ? 316 GLU A CB     1 
ATOM   2354 N N      . LEU A 1 326 ? 5.730  34.011 12.777 1.00 17.70 ? 317 LEU A N      1 
ATOM   2355 C CA     . LEU A 1 326 ? 6.688  34.778 13.575 1.00 17.95 ? 317 LEU A CA     1 
ATOM   2356 C C      . LEU A 1 326 ? 8.059  34.795 12.927 1.00 17.14 ? 317 LEU A C      1 
ATOM   2357 O O      . LEU A 1 326 ? 8.780  35.796 13.044 1.00 17.65 ? 317 LEU A O      1 
ATOM   2358 C CB     . LEU A 1 326 ? 6.761  34.248 15.000 1.00 20.56 ? 317 LEU A CB     1 
ATOM   2359 C CG     . LEU A 1 326 ? 5.531  34.484 15.888 1.00 24.53 ? 317 LEU A CG     1 
ATOM   2360 C CD1    . LEU A 1 326 ? 5.658  33.653 17.142 1.00 26.77 ? 317 LEU A CD1    1 
ATOM   2361 C CD2    . LEU A 1 326 ? 5.414  35.968 16.223 1.00 22.06 ? 317 LEU A CD2    1 
ATOM   2362 N N      . GLY A 1 327 ? 8.433  33.713 12.231 1.00 16.92 ? 318 GLY A N      1 
ATOM   2363 C CA     . GLY A 1 327 ? 9.683  33.718 11.499 1.00 16.98 ? 318 GLY A CA     1 
ATOM   2364 C C      . GLY A 1 327 ? 9.675  34.717 10.364 1.00 14.92 ? 318 GLY A C      1 
ATOM   2365 O O      . GLY A 1 327 ? 10.649 35.452 10.157 1.00 16.80 ? 318 GLY A O      1 
ATOM   2366 N N      . ILE A 1 328 ? 8.590  34.716 9.563  1.00 16.89 ? 319 ILE A N      1 
ATOM   2367 C CA     . ILE A 1 328 ? 8.465  35.687 8.470  1.00 14.39 ? 319 ILE A CA     1 
ATOM   2368 C C      . ILE A 1 328 ? 8.584  37.103 9.007  1.00 15.47 ? 319 ILE A C      1 
ATOM   2369 O O      . ILE A 1 328 ? 9.328  37.935 8.453  1.00 17.97 ? 319 ILE A O      1 
ATOM   2370 C CB     . ILE A 1 328 ? 7.111  35.488 7.753  1.00 17.85 ? 319 ILE A CB     1 
ATOM   2371 C CG1    . ILE A 1 328 ? 7.142  34.181 6.964  1.00 18.40 ? 319 ILE A CG1    1 
ATOM   2372 C CG2    . ILE A 1 328 ? 6.735  36.702 6.897  1.00 22.94 ? 319 ILE A CG2    1 
ATOM   2373 C CD1    . ILE A 1 328 ? 5.766  33.700 6.452  1.00 20.83 ? 319 ILE A CD1    1 
ATOM   2374 N N      . GLU A 1 329 ? 7.868  37.375 10.118 1.00 17.06 ? 320 GLU A N      1 
ATOM   2375 C CA     . GLU A 1 329 ? 7.848  38.703 10.714 1.00 19.08 ? 320 GLU A CA     1 
ATOM   2376 C C      . GLU A 1 329 ? 9.236  39.091 11.208 1.00 20.36 ? 320 GLU A C      1 
ATOM   2377 O O      . GLU A 1 329 ? 9.685  40.244 11.007 1.00 21.72 ? 320 GLU A O      1 
ATOM   2378 C CB     . GLU A 1 329 ? 6.841  38.739 11.859 1.00 22.00 ? 320 GLU A CB     1 
ATOM   2379 N N      . ALA A 1 330 ? 9.956  38.130 11.805 1.00 17.67 ? 321 ALA A N      1 
ATOM   2380 C CA     . ALA A 1 330 ? 11.280 38.451 12.337 1.00 17.39 ? 321 ALA A CA     1 
ATOM   2381 C C      . ALA A 1 330 ? 12.210 38.922 11.234 1.00 17.87 ? 321 ALA A C      1 
ATOM   2382 O O      . ALA A 1 330 ? 12.956 39.900 11.408 1.00 18.12 ? 321 ALA A O      1 
ATOM   2383 C CB     . ALA A 1 330 ? 11.878 37.211 13.023 1.00 19.60 ? 321 ALA A CB     1 
ATOM   2384 N N      . VAL A 1 331 ? 12.219 38.206 10.112 1.00 15.15 ? 322 VAL A N      1 
ATOM   2385 C CA     . VAL A 1 331 ? 13.070 38.576 8.993  1.00 16.63 ? 322 VAL A CA     1 
ATOM   2386 C C      . VAL A 1 331 ? 12.570 39.862 8.341  1.00 16.92 ? 322 VAL A C      1 
ATOM   2387 O O      . VAL A 1 331 ? 13.351 40.787 8.104  1.00 18.86 ? 322 VAL A O      1 
ATOM   2388 C CB     . VAL A 1 331 ? 13.214 37.416 7.988  1.00 15.19 ? 322 VAL A CB     1 
ATOM   2389 C CG1    . VAL A 1 331 ? 14.036 37.888 6.780  1.00 18.36 ? 322 VAL A CG1    1 
ATOM   2390 C CG2    . VAL A 1 331 ? 13.923 36.250 8.673  1.00 16.41 ? 322 VAL A CG2    1 
ATOM   2391 N N      . ALA A 1 332 ? 11.267 39.955 8.082  1.00 17.35 ? 323 ALA A N      1 
ATOM   2392 C CA     . ALA A 1 332 ? 10.730 41.138 7.401  1.00 17.77 ? 323 ALA A CA     1 
ATOM   2393 C C      . ALA A 1 332 ? 11.006 42.419 8.173  1.00 20.36 ? 323 ALA A C      1 
ATOM   2394 O O      . ALA A 1 332 ? 11.275 43.475 7.563  1.00 23.08 ? 323 ALA A O      1 
ATOM   2395 C CB     . ALA A 1 332 ? 9.224  40.985 7.225  1.00 19.83 ? 323 ALA A CB     1 
ATOM   2396 N N      . GLN A 1 333 ? 10.942 42.345 9.504  1.00 17.33 ? 324 GLN A N      1 
ATOM   2397 C CA     . GLN A 1 333 ? 11.157 43.523 10.346 1.00 19.91 ? 324 GLN A CA     1 
ATOM   2398 C C      . GLN A 1 333 ? 12.597 43.795 10.670 1.00 19.10 ? 324 GLN A C      1 
ATOM   2399 O O      . GLN A 1 333 ? 12.863 44.771 11.387 1.00 20.42 ? 324 GLN A O      1 
ATOM   2400 C CB     . GLN A 1 333 ? 10.379 43.432 11.664 1.00 23.17 ? 324 GLN A CB     1 
ATOM   2401 C CG     . GLN A 1 333 ? 8.864  43.392 11.471 1.00 25.64 ? 324 GLN A CG     1 
ATOM   2402 C CD     . GLN A 1 333 ? 8.116  42.749 12.601 1.00 44.98 ? 324 GLN A CD     1 
ATOM   2403 O OE1    . GLN A 1 333 ? 8.597  42.696 13.737 1.00 44.84 ? 324 GLN A OE1    1 
ATOM   2404 N NE2    . GLN A 1 333 ? 6.892  42.307 12.317 1.00 58.05 ? 324 GLN A NE2    1 
ATOM   2405 N N      . GLY A 1 334 ? 13.536 42.964 10.206 1.00 18.05 ? 325 GLY A N      1 
ATOM   2406 C CA     . GLY A 1 334 ? 14.932 43.178 10.487 1.00 17.79 ? 325 GLY A CA     1 
ATOM   2407 C C      . GLY A 1 334 ? 15.347 42.709 11.863 1.00 17.09 ? 325 GLY A C      1 
ATOM   2408 O O      . GLY A 1 334 ? 16.456 43.036 12.284 1.00 18.14 ? 325 GLY A O      1 
ATOM   2409 N N      . ASP A 1 335 ? 14.491 41.968 12.580 1.00 16.27 ? 326 ASP A N      1 
ATOM   2410 C CA     . ASP A 1 335 ? 14.801 41.537 13.941 1.00 16.28 ? 326 ASP A CA     1 
ATOM   2411 C C      . ASP A 1 335 ? 15.768 40.359 13.993 1.00 15.45 ? 326 ASP A C      1 
ATOM   2412 O O      . ASP A 1 335 ? 16.359 40.105 15.050 1.00 17.07 ? 326 ASP A O      1 
ATOM   2413 C CB     . ASP A 1 335 ? 13.541 41.029 14.642 1.00 18.91 ? 326 ASP A CB     1 
ATOM   2414 C CG     . ASP A 1 335 ? 12.406 42.082 14.767 1.00 35.79 ? 326 ASP A CG     1 
ATOM   2415 O OD1    . ASP A 1 335 ? 12.658 43.310 14.748 1.00 29.70 ? 326 ASP A OD1    1 
ATOM   2416 O OD2    . ASP A 1 335 ? 11.238 41.633 14.973 1.00 30.71 ? 326 ASP A OD2    1 
ATOM   2417 N N      . ALA A 1 336 ? 15.878 39.586 12.913 1.00 14.12 ? 327 ALA A N      1 
ATOM   2418 C CA     . ALA A 1 336 ? 16.844 38.501 12.856 1.00 13.81 ? 327 ALA A CA     1 
ATOM   2419 C C      . ALA A 1 336 ? 17.156 38.255 11.407 1.00 13.74 ? 327 ALA A C      1 
ATOM   2420 O O      . ALA A 1 336 ? 16.380 38.655 10.516 1.00 14.93 ? 327 ALA A O      1 
ATOM   2421 C CB     . ALA A 1 336 ? 16.267 37.229 13.449 1.00 14.58 ? 327 ALA A CB     1 
ATOM   2422 N N      . ASP A 1 337 ? 18.311 37.640 11.161 1.00 11.11 ? 328 ASP A N      1 
ATOM   2423 C CA     . ASP A 1 337 ? 18.647 37.264 9.780  1.00 10.97 ? 328 ASP A CA     1 
ATOM   2424 C C      . ASP A 1 337 ? 18.220 35.864 9.434  1.00 12.56 ? 328 ASP A C      1 
ATOM   2425 O O      . ASP A 1 337 ? 17.825 35.598 8.288  1.00 12.86 ? 328 ASP A O      1 
ATOM   2426 C CB     . ASP A 1 337 ? 20.148 37.449 9.507  1.00 14.06 ? 328 ASP A CB     1 
ATOM   2427 C CG     . ASP A 1 337 ? 20.616 38.807 9.932  1.00 14.11 ? 328 ASP A CG     1 
ATOM   2428 O OD1    . ASP A 1 337 ? 20.202 39.796 9.258  1.00 14.42 ? 328 ASP A OD1    1 
ATOM   2429 O OD2    . ASP A 1 337 ? 21.355 38.952 10.934 1.00 13.36 ? 328 ASP A OD2    1 
ATOM   2430 N N      . LEU A 1 338 ? 18.277 34.956 10.388 1.00 11.77 ? 329 LEU A N      1 
ATOM   2431 C CA     . LEU A 1 338 ? 17.925 33.566 10.192 1.00 11.10 ? 329 LEU A CA     1 
ATOM   2432 C C      . LEU A 1 338 ? 17.073 33.146 11.382 1.00 9.56  ? 329 LEU A C      1 
ATOM   2433 O O      . LEU A 1 338 ? 17.188 33.744 12.482 1.00 11.24 ? 329 LEU A O      1 
ATOM   2434 C CB     . LEU A 1 338 ? 19.197 32.661 10.198 1.00 12.12 ? 329 LEU A CB     1 
ATOM   2435 C CG     . LEU A 1 338 ? 20.229 33.058 9.112  1.00 13.34 ? 329 LEU A CG     1 
ATOM   2436 C CD1    . LEU A 1 338 ? 21.539 32.354 9.347  1.00 13.69 ? 329 LEU A CD1    1 
ATOM   2437 C CD2    . LEU A 1 338 ? 19.691 32.634 7.748  1.00 14.53 ? 329 LEU A CD2    1 
ATOM   2438 N N      . VAL A 1 339 ? 16.245 32.102 11.171 1.00 10.51 ? 330 VAL A N      1 
ATOM   2439 C CA     . VAL A 1 339 ? 15.284 31.619 12.174 1.00 11.28 ? 330 VAL A CA     1 
ATOM   2440 C C      . VAL A 1 339 ? 15.488 30.123 12.314 1.00 10.82 ? 330 VAL A C      1 
ATOM   2441 O O      . VAL A 1 339 ? 15.355 29.396 11.322 1.00 11.71 ? 330 VAL A O      1 
ATOM   2442 C CB     . VAL A 1 339 ? 13.828 31.909 11.776 1.00 12.92 ? 330 VAL A CB     1 
ATOM   2443 C CG1    . VAL A 1 339 ? 12.888 31.449 12.903 1.00 13.09 ? 330 VAL A CG1    1 
ATOM   2444 C CG2    . VAL A 1 339 ? 13.649 33.425 11.537 1.00 13.77 ? 330 VAL A CG2    1 
ATOM   2445 N N      . SER A 1 340 ? 15.840 29.652 13.509 1.00 10.77 ? 331 SER A N      1 
ATOM   2446 C CA     . SER A 1 340 ? 16.026 28.211 13.686 1.00 10.19 ? 331 SER A CA     1 
ATOM   2447 C C      . SER A 1 340 ? 14.782 27.584 14.298 1.00 10.80 ? 331 SER A C      1 
ATOM   2448 O O      . SER A 1 340 ? 14.129 28.185 15.171 1.00 12.49 ? 331 SER A O      1 
ATOM   2449 C CB     . SER A 1 340 ? 17.296 27.854 14.463 1.00 12.01 ? 331 SER A CB     1 
ATOM   2450 O OG     . SER A 1 340 ? 17.160 28.280 15.823 1.00 13.64 ? 331 SER A OG     1 
ATOM   2451 N N      . TYR A 1 341 ? 14.447 26.381 13.844 1.00 11.29 ? 332 TYR A N      1 
ATOM   2452 C CA     . TYR A 1 341 ? 13.320 25.607 14.337 1.00 10.75 ? 332 TYR A CA     1 
ATOM   2453 C C      . TYR A 1 341 ? 13.858 24.281 14.824 1.00 10.66 ? 332 TYR A C      1 
ATOM   2454 O O      . TYR A 1 341 ? 14.679 23.644 14.131 1.00 11.66 ? 332 TYR A O      1 
ATOM   2455 C CB     . TYR A 1 341 ? 12.317 25.346 13.187 1.00 11.72 ? 332 TYR A CB     1 
ATOM   2456 C CG     . TYR A 1 341 ? 11.679 26.620 12.686 1.00 11.45 ? 332 TYR A CG     1 
ATOM   2457 C CD1    . TYR A 1 341 ? 12.276 27.405 11.695 1.00 12.77 ? 332 TYR A CD1    1 
ATOM   2458 C CD2    . TYR A 1 341 ? 10.449 27.017 13.163 1.00 12.99 ? 332 TYR A CD2    1 
ATOM   2459 C CE1    . TYR A 1 341 ? 11.688 28.588 11.237 1.00 12.08 ? 332 TYR A CE1    1 
ATOM   2460 C CE2    . TYR A 1 341 ? 9.843  28.210 12.702 1.00 13.07 ? 332 TYR A CE2    1 
ATOM   2461 C CZ     . TYR A 1 341 ? 10.452 28.959 11.736 1.00 12.61 ? 332 TYR A CZ     1 
ATOM   2462 O OH     . TYR A 1 341 ? 9.916  30.141 11.250 1.00 16.19 ? 332 TYR A OH     1 
ATOM   2463 N N      . GLY A 1 342 ? 13.407 23.878 16.007 1.00 10.22 ? 333 GLY A N      1 
ATOM   2464 C CA     . GLY A 1 342 ? 13.826 22.601 16.589 1.00 11.96 ? 333 GLY A CA     1 
ATOM   2465 C C      . GLY A 1 342 ? 12.731 21.571 16.470 1.00 12.15 ? 333 GLY A C      1 
ATOM   2466 O O      . GLY A 1 342 ? 12.723 20.745 15.568 1.00 13.35 ? 333 GLY A O      1 
ATOM   2467 N N      . ARG A 1 343 ? 11.756 21.623 17.381 1.00 11.53 ? 334 ARG A N      1 
ATOM   2468 C CA     . ARG A 1 343 ? 10.800 20.523 17.471 1.00 11.91 ? 334 ARG A CA     1 
ATOM   2469 C C      . ARG A 1 343 ? 10.025 20.280 16.164 1.00 11.39 ? 334 ARG A C      1 
ATOM   2470 O O      . ARG A 1 343 ? 9.766  19.121 15.817 1.00 11.62 ? 334 ARG A O      1 
ATOM   2471 C CB     . ARG A 1 343 ? 9.856  20.747 18.650 1.00 10.87 ? 334 ARG A CB     1 
ATOM   2472 C CG     . ARG A 1 343 ? 10.606 20.528 19.969 1.00 12.93 ? 334 ARG A CG     1 
ATOM   2473 C CD     . ARG A 1 343 ? 9.807  21.073 21.166 1.00 13.77 ? 334 ARG A CD     1 
ATOM   2474 N NE     . ARG A 1 343 ? 9.793  22.531 21.149 1.00 11.52 ? 334 ARG A NE     1 
ATOM   2475 C CZ     . ARG A 1 343 ? 9.261  23.277 22.106 1.00 13.44 ? 334 ARG A CZ     1 
ATOM   2476 N NH1    . ARG A 1 343 ? 8.587  22.723 23.116 1.00 17.42 ? 334 ARG A NH1    1 
ATOM   2477 N NH2    . ARG A 1 343 ? 9.420  24.612 22.077 1.00 14.97 ? 334 ARG A NH2    1 
ATOM   2478 N N      . LEU A 1 344 ? 9.624  21.345 15.428 1.00 11.20 ? 335 LEU A N      1 
ATOM   2479 C CA     . LEU A 1 344 ? 8.912  21.082 14.195 1.00 11.45 ? 335 LEU A CA     1 
ATOM   2480 C C      . LEU A 1 344 ? 9.762  20.352 13.188 1.00 12.35 ? 335 LEU A C      1 
ATOM   2481 O O      . LEU A 1 344 ? 9.222  19.612 12.372 1.00 12.85 ? 335 LEU A O      1 
ATOM   2482 C CB     . LEU A 1 344 ? 8.414  22.377 13.569 1.00 11.75 ? 335 LEU A CB     1 
ATOM   2483 C CG     . LEU A 1 344 ? 7.221  23.027 14.296 1.00 14.40 ? 335 LEU A CG     1 
ATOM   2484 C CD1    . LEU A 1 344 ? 6.927  24.405 13.681 1.00 17.54 ? 335 LEU A CD1    1 
ATOM   2485 C CD2    . LEU A 1 344 ? 5.963  22.093 14.249 1.00 14.65 ? 335 LEU A CD2    1 
ATOM   2486 N N      . PHE A 1 345 ? 11.093 20.488 13.262 1.00 11.34 ? 336 PHE A N      1 
ATOM   2487 C CA     . PHE A 1 345 ? 11.925 19.731 12.338 1.00 13.10 ? 336 PHE A CA     1 
ATOM   2488 C C      . PHE A 1 345 ? 12.048 18.276 12.746 1.00 13.83 ? 336 PHE A C      1 
ATOM   2489 O O      . PHE A 1 345 ? 12.381 17.444 11.891 1.00 14.01 ? 336 PHE A O      1 
ATOM   2490 C CB     . PHE A 1 345 ? 13.351 20.316 12.286 1.00 13.32 ? 336 PHE A CB     1 
ATOM   2491 C CG     . PHE A 1 345 ? 13.683 21.040 11.007 1.00 11.75 ? 336 PHE A CG     1 
ATOM   2492 C CD1    . PHE A 1 345 ? 13.745 20.321 9.831  1.00 11.52 ? 336 PHE A CD1    1 
ATOM   2493 C CD2    . PHE A 1 345 ? 14.126 22.353 10.989 1.00 12.96 ? 336 PHE A CD2    1 
ATOM   2494 C CE1    . PHE A 1 345 ? 14.131 20.854 8.661  1.00 15.10 ? 336 PHE A CE1    1 
ATOM   2495 C CE2    . PHE A 1 345 ? 14.544 22.936 9.771  1.00 15.24 ? 336 PHE A CE2    1 
ATOM   2496 C CZ     . PHE A 1 345 ? 14.527 22.159 8.603  1.00 15.01 ? 336 PHE A CZ     1 
ATOM   2497 N N      . ILE A 1 346 ? 11.736 17.912 13.993 1.00 12.03 ? 337 ILE A N      1 
ATOM   2498 C CA     . ILE A 1 346 ? 11.726 16.501 14.372 1.00 12.78 ? 337 ILE A CA     1 
ATOM   2499 C C      . ILE A 1 346 ? 10.707 15.742 13.536 1.00 10.59 ? 337 ILE A C      1 
ATOM   2500 O O      . ILE A 1 346 ? 11.002 14.695 12.950 1.00 11.60 ? 337 ILE A O      1 
ATOM   2501 C CB     . ILE A 1 346 ? 11.418 16.343 15.882 1.00 11.66 ? 337 ILE A CB     1 
ATOM   2502 C CG1    . ILE A 1 346 ? 12.611 16.885 16.640 1.00 12.32 ? 337 ILE A CG1    1 
ATOM   2503 C CG2    . ILE A 1 346 ? 11.117 14.864 16.226 1.00 13.25 ? 337 ILE A CG2    1 
ATOM   2504 C CD1    . ILE A 1 346 ? 12.388 16.838 18.160 1.00 15.58 ? 337 ILE A CD1    1 
ATOM   2505 N N      . SER A 1 347 ? 9.499  16.282 13.447 1.00 11.93 ? 338 SER A N      1 
ATOM   2506 C CA     . SER A 1 347 ? 8.410  15.561 12.829 1.00 13.15 ? 338 SER A CA     1 
ATOM   2507 C C      . SER A 1 347 ? 8.070  16.039 11.433 1.00 12.55 ? 338 SER A C      1 
ATOM   2508 O O      . SER A 1 347 ? 7.164  15.471 10.811 1.00 14.40 ? 338 SER A O      1 
ATOM   2509 C CB     . SER A 1 347 ? 7.170  15.706 13.718 1.00 13.64 ? 338 SER A CB     1 
ATOM   2510 O OG     . SER A 1 347 ? 6.891  17.073 14.007 1.00 14.41 ? 338 SER A OG     1 
ATOM   2511 N N      . ASN A 1 348 ? 8.761  17.057 10.909 1.00 11.37 ? 339 ASN A N      1 
ATOM   2512 C CA     . ASN A 1 348 ? 8.511  17.533 9.547  1.00 12.96 ? 339 ASN A CA     1 
ATOM   2513 C C      . ASN A 1 348 ? 9.855  17.565 8.862  1.00 12.57 ? 339 ASN A C      1 
ATOM   2514 O O      . ASN A 1 348 ? 10.524 18.600 8.870  1.00 12.76 ? 339 ASN A O      1 
ATOM   2515 C CB     . ASN A 1 348 ? 7.871  18.911 9.551  1.00 13.48 ? 339 ASN A CB     1 
ATOM   2516 C CG     . ASN A 1 348 ? 6.521  18.883 10.220 1.00 12.23 ? 339 ASN A CG     1 
ATOM   2517 O OD1    . ASN A 1 348 ? 5.542  18.559 9.561  1.00 13.62 ? 339 ASN A OD1    1 
ATOM   2518 N ND2    . ASN A 1 348 ? 6.474  19.145 11.524 1.00 12.29 ? 339 ASN A ND2    1 
ATOM   2519 N N      . PRO A 1 349 ? 10.286 16.451 8.261  1.00 12.27 ? 340 PRO A N      1 
ATOM   2520 C CA     . PRO A 1 349 ? 11.635 16.475 7.649  1.00 12.53 ? 340 PRO A CA     1 
ATOM   2521 C C      . PRO A 1 349 ? 11.714 17.506 6.552  1.00 12.69 ? 340 PRO A C      1 
ATOM   2522 O O      . PRO A 1 349 ? 12.768 18.144 6.410  1.00 14.07 ? 340 PRO A O      1 
ATOM   2523 C CB     . PRO A 1 349 ? 11.790 15.044 7.092  1.00 14.88 ? 340 PRO A CB     1 
ATOM   2524 C CG     . PRO A 1 349 ? 10.356 14.516 6.955  1.00 14.26 ? 340 PRO A CG     1 
ATOM   2525 C CD     . PRO A 1 349 ? 9.602  15.152 8.104  1.00 13.66 ? 340 PRO A CD     1 
ATOM   2526 N N      . ASP A 1 350 ? 10.626 17.704 5.812  1.00 13.88 ? 341 ASP A N      1 
ATOM   2527 C CA     . ASP A 1 350 ? 10.517 18.747 4.803  1.00 11.92 ? 341 ASP A CA     1 
ATOM   2528 C C      . ASP A 1 350 ? 9.935  20.030 5.375  1.00 12.06 ? 341 ASP A C      1 
ATOM   2529 O O      . ASP A 1 350 ? 9.125  20.708 4.738  1.00 14.53 ? 341 ASP A O      1 
ATOM   2530 C CB     . ASP A 1 350 ? 9.705  18.223 3.608  1.00 13.77 ? 341 ASP A CB     1 
ATOM   2531 C CG     . ASP A 1 350 ? 8.381  17.588 4.004  1.00 18.91 ? 341 ASP A CG     1 
ATOM   2532 O OD1    . ASP A 1 350 ? 8.009  17.441 5.197  1.00 16.30 ? 341 ASP A OD1    1 
ATOM   2533 O OD2    . ASP A 1 350 ? 7.641  17.212 3.048  1.00 19.92 ? 341 ASP A OD2    1 
ATOM   2534 N N      . LEU A 1 351 ? 10.349 20.438 6.574  1.00 12.34 ? 342 LEU A N      1 
ATOM   2535 C CA     . LEU A 1 351 ? 9.788  21.648 7.153  1.00 11.03 ? 342 LEU A CA     1 
ATOM   2536 C C      . LEU A 1 351 ? 10.010 22.845 6.262  1.00 12.19 ? 342 LEU A C      1 
ATOM   2537 O O      . LEU A 1 351 ? 9.140  23.715 6.172  1.00 14.46 ? 342 LEU A O      1 
ATOM   2538 C CB     . LEU A 1 351 ? 10.411 21.894 8.542  1.00 12.08 ? 342 LEU A CB     1 
ATOM   2539 C CG     . LEU A 1 351 ? 9.896  23.148 9.201  1.00 11.33 ? 342 LEU A CG     1 
ATOM   2540 C CD1    . LEU A 1 351 ? 8.375  23.052 9.552  1.00 13.71 ? 342 LEU A CD1    1 
ATOM   2541 C CD2    . LEU A 1 351 ? 10.678 23.360 10.502 1.00 14.54 ? 342 LEU A CD2    1 
ATOM   2542 N N      . VAL A 1 352 ? 11.187 22.959 5.613  1.00 13.02 ? 343 VAL A N      1 
ATOM   2543 C CA     . VAL A 1 352 ? 11.422 24.119 4.745  1.00 13.85 ? 343 VAL A CA     1 
ATOM   2544 C C      . VAL A 1 352 ? 10.330 24.194 3.680  1.00 13.89 ? 343 VAL A C      1 
ATOM   2545 O O      . VAL A 1 352 ? 9.734  25.261 3.465  1.00 14.90 ? 343 VAL A O      1 
ATOM   2546 C CB     . VAL A 1 352 ? 12.836 24.072 4.128  1.00 14.06 ? 343 VAL A CB     1 
ATOM   2547 C CG1    . VAL A 1 352 ? 13.029 25.295 3.262  1.00 16.05 ? 343 VAL A CG1    1 
ATOM   2548 C CG2    . VAL A 1 352 ? 13.919 24.039 5.251  1.00 13.61 ? 343 VAL A CG2    1 
ATOM   2549 N N      . MET A 1 353 ? 10.054 23.062 3.039  1.00 13.13 ? 344 MET A N      1 
ATOM   2550 C CA     . MET A 1 353 ? 9.040  23.025 1.983  1.00 14.74 ? 344 MET A CA     1 
ATOM   2551 C C      . MET A 1 353 ? 7.653  23.300 2.530  1.00 16.17 ? 344 MET A C      1 
ATOM   2552 O O      . MET A 1 353 ? 6.875  24.058 1.929  1.00 17.40 ? 344 MET A O      1 
ATOM   2553 C CB     . MET A 1 353 ? 9.116  21.692 1.249  1.00 17.97 ? 344 MET A CB     1 
ATOM   2554 C CG     . MET A 1 353 ? 8.080  21.577 0.150  1.00 25.58 ? 344 MET A CG     1 
ATOM   2555 S SD     . MET A 1 353 ? 8.512  22.575 -1.357 1.00 43.39 ? 344 MET A SD     1 
ATOM   2556 C CE     . MET A 1 353 ? 10.286 22.992 -1.121 1.00 32.00 ? 344 MET A CE     1 
ATOM   2557 N N      . ARG A 1 354 ? 7.346  22.785 3.729  1.00 14.07 ? 345 ARG A N      1 
ATOM   2558 C CA     . ARG A 1 354 ? 6.034  23.042 4.293  1.00 14.55 ? 345 ARG A CA     1 
ATOM   2559 C C      . ARG A 1 354 ? 5.876  24.506 4.616  1.00 17.09 ? 345 ARG A C      1 
ATOM   2560 O O      . ARG A 1 354 ? 4.795  25.081 4.422  1.00 17.75 ? 345 ARG A O      1 
ATOM   2561 C CB     . ARG A 1 354 ? 5.860  22.206 5.560  1.00 13.31 ? 345 ARG A CB     1 
ATOM   2562 C CG     . ARG A 1 354 ? 5.798  20.746 5.244  1.00 15.31 ? 345 ARG A CG     1 
ATOM   2563 C CD     . ARG A 1 354 ? 5.421  19.932 6.468  1.00 15.41 ? 345 ARG A CD     1 
ATOM   2564 N NE     . ARG A 1 354 ? 5.653  18.516 6.210  1.00 16.86 ? 345 ARG A NE     1 
ATOM   2565 C CZ     . ARG A 1 354 ? 4.753  17.577 6.442  1.00 19.76 ? 345 ARG A CZ     1 
ATOM   2566 N NH1    . ARG A 1 354 ? 3.547  17.874 6.897  1.00 18.40 ? 345 ARG A NH1    1 
ATOM   2567 N NH2    . ARG A 1 354 ? 5.073  16.301 6.219  1.00 20.64 ? 345 ARG A NH2    1 
ATOM   2568 N N      . ILE A 1 355 ? 6.939  25.149 5.087  1.00 14.85 ? 346 ILE A N      1 
ATOM   2569 C CA     . ILE A 1 355 ? 6.864  26.587 5.355  1.00 17.40 ? 346 ILE A CA     1 
ATOM   2570 C C      . ILE A 1 355 ? 6.683  27.359 4.045  1.00 18.18 ? 346 ILE A C      1 
ATOM   2571 O O      . ILE A 1 355 ? 5.883  28.301 3.965  1.00 20.84 ? 346 ILE A O      1 
ATOM   2572 C CB     . ILE A 1 355 ? 8.114  27.033 6.152  1.00 15.43 ? 346 ILE A CB     1 
ATOM   2573 C CG1    . ILE A 1 355 ? 7.982  26.539 7.592  1.00 15.85 ? 346 ILE A CG1    1 
ATOM   2574 C CG2    . ILE A 1 355 ? 8.277  28.558 6.153  1.00 18.43 ? 346 ILE A CG2    1 
ATOM   2575 C CD1    . ILE A 1 355 ? 9.201  26.883 8.471  1.00 17.64 ? 346 ILE A CD1    1 
ATOM   2576 N N      . LYS A 1 356 ? 7.384  26.958 2.992  1.00 15.74 ? 347 LYS A N      1 
ATOM   2577 C CA     . LYS A 1 356 ? 7.262  27.639 1.699  1.00 18.34 ? 347 LYS A CA     1 
ATOM   2578 C C      . LYS A 1 356 ? 5.837  27.539 1.167  1.00 19.34 ? 347 LYS A C      1 
ATOM   2579 O O      . LYS A 1 356 ? 5.291  28.527 0.651  1.00 20.95 ? 347 LYS A O      1 
ATOM   2580 C CB     . LYS A 1 356 ? 8.251  27.026 0.712  1.00 18.61 ? 347 LYS A CB     1 
ATOM   2581 C CG     . LYS A 1 356 ? 8.240  27.750 -0.662 1.00 23.98 ? 347 LYS A CG     1 
ATOM   2582 C CD     . LYS A 1 356 ? 9.618  28.024 -1.166 1.00 31.66 ? 347 LYS A CD     1 
ATOM   2583 C CE     . LYS A 1 356 ? 9.553  28.765 -2.514 1.00 37.99 ? 347 LYS A CE     1 
ATOM   2584 N NZ     . LYS A 1 356 ? 10.487 29.954 -2.541 1.00 49.89 ? 347 LYS A NZ     1 
ATOM   2585 N N      . LEU A 1 357 ? 5.232  26.349 1.266  1.00 18.75 ? 348 LEU A N      1 
ATOM   2586 C CA     . LEU A 1 357 ? 3.894  26.126 0.734  1.00 17.25 ? 348 LEU A CA     1 
ATOM   2587 C C      . LEU A 1 357 ? 2.796  26.505 1.711  1.00 18.22 ? 348 LEU A C      1 
ATOM   2588 O O      . LEU A 1 357 ? 1.615  26.436 1.328  1.00 21.31 ? 348 LEU A O      1 
ATOM   2589 C CB     . LEU A 1 357 ? 3.714  24.660 0.369  1.00 19.40 ? 348 LEU A CB     1 
ATOM   2590 C CG     . LEU A 1 357 ? 4.728  24.130 -0.629 1.00 21.84 ? 348 LEU A CG     1 
ATOM   2591 C CD1    . LEU A 1 357 ? 4.533  22.637 -0.868 1.00 23.42 ? 348 LEU A CD1    1 
ATOM   2592 C CD2    . LEU A 1 357 ? 4.622  24.899 -1.968 1.00 28.55 ? 348 LEU A CD2    1 
ATOM   2593 N N      . ASN A 1 358 ? 3.126  26.870 2.957  1.00 17.54 ? 349 ASN A N      1 
ATOM   2594 C CA     . ASN A 1 358 ? 2.138  26.989 4.023  1.00 17.50 ? 349 ASN A CA     1 
ATOM   2595 C C      . ASN A 1 358 ? 1.279  25.736 4.167  1.00 18.32 ? 349 ASN A C      1 
ATOM   2596 O O      . ASN A 1 358 ? 0.067  25.801 4.377  1.00 21.77 ? 349 ASN A O      1 
ATOM   2597 C CB     . ASN A 1 358 ? 1.324  28.282 3.932  1.00 20.10 ? 349 ASN A CB     1 
ATOM   2598 C CG     . ASN A 1 358 ? 0.666  28.631 5.249  1.00 21.00 ? 349 ASN A CG     1 
ATOM   2599 O OD1    . ASN A 1 358 ? 1.000  28.096 6.315  1.00 21.68 ? 349 ASN A OD1    1 
ATOM   2600 N ND2    . ASN A 1 358 ? -0.324 29.509 5.176  1.00 29.72 ? 349 ASN A ND2    1 
ATOM   2601 N N      . ALA A 1 359 ? 1.939  24.573 4.124  1.00 16.10 ? 350 ALA A N      1 
ATOM   2602 C CA     . ALA A 1 359 ? 1.273  23.286 4.239  1.00 17.46 ? 350 ALA A CA     1 
ATOM   2603 C C      . ALA A 1 359 ? 1.106  22.908 5.707  1.00 18.95 ? 350 ALA A C      1 
ATOM   2604 O O      . ALA A 1 359 ? 1.863  23.369 6.566  1.00 17.70 ? 350 ALA A O      1 
ATOM   2605 C CB     . ALA A 1 359 ? 2.104  22.211 3.563  1.00 17.17 ? 350 ALA A CB     1 
ATOM   2606 N N      . PRO A 1 360 ? 0.111  22.109 6.087  1.00 20.31 ? 351 PRO A N      1 
ATOM   2607 C CA     . PRO A 1 360 ? -0.052 21.767 7.502  1.00 21.06 ? 351 PRO A CA     1 
ATOM   2608 C C      . PRO A 1 360 ? 1.169  21.004 8.015  1.00 16.18 ? 351 PRO A C      1 
ATOM   2609 O O      . PRO A 1 360 ? 1.787  20.219 7.308  1.00 19.88 ? 351 PRO A O      1 
ATOM   2610 C CB     . PRO A 1 360 ? -1.288 20.853 7.510  1.00 23.36 ? 351 PRO A CB     1 
ATOM   2611 C CG     . PRO A 1 360 ? -1.783 20.781 6.073  1.00 34.52 ? 351 PRO A CG     1 
ATOM   2612 C CD     . PRO A 1 360 ? -1.072 21.781 5.270  1.00 23.27 ? 351 PRO A CD     1 
ATOM   2613 N N      . LEU A 1 361 ? 1.461  21.197 9.278  1.00 14.81 ? 352 LEU A N      1 
ATOM   2614 C CA     . LEU A 1 361 ? 2.582  20.576 9.964  1.00 13.43 ? 352 LEU A CA     1 
ATOM   2615 C C      . LEU A 1 361 ? 2.139  19.381 10.777 1.00 11.50 ? 352 LEU A C      1 
ATOM   2616 O O      . LEU A 1 361 ? 1.031  19.355 11.309 1.00 13.20 ? 352 LEU A O      1 
ATOM   2617 C CB     . LEU A 1 361 ? 3.196  21.602 10.903 1.00 13.59 ? 352 LEU A CB     1 
ATOM   2618 C CG     . LEU A 1 361 ? 3.672  22.876 10.191 1.00 13.91 ? 352 LEU A CG     1 
ATOM   2619 C CD1    . LEU A 1 361 ? 4.298  23.827 11.208 1.00 19.13 ? 352 LEU A CD1    1 
ATOM   2620 C CD2    . LEU A 1 361 ? 4.681  22.572 9.090  1.00 15.08 ? 352 LEU A CD2    1 
ATOM   2621 N N      . ASN A 1 362 ? 2.988  18.373 10.848 1.00 11.80 ? 353 ASN A N      1 
ATOM   2622 C CA     . ASN A 1 362 ? 2.689  17.154 11.584 1.00 12.69 ? 353 ASN A CA     1 
ATOM   2623 C C      . ASN A 1 362 ? 3.248  17.197 12.987 1.00 14.78 ? 353 ASN A C      1 
ATOM   2624 O O      . ASN A 1 362 ? 4.309  17.781 13.241 1.00 13.82 ? 353 ASN A O      1 
ATOM   2625 C CB     . ASN A 1 362 ? 3.305  15.958 10.900 1.00 12.83 ? 353 ASN A CB     1 
ATOM   2626 C CG     . ASN A 1 362 ? 2.572  15.605 9.576  1.00 17.68 ? 353 ASN A CG     1 
ATOM   2627 O OD1    . ASN A 1 362 ? 1.505  16.154 9.285  1.00 19.60 ? 353 ASN A OD1    1 
ATOM   2628 N ND2    . ASN A 1 362 ? 3.153  14.760 8.741  1.00 19.09 ? 353 ASN A ND2    1 
ATOM   2629 N N      . LYS A 1 363 ? 2.529  16.542 13.908 1.00 12.68 ? 354 LYS A N      1 
ATOM   2630 C CA     . LYS A 1 363 ? 2.920  16.538 15.317 1.00 12.16 ? 354 LYS A CA     1 
ATOM   2631 C C      . LYS A 1 363 ? 4.150  15.664 15.543 1.00 14.05 ? 354 LYS A C      1 
ATOM   2632 O O      . LYS A 1 363 ? 4.454  14.748 14.764 1.00 13.60 ? 354 LYS A O      1 
ATOM   2633 C CB     . LYS A 1 363 ? 1.784  16.042 16.221 1.00 14.47 ? 354 LYS A CB     1 
ATOM   2634 C CG     . LYS A 1 363 ? 1.396  14.594 15.941 1.00 18.30 ? 354 LYS A CG     1 
ATOM   2635 C CD     . LYS A 1 363 ? 0.326  14.140 17.004 1.00 18.64 ? 354 LYS A CD     1 
ATOM   2636 C CE     . LYS A 1 363 ? 1.031  13.761 18.235 1.00 22.47 ? 354 LYS A CE     1 
ATOM   2637 N NZ     . LYS A 1 363 ? 0.021  13.384 19.261 1.00 33.36 ? 354 LYS A NZ     1 
ATOM   2638 N N      . TYR A 1 364 ? 4.831  15.963 16.636 1.00 13.35 ? 355 TYR A N      1 
ATOM   2639 C CA     . TYR A 1 364 ? 5.948  15.132 17.077 1.00 12.84 ? 355 TYR A CA     1 
ATOM   2640 C C      . TYR A 1 364 ? 5.569  14.309 18.288 1.00 17.08 ? 355 TYR A C      1 
ATOM   2641 O O      . TYR A 1 364 ? 4.627  14.627 19.021 1.00 17.70 ? 355 TYR A O      1 
ATOM   2642 C CB     . TYR A 1 364 ? 7.186  15.981 17.380 1.00 16.10 ? 355 TYR A CB     1 
ATOM   2643 C CG     . TYR A 1 364 ? 6.934  17.245 18.135 1.00 13.76 ? 355 TYR A CG     1 
ATOM   2644 C CD1    . TYR A 1 364 ? 6.771  17.196 19.501 1.00 15.17 ? 355 TYR A CD1    1 
ATOM   2645 C CD2    . TYR A 1 364 ? 6.855  18.484 17.479 1.00 14.13 ? 355 TYR A CD2    1 
ATOM   2646 C CE1    . TYR A 1 364 ? 6.490  18.373 20.235 1.00 13.84 ? 355 TYR A CE1    1 
ATOM   2647 C CE2    . TYR A 1 364 ? 6.618  19.673 18.190 1.00 16.57 ? 355 TYR A CE2    1 
ATOM   2648 C CZ     . TYR A 1 364 ? 6.457  19.585 19.550 1.00 15.88 ? 355 TYR A CZ     1 
ATOM   2649 O OH     . TYR A 1 364 ? 6.227  20.747 20.244 1.00 20.48 ? 355 TYR A OH     1 
ATOM   2650 N N      . ASN A 1 365 ? 6.353  13.255 18.518 1.00 17.60 ? 356 ASN A N      1 
ATOM   2651 C CA     . ASN A 1 365 ? 6.128  12.358 19.649 1.00 17.60 ? 356 ASN A CA     1 
ATOM   2652 C C      . ASN A 1 365 ? 7.272  12.548 20.630 1.00 17.57 ? 356 ASN A C      1 
ATOM   2653 O O      . ASN A 1 365 ? 8.365  12.017 20.410 1.00 15.25 ? 356 ASN A O      1 
ATOM   2654 C CB     . ASN A 1 365 ? 6.067  10.926 19.132 1.00 19.63 ? 356 ASN A CB     1 
ATOM   2655 C CG     . ASN A 1 365 ? 5.017  10.730 18.019 1.00 29.73 ? 356 ASN A CG     1 
ATOM   2656 O OD1    . ASN A 1 365 ? 5.285  10.084 16.999 1.00 36.90 ? 356 ASN A OD1    1 
ATOM   2657 N ND2    . ASN A 1 365 ? 3.820  11.270 18.230 1.00 36.29 ? 356 ASN A ND2    1 
ATOM   2658 N N      . ARG A 1 366 ? 7.023  13.249 21.743 1.00 16.45 ? 357 ARG A N      1 
ATOM   2659 C CA     . ARG A 1 366 ? 8.050  13.472 22.733 1.00 16.73 ? 357 ARG A CA     1 
ATOM   2660 C C      . ARG A 1 366 ? 8.646  12.174 23.265 1.00 12.85 ? 357 ARG A C      1 
ATOM   2661 O O      . ARG A 1 366 ? 9.817  12.155 23.688 1.00 15.22 ? 357 ARG A O      1 
ATOM   2662 C CB     . ARG A 1 366 ? 7.459  14.292 23.879 1.00 19.34 ? 357 ARG A CB     1 
ATOM   2663 C CG     . ARG A 1 366 ? 6.850  15.578 23.294 1.00 31.07 ? 357 ARG A CG     1 
ATOM   2664 C CD     . ARG A 1 366 ? 5.980  16.380 24.295 1.00 46.92 ? 357 ARG A CD     1 
ATOM   2665 N NE     . ARG A 1 366 ? 4.722  15.705 24.607 1.00 59.02 ? 357 ARG A NE     1 
ATOM   2666 C CZ     . ARG A 1 366 ? 3.799  16.192 25.429 1.00 59.67 ? 357 ARG A CZ     1 
ATOM   2667 N NH1    . ARG A 1 366 ? 3.969  17.352 26.048 1.00 53.06 ? 357 ARG A NH1    1 
ATOM   2668 N NH2    . ARG A 1 366 ? 2.673  15.505 25.622 1.00 45.06 ? 357 ARG A NH2    1 
ATOM   2669 N N      . LYS A 1 367 ? 7.839  11.094 23.324 1.00 15.24 ? 358 LYS A N      1 
ATOM   2670 C CA     . LYS A 1 367 ? 8.360  9.860  23.916 1.00 15.30 ? 358 LYS A CA     1 
ATOM   2671 C C      . LYS A 1 367 ? 9.547  9.290  23.147 1.00 13.17 ? 358 LYS A C      1 
ATOM   2672 O O      . LYS A 1 367 ? 10.348 8.565  23.731 1.00 17.43 ? 358 LYS A O      1 
ATOM   2673 C CB     . LYS A 1 367 ? 7.243  8.817  24.020 1.00 18.39 ? 358 LYS A CB     1 
ATOM   2674 N N      . THR A 1 368 ? 9.731  9.651  21.882 1.00 14.03 ? 359 THR A N      1 
ATOM   2675 C CA     . THR A 1 368 ? 10.845 9.156  21.079 1.00 12.11 ? 359 THR A CA     1 
ATOM   2676 C C      . THR A 1 368 ? 11.850 10.256 20.741 1.00 11.45 ? 359 THR A C      1 
ATOM   2677 O O      . THR A 1 368 ? 12.685 10.065 19.841 1.00 12.33 ? 359 THR A O      1 
ATOM   2678 C CB     . THR A 1 368 ? 10.346 8.432  19.836 1.00 14.43 ? 359 THR A CB     1 
ATOM   2679 O OG1    . THR A 1 368 ? 9.472  9.278  19.097 1.00 14.64 ? 359 THR A OG1    1 
ATOM   2680 C CG2    . THR A 1 368 ? 9.586  7.121  20.275 1.00 15.03 ? 359 THR A CG2    1 
ATOM   2681 N N      . PHE A 1 369 ? 11.885 11.327 21.543 1.00 12.00 ? 360 PHE A N      1 
ATOM   2682 C CA     . PHE A 1 369 ? 12.920 12.335 21.359 1.00 11.17 ? 360 PHE A CA     1 
ATOM   2683 C C      . PHE A 1 369 ? 14.304 11.745 21.602 1.00 12.12 ? 360 PHE A C      1 
ATOM   2684 O O      . PHE A 1 369 ? 15.252 12.058 20.854 1.00 11.12 ? 360 PHE A O      1 
ATOM   2685 C CB     . PHE A 1 369 ? 12.728 13.533 22.301 1.00 12.35 ? 360 PHE A CB     1 
ATOM   2686 C CG     . PHE A 1 369 ? 11.729 14.555 21.867 1.00 12.11 ? 360 PHE A CG     1 
ATOM   2687 C CD1    . PHE A 1 369 ? 10.955 14.410 20.733 1.00 12.97 ? 360 PHE A CD1    1 
ATOM   2688 C CD2    . PHE A 1 369 ? 11.531 15.668 22.712 1.00 13.46 ? 360 PHE A CD2    1 
ATOM   2689 C CE1    . PHE A 1 369 ? 10.048 15.449 20.384 1.00 14.72 ? 360 PHE A CE1    1 
ATOM   2690 C CE2    . PHE A 1 369 ? 10.612 16.687 22.338 1.00 14.74 ? 360 PHE A CE2    1 
ATOM   2691 C CZ     . PHE A 1 369 ? 9.899  16.556 21.206 1.00 15.49 ? 360 PHE A CZ     1 
ATOM   2692 N N      . TYR A 1 370 ? 14.469 10.913 22.663 1.00 12.30 ? 361 TYR A N      1 
ATOM   2693 C CA     . TYR A 1 370 ? 15.782 10.531 23.167 1.00 10.77 ? 361 TYR A CA     1 
ATOM   2694 C C      . TYR A 1 370 ? 15.953 9.020  23.233 1.00 11.47 ? 361 TYR A C      1 
ATOM   2695 O O      . TYR A 1 370 ? 16.878 8.558  23.910 1.00 14.95 ? 361 TYR A O      1 
ATOM   2696 C CB     . TYR A 1 370 ? 16.024 11.104 24.556 1.00 12.21 ? 361 TYR A CB     1 
ATOM   2697 C CG     . TYR A 1 370 ? 15.868 12.589 24.651 1.00 11.74 ? 361 TYR A CG     1 
ATOM   2698 C CD1    . TYR A 1 370 ? 16.692 13.448 23.949 1.00 12.44 ? 361 TYR A CD1    1 
ATOM   2699 C CD2    . TYR A 1 370 ? 14.909 13.129 25.457 1.00 14.75 ? 361 TYR A CD2    1 
ATOM   2700 C CE1    . TYR A 1 370 ? 16.611 14.823 24.078 1.00 12.84 ? 361 TYR A CE1    1 
ATOM   2701 C CE2    . TYR A 1 370 ? 14.780 14.516 25.607 1.00 15.56 ? 361 TYR A CE2    1 
ATOM   2702 C CZ     . TYR A 1 370 ? 15.652 15.362 24.902 1.00 13.76 ? 361 TYR A CZ     1 
ATOM   2703 O OH     . TYR A 1 370 ? 15.485 16.741 25.087 1.00 15.75 ? 361 TYR A OH     1 
ATOM   2704 N N      . THR A 1 371 ? 15.117 8.273  22.529 1.00 12.94 ? 362 THR A N      1 
ATOM   2705 C CA     . THR A 1 371 ? 15.269 6.822  22.450 1.00 14.71 ? 362 THR A CA     1 
ATOM   2706 C C      . THR A 1 371 ? 16.312 6.458  21.407 1.00 14.83 ? 362 THR A C      1 
ATOM   2707 O O      . THR A 1 371 ? 16.861 7.326  20.701 1.00 13.82 ? 362 THR A O      1 
ATOM   2708 C CB     . THR A 1 371 ? 13.903 6.228  22.125 1.00 13.14 ? 362 THR A CB     1 
ATOM   2709 O OG1    . THR A 1 371 ? 13.306 6.972  21.044 1.00 15.00 ? 362 THR A OG1    1 
ATOM   2710 C CG2    . THR A 1 371 ? 12.993 6.324  23.345 1.00 16.75 ? 362 THR A CG2    1 
ATOM   2711 N N      . GLN A 1 372 ? 16.639 5.158  21.316 1.00 15.71 ? 363 GLN A N      1 
ATOM   2712 C CA     . GLN A 1 372 ? 17.794 4.723  20.531 1.00 14.16 ? 363 GLN A CA     1 
ATOM   2713 C C      . GLN A 1 372 ? 17.447 4.075  19.210 1.00 13.55 ? 363 GLN A C      1 
ATOM   2714 O O      . GLN A 1 372 ? 18.369 3.747  18.450 1.00 13.43 ? 363 GLN A O      1 
ATOM   2715 C CB     . GLN A 1 372 ? 18.657 3.726  21.339 1.00 13.95 ? 363 GLN A CB     1 
ATOM   2716 C CG     . GLN A 1 372 ? 19.616 4.423  22.322 1.00 13.72 ? 363 GLN A CG     1 
ATOM   2717 C CD     . GLN A 1 372 ? 18.860 5.259  23.334 1.00 16.49 ? 363 GLN A CD     1 
ATOM   2718 O OE1    . GLN A 1 372 ? 18.177 4.734  24.240 1.00 16.10 ? 363 GLN A OE1    1 
ATOM   2719 N NE2    . GLN A 1 372 ? 18.970 6.581  23.192 1.00 13.84 ? 363 GLN A NE2    1 
ATOM   2720 N N      . ASP A 1 373 ? 16.177 3.878  18.905 1.00 13.45 ? 364 ASP A N      1 
ATOM   2721 C CA     . ASP A 1 373 ? 15.853 3.197  17.677 1.00 12.72 ? 364 ASP A CA     1 
ATOM   2722 C C      . ASP A 1 373 ? 16.336 4.010  16.473 1.00 15.02 ? 364 ASP A C      1 
ATOM   2723 O O      . ASP A 1 373 ? 16.111 5.223  16.412 1.00 14.57 ? 364 ASP A O      1 
ATOM   2724 C CB     . ASP A 1 373 ? 14.335 2.989  17.543 1.00 15.43 ? 364 ASP A CB     1 
ATOM   2725 C CG     . ASP A 1 373 ? 14.000 1.906  16.517 1.00 17.63 ? 364 ASP A CG     1 
ATOM   2726 O OD1    . ASP A 1 373 ? 13.969 2.205  15.335 1.00 16.53 ? 364 ASP A OD1    1 
ATOM   2727 O OD2    . ASP A 1 373 ? 13.800 0.725  16.946 1.00 21.56 ? 364 ASP A OD2    1 
ATOM   2728 N N      . PRO A 1 374 ? 16.975 3.386  15.479 1.00 14.06 ? 365 PRO A N      1 
ATOM   2729 C CA     . PRO A 1 374 ? 17.477 4.150  14.344 1.00 16.79 ? 365 PRO A CA     1 
ATOM   2730 C C      . PRO A 1 374 ? 16.397 4.662  13.428 1.00 14.30 ? 365 PRO A C      1 
ATOM   2731 O O      . PRO A 1 374 ? 16.697 5.494  12.569 1.00 16.49 ? 365 PRO A O      1 
ATOM   2732 C CB     . PRO A 1 374 ? 18.365 3.133  13.604 1.00 17.97 ? 365 PRO A CB     1 
ATOM   2733 C CG     . PRO A 1 374 ? 17.766 1.781  14.029 1.00 16.69 ? 365 PRO A CG     1 
ATOM   2734 C CD     . PRO A 1 374 ? 17.378 1.958  15.451 1.00 15.34 ? 365 PRO A CD     1 
ATOM   2735 N N      . VAL A 1 375 ? 15.161 4.156  13.530 1.00 13.76 ? 366 VAL A N      1 
ATOM   2736 C CA     . VAL A 1 375 ? 14.078 4.536  12.638 1.00 14.74 ? 366 VAL A CA     1 
ATOM   2737 C C      . VAL A 1 375 ? 12.930 5.170  13.416 1.00 13.66 ? 366 VAL A C      1 
ATOM   2738 O O      . VAL A 1 375 ? 12.452 6.273  13.065 1.00 14.01 ? 366 VAL A O      1 
ATOM   2739 C CB     . VAL A 1 375 ? 13.575 3.312  11.851 1.00 15.61 ? 366 VAL A CB     1 
ATOM   2740 C CG1    . VAL A 1 375 ? 12.365 3.644  11.009 1.00 16.49 ? 366 VAL A CG1    1 
ATOM   2741 C CG2    . VAL A 1 375 ? 14.698 2.794  10.970 1.00 16.80 ? 366 VAL A CG2    1 
ATOM   2742 N N      . VAL A 1 376 ? 12.430 4.462  14.438 1.00 13.74 ? 367 VAL A N      1 
ATOM   2743 C CA     . VAL A 1 376 ? 11.145 4.815  15.050 1.00 13.88 ? 367 VAL A CA     1 
ATOM   2744 C C      . VAL A 1 376 ? 11.269 6.163  15.761 1.00 13.21 ? 367 VAL A C      1 
ATOM   2745 O O      . VAL A 1 376 ? 12.091 6.315  16.677 1.00 14.49 ? 367 VAL A O      1 
ATOM   2746 C CB     . VAL A 1 376 ? 10.699 3.722  16.025 1.00 13.50 ? 367 VAL A CB     1 
ATOM   2747 C CG1    . VAL A 1 376 ? 9.473  4.185  16.814 1.00 16.76 ? 367 VAL A CG1    1 
ATOM   2748 C CG2    . VAL A 1 376 ? 10.304 2.475  15.250 1.00 15.95 ? 367 VAL A CG2    1 
ATOM   2749 N N      . GLY A 1 377 ? 10.429 7.114  15.364 1.00 13.92 ? 368 GLY A N      1 
ATOM   2750 C CA     . GLY A 1 377 ? 10.487 8.449  15.950 1.00 14.38 ? 368 GLY A CA     1 
ATOM   2751 C C      . GLY A 1 377 ? 11.677 9.244  15.510 1.00 12.85 ? 368 GLY A C      1 
ATOM   2752 O O      . GLY A 1 377 ? 11.960 10.286 16.111 1.00 13.50 ? 368 GLY A O      1 
ATOM   2753 N N      . TYR A 1 378 ? 12.384 8.803  14.477 1.00 12.98 ? 369 TYR A N      1 
ATOM   2754 C CA     . TYR A 1 378 ? 13.624 9.466  14.081 1.00 12.40 ? 369 TYR A CA     1 
ATOM   2755 C C      . TYR A 1 378 ? 13.619 9.751  12.578 1.00 13.39 ? 369 TYR A C      1 
ATOM   2756 O O      . TYR A 1 378 ? 13.635 10.914 12.171 1.00 13.39 ? 369 TYR A O      1 
ATOM   2757 C CB     . TYR A 1 378 ? 14.804 8.584  14.487 1.00 13.60 ? 369 TYR A CB     1 
ATOM   2758 C CG     . TYR A 1 378 ? 16.177 9.258  14.395 1.00 11.46 ? 369 TYR A CG     1 
ATOM   2759 C CD1    . TYR A 1 378 ? 16.432 10.503 14.996 1.00 13.07 ? 369 TYR A CD1    1 
ATOM   2760 C CD2    . TYR A 1 378 ? 17.223 8.648  13.713 1.00 12.64 ? 369 TYR A CD2    1 
ATOM   2761 C CE1    . TYR A 1 378 ? 17.694 11.122 14.911 1.00 12.37 ? 369 TYR A CE1    1 
ATOM   2762 C CE2    . TYR A 1 378 ? 18.473 9.274  13.641 1.00 13.15 ? 369 TYR A CE2    1 
ATOM   2763 C CZ     . TYR A 1 378 ? 18.696 10.467 14.269 1.00 13.31 ? 369 TYR A CZ     1 
ATOM   2764 O OH     . TYR A 1 378 ? 19.916 11.115 14.193 1.00 16.76 ? 369 TYR A OH     1 
ATOM   2765 N N      . THR A 1 379 ? 13.534 8.707  11.737 1.00 13.56 ? 370 THR A N      1 
ATOM   2766 C CA     . THR A 1 379 ? 13.492 8.873  10.291 1.00 14.64 ? 370 THR A CA     1 
ATOM   2767 C C      . THR A 1 379 ? 12.185 8.418  9.689  1.00 13.29 ? 370 THR A C      1 
ATOM   2768 O O      . THR A 1 379 ? 12.047 8.483  8.464  1.00 16.55 ? 370 THR A O      1 
ATOM   2769 C CB     . THR A 1 379 ? 14.654 8.145  9.618  1.00 15.35 ? 370 THR A CB     1 
ATOM   2770 O OG1    . THR A 1 379 ? 14.549 6.771  9.973  1.00 16.44 ? 370 THR A OG1    1 
ATOM   2771 C CG2    . THR A 1 379 ? 15.967 8.719  10.115 1.00 17.91 ? 370 THR A CG2    1 
ATOM   2772 N N      . ASP A 1 380 ? 11.209 8.011  10.490 1.00 15.06 ? 371 ASP A N      1 
ATOM   2773 C CA     . ASP A 1 380 ? 9.938  7.537  9.932  1.00 14.80 ? 371 ASP A CA     1 
ATOM   2774 C C      . ASP A 1 380 ? 8.844  8.591  9.941  1.00 17.53 ? 371 ASP A C      1 
ATOM   2775 O O      . ASP A 1 380 ? 7.698  8.256  9.676  1.00 20.56 ? 371 ASP A O      1 
ATOM   2776 C CB     . ASP A 1 380 ? 9.498  6.236  10.634 1.00 18.93 ? 371 ASP A CB     1 
ATOM   2777 C CG     . ASP A 1 380 ? 9.207  6.404  12.114 1.00 22.70 ? 371 ASP A CG     1 
ATOM   2778 O OD1    . ASP A 1 380 ? 9.422  7.480  12.656 1.00 17.78 ? 371 ASP A OD1    1 
ATOM   2779 O OD2    . ASP A 1 380 ? 8.732  5.412  12.757 1.00 24.28 ? 371 ASP A OD2    1 
ATOM   2780 N N      . TYR A 1 381 ? 9.135  9.858  10.243 1.00 13.85 ? 372 TYR A N      1 
ATOM   2781 C CA     . TYR A 1 381 ? 8.094  10.860 10.027 1.00 14.33 ? 372 TYR A CA     1 
ATOM   2782 C C      . TYR A 1 381 ? 8.016  11.151 8.534  1.00 16.65 ? 372 TYR A C      1 
ATOM   2783 O O      . TYR A 1 381 ? 9.038  11.438 7.905  1.00 17.84 ? 372 TYR A O      1 
ATOM   2784 C CB     . TYR A 1 381 ? 8.451  12.145 10.772 1.00 14.92 ? 372 TYR A CB     1 
ATOM   2785 C CG     . TYR A 1 381 ? 8.343  12.086 12.260 1.00 12.89 ? 372 TYR A CG     1 
ATOM   2786 C CD1    . TYR A 1 381 ? 7.102  12.246 12.917 1.00 13.46 ? 372 TYR A CD1    1 
ATOM   2787 C CD2    . TYR A 1 381 ? 9.487  11.938 13.074 1.00 12.69 ? 372 TYR A CD2    1 
ATOM   2788 C CE1    . TYR A 1 381 ? 7.015  12.281 14.314 1.00 15.62 ? 372 TYR A CE1    1 
ATOM   2789 C CE2    . TYR A 1 381 ? 9.406  11.948 14.469 1.00 14.15 ? 372 TYR A CE2    1 
ATOM   2790 C CZ     . TYR A 1 381 ? 8.160  12.119 15.088 1.00 14.25 ? 372 TYR A CZ     1 
ATOM   2791 O OH     . TYR A 1 381 ? 8.100  12.185 16.446 1.00 15.12 ? 372 TYR A OH     1 
ATOM   2792 N N      . PRO A 1 382 ? 6.838  11.087 7.922  1.00 16.29 ? 373 PRO A N      1 
ATOM   2793 C CA     . PRO A 1 382 ? 6.791  11.180 6.463  1.00 18.14 ? 373 PRO A CA     1 
ATOM   2794 C C      . PRO A 1 382 ? 6.955  12.599 5.922  1.00 17.41 ? 373 PRO A C      1 
ATOM   2795 O O      . PRO A 1 382 ? 6.719  13.622 6.589  1.00 16.50 ? 373 PRO A O      1 
ATOM   2796 C CB     . PRO A 1 382 ? 5.387  10.651 6.123  1.00 21.22 ? 373 PRO A CB     1 
ATOM   2797 C CG     . PRO A 1 382 ? 4.598  10.891 7.346  1.00 21.71 ? 373 PRO A CG     1 
ATOM   2798 C CD     . PRO A 1 382 ? 5.567  10.653 8.519  1.00 19.65 ? 373 PRO A CD     1 
ATOM   2799 N N      . PHE A 1 383 ? 7.324  12.641 4.659  1.00 18.18 ? 374 PHE A N      1 
ATOM   2800 C CA     . PHE A 1 383 ? 7.299  13.856 3.870  1.00 16.34 ? 374 PHE A CA     1 
ATOM   2801 C C      . PHE A 1 383 ? 5.869  14.155 3.419  1.00 20.53 ? 374 PHE A C      1 
ATOM   2802 O O      . PHE A 1 383 ? 4.966  13.315 3.526  1.00 21.96 ? 374 PHE A O      1 
ATOM   2803 C CB     . PHE A 1 383 ? 8.173  13.679 2.618  1.00 17.29 ? 374 PHE A CB     1 
ATOM   2804 C CG     . PHE A 1 383 ? 9.615  13.647 2.937  1.00 16.68 ? 374 PHE A CG     1 
ATOM   2805 C CD1    . PHE A 1 383 ? 10.196 12.484 3.402  1.00 19.47 ? 374 PHE A CD1    1 
ATOM   2806 C CD2    . PHE A 1 383 ? 10.382 14.773 2.824  1.00 17.08 ? 374 PHE A CD2    1 
ATOM   2807 C CE1    . PHE A 1 383 ? 11.540 12.465 3.743  1.00 22.64 ? 374 PHE A CE1    1 
ATOM   2808 C CE2    . PHE A 1 383 ? 11.748 14.743 3.140  1.00 19.67 ? 374 PHE A CE2    1 
ATOM   2809 C CZ     . PHE A 1 383 ? 12.298 13.595 3.609  1.00 20.22 ? 374 PHE A CZ     1 
ATOM   2810 N N      . LEU A 1 384 ? 5.664  15.371 2.895  1.00 18.18 ? 375 LEU A N      1 
ATOM   2811 C CA     . LEU A 1 384 ? 4.364  15.695 2.280  1.00 21.66 ? 375 LEU A CA     1 
ATOM   2812 C C      . LEU A 1 384 ? 3.933  14.698 1.201  1.00 25.33 ? 375 LEU A C      1 
ATOM   2813 O O      . LEU A 1 384 ? 4.788  14.260 0.438  1.00 29.40 ? 375 LEU A O      1 
ATOM   2814 C CB     . LEU A 1 384 ? 4.440  17.052 1.609  1.00 24.94 ? 375 LEU A CB     1 
ATOM   2815 C CG     . LEU A 1 384 ? 4.422  18.185 2.595  1.00 22.28 ? 375 LEU A CG     1 
ATOM   2816 C CD1    . LEU A 1 384 ? 4.760  19.468 1.796  1.00 22.01 ? 375 LEU A CD1    1 
ATOM   2817 C CD2    . LEU A 1 384 ? 3.026  18.261 3.279  1.00 26.92 ? 375 LEU A CD2    1 
HETATM 2818 N N1     . FMN B 2 .   ? 19.737 22.887 21.988 1.00 9.23  ? 401 FMN A N1     1 
HETATM 2819 C C2     . FMN B 2 .   ? 21.083 22.857 21.811 1.00 9.92  ? 401 FMN A C2     1 
HETATM 2820 O O2     . FMN B 2 .   ? 21.718 23.935 21.788 1.00 9.14  ? 401 FMN A O2     1 
HETATM 2821 N N3     . FMN B 2 .   ? 21.744 21.640 21.659 1.00 10.02 ? 401 FMN A N3     1 
HETATM 2822 C C4     . FMN B 2 .   ? 21.108 20.440 21.678 1.00 10.45 ? 401 FMN A C4     1 
HETATM 2823 O O4     . FMN B 2 .   ? 21.754 19.394 21.491 1.00 9.87  ? 401 FMN A O4     1 
HETATM 2824 C C4A    . FMN B 2 .   ? 19.746 20.467 21.895 1.00 9.18  ? 401 FMN A C4A    1 
HETATM 2825 N N5     . FMN B 2 .   ? 19.033 19.281 21.999 1.00 11.64 ? 401 FMN A N5     1 
HETATM 2826 C C5A    . FMN B 2 .   ? 17.641 19.318 21.992 1.00 10.74 ? 401 FMN A C5A    1 
HETATM 2827 C C6     . FMN B 2 .   ? 16.939 18.112 21.949 1.00 10.09 ? 401 FMN A C6     1 
HETATM 2828 C C7     . FMN B 2 .   ? 15.596 18.098 21.950 1.00 10.79 ? 401 FMN A C7     1 
HETATM 2829 C C7M    . FMN B 2 .   ? 14.883 16.751 21.836 1.00 13.95 ? 401 FMN A C7M    1 
HETATM 2830 C C8     . FMN B 2 .   ? 14.911 19.311 22.033 1.00 13.56 ? 401 FMN A C8     1 
HETATM 2831 C C8M    . FMN B 2 .   ? 13.387 19.357 22.070 1.00 18.59 ? 401 FMN A C8M    1 
HETATM 2832 C C9     . FMN B 2 .   ? 15.596 20.532 22.069 1.00 13.15 ? 401 FMN A C9     1 
HETATM 2833 C C9A    . FMN B 2 .   ? 16.974 20.526 22.053 1.00 10.52 ? 401 FMN A C9A    1 
HETATM 2834 N N10    . FMN B 2 .   ? 17.688 21.717 22.066 1.00 9.97  ? 401 FMN A N10    1 
HETATM 2835 C C10    . FMN B 2 .   ? 19.070 21.695 21.988 1.00 9.50  ? 401 FMN A C10    1 
HETATM 2836 C "C1'"  . FMN B 2 .   ? 16.986 23.037 22.046 1.00 10.46 ? 401 FMN A "C1'"  1 
HETATM 2837 C "C2'"  . FMN B 2 .   ? 16.560 23.281 20.568 1.00 10.43 ? 401 FMN A "C2'"  1 
HETATM 2838 O "O2'"  . FMN B 2 .   ? 17.690 23.565 19.739 1.00 10.80 ? 401 FMN A "O2'"  1 
HETATM 2839 C "C3'"  . FMN B 2 .   ? 15.589 24.468 20.414 1.00 9.93  ? 401 FMN A "C3'"  1 
HETATM 2840 O "O3'"  . FMN B 2 .   ? 16.290 25.660 20.777 1.00 10.75 ? 401 FMN A "O3'"  1 
HETATM 2841 C "C4'"  . FMN B 2 .   ? 14.346 24.407 21.297 1.00 11.59 ? 401 FMN A "C4'"  1 
HETATM 2842 O "O4'"  . FMN B 2 .   ? 13.675 23.196 20.956 1.00 12.93 ? 401 FMN A "O4'"  1 
HETATM 2843 C "C5'"  . FMN B 2 .   ? 13.369 25.570 21.057 1.00 11.86 ? 401 FMN A "C5'"  1 
HETATM 2844 O "O5'"  . FMN B 2 .   ? 13.078 25.756 19.653 1.00 11.38 ? 401 FMN A "O5'"  1 
HETATM 2845 P P      . FMN B 2 .   ? 11.682 25.193 19.058 1.00 11.11 ? 401 FMN A P      1 
HETATM 2846 O O1P    . FMN B 2 .   ? 10.537 25.887 19.796 1.00 11.80 ? 401 FMN A O1P    1 
HETATM 2847 O O2P    . FMN B 2 .   ? 11.752 25.551 17.605 1.00 10.58 ? 401 FMN A O2P    1 
HETATM 2848 O O3P    . FMN B 2 .   ? 11.686 23.712 19.300 1.00 11.91 ? 401 FMN A O3P    1 
HETATM 2849 O O7N    A WI6 C 3 .   ? 20.966 21.858 24.862 0.55 7.45  ? 402 WI6 A O7N    1 
HETATM 2850 O O7N    B WI6 C 3 .   ? 19.816 19.568 26.107 0.45 14.41 ? 402 WI6 A O7N    1 
HETATM 2851 C C7N    A WI6 C 3 .   ? 20.570 20.744 24.950 0.55 13.25 ? 402 WI6 A C7N    1 
HETATM 2852 C C7N    B WI6 C 3 .   ? 18.650 19.262 25.859 0.45 16.74 ? 402 WI6 A C7N    1 
HETATM 2853 N N7N    A WI6 C 3 .   ? 21.365 19.686 24.646 0.55 13.92 ? 402 WI6 A N7N    1 
HETATM 2854 N N7N    B WI6 C 3 .   ? 18.333 18.156 25.210 0.45 11.36 ? 402 WI6 A N7N    1 
HETATM 2855 C C3N    A WI6 C 3 .   ? 19.079 20.488 25.215 0.55 19.88 ? 402 WI6 A C3N    1 
HETATM 2856 C C3N    B WI6 C 3 .   ? 17.513 20.132 26.332 0.45 20.64 ? 402 WI6 A C3N    1 
HETATM 2857 C C2N    A WI6 C 3 .   ? 18.423 21.580 26.033 0.55 18.14 ? 402 WI6 A C2N    1 
HETATM 2858 C C2N    B WI6 C 3 .   ? 16.377 20.188 25.317 0.45 17.20 ? 402 WI6 A C2N    1 
HETATM 2859 C C4N    A WI6 C 3 .   ? 18.596 19.154 25.681 0.55 15.74 ? 402 WI6 A C4N    1 
HETATM 2860 C C4N    B WI6 C 3 .   ? 17.972 21.533 26.644 0.45 14.22 ? 402 WI6 A C4N    1 
HETATM 2861 C C5N    A WI6 C 3 .   ? 17.359 19.109 26.150 0.55 26.65 ? 402 WI6 A C5N    1 
HETATM 2862 C C5N    B WI6 C 3 .   ? 17.056 22.465 26.805 0.45 20.52 ? 402 WI6 A C5N    1 
HETATM 2863 C C6N    A WI6 C 3 .   ? 16.384 20.218 25.889 0.55 17.52 ? 402 WI6 A C6N    1 
HETATM 2864 C C6N    B WI6 C 3 .   ? 15.759 22.459 26.086 0.45 18.98 ? 402 WI6 A C6N    1 
HETATM 2865 N N1N    A WI6 C 3 .   ? 17.005 21.524 25.865 0.55 20.45 ? 402 WI6 A N1N    1 
HETATM 2866 N N1N    B WI6 C 3 .   ? 15.319 21.085 25.802 0.45 14.72 ? 402 WI6 A N1N    1 
HETATM 2867 C "C1'A" A WI6 C 3 .   ? 16.310 22.665 26.406 0.55 16.97 ? 402 WI6 A "C1'A" 1 
HETATM 2868 C "C1'A" B WI6 C 3 .   ? 14.087 20.988 25.070 0.45 14.76 ? 402 WI6 A "C1'A" 1 
HETATM 2869 O "O4'A" A WI6 C 3 .   ? 16.221 22.514 27.814 0.55 19.67 ? 402 WI6 A "O4'A" 1 
HETATM 2870 O "O4'A" B WI6 C 3 .   ? 13.902 22.110 24.239 0.45 13.35 ? 402 WI6 A "O4'A" 1 
HETATM 2871 C "C2'A" A WI6 C 3 .   ? 14.860 22.962 25.979 0.55 19.23 ? 402 WI6 A "C2'A" 1 
HETATM 2872 C "C2'A" B WI6 C 3 .   ? 12.871 20.966 25.981 0.45 13.40 ? 402 WI6 A "C2'A" 1 
HETATM 2873 O "O2'A" A WI6 C 3 .   ? 14.804 23.587 24.724 0.55 17.50 ? 402 WI6 A "O2'A" 1 
HETATM 2874 O "O2'A" B WI6 C 3 .   ? 12.685 19.686 26.567 0.45 12.04 ? 402 WI6 A "O2'A" 1 
HETATM 2875 C "C3'A" A WI6 C 3 .   ? 14.351 23.842 27.145 0.55 19.51 ? 402 WI6 A "C3'A" 1 
HETATM 2876 C "C3'A" B WI6 C 3 .   ? 11.768 21.391 25.017 0.45 14.51 ? 402 WI6 A "C3'A" 1 
HETATM 2877 O "O3'A" A WI6 C 3 .   ? 14.660 25.224 27.016 0.55 22.17 ? 402 WI6 A "O3'A" 1 
HETATM 2878 O "O3'A" B WI6 C 3 .   ? 11.293 20.271 24.293 0.45 16.25 ? 402 WI6 A "O3'A" 1 
HETATM 2879 C "C4'A" A WI6 C 3 .   ? 15.038 23.189 28.328 0.55 21.89 ? 402 WI6 A "C4'A" 1 
HETATM 2880 C "C4'A" B WI6 C 3 .   ? 12.487 22.401 24.107 0.45 9.08  ? 402 WI6 A "C4'A" 1 
HETATM 2881 C "C5'A" A WI6 C 3 .   ? 13.996 22.359 29.079 0.55 22.61 ? 402 WI6 A "C5'A" 1 
HETATM 2882 C "C5'A" B WI6 C 3 .   ? 12.253 23.850 24.449 0.45 19.02 ? 402 WI6 A "C5'A" 1 
HETATM 2883 O "O5'A" A WI6 C 3 .   ? 12.658 22.784 28.801 0.55 36.95 ? 402 WI6 A "O5'A" 1 
HETATM 2884 O "O5'A" B WI6 C 3 .   ? 12.494 24.035 25.870 0.45 18.58 ? 402 WI6 A "O5'A" 1 
HETATM 2885 P PN     A WI6 C 3 .   ? 11.415 21.701 28.534 0.55 46.78 ? 402 WI6 A PN     1 
HETATM 2886 P PN     B WI6 C 3 .   ? 11.682 25.166 26.667 0.45 20.26 ? 402 WI6 A PN     1 
HETATM 2887 O O1N    A WI6 C 3 .   ? 12.173 20.466 28.142 0.55 26.26 ? 402 WI6 A O1N    1 
HETATM 2888 O O1N    B WI6 C 3 .   ? 10.267 25.163 26.199 0.45 25.03 ? 402 WI6 A O1N    1 
HETATM 2889 O O2N    A WI6 C 3 .   ? 10.509 21.692 29.735 0.55 46.18 ? 402 WI6 A O2N    1 
HETATM 2890 O O2N    B WI6 C 3 .   ? 12.446 26.441 26.589 0.45 30.00 ? 402 WI6 A O2N    1 
HETATM 2891 O O3     A WI6 C 3 .   ? 10.629 22.421 27.236 0.55 42.77 ? 402 WI6 A O3     1 
HETATM 2892 O O3     B WI6 C 3 .   ? 11.736 24.626 28.182 0.45 22.98 ? 402 WI6 A O3     1 
HETATM 2893 P PA     A WI6 C 3 .   ? 9.084  23.052 27.089 0.55 52.81 ? 402 WI6 A PA     1 
HETATM 2894 P PA     B WI6 C 3 .   ? 11.850 23.204 28.928 0.45 30.06 ? 402 WI6 A PA     1 
HETATM 2895 O O2P    A WI6 C 3 .   ? 8.970  24.260 26.187 0.55 41.19 ? 402 WI6 A O2P    1 
HETATM 2896 O O2P    B WI6 C 3 .   ? 10.882 22.245 28.324 0.45 36.51 ? 402 WI6 A O2P    1 
HETATM 2897 O O1     A WI6 C 3 .   ? 8.099  21.936 26.922 0.55 41.76 ? 402 WI6 A O1     1 
HETATM 2898 O O1     B WI6 C 3 .   ? 13.284 22.797 29.013 0.45 30.88 ? 402 WI6 A O1     1 
HETATM 2899 O "O5'"  A WI6 C 3 .   ? 9.012  23.680 28.603 0.55 51.00 ? 402 WI6 A "O5'"  1 
HETATM 2900 O "O5'"  B WI6 C 3 .   ? 11.348 23.614 30.393 0.45 32.12 ? 402 WI6 A "O5'"  1 
HETATM 2901 C "C5'"  B WI6 C 3 .   ? 9.934  23.543 30.678 0.00 30.00 ? 402 WI6 A "C5'"  1 
HETATM 2902 C "C4'"  B WI6 C 3 .   ? 9.742  23.046 32.089 0.00 30.00 ? 402 WI6 A "C4'"  1 
HETATM 2903 O "O4'"  B WI6 C 3 .   ? 9.841  21.599 32.105 0.00 30.00 ? 402 WI6 A "O4'"  1 
HETATM 2904 C "C1'"  B WI6 C 3 .   ? 10.436 21.167 33.309 0.45 24.72 ? 402 WI6 A "C1'"  1 
HETATM 2905 C "C2'"  B WI6 C 3 .   ? 10.615 22.407 34.181 0.45 24.72 ? 402 WI6 A "C2'"  1 
HETATM 2906 C "C3'"  B WI6 C 3 .   ? 10.785 23.496 33.119 0.00 30.00 ? 402 WI6 A "C3'"  1 
HETATM 2907 N N9A    B WI6 C 3 .   ? 11.687 20.486 32.997 0.45 25.31 ? 402 WI6 A N9A    1 
HETATM 2908 C C4A    B WI6 C 3 .   ? 12.400 19.645 33.819 0.45 25.17 ? 402 WI6 A C4A    1 
HETATM 2909 C C5A    B WI6 C 3 .   ? 13.508 19.258 33.093 0.45 26.04 ? 402 WI6 A C5A    1 
HETATM 2910 N N7A    B WI6 C 3 .   ? 13.494 19.847 31.837 0.45 27.59 ? 402 WI6 A N7A    1 
HETATM 2911 C C8A    B WI6 C 3 .   ? 12.398 20.562 31.826 0.45 26.44 ? 402 WI6 A C8A    1 
HETATM 2912 C C6A    B WI6 C 3 .   ? 14.415 18.382 33.720 0.45 25.73 ? 402 WI6 A C6A    1 
HETATM 2913 N N1A    B WI6 C 3 .   ? 14.131 17.979 34.982 0.45 17.10 ? 402 WI6 A N1A    1 
HETATM 2914 C C2A    B WI6 C 3 .   ? 13.017 18.442 35.558 0.45 27.07 ? 402 WI6 A C2A    1 
HETATM 2915 N N3A    B WI6 C 3 .   ? 12.098 19.270 35.071 0.45 27.05 ? 402 WI6 A N3A    1 
HETATM 2916 O "O2'"  B WI6 C 3 .   ? 9.483  22.618 34.994 0.00 30.00 ? 402 WI6 A "O2'"  1 
HETATM 2917 O "O3'"  B WI6 C 3 .   ? 10.526 24.798 33.630 0.00 30.00 ? 402 WI6 A "O3'"  1 
HETATM 2918 N N6A    B WI6 C 3 .   ? 15.524 17.935 33.142 0.45 26.66 ? 402 WI6 A N6A    1 
HETATM 2919 S S      . SO4 D 4 .   ? 3.624  12.067 22.781 1.00 94.76 ? 403 SO4 A S      1 
HETATM 2920 O O1     . SO4 D 4 .   ? 3.996  13.451 22.619 1.00 41.53 ? 403 SO4 A O1     1 
HETATM 2921 O O2     . SO4 D 4 .   ? 2.709  11.693 21.744 1.00 60.06 ? 403 SO4 A O2     1 
HETATM 2922 O O3     . SO4 D 4 .   ? 2.994  11.886 24.057 1.00 71.13 ? 403 SO4 A O3     1 
HETATM 2923 O O4     . SO4 D 4 .   ? 4.797  11.234 22.706 1.00 44.12 ? 403 SO4 A O4     1 
HETATM 2924 O O      . HOH E 5 .   ? 22.752 41.915 39.198 1.00 37.14 ? 501 HOH A O      1 
HETATM 2925 O O      . HOH E 5 .   ? 30.253 44.937 27.953 1.00 28.49 ? 502 HOH A O      1 
HETATM 2926 O O      . HOH E 5 .   ? 31.313 47.607 27.315 1.00 39.74 ? 503 HOH A O      1 
HETATM 2927 O O      . HOH E 5 .   ? 37.144 34.467 9.051  1.00 32.39 ? 504 HOH A O      1 
HETATM 2928 O O      . HOH E 5 .   ? 13.172 17.641 25.527 1.00 37.62 ? 505 HOH A O      1 
HETATM 2929 O O      . HOH E 5 .   ? 23.226 44.273 37.323 1.00 31.82 ? 506 HOH A O      1 
HETATM 2930 O O      . HOH E 5 .   ? 10.267 34.113 29.271 1.00 41.37 ? 507 HOH A O      1 
HETATM 2931 O O      . HOH E 5 .   ? 40.402 38.060 18.222 1.00 36.42 ? 508 HOH A O      1 
HETATM 2932 O O      . HOH E 5 .   ? 19.094 18.823 30.054 1.00 28.47 ? 509 HOH A O      1 
HETATM 2933 O O      . HOH E 5 .   ? 14.834 30.348 -1.330 1.00 42.08 ? 510 HOH A O      1 
HETATM 2934 O O      . HOH E 5 .   ? 20.190 17.053 31.504 1.00 24.93 ? 511 HOH A O      1 
HETATM 2935 O O      . HOH E 5 .   ? 29.161 0.866  19.318 1.00 38.93 ? 512 HOH A O      1 
HETATM 2936 O O      . HOH E 5 .   ? 15.778 21.413 45.160 1.00 43.38 ? 513 HOH A O      1 
HETATM 2937 O O      . HOH E 5 .   ? 27.753 40.658 38.565 1.00 30.86 ? 514 HOH A O      1 
HETATM 2938 O O      . HOH E 5 .   ? 31.745 9.599  2.635  1.00 35.40 ? 515 HOH A O      1 
HETATM 2939 O O      . HOH E 5 .   ? 16.969 6.300  38.038 1.00 32.47 ? 516 HOH A O      1 
HETATM 2940 O O      . HOH E 5 .   ? 38.350 41.278 36.006 1.00 37.97 ? 517 HOH A O      1 
HETATM 2941 O O      . HOH E 5 .   ? 24.086 40.599 7.138  1.00 37.79 ? 518 HOH A O      1 
HETATM 2942 O O      . HOH E 5 .   ? 28.627 5.409  11.021 1.00 28.06 ? 519 HOH A O      1 
HETATM 2943 O O      . HOH E 5 .   ? 29.046 -1.602 22.187 1.00 22.97 ? 520 HOH A O      1 
HETATM 2944 O O      . HOH E 5 .   ? 0.470  28.349 8.843  1.00 32.49 ? 521 HOH A O      1 
HETATM 2945 O O      . HOH E 5 .   ? 20.790 17.058 42.460 1.00 17.13 ? 522 HOH A O      1 
HETATM 2946 O O      . HOH E 5 .   ? 25.527 27.507 0.485  1.00 33.38 ? 523 HOH A O      1 
HETATM 2947 O O      . HOH E 5 .   ? 35.215 3.058  19.836 1.00 33.43 ? 524 HOH A O      1 
HETATM 2948 O O      . HOH E 5 .   ? 43.886 34.212 34.341 1.00 27.80 ? 525 HOH A O      1 
HETATM 2949 O O      . HOH E 5 .   ? 10.186 11.694 17.934 1.00 15.58 ? 526 HOH A O      1 
HETATM 2950 O O      . HOH E 5 .   ? 7.722  31.999 26.916 1.00 38.41 ? 527 HOH A O      1 
HETATM 2951 O O      . HOH E 5 .   ? 20.148 28.868 30.030 1.00 19.28 ? 528 HOH A O      1 
HETATM 2952 O O      . HOH E 5 .   ? 22.451 28.953 -2.169 1.00 28.33 ? 529 HOH A O      1 
HETATM 2953 O O      . HOH E 5 .   ? 38.663 17.548 21.501 1.00 32.67 ? 530 HOH A O      1 
HETATM 2954 O O      . HOH E 5 .   ? 36.381 42.361 37.019 1.00 28.74 ? 531 HOH A O      1 
HETATM 2955 O O      . HOH E 5 .   ? 37.888 21.959 43.255 1.00 33.76 ? 532 HOH A O      1 
HETATM 2956 O O      . HOH E 5 .   ? 23.594 14.805 -4.990 1.00 21.84 ? 533 HOH A O      1 
HETATM 2957 O O      . HOH E 5 .   ? 11.599 -0.634 17.401 1.00 22.63 ? 534 HOH A O      1 
HETATM 2958 O O      . HOH E 5 .   ? 44.742 31.527 37.284 1.00 18.79 ? 535 HOH A O      1 
HETATM 2959 O O      . HOH E 5 .   ? 29.130 15.257 48.572 1.00 22.71 ? 536 HOH A O      1 
HETATM 2960 O O      . HOH E 5 .   ? 8.030  31.057 23.736 1.00 33.23 ? 537 HOH A O      1 
HETATM 2961 O O      . HOH E 5 .   ? 7.505  8.925  13.740 1.00 29.03 ? 538 HOH A O      1 
HETATM 2962 O O      . HOH E 5 .   ? 27.928 6.207  29.715 1.00 24.77 ? 539 HOH A O      1 
HETATM 2963 O O      . HOH E 5 .   ? 14.325 26.364 32.979 1.00 40.59 ? 540 HOH A O      1 
HETATM 2964 O O      . HOH E 5 .   ? 21.808 41.879 9.070  1.00 26.90 ? 541 HOH A O      1 
HETATM 2965 O O      . HOH E 5 .   ? 13.686 26.912 24.308 1.00 17.35 ? 542 HOH A O      1 
HETATM 2966 O O      . HOH E 5 .   ? 14.990 26.807 17.732 1.00 14.98 ? 543 HOH A O      1 
HETATM 2967 O O      . HOH E 5 .   ? 36.131 18.028 30.867 1.00 20.77 ? 544 HOH A O      1 
HETATM 2968 O O      . HOH E 5 .   ? 22.337 13.025 20.136 1.00 13.24 ? 545 HOH A O      1 
HETATM 2969 O O      . HOH E 5 .   ? 46.349 18.919 28.945 1.00 39.75 ? 546 HOH A O      1 
HETATM 2970 O O      . HOH E 5 .   ? 33.179 24.150 3.923  1.00 24.15 ? 547 HOH A O      1 
HETATM 2971 O O      . HOH E 5 .   ? 24.153 45.071 14.329 1.00 29.36 ? 548 HOH A O      1 
HETATM 2972 O O      . HOH E 5 .   ? 10.967 39.084 15.647 1.00 26.41 ? 549 HOH A O      1 
HETATM 2973 O O      . HOH E 5 .   ? 22.524 12.959 -0.374 1.00 21.71 ? 550 HOH A O      1 
HETATM 2974 O O      . HOH E 5 .   ? 11.252 37.610 18.681 1.00 24.39 ? 551 HOH A O      1 
HETATM 2975 O O      . HOH E 5 .   ? 41.188 39.269 35.457 1.00 51.17 ? 552 HOH A O      1 
HETATM 2976 O O      . HOH E 5 .   ? 29.929 35.039 40.153 1.00 23.22 ? 553 HOH A O      1 
HETATM 2977 O O      . HOH E 5 .   ? 6.674  5.181  14.428 1.00 36.96 ? 554 HOH A O      1 
HETATM 2978 O O      . HOH E 5 .   ? 16.373 36.811 36.346 1.00 38.36 ? 555 HOH A O      1 
HETATM 2979 O O      . HOH E 5 .   ? 14.547 17.967 2.727  1.00 27.33 ? 556 HOH A O      1 
HETATM 2980 O O      . HOH E 5 .   ? 10.285 6.926  25.830 1.00 33.99 ? 557 HOH A O      1 
HETATM 2981 O O      . HOH E 5 .   ? 37.996 13.278 6.686  1.00 45.40 ? 558 HOH A O      1 
HETATM 2982 O O      . HOH E 5 .   ? 20.503 12.703 30.103 1.00 16.86 ? 559 HOH A O      1 
HETATM 2983 O O      . HOH E 5 .   ? 6.569  23.032 18.911 1.00 24.74 ? 560 HOH A O      1 
HETATM 2984 O O      . HOH E 5 .   ? 27.676 35.760 8.816  1.00 15.95 ? 561 HOH A O      1 
HETATM 2985 O O      . HOH E 5 .   ? 32.927 18.140 44.562 1.00 37.18 ? 562 HOH A O      1 
HETATM 2986 O O      . HOH E 5 .   ? 13.787 36.480 24.277 1.00 17.93 ? 563 HOH A O      1 
HETATM 2987 O O      . HOH E 5 .   ? 12.360 42.785 27.468 1.00 27.15 ? 564 HOH A O      1 
HETATM 2988 O O      . HOH E 5 .   ? -0.699 21.225 12.116 1.00 13.87 ? 565 HOH A O      1 
HETATM 2989 O O      . HOH E 5 .   ? 8.008  25.353 19.117 1.00 18.10 ? 566 HOH A O      1 
HETATM 2990 O O      . HOH E 5 .   ? 5.332  30.995 1.683  1.00 31.71 ? 567 HOH A O      1 
HETATM 2991 O O      . HOH E 5 .   ? 29.653 23.605 24.765 1.00 12.88 ? 568 HOH A O      1 
HETATM 2992 O O      . HOH E 5 .   ? 17.640 5.187  10.051 1.00 23.98 ? 569 HOH A O      1 
HETATM 2993 O O      . HOH E 5 .   ? 12.651 5.180  19.160 1.00 19.28 ? 570 HOH A O      1 
HETATM 2994 O O      . HOH E 5 .   ? 26.723 27.332 42.547 1.00 19.30 ? 571 HOH A O      1 
HETATM 2995 O O      . HOH E 5 .   ? 27.292 22.845 0.760  1.00 19.54 ? 572 HOH A O      1 
HETATM 2996 O O      . HOH E 5 .   ? 17.497 22.405 5.173  1.00 15.17 ? 573 HOH A O      1 
HETATM 2997 O O      . HOH E 5 .   ? 38.540 18.233 32.367 1.00 29.39 ? 574 HOH A O      1 
HETATM 2998 O O      . HOH E 5 .   ? 29.555 21.303 47.099 1.00 27.55 ? 575 HOH A O      1 
HETATM 2999 O O      . HOH E 5 .   ? 10.650 43.957 4.992  1.00 35.88 ? 576 HOH A O      1 
HETATM 3000 O O      . HOH E 5 .   ? 36.083 14.547 38.592 1.00 28.88 ? 577 HOH A O      1 
HETATM 3001 O O      . HOH E 5 .   ? 5.770  13.887 9.092  1.00 19.39 ? 578 HOH A O      1 
HETATM 3002 O O      . HOH E 5 .   ? 30.953 8.020  26.850 1.00 22.60 ? 579 HOH A O      1 
HETATM 3003 O O      . HOH E 5 .   ? 22.624 16.329 30.886 1.00 18.25 ? 580 HOH A O      1 
HETATM 3004 O O      . HOH E 5 .   ? 18.906 16.704 15.532 1.00 13.35 ? 581 HOH A O      1 
HETATM 3005 O O      . HOH E 5 .   ? 24.512 40.109 36.082 1.00 27.49 ? 582 HOH A O      1 
HETATM 3006 O O      . HOH E 5 .   ? 31.193 12.294 29.526 1.00 15.17 ? 583 HOH A O      1 
HETATM 3007 O O      . HOH E 5 .   ? 15.077 39.516 17.350 1.00 23.50 ? 584 HOH A O      1 
HETATM 3008 O O      . HOH E 5 .   ? 23.443 15.326 21.210 1.00 12.38 ? 585 HOH A O      1 
HETATM 3009 O O      . HOH E 5 .   ? 16.252 25.134 -1.314 1.00 37.53 ? 586 HOH A O      1 
HETATM 3010 O O      . HOH E 5 .   ? 48.915 18.515 32.705 1.00 18.73 ? 587 HOH A O      1 
HETATM 3011 O O      . HOH E 5 .   ? 29.910 13.559 42.820 1.00 20.57 ? 588 HOH A O      1 
HETATM 3012 O O      . HOH E 5 .   ? 18.550 39.870 7.122  1.00 16.71 ? 589 HOH A O      1 
HETATM 3013 O O      . HOH E 5 .   ? 14.666 -0.163 19.346 1.00 30.59 ? 590 HOH A O      1 
HETATM 3014 O O      . HOH E 5 .   ? 41.864 30.008 40.655 1.00 19.76 ? 591 HOH A O      1 
HETATM 3015 O O      . HOH E 5 .   ? 40.752 5.024  15.081 1.00 36.42 ? 592 HOH A O      1 
HETATM 3016 O O      . HOH E 5 .   ? 36.592 18.592 28.275 1.00 17.38 ? 593 HOH A O      1 
HETATM 3017 O O      . HOH E 5 .   ? 35.566 38.972 29.703 1.00 26.09 ? 594 HOH A O      1 
HETATM 3018 O O      . HOH E 5 .   ? 33.224 15.414 4.306  1.00 29.50 ? 595 HOH A O      1 
HETATM 3019 O O      . HOH E 5 .   ? 23.871 11.058 41.620 1.00 27.53 ? 596 HOH A O      1 
HETATM 3020 O O      . HOH E 5 .   ? 23.722 31.305 27.835 1.00 14.36 ? 597 HOH A O      1 
HETATM 3021 O O      . HOH E 5 .   ? 20.149 13.602 15.406 1.00 16.22 ? 598 HOH A O      1 
HETATM 3022 O O      . HOH E 5 .   ? 40.910 11.445 21.436 1.00 35.74 ? 599 HOH A O      1 
HETATM 3023 O O      . HOH E 5 .   ? 20.016 29.554 40.290 1.00 37.54 ? 600 HOH A O      1 
HETATM 3024 O O      . HOH E 5 .   ? 7.676  25.976 16.519 1.00 18.00 ? 601 HOH A O      1 
HETATM 3025 O O      . HOH E 5 .   ? 42.211 17.557 36.640 1.00 32.58 ? 602 HOH A O      1 
HETATM 3026 O O      . HOH E 5 .   ? 24.754 45.862 30.876 1.00 19.85 ? 603 HOH A O      1 
HETATM 3027 O O      . HOH E 5 .   ? 16.180 26.557 23.409 1.00 13.27 ? 604 HOH A O      1 
HETATM 3028 O O      . HOH E 5 .   ? 31.748 32.238 30.278 1.00 13.74 ? 605 HOH A O      1 
HETATM 3029 O O      . HOH E 5 .   ? 31.110 34.823 42.724 1.00 29.29 ? 606 HOH A O      1 
HETATM 3030 O O      . HOH E 5 .   ? 16.713 32.210 -2.619 1.00 33.77 ? 607 HOH A O      1 
HETATM 3031 O O      . HOH E 5 .   ? 32.072 32.454 -0.561 1.00 26.94 ? 608 HOH A O      1 
HETATM 3032 O O      . HOH E 5 .   ? 18.221 38.647 0.080  1.00 32.79 ? 609 HOH A O      1 
HETATM 3033 O O      . HOH E 5 .   ? 18.906 15.950 40.739 1.00 16.90 ? 610 HOH A O      1 
HETATM 3034 O O      . HOH E 5 .   ? 15.264 14.720 32.658 1.00 35.77 ? 611 HOH A O      1 
HETATM 3035 O O      . HOH E 5 .   ? 35.403 6.660  19.027 1.00 24.49 ? 612 HOH A O      1 
HETATM 3036 O O      . HOH E 5 .   ? 29.807 23.261 1.749  1.00 22.40 ? 613 HOH A O      1 
HETATM 3037 O O      . HOH E 5 .   ? 32.506 31.000 6.211  1.00 32.86 ? 614 HOH A O      1 
HETATM 3038 O O      . HOH E 5 .   ? 7.866  29.423 27.481 1.00 35.67 ? 615 HOH A O      1 
HETATM 3039 O O      . HOH E 5 .   ? 33.834 1.088  17.542 1.00 40.47 ? 616 HOH A O      1 
HETATM 3040 O O      . HOH E 5 .   ? 25.248 39.161 4.688  1.00 34.11 ? 617 HOH A O      1 
HETATM 3041 O O      . HOH E 5 .   ? 16.252 1.784  37.016 1.00 32.68 ? 618 HOH A O      1 
HETATM 3042 O O      . HOH E 5 .   ? 43.640 32.037 39.796 1.00 21.08 ? 619 HOH A O      1 
HETATM 3043 O O      . HOH E 5 .   ? 12.010 28.232 17.141 1.00 13.23 ? 620 HOH A O      1 
HETATM 3044 O O      . HOH E 5 .   ? 22.673 6.488  6.190  1.00 31.20 ? 621 HOH A O      1 
HETATM 3045 O O      . HOH E 5 .   ? 31.757 9.918  41.360 1.00 38.97 ? 622 HOH A O      1 
HETATM 3046 O O      . HOH E 5 .   ? 28.195 37.314 12.281 1.00 15.01 ? 623 HOH A O      1 
HETATM 3047 O O      . HOH E 5 .   ? 38.178 14.581 29.289 1.00 26.06 ? 624 HOH A O      1 
HETATM 3048 O O      . HOH E 5 .   ? 41.064 21.433 38.499 1.00 19.34 ? 625 HOH A O      1 
HETATM 3049 O O      . HOH E 5 .   ? 27.110 21.197 -1.427 1.00 20.06 ? 626 HOH A O      1 
HETATM 3050 O O      . HOH E 5 .   ? 16.150 40.637 8.633  1.00 19.13 ? 627 HOH A O      1 
HETATM 3051 O O      . HOH E 5 .   ? 12.890 0.307  13.664 1.00 19.24 ? 628 HOH A O      1 
HETATM 3052 O O      . HOH E 5 .   ? 12.957 12.846 14.008 1.00 12.38 ? 629 HOH A O      1 
HETATM 3053 O O      . HOH E 5 .   ? 44.702 25.899 12.563 1.00 27.99 ? 630 HOH A O      1 
HETATM 3054 O O      . HOH E 5 .   ? 0.288  18.659 5.608  1.00 32.91 ? 631 HOH A O      1 
HETATM 3055 O O      . HOH E 5 .   ? 2.450  32.921 15.132 1.00 34.87 ? 632 HOH A O      1 
HETATM 3056 O O      . HOH E 5 .   ? 44.522 18.797 35.059 1.00 30.46 ? 633 HOH A O      1 
HETATM 3057 O O      . HOH E 5 .   ? 18.855 2.173  25.000 1.00 19.20 ? 634 HOH A O      1 
HETATM 3058 O O      . HOH E 5 .   ? 31.698 16.924 1.861  1.00 28.68 ? 635 HOH A O      1 
HETATM 3059 O O      . HOH E 5 .   ? 17.708 24.238 7.112  1.00 13.87 ? 636 HOH A O      1 
HETATM 3060 O O      . HOH E 5 .   ? 21.982 21.917 44.894 1.00 37.55 ? 637 HOH A O      1 
HETATM 3061 O O      . HOH E 5 .   ? 26.184 39.138 40.241 1.00 27.08 ? 638 HOH A O      1 
HETATM 3062 O O      . HOH E 5 .   ? 13.874 9.068  3.770  1.00 36.42 ? 639 HOH A O      1 
HETATM 3063 O O      . HOH E 5 .   ? 10.876 36.689 20.987 1.00 20.99 ? 640 HOH A O      1 
HETATM 3064 O O      . HOH E 5 .   ? 26.889 44.961 24.278 1.00 22.03 ? 641 HOH A O      1 
HETATM 3065 O O      . HOH E 5 .   ? 34.980 8.251  6.325  1.00 23.31 ? 642 HOH A O      1 
HETATM 3066 O O      . HOH E 5 .   ? 35.828 4.574  11.350 1.00 40.47 ? 643 HOH A O      1 
HETATM 3067 O O      . HOH E 5 .   ? 21.374 11.052 17.302 1.00 14.45 ? 644 HOH A O      1 
HETATM 3068 O O      . HOH E 5 .   ? 28.487 37.433 40.390 1.00 24.17 ? 645 HOH A O      1 
HETATM 3069 O O      . HOH E 5 .   ? 8.405  17.584 0.417  1.00 26.40 ? 646 HOH A O      1 
HETATM 3070 O O      . HOH E 5 .   ? 39.904 16.169 28.109 1.00 31.50 ? 647 HOH A O      1 
HETATM 3071 O O      . HOH E 5 .   ? 2.841  25.812 7.415  1.00 24.33 ? 648 HOH A O      1 
HETATM 3072 O O      . HOH E 5 .   ? 23.690 42.153 10.825 1.00 28.08 ? 649 HOH A O      1 
HETATM 3073 O O      . HOH E 5 .   ? 9.603  18.464 25.530 1.00 34.09 ? 650 HOH A O      1 
HETATM 3074 O O      . HOH E 5 .   ? 11.564 11.691 9.341  1.00 15.55 ? 651 HOH A O      1 
HETATM 3075 O O      . HOH E 5 .   ? 25.119 18.667 39.269 1.00 13.49 ? 652 HOH A O      1 
HETATM 3076 O O      . HOH E 5 .   ? 43.984 26.611 26.191 1.00 18.86 ? 653 HOH A O      1 
HETATM 3077 O O      . HOH E 5 .   ? 27.575 28.966 46.492 1.00 19.88 ? 654 HOH A O      1 
HETATM 3078 O O      . HOH E 5 .   ? 32.868 43.367 15.621 1.00 19.97 ? 655 HOH A O      1 
HETATM 3079 O O      . HOH E 5 .   ? 17.271 33.714 26.340 1.00 23.34 ? 656 HOH A O      1 
HETATM 3080 O O      . HOH E 5 .   ? 28.347 35.624 -2.626 1.00 38.62 ? 657 HOH A O      1 
HETATM 3081 O O      . HOH E 5 .   ? 28.148 16.323 25.379 1.00 13.54 ? 658 HOH A O      1 
HETATM 3082 O O      . HOH E 5 .   ? 9.931  24.205 16.004 1.00 13.52 ? 659 HOH A O      1 
HETATM 3083 O O      . HOH E 5 .   ? 43.534 26.175 23.409 1.00 21.67 ? 660 HOH A O      1 
HETATM 3084 O O      . HOH E 5 .   ? 13.571 20.511 5.198  1.00 15.55 ? 661 HOH A O      1 
HETATM 3085 O O      . HOH E 5 .   ? 19.894 19.216 14.826 1.00 12.48 ? 662 HOH A O      1 
HETATM 3086 O O      . HOH E 5 .   ? 17.418 10.102 3.892  1.00 38.71 ? 663 HOH A O      1 
HETATM 3087 O O      . HOH E 5 .   ? 3.253  12.876 13.097 1.00 18.09 ? 664 HOH A O      1 
HETATM 3088 O O      . HOH E 5 .   ? 30.724 32.998 7.548  1.00 30.04 ? 665 HOH A O      1 
HETATM 3089 O O      . HOH E 5 .   ? 30.998 25.754 45.042 1.00 19.59 ? 666 HOH A O      1 
HETATM 3090 O O      . HOH E 5 .   ? 41.963 17.415 13.266 1.00 30.68 ? 667 HOH A O      1 
HETATM 3091 O O      . HOH E 5 .   ? 20.882 46.946 21.976 1.00 16.83 ? 668 HOH A O      1 
HETATM 3092 O O      . HOH E 5 .   ? 6.114  26.445 20.809 1.00 25.56 ? 669 HOH A O      1 
HETATM 3093 O O      . HOH E 5 .   ? 26.839 10.308 39.831 1.00 24.40 ? 670 HOH A O      1 
HETATM 3094 O O      . HOH E 5 .   ? 17.322 5.145  26.859 1.00 30.48 ? 671 HOH A O      1 
HETATM 3095 O O      . HOH E 5 .   ? 31.020 5.273  34.603 1.00 33.69 ? 672 HOH A O      1 
HETATM 3096 O O      . HOH E 5 .   ? 7.507  7.914  17.664 1.00 24.66 ? 673 HOH A O      1 
HETATM 3097 O O      . HOH E 5 .   ? 42.060 29.466 29.165 1.00 23.06 ? 674 HOH A O      1 
HETATM 3098 O O      . HOH E 5 .   ? 4.471  10.811 2.398  1.00 37.36 ? 675 HOH A O      1 
HETATM 3099 O O      . HOH E 5 .   ? 12.587 40.258 18.422 1.00 22.75 ? 676 HOH A O      1 
HETATM 3100 O O      . HOH E 5 .   ? -1.056 17.218 9.610  1.00 15.89 ? 677 HOH A O      1 
HETATM 3101 O O      . HOH E 5 .   ? 39.046 37.452 42.526 1.00 40.16 ? 678 HOH A O      1 
HETATM 3102 O O      . HOH E 5 .   ? 19.807 22.012 4.673  1.00 34.52 ? 679 HOH A O      1 
HETATM 3103 O O      . HOH E 5 .   ? 41.324 8.730  10.547 1.00 36.62 ? 680 HOH A O      1 
HETATM 3104 O O      . HOH E 5 .   ? 35.785 21.343 6.410  1.00 22.70 ? 681 HOH A O      1 
HETATM 3105 O O      . HOH E 5 .   ? 28.675 3.595  32.399 1.00 22.41 ? 682 HOH A O      1 
HETATM 3106 O O      . HOH E 5 .   ? 41.449 20.325 10.574 1.00 20.61 ? 683 HOH A O      1 
HETATM 3107 O O      . HOH E 5 .   ? 33.809 21.030 3.603  1.00 36.90 ? 684 HOH A O      1 
HETATM 3108 O O      . HOH E 5 .   ? 32.961 48.026 24.911 1.00 39.55 ? 685 HOH A O      1 
HETATM 3109 O O      . HOH E 5 .   ? 41.744 30.996 24.262 1.00 19.59 ? 686 HOH A O      1 
HETATM 3110 O O      . HOH E 5 .   ? 32.955 45.269 21.778 1.00 44.39 ? 687 HOH A O      1 
HETATM 3111 O O      . HOH E 5 .   ? 33.297 8.950  27.687 1.00 22.69 ? 688 HOH A O      1 
HETATM 3112 O O      . HOH E 5 .   ? 28.626 9.060  2.806  1.00 23.92 ? 689 HOH A O      1 
HETATM 3113 O O      . HOH E 5 .   ? 8.817  2.971  11.348 1.00 30.61 ? 690 HOH A O      1 
HETATM 3114 O O      . HOH E 5 .   ? 34.205 32.795 32.979 1.00 13.26 ? 691 HOH A O      1 
HETATM 3115 O O      . HOH E 5 .   ? 18.511 34.097 33.457 1.00 23.26 ? 692 HOH A O      1 
HETATM 3116 O O      . HOH E 5 .   ? 39.514 16.575 23.068 1.00 28.73 ? 693 HOH A O      1 
HETATM 3117 O O      . HOH E 5 .   ? 23.121 48.471 15.813 1.00 21.56 ? 694 HOH A O      1 
HETATM 3118 O O      . HOH E 5 .   ? 23.541 23.760 35.558 1.00 12.14 ? 695 HOH A O      1 
HETATM 3119 O O      . HOH E 5 .   ? 41.926 32.712 12.686 1.00 38.30 ? 696 HOH A O      1 
HETATM 3120 O O      . HOH E 5 .   ? 16.468 47.619 22.132 1.00 25.95 ? 697 HOH A O      1 
HETATM 3121 O O      . HOH E 5 .   ? 2.900  16.115 20.692 1.00 27.25 ? 698 HOH A O      1 
HETATM 3122 O O      . HOH E 5 .   ? 8.613  43.810 21.798 1.00 38.14 ? 699 HOH A O      1 
HETATM 3123 O O      . HOH E 5 .   ? 47.493 26.849 30.992 1.00 15.25 ? 700 HOH A O      1 
HETATM 3124 O O      . HOH E 5 .   ? 18.724 14.612 30.968 1.00 18.97 ? 701 HOH A O      1 
HETATM 3125 O O      . HOH E 5 .   ? 0.996  16.238 6.498  1.00 32.13 ? 702 HOH A O      1 
HETATM 3126 O O      . HOH E 5 .   ? 12.141 46.123 8.092  1.00 38.15 ? 703 HOH A O      1 
HETATM 3127 O O      . HOH E 5 .   ? 22.884 26.577 40.716 1.00 35.56 ? 704 HOH A O      1 
HETATM 3128 O O      . HOH E 5 .   ? 41.627 25.212 10.198 1.00 31.49 ? 705 HOH A O      1 
HETATM 3129 O O      . HOH E 5 .   ? 33.830 29.695 45.684 1.00 37.10 ? 706 HOH A O      1 
HETATM 3130 O O      . HOH E 5 .   ? 20.232 46.226 14.166 1.00 31.66 ? 707 HOH A O      1 
HETATM 3131 O O      . HOH E 5 .   ? 22.771 41.156 14.787 1.00 14.08 ? 708 HOH A O      1 
HETATM 3132 O O      . HOH E 5 .   ? 15.992 7.575  26.424 1.00 20.70 ? 709 HOH A O      1 
HETATM 3133 O O      . HOH E 5 .   ? 17.863 15.067 45.917 1.00 37.91 ? 710 HOH A O      1 
HETATM 3134 O O      . HOH E 5 .   ? 28.224 7.616  9.674  1.00 22.81 ? 711 HOH A O      1 
HETATM 3135 O O      . HOH E 5 .   ? 42.589 33.848 31.831 1.00 31.39 ? 712 HOH A O      1 
HETATM 3136 O O      . HOH E 5 .   ? 33.136 6.871  20.884 1.00 20.25 ? 713 HOH A O      1 
HETATM 3137 O O      . HOH E 5 .   ? 39.471 44.941 12.705 1.00 42.15 ? 714 HOH A O      1 
HETATM 3138 O O      . HOH E 5 .   ? 20.705 3.146  26.636 1.00 16.25 ? 715 HOH A O      1 
HETATM 3139 O O      . HOH E 5 .   ? 36.934 30.354 43.335 1.00 29.66 ? 716 HOH A O      1 
HETATM 3140 O O      . HOH E 5 .   ? 34.654 14.573 34.804 1.00 25.87 ? 717 HOH A O      1 
HETATM 3141 O O      . HOH E 5 .   ? 28.945 8.892  28.541 1.00 19.08 ? 718 HOH A O      1 
HETATM 3142 O O      . HOH E 5 .   ? 28.430 24.384 27.482 1.00 13.50 ? 719 HOH A O      1 
HETATM 3143 O O      . HOH E 5 .   ? 27.158 9.336  26.489 1.00 14.99 ? 720 HOH A O      1 
HETATM 3144 O O      . HOH E 5 .   ? 10.209 9.286  6.426  1.00 27.27 ? 721 HOH A O      1 
HETATM 3145 O O      . HOH E 5 .   ? 25.676 2.647  11.713 1.00 26.24 ? 722 HOH A O      1 
HETATM 3146 O O      . HOH E 5 .   ? 39.395 20.378 40.609 1.00 25.85 ? 723 HOH A O      1 
HETATM 3147 O O      . HOH E 5 .   ? 31.422 17.120 33.170 1.00 13.68 ? 724 HOH A O      1 
HETATM 3148 O O      . HOH E 5 .   ? 24.332 25.891 42.250 1.00 34.53 ? 725 HOH A O      1 
HETATM 3149 O O      . HOH E 5 .   ? 24.853 42.938 35.342 1.00 22.83 ? 726 HOH A O      1 
HETATM 3150 O O      . HOH E 5 .   ? 39.370 34.682 11.833 1.00 22.24 ? 727 HOH A O      1 
HETATM 3151 O O      . HOH E 5 .   ? 12.562 10.166 24.668 1.00 17.95 ? 728 HOH A O      1 
HETATM 3152 O O      . HOH E 5 .   ? 3.595  27.851 11.901 1.00 23.21 ? 729 HOH A O      1 
HETATM 3153 O O      . HOH E 5 .   ? 11.156 13.009 26.079 1.00 35.02 ? 730 HOH A O      1 
HETATM 3154 O O      . HOH E 5 .   ? 8.161  36.774 21.900 1.00 31.64 ? 731 HOH A O      1 
HETATM 3155 O O      . HOH E 5 .   ? 8.486  37.710 15.166 1.00 25.38 ? 732 HOH A O      1 
HETATM 3156 O O      . HOH E 5 .   ? 2.384  30.590 11.657 1.00 23.82 ? 733 HOH A O      1 
HETATM 3157 O O      . HOH E 5 .   ? 12.520 7.581  36.888 1.00 29.41 ? 734 HOH A O      1 
HETATM 3158 O O      . HOH E 5 .   ? 13.642 5.300  7.669  1.00 32.53 ? 735 HOH A O      1 
HETATM 3159 O O      . HOH E 5 .   ? 20.690 4.256  16.572 1.00 15.29 ? 736 HOH A O      1 
HETATM 3160 O O      . HOH E 5 .   ? 33.223 27.763 42.526 1.00 18.59 ? 737 HOH A O      1 
HETATM 3161 O O      . HOH E 5 .   ? 38.084 30.038 7.794  1.00 27.50 ? 738 HOH A O      1 
HETATM 3162 O O      . HOH E 5 .   ? 30.790 32.683 46.367 1.00 21.45 ? 739 HOH A O      1 
HETATM 3163 O O      . HOH E 5 .   ? 32.947 43.545 34.520 1.00 18.34 ? 740 HOH A O      1 
HETATM 3164 O O      . HOH E 5 .   ? 12.284 8.147  29.529 1.00 47.09 ? 741 HOH A O      1 
HETATM 3165 O O      . HOH E 5 .   ? 39.991 18.999 29.905 1.00 34.95 ? 742 HOH A O      1 
HETATM 3166 O O      . HOH E 5 .   ? 22.918 33.269 -1.193 1.00 22.92 ? 743 HOH A O      1 
HETATM 3167 O O      . HOH E 5 .   ? 43.708 28.509 18.927 1.00 40.06 ? 744 HOH A O      1 
HETATM 3168 O O      . HOH E 5 .   ? 33.197 7.249  23.629 1.00 23.21 ? 745 HOH A O      1 
HETATM 3169 O O      . HOH E 5 .   ? 5.137  28.219 18.791 1.00 26.85 ? 746 HOH A O      1 
HETATM 3170 O O      . HOH E 5 .   ? 26.361 6.798  26.042 1.00 16.71 ? 747 HOH A O      1 
HETATM 3171 O O      . HOH E 5 .   ? 45.039 15.857 14.464 1.00 37.55 ? 748 HOH A O      1 
HETATM 3172 O O      . HOH E 5 .   ? 30.585 45.900 11.910 1.00 38.12 ? 749 HOH A O      1 
HETATM 3173 O O      . HOH E 5 .   ? 43.935 32.544 20.425 1.00 40.67 ? 750 HOH A O      1 
HETATM 3174 O O      . HOH E 5 .   ? 42.293 17.990 16.577 1.00 23.73 ? 751 HOH A O      1 
HETATM 3175 O O      . HOH E 5 .   ? 24.648 34.939 -0.621 1.00 29.09 ? 752 HOH A O      1 
HETATM 3176 O O      . HOH E 5 .   ? 26.383 26.081 28.322 1.00 12.09 ? 753 HOH A O      1 
HETATM 3177 O O      . HOH E 5 .   ? 19.100 40.478 4.422  1.00 32.12 ? 754 HOH A O      1 
HETATM 3178 O O      . HOH E 5 .   ? 27.499 45.835 21.819 1.00 26.77 ? 755 HOH A O      1 
HETATM 3179 O O      . HOH E 5 .   ? 18.922 28.078 6.054  1.00 13.76 ? 756 HOH A O      1 
HETATM 3180 O O      . HOH E 5 .   ? 19.202 19.295 -3.466 1.00 27.52 ? 757 HOH A O      1 
HETATM 3181 O O      . HOH E 5 .   ? 33.731 43.346 12.868 1.00 41.93 ? 758 HOH A O      1 
HETATM 3182 O O      . HOH E 5 .   ? 25.803 15.178 26.451 1.00 12.61 ? 759 HOH A O      1 
HETATM 3183 O O      . HOH E 5 .   ? 40.564 15.398 20.231 1.00 33.28 ? 760 HOH A O      1 
HETATM 3184 O O      . HOH E 5 .   ? 15.304 3.205  23.026 1.00 26.15 ? 761 HOH A O      1 
HETATM 3185 O O      . HOH E 5 .   ? 4.447  28.659 -2.144 1.00 41.20 ? 762 HOH A O      1 
HETATM 3186 O O      . HOH E 5 .   ? 3.136  14.133 5.655  1.00 28.57 ? 763 HOH A O      1 
HETATM 3187 O O      . HOH E 5 .   ? 27.942 28.647 -0.192 1.00 23.05 ? 764 HOH A O      1 
HETATM 3188 O O      . HOH E 5 .   ? 37.816 38.036 28.301 1.00 29.51 ? 765 HOH A O      1 
HETATM 3189 O O      . HOH E 5 .   ? 7.448  10.072 3.261  1.00 26.11 ? 766 HOH A O      1 
HETATM 3190 O O      . HOH E 5 .   ? 29.665 43.116 37.001 1.00 18.04 ? 767 HOH A O      1 
HETATM 3191 O O      . HOH E 5 .   ? 41.523 8.951  17.847 1.00 26.93 ? 768 HOH A O      1 
HETATM 3192 O O      . HOH E 5 .   ? 40.194 37.097 22.856 1.00 29.07 ? 769 HOH A O      1 
HETATM 3193 O O      . HOH E 5 .   ? 16.557 20.976 -1.776 1.00 29.88 ? 770 HOH A O      1 
HETATM 3194 O O      . HOH E 5 .   ? 46.202 23.832 28.773 1.00 33.53 ? 771 HOH A O      1 
HETATM 3195 O O      . HOH E 5 .   ? 39.183 26.145 8.649  1.00 26.20 ? 772 HOH A O      1 
HETATM 3196 O O      . HOH E 5 .   ? 22.347 3.310  12.180 1.00 17.76 ? 773 HOH A O      1 
HETATM 3197 O O      . HOH E 5 .   ? 19.618 3.976  36.227 1.00 39.68 ? 774 HOH A O      1 
HETATM 3198 O O      . HOH E 5 .   ? 36.346 37.600 41.541 1.00 27.25 ? 775 HOH A O      1 
HETATM 3199 O O      . HOH E 5 .   ? 39.324 39.311 39.237 1.00 35.97 ? 776 HOH A O      1 
HETATM 3200 O O      . HOH E 5 .   ? 26.483 44.573 29.600 1.00 25.06 ? 777 HOH A O      1 
HETATM 3201 O O      . HOH E 5 .   ? 18.125 45.281 11.332 1.00 41.84 ? 778 HOH A O      1 
HETATM 3202 O O      . HOH E 5 .   ? 23.034 38.755 2.677  1.00 24.95 ? 779 HOH A O      1 
HETATM 3203 O O      . HOH E 5 .   ? 3.952  37.067 9.253  1.00 41.76 ? 780 HOH A O      1 
HETATM 3204 O O      . HOH E 5 .   ? 44.853 27.555 17.027 1.00 29.42 ? 781 HOH A O      1 
HETATM 3205 O O      . HOH E 5 .   ? 27.647 13.542 44.532 1.00 20.60 ? 782 HOH A O      1 
HETATM 3206 O O      . HOH E 5 .   ? 12.059 20.869 2.886  1.00 15.71 ? 783 HOH A O      1 
HETATM 3207 O O      . HOH E 5 .   ? 43.098 19.269 26.742 1.00 34.89 ? 784 HOH A O      1 
HETATM 3208 O O      . HOH E 5 .   ? 15.275 18.743 48.765 1.00 38.46 ? 785 HOH A O      1 
HETATM 3209 O O      . HOH E 5 .   ? 4.069  20.656 22.298 1.00 38.99 ? 786 HOH A O      1 
HETATM 3210 O O      . HOH E 5 .   ? 16.872 41.397 31.841 1.00 26.35 ? 787 HOH A O      1 
HETATM 3211 O O      . HOH E 5 .   ? 34.884 40.085 40.365 1.00 22.51 ? 788 HOH A O      1 
HETATM 3212 O O      . HOH E 5 .   ? 31.241 35.697 8.703  1.00 26.63 ? 789 HOH A O      1 
HETATM 3213 O O      . HOH E 5 .   ? -0.098 23.396 10.602 1.00 21.58 ? 790 HOH A O      1 
HETATM 3214 O O      . HOH E 5 .   ? 35.351 20.945 43.959 1.00 29.37 ? 791 HOH A O      1 
HETATM 3215 O O      . HOH E 5 .   ? 28.639 1.399  16.867 1.00 37.91 ? 792 HOH A O      1 
HETATM 3216 O O      . HOH E 5 .   ? 39.796 6.689  17.074 1.00 22.13 ? 793 HOH A O      1 
HETATM 3217 O O      . HOH E 5 .   ? 7.294  15.392 -0.832 1.00 33.57 ? 794 HOH A O      1 
HETATM 3218 O O      . HOH E 5 .   ? 39.911 36.116 28.377 1.00 43.79 ? 795 HOH A O      1 
HETATM 3219 O O      . HOH E 5 .   ? 23.319 24.619 -2.925 1.00 38.17 ? 796 HOH A O      1 
HETATM 3220 O O      . HOH E 5 .   ? 31.329 6.043  40.593 1.00 45.32 ? 797 HOH A O      1 
HETATM 3221 O O      . HOH E 5 .   ? 30.565 46.710 20.743 1.00 34.88 ? 798 HOH A O      1 
HETATM 3222 O O      . HOH E 5 .   ? 11.345 49.306 25.123 1.00 28.94 ? 799 HOH A O      1 
HETATM 3223 O O      . HOH E 5 .   ? 41.361 13.163 17.677 1.00 29.04 ? 800 HOH A O      1 
HETATM 3224 O O      . HOH E 5 .   ? 34.237 36.741 42.905 1.00 36.80 ? 801 HOH A O      1 
HETATM 3225 O O      . HOH E 5 .   ? 0.501  16.633 27.475 1.00 26.64 ? 802 HOH A O      1 
HETATM 3226 O O      . HOH E 5 .   ? 13.345 37.668 16.215 1.00 27.97 ? 803 HOH A O      1 
HETATM 3227 O O      . HOH E 5 .   ? 35.888 42.428 11.977 1.00 34.21 ? 804 HOH A O      1 
HETATM 3228 O O      . HOH E 5 .   ? 18.619 48.108 20.923 1.00 17.26 ? 805 HOH A O      1 
HETATM 3229 O O      . HOH E 5 .   ? 20.905 8.776  40.437 1.00 26.96 ? 806 HOH A O      1 
HETATM 3230 O O      . HOH E 5 .   ? 1.656  31.038 8.852  1.00 32.79 ? 807 HOH A O      1 
HETATM 3231 O O      . HOH E 5 .   ? 22.349 24.785 41.796 1.00 34.63 ? 808 HOH A O      1 
HETATM 3232 O O      . HOH E 5 .   ? 31.099 19.885 48.868 1.00 33.91 ? 809 HOH A O      1 
HETATM 3233 O O      . HOH E 5 .   ? 28.180 4.720  25.383 1.00 26.88 ? 810 HOH A O      1 
HETATM 3234 O O      . HOH E 5 .   ? 8.266  19.664 23.986 1.00 38.10 ? 811 HOH A O      1 
HETATM 3235 O O      . HOH E 5 .   ? 46.829 23.191 15.536 1.00 39.74 ? 812 HOH A O      1 
HETATM 3236 O O      . HOH E 5 .   ? 32.853 49.070 16.878 1.00 38.92 ? 813 HOH A O      1 
HETATM 3237 O O      . HOH E 5 .   ? 25.626 9.067  5.811  1.00 27.23 ? 814 HOH A O      1 
HETATM 3238 O O      . HOH E 5 .   ? -0.410 11.587 21.910 1.00 37.57 ? 815 HOH A O      1 
HETATM 3239 O O      . HOH E 5 .   ? 20.999 42.860 40.667 1.00 35.69 ? 816 HOH A O      1 
HETATM 3240 O O      . HOH E 5 .   ? 39.719 10.486 10.777 1.00 33.54 ? 817 HOH A O      1 
HETATM 3241 O O      . HOH E 5 .   ? 8.152  34.555 23.231 1.00 41.79 ? 818 HOH A O      1 
HETATM 3242 O O      . HOH E 5 .   ? 7.589  32.416 20.585 1.00 43.05 ? 819 HOH A O      1 
HETATM 3243 O O      . HOH E 5 .   ? 21.947 47.261 34.514 1.00 20.92 ? 820 HOH A O      1 
HETATM 3244 O O      . HOH E 5 .   ? 20.240 45.931 38.493 1.00 37.40 ? 821 HOH A O      1 
HETATM 3245 O O      . HOH E 5 .   ? 37.275 14.695 34.993 1.00 30.71 ? 822 HOH A O      1 
HETATM 3246 O O      . HOH E 5 .   ? 3.945  12.322 10.645 1.00 29.81 ? 823 HOH A O      1 
HETATM 3247 O O      . HOH E 5 .   ? 8.919  33.714 19.103 1.00 37.23 ? 824 HOH A O      1 
HETATM 3248 O O      . HOH E 5 .   ? 16.086 3.476  27.883 1.00 35.04 ? 825 HOH A O      1 
HETATM 3249 O O      . HOH E 5 .   ? 42.521 35.203 15.878 1.00 45.20 ? 826 HOH A O      1 
HETATM 3250 O O      . HOH E 5 .   ? 27.776 45.582 27.006 1.00 26.89 ? 827 HOH A O      1 
HETATM 3251 O O      . HOH E 5 .   ? 19.616 31.505 -3.696 1.00 43.64 ? 828 HOH A O      1 
HETATM 3252 O O      . HOH E 5 .   ? 7.078  7.003  15.369 1.00 47.06 ? 829 HOH A O      1 
HETATM 3253 O O      . HOH E 5 .   ? 2.651  10.884 15.061 1.00 28.97 ? 830 HOH A O      1 
HETATM 3254 O O      . HOH E 5 .   ? 35.461 41.528 29.559 1.00 40.10 ? 831 HOH A O      1 
HETATM 3255 O O      . HOH E 5 .   ? 32.854 34.535 0.064  1.00 43.28 ? 832 HOH A O      1 
HETATM 3256 O O      . HOH E 5 .   ? 20.314 16.781 -4.327 1.00 23.34 ? 833 HOH A O      1 
HETATM 3257 O O      . HOH E 5 .   ? 15.053 4.271  25.572 1.00 40.06 ? 834 HOH A O      1 
HETATM 3258 O O      . HOH E 5 .   ? 11.182 5.344  7.366  1.00 45.56 ? 835 HOH A O      1 
HETATM 3259 O O      . HOH E 5 .   ? 23.063 8.973  42.127 1.00 43.22 ? 836 HOH A O      1 
HETATM 3260 O O      . HOH E 5 .   ? 46.391 21.214 28.525 1.00 44.48 ? 837 HOH A O      1 
HETATM 3261 O O      . HOH E 5 .   ? 25.280 44.052 11.649 1.00 35.24 ? 838 HOH A O      1 
HETATM 3262 O O      . HOH E 5 .   ? 30.662 40.832 41.402 1.00 42.03 ? 839 HOH A O      1 
HETATM 3263 O O      . HOH E 5 .   ? 32.986 48.047 29.196 1.00 26.37 ? 840 HOH A O      1 
HETATM 3264 O O      . HOH E 5 .   ? 27.891 44.315 11.298 1.00 38.33 ? 841 HOH A O      1 
HETATM 3265 O O      . HOH E 5 .   ? 14.159 47.220 9.251  1.00 44.83 ? 842 HOH A O      1 
HETATM 3266 O O      . HOH E 5 .   ? 18.017 43.175 8.540  1.00 42.63 ? 843 HOH A O      1 
HETATM 3267 O O      . HOH E 5 .   ? 40.592 37.542 40.982 1.00 43.40 ? 844 HOH A O      1 
HETATM 3268 O O      . HOH E 5 .   ? 27.191 11.534 -0.824 1.00 29.77 ? 845 HOH A O      1 
HETATM 3269 O O      . HOH E 5 .   ? 32.111 21.450 1.176  1.00 38.53 ? 846 HOH A O      1 
HETATM 3270 O O      . HOH E 5 .   ? 32.933 40.834 42.018 1.00 44.70 ? 847 HOH A O      1 
HETATM 3271 O O      . HOH E 5 .   ? 9.149  5.171  23.971 1.00 43.95 ? 848 HOH A O      1 
HETATM 3272 O O      . HOH E 5 .   ? 13.943 13.332 29.629 1.00 38.93 ? 849 HOH A O      1 
HETATM 3273 O O      . HOH E 5 .   ? 40.343 35.264 24.588 1.00 31.38 ? 850 HOH A O      1 
HETATM 3274 O O      . HOH E 5 .   ? 39.081 25.131 6.266  1.00 33.97 ? 851 HOH A O      1 
HETATM 3275 O O      . HOH E 5 .   ? 21.933 44.577 13.290 1.00 38.44 ? 852 HOH A O      1 
HETATM 3276 O O      . HOH E 5 .   ? 36.422 42.022 39.475 1.00 36.37 ? 853 HOH A O      1 
HETATM 3277 O O      . HOH E 5 .   ? 21.019 44.372 10.906 1.00 42.34 ? 854 HOH A O      1 
HETATM 3278 O O      . HOH E 5 .   ? 42.510 17.947 39.360 1.00 43.81 ? 855 HOH A O      1 
HETATM 3279 O O      . HOH E 5 .   ? -0.439 14.090 27.059 1.00 30.77 ? 856 HOH A O      1 
HETATM 3280 O O      . HOH E 5 .   ? 38.822 15.753 33.044 1.00 36.19 ? 857 HOH A O      1 
HETATM 3281 O O      . HOH E 5 .   ? 41.440 19.352 8.181  1.00 32.94 ? 858 HOH A O      1 
HETATM 3282 O O      . HOH E 5 .   ? 27.979 3.216  9.571  1.00 43.10 ? 859 HOH A O      1 
HETATM 3283 O O      . HOH E 5 .   ? 33.854 8.493  3.781  1.00 31.18 ? 860 HOH A O      1 
HETATM 3284 O O      . HOH E 5 .   ? 15.507 39.364 35.939 1.00 44.96 ? 861 HOH A O      1 
HETATM 3285 O O      . HOH E 5 .   ? 37.268 23.202 5.208  1.00 36.48 ? 862 HOH A O      1 
HETATM 3286 O O      . HOH E 5 .   ? 35.280 44.412 35.691 1.00 22.63 ? 863 HOH A O      1 
HETATM 3287 O O      . HOH E 5 .   ? 2.841  18.203 22.325 1.00 33.13 ? 864 HOH A O      1 
HETATM 3288 O O      . HOH E 5 .   ? 38.674 5.929  19.473 1.00 38.43 ? 865 HOH A O      1 
HETATM 3289 O O      . HOH E 5 .   ? 41.535 16.494 40.590 1.00 51.87 ? 866 HOH A O      1 
HETATM 3290 O O      . HOH E 5 .   ? 33.598 26.309 44.731 1.00 28.89 ? 867 HOH A O      1 
HETATM 3291 O O      . HOH E 5 .   ? 46.450 15.272 30.897 1.00 42.45 ? 868 HOH A O      1 
HETATM 3292 O O      . HOH E 5 .   ? 28.666 -2.108 19.374 1.00 30.48 ? 869 HOH A O      1 
HETATM 3293 O O      . HOH E 5 .   ? 38.094 11.104 8.109  1.00 38.79 ? 870 HOH A O      1 
HETATM 3294 O O      . HOH E 5 .   ? 5.698  6.753  19.070 1.00 44.66 ? 871 HOH A O      1 
HETATM 3295 O O      . HOH E 5 .   ? 25.712 28.443 44.980 1.00 29.91 ? 872 HOH A O      1 
HETATM 3296 O O      . HOH E 5 .   ? 23.194 8.183  4.437  1.00 33.95 ? 873 HOH A O      1 
HETATM 3297 O O      . HOH E 5 .   ? 22.148 42.172 6.642  1.00 44.51 ? 874 HOH A O      1 
HETATM 3298 O O      . HOH E 5 .   ? 33.862 45.749 30.512 1.00 29.48 ? 875 HOH A O      1 
HETATM 3299 O O      . HOH E 5 .   ? 0.756  31.231 13.596 1.00 32.65 ? 876 HOH A O      1 
HETATM 3300 O O      . HOH E 5 .   ? 26.443 7.288  7.629  1.00 30.57 ? 877 HOH A O      1 
HETATM 3301 O O      . HOH E 5 .   ? 2.348  26.759 9.923  1.00 25.62 ? 878 HOH A O      1 
HETATM 3302 O O      . HOH E 5 .   ? 39.604 14.138 24.139 1.00 33.38 ? 879 HOH A O      1 
HETATM 3303 O O      . HOH E 5 .   ? 41.659 33.121 43.754 1.00 39.18 ? 880 HOH A O      1 
HETATM 3304 O O      . HOH E 5 .   ? 11.259 15.803 26.473 1.00 33.11 ? 881 HOH A O      1 
HETATM 3305 O O      . HOH E 5 .   ? 24.442 11.147 -1.389 1.00 28.14 ? 882 HOH A O      1 
HETATM 3306 O O      . HOH E 5 .   ? 28.855 13.298 -2.597 1.00 23.73 ? 883 HOH A O      1 
HETATM 3307 O O      . HOH E 5 .   ? 21.294 13.166 -2.806 1.00 36.83 ? 884 HOH A O      1 
HETATM 3308 O O      . HOH E 5 .   ? 32.864 36.542 6.965  1.00 42.64 ? 885 HOH A O      1 
HETATM 3309 O O      . HOH E 5 .   ? 33.433 10.903 43.051 1.00 39.30 ? 886 HOH A O      1 
HETATM 3310 O O      . HOH E 5 .   ? 29.572 11.704 40.599 1.00 25.68 ? 887 HOH A O      1 
HETATM 3311 O O      . HOH E 5 .   ? 41.695 34.958 13.453 1.00 36.66 ? 888 HOH A O      1 
HETATM 3312 O O      . HOH E 5 .   ? 38.457 10.012 3.953  1.00 40.62 ? 889 HOH A O      1 
HETATM 3313 O O      . HOH E 5 .   ? 18.425 2.524  9.692  1.00 29.24 ? 890 HOH A O      1 
HETATM 3314 O O      . HOH E 5 .   ? 29.897 24.443 47.388 1.00 41.40 ? 891 HOH A O      1 
HETATM 3315 O O      . HOH E 5 .   ? 30.807 35.306 -3.793 1.00 35.11 ? 892 HOH A O      1 
HETATM 3316 O O      . HOH E 5 .   ? 16.435 36.038 24.117 1.00 26.13 ? 893 HOH A O      1 
HETATM 3317 O O      . HOH E 5 .   ? 16.078 15.090 30.058 1.00 41.51 ? 894 HOH A O      1 
HETATM 3318 O O      . HOH E 5 .   ? 43.565 19.331 11.763 1.00 39.25 ? 895 HOH A O      1 
HETATM 3319 O O      . HOH E 5 .   ? 1.078  14.995 3.298  1.00 37.57 ? 896 HOH A O      1 
HETATM 3320 O O      . HOH E 5 .   ? 23.199 46.355 38.657 1.00 32.78 ? 897 HOH A O      1 
HETATM 3321 O O      . HOH E 5 .   ? 14.546 34.981 26.541 1.00 34.50 ? 898 HOH A O      1 
HETATM 3322 O O      . HOH E 5 .   ? 12.792 11.475 28.091 1.00 34.65 ? 899 HOH A O      1 
HETATM 3323 O O      . HOH E 5 .   ? -0.996 15.372 22.909 1.00 26.31 ? 900 HOH A O      1 
HETATM 3324 O O      . HOH E 5 .   ? 6.070  2.654  14.708 1.00 43.96 ? 901 HOH A O      1 
HETATM 3325 O O      . HOH E 5 .   ? 43.636 37.374 34.454 1.00 42.31 ? 902 HOH A O      1 
HETATM 3326 O O      . HOH E 5 .   ? 27.002 43.291 37.187 1.00 23.33 ? 903 HOH A O      1 
HETATM 3327 O O      . HOH E 5 .   ? 24.384 12.259 44.261 1.00 35.44 ? 904 HOH A O      1 
HETATM 3328 O O      . HOH E 5 .   ? 31.471 2.185  13.399 1.00 41.07 ? 905 HOH A O      1 
HETATM 3329 O O      . HOH E 5 .   ? 13.645 8.676  26.820 1.00 23.88 ? 906 HOH A O      1 
HETATM 3330 O O      . HOH E 5 .   ? 27.516 6.670  3.768  1.00 42.28 ? 907 HOH A O      1 
HETATM 3331 O O      . HOH E 5 .   ? 2.008  35.623 14.453 1.00 37.53 ? 908 HOH A O      1 
HETATM 3332 O O      . HOH E 5 .   ? 8.846  28.015 29.311 1.00 45.82 ? 909 HOH A O      1 
HETATM 3333 O O      . HOH E 5 .   ? 8.635  37.309 17.712 1.00 35.29 ? 910 HOH A O      1 
HETATM 3334 O O      . HOH E 5 .   ? 27.958 10.381 41.593 1.00 34.16 ? 911 HOH A O      1 
HETATM 3335 O O      . HOH E 5 .   ? 31.625 12.721 46.700 1.00 41.32 ? 912 HOH A O      1 
HETATM 3336 O O      . HOH E 5 .   ? 47.292 18.082 35.000 1.00 25.65 ? 913 HOH A O      1 
HETATM 3337 O O      . HOH E 5 .   ? 29.343 38.383 43.106 1.00 38.25 ? 914 HOH A O      1 
HETATM 3338 O O      . HOH E 5 .   ? 3.654  7.126  8.160  1.00 49.85 ? 915 HOH A O      1 
HETATM 3339 O O      . HOH E 5 .   ? 24.870 37.433 -1.523 1.00 42.77 ? 916 HOH A O      1 
HETATM 3340 O O      . HOH E 5 .   ? 34.431 17.946 2.171  1.00 46.08 ? 917 HOH A O      1 
HETATM 3341 O O      . HOH E 5 .   ? 38.536 26.688 42.858 1.00 42.23 ? 918 HOH A O      1 
HETATM 3342 O O      . HOH E 5 .   ? 37.108 28.464 44.250 1.00 47.67 ? 919 HOH A O      1 
HETATM 3343 O O      . HOH E 5 .   ? 32.102 12.957 44.254 1.00 33.91 ? 920 HOH A O      1 
HETATM 3344 O O      . HOH E 5 .   ? 20.722 45.476 40.963 1.00 35.36 ? 921 HOH A O      1 
HETATM 3345 O O      . HOH E 5 .   ? 40.587 11.466 23.943 1.00 43.35 ? 922 HOH A O      1 
HETATM 3346 O O      . HOH E 5 .   ? 30.588 43.580 39.676 1.00 29.48 ? 923 HOH A O      1 
HETATM 3347 O O      . HOH E 5 .   ? 12.238 6.460  27.306 1.00 43.36 ? 924 HOH A O      1 
HETATM 3348 O O      . HOH E 5 .   ? 10.932 17.490 -0.135 1.00 37.88 ? 925 HOH A O      1 
HETATM 3349 O O      . HOH E 5 .   ? 42.101 30.123 43.303 1.00 36.15 ? 926 HOH A O      1 
HETATM 3350 O O      . HOH E 5 .   ? 40.005 29.671 46.937 1.00 44.76 ? 927 HOH A O      1 
HETATM 3351 O O      . HOH E 5 .   ? 34.887 8.311  25.408 1.00 29.34 ? 928 HOH A O      1 
HETATM 3352 O O      . HOH E 5 .   ? 19.547 6.391  39.003 1.00 43.04 ? 929 HOH A O      1 
HETATM 3353 O O      . HOH E 5 .   ? 41.510 8.881  20.583 1.00 42.81 ? 930 HOH A O      1 
HETATM 3354 O O      . HOH E 5 .   ? 42.391 33.586 24.900 1.00 28.73 ? 931 HOH A O      1 
HETATM 3355 O O      . HOH E 5 .   ? 37.566 9.080  6.180  1.00 33.07 ? 932 HOH A O      1 
HETATM 3356 O O      . HOH E 5 .   ? 35.170 48.752 28.221 1.00 41.01 ? 933 HOH A O      1 
HETATM 3357 O O      . HOH E 5 .   ? 25.423 6.011  28.415 1.00 20.50 ? 934 HOH A O      1 
HETATM 3358 O O      . HOH E 5 .   ? 12.878 19.034 1.080  1.00 32.22 ? 935 HOH A O      1 
HETATM 3359 O O      . HOH E 5 .   ? 39.277 12.220 30.111 1.00 34.57 ? 936 HOH A O      1 
HETATM 3360 O O      . HOH E 5 .   ? 2.020  32.870 17.867 1.00 39.50 ? 937 HOH A O      1 
HETATM 3361 O O      . HOH E 5 .   ? 28.092 9.332  0.247  1.00 33.08 ? 938 HOH A O      1 
HETATM 3362 O O      . HOH E 5 .   ? 31.211 48.722 22.889 1.00 44.06 ? 939 HOH A O      1 
HETATM 3363 O O      . HOH E 5 .   ? 10.733 0.742  11.838 1.00 26.32 ? 940 HOH A O      1 
HETATM 3364 O O      . HOH E 5 .   ? 24.239 4.425  5.155  1.00 41.72 ? 941 HOH A O      1 
HETATM 3365 O O      . HOH E 5 .   ? 9.607  3.406  8.394  1.00 41.46 ? 942 HOH A O      1 
HETATM 3366 O O      . HOH E 5 .   ? 44.887 23.141 10.712 1.00 45.39 ? 943 HOH A O      1 
HETATM 3367 O O      . HOH E 5 .   ? 2.697  36.465 6.665  1.00 49.58 ? 944 HOH A O      1 
HETATM 3368 O O      . HOH E 5 .   ? 33.270 5.871  3.157  1.00 41.61 ? 945 HOH A O      1 
HETATM 3369 O O      . HOH E 5 .   ? 39.122 7.035  6.228  1.00 38.52 ? 946 HOH A O      1 
HETATM 3370 O O      . HOH E 5 .   ? 32.977 44.537 39.764 1.00 36.16 ? 947 HOH A O      1 
HETATM 3371 O O      . HOH E 5 .   ? 39.515 23.315 5.418  1.00 51.72 ? 948 HOH A O      1 
HETATM 3372 O O      . HOH E 5 .   ? 26.550 11.111 43.855 1.00 38.04 ? 949 HOH A O      1 
HETATM 3373 O O      . HOH E 5 .   ? 42.358 22.637 9.623  1.00 27.50 ? 950 HOH A O      1 
HETATM 3374 O O      . HOH E 5 .   ? 26.898 4.967  6.153  1.00 37.11 ? 951 HOH A O      1 
HETATM 3375 O O      . HOH E 5 .   ? 7.050  4.775  19.384 1.00 45.02 ? 952 HOH A O      1 
HETATM 3376 O O      . HOH E 5 .   ? 43.199 17.579 7.308  1.00 48.58 ? 953 HOH A O      1 
HETATM 3377 O O      . HOH E 5 .   ? 40.301 6.959  21.455 1.00 43.97 ? 954 HOH A O      1 
HETATM 3378 O O      . HOH E 5 .   ? 39.376 9.013  23.752 1.00 42.00 ? 955 HOH A O      1 
HETATM 3379 O O      . HOH E 5 .   ? 37.706 7.808  25.423 1.00 38.47 ? 956 HOH A O      1 
HETATM 3380 O O      . HOH E 5 .   ? 38.843 9.409  29.775 1.00 40.75 ? 957 HOH A O      1 
HETATM 3381 O O      . HOH E 5 .   ? 37.897 7.829  28.484 1.00 42.29 ? 958 HOH A O      1 
HETATM 3382 O O      . HOH E 5 .   ? 26.408 45.045 39.115 1.00 32.95 ? 959 HOH A O      1 
HETATM 3383 O O      . HOH E 5 .   ? 23.029 1.910  6.378  1.00 48.67 ? 960 HOH A O      1 
HETATM 3384 O O      . HOH E 5 .   ? 29.568 8.014  -1.117 1.00 53.40 ? 961 HOH A O      1 
HETATM 3385 O O      . HOH E 5 .   ? 36.047 45.350 31.114 1.00 37.73 ? 962 HOH A O      1 
HETATM 3386 O O      . HOH E 5 .   ? 7.277  0.371  15.682 1.00 39.36 ? 963 HOH A O      1 
HETATM 3387 O O      . HOH E 5 .   ? 15.173 0.053  8.600  1.00 37.23 ? 964 HOH A O      1 
HETATM 3388 O O      . HOH E 5 .   ? 2.257  34.970 18.868 1.00 46.60 ? 965 HOH A O      1 
HETATM 3389 O O      . HOH E 5 .   ? 23.729 4.123  2.753  1.00 48.15 ? 966 HOH A O      1 
# 
